AUTHOR ASSIGNMENTS - 1 DOMAIN STRUCTURES

AUTHOR ASSIGNMENTS - 1 DOMAIN STRUCTURES


1AAF

PRELIMINARY 06-APR-92 :: HIV-1 NUCLEOCAPSID PROTEIN, MN STRAIN

DOMAIN 1: 1 to 55 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AAK

UBIQUITIN CONJUGATION 08-APR-92 :: UBIQUITIN CONJUGATING ENZYME (E.C.6.3.2.19)

DOMAIN 1: 1 to 151 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AAP A

PROTEINASE INHIBITOR (TRYPSIN) 14-SEP-90 :: PROTEASE INHIBITOR DOMAIN OF ALZHEIMER'S AMYLOID

DOMAIN 1: A 1 to A 56 ; The following residues NOT assigned to any domain: Chain "A" 1 - 56
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ABA

ELECTRON TRANSPORT 24-APR-92 :: GLUTAREDOXIN MUTANT WITH VAL 15 REPLACED BY GLY AN

DOMAIN 1: 1 to 87 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ACE

HYDROLASE(CARBOXYLIC ESTERASE) 08-OCT-91 :: ACETYLCHOLINESTERASE (E.C.3.1.1.7)

DOMAIN 1: 4 to 534 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ADS

OXIDOREDUCTASE 08-JUL-92 :: ALDOSE REDUCTASE (E.C.1.1.1.21) COMPLEX WITH NADPH

DOMAIN 1: 1 to 315 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1APS

HYDROLASE(ACTING ON ACID ANHYDRIDES) 20-FEB-91 :: ACYLPHOSPHATASE (E.C.3.6.1.7) (NMR, 5 STRUCTURES)

DOMAIN 1: 1 to 98 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ATX

SEA ANEMONE TOXIN 14-MAY-90 :: /ATX$ IA (/NMR$, 8 STRUCTURES)

DOMAIN 1: 1 to 46 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AYH

HYDROLASE 31-DEC-92 :: HYBRID (1,3-1,4)-BETA-D-GLUCAN 4-GLUCANOHYDROLASE

DOMAIN 1: 1 to 214 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BAR B

GROWTH FACTOR 29-SEP-92 :: ACIDIC FIBROBLAST GROWTH FACTOR (AFGF) MUTANT WITH

DOMAIN 1: B 1 to B 138 ; The following residues NOT assigned to any domain: Chain "B" 11 - 137
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BBA

PANCREATIC HORMONE 10-MAR-92 :: BOVINE PANCREATIC POLYPEPTIDE (BPP) (NMR, MEAN STR

DOMAIN 1: 1 to 36 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BBH A

PRELIMINARY 18-MAY-92 :: CYTOCHROME $C'

DOMAIN 1: A 1 to A 131 ; The following residues NOT assigned to any domain: Chain "A" 1 - 131
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BBL

PRELIMINARY 20-FEB-92 :: E3-BINDING DOMAIN OF THE DIHYDROLIPOAMIDE

DOMAIN 1: 12 to 48 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BBP A

BILIN BINDING 19-SEP-90 :: BILIN BINDING PROTEIN (/BBP$)

DOMAIN 1: A 2 to A 178 ; The following residues NOT assigned to any domain: Chain "A" 2 - 178 The following residues NOT assigned to any domain: Chain "A" 2 - 178 The following residues NOT assigned to any domain: Chain "A" 2 - 178
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BBT 1

PRELIMINARY 18-MAY-92 :: FOOT AND MOUTH DISEASE VIRUS O=1=BFS 1860 (FMDVO=1

DOMAIN 1: 1 31 to 1 189 ; The following residues NOT assigned to any domain: Chain "1" 1 - 30 Chain "1" 190 - 208 The following residues NOT assigned to any domain: Chain "1" 9 - 218 The following residues NOT assigned to any domain: Chain "1" 1 - 220 The following residues NOT assigned to any domain: Chain "1" 15 - 85
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BBT 2

PRELIMINARY 18-MAY-92 :: FOOT AND MOUTH DISEASE VIRUS O=1=BFS 1860 (FMDVO=1

DOMAIN 1: 2 9 to 2 218 ; The following residues NOT assigned to any domain: Chain "2" 1 - 208 The following residues NOT assigned to any domain: Chain "2" 1 - 220 The following residues NOT assigned to any domain: Chain "2" 15 - 85
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BGC

CYTOKINE 27-APR-93 :: GRANULOCYTE COLONY-STIMULATING FACTOR (RBG-CSF)

DOMAIN 1: 9 to 173 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BOP

PRELIMINARY 10-DEC-92 :: BOVINE PAPILLOMAVIRUS-1 E2 DNA-BINDING DOMAIN/DNA

DOMAIN 1: 326 to 410 ; The following residues NOT assigned to any domain: Chain " " 1 - 17
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BOV A

TOXIN 08-OCT-91 :: VEROTOXIN-1 (B-OLIGOMER, ALSO CALLED SHIGA-LIKE TO

DOMAIN 1: A 1 to A 69 ; The following residues NOT assigned to any domain: Chain "A" 1 - 69 The following residues NOT assigned to any domain: Chain "A" 1 - 69 The following residues NOT assigned to any domain: Chain "A" 1 - 69 The following residues NOT assigned to any domain: Chain "A" 1 - 69
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BRD

PHOTORECEPTOR 23-MAY-90 :: BACTERIORHODOPSIN

DOMAIN 1: 8 to 226 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BTC

HYDROLASE(O-GLYCOSYL) 18-FEB-93 :: BETA-AMYLASE (E.C.3.2.1.2) COMPLEX WITH ALPHA-CYCL

DOMAIN 1: 5 to 495 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BW4

LECTIN 06-JUL-92 :: BARWIN, BASIC BARLEY SEED PROTEIN (NMR, 20 STRUCTU

DOMAIN 1: 1 to 125 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1C2R A

ELECTRON TRANSPORT PROTEIN (CYTOCHROME) 19-MAR-91 :: CYTOCHROME $C=2=

DOMAIN 1: A 1 to A 116 ; The following residues NOT assigned to any domain: Chain "A" 1 - 116
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1C5A

COMPLEMENT FACTOR 12-JUN-90 :: DES-ARG==74==-COMPLEMENT C5A

DOMAIN 1: 1 to 65 ; The following residues NOT assigned to any domain: Chain " " 66 - 66
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CAJ

LYASE(OXO-ACID) 17-SEP-92 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) MUTANT WITH GL

DOMAIN 1: 3 to 261 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CBN

PLANT SEED PROTEIN 11-OCT-91 :: CRAMBIN

DOMAIN 1: 1 to 46 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CBP

TYPE 1 COPPER PROTEIN 14-SEP-88 :: CUCUMBER BASIC PROTEIN

DOMAIN 1: 11 to 96 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CD8

PRELIMINARY 16-JAN-92 :: C*D8

DOMAIN 1: 1 to 114 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CDT A

CYTOTOXIN 17-MAY-90 :: CARDIOTOXIN V=4===/II$== (TOXIN /III$)

DOMAIN 1: A 1 to A 60 ; The following residues NOT assigned to any domain: Chain "A" 1 - 60
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CIS

HYBRID PROTEIN 23-APR-93 :: HYBRID PROTEIN FORMED FROM CHYMOTRYPSIN INHIBITOR-

DOMAIN 1: 20 to 85 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CMB A

DNA-BINDING REGULATORY PROTEIN 28-AUG-92 :: MET APO-REPRESSOR (METJ)

DOMAIN 1: A 1 to A 104 ; The following residues NOT assigned to any domain: Chain "A" 1 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1COB A

OXIDOREDUCTASE 19-FEB-92 :: SUPEROXIDE DISMUTASE (CO SUBSTITUTED) (E.C.1.15.1.

DOMAIN 1: A 1 to A 151 ; The following residues NOT assigned to any domain: Chain "A" 1 - 151
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CSE I

COMPLEX(SERINE PROTEINASE-INHIBITOR) 03-JUN-88 :: SUBTILISIN CARLSBERG (E.C.3.4.21.62) (COMMERCIAL P

DOMAIN 1: I 8 to I 70 ; The following residues NOT assigned to any domain: Chain "I" 1 - 275
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CTC

02-APR-93 :: CARBOXYPEPTIDASE A COMPLEXED WITH L-PHENYL LACTATE

DOMAIN 1: 1 to 307 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1D66 A

TRANSCRIPTION REGULATION 06-MAR-92 :: GAL4 (RESIDUES 1 - 65) COMPLEX WITH 19MER DNA

DOMAIN 1: A 8 to A 64 ; The following residues NOT assigned to any domain: Chain "A" 1 - 19 The following residues NOT assigned to any domain: Chain "A" 20 - 38 The following residues NOT assigned to any domain: Chain "A" 8 - 64
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DHR

OXIDOREDUCTASE(ACTING ON NADH OR NADPH) 30-MAR-92 :: DIHYDROPTERIDINE REDUCTASE (DHPR) (E.C.1.6.99.10)

DOMAIN 1: 5 to 240 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DNK A

PRELIMINARY 10-AUG-92 :: DEOXYRIBONUCLEASE I (D*NASE I) (E.C.3.1.21.1) COMP

DOMAIN 1: A 1 to A 260 ; The following residues NOT assigned to any domain: Chain "A" 301 - 307 The following residues NOT assigned to any domain: Chain "A" 309 - 316
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EAF

DIHYDROLIPOAMIDE ACETYLTRANSFERASE 16-DEC-92 :: DIHYDROLIPOYL TRANSACETYLASE (E.C.2.3.1.12) (CATAL

DOMAIN 1: 415 to 637 ; The following residues NOT assigned to any domain: Chain " " 395 - 414
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ECO

OXYGEN TRANSPORT 07-MAR-79 :: HEMOGLOBIN (ERYTHROCRUORIN, CARBONMONOXY)

DOMAIN 1: 1 to 136 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EFM

ELONGATION FACTOR 29-MAY-87 :: TRYPSIN-MODIFIED ELONGATION FACTOR TU (/EF$-*TU-/G

DOMAIN 1: 12 to 190 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EGF

PRELIMINARY 01-OCT-91 :: EPIDERMAL GROWTH FACTOR (/EGF$) (16 MODELS)

DOMAIN 1: 1 to 53 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1END

ENDONUCLEASE 15-JUN-92 :: ENDONUCLEASE V

DOMAIN 1: 2 to 138 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ERP

PHEROMONE 02-DEC-92 :: PHEROMONE ER-10 (NMR, 20 STRUCTURES)

DOMAIN 1: 1 to 38 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FAS

TOXIN 07-AUG-92 :: FASCICULIN 1

DOMAIN 1: 1 to 61 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FBA A

LYASE(ALDEHYDE) 08-JUN-92 :: FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE (E.C.4.1.2.13)

DOMAIN 1: A 1 to A 363 ; The following residues NOT assigned to any domain: Chain "A" 0 - 0 The following residues NOT assigned to any domain: Chain "A" 0 - 363 The following residues NOT assigned to any domain: Chain "A" 0 - 363 The following residues NOT assigned to any domain: Chain "A" 0 - 363
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FC2 C

IMMUNOGLOBULIN 21-MAY-81 :: IMMUNOGLOBULIN FC AND FRAGMENT B OF PROTEIN A COMP

DOMAIN 1: C 124 to C 167 ; The following residues NOT assigned to any domain: Chain "C" 238 - 444
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FCS

OXYGEN TRANSPORT 20-APR-93 :: MYOGLOBIN MUTANT WITH HIS 64 REPLACED BY VAL AND T

DOMAIN 1: 0 to 153 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FDD

ELECTRON TRANSPORT(IRON-SULFUR) 17-JAN-93 :: FERREDOXIN MUTANT WITH ASP 15 REPLACED BY ASN (D15

DOMAIN 1: 1 to 106 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FHA

IRON STORAGE 20-DEC-90 :: FERRITIN (H-CHAIN) MUTANT (LYS 86 REPLACED BY GLN)

DOMAIN 1: 5 to 184 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FIA B

DNA-BINDING PROTEIN 18-DEC-91 :: FIS PROTEIN (FACTOR FOR INVERSION STIMULATION)

DOMAIN 1: B 10 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 10 - 98
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FXI A

ELECTRON TRANSFER (IRON-SULFUR PROTEIN) 28-AUG-90 :: FERREDOXIN I

DOMAIN 1: A 1 to A 96 ; The following residues NOT assigned to any domain: Chain "A" 1 - 96 The following residues NOT assigned to any domain: Chain "A" 1 - 96 The following residues NOT assigned to any domain: Chain "A" 1 - 96
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GKY

PRELIMINARY 23-DEC-91 :: GUANYLATE KINASE (E.C.2.7.4.8) COMPLEX WITH

DOMAIN 1: 1 to 186 ; The following residues NOT assigned to any domain: Chain " " 0 - 0
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GLA F

PHOSPHOTRANSFERASE 28-OCT-92 :: GLYCEROL KINASE (E.C.2.7.1.30) COMPLEX WITH GLYCER

DOMAIN 1: F 1 to F 168 ; The following residues NOT assigned to any domain: Chain "F" 4 - 499
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GLU A

GLUCOCORTICOID RECEPTOR 30-AUG-92 :: GLUCOCORTICOID RECEPTOR (DNA-BINDING DOMAIN) COMPL

DOMAIN 1: A 434 to A 514 ; The following residues NOT assigned to any domain: Chain "A" 434 - 514 The following residues NOT assigned to any domain: Chain "A" -10 - 9 The following residues NOT assigned to any domain: Chain "A" -10 - 9
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GMF A

GROWTH FACTOR 01-DEC-91 :: GRANULOCYTE-MACROPHAGE COLONY-STIMULATING FACTOR

DOMAIN 1: A 5 to A 123 ; The following residues NOT assigned to any domain: Chain "A" 5 - 123
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GMP A

HYDROLASE(GUANYLORIBONUCLEASE) 01-OCT-92 :: RIBONUCLEASE FROM STREPTOMYCES AUREOFACIENS (RNASE

DOMAIN 1: A 1 to A 96 ; The following residues NOT assigned to any domain: Chain "A" 1 - 96
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GOX

OXIDOREDUCTASE (OXYGEN(A)) 14-JUN-89 :: GLYCOLATE OXIDASE (E.C.1.1.3.1)

DOMAIN 1: 1 to 359 ; The following residues NOT assigned to any domain: Chain " " 0 - 0
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GPS

PLANT TOXIN 29-JUL-92 :: GAMMA-1-P THIONIN (NMR, 8 STRUCTURES)

DOMAIN 1: 1 to 47 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HCC

GLYCOPROTEIN 28-NOV-90 :: 16TH COMPLEMENT CONTROL PROTEIN (/CCP$) OF FACTOR

DOMAIN 1: 1 to 59 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HDD C

DNA BINDING 16-SEP-91 :: ENGRAILED HOMEODOMAIN COMPLEX WITH /DNA$

DOMAIN 1: C 3 to C 59 ; The following residues NOT assigned to any domain: Chain "C" 3 - 59 The following residues NOT assigned to any domain: Chain "C" 1 - 21 The following residues NOT assigned to any domain: Chain "C" 22 - 42
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGE B

PRELIMINARY 01-NOV-91 :: HEMAGGLUTININ (BROMELAIN DIGESTED) CONTAINING *GLY

DOMAIN 1: B 1 to B 175 ; The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 175 The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HIG A

GLYCOPROTEIN 03-OCT-91 :: INTERFERON-GAMMA

DOMAIN 1: A 1 to A 123 ; The following residues NOT assigned to any domain: Chain "A" 1 - 123 The following residues NOT assigned to any domain: Chain "A" 1 - 123 The following residues NOT assigned to any domain: Chain "A" 1 - 123
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HIV A

HYDROLASE(ACID PROTEINASE) 12-FEB-92 :: HIV-1 PROTEASE (HIV-1 PR) COMPLEX WITH U75875

DOMAIN 1: A 1 to A 99 ; The following residues NOT assigned to any domain: Chain "A" 1 - 99 The following residues NOT assigned to any domain: Chain "A" 2 - 4
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HSD A

OXIDOREDUCTASE 15-AUG-91 :: 3ALPHA,20BETA-*HYDROXYSTEROID DEHYDROGENASE (HOLO

DOMAIN 1: A 1 to A 255 ; The following residues NOT assigned to any domain: Chain "A" 1 - 255 The following residues NOT assigned to any domain: Chain "A" 1 - 255 The following residues NOT assigned to any domain: Chain "A" 1 - 255
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IFA

PRELIMINARY 29-OCT-91 :: MURINE INTERFERON-BETA

DOMAIN 1: 3 to 160 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IFC

PRELIMINARY 19-DEC-91 :: INTESTINAL FATTY ACID BINDING PROTEIN - APO FORM 2

DOMAIN 1: 1 to 131 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ISU A

PRELIMINARY 09-SEP-92 :: HIGH-POTENTIAL IRON-SULFUR PROTEIN (HIPIP)

DOMAIN 1: A 1 to A 62 ; The following residues NOT assigned to any domain: Chain "A" 1 - 62
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IXA

HUMAN FACTOR IX 14-NOV-91 :: EGF-LIKE MODULE OF HUMAN FACTOR IX (NMR, MINIMIZED

DOMAIN 1: 46 to 84 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LE4

LIPOPROTEIN 22-AUG-91 :: APOLIPOPROTEIN-*E4 (/LDL$ RECEPTOR BINDING DOMAIN)

DOMAIN 1: 24 to 162 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTS A

PRELIMINARY 15-JUL-92 :: HEAT-LABILE ENTEROTOXIN (LT); CHOLERA-LIKE TOXIN,

DOMAIN 1: A 4 to A 188 ; The following residues NOT assigned to any domain: Chain "A" 1 - 103 The following residues NOT assigned to any domain: Chain "A" 1 - 103 The following residues NOT assigned to any domain: Chain "A" 1 - 103 The following residues NOT assigned to any domain: Chain "A" 1 - 103 The following residues NOT assigned to any domain: Chain "A" 1 - 103 The following residues NOT assigned to any domain: Chain "A" 196 - 236
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTS C

PRELIMINARY 15-JUL-92 :: HEAT-LABILE ENTEROTOXIN (LT); CHOLERA-LIKE TOXIN,

DOMAIN 1: C 196 to C 236 ; The following residues NOT assigned to any domain: Chain "C" 1 - 103 The following residues NOT assigned to any domain: Chain "C" 1 - 103 The following residues NOT assigned to any domain: Chain "C" 1 - 103 The following residues NOT assigned to any domain: Chain "C" 1 - 103 The following residues NOT assigned to any domain: Chain "C" 1 - 103 The following residues NOT assigned to any domain: Chain "C" 4 - 188
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTS D

PRELIMINARY 15-JUL-92 :: HEAT-LABILE ENTEROTOXIN (LT); CHOLERA-LIKE TOXIN,

DOMAIN 1: D 1 to D 103 ; The following residues NOT assigned to any domain: Chain "D" 1 - 103 The following residues NOT assigned to any domain: Chain "D" 1 - 103 The following residues NOT assigned to any domain: Chain "D" 1 - 103 The following residues NOT assigned to any domain: Chain "D" 1 - 103 The following residues NOT assigned to any domain: Chain "D" 4 - 188 The following residues NOT assigned to any domain: Chain "D" 196 - 236
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MDA A

ELECTRON TRANSPORT 02-MAR-92 :: METHYLAMINE DEHYDROGENASE (E.C.1.4.99.3) COMPLEX W

DOMAIN 1: A 3 to A 105 ; The following residues NOT assigned to any domain: Chain "A" 1 - 368 The following residues NOT assigned to any domain: Chain "A" 7 - 127 The following residues NOT assigned to any domain: Chain "A" 1 - 368 The following residues NOT assigned to any domain: Chain "A" 7 - 127 The following residues NOT assigned to any domain: Chain "A" 3 - 105
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MDA H

ELECTRON TRANSPORT 02-MAR-92 :: METHYLAMINE DEHYDROGENASE (E.C.1.4.99.3) COMPLEX W

DOMAIN 1: H 1 to H 368 ; The following residues NOT assigned to any domain: Chain "H" 7 - 127 The following residues NOT assigned to any domain: Chain "H" 1 - 368 The following residues NOT assigned to any domain: Chain "H" 7 - 127 The following residues NOT assigned to any domain: Chain "H" 3 - 105 The following residues NOT assigned to any domain: Chain "H" 3 - 105
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MDC

BINDING PROTEIN 20-JUL-92 :: FATTY ACID BINDING PROTEIN (MANDUCA SEXTA) (MFB2)

DOMAIN 1: 1 to 132 ; The following residues NOT assigned to any domain: Chain " " 0 - 0
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MRR A

REDUCTASE (ACTING ON CH2) 28-JUL-92 :: MANGANESE SUBSTITUTED PROTEIN R2 OF

DOMAIN 1: A 1 to A 340 ; The following residues NOT assigned to any domain: Chain "A" 1 - 340
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MS2 A

PRELIMINARY 28-MAY-91 :: /MS$2 VIRUS (BACTERIOPHAGE)

DOMAIN 1: A 1 to A 129 ; The following residues NOT assigned to any domain: Chain "A" 1 - 129 The following residues NOT assigned to any domain: Chain "A" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MUP

PRELIMINARY 21-SEP-92 :: MAJOR URINARY PROTEIN COMPLEX WITH 2-(SEC-BUTYL)

DOMAIN 1: 5 to 161 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NIP B

IRON PROTEIN 29-SEP-92 :: NITROGENASE IRON PROTEIN

DOMAIN 1: B 1 to B 287 ; The following residues NOT assigned to any domain: Chain "B" 1 - 283
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NRC A

PRELIMINARY 12-MAR-92 :: N-TERMINAL FRAGMENT (RESIDUES 1-95) OF A PROTEIN F

DOMAIN 1: A 6 to A 90 ; The following residues NOT assigned to any domain: Chain "A" 6 - 88
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NXB

NEUROTOXIN (POST-SYNAPTIC) 08-AUG-80 :: NEUROTOXIN $B (PROBABLY IDENTICAL TO ERABUTOXIN $B

DOMAIN 1: 1 to 62 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1OFV

PRELIMINARY 22-JUN-92 :: OXIDIZED FLAVODOXIN

DOMAIN 1: 1 to 169 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1OMF

PRELIMINARY 15-JAN-93 :: MATRIX PORIN (OMPF)

DOMAIN 1: 1 to 340 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1OVB

PRELIMINARY 05-OCT-92 :: OVOTRANSFERRIN (18KD FRAGMENT, DOMAIN II FROM N-TE

DOMAIN 1: 94 to 248 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PAZ

ELECTRON TRANSFER(CUPROPROTEIN) 28-JUN-88 :: PSEUDOAZURIN (OXIDIZED CU ++ AT $P*H 6.8)

DOMAIN 1: 1 to 120 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PCD A

OXIDOREDUCTASE (INCORPORATION OF O2) 07-SEP-90 :: PROTOCATECHUATE 3,4-*DIOXYGENASE (E.C.1.13.11.3)

DOMAIN 1: A 1 to A 201 ; The following residues NOT assigned to any domain: Chain "A" 1 - 239
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PDC

PRELIMINARY 10-OCT-91 :: /PDC$-109 TYPE /II$ $B-DOMAIN

DOMAIN 1: -4 to 42 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PHY

PHOTORECEPTOR 04-AUG-89 :: PHOTOACTIVE YELLOW PROTEIN

DOMAIN 1: 1 to 126 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1POA

HYDROLASE 07-SEP-92 :: PHOSPHOLIPASE A2 (E.C.3.1.1.4)

DOMAIN 1: 1 to 118 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1POC

HYDROLASE 07-SEP-92 :: PHOSPHOLIPASE A2 (E.C.3.1.1.4) COMPLEX WITH THE

DOMAIN 1: 1 to 134 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PPB L

PRELIMINARY 24-OCT-91 :: THROMBIN EC 3.4.21.5 IN COVALENT COMPLEX WITH D-PH

DOMAIN 1: A 1 H to A 15 ; The following residues NOT assigned to any domain: Chain "A" 16 - 247 The following residues NOT assigned to any domain: Chain "A" 1 - 3
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PRC C

PHOTOSYNTHETIC REACTION CENTER 04-FEB-88 :: PHOTOSYNTHETIC REACTION CENTER

DOMAIN 1: C 1 to C 332 ; The following residues NOT assigned to any domain: Chain "C" 333 - 333 The following residues NOT assigned to any domain: Chain "C" 1 - 273 The following residues NOT assigned to any domain: Chain "C" 1 - 323 The following residues NOT assigned to any domain: Chain "C" 0 - 258
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PRC M

PHOTOSYNTHETIC REACTION CENTER 04-FEB-88 :: PHOTOSYNTHETIC REACTION CENTER

DOMAIN 1: M 1 to M 323 ; The following residues NOT assigned to any domain: Chain "M" 1 - 333 The following residues NOT assigned to any domain: Chain "M" 1 - 273 The following residues NOT assigned to any domain: Chain "M" 0 - 258
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PRF

PRELIMINARY 23-JUN-93 :: PROFILIN 1A

DOMAIN 1: 1 to 125 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PTE

HYDROLASE-TRANSPEPTIDASE 21-OCT-85 :: D-ALANYL-*D-ALANINE CARBOXYPEPTIDASE(SLASH)TRANSPE

DOMAIN 1: 14 to 353 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PYP

ACID ANHYDRIDE HYDROLASE 03-FEB-83 :: INORGANIC PYROPHOSPHATASE (E.C.3.6.1.1)

DOMAIN 1: 1 to 281 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1R09 4

RHINOVIRUS COAT PROTEIN 04-MAY-90 :: RHINOVIRUS 14 (/HRV$14) COMPLEX WITH ANTIVIRAL AGE

DOMAIN 1: 4 29 to 4 68 ; The following residues NOT assigned to any domain: Chain "4" 17 - 289 The following residues NOT assigned to any domain: Chain "4" 8 - 262 The following residues NOT assigned to any domain: Chain "4" 1 - 236
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1R1A 2

RHINOVIRUS COAT PROTEIN 15-MAR-89 :: RHINOVIRUS SEROTYPE 1 (/HRV$1) COAT PROTEIN

DOMAIN 1: 2 11 to 2 263 ; The following residues NOT assigned to any domain: Chain "2" 5 - 287 The following residues NOT assigned to any domain: Chain "2" 1 - 238 The following residues NOT assigned to any domain: Chain "2" 26 - 44
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ERI A

COMPLEX (ENDONUCLEASE/DNA) 18-MAY-94 :: ECO RI ENDONUCLEASE (ENDODEOXYRIBONUCLEASE ECORI)

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 1 - 13
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RBP

RETINOL TRANSPORT 02-APR-90 :: RETINOL BINDING PROTEIN

DOMAIN 1: 1 to 175 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RCB

CYTOKINE 26-AUG-92 :: INTERLEUKIN 4

DOMAIN 1: 1 to 129 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RND

PRELIMINARY 21-OCT-91 :: RIBONUCLEASE *A (E.C.3.1.27.5) COMPLEXED WITH

DOMAIN 1: 1 to 124 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RPR A

PRELIMINARY 09-OCT-91 :: ROP (REPRESSOR OF PRIMER) (10 STRUCTURES)

DOMAIN 1: A 1 to A 63 ; The following residues NOT assigned to any domain: Chain "A" 1 - 63
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RRO

CALCIUM-BINDING PROTEIN 27-AUG-92 :: RAT ONCOMODULIN

DOMAIN 1: 1 to 108 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RVE A

PRELIMINARY 24-FEB-92 :: ECO RV ENDONUCLEASE (E.C.3.1.21.4)

DOMAIN 1: A 2 to A 245 ; The following residues NOT assigned to any domain: Chain "A" 2 - 245
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1S01

HYDROLASE (SERINE PROTEINASE) 21-AUG-89 :: SUBTILISIN /BPN$(PRIME) 8350 (E.C.3.4.21.14) (MUTA

DOMAIN 1: 1 to 275 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SHA A

PHOSPHOTRANSFERASE 18-AUG-92 :: V-SRC TYROSINE KINASE TRANSFORMING PROTEIN (PHOSPH

DOMAIN 1: A 2 to A 104 ; The following residues NOT assigned to any domain: Chain "A" 201 - 205
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SHF A

PHOSPHOTRANSFERASE 19-MAY-93 :: FYN PROTO-ONCOGENE TYROSINE KINASE (E.C.2.7.1.112)

DOMAIN 1: A 84 to A 142 ; The following residues NOT assigned to any domain: Chain "A" 84 - 142
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SNC

HYDROLASE (PHOSPHORIC DIESTER) 21-JUL-89 :: STAPHYLOCOCCAL NUCLEASE (E.C.3.1.31.1) COMPLEX WIT

DOMAIN 1: 7 to 141 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TAB I

HYDROLASE (SERINE PROTEINASE) 15-OCT-90 :: TRYPSIN (E.C.3.4.21.4) COMPLEX WITH BOWMAN-*BIRK I

DOMAIN 1: I 12 to I 73 ; The following residues NOT assigned to any domain: Chain "I" 16 - 245
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TEN

CELL ADHESION PROTEIN 28-AUG-92 :: TENASCIN (THIRD FIBRONECTIN TYPE III REPEAT)

DOMAIN 1: 803 to 891 ; The following residues NOT assigned to any domain: Chain " " 802 - 802
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TFG

GROWTH FACTOR 17-NOV-92 :: TRANSFORMING GROWTH FACTOR TYPE BETA 2 (TGF-B2)

DOMAIN 1: 1 to 112 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TFI

TRANSCRIPTION REGULATION 27-APR-93 :: TRANSCRIPTIONAL ELONGATION FACTOR SII (TFIIS, NUCL

DOMAIN 1: 1 to 50 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TGS I

COMPLEX (PROTEINASE/INHIBITOR) 27-SEP-82 :: TRYPSINOGEN COMPLEX WITH PORCINE PANCREATIC SECRET

DOMAIN 1: I 1 to I 56 ; The following residues NOT assigned to any domain: Chain "I" 14 - 245
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1THO

ELECTRON TRANSPORT 28-JAN-93 :: THIOREDOXIN MUTANT WITH ARG INSERTED BETWEEN GLY 3

DOMAIN 1: 1 to 108 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TIE

PROTEINASE INHIBITOR (TRYPSIN) 14-FEB-91 :: ERYTHRINA TRYPSIN INHIBITOR (KUNITZ) DE-3

DOMAIN 1: 1 to 170 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TIM A

ISOMERASE(INTRAMOLECULAR OXIDOREDUCTSE) 01-SEP-76 :: TRIOSE PHOSPHATE ISOMERASE (E.C.5.3.1.1)

DOMAIN 1: A 1 to A 248 ; The following residues NOT assigned to any domain: Chain "A" 1 - 248
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TLK

CALMODULIN-BINDING 20-JUL-92 :: TELOKIN (E.C.2.7.1.117)

DOMAIN 1: 33 to 135 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TNF A

LYMPHOKINE 25-AUG-89 :: TUMOR NECROSIS FACTOR-ALPHA (CACHECTIN)

DOMAIN 1: A 6 to A 157 ; The following residues NOT assigned to any domain: Chain "A" 6 - 157 The following residues NOT assigned to any domain: Chain "A" 6 - 157
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TTB A

TRANSPORT(THYROXINE) 02-NOV-92 :: TRANSTHYRETIN (FORMERLY PREALBUMIN) MUTANT WITH AL

DOMAIN 1: A 1 to A 127 ; The following residues NOT assigned to any domain: Chain "A" 1 - 127
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ULA

PENTOSYLTRANSFERASE 05-NOV-91 :: PURINE NUCLEOSIDE PHOSPHORYLASE (E.C.2.4.2.1)

DOMAIN 1: 1 to 289 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1UTG

STEROID BINDING 03-APR-89 :: UTEROGLOBIN (OXIDIZED)

DOMAIN 1: 1 to 70 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1VAA B

HISTOCOMPATIBILITY ANTIGEN 28-JUL-92 :: MHC CLASS I H-2K==B== COMPLEXED WITH VESICULAR STO

DOMAIN 1: B 1 to B 99 ; The following residues NOT assigned to any domain: Chain "B" 1 - 274 The following residues NOT assigned to any domain: Chain "B" 1 - 8
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1WRP R

DNA BINDING REGULATORY PROTEIN 01-DEC-87 :: $TRP REPRESSOR (TRIGONAL FORM)

DOMAIN 1: R 4 to R 105 ; The following residues NOT assigned to any domain: Chain "R" 1 - 1
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1WSY A

LYASE(CARBON-OXYGEN) 19-SEP-88 :: TRYPTOPHAN SYNTHASE (E.C.4.2.1.20)

DOMAIN 1: A 1 to A 265 ; The following residues NOT assigned to any domain: Chain "A" 9 - 393
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1XIM A

ISOMERASE(INTRAMOLECULAR OXIDOREDUCTSE) 29-MAY-91 :: D-XYLOSE ISOMERASE (E.C.5.3.1.5) COMPLEX WITH XYLI

DOMAIN 1: A 3 to A 328 ; The following residues NOT assigned to any domain: Chain "A" 329 - 394 The following residues NOT assigned to any domain: Chain "A" 3 - 394 The following residues NOT assigned to any domain: Chain "A" 3 - 394 The following residues NOT assigned to any domain: Chain "A" 3 - 394
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1YCC

ELECTRON TRANSPORT (CYTOCHROME) 09-MAY-90 :: CYTOCHROME C (ISOZYME 1) (REDUCED)

DOMAIN 1: -5 to 103 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

256B A

ELECTRON TRANSPORT 16-JAN-90 :: CYTOCHROME $B562 (OXIDIZED)

DOMAIN 1: A 1 to A 106 ; The following residues NOT assigned to any domain: Chain "A" 1 - 106
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2ACH A

PROTEINASE INHIBITOR 26-APR-93 :: ALPHA1 ANTICHYMOTRYPSIN

DOMAIN 1: A * to A * ; B * to B * ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2AVI A

BIOTIN BINDING PROTEIN 23-APR-93 :: AVIDIN COMPLEX WITH BIOTIN

DOMAIN 1: A 3 to A 123 ; The following residues NOT assigned to any domain: Chain "A" 3 - 123
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2AZA A

ELECTRON TRANSPORT PROTEIN(CUPROPROTEIN)14-OCT-86 :: AZURIN (OXIDIZED)

DOMAIN 1: A 1 to A 129 ; The following residues NOT assigned to any domain: Chain "A" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2BDS

ANTI-HYPERTENSIVE, ANTI-VIRAL PROTEIN 14-NOV-88 :: /BDS-I$ (NMR, 42 SIMULATED ANNEALING STRUCTURES)

DOMAIN 1: 1 to 43 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2BPA 1

BACTERIOPHAGE PHIX174 COAT PROTEINS 03-DEC-91 :: BACTERIOPHAGE PHIX174 CAPSID PROTEINS GPF, GPG, GP

DOMAIN 1: 1 1 to 1 426 ; The following residues NOT assigned to any domain: Chain "1" 1 - 175 The following residues NOT assigned to any domain: Chain "1" 2 - 37 The following residues NOT assigned to any domain: Chain "1" 0 - 4
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2BPA 2

BACTERIOPHAGE PHIX174 COAT PROTEINS 03-DEC-91 :: BACTERIOPHAGE PHIX174 CAPSID PROTEINS GPF, GPG, GP

DOMAIN 1: 2 1 to 2 175 ; The following residues NOT assigned to any domain: Chain "2" 1 - 426 The following residues NOT assigned to any domain: Chain "2" 2 - 37 The following residues NOT assigned to any domain: Chain "2" 0 - 4
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2BPA 3

BACTERIOPHAGE PHIX174 COAT PROTEINS 03-DEC-91 :: BACTERIOPHAGE PHIX174 CAPSID PROTEINS GPF, GPG, GP

DOMAIN 1: 3 2 to 3 37 ; The following residues NOT assigned to any domain: Chain "3" 1 - 426 The following residues NOT assigned to any domain: Chain "3" 1 - 175 The following residues NOT assigned to any domain: Chain "3" 0 - 4
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CBH

HYDROLASE (O-GLYCOSYL) 30-MAY-89 :: C-TERMINAL DOMAIN OF CELLOBIOHYDROLASE I (/CT-CBH$

DOMAIN 1: 1 to 36 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CCY A

ELECTRON TRANSPORT (HEME PROTEIN) 27-AUG-85 :: CYTOCHROME $C(PRIME)

DOMAIN 1: A 2 to A 128 ; The following residues NOT assigned to any domain: Chain "A" 2 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CDV

HEME PROTEIN OF ELECTRON TRANSPORT 15-NOV-83 :: CYTOCHROME $C=3=

DOMAIN 1: 1 to 107 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CPL

ISOMERASE(PEPTIDYL-PROLYL CIS-TRANS) 30-JUN-92 :: CYCLOPHILIN A

DOMAIN 1: 2 to 165 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CRD

NEUROTOXIN 17-FEB-93 :: CHARYBDOTOXIN (NMR, 12 STRUCTURES)

DOMAIN 1: 2 to 37 ; The following residues NOT assigned to any domain: Chain " " 1 - 1
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CRO

GENE REGULATING PROTEIN 08-DEC-88 :: 434 CRO PROTEIN

DOMAIN 1: -1 to 63 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2DPV

PARVOVIRUS COAT PROTEIN 22-JUL-92 :: CANINE PARVOVIRUS, STRAIN D, VIRAL PROTEIN 2

DOMAIN 1: 37 to 584 ; The following residues NOT assigned to any domain: Chain " " 1 - 11
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2ECH

BLOOD COAGULATION INHIBITOR 13-APR-93 :: ECHISTATIN (NMR, 8 STRUCTURES)

DOMAIN 1: 1 to 49 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2GB1

IMMUNOGLOBULIN BINDING PROTEIN 15-MAY-91 :: PROTEIN G (B1 DOMAIN) (/NMR$, RESTRAINED MINIMIZED

DOMAIN 1: 1 to 56 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HIP A

ELECTRON TRANSFER (IRON-SULFUR PROTEIN) 24-JUN-91 :: HIGH POTENTIAL IRON SULFUR PROTEIN (HI/PIP$)

DOMAIN 1: A 1 to A 71 ; The following residues NOT assigned to any domain: Chain "A" 1 - 71
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2IHL

HYDROLASE (O-GLYCOSYL) 29-JUN-93 :: LYSOZYME (E.C.3.2.1.17)

DOMAIN 1: 1 to 36 ; 88 to 129 ; The following residues NOT assigned to any domain: Chain " " 37 - 87
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2ILA

CYTOKINE 01-MAY-91 :: INTERLEUKIN-1*ALPHA (/IL$-1*ALPHA)

DOMAIN 1: 37 to 87 ; The following residues NOT assigned to any domain: Chain " " 5 - 36 Chain " " 88 - 152
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2LAL A

LECTIN 10-JUN-93 :: LENTIL LECTIN

DOMAIN 1: A * to A * ; B * to B * ; The following residues NOT assigned to any domain: Chain "B" 1 - 181 The following residues NOT assigned to any domain: Chain "B" 1 - 47
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MAD L

PRELIMINARY 20-MAY-92 :: METHYLAMINE DEHYDROGENASE (/MADH$) (E.C.1.4.99.3)

DOMAIN 1: L 7 to L 130 ; The following residues NOT assigned to any domain: Chain "L" 1 - 373
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MEV 1

CARDIO PICORNAVIRUS COAT PROTEIN 21-APR-89 :: MENGO ENCEPHALOMYOCARDITIS VIRUS COAT PROTEIN

DOMAIN 1: 1 32 to 1 250 ; The following residues NOT assigned to any domain: Chain "1" 1 - 31 Chain "1" 251 - 268 The following residues NOT assigned to any domain: Chain "1" 8 - 256 The following residues NOT assigned to any domain: Chain "1" 1 - 231 The following residues NOT assigned to any domain: Chain "1" 13 - 70
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MEV 4

CARDIO PICORNAVIRUS COAT PROTEIN 21-APR-89 :: MENGO ENCEPHALOMYOCARDITIS VIRUS COAT PROTEIN

DOMAIN 1: 4 13 to 4 70 ; The following residues NOT assigned to any domain: Chain "4" 1 - 268 The following residues NOT assigned to any domain: Chain "4" 8 - 256 The following residues NOT assigned to any domain: Chain "4" 1 - 231
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MHR

OXYGEN BINDING 20-APR-87 :: MYOHEMERYTHRIN

DOMAIN 1: 1 to 118 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MSB A

LECTIN 28-JUL-92 :: MANNOSE-BINDING PROTEIN A (LECTIN DOMAIN) COMPLEX

DOMAIN 1: A 110 to A 220 ; The following residues NOT assigned to any domain: Chain "A" 109 - 109 The following residues NOT assigned to any domain: Chain "A" 109 - 221
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PF2

PRELIMINARY 08-DEC-91 :: CALCIUM PROTHROMBIN FRAGMENT 1

DOMAIN 1: 1 to 145 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PLV 1

PICORNAVIRUS 17-OCT-89 :: POLIOVIRUS (TYPE 1, MAHONEY STRAIN)

DOMAIN 1: 1 73 to 1 270 ; The following residues NOT assigned to any domain: Chain "1" 6 - 72 Chain "1" 271 - 302 The following residues NOT assigned to any domain: Chain "1" 5 - 272 The following residues NOT assigned to any domain: Chain "1" 1 - 235 The following residues NOT assigned to any domain: Chain "1" 2 - 69
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PLV 3

PICORNAVIRUS 17-OCT-89 :: POLIOVIRUS (TYPE 1, MAHONEY STRAIN)

DOMAIN 1: 3 42 to 3 227 ; The following residues NOT assigned to any domain: Chain "3" 6 - 302 The following residues NOT assigned to any domain: Chain "3" 5 - 272 The following residues NOT assigned to any domain: Chain "3" 1 - 41 Chain "3" 228 - 235 The following residues NOT assigned to any domain: Chain "3" 2 - 69
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2POR

INTEGRAL MEMBRANE PROTEIN PORIN 24-APR-92 :: PORIN (CRYSTAL FORM B)

DOMAIN 1: 1 to 301 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2RN2

HYDROLASE(ENDORIBONUCLEASE) 15-APR-92 :: RIBONUCLEASE H (E.C.3.1.26.4)

DOMAIN 1: 1 to 155 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2SCP A

BINDING PROTEIN 22-AUG-91 :: SARCOPLASMIC CALCIUM-BINDING PROTEIN

DOMAIN 1: A 1 to A 174 ; The following residues NOT assigned to any domain: Chain "A" 1 - 174
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2SN3

PRELIMINARY 20-FEB-92 :: PROTEIN NEUROTOXIN VARIANT-3

DOMAIN 1: 1 to 65 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2STV

VIRUS 08-JUN-84 :: SATELLITE TOBACCO NECROSIS VIRUS

DOMAIN 1: 12 to 195 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2TMV P

VIRUS 15-SEP-88 :: INTACT TOBACCO MOSAIC VIRUS (FIBER DIFFRACTION STU

DOMAIN 1: P 1 to P 154 ; The following residues NOT assigned to any domain: Chain "P" 1 - 3
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3ADK

TRANSFERASE(PHOSPHOTRANSFERASE) 19-NOV-87 :: ADENYLATE KINASE (E.C.2.7.4.3)

DOMAIN 1: 1 to 194 ; The following residues NOT assigned to any domain: Chain " " 0 - 0
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3B5C

ELECTRON TRANSPORT 16-JAN-90 :: CYTOCHROME $B5 (OXIDIZED)

DOMAIN 1: 3 to 88 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3CBH

HYDROLASE (O-GLYCOSYL) 06-AUG-90 :: CELLOBIOHYDROLASE /II$ CORE PROTEIN (E.C.3.2.1.91)

DOMAIN 1: 83 to 447 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3CHY

SIGNAL TRANSDUCTION PROTEIN 22-APR-91 :: CHE*Y

DOMAIN 1: 2 to 129 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3CLA

TRANSFERASE (ACYLTRANSFERASE) 09-JUL-90 :: TYPE /III$ CHLORAMPHENICOL ACETYLTRANSFERASE (/CAT

DOMAIN 1: 6 to 219 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3DFR

OXIDO-REDUCTASE 25-JUN-82 :: DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEX WITH

DOMAIN 1: 1 to 162 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3IL8

PRELIMINARY 07-DEC-90 :: INTERLEUKIN 8

DOMAIN 1: 5 to 72 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3MON A

SWEET-TASTING PROTEIN 26-AUG-92 :: MONELLIN

DOMAIN 1: A 2 to A 45 ; The following residues NOT assigned to any domain: Chain "A" 1 - 50 The following residues NOT assigned to any domain: Chain "A" 2 - 45 The following residues NOT assigned to any domain: Chain "A" 1 - 50 The following residues NOT assigned to any domain: Chain "A" 2 - 45 The following residues NOT assigned to any domain: Chain "A" 1 - 50 The following residues NOT assigned to any domain: Chain "A" 2 - 45 The following residues NOT assigned to any domain: Chain "A" 1 - 50
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3PGM

TRANSFERASE (PHOSPHORYL) 06-APR-82 :: PHOSPHOGLYCERATE MUTASE (E.C.2.7.5.3) DE-PHOSPHO E

DOMAIN 1: 1 to 230 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3RUB S

LYASE(CARBON-CARBON) 25-MAY-90 :: RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE(SLASH)OXYGEN

DOMAIN 1: S 1 to S 123 ; The following residues NOT assigned to any domain: Chain "S" 22 - 467 The following residues NOT assigned to any domain: Chain "S" 468 - 468
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3SC2 A

HYDROLASE(CARBOXYPEPTIDASE) 01-JUL-92 :: SERINE CARBOXYPEPTIDASE II (E.C.3.4.16.1) (CPDW-II

DOMAIN 1: A * to A * ; B * to B * ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3SGB I

COMPLEX(SERINE PROTEINASE-INHIBITOR) 21-JAN-83 :: PROTEINASE B FROM STREPTOMYCES GRISEUS (/SGPB$)

DOMAIN 1: I 7 to I 56 ; The following residues NOT assigned to any domain: Chain "I" 16 - 242
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3SIC I

PRELIMINARY 30-AUG-91 :: SUBTILISIN/BPN$'(PRIME)(E.C.3.4.21.14) COMPLEXED W

DOMAIN 1: I 7 to I 113 ; The following residues NOT assigned to any domain: Chain "I" 1 - 275
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4BLM A

HYDROLASE(ACTING IN CYCLIC AMIDES) 28-MAY-91 :: BETA-*LACTAMASE (E.C.3.5.2.6) (PENICILLINASE)

DOMAIN 1: A 31 to A 291 ; The following residues NOT assigned to any domain: Chain "A" 31 - 291
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4CPA I

HYDROLASE (C-TERMINAL PEPTIDASE) 24-MAR-82 :: CARBOXYPEPTIDASE A=ALPHA= (COX) (E.C.3.4.17.1) COM

DOMAIN 1: I 2 to I 38 ; The following residues NOT assigned to any domain: Chain "I" 1 - 307 The following residues NOT assigned to any domain: Chain "I" 1 - 1
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4FXN

ELECTRON TRANSPORT 16-DEC-77 :: FLAVODOXIN (SEMIQUINONE FORM)

DOMAIN 1: 1 to 138 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4HTC I

HYDROLASE (SERINE PROTEINASE) 25-JUN-93 :: ALPHA-THROMBIN (E.C.3.4.21.5) COMPLEX WITH RECOMBI

DOMAIN 1: I 1 to I 65 ; The following residues NOT assigned to any domain: Chain "I" 1F - 14M The following residues NOT assigned to any domain: Chain "I" 16 - 245
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4SBV A

COAT PROTEIN (VIRAL) 01-APR-85 :: SOUTHERN BEAN MOSAIC VIRUS COAT PROTEIN

DOMAIN 1: A 62 to A 260 ; The following residues NOT assigned to any domain: Chain "A" 62 - 260 The following residues NOT assigned to any domain: Chain "A" 39 - 260
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4SGB I

COMPLEX(SERINE PROTEINASE-INHIBITOR) 21-SEP-89 :: SERINE PROTEINASE B COMPLEX WITH THE POTATO INHIBI

DOMAIN 1: I 1 to I 51 ; The following residues NOT assigned to any domain: Chain "I" 16 - 243
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4TGF

GROWTH FACTOR 13-JUN-90 :: DES-VAL==1==,VAL==2==-TRANSFORMING GROWTH FACTOR A

DOMAIN 1: 1 to 50 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5NN9

HYDROLASE(O-GLYCOSYL) 28-MAR-91 :: NEURAMINIDASE N9 (E.C.3.2.1.18) (SIALIDASE) (MUTAN

DOMAIN 1: 82 to 468 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5P21

ONCOGENE PROTEIN 30-APR-90 :: $C-*H-RAS $P21 PROTEIN (AMINO ACIDS 1 - 166) COMPL

DOMAIN 1: 1 to 166 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5TGL

PRELIMINARY 30-OCT-91 :: TRIACYLGLYCEROL ACYLHYDROLASE (EC 3.1.1.3) WITH IN

DOMAIN 1: E 5 to E 269 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7API A

PROTEINASE INHIBITOR 08-SEP-88 :: MODIFIED ALPHA=1=-*ANTITRYPSIN

DOMAIN 1: A * to A * ; B * to B * ; The following residues NOT assigned to any domain: Chain "B" 395 - 395
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8I1B

CYTOKINE 29-JAN-91 :: INTERLEUKIN 1-*BETA

DOMAIN 1: 5 to 151 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8RXN A

ELECTRON TRANSPORT(IRON) 26-AUG-91 :: RUBREDOXIN

DOMAIN 1: A 1 to A 52 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

9RNT

HYDROLASE(ENDORIBONUCLEASE) 25-SEP-91 :: RIBONUCLEASE T=1= (E.C.3.1.27.3) COMPLEX WITH CA==

DOMAIN 1: 1 to 104 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3AAH A

OXIDOREDUCTASE(PQQ(A)-CHOH(D)) 13-OCT-93 :: METHANOL DEHYDROGENASE (E.C.1.1.99.8) (MEDH)

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 1 - 57 The following residues NOT assigned to any domain: Chain "A" 1 - 571 The following residues NOT assigned to any domain: Chain "A" 1 - 57
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BNH

RIBONUCLEASE INHIBITOR 20-JAN-94 :: RIBONUCLEASE INHIBITOR

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 456
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ALK A

ALKALINE PHOSPHATASE 03-MAR-93 :: ALKALINE PHOSPHATASE (E.C.3.1.3.1)

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 1 - 449
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CEL A

HYDROLASE(O-GLYCOSYL) 17-MAY-94 :: 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE I (CELLULASE)

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 1 - 434
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1OYB

OXIDOREDUCTASE(FLAVOPROTEIN) 25-AUG-94 :: OLD YELLOW ENZYME (OXIDIZED) (OYE) (E.C.1.6.99.1)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 399
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2SIL

HYDROLASE 13-JUL-94 :: SIALIDASE (E.C.3.2.1.18) (NEURAMINIDASE)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 2 - 382
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PEC

LYASE(ACTING ON POLYSACCHARIDES) 06-APR-93 :: PECTATE LYASE C (PLC) (E.C.4.2.2.2)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 352
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ADD

HYDROLASE(ACTING IN CYCLICAMIDINES) 22-DEC-92 :: ADENOSINE DEAMINASE (E.C.3.5.4.4) COMPLEXED WITH

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 4 - 352
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HLE A

HYDROLASE(SERINE PROTEINASE-INHIBITOR) 13-APR-92 :: HORSE LEUCOCYTE ELASTASE INHIBITOR (HLEI)

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 361 - 391
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3BCL

EXCITATION ENERGY TRANSFER 29-JUN-87 :: BACTERIOCHLOROPHYLL-A PROTEIN

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 3 - 358
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TCA

HYDROLASE(CARBOXYLIC ESTERASE) 28-FEB-94 :: LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 317
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2BBV A

COMPLEX(VIRUS COAT PROTEIN/RNA) 06-JUN-94 :: BLACK BEETLE VIRUS CAPSID PROTEIN (BBV) COMPLEXED

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 364 - 379 The following residues NOT assigned to any domain: Chain "A" 56 - 363 The following residues NOT assigned to any domain: Chain "A" 364 - 379 The following residues NOT assigned to any domain: Chain "A" 20 - 363 The following residues NOT assigned to any domain: Chain "A" 364 - 379 The following residues NOT assigned to any domain: Chain "A" 1 - 10
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GHR

HYDROLASE 11-OCT-93 :: 1,3-1,4-BETA-GLUCANASE (E.C.3.2.1.73)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 306
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AMP

HYDROLASE(AMINOPEPTIDASE) 22-APR-94 :: AMINOPEPTIDASE (AEROMONAS PROTEOLYTICA) (E.C.3.4.1

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 291
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NAR

PLANT SEED PROTEIN 10-SEP-93 :: NARBONIN

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 289
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PRN

INTEGRAL MEMBRANE PROTEIN PORIN 13-JUL-94 :: PORIN

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 289
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TML

BETA-AMYLASE 08-JUN-93 :: ENDO-1,4-BETA-D-GLUCANASE (E.C.3.2.1.4)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 286
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2TMA A

CONTRACTILE SYSTEM PROTEIN 16-SEP-87 :: TROPOMYOSIN

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 1 - 284
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1YPT A

HYDROLASE 16-SEP-94 :: PROTEIN-TYROSINE PHOSPHATASE (YERSINIA) (E.C.3.1.3

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 189 - 468
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HNP

HYDROLASE(PHOSPHORYLATION) 19-SEP-94 :: PROTEIN-TYROSINE PHOSPHATASE 1B (HUMAN) (E.C.3.1.3

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 5 - 282
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3TGL

HYDROLASE(CARBOXYLIC ESTERASE) 29-JUL-91 :: TRIACYLGLYCEROL ACYLHYDROLASE (E.C.3.1.1.3)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 5 - 269
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NBA A

HYDROLASE(IN LINEAR AMIDES) 18-MAY-92 :: N-CARBAMOYLSARCOSINE AMIDOHYDROLASE (E.C.3.5.1.59)

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 8 - 259 The following residues NOT assigned to any domain: Chain "A" 7 - 259 The following residues NOT assigned to any domain: Chain "A" 7 - 259
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HSD A

OXIDOREDUCTASE 28-MAR-94 :: 3 ALPHA, 20 BETA-HYDROXYSTEROID DEHYDROGENASE (HOL

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 2 - 255 The following residues NOT assigned to any domain: Chain "A" 2 - 255 The following residues NOT assigned to any domain: Chain "A" 2 - 255
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LEC

PRELIMINARY 17-DEC-92 :: FOURTH LECTIN ISOLATED FROM GRIFFONIA SIMPLICIFOLI

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 243
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PCD M

DIOXYGENASE 21-JUN-94 :: PROTOCATECHUATE 3,4-DIOXYGENASE (E.C.1.13.11.3)

DOMAIN 1: M 347 to M 530 ; The following residues NOT assigned to any domain: Chain "M" 1 - 200 The following residues NOT assigned to any domain: Chain "M" 301 - 346 Chain "M" 531 - 536 The following residues NOT assigned to any domain: Chain "M" 1 - 200 The following residues NOT assigned to any domain: Chain "M" 301 - 536 The following residues NOT assigned to any domain: Chain "M" 1 - 200 The following residues NOT assigned to any domain: Chain "M" 301 - 536 The following residues NOT assigned to any domain: Chain "M" 1 - 200 The following residues NOT assigned to any domain: Chain "M" 301 - 536 The following residues NOT assigned to any domain: Chain "M" 1 - 200 The following residues NOT assigned to any domain: Chain "M" 301 - 536 The following residues NOT assigned to any domain: Chain "M" 1 - 200 The following residues NOT assigned to any domain: Chain "M" 301 - 536
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ENG

HYDROLASE(GLYCOSIDASE) 25-MAR-93 :: ENDOGLUCANASE V (E.C.3.2.1.4)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 213
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1STO

PHOSPHORIBOSYLTRANSFERASE 20-DEC-93 :: OROTATE PHOSPHORIBOSYLTRANSFERASE (OPRTASE) (E.C.2

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 213
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1THV

SWEET TASTING PROTEIN 10-JUN-94 :: THAUMATIN ISOFORM A (ORTHORHOMBIC CRYSTAL FORM)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 207
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SAC A

AMYLOID PROTEIN 27-JAN-94 :: SERUM AMYLOID P COMPONENT (SAP)

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 1 - 204 The following residues NOT assigned to any domain: Chain "A" 1 - 204 The following residues NOT assigned to any domain: Chain "A" 1 - 204 The following residues NOT assigned to any domain: Chain "A" 1 - 204
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PCD A

DIOXYGENASE 21-JUN-94 :: PROTOCATECHUATE 3,4-DIOXYGENASE (E.C.1.13.11.3)

DOMAIN 1: A 15 to A 200 ; The following residues NOT assigned to any domain: Chain "A" 1 - 14 The following residues NOT assigned to any domain: Chain "A" 301 - 536 The following residues NOT assigned to any domain: Chain "A" 1 - 200 The following residues NOT assigned to any domain: Chain "A" 301 - 536 The following residues NOT assigned to any domain: Chain "A" 1 - 200 The following residues NOT assigned to any domain: Chain "A" 301 - 536 The following residues NOT assigned to any domain: Chain "A" 1 - 200 The following residues NOT assigned to any domain: Chain "A" 301 - 536 The following residues NOT assigned to any domain: Chain "A" 1 - 200 The following residues NOT assigned to any domain: Chain "A" 301 - 536 The following residues NOT assigned to any domain: Chain "A" 1 - 200 The following residues NOT assigned to any domain: Chain "A" 301 - 536
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CUT

COMPLEX(SERINE ESTERASE/INHIBITOR) 03-JUN-94 :: CUTINASE (E.C.3.1.1.-) COMPLEXED WITH THE INHIBITO

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 15 - 212
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1COL A

ANTIBACTERIAL PROTEIN 06-JUL-91 :: COLICIN *A (C-TERMINAL DOMAIN) (PORE-FORMING DOMAI

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 5 - 201
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8DFR

OXIDOREDUCTASE(CHNH(D)-NAD+ OR NADP+(A))30-MAY-89 :: DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 186
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BCX

HYDROLASE(XYLAN DEGRADATION) 01-APR-94 :: XYLANASE (INACTIVE FORM, ENDO-BETA-1,4-XYLANASE)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 185
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BMV 1

VIRUS 09-OCT-89 :: BEAN POD MOTTLE VIRUS (MIDDLE COMPONENT)

DOMAIN 1: 1 * to 1 * ; The following residues NOT assigned to any domain: Chain "1" 3001 - 2192 The following residues NOT assigned to any domain: Chain "1" 1 - 11
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GP1 A

OXIDOREDUCTASE(H2O2(A)) 11-JUN-85 :: GLUTATHIONE PEROXIDASE (E.C.1.11.1.9)

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 10 - 194
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IGP

ACID ANHYDRIDE HYDROLASE 01-AUG-94 :: INORGANIC PYROPHOSPHATASE (E.C.3.6.1.1)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CLH

ISOMERASE(PEPTIDYL-PROLYL CIS-TRANS) 20-DEC-93 :: CYCLOPHILIN (NMR, 12 STRUCTURES)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 166
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HUW

HORMONE 22-SEP-93 :: HUMAN GROWTH HORMONE MUTANT WITH PHE 10 REPLACED B

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 191
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1VMO A

MEMBRANE PROTEIN 06-JAN-94 :: VITELLINE MEMBRANE OUTER LAYER PROTEIN I

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 1 - 163
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EPA A

RETINOIC ACID-BINDING PROTEIN 15-JUN-93 :: EPIDIDYMAL RETINOIC ACID-BINDING PROTEIN

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 1 - 164
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DHI A

OXIDOREDUCTASE 29-OCT-93 :: DIHYDROFOLATE REDUCTASE (DHFR) (E.C.1.5.1.3) MUTAN

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 1 - 159
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BCF A

IRON STORAGE AND ELECTRON TRANSPORT 06-DEC-93 :: BACTERIOFERRITIN (CYTOCHROME B1)

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 1 - 158
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BVH

HYDROLASE 03-MAY-94 :: TYROSINE PHOSPHATASE (E.C.3.1.3.2) (ORTHOPHOSPHORI

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 157
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HLB

OXYGEN TRANSPORT 22-MAR-94 :: HEMOGLOBIN (SEA CUCUMBER)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 0 - 157
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AEP

LIPOPROTEIN 30-NOV-92 :: APOLIPOPHORIN III

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 6 - 158
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LH1

OXYGEN TRANSPORT 23-APR-82 :: LEGHEMOGLOBIN (ACETATE,MET)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2LHB

OXYGEN TRANSPORT 16-AUG-85 :: HEMOGLOBIN V (CYANO,MET)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 149
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HMC A

MACROPHAGE COLONY STIMULATING FACTOR 22-DEC-93 :: HUMAN MACROPHAGE COLONY STIMULATING FACTOR

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 4 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HBG

OXYGEN TRANSPORT 11-FEB-91 :: HEMOGLOBIN (CARBON MONOXY)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 147
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MTA C

ELECTRON TRANSPORT 26-OCT-93 :: METHYLAMINE DEHYDROGENASE (E.C.1.4.99.3) COMPLEX W

DOMAIN 1: C * to C * ; The following residues NOT assigned to any domain: Chain "C" 1 - 373 The following residues NOT assigned to any domain: Chain "C" 7 - 131 The following residues NOT assigned to any domain: Chain "C" 1 - 105
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4FX2

ELECTRON TRANSPORT 17-OCT-91 :: FLAVODOXIN (LOW TEMPERATURE (-150 C), REDUCED FORM

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 2 - 148
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LBA

HYDROLASE(ACTING ON LINEAR AMIDES) 22-DEC-93 :: LYSOZYME (E.C.3.5.1.28) MUTANT WITH ALA 6 REPLACED

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 150
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4MBA

OXYGEN STORAGE 22-FEB-89 :: MYOGLOBIN (IMIDAZOLE COMPLEX) ($P*H 7.0)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 0 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2IRT A

SIGNAL PROTEIN 13-JUL-94 :: INTERLEUKIN-1 RECEPTOR ANTAGONIST PROTEIN

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 8 - 152
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3SDH A

OXYGEN TRANSPORT 23-JUN-93 :: HEMOGLOBIN I (HOMODIMER) (CARBON-MONOXY)

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 2 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2NCK R

PHOSPHOTRANSFERASE(PO4 AS ACCEPTOR) 15-NOV-93 :: NUCLEOSIDE DIPHOSPHATE KINASE (E.C.2.7.4.6)

DOMAIN 1: R * to R * ; The following residues NOT assigned to any domain: Chain "R" 2 - 144
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FLP

OXYGEN TRANSPORT 16-MAY-94 :: HEMOGLOBIN I (MONOMERIC) (FERRIC)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 142
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2ASR

CHEMOTAXIS 23-AUG-94 :: ASPARTATE RECEPTOR (LIGAND BINDING DOMAIN)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 38 - 179
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ITH A

OXYGEN TRANSPORT 03-DEC-91 :: HEMOGLOBIN (CYANOMET)

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 1 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2BTF P

ACETYLATION AND ACTIN-BINDING 18-JAN-94 :: BETA-ACTIN-PROFILIN COMPLEX

DOMAIN 1: P * to P * ; The following residues NOT assigned to any domain: Chain "P" 0 - 375
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2END

ENDONUCLEASE 08-AUG-94 :: ENDONUCLEASE V (E.C.3.1.25.1)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 2 - 138
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SLT B

LECTIN 20-OCT-93 :: S-LECTIN (A VERTEBRATE 14 KDA BETA-GALACTOSIDE BIN

DOMAIN 1: B * to B * ; The following residues NOT assigned to any domain: Chain "B" 2 - 134
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LIS

FERTILIZATION PROTEIN 29-JUN-93 :: LYSIN

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 4 - 134
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1VIL

ACTIN-BINDING PROTEIN 20-OCT-93 :: VILLIN (DOMAIN ONE COMPRISING RESIDUES 1 - 126) (A

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 126
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ACF

ACTIN-BINDING PROTEIN 29-JUL-94 :: PROFILIN I

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 125
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HRH A

HYDROLASE(ENDORIBONUCLEASE) 06-MAR-91 :: RIBONUCLEASE H DOMAIN OF /HIV-1$ REVERSE TRANSCRIP

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 427 - 554
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3INK C

CYTOKINE 09-DEC-92 :: INTERLEUKIN 2 MUTANT WITH CYS 125 REPLACED BY ALA

DOMAIN 1: C * to C * ; The following residues NOT assigned to any domain: Chain "C" 6 - 133
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PTS A

GLYCOPROTEIN 23-JUL-92 :: STREPTAVIDIN COMPLEX WITH THE PEPTIDE (FSHPQNT)

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 13 - 133 The following residues NOT assigned to any domain: Chain "A" 1 - 3
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HCD

ACTIN BINDING 03-MAY-94 :: HISACTOPHILIN (NMR, 1 STRUCTURE)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 118
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2RSL A

SITE-SPECIFIC RECOMBINASE 08-SEP-93 :: GAMMA DELTA RESOLVASE (LARGE FRAGMENT, CATALYTIC D

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 1 - 120 The following residues NOT assigned to any domain: Chain "A" 1 - 119
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2RSP A

HYDROLASE(ASPARTYL PROTEINASE) 17-OCT-89 :: ROUS SARCOMA VIRUS PROTEASE (/RSV PR$)

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 1 - 124
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CHS A

ISOMERASE 08-APR-94 :: CHORISMATE MUTASE (E.C.5.4.99.5)

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 2 - 115 The following residues NOT assigned to any domain: Chain "A" 2 - 115 The following residues NOT assigned to any domain: Chain "A" 2 - 115 The following residues NOT assigned to any domain: Chain "A" 2 - 115 The following residues NOT assigned to any domain: Chain "A" 2 - 115 The following residues NOT assigned to any domain: Chain "A" 2 - 115 The following residues NOT assigned to any domain: Chain "A" 2 - 115 The following residues NOT assigned to any domain: Chain "A" 2 - 115 The following residues NOT assigned to any domain: Chain "A" 2 - 115 The following residues NOT assigned to any domain: Chain "A" 2 - 115 The following residues NOT assigned to any domain: Chain "A" 2 - 115
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MCM

APOPROTEIN 08-MAY-91 :: MACROMOMYCIN

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 112
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HCN B

HORMONE 01-JUL-94 :: HUMAN CHORIONIC GONADOTROPIN

DOMAIN 1: B * to B * ; The following residues NOT assigned to any domain: Chain "B" 5 - 89
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AB2

TRANSFERASE(PHOSPHOTRANSFERASE) 19-JUL-93 :: PROTO-ONCOGENE TYROSINE KINASE (E.C.2.7.1.112)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 109
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5PAL

CALCIUM-BINDING PROTEIN 25-SEP-91 :: PARVALBUMIN (ALPHA LINEAGE)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 109
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BRN L

ENDONUCLEASE 15-NOV-93 :: BARNASE (G SPECIFIC ENDONUCLEASE) (E.C.3.1.27.-) C

DOMAIN 1: L * to L * ; The following residues NOT assigned to any domain: Chain "L" 3 - 110 The following residues NOT assigned to any domain: Chain "L" 1 - 4 The following residues NOT assigned to any domain: Chain "L" 1 - 4
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CEW I

PROTEINASE INHIBITOR(CYSTEINE) 21-APR-93 :: CYSTATIN

DOMAIN 1: I * to I * ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4CPV

CALCIUM BINDING 18-OCT-89 :: CALCIUM-BINDING PARVALBUMIN ($P*I=4.25)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 0 - 108
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BET

GROWTH FACTOR 08-APR-93 :: BETA-NERVE GROWTH FACTOR

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 10 - 116
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FKB

ISOMERASE 02-JUL-92 :: FK506 BINDING PROTEIN (FKBP) COMPLEX WITH IMMUNOSU

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 107
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2SPC A

CYTOSKELETON 01-MAR-94 :: SPECTRIN (ONE REPEAT UNIT)

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 0 - 106
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HKS

TRANSCRIPTION REGULATION 18-JUL-94 :: HEAT SHOCK TRANSCRIPTION FACTOR

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 43 - 148
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PUT

ELECTRON TRANSPORT 09-JUL-94 :: PUTIDAREDOXIN (NMR, 12 STRUCTURES)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 106
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CDB

T LYMPHOCYTE ADHESION GLYCOPROTEIN 15-SEP-93 :: CD2 (T LYMPHOCYTE GLYCOPROTEIN, ADHESION DOMAIN)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 105
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3TRX

ELECTRON TRANSPORT 17-DEC-90 :: THIOREDOXIN (REDUCED FORM)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 105
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MYP A

MYELOPEROXIDASE 15-APR-92 :: MYELOPEROXIDASE (E.C.1.11.1.7)

DOMAIN 1: A * to A * ; C * to C * ; The following residues NOT assigned to any domain: Chain "C" 1 - 104 The following residues NOT assigned to any domain: Chain "C" 114 - 575
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ONC

PANCREATIC RIBONUCLEASE 30-AUG-93 :: P-30 PROTEIN

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PNA

SIGNALLING PROTEIN 30-JUN-92 :: PHOSPHATIDYLINOSITOL 3-KINASE (E.C.2.7.1.137) (N-T

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 17 - 120
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AYA A

HYDROLASE(SH2 DOMAIN) 15-MAY-94 :: TYROSINE PHOSPHATASE SYP (N-TERMINAL SH2 DOMAIN)

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" -3 - 5 The following residues NOT assigned to any domain: Chain "A" 3 - 103 The following residues NOT assigned to any domain: Chain "A" -2 - 5
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HSB B

HISTOCOMPATIBILITY ANTIGEN 30-MAR-93 :: CLASS I HISTOCOMPATIBILITY ANTIGEN AW68.1 (LEUCOCY

DOMAIN 1: B * to B * ; The following residues NOT assigned to any domain: Chain "B" 1 - 270 The following residues NOT assigned to any domain: Chain "B" 1 - 3 The following residues NOT assigned to any domain: Chain "B" 1 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PND

ELECTRON TRANSPORT 22-SEP-93 :: PLASTOCYANIN (EREF REFINEMENT)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1STF I

HYDROLASE(SULFHYDRYL PROTEINASE) 21-APR-93 :: PAPAIN (CYS 25 CARBOXYMETHYLATED) (E.C.3.4.22.2) C

DOMAIN 1: I * to I * ; The following residues NOT assigned to any domain: Chain "I" 1 - 212
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RIS

RIBOSOMAL PROTEIN 31-MAY-94 :: RIBOSOMAL PROTEIN S6

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 97
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SXL

RNA-BINDING PROTEIN 01-JUL-94 :: SEX-LETHAL PROTEIN (C-TERMINUS, OR SECOND RNA-BIND

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 97
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MLI

INTRAMOLECULAR OXIDOREDUCTASE 02-NOV-89 :: MUCONOLACTONE ISOMERASE (E.C.5.3.3.4)

DOMAIN 1: 1 to 86 ; The following residues NOT assigned to any domain: Chain " " 87 - 96
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ADN

TRANSCRIPTION REGULATION 30-SEP-93 :: N-ADA 10 (DNA METHYLPHOSPHOTRIESTER REPAIR DOMAIN,

DOMAIN 1: 5 to 78 ; The following residues NOT assigned to any domain: Chain " " 1 - 4 Chain " " 79 - 92
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FNA

CELL ADHESION PROTEIN 11-JAN-94 :: FIBRONECTIN CELL-ADHESION MODULE TYPE III-10

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 6 - 96
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BRS F

ENDONUCLEASE 11-MAR-94 :: BARNASE (G SPECIFIC ENDONUCLEASE) (E.C.3.1.27.-) C

DOMAIN 1: F * to F * ; The following residues NOT assigned to any domain: Chain "F" 3 - 110 The following residues NOT assigned to any domain: Chain "F" 1 - 110 The following residues NOT assigned to any domain: Chain "F" 3 - 110 The following residues NOT assigned to any domain: Chain "F" 1 - 89 The following residues NOT assigned to any domain: Chain "F" 2 - 89
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LLI A

TRANSCRIPTION REGULATION PROTEIN/DNA 25-MAR-94 :: LAMBDA REPRESSOR MUTANT WITH VAL 36 REPLACED BY LE

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 1 - 92 The following residues NOT assigned to any domain: Chain "A" 1 - 20 The following residues NOT assigned to any domain: Chain "A" 1 - 20
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PDG A

GROWTH FACTOR 14-JUL-92 :: PLATELET-DERIVED GROWTH FACTOR BB

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 7 - 100 The following residues NOT assigned to any domain: Chain "A" 7 - 102
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PNJ

PHOSPHOTRANSFERASE 19-JUL-93 :: PHOSPHATIDYLINOSITOL 3-KINASE (P85-ALPHA SUBUNIT,

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1A - 84
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2ABD

ACYL-COENZYME A BINDING PROTEIN 05-MAR-93 :: ACYL-COENZYME A BINDING PROTEIN (ACBP)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 86
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BGH

DNA-BINDING PROTEIN 03-AUG-93 :: GENE V PROTEIN (SINGLE-STRANDED DNA BINDING PROTEI

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 2 - 86
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GRX

ELECTRON TRANSPORT 01-OCT-93 :: GLUTAREDOXIN MUTANT WITH CYS 14 REPLACED BY SER (C

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 85
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HCN A

HORMONE 01-JUL-94 :: HUMAN CHORIONIC GONADOTROPIN

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 2 - 111
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HIP

ELECTRON TRANSFER (IRON-SULFUR PROTEIN) 01-APR-75 :: OXIDIZED HIGH POTENTIAL IRON PROTEIN (HIPIP).

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 85
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LPB A

HYDROLASE(CARBOXYLIC ESTERASE) 19-AUG-94 :: LIPASE (E.C.3.1.1.3) COMPLEXED WITH COLIPASE AND I

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 1 - 449
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1POH

PHOSPHOTRANSFERASE 19-OCT-93 :: PHOSPHOTRANSFERASE (HISTIDINE-CONTAINING PHOSPHOCA

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 85
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2BOP A

TRANSCRIPTION REGULATION 13-JAN-94 :: BOVINE PAPILLOMAVIRUS-1 E2 (DNA-BINDING DOMAIN)

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 1 - 17
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CC5

ELECTRON TRANSPORT (HEME PROTEIN) 10-AUG-84 :: CYTOCHROME C=5= (OXIDIZED)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 5 - 87
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

451C

ELECTRON TRANSPORT 20-JUL-81 :: CYTOCHROME $C=551= (REDUCED)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 82
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PBA

HYDROLASE(C-TERMINAL PEPTIDASE) 18-NOV-91 :: PROCARBOXYPEPTIDASE B (E.C.3.4.17.2) (ACTIVATION D

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 81
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PYA A

PRELIMINARY 18-DEC-92 :: PYRUVOYL-DEPENDENT HISTIDINE DECARBOXYLASE (L-HIST

DOMAIN 1: A * to A * ; B * to B * ; The following residues NOT assigned to any domain: Chain "B" 1 - 81 The following residues NOT assigned to any domain: Chain "B" 83 - 310 The following residues NOT assigned to any domain: Chain "B" 1 - 81 The following residues NOT assigned to any domain: Chain "B" 83 - 310
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RIP

RIBOSOMAL PROTEIN 17-AUG-93 :: RIBOSOMAL PROTEIN S17 (NMR, 6 STRUCTURES)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 5 - 85
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2FXB

ELECTRON TRANSPORT 08-FEB-90 :: FERREDOXIN

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 81
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LAB

TRANSFERASE (ACYLTRANSFERASE) 02-SEP-92 :: DIHYDROLIPOAMIDE ACETYLTRANSFERASE (E2P) (E.C.2.3.

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 80
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1C53

ELECTRON TRANSPORT 26-AUG-91 :: CYTOCHROME C553

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 79
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FLX

FELIX 08-AUG-90 :: FELIX (DE NOVO DESIGNED PROTEIN) (MODEL 1) (THEORE

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 79
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PK4

HYDROLASE(SERINE PROTEASE) 18-JUL-91 :: PLASMINOGEN KRINGLE 4

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 0 - 80
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PTL

BINDING PROTEIN(IMMUNOGLOBULIN L CHAIN) 12-AUG-94 :: PROTEIN L (B1 DOMAIN) (NMR, 21 STRUCTURES)

DOMAIN 1: 17 to 78 ; The following residues NOT assigned to any domain: Chain " " 1 - 16
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ACP

FATTY ACID SYNTHESIS PROTEIN 29-JUL-90 :: ACYL CARRIER PROTEIN (NMR, 2 STRUCTURES)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 77
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HME

DNA-BINDING 10-FEB-94 :: HIGH MOBILITY GROUP PROTEIN FRAGMENT-B (HMGB) (DNA

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 77
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LFB

TRANSCRIPTION REGULATION 28-JUN-93 :: TRANSCRIPTION FACTOR LFB1 (HOMEODOMAIN)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 13 - 90
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ADR

TRANSCRIPTION REGULATION 19-JUL-93 :: P22 C2 REPRESSOR (AMINO-TERMINAL DNA-BINDING DOMAI

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 76
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1UBI

CHROMOSOMAL PROTEIN 03-FEB-94 :: UBIQUITIN

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 76
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HYP

HYDROPHOBIC SEED PROTEIN 05-FEB-93 :: HYDROPHOBIC PROTEIN FROM SOYBEAN

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 6 - 80
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TVS

TRANSCRIPTION REGULATION 14-SEP-94 :: TRANSACTIVATOR PROTEIN (TAT) (TAT EIAVY) (NMR, 8 S

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 75
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HOE

GLYCOSIDASE INHIBITOR 27-JAN-89 :: ALPHA-*AMYLASE INHIBITOR HOE-467*A

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 74
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HST A

CHROMOSOMAL PROTEIN 30-MAR-93 :: HISTONE H5 (GLOBULAR DOMAIN)

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 24 - 97
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HMA

DNA-BINDING 12-MAY-94 :: HMG-D (HMG-BOX DOMAIN, RESIDUES 2 - 74) (NMR, 20 S

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 2 - 74
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LEA

TRANSCRIPTION REGULATION 11-MAY-94 :: LEXA REPRESSOR DNA BINDING DOMAIN

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 72
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HPI

ELECTRON TRANSFER(IRON-SULFUR PROTEIN) 09-DEC-93 :: HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM ECTOTHIORH

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 71
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HSQ

PHOSPHORIC DIESTER HYDROLASE 13-JUN-94 :: PHOSPHOLIPASE C-GAMMA (SH3 DOMAIN) (E.C.3.1.4.11)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 71
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1POU

DNA-BINDING PROTEIN 14-JUN-93 :: OCT-1 (POU-SPECIFIC DOMAIN) (NMR, 20 STRUCTURES)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 5 - 75
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ERG

COMPLEMENT FACTOR 13-DEC-93 :: HUMAN COMPLEMENT REGULATORY PROTEIN CD59 (EXTRACEL

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 70
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HUM A

CYTOKINE(CHEMOTACTIC) 31-JAN-94 :: HUMAN MACROPHAGE INFLAMMATORY PROTEIN 1 BETA (HMIP

DOMAIN 1: A 10 to A 69 ; The following residues NOT assigned to any domain: Chain "A" 1 - 9 The following residues NOT assigned to any domain: Chain "A" 1 - 69
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MJC

TRANSCRIPTION REGULATION 18-MAR-94 :: MAJOR COLD SHOCK PROTEIN 7.4 (CSPA (CS 7.4)) OF

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 2 - 70
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CHC

VIRUS 02-FEB-94 :: EQUINE HERPES VIRUS-1 (C3HC4, OR RING DOMAIN)

DOMAIN 1: 4 to 59 ; The following residues NOT assigned to any domain: Chain " " 1 - 3 Chain " " 60 - 68
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CTF

RIBOSOMAL PROTEIN 02-SEP-86 :: L7(SLASH)*L12 50 S RIBOSOMAL PROTEIN (C-TERMINAL D

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 53 - 120
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MDY A

TRANSCRIPTION ACTIVATION/DNA 09-JUN-94 :: MYOD BASIC-HELIX-LOOP-HELIX (BHLH) DOMAIN

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 105 - 166 The following residues NOT assigned to any domain: Chain "A" 105 - 166 The following residues NOT assigned to any domain: Chain "A" 105 - 166 The following residues NOT assigned to any domain: Chain "A" 1 - 14 The following residues NOT assigned to any domain: Chain "A" 1 - 14 The following residues NOT assigned to any domain: Chain "A" 1 - 14 The following residues NOT assigned to any domain: Chain "A" 1 - 14
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HRE

GROWTH FACTOR 21-JUL-94 :: HEREGULIN-ALPHA (EPIDERMAL GROWTH FACTOR-LIKE DOMA

DOMAIN 1: 175 to 226 ; The following residues NOT assigned to any domain: Chain " " 227 - 241
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MNT A

TRANSCRIPTION REGULATION 28-JUN-94 :: MNT REPRESSOR MUTANT WITH C-TERMINAL RESIDUES DELE

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 1 - 66
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4CRO A

GENE REGULATING PROTEIN 07-SEP-90 :: CRO REPRESSOR

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 3 - 66 The following residues NOT assigned to any domain: Chain "A" 3 - 66 The following residues NOT assigned to any domain: Chain "A" 3 - 66 The following residues NOT assigned to any domain: Chain "A" 3 - 66 The following residues NOT assigned to any domain: Chain "A" 3 - 66 The following residues NOT assigned to any domain: Chain "A" 2 - 17 The following residues NOT assigned to any domain: Chain "A" 2 - 17 The following residues NOT assigned to any domain: Chain "A" 2 - 17 The following residues NOT assigned to any domain: Chain "A" 2 - 17 The following residues NOT assigned to any domain: Chain "A" 2 - 17 The following residues NOT assigned to any domain: Chain "A" 2 - 17
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ATA

PROTEINASE INHIBITOR(TRYPSIN) 20-MAY-94 :: TRYPSIN INHIBITOR (PH 4.75)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 62
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GAT A

TRANSCRIPTION REGULATION 28-JUN-93 :: ERYTHROID TRANSCRIPTION FACTOR GATA-1 (ZINC-CONTAI

DOMAIN 1: A 1 to A 51 ; The following residues NOT assigned to any domain: Chain "A" 52 - 60 The following residues NOT assigned to any domain: Chain "A" 106 - 127
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SCM A

CALCIUM-BINDING PROTEIN 06-JAN-94 :: MYOSIN (REGULATORY DOMAIN)

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 12 - 149 The following residues NOT assigned to any domain: Chain "A" 4 - 152
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TAP

PROTEINASE INHIBITOR 16-AUG-94 :: FACTOR XA INHIBITOR (NMR, 20 STRUCTURES)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 60
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GFC

ADAPTOR PROTEIN CONTAINING SH2 AND SH3 13-JUN-94 :: GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2 (GRB2)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 59
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CSK A

PHOSPHOTRANSFERASE 22-MAR-94 :: C-SRC KINASE (SH3 DOMAIN) (E.C.2.7.1.112)

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 11 - 68 The following residues NOT assigned to any domain: Chain "A" 11 - 68 The following residues NOT assigned to any domain: Chain "A" 11 - 68
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FXD

ELECTRON TRANSFER(IRON-SULFUR) 08-APR-91 :: FERREDOXIN II

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 58
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SHG

CYTOSKELETON 19-MAY-93 :: ALPHA SPECTRIN (SH3 DOMAIN)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 6 - 62
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3AAH B

OXIDOREDUCTASE(PQQ(A)-CHOH(D)) 13-OCT-93 :: METHANOL DEHYDROGENASE (E.C.1.1.99.8) (MEDH)

DOMAIN 1: B * to B * ; The following residues NOT assigned to any domain: Chain "B" 1 - 571 The following residues NOT assigned to any domain: Chain "B" 1 - 571 The following residues NOT assigned to any domain: Chain "B" 1 - 57
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HPT

SERINE PROTEASE INHIBITOR 27-MAR-92 :: HUMAN PANCREATIC SECRETORY TRYPSIN INHIBITOR VARIA

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 56
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HCR A

DNA-BINDING 17-DEC-93 :: HIN RECOMBINASE (DNA-BINDING DOMAIN) COMPLEXED WIT

DOMAIN 1: A 139 to A 182 ; The following residues NOT assigned to any domain: Chain "A" 183 - 190 The following residues NOT assigned to any domain: Chain "A" 2 - 15 The following residues NOT assigned to any domain: Chain "A" 17 - 29
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PAR A

GENE-REGULATING PROTEIN 22-MAR-94 :: ARC REPRESSOR AND A SYNTHETIC 22-MER DNA (21 BASE-

DOMAIN 1: A * to A * ; B * to B * ; The following residues NOT assigned to any domain: Chain "B" 1 - 50 The following residues NOT assigned to any domain: Chain "B" 1 - 53 The following residues NOT assigned to any domain: Chain "B" 1 - 22 The following residues NOT assigned to any domain: Chain "B" 1 - 22
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LCC A

GENE-REGULATING PROTEIN 25-MAR-93 :: LAC REPRESSOR ("HEADPIECE") COMPLEX WITH AN 11 BAS

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 1 - 11 The following residues NOT assigned to any domain: Chain "A" 1 - 11
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IFD

VIRUS 16-FEB-92 :: INOVIRUS (FILAMENTOUS BACTERIOPHAGE) STRAIN FD MAJ

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 50
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TPM

PLASMINOGEN ACTIVATOR 26-MAY-93 :: TISSUE-TYPE PLASMINOGEN ACTIVATOR (TYPE 1 FIBRIN-B

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 50
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1OMA

TOXIN 09-SEP-93 :: OMEGA-AGA-IVB (NMR, 21 STRUCTURES)

DOMAIN 1: 1 to 40 ; The following residues NOT assigned to any domain: Chain " " 41 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2SH1

NEUROTOXIN 03-MAY-90 :: NEUROTOXIN I (SH I) (NMR, 8 STRUCTURES)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ATY

MEMBRANE PROTEIN 05-OCT-94 :: F1FO ATP SYNTHASE (E.C.3.6.1.34) SUBUNIT C (RESIDU

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 9 - 79
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BBT 4

PRELIMINARY 18-MAY-92 :: FOOT AND MOUTH DISEASE VIRUS O=1=BFS 1860 (FMDVO=1

DOMAIN 1: 4 * to 4 * ; The following residues NOT assigned to any domain: Chain "4" 1 - 208 The following residues NOT assigned to any domain: Chain "4" 9 - 218 The following residues NOT assigned to any domain: Chain "4" 1 - 220
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IFM

VIRUS 31-JAN-94 :: INOVIRUS (FILAMENTOUS BACTERIOPHAGE) STRAIN PF1 MA

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 46
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2IFO

VIRUS 08-AUG-94 :: INOVIRUS (FILAMENTOUS BACTERIOPHAGE) STRAIN XF MAJ

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 46
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RES

SITE-SPECIFIC RECOMBINASE 29-JUN-94 :: GAMMA DELTA RESOLVASE (DNA BINDING DOMAIN)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 43
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PDD

OXIDO-REDUCTASE(ACYLTRANSFERASE) 25-NOV-92 :: DIHYDROLIPOAMIDE ACETYLTRANSFERASE (E2P) (E.C.2.3.

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 43
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ERC

PHEROMONE 14-FEB-94 :: PHEROMONE ER-1 (NMR, 20 STRUCTURES)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 40
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ERD

PHEROMONE 14-FEB-94 :: PHEROMONE ER-2 (NMR, 20 STRUCTURES)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 40
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DEC

BLOOD COAGULATION 17-MAY-94 :: DECORSIN (NMR, 25 STRUCTURES)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 39
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PPT

PANCREATIC HORMONE 16-JAN-81 :: AVIAN PANCREATIC POLYPEPTIDE

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 36
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SIS

TOXIN 11-NOV-93 :: SCORPION INSECTOTOXIN I5A (NMR, 10 STRUCTURES)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 35
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SPF

LIPOPROTEIN(SURFACE FILM) 26-SEP-94 :: PULMONARY SURFACTANT-ASSOCIATED POLYPEPTIDE C(SP-C

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 35
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FCT

TRANSIT PEPTIDE 30-MAR-94 :: FERREDOXIN CHLOROPLASTIC TRANSIT PEPTIDE SEQUENCE

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 32
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HLE B

HYDROLASE(SERINE PROTEINASE-INHIBITOR) 13-APR-92 :: HORSE LEUCOCYTE ELASTASE INHIBITOR (HLEI)

DOMAIN 1: B * to B * ; The following residues NOT assigned to any domain: Chain "B" 22 - 358
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PNH

TOXIN 25-AUG-93 :: SCORPION TOXIN (PO5-NH2) ANALOG WITH HIGH AFFINITY

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 31
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2ZTA A

LEUCINE ZIPPER 05-JUL-91 :: /GCN4$ LEUCINE ZIPPER

DOMAIN 1: A * to A * ; B * to B * ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CAG B

COLLAGEN 29-MAR-94 :: COLLAGEN-LIKE PEPTIDE (PRO-HYP-GLY)4 PRO-HYP-ALA

DOMAIN 1: B * to B * ; The following residues NOT assigned to any domain: Chain "B" 1 - 29 The following residues NOT assigned to any domain: Chain "B" 61 - 89
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DFN A

DEFENSIN 18-JAN-91 :: DEFENSIN /HNP$-3

DOMAIN 1: A * to A * ; The following residues NOT assigned to any domain: Chain "A" 2 - 31
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PAA

TRANSCRIPTION REGULATION 15-JUL-94 :: YEAST TRANSCRIPTION FACTOR ADR1 (RESIDUES 130 - 15

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 130 - 159
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4INS A

HORMONE 10-JUL-89 :: INSULIN

DOMAIN 1: A * to A * ; B * to B * ; The following residues NOT assigned to any domain: Chain "B" 1 - 21 The following residues NOT assigned to any domain: Chain "B" 1 - 30
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5ZNF

PRELIMINARY 22-AUG-91 :: ZINC-FINGER (ZFY-6T)(NMR)(12 STRUCTURES)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 30
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ARD

TRANSCRIPTION REGULATION 01-OCT-93 :: YEAST TRANSCRIPTION FACTOR ADR1 (RESIDUES 102 - 13

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 102 - 130
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1COS A

ALPHA-HELICAL BUNDLE 22-JAN-93 :: COILED SERINE

DOMAIN 1: A * to A * ; B * to B * ; C * to C * ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GCN

HORMONE 17-OCT-77 :: GLUCAGON (PH 6 - PH 7 FORM)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 29
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PPE I

PRELIMINARY 24-OCT-91 :: TRYPSIN (E.C.3.4.21.4) AND CUCURBITA MAXIMA TRYPSI

DOMAIN 1: I * to I * ; The following residues NOT assigned to any domain: Chain "I" 16 - 245
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AMB

PROTEINASE INHIBITOR(TRYPSIN) 21-OCT-94 :: ALZHEIMER'S DISEASE AMYLOID BETA-PEPTIDE (RESIDUES

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 28
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MEA

AMINOACYL-TRNA SYNTHASE 09-NOV-92 :: METHIONYL-TRNA SYNTHETASE (E.C.6.1.1.10) (ZINC BIN

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 28
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ANS

TOXIN 09-JUN-94 :: NEUROTOXIN III (ATX III) (NMR, 28 STRUCTURES)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 27
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CCO

CONOTOXIN 24-AUG-93 :: OMEGA-CONOTOXIN GVIA (NMR, 24 STRUCTURES)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 27
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6RLX A

HORMONE(MUSCLE RELAXANT) 21-JUN-91 :: RELAXIN

DOMAIN 1: A * to A * ; B * to B * ; The following residues NOT assigned to any domain: Chain "B" -3 - 20 The following residues NOT assigned to any domain: Chain "B" -2 - 22
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DTC

TOXIN 14-OCT-92 :: ACETYL-DELTA-TOXIN (ACETYL-DELTA-HAEMOLYSIN) (NMR,

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 26
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2BBM B

PRELIMINARY 16-JUL-92 :: CALCIUM-BOUND CALMODULIN COMPLEX WITH CALMODULIN B

DOMAIN 1: B * to B * ; The following residues NOT assigned to any domain: Chain "B" 1 - 148
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MLT A

TOXIN (HEMOLYTIC POLYPEPTIDE) 04-OCT-90 :: MELITTIN

DOMAIN 1: A * to A * ; B * to B * ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ZNF

ZINC FINGER DNA BINDING DOMAIN 25-SEP-89 :: 31ST ZINC FINGER FROM /XFIN$ (/XFIN$-31) (37 MODEL

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 0 - 25
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TCG

PRELIMINARY 12-DEC-92 :: MU-CONOTOXIN GIIIA (PREVIOUSLY KNOWN AS GEOGRAPHUT

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 22
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BTS

TRANSMEMBRANE PROTEIN 03-AUG-94 :: BAND 3 (SYNTHETIC PEPTIDE COMPRISING RESIDUES 436

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 22
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RPB

HIV REPLICATION INHIBITOR 31-AUG-93 :: RP 71955 (TRICYCLIC PEPTIDE ACTIVE AGAINST HIV-1)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 21
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SRB

TOXIN 06-SEP-94 :: SARAFOTOXIN S6B (SRTB S6B) (PH 3.0, 303K)

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 21
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1APM I

TRANSFERASE(PHOSPHOTRANSFERASE) 18-JAN-93 :: $C-/AMP$-DEPENDENT PROTEIN KINASE (E.C.2.7.1.37) (

DOMAIN 1: I * to I * ; The following residues NOT assigned to any domain: Chain "I" 10 - 350
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BOM A

INSULIN-LIKE BRAIN-SECRETORY PEPTIDE 21-JUL-94 :: BOMBYXIN-II (NMR, MINIMIZED AVERAGE STRUCTURE)

DOMAIN 1: A * to A * ; B * to B * ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BTQ

ANION TRANSPORT 03-AUG-94 :: BAND 3 (SYNTHETIC PEPTIDE COMPRISING RESIDUES 405

DOMAIN 1: * * to * * ; The following residues NOT assigned to any domain: Chain " " 1 - 21
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CDL G

CALCIUM-BINDING PROTEIN 08-OCT-93 :: CALMODULIN COMPLEXED WITH CALMODULIN-BINDING PEPTI

DOMAIN 1: G * to G * ; The following residues NOT assigned to any domain: Chain "G" 5 - 146 The following residues NOT assigned to any domain: Chain "G" 797 - 815 The following residues NOT assigned to any domain: Chain "G" 5 - 146 The following residues NOT assigned to any domain: Chain "G" 797 - 815 The following residues NOT assigned to any domain: Chain "G" 5 - 146 The following residues NOT assigned to any domain: Chain "G" 5 - 146 The following residues NOT assigned to any domain: Chain "G" 798 - 815
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3TPI I

COMPLEX (PROTEINASE/INHIBITOR) 27-SEP-82 :: TRYPSINOGEN COMPLEX WITH PANCREATIC TRYPSIN INHIBI

DOMAIN 1: [Assigned by homology with 1AAPA]I 1 to I 55 ; The following residues NOT assigned to any domain: Chain "I" 16 - 245 The following residues NOT assigned to any domain: Chain "I" 56 - 58 The following residues NOT assigned to any domain: Chain "I" 16 - 17
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4PTI

PROTEINASE INHIBITOR (TRYPSIN) 27-SEP-82 :: TRYPSIN INHIBITOR

DOMAIN 1: [Assigned by homology with 1AAPA] 1 to 55 ; The following residues NOT assigned to any domain: Chain " " 56 - 58
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PTC I

COMPLEX (PROTEINASE/INHIBITOR) 27-SEP-82 :: BETA-TRYPSIN (E.C.3.4.21.4) COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1AAPA]I 1 to I 55 ; The following residues NOT assigned to any domain: Chain "I" 16 - 245 The following residues NOT assigned to any domain: Chain "I" 56 - 58
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5PTI

PROTEINASE INHIBITOR (TRYPSIN) 05-OCT-84 :: TRYPSIN INHIBITOR (CRYSTAL FORM /II$)

DOMAIN 1: [Assigned by homology with 1AAPA] 1 to 55 ; The following residues NOT assigned to any domain: Chain " " 56 - 58
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2TGP I

COMPLEX (PROTEINASE/INHIBITOR) 27-SEP-82 :: TRYPSINOGEN COMPLEX WITH PANCREATIC TRYPSIN INHIBI

DOMAIN 1: [Assigned by homology with 1AAPA]I 1 to I 55 ; The following residues NOT assigned to any domain: Chain "I" 16 - 245 The following residues NOT assigned to any domain: Chain "I" 56 - 58
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PIT

PRELIMINARY 30-APR-92 :: TRYPSIN INHIBITOR

DOMAIN 1: [Assigned by homology with 1AAPA] 1 to 55 ; The following residues NOT assigned to any domain: Chain " " 56 - 58
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

9PTI

PROTEINASE INHIBITOR (TRYPSIN) 08-APR-91 :: BASIC PANCREATIC TRYPSIN INHIBITOR (MET 52 OXIDIZE

DOMAIN 1: [Assigned by homology with 1AAPA] 1 to 55 ; The following residues NOT assigned to any domain: Chain " " 56 - 58
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TPA I

COMPLEX (PROTEINASE/INHIBITOR) 27-SEP-82 :: ANHYDRO-TRYPSIN (E.C.3.4.21.4) COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1AAPA]I 1 to I 55 ; The following residues NOT assigned to any domain: Chain "I" 16 - 245 The following residues NOT assigned to any domain: Chain "I" 56 - 58
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4TPI I

COMPLEX (PROTEINASE/INHIBITOR) 11-JUN-85 :: TRYPSINOGEN COMPLEX WITH THE ARG==15==-ANALOGUE OF

DOMAIN 1: [Assigned by homology with 1AAPA]I 1 to I 55 ; The following residues NOT assigned to any domain: Chain "I" 16 - 245 The following residues NOT assigned to any domain: Chain "I" 56 - 58 The following residues NOT assigned to any domain: Chain "I" 16 - 17
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6PTI

PROTEINASE INHIBITOR (TRYPSIN) 13-MAY-87 :: BOVINE PANCREATIC TRYPSIN INHIBITOR (/BPTI$,CRYSTA

DOMAIN 1: [Assigned by homology with 1AAPA] 1 to 55 ; The following residues NOT assigned to any domain: Chain " " 56 - 57
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2KAI I

COMPLEX (PROTEINASE-INHIBITOR) 21-MAY-84 :: KALLIKREIN A (E.C.3.4.21.8) COMPLEX WITH BOVINE PA

DOMAIN 1: [Assigned by homology with 1AAPA]I 2 to I 55 ; The following residues NOT assigned to any domain: Chain "I" 16 - 95B The following residues NOT assigned to any domain: Chain "I" 95Y - 246 The following residues NOT assigned to any domain: Chain "I" 56 - 58
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2TPI I

COMPLEX (PROTEINASE/INHIBITOR) 26-OCT-81 :: TRYPSINOGEN - PANCREATIC TRYPSIN INHIBITOR - ILE-V

DOMAIN 1: [Assigned by homology with 1AAPA]I 2 to I 55 ; The following residues NOT assigned to any domain: Chain "I" 16 - 17 The following residues NOT assigned to any domain: Chain "I" 19 - 245 The following residues NOT assigned to any domain: Chain "I" 56 - 58
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NAG

SERINE PROTEASE INHIBITOR 18-AUG-92 :: BOVINE PANCREATIC TRYPSIN INHIBITOR (BPTI) MUTANT

DOMAIN 1: [Assigned by homology with 1AAPA] 1 to 55 ; The following residues NOT assigned to any domain: Chain " " 56 - 56
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BTI

SERINE PROTEASE INHIBITOR 11-JUL-91 :: BOVINE PANCREATIC TRYPSIN INHIBITOR (BPTI) MUTANT

DOMAIN 1: [Assigned by homology with 1AAPA] 1 to 55 ; The following residues NOT assigned to any domain: Chain " " 56 - 58
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FAN

SERINE PROTEASE INHIBITOR 21-AUG-92 :: BOVINE PANCREATIC TRYPSIN INHIBITOR (BPTI) MUTANT

DOMAIN 1: [Assigned by homology with 1AAPA] 1 to 55 ; The following residues NOT assigned to any domain: Chain " " 56 - 58
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8PTI

PROTEINASE INHIBITOR (TRYPSIN) 17-DEC-90 :: BOVINE PANCREATIC TRYPSIN INHIBITOR (/BPTI$) MUTAN

DOMAIN 1: [Assigned by homology with 1AAPA] 1 to 55 ; The following residues NOT assigned to any domain: Chain " " 56 - 58
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BPT

PROTEINASE INHIBITOR (TRYPSIN) 11-DEC-91 :: BOVINE PANCREATIC TRYPSIN INHIBITOR (/BPTI$) MUTAN

DOMAIN 1: [Assigned by homology with 1AAPA] 1 to 55 ; The following residues NOT assigned to any domain: Chain " " 56 - 56
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AAL A

SERINE PROTEASE INHIBITOR 09-APR-92 :: BOVINE PANCREATIC TRYPSIN INHIBITOR (BPTI, BASIC)

DOMAIN 1: [Assigned by homology with 1AAPA]A 1 to A 55 ; The following residues NOT assigned to any domain: Chain "A" 56 - 58 The following residues NOT assigned to any domain: Chain "A" 1 - 57
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7PTI

PROTEINASE INHIBITOR (TRYPSIN) 08-MAR-90 :: BOVINE PANCREATIC TRYPSIN INHIBITOR (/BPTI$) MUTAN

DOMAIN 1: [Assigned by homology with 1AAPA] 1 to 55 ; The following residues NOT assigned to any domain: Chain " " 56 - 58
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AAL B

SERINE PROTEASE INHIBITOR 09-APR-92 :: BOVINE PANCREATIC TRYPSIN INHIBITOR (BPTI, BASIC)

DOMAIN 1: [Assigned by homology with 1AAPA]B 1 to B 55 ; The following residues NOT assigned to any domain: Chain "B" 1 - 58 The following residues NOT assigned to any domain: Chain "B" 56 - 57
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BRB I

COMPLEX(PROTEINASE/INHIBITOR) 17-DEC-92 :: TRYPSIN (E.C.3.4.21.4) VARIANT (D189G, G226D) COMP

DOMAIN 1: [Assigned by homology with 1AAPA]I 5 to I 55 ; The following residues NOT assigned to any domain: Chain "I" 16 - 245
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BRC I

COMPLEX(PROTEINASE/INHIBITOR) 17-DEC-92 :: TRYPSIN (E.C.3.4.21.4) VARIANT (D189G,G226D) COMPL

DOMAIN 1: [Assigned by homology with 1AAPA]I 1 to I 55 ; The following residues NOT assigned to any domain: Chain "I" 16 - 245 The following residues NOT assigned to any domain: Chain "I" 56 - 56
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AAP B

PROTEINASE INHIBITOR (TRYPSIN) 14-SEP-90 :: PROTEASE INHIBITOR DOMAIN OF ALZHEIMER'S AMYLOID

DOMAIN 1: [Assigned by homology with 1AAPA]B 1 to B 55 ; The following residues NOT assigned to any domain: Chain "B" 1 - 56 The following residues NOT assigned to any domain: Chain "B" 56 - 56
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DTK

PRESYNAPTIC NEUROTOXIN 02-APR-93 :: DENDROTOXIN K (NMR, 20 STRUCTURES)

DOMAIN 1: [Assigned by homology with 1AAPA] 1 to 55 ; The following residues NOT assigned to any domain: Chain " " 56 - 57
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DTX

PRESYNAPTIC NEUROTOXIN 29-APR-91 :: ALPHA-*DENDROTOXIN

DOMAIN 1: [Assigned by homology with 1AAPA] 1 to 57 ; The following residues NOT assigned to any domain: Chain " " 58 - 59
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SHP

PRELIMINARY 17-NOV-92 :: TRYPSIN INHIBITOR

DOMAIN 1: [Assigned by homology with 1AAPA] 1 to 53 ; The following residues NOT assigned to any domain: Chain " " 54 - 55
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DEM

VENOM(POTASSIUM CHANNEL INHIBITOR) 07-MAR-94 :: DENDROTOXIN I (NMR, MINIMIZED AVERAGE STRUCTURE)

DOMAIN 1: [Assigned by homology with 1AAPA] 1 to 57 ; The following residues NOT assigned to any domain: Chain " " 58 - 60
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DEN

VENOM(POTASSIUM CHANNEL INHIBITOR) 07-MAR-94 :: DENDROTOXIN I (NMR, 29 STRUCTURES)

DOMAIN 1: [Assigned by homology with 1AAPA] 1 to 57 ; The following residues NOT assigned to any domain: Chain " " 58 - 60
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1KNT

COLLAGEN TYPE VI FRAGMENT 18-AUG-94 :: COLLAGEN TYPE VI (KUNITZ-TYPE DOMAIN C5 FROM THE A

DOMAIN 1: [Assigned by homology with 1AAPA] 2 to 55 ; The following residues NOT assigned to any domain: Chain " " 56 - 56
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AAZ A

ELECTRON TRANSPORT 24-APR-92 :: GLUTAREDOXIN

DOMAIN 1: A 1 to A 87 ; The following residues NOT assigned to any domain: Chain "A" 1 - 87
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AAZ B

ELECTRON TRANSPORT 24-APR-92 :: GLUTAREDOXIN

DOMAIN 1: B 1 to B 87 ; The following residues NOT assigned to any domain: Chain "B" 1 - 87
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DLA A

OXIDOREDUCTASE(NADP) 08-FEB-93 :: ALDOSE REDUCTASE (E.C.1.1.1.21)

DOMAIN 1: A 1 to A 313 ; The following residues NOT assigned to any domain: Chain "A" 314 - 314 The following residues NOT assigned to any domain: Chain "A" 1 - 314 The following residues NOT assigned to any domain: Chain "A" 1 - 314 The following residues NOT assigned to any domain: Chain "A" 1 - 314
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DLA C

OXIDOREDUCTASE(NADP) 08-FEB-93 :: ALDOSE REDUCTASE (E.C.1.1.1.21)

DOMAIN 1: C 1 to C 313 ; The following residues NOT assigned to any domain: Chain "C" 1 - 314 The following residues NOT assigned to any domain: Chain "C" 1 - 314 The following residues NOT assigned to any domain: Chain "C" 314 - 314 The following residues NOT assigned to any domain: Chain "C" 1 - 314
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DLA B

OXIDOREDUCTASE(NADP) 08-FEB-93 :: ALDOSE REDUCTASE (E.C.1.1.1.21)

DOMAIN 1: B 1 to B 313 ; The following residues NOT assigned to any domain: Chain "B" 1 - 314 The following residues NOT assigned to any domain: Chain "B" 314 - 314 The following residues NOT assigned to any domain: Chain "B" 1 - 314 The following residues NOT assigned to any domain: Chain "B" 1 - 314
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DLA D

OXIDOREDUCTASE(NADP) 08-FEB-93 :: ALDOSE REDUCTASE (E.C.1.1.1.21)

DOMAIN 1: D 1 to D 313 ; The following residues NOT assigned to any domain: Chain "D" 1 - 314 The following residues NOT assigned to any domain: Chain "D" 1 - 314 The following residues NOT assigned to any domain: Chain "D" 1 - 314 The following residues NOT assigned to any domain: Chain "D" 314 - 314
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2ACQ

OXIDOREDUCTASE 15-APR-94 :: ALDOSE REDUCTASE (E.C.1.1.1.21) WILD TYPE COMPLEXE

DOMAIN 1: 1 to 314 ; The following residues NOT assigned to any domain: Chain " " 315 - 315
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2ACR

OXIDOREDUCTASE 15-APR-94 :: ALDOSE REDUCTASE (E.C.1.1.1.21) WILD TYPE COMPLEXE

DOMAIN 1: 1 to 314 ; The following residues NOT assigned to any domain: Chain " " 315 - 315
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2ACS

OXIDOREDUCTASE 15-APR-94 :: ALDOSE REDUCTASE (E.C.1.1.1.21) WILD TYPE COMPLEXE

DOMAIN 1: 2 to 314 ; The following residues NOT assigned to any domain: Chain " " 315 - 315
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2ACU

OXIDOREDUCTASE 15-APR-94 :: ALDOSE REDUCTASE (E.C.1.1.1.21) MUTANT WITH TYR 48

DOMAIN 1: 1 to 314 ; The following residues NOT assigned to any domain: Chain " " 315 - 315
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ABN

OXIDOREDUCTASE 03-SEP-92 :: ALDOSE REDUCTASE (E.C.1.1.1.21) MUTANT WITH CYS 29

DOMAIN 1: 2 to 314 ; The following residues NOT assigned to any domain: Chain " " 315 - 315
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAL

OXIDOREDUCTASE 04-FEB-94 :: 3-ALPHA-HYDROXYSTEROID DEHYDROGENASE (E.C.1.1.1.50

DOMAIN 1: 1 to 308 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BYH

HYDROLASE 31-DEC-92 :: HYBRID (1,3-1,4)-BETA-D-GLUCAN 4-GLUCANOHYDROLASE

DOMAIN 1: 1 to 214 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CPM

HYDROLASE(GLUCANASE) 11-MAR-94 :: CIRCULARLY PERMUTED (1-3,1-4)-BETA-D-GLUCAN

DOMAIN 1: 1 to 156 ; The following residues NOT assigned to any domain: Chain " " 157 - 214
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CPN

HYDROLASE(GLUCANASE) 11-MAR-94 :: CIRCULARLY PERMUTED (1-3,1-4)-BETA-D-GLUCAN

DOMAIN 1: 1 to 156 ; The following residues NOT assigned to any domain: Chain " " 157 - 208
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BBH B

PRELIMINARY 18-MAY-92 :: CYTOCHROME $C'

DOMAIN 1: [Assigned by homology with 1BBHA]B 1 to B 131 ; The following residues NOT assigned to any domain: Chain "B" 1 - 131
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BAL

PRELIMINARY 20-FEB-92 :: E3-BINDING DOMAIN OF THE DIHYDROLIPOAMIDE

DOMAIN 1: 1 to 47 ; The following residues NOT assigned to any domain: Chain " " 48 - 51
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BBP B

BILIN BINDING 19-SEP-90 :: BILIN BINDING PROTEIN (/BBP$)

DOMAIN 1: B 2 to B 178 ; The following residues NOT assigned to any domain: Chain "B" 2 - 178 The following residues NOT assigned to any domain: Chain "B" 2 - 178 The following residues NOT assigned to any domain: Chain "B" 2 - 178
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BBP C

BILIN BINDING 19-SEP-90 :: BILIN BINDING PROTEIN (/BBP$)

DOMAIN 1: [Assigned by homology with 1BBPA]C 2 to C 178 ; The following residues NOT assigned to any domain: Chain "C" 2 - 178 The following residues NOT assigned to any domain: Chain "C" 2 - 178 The following residues NOT assigned to any domain: Chain "C" 2 - 178
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BBP D

BILIN BINDING 19-SEP-90 :: BILIN BINDING PROTEIN (/BBP$)

DOMAIN 1: [Assigned by homology with 1BBPA]D 2 to D 178 ; The following residues NOT assigned to any domain: Chain "D" 2 - 178 The following residues NOT assigned to any domain: Chain "D" 2 - 178 The following residues NOT assigned to any domain: Chain "D" 2 - 178
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BGE A

CYTOKINE 27-APR-93 :: GRANULOCYTE COLONY-STIMULATING FACTOR (FORM II RCG

DOMAIN 1: A 9 to A 172 ; The following residues NOT assigned to any domain: Chain "A" 173 - 174 The following residues NOT assigned to any domain: Chain "A" 9 - 173
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BGD

CYTOKINE 27-APR-93 :: GRANULOCYTE COLONY-STIMULATING FACTOR (FORM I, RCG

DOMAIN 1: 10 to 172 ; The following residues NOT assigned to any domain: Chain " " 173 - 173
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BGE B

CYTOKINE 27-APR-93 :: GRANULOCYTE COLONY-STIMULATING FACTOR (FORM II RCG

DOMAIN 1: B 9 to B 172 ; The following residues NOT assigned to any domain: Chain "B" 9 - 174 The following residues NOT assigned to any domain: Chain "B" 173 - 173
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GNC

GROWTH FACTOR 08-MAR-94 :: GRANULOCYTE COLONY STIMULATING FACTOR (RH-G-CSF)

DOMAIN 1: 1 to 172 ; The following residues NOT assigned to any domain: Chain " " 173 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RHG B

GROWTH FACTOR 29-JAN-93 :: R-HU-GCSF GRANULOCYTE-COLONY STIMULATING FACTOR

DOMAIN 1: B 9 to B 171 ; The following residues NOT assigned to any domain: Chain "B" 9 - 172 The following residues NOT assigned to any domain: Chain "B" 172 - 172 The following residues NOT assigned to any domain: Chain "B" 9 - 172
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RHG A

GROWTH FACTOR 29-JAN-93 :: R-HU-GCSF GRANULOCYTE-COLONY STIMULATING FACTOR

DOMAIN 1: A 9 to A 171 ; The following residues NOT assigned to any domain: Chain "A" 172 - 172 The following residues NOT assigned to any domain: Chain "A" 9 - 172 The following residues NOT assigned to any domain: Chain "A" 9 - 172
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RHG C

GROWTH FACTOR 29-JAN-93 :: R-HU-GCSF GRANULOCYTE-COLONY STIMULATING FACTOR

DOMAIN 1: C 9 to C 171 ; The following residues NOT assigned to any domain: Chain "C" 9 - 172 The following residues NOT assigned to any domain: Chain "C" 9 - 172 The following residues NOT assigned to any domain: Chain "C" 172 - 172
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BOV B

TOXIN 08-OCT-91 :: VEROTOXIN-1 (B-OLIGOMER, ALSO CALLED SHIGA-LIKE TO

DOMAIN 1: [Assigned by homology with 1BOVA]B 1 to B 69 ; The following residues NOT assigned to any domain: Chain "B" 1 - 69 The following residues NOT assigned to any domain: Chain "B" 1 - 69 The following residues NOT assigned to any domain: Chain "B" 1 - 69 The following residues NOT assigned to any domain: Chain "B" 1 - 69
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BOV C

TOXIN 08-OCT-91 :: VEROTOXIN-1 (B-OLIGOMER, ALSO CALLED SHIGA-LIKE TO

DOMAIN 1: [Assigned by homology with 1BOVA]C 1 to C 69 ; The following residues NOT assigned to any domain: Chain "C" 1 - 69 The following residues NOT assigned to any domain: Chain "C" 1 - 69 The following residues NOT assigned to any domain: Chain "C" 1 - 69 The following residues NOT assigned to any domain: Chain "C" 1 - 69
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BOV D

TOXIN 08-OCT-91 :: VEROTOXIN-1 (B-OLIGOMER, ALSO CALLED SHIGA-LIKE TO

DOMAIN 1: [Assigned by homology with 1BOVA]D 1 to D 69 ; The following residues NOT assigned to any domain: Chain "D" 1 - 69 The following residues NOT assigned to any domain: Chain "D" 1 - 69 The following residues NOT assigned to any domain: Chain "D" 1 - 69 The following residues NOT assigned to any domain: Chain "D" 1 - 69
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BOV E

TOXIN 08-OCT-91 :: VEROTOXIN-1 (B-OLIGOMER, ALSO CALLED SHIGA-LIKE TO

DOMAIN 1: [Assigned by homology with 1BOVA]E 1 to E 69 ; The following residues NOT assigned to any domain: Chain "E" 1 - 69 The following residues NOT assigned to any domain: Chain "E" 1 - 69 The following residues NOT assigned to any domain: Chain "E" 1 - 69 The following residues NOT assigned to any domain: Chain "E" 1 - 69
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BYA

HYDROLASE(O-GLYCOSYL) 25-JAN-94 :: BETA-AMYLASE (E.C.3.2.1.2)

DOMAIN 1: 5 to 495 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BYB

HYDROLASE(O-GLYCOSYL) 25-JAN-94 :: BETA-AMYLASE (E.C.3.2.1.2) REACTED WITH 200 MM MAL

DOMAIN 1: 5 to 494 ; The following residues NOT assigned to any domain: Chain " " 495 - 495
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BYC

HYDROLASE(O-GLYCOSYL) 25-JAN-94 :: BETA-AMYLASE (E.C.3.2.1.2) REACTED WITH 8 MM MALTO

DOMAIN 1: 5 to 494 ; The following residues NOT assigned to any domain: Chain " " 495 - 495
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BYD

HYDROLASE(O-GLYCOSYL) 25-JAN-94 :: BETA-AMYLASE (E.C.3.2.1.2) REACTED WITH 100 MM MAL

DOMAIN 1: 5 to 494 ; The following residues NOT assigned to any domain: Chain " " 495 - 495
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AZM

LYASE(OXO-ACID) 28-NOV-93 :: CARBONIC ANHYDRASE I (E.C.4.2.1.1) COMPLEXED WITH

DOMAIN 1: 3 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HCB

LYASE(OXO-ACID) 07-JAN-94 :: CARBONIC ANHYDRASE I (E.C.4.2.1.1) COMPLEXED WITH

DOMAIN 1: 3 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BZM

LYASE(OXO-ACID) 28-NOV-93 :: CARBONIC ANHYDRASE I (E.C.4.2.1.1) COMPLEXED WITH

DOMAIN 1: 1 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CZM

LYASE(OXO-ACID) 28-NOV-93 :: CARBONIC ANHYDRASE I (E.C.4.2.1.1) COMPLEXED WITH

DOMAIN 1: 1 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HUH

LYASE(OXO-ACID) 28-OCT-93 :: CARBONIC ANHYDRASE I (E.C.4.2.1.1) COMPLEXED WITH

DOMAIN 1: 4 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HUG

LYASE(OXO-ACID) 28-OCT-93 :: CARBONIC ANHYDRASE I (E.C.4.2.1.1) COMPLEXED WITH

DOMAIN 1: 5 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CAB

HYDRO-LYASE 05-OCT-83 :: CARBONIC ANHYDRASE FORM B (CARBONATE DEHYDRATASE)

DOMAIN 1: 5 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BIC

LYASE(OXO-ACID) 01-SEP-92 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) MUTANT WITH TH

DOMAIN 1: 3 to 260 ; The following residues NOT assigned to any domain: Chain " " 261 - 261
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5CA2

LYASE(OXO-ACID) 08-JUN-91 :: CARBONIC ANHYDRASE /II$ (CARBONATE DEHYDRATASE) (/

DOMAIN 1: 5 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HCA

LYASE(OXO-ACID) 02-APR-92 :: CARBONIC ANHYDRASE /II$ (CARBONATE DEHYDRATASE) (/

DOMAIN 1: 5 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4CA2

LYASE(OXO-ACID) 08-JUN-91 :: CARBONIC ANHYDRASE /II$ (CARBONATE DEHYDRATASE) (/

DOMAIN 1: 5 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

12CA

LYASE(OXO-ACID) 01-OCT-91 :: CARBONIC ANHYDRASE /II$ (CARBONATE DEHYDRATASE) (/

DOMAIN 1: 5 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CA3

LYASE(OXO-ACID) 18-NOV-91 :: CARBONIC ANHYDRASE /II$ (CARBONATE DEHYDRATASE) (/

DOMAIN 1: 5 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CVC

HYDROLASE 22-SEP-93 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) MUTANT WITH HI

DOMAIN 1: 5 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CVE

LYASE(OXO-ACID) 21-JUN-94 :: CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE)(HCA

DOMAIN 1: 5 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4CAC

PRELIMINARY 05-SEP-91 :: CARBONIC ANHYDRASE FORM C (CARBONATE DEHYDRATASE /

DOMAIN 1: 4 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CA2

LYASE(OXO-ACID) 06-FEB-89 :: CARBONIC ANHYDRASE /II$ (CARBONATE DEHYDRATASE) (/

DOMAIN 1: 4 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5CAC

PRELIMINARY 05-SEP-91 :: CARBONIC ANHYDRASE FORM C (CARBONATE DEHYDRATASE /

DOMAIN 1: 4 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CA2

LYASE(OXO-ACID) 06-FEB-89 :: CARBONIC ANHYDRASE /II$ (CARBONATE DEHYDRATASE) (/

DOMAIN 1: 4 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CIL

LYASE(OXO-ACID) 20-OCT-93 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) COMPLEXED WITH

DOMAIN 1: 4 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CIM

LYASE(OXO-ACID) 20-OCT-93 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) COMPLEXED WITH

DOMAIN 1: 4 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CIN

LYASE(OXO-ACID) 20-OCT-93 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) COMPLEXED WITH

DOMAIN 1: 4 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3CA2

LYASE(OXO-ACID) 02-OCT-89 :: CARBONIC ANHYDRASE /II$ (CARBONATE DEHYDRATASE) (/

DOMAIN 1: 4 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BCD

LYASE(OXO-ACID) 31-AUG-93 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) COMPLEX WITH

DOMAIN 1: 3 to 260 ; The following residues NOT assigned to any domain: Chain " " 261 - 261
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAY

LYASE(OXO-ACID) 02-APR-93 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) COMPLEX WITH A

DOMAIN 1: 3 to 260 ; The following residues NOT assigned to any domain: Chain " " 261 - 261
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAZ

LYASE(OXO-ACID) 02-APR-93 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) COMPLEX WITH B

DOMAIN 1: 3 to 260 ; The following residues NOT assigned to any domain: Chain " " 261 - 261
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CAH

LYASE(OXO-ACID) 25-JUN-92 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) (NATIVE ZINC R

DOMAIN 1: 3 to 260 ; The following residues NOT assigned to any domain: Chain " " 261 - 261
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CAI

LYASE(OXO-ACID) 17-SEP-92 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) MUTANT WITH GL

DOMAIN 1: 3 to 260 ; The following residues NOT assigned to any domain: Chain " " 261 - 261
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CAK

LYASE(OXO-ACID) 17-SEP-92 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) MUTANT WITH GL

DOMAIN 1: 3 to 260 ; The following residues NOT assigned to any domain: Chain " " 261 - 261
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CAY

LYASE(OXO-ACID) 26-FEB-93 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) COMPLEX WITH A

DOMAIN 1: 3 to 260 ; The following residues NOT assigned to any domain: Chain " " 261 - 261
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CAZ

LYASE(OXO-ACID) 26-FEB-93 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) MUTANT WITH GL

DOMAIN 1: 3 to 260 ; The following residues NOT assigned to any domain: Chain " " 261 - 261
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RZA

LYASE(OXO-ACID) 25-MAY-93 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) WITH ZINC REPL

DOMAIN 1: 3 to 260 ; The following residues NOT assigned to any domain: Chain " " 261 - 261
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RZB

LYASE(OXO-ACID) 25-MAY-93 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) WITH ZINC REPL

DOMAIN 1: 3 to 260 ; The following residues NOT assigned to any domain: Chain " " 261 - 261
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RZC

LYASE(OXO-ACID) 25-MAY-93 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) WITH ZINC REPL

DOMAIN 1: 3 to 260 ; The following residues NOT assigned to any domain: Chain " " 261 - 261
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RZD

LYASE(OXO-ACID) 25-MAY-93 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) WITH ZINC REPL

DOMAIN 1: 3 to 260 ; The following residues NOT assigned to any domain: Chain " " 261 - 261
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RZE

LYASE(OXO-ACID) 25-MAY-93 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) WITH ZINC REPL

DOMAIN 1: 3 to 260 ; The following residues NOT assigned to any domain: Chain " " 261 - 261
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CBA

LYASE(OXO-ACID) 01-JUN-92 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) (50 MM TRIS,

DOMAIN 1: 3 to 260 ; The following residues NOT assigned to any domain: Chain " " 261 - 261
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CBB

LYASE(OXO-ACID) 01-JUN-92 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) (80 MM SODIUM

DOMAIN 1: 3 to 260 ; The following residues NOT assigned to any domain: Chain " " 261 - 261
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CBC

LYASE(OXO-ACID) 01-JUN-92 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) (50 MM TRIS,

DOMAIN 1: 3 to 260 ; The following residues NOT assigned to any domain: Chain " " 261 - 261
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CBD

LYASE(OXO-ACID) 01-JUN-92 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) (2.4 M AMMONIU

DOMAIN 1: 3 to 260 ; The following residues NOT assigned to any domain: Chain " " 261 - 261
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CBE

LYASE(OXO-ACID) 01-JUN-92 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) (50 MM TRIS,

DOMAIN 1: 3 to 260 ; The following residues NOT assigned to any domain: Chain " " 261 - 261
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CAN

PRELIMINARY 02-JUL-92 :: CARBONIC ANHYDRASE (CARBONATE HYDRO-LASE EC 4.2.1.

DOMAIN 1: 2 to 260 ; The following residues NOT assigned to any domain: Chain " " 1 - 1 Chain " " 261 - 261
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CAO

PRELIMINARY 02-JUL-92 :: CARBONIC ANHYDRASE (CARBONATE HYDRO-LYASE, EC 4.2.

DOMAIN 1: 2 to 260 ; The following residues NOT assigned to any domain: Chain " " 1 - 1
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CRA

21-OCT-92 :: CARBONIC ANHYDRASE (CARBONATE HYDRO-LYASE, EC 4.2.

DOMAIN 1: 2 to 260 ; The following residues NOT assigned to any domain: Chain " " 1 - 1 Chain " " 261 - 261
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CVF

LYASE(OXO-ACID) 21-JUN-94 :: CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE)(HCA

DOMAIN 1: 5 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CAL

LYASE(OXO-ACID) 17-SEP-92 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) MUTANT WITH TH

DOMAIN 1: 3 to 260 ; The following residues NOT assigned to any domain: Chain " " 261 - 261
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CAM

LYASE(OXO-ACID) 17-SEP-92 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) MUTANT WITH TH

DOMAIN 1: 3 to 260 ; The following residues NOT assigned to any domain: Chain " " 261 - 261
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HVA

LYASE(OXO-ACID) 27-OCT-92 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) MUTANT WITH HI

DOMAIN 1: 5 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CNB

LYASE(OXO-ACID) 13-JUN-94 :: CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE, HCA

DOMAIN 1: 5 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CNC

LYASE(OXO-ACID) 13-JUN-94 :: CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE, HCA

DOMAIN 1: 5 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CVD

LYASE(OXO-ACID) 21-JUN-94 :: CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (HCA

DOMAIN 1: 5 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CVA

LYASE(OXO-ACID) 04-FEB-93 :: CARBONIC ANHYDRASE II (HCA II) (E.C.4.2.1.1) MUTAN

DOMAIN 1: 5 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CVB

LYASE(OXO-ACID) 04-FEB-93 :: CARBONIC ANHYDRASE II (HCA II) (E.C.4.2.1.1) MUTAN

DOMAIN 1: 5 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MUA

LYASE(OXO-ACID) 18-JUN-93 :: CARBONIC ANHYDRASE II (E.C.4.2.1.1) MUTANT WITH PR

DOMAIN 1: 4 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DCA

LYASE(OXO-ACID) 18-DEC-92 :: CARBONIC ANHYDRASE /II$ (CARBONATE DEHYDRATASE) (/

DOMAIN 1: 5 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DCB

LYASE(OXO-ACID) 10-MAR-93 :: CARBONIC ANHYDRASE /II$ (CARBONATE DEHYDRATASE) (/

DOMAIN 1: 5 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7CA2

LYASE(OXO-ACID) 09-JUL-91 :: CARBONIC ANHYDRASE /II$ (CARBONATE DEHYDRATASE) (/

DOMAIN 1: 5 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HED

LYASE(OXO-ACID) 16-JUL-92 :: CARBONIC ANHYDRASE /II$ (CARBONATE DEHYDRATASE) (/

DOMAIN 1: 5 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6CA2

LYASE(OXO-ACID) 09-JUL-91 :: CARBONIC ANHYDRASE /II$ (CARBONATE DEHYDRATASE) (/

DOMAIN 1: 5 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8CA2

LYASE(OXO-ACID) 09-JUL-91 :: CARBONIC ANHYDRASE /II$ (CARBONATE DEHYDRATASE) (/

DOMAIN 1: 5 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

9CA2

LYASE(OXO-ACID) 09-JUL-91 :: CARBONIC ANHYDRASE /II$ (CARBONATE DEHYDRATASE) (/

DOMAIN 1: 5 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HEC

LYASE(OXO-ACID) 16-JUL-92 :: CARBONIC ANHYDRASE /II$ (CARBONATE DEHYDRATASE) (/

DOMAIN 1: 4 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HEB

LYASE(OXO-ACID) 16-JUL-92 :: CARBONIC ANHYDRASE /II$ (CARBONATE DEHYDRATASE) (/

DOMAIN 1: 5 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HEA

LYASE(OXO-ACID) 16-JUL-92 :: CARBONIC ANHYDRASE /II$ (CARBONATE DEHYDRATASE) (/

DOMAIN 1: 4 to 260 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CRN

PLANT SEED PROTEIN 30-APR-81 :: CRAMBIN

DOMAIN 1: 1 to 46 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CCM

PLANT SEED PROTEIN 14-APR-93 :: CRAMBIN (PRO 22/LEU 25) (NMR, 8 STRUCTURES)

DOMAIN 1: 1 to 46 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CCN

PLANT SEED PROTEIN 14-APR-93 :: CRAMBIN (PRO 22/LEU 25) (NMR, MINIMIZED AVERAGE ST

DOMAIN 1: 1 to 46 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CNR

PLANT SEED PROTEIN 15-JUL-93 :: CRAMBIN (PL FORM)

DOMAIN 1: 1 to 46 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CMA A

DNA-BINDING REGULATORY PROTEIN 24-AUG-92 :: MET REPRESSOR-OPERATOR COMPLEX (METJ)

DOMAIN 1: [Assigned by homology with 1CMBA]A 1 to A 104 ; The following residues NOT assigned to any domain: Chain "A" 1 - 104 The following residues NOT assigned to any domain: Chain "A" 1 - 10 The following residues NOT assigned to any domain: Chain "A" 11 - 19
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CMA B

DNA-BINDING REGULATORY PROTEIN 24-AUG-92 :: MET REPRESSOR-OPERATOR COMPLEX (METJ)

DOMAIN 1: [Assigned by homology with 1CMBA]B 1 to B 104 ; The following residues NOT assigned to any domain: Chain "B" 1 - 104 The following residues NOT assigned to any domain: Chain "B" 1 - 10 The following residues NOT assigned to any domain: Chain "B" 11 - 19
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CMB B

DNA-BINDING REGULATORY PROTEIN 28-AUG-92 :: MET APO-REPRESSOR (METJ)

DOMAIN 1: [Assigned by homology with 1CMBA]B 1 to B 104 ; The following residues NOT assigned to any domain: Chain "B" 1 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CMC A

DNA-BINDING REGULATORY PROTEIN 28-AUG-92 :: MET HOLO-REPRESSOR (METJ) COMPLEX WITH COREPRESSOR

DOMAIN 1: [Assigned by homology with 1CMBA]A 1 to A 104 ; The following residues NOT assigned to any domain: Chain "A" 1 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CMC B

DNA-BINDING REGULATORY PROTEIN 28-AUG-92 :: MET HOLO-REPRESSOR (METJ) COMPLEX WITH COREPRESSOR

DOMAIN 1: [Assigned by homology with 1CMBA]B 1 to B 104 ; The following residues NOT assigned to any domain: Chain "B" 1 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3SOD O

OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR) 26-JUN-90 :: CU,ZN SUPEROXIDE DISMUTASE (E.C.1.15.1.1) MUTANT W

DOMAIN 1: [Assigned by homology with 1COBA]O 1 to O 150 ; The following residues NOT assigned to any domain: Chain "O" 0 - 0 Chain "O" 151 - 151
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2SOD O

OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR) 25-MAR-80 :: CU,ZN SUPEROXIDE DISMUTASE (E.C.1.15.1.1)

DOMAIN 1: [Assigned by homology with 1COBA]O 1 to O 150 ; The following residues NOT assigned to any domain: Chain "O" 0 - 0 Chain "O" 151 - 151 The following residues NOT assigned to any domain: Chain "O" 0 - 151 The following residues NOT assigned to any domain: Chain "O" 0 - 151 The following residues NOT assigned to any domain: Chain "O" 0 - 151
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2SOD Y

OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR) 25-MAR-80 :: CU,ZN SUPEROXIDE DISMUTASE (E.C.1.15.1.1)

DOMAIN 1: [Assigned by homology with 1COBA]Y 1 to Y 150 ; The following residues NOT assigned to any domain: Chain "Y" 0 - 151 The following residues NOT assigned to any domain: Chain "Y" 0 - 0 Chain "Y" 151 - 151 The following residues NOT assigned to any domain: Chain "Y" 0 - 151 The following residues NOT assigned to any domain: Chain "Y" 0 - 151
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2SOD B

OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR) 25-MAR-80 :: CU,ZN SUPEROXIDE DISMUTASE (E.C.1.15.1.1)

DOMAIN 1: [Assigned by homology with 1COBA]B 1 to B 150 ; The following residues NOT assigned to any domain: Chain "B" 0 - 151 The following residues NOT assigned to any domain: Chain "B" 0 - 151 The following residues NOT assigned to any domain: Chain "B" 0 - 0 Chain "B" 151 - 151 The following residues NOT assigned to any domain: Chain "B" 0 - 151
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2SOD G

OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR) 25-MAR-80 :: CU,ZN SUPEROXIDE DISMUTASE (E.C.1.15.1.1)

DOMAIN 1: [Assigned by homology with 1COBA]G 1 to G 150 ; The following residues NOT assigned to any domain: Chain "G" 0 - 151 The following residues NOT assigned to any domain: Chain "G" 0 - 151 The following residues NOT assigned to any domain: Chain "G" 0 - 151 The following residues NOT assigned to any domain: Chain "G" 0 - 0 Chain "G" 151 - 151
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SDA O

OXIDOREDUCTASE(COPPER) 13-JAN-93 :: CU,ZN SUPEROXIDE DISMUTASE (E.C.1.15.1.1) NITRATED

DOMAIN 1: [Assigned by homology with 1COBA]O 1 to O 150 ; The following residues NOT assigned to any domain: Chain "O" 0 - 0 Chain "O" 151 - 151 The following residues NOT assigned to any domain: Chain "O" 0 - 151 The following residues NOT assigned to any domain: Chain "O" 0 - 151 The following residues NOT assigned to any domain: Chain "O" 0 - 151
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SDA Y

OXIDOREDUCTASE(COPPER) 13-JAN-93 :: CU,ZN SUPEROXIDE DISMUTASE (E.C.1.15.1.1) NITRATED

DOMAIN 1: [Assigned by homology with 1COBA]Y 1 to Y 150 ; The following residues NOT assigned to any domain: Chain "Y" 0 - 151 The following residues NOT assigned to any domain: Chain "Y" 0 - 0 Chain "Y" 151 - 151 The following residues NOT assigned to any domain: Chain "Y" 0 - 151 The following residues NOT assigned to any domain: Chain "Y" 0 - 151
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SDA B

OXIDOREDUCTASE(COPPER) 13-JAN-93 :: CU,ZN SUPEROXIDE DISMUTASE (E.C.1.15.1.1) NITRATED

DOMAIN 1: [Assigned by homology with 1COBA]B 1 to B 150 ; The following residues NOT assigned to any domain: Chain "B" 0 - 151 The following residues NOT assigned to any domain: Chain "B" 0 - 151 The following residues NOT assigned to any domain: Chain "B" 0 - 0 Chain "B" 151 - 151 The following residues NOT assigned to any domain: Chain "B" 0 - 151
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SDA G

OXIDOREDUCTASE(COPPER) 13-JAN-93 :: CU,ZN SUPEROXIDE DISMUTASE (E.C.1.15.1.1) NITRATED

DOMAIN 1: [Assigned by homology with 1COBA]G 1 to G 150 ; The following residues NOT assigned to any domain: Chain "G" 0 - 151 The following residues NOT assigned to any domain: Chain "G" 0 - 151 The following residues NOT assigned to any domain: Chain "G" 0 - 151 The following residues NOT assigned to any domain: Chain "G" 0 - 0 Chain "G" 151 - 151
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1COB B

OXIDOREDUCTASE 19-FEB-92 :: SUPEROXIDE DISMUTASE (CO SUBSTITUTED) (E.C.1.15.1.

DOMAIN 1: [Assigned by homology with 1COBA]B 1 to B 150 ; The following residues NOT assigned to any domain: Chain "B" 1 - 151 The following residues NOT assigned to any domain: Chain "B" 151 - 151
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4SOD

OXIDOREDUCTASE(SUPEROXIDE ACCEPTOR) 14-JAN-93 :: CU,ZN SUPEROXIDE DISMUTASE (E.C.1.15.1.1) MUTANT W

DOMAIN 1: [Assigned by homology with 1COBA] 1 to 152 ; The following residues NOT assigned to any domain: Chain " " 0 - 0 Chain " " 153 - 171
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SOS A

OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR) 11-FEB-92 :: SUPEROXIDE DISMUTASE (E.C.1.15.1.1) MUTANT WITH CY

DOMAIN 1: [Assigned by homology with 1COBA]A 1 to A 152 ; The following residues NOT assigned to any domain: Chain "A" 0 - 0 Chain "A" 153 - 153 The following residues NOT assigned to any domain: Chain "A" 0 - 0 The following residues NOT assigned to any domain: Chain "A" 1 - 153 The following residues NOT assigned to any domain: Chain "A" 0 - 153 The following residues NOT assigned to any domain: Chain "A" 0 - 0 The following residues NOT assigned to any domain: Chain "A" 1 - 153 The following residues NOT assigned to any domain: Chain "A" 0 - 153 The following residues NOT assigned to any domain: Chain "A" 0 - 0 The following residues NOT assigned to any domain: Chain "A" 1 - 153 The following residues NOT assigned to any domain: Chain "A" 0 - 153 The following residues NOT assigned to any domain: Chain "A" 0 - 0 The following residues NOT assigned to any domain: Chain "A" 1 - 153 The following residues NOT assigned to any domain: Chain "A" 0 - 153 The following residues NOT assigned to any domain: Chain "A" 0 - 0 The following residues NOT assigned to any domain: Chain "A" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SOS F

OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR) 11-FEB-92 :: SUPEROXIDE DISMUTASE (E.C.1.15.1.1) MUTANT WITH CY

DOMAIN 1: [Assigned by homology with 1COBA]F 1 to F 152 ; The following residues NOT assigned to any domain: Chain "F" 0 - 153 The following residues NOT assigned to any domain: Chain "F" 0 - 0 The following residues NOT assigned to any domain: Chain "F" 153 - 153 The following residues NOT assigned to any domain: Chain "F" 0 - 153 The following residues NOT assigned to any domain: Chain "F" 0 - 0 The following residues NOT assigned to any domain: Chain "F" 1 - 153 The following residues NOT assigned to any domain: Chain "F" 0 - 153 The following residues NOT assigned to any domain: Chain "F" 0 - 0 The following residues NOT assigned to any domain: Chain "F" 1 - 153 The following residues NOT assigned to any domain: Chain "F" 0 - 153 The following residues NOT assigned to any domain: Chain "F" 0 - 0 The following residues NOT assigned to any domain: Chain "F" 1 - 153 The following residues NOT assigned to any domain: Chain "F" 0 - 153 The following residues NOT assigned to any domain: Chain "F" 0 - 0 The following residues NOT assigned to any domain: Chain "F" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SOS B

OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR) 11-FEB-92 :: SUPEROXIDE DISMUTASE (E.C.1.15.1.1) MUTANT WITH CY

DOMAIN 1: [Assigned by homology with 1COBA]B 1 to B 152 ; The following residues NOT assigned to any domain: Chain "B" 0 - 153 The following residues NOT assigned to any domain: Chain "B" 0 - 0 The following residues NOT assigned to any domain: Chain "B" 1 - 153 The following residues NOT assigned to any domain: Chain "B" 0 - 0 Chain "B" 153 - 153 The following residues NOT assigned to any domain: Chain "B" 0 - 0 The following residues NOT assigned to any domain: Chain "B" 1 - 153 The following residues NOT assigned to any domain: Chain "B" 0 - 153 The following residues NOT assigned to any domain: Chain "B" 0 - 0 The following residues NOT assigned to any domain: Chain "B" 1 - 153 The following residues NOT assigned to any domain: Chain "B" 0 - 153 The following residues NOT assigned to any domain: Chain "B" 0 - 0 The following residues NOT assigned to any domain: Chain "B" 1 - 153 The following residues NOT assigned to any domain: Chain "B" 0 - 153 The following residues NOT assigned to any domain: Chain "B" 0 - 0 The following residues NOT assigned to any domain: Chain "B" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SOS G

OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR) 11-FEB-92 :: SUPEROXIDE DISMUTASE (E.C.1.15.1.1) MUTANT WITH CY

DOMAIN 1: [Assigned by homology with 1COBA]G 1 to G 152 ; The following residues NOT assigned to any domain: Chain "G" 0 - 153 The following residues NOT assigned to any domain: Chain "G" 0 - 0 The following residues NOT assigned to any domain: Chain "G" 1 - 153 The following residues NOT assigned to any domain: Chain "G" 0 - 153 The following residues NOT assigned to any domain: Chain "G" 0 - 0 The following residues NOT assigned to any domain: Chain "G" 153 - 153 The following residues NOT assigned to any domain: Chain "G" 0 - 153 The following residues NOT assigned to any domain: Chain "G" 0 - 0 The following residues NOT assigned to any domain: Chain "G" 1 - 153 The following residues NOT assigned to any domain: Chain "G" 0 - 153 The following residues NOT assigned to any domain: Chain "G" 0 - 0 The following residues NOT assigned to any domain: Chain "G" 1 - 153 The following residues NOT assigned to any domain: Chain "G" 0 - 153 The following residues NOT assigned to any domain: Chain "G" 0 - 0 The following residues NOT assigned to any domain: Chain "G" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SOS C

OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR) 11-FEB-92 :: SUPEROXIDE DISMUTASE (E.C.1.15.1.1) MUTANT WITH CY

DOMAIN 1: [Assigned by homology with 1COBA]C 1 to C 152 ; The following residues NOT assigned to any domain: Chain "C" 0 - 153 The following residues NOT assigned to any domain: Chain "C" 0 - 0 The following residues NOT assigned to any domain: Chain "C" 1 - 153 The following residues NOT assigned to any domain: Chain "C" 0 - 153 The following residues NOT assigned to any domain: Chain "C" 0 - 0 The following residues NOT assigned to any domain: Chain "C" 1 - 153 The following residues NOT assigned to any domain: Chain "C" 0 - 0 Chain "C" 153 - 153 The following residues NOT assigned to any domain: Chain "C" 0 - 0 The following residues NOT assigned to any domain: Chain "C" 1 - 153 The following residues NOT assigned to any domain: Chain "C" 0 - 153 The following residues NOT assigned to any domain: Chain "C" 0 - 0 The following residues NOT assigned to any domain: Chain "C" 1 - 153 The following residues NOT assigned to any domain: Chain "C" 0 - 153 The following residues NOT assigned to any domain: Chain "C" 0 - 0 The following residues NOT assigned to any domain: Chain "C" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SOS H

OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR) 11-FEB-92 :: SUPEROXIDE DISMUTASE (E.C.1.15.1.1) MUTANT WITH CY

DOMAIN 1: [Assigned by homology with 1COBA]H 1 to H 152 ; The following residues NOT assigned to any domain: Chain "H" 0 - 153 The following residues NOT assigned to any domain: Chain "H" 0 - 0 The following residues NOT assigned to any domain: Chain "H" 1 - 153 The following residues NOT assigned to any domain: Chain "H" 0 - 153 The following residues NOT assigned to any domain: Chain "H" 0 - 0 The following residues NOT assigned to any domain: Chain "H" 1 - 153 The following residues NOT assigned to any domain: Chain "H" 0 - 153 The following residues NOT assigned to any domain: Chain "H" 0 - 0 The following residues NOT assigned to any domain: Chain "H" 153 - 153 The following residues NOT assigned to any domain: Chain "H" 0 - 153 The following residues NOT assigned to any domain: Chain "H" 0 - 0 The following residues NOT assigned to any domain: Chain "H" 1 - 153 The following residues NOT assigned to any domain: Chain "H" 0 - 153 The following residues NOT assigned to any domain: Chain "H" 0 - 0 The following residues NOT assigned to any domain: Chain "H" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SOS D

OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR) 11-FEB-92 :: SUPEROXIDE DISMUTASE (E.C.1.15.1.1) MUTANT WITH CY

DOMAIN 1: [Assigned by homology with 1COBA]D 1 to D 152 ; The following residues NOT assigned to any domain: Chain "D" 0 - 153 The following residues NOT assigned to any domain: Chain "D" 0 - 0 The following residues NOT assigned to any domain: Chain "D" 1 - 153 The following residues NOT assigned to any domain: Chain "D" 0 - 153 The following residues NOT assigned to any domain: Chain "D" 0 - 0 The following residues NOT assigned to any domain: Chain "D" 1 - 153 The following residues NOT assigned to any domain: Chain "D" 0 - 153 The following residues NOT assigned to any domain: Chain "D" 0 - 0 The following residues NOT assigned to any domain: Chain "D" 1 - 153 The following residues NOT assigned to any domain: Chain "D" 0 - 0 Chain "D" 153 - 153 The following residues NOT assigned to any domain: Chain "D" 0 - 0 The following residues NOT assigned to any domain: Chain "D" 1 - 153 The following residues NOT assigned to any domain: Chain "D" 0 - 153 The following residues NOT assigned to any domain: Chain "D" 0 - 0 The following residues NOT assigned to any domain: Chain "D" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SOS I

OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR) 11-FEB-92 :: SUPEROXIDE DISMUTASE (E.C.1.15.1.1) MUTANT WITH CY

DOMAIN 1: [Assigned by homology with 1COBA]I 1 to I 152 ; The following residues NOT assigned to any domain: Chain "I" 0 - 153 The following residues NOT assigned to any domain: Chain "I" 0 - 0 The following residues NOT assigned to any domain: Chain "I" 1 - 153 The following residues NOT assigned to any domain: Chain "I" 0 - 153 The following residues NOT assigned to any domain: Chain "I" 0 - 0 The following residues NOT assigned to any domain: Chain "I" 1 - 153 The following residues NOT assigned to any domain: Chain "I" 0 - 153 The following residues NOT assigned to any domain: Chain "I" 0 - 0 The following residues NOT assigned to any domain: Chain "I" 1 - 153 The following residues NOT assigned to any domain: Chain "I" 0 - 153 The following residues NOT assigned to any domain: Chain "I" 0 - 0 The following residues NOT assigned to any domain: Chain "I" 153 - 153 The following residues NOT assigned to any domain: Chain "I" 0 - 153 The following residues NOT assigned to any domain: Chain "I" 0 - 0 The following residues NOT assigned to any domain: Chain "I" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SOS E

OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR) 11-FEB-92 :: SUPEROXIDE DISMUTASE (E.C.1.15.1.1) MUTANT WITH CY

DOMAIN 1: [Assigned by homology with 1COBA]E 1 to E 152 ; The following residues NOT assigned to any domain: Chain "E" 0 - 153 The following residues NOT assigned to any domain: Chain "E" 0 - 0 The following residues NOT assigned to any domain: Chain "E" 1 - 153 The following residues NOT assigned to any domain: Chain "E" 0 - 153 The following residues NOT assigned to any domain: Chain "E" 0 - 0 The following residues NOT assigned to any domain: Chain "E" 1 - 153 The following residues NOT assigned to any domain: Chain "E" 0 - 153 The following residues NOT assigned to any domain: Chain "E" 0 - 0 The following residues NOT assigned to any domain: Chain "E" 1 - 153 The following residues NOT assigned to any domain: Chain "E" 0 - 153 The following residues NOT assigned to any domain: Chain "E" 0 - 0 The following residues NOT assigned to any domain: Chain "E" 1 - 153 The following residues NOT assigned to any domain: Chain "E" 0 - 0 Chain "E" 153 - 153 The following residues NOT assigned to any domain: Chain "E" 0 - 0 The following residues NOT assigned to any domain: Chain "E" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SOS J

OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR) 11-FEB-92 :: SUPEROXIDE DISMUTASE (E.C.1.15.1.1) MUTANT WITH CY

DOMAIN 1: [Assigned by homology with 1COBA]J 1 to J 152 ; The following residues NOT assigned to any domain: Chain "J" 0 - 153 The following residues NOT assigned to any domain: Chain "J" 0 - 0 The following residues NOT assigned to any domain: Chain "J" 1 - 153 The following residues NOT assigned to any domain: Chain "J" 0 - 153 The following residues NOT assigned to any domain: Chain "J" 0 - 0 The following residues NOT assigned to any domain: Chain "J" 1 - 153 The following residues NOT assigned to any domain: Chain "J" 0 - 153 The following residues NOT assigned to any domain: Chain "J" 0 - 0 The following residues NOT assigned to any domain: Chain "J" 1 - 153 The following residues NOT assigned to any domain: Chain "J" 0 - 153 The following residues NOT assigned to any domain: Chain "J" 0 - 0 The following residues NOT assigned to any domain: Chain "J" 1 - 153 The following residues NOT assigned to any domain: Chain "J" 0 - 153 The following residues NOT assigned to any domain: Chain "J" 0 - 0 The following residues NOT assigned to any domain: Chain "J" 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SPD A

OXIDOREDUCTASE(SUPEROXIDE ACCEPTOR) 21-JUL-93 :: SUPEROXIDE DISMUTASE (E.C.1.15.1.1)

DOMAIN 1: [Assigned by homology with 1COBA]A 1 to A 152 ; The following residues NOT assigned to any domain: Chain "A" 0 - 0 Chain "A" 153 - 153 The following residues NOT assigned to any domain: Chain "A" 0 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SPD B

OXIDOREDUCTASE(SUPEROXIDE ACCEPTOR) 21-JUL-93 :: SUPEROXIDE DISMUTASE (E.C.1.15.1.1)

DOMAIN 1: [Assigned by homology with 1COBA]B 1 to B 152 ; The following residues NOT assigned to any domain: Chain "B" 0 - 153 The following residues NOT assigned to any domain: Chain "B" 0 - 0 Chain "B" 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SRD A

OXIDOREDUCTASE(SUPEROXIDE ACCEPTOR) 15-APR-93 :: CU,ZN SUPEROXIDE DISMUTASE (E.C.1.15.1.1)

DOMAIN 1: [Assigned by homology with 1COBA]A 1 to A 152 ; The following residues NOT assigned to any domain: Chain "A" 153 - 154 The following residues NOT assigned to any domain: Chain "A" 1 - 154 The following residues NOT assigned to any domain: Chain "A" 1 - 154 The following residues NOT assigned to any domain: Chain "A" 1 - 154
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SRD B

OXIDOREDUCTASE(SUPEROXIDE ACCEPTOR) 15-APR-93 :: CU,ZN SUPEROXIDE DISMUTASE (E.C.1.15.1.1)

DOMAIN 1: [Assigned by homology with 1COBA]B 1 to B 152 ; The following residues NOT assigned to any domain: Chain "B" 1 - 154 The following residues NOT assigned to any domain: Chain "B" 153 - 154 The following residues NOT assigned to any domain: Chain "B" 1 - 154 The following residues NOT assigned to any domain: Chain "B" 1 - 154
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SRD C

OXIDOREDUCTASE(SUPEROXIDE ACCEPTOR) 15-APR-93 :: CU,ZN SUPEROXIDE DISMUTASE (E.C.1.15.1.1)

DOMAIN 1: [Assigned by homology with 1COBA]C 1 to C 152 ; The following residues NOT assigned to any domain: Chain "C" 1 - 154 The following residues NOT assigned to any domain: Chain "C" 1 - 154 The following residues NOT assigned to any domain: Chain "C" 153 - 154 The following residues NOT assigned to any domain: Chain "C" 1 - 154
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SRD D

OXIDOREDUCTASE(SUPEROXIDE ACCEPTOR) 15-APR-93 :: CU,ZN SUPEROXIDE DISMUTASE (E.C.1.15.1.1)

DOMAIN 1: [Assigned by homology with 1COBA]D 1 to D 152 ; The following residues NOT assigned to any domain: Chain "D" 1 - 154 The following residues NOT assigned to any domain: Chain "D" 1 - 154 The following residues NOT assigned to any domain: Chain "D" 1 - 154 The following residues NOT assigned to any domain: Chain "D" 153 - 154
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SDY A

OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR) 14-JUN-91 :: CU, ZN SUPEROXIDE DISMUTASE (E.C.1.15.1.1)

DOMAIN 1: [Assigned by homology with 1COBA]A 2 to A 150 ; The following residues NOT assigned to any domain: Chain "A" 151 - 151 The following residues NOT assigned to any domain: Chain "A" 2 - 151 The following residues NOT assigned to any domain: Chain "A" 2 - 151 The following residues NOT assigned to any domain: Chain "A" 2 - 151
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SDY B

OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR) 14-JUN-91 :: CU, ZN SUPEROXIDE DISMUTASE (E.C.1.15.1.1)

DOMAIN 1: [Assigned by homology with 1COBA]B 2 to B 150 ; The following residues NOT assigned to any domain: Chain "B" 2 - 151 The following residues NOT assigned to any domain: Chain "B" 151 - 151 The following residues NOT assigned to any domain: Chain "B" 2 - 151 The following residues NOT assigned to any domain: Chain "B" 2 - 151
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SDY C

OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR) 14-JUN-91 :: CU, ZN SUPEROXIDE DISMUTASE (E.C.1.15.1.1)

DOMAIN 1: [Assigned by homology with 1COBA]C 2 to C 150 ; The following residues NOT assigned to any domain: Chain "C" 2 - 151 The following residues NOT assigned to any domain: Chain "C" 2 - 151 The following residues NOT assigned to any domain: Chain "C" 151 - 151 The following residues NOT assigned to any domain: Chain "C" 2 - 151
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SDY D

OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR) 14-JUN-91 :: CU, ZN SUPEROXIDE DISMUTASE (E.C.1.15.1.1)

DOMAIN 1: [Assigned by homology with 1COBA]D 2 to D 150 ; The following residues NOT assigned to any domain: Chain "D" 2 - 151 The following residues NOT assigned to any domain: Chain "D" 2 - 151 The following residues NOT assigned to any domain: Chain "D" 2 - 151 The following residues NOT assigned to any domain: Chain "D" 151 - 151
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EGL

PROTEINASE INHIBITOR 03-SEP-93 :: EGLIN C (NMR, 25 STRUCTURES)

DOMAIN 1: [Assigned by homology with 1CSEI] 1 to 69 ; The following residues NOT assigned to any domain: Chain " " 70 - 70
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3TEC I

COMPLEX(SERINE PROTEINASE-INHIBITOR) 26-OCT-90 :: THERMITASE (E.C.3.4.21.14) COMPLEX WITH EGLIN-C

DOMAIN 1: [Assigned by homology with 1CSEI]I 8 to I 69 ; The following residues NOT assigned to any domain: Chain "I" 1 - 279 The following residues NOT assigned to any domain: Chain "I" 70 - 70
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2TEC I

COMPLEX(SERINE PROTEINASE-INHIBITOR) 26-OCT-90 :: THERMITASE (E.C.3.4.21.14) COMPLEX WITH EGLIN-C

DOMAIN 1: [Assigned by homology with 1CSEI]I 8 to I 69 ; The following residues NOT assigned to any domain: Chain "I" 1 - 279 The following residues NOT assigned to any domain: Chain "I" 70 - 70
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ACB I

HYDROLASE(SERINE PROTEASE) 08-NOV-91 :: ALPHA-CHYMOTRYPSIN (E.C.3.4.21.1) COMPLEX WITH EGL

DOMAIN 1: [Assigned by homology with 1CSEI]I 8 to I 69 ; The following residues NOT assigned to any domain: Chain "I" 1 - 13 The following residues NOT assigned to any domain: Chain "I" 16 - 146 The following residues NOT assigned to any domain: Chain "I" 149 - 245 The following residues NOT assigned to any domain: Chain "I" 70 - 70
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TEC I

COMPLEX(SERINE PROTEINASE-INHIBITOR) 24-MAY-89 :: THERMITASE (E.C.3.4.21.14) COMPLEX WITH EGLIN-C

DOMAIN 1: [Assigned by homology with 1CSEI]I 8 to I 69 ; The following residues NOT assigned to any domain: Chain "I" 1 - 279 The following residues NOT assigned to any domain: Chain "I" 70 - 70
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MEE I

COMPLEX(SERINE PROTEINASE-INHIBITOR) 15-APR-91 :: MESENTERICOPEPTIDASE (E.C.3.4.21.14) PEPTIDYL PEPT

DOMAIN 1: [Assigned by homology with 1CSEI]I 7 to I 69 ; The following residues NOT assigned to any domain: Chain "I" 1 - 275 The following residues NOT assigned to any domain: Chain "I" 70 - 70
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2SEC I

COMPLEX(SERINE PROTEINASE-INHIBITOR) 05-SEP-88 :: SUBTILISIN CARLSBERG (E.C.3.4.21.62) COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1CSEI]I 21 to I 82 ; The following residues NOT assigned to any domain: Chain "I" 1 - 275 The following residues NOT assigned to any domain: Chain "I" 83 - 83
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SIB I

SERINE PROTEASE/INHIBITOR COMPLEX 02-AUG-93 :: SUBTILISIN NOVO (BPN') (E.C.3.4.21.62) COMPLEX WIT

DOMAIN 1: [Assigned by homology with 1CSEI]I 8 to I 69 ; The following residues NOT assigned to any domain: Chain "I" 1 - 275 The following residues NOT assigned to any domain: Chain "I" 70 - 70
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SBN I

PRELIMINARY 20-DEC-91 :: SUBTILISIN *NOVO (/BPN$')(E.C.3.4.21.14) COMPLEXED

DOMAIN 1: [Assigned by homology with 1CSEI]I 8 to I 69 ; The following residues NOT assigned to any domain: Chain "I" 70 - 70 The following residues NOT assigned to any domain: Chain "I" 1 - 275
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EAA

DIHYDROLIPOAMIDE ACETYLTRANSFERASE 16-DEC-92 :: DIHYDROLIPOYL TRANSACETYLASE (E.C.2.3.1.12) (CATAL

DOMAIN 1: 395 to 637 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EAB

DIHYDROLIPOAMIDE ACETYLTRANSFERASE 16-DEC-92 :: DIHYDROLIPOYL TRANSACETYLASE (E.C.2.3.1.12) (CATAL

DOMAIN 1: 395 to 637 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EAC

DIHYDROLIPOAMIDE ACETYLTRANSFERASE 16-DEC-92 :: DIHYDROLIPOYL TRANSACETYLASE (E.C.2.3.1.12) (CATAL

DOMAIN 1: 395 to 637 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EAD

DIHYDROLIPOAMIDE ACETYLTRANSFERASE 16-DEC-92 :: DIHYDROLIPOYL TRANSACETYLASE (E.C.2.3.1.12) (CATAL

DOMAIN 1: 395 to 637 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EAE

DIHYDROLIPOAMIDE ACETYLTRANSFERASE 16-DEC-92 :: DIHYDROLIPOYL TRANSACETYLASE (E.C.2.3.1.12) (CATAL

DOMAIN 1: 395 to 637 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ECA

OXYGEN TRANSPORT 07-MAR-79 :: HEMOGLOBIN (ERYTHROCRUORIN, AQUO MET)

DOMAIN 1: 1 to 136 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ECD

OXYGEN TRANSPORT 07-MAR-79 :: HEMOGLOBIN (ERYTHROCRUORIN, DEOXY)

DOMAIN 1: 1 to 136 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ECN

OXYGEN TRANSPORT 07-MAR-79 :: HEMOGLOBIN (ERYTHROCRUORIN, CYANO MET)

DOMAIN 1: 1 to 136 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EPG

PRELIMINARY 24-MAR-92 :: EPIDERMAL GROWTH FACTOR (EGF) IN PH 2 SOLUTION (/N

DOMAIN 1: 1 to 53 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EPH

PRELIMINARY 24-MAR-92 :: EPIDERMAL GROWTH FACTOR (EGF) IN PH 2 SOLUTION (/N

DOMAIN 1: 1 to 53 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EPI

PRELIMINARY 24-MAR-92 :: EPIDERMAL GROWTH FACTOR (EGF) IN PH 6.8 SOLUTION (

DOMAIN 1: 1 to 53 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EPJ

PRELIMINARY 24-MAR-92 :: EPIDERMAL GROWTH FACTOR (EGF) IN PH 6.8 SOLUTION (

DOMAIN 1: 1 to 53 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3EGF

GROWTH FACTOR 30-AUG-92 :: EPIDERMAL GROWTH FACTOR (EGF) (NMR, 16 STRUCTURES

DOMAIN 1: 1 to 53 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NTX

PRELIMINARY 30-APR-92 :: ALPHA-NEUROTOXIN (NMR,20 STRUCTURES)

DOMAIN 1: 1 to 62 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NOR

NEUROTOXIN 05-APR-93 :: NEUROTOXIN II (NMR, 19 STRUCTURES)

DOMAIN 1: 1 to 61 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NEA

TOXIN 22-SEP-92 :: TOXIN ALPHA (NMR, 8 STRUCTURES)

DOMAIN 1: 1 to 61 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5EBX

TOXIN 20-DEC-89 :: ERABUTOXIN $A

DOMAIN 1: 1 to 62 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ERA

TOXIN 28-MAR-94 :: ERABUTOXIN B (NMR, MINIMIZED AVERAGE STRUCTURE)

DOMAIN 1: 1 to 62 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6EBX A

TOXIN 31-MAY-91 :: ERABUTOXIN $B (DIMERIC FORM) CRYSTALLIZED FROM KSC

DOMAIN 1: A 1 to A 62 ; The following residues NOT assigned to any domain: Chain "A" 1 - 62
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6EBX B

TOXIN 31-MAY-91 :: ERABUTOXIN $B (DIMERIC FORM) CRYSTALLIZED FROM KSC

DOMAIN 1: B 1 to B 62 ; The following residues NOT assigned to any domain: Chain "B" 1 - 62
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FRA

TOXIN 28-MAR-94 :: ERABUTOXIN B (NMR, 14 STRUCTURES)

DOMAIN 1: 1 to 62 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NXB

NEUROTOXIN (POST-SYNAPTIC) 08-AUG-80 :: NEUROTOXIN $B (PROBABLY IDENTICAL TO ERABUTOXIN $B

DOMAIN 1: 1 to 62 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3EBX

TOXIN 15-JAN-88 :: ERABUTOXIN $B

DOMAIN 1: 1 to 62 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DRS

CELL ADHESION PROTEIN 29-SEP-94 :: DENDROASPIN (MAMBIN, S5C1/SH04) (NMR, 39 STRUCTURE

DOMAIN 1: 1 to 59 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FBA B

LYASE(ALDEHYDE) 08-JUN-92 :: FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE (E.C.4.1.2.13)

DOMAIN 1: [Assigned by homology with 1FBAA]B 1 to B 363 ; The following residues NOT assigned to any domain: Chain "B" 0 - 363 The following residues NOT assigned to any domain: Chain "B" 0 - 0 The following residues NOT assigned to any domain: Chain "B" 0 - 363 The following residues NOT assigned to any domain: Chain "B" 0 - 363
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FBA C

LYASE(ALDEHYDE) 08-JUN-92 :: FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE (E.C.4.1.2.13)

DOMAIN 1: [Assigned by homology with 1FBAA]C 1 to C 363 ; The following residues NOT assigned to any domain: Chain "C" 0 - 363 The following residues NOT assigned to any domain: Chain "C" 0 - 363 The following residues NOT assigned to any domain: Chain "C" 0 - 0 The following residues NOT assigned to any domain: Chain "C" 0 - 363
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FBA D

LYASE(ALDEHYDE) 08-JUN-92 :: FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE (E.C.4.1.2.13)

DOMAIN 1: [Assigned by homology with 1FBAA]D 1 to D 363 ; The following residues NOT assigned to any domain: Chain "D" 0 - 363 The following residues NOT assigned to any domain: Chain "D" 0 - 363 The following residues NOT assigned to any domain: Chain "D" 0 - 363 The following residues NOT assigned to any domain: Chain "D" 0 - 0
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ALD

LYASE (ALDEHYDE) 05-MAY-91 :: ALDOLASE *A (E.C.4.1.2.13)

DOMAIN 1: [Assigned by homology with 1FBAA] 1 to 363 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MB5

OXYGEN STORAGE 11-OCT-89 :: MYOGLOBIN (CARBONMONOXYMYOGLOBIN) (NEUTRON STUDY)

DOMAIN 1: 1 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MYA

OXYGEN STORAGE 04-AUG-93 :: MYOGLOBIN (ETHYL ISOCYANIDE, PH 7.0)

DOMAIN 1: 1 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MYB

OXYGEN STORAGE 04-AUG-93 :: MYOGLOBIN (METHYL ISOCYANIDE, PH 7.0)

DOMAIN 1: 1 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4MBN

OXYGEN STORAGE 14-JAN-88 :: MYOGLOBIN (MET)

DOMAIN 1: 1 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MYC

OXYGEN STORAGE 04-AUG-93 :: MYOGLOBIN (N-BUTYL ISOCYANIDE, PH 7.0)

DOMAIN 1: 1 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MYD

OXYGEN STORAGE 04-AUG-93 :: MYOGLOBIN (N-PROPYL ISOCYANIDE, PH 7.0)

DOMAIN 1: 1 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MYE

OXYGEN STORAGE 04-AUG-93 :: MYOGLOBIN (ETHYL ISOCYANIDE, PH <<7.0)

DOMAIN 1: 1 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MBC

OXYGEN STORAGE 15-SEP-88 :: MYOGLOBIN (FE /II$, CARBONMONOXY, 260 DEGREES K)

DOMAIN 1: 1 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MBD

OXYGEN STORAGE 27-AUG-81 :: MYOGLOBIN (DEOXY, $P*H 8.4)

DOMAIN 1: 1 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MBI

OXYGEN STORAGE 25-JUN-90 :: MYOGLOBIN (FERRIC) COMPLEX WITH IMIDAZOLE

DOMAIN 1: 1 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MBN

OXYGEN STORAGE 05-APR-73 :: MYOGLOBIN (FERRIC IRON - METMYOGLOBIN)

DOMAIN 1: 1 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MBO

OXYGEN STORAGE 27-AUG-81 :: MYOGLOBIN (OXY, $P*H 8.4)

DOMAIN 1: 1 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5MBN

OXYGEN STORAGE 14-JAN-88 :: MYOGLOBIN (DEOXY)

DOMAIN 1: 1 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CMM

OXYGEN TRANSPORT 24-DEC-93 :: MYOGLOBIN (CYANO,MET) RECONSTITUTED WITH IRON (III

DOMAIN 1: 1 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SWM

PRELIMINARY 03-MAR-92 :: FERRIC MYOGLOBIN COMPLEX WITH AZIDE

DOMAIN 1: 1 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MGK

OXYGEN STORAGE 10-MAY-93 :: MYOGLOBIN (CARBONMONOXY) MUTANT WITH INITIATOR MET

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MGL

OXYGEN STORAGE 10-MAY-93 :: MYOGLOBIN (DEOXY) MUTANT WITH INITIATOR MET AND AS

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MGM

OXYGEN STORAGE 10-MAY-93 :: MYOGLOBIN (OXY) MUTANT WITH INITIATOR MET AND ASP

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MBW

OXYGEN STORAGE 05-OCT-89 :: MYOGLOBIN (MET) (MUTANT WITH INITIATOR MET AND WIT

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MLM

OXYGEN STORAGE 15-JUN-94 :: MYOGLOBIN (CARBONMONOXY) MUTANT WITH INITIATOR MET

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MLN

OXYGEN STORAGE 15-JUN-94 :: MYOGLOBIN (DEOXY) MUTANT WITH INITIATOR MET, VAL 6

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MLO

OXYGEN STORAGE 15-JUN-94 :: MYOGLOBIN (MET) MUTANT WITH INITIATOR MET, VAL 68

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MGF

OXYGEN STORAGE 10-MAY-93 :: MYOGLOBIN (CARBONMONOXY) MUTANT WITH INITIATOR MET

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MGG

OXYGEN STORAGE 10-MAY-93 :: MYOGLOBIN (DEOXY) MUTANT WITH INITIATOR MET AND

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MGH

OXYGEN STORAGE 10-MAY-93 :: MYOGLOBIN (MET) MUTANT WITH INITIATOR MET, HIS 64

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MLR

OXYGEN STORAGE 15-JUN-94 :: MYOGLOBIN (DEOXY) MUTANT WITH INITIATOR MET, VAL 6

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MLS

OXYGEN STORAGE 15-JUN-94 :: MYOGLOBIN (MET) MUTANT WITH INITIATOR MET, VAL 68

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2SPO

OXYGEN STORAGE 25-AUG-93 :: MYOGLOBIN (MET) MUTANT WITH INITIATOR MET, LEU 29

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MLF

OXYGEN STORAGE 15-JUN-94 :: MYOGLOBIN (CARBONMONOXY) MUTANT WITH INITIATOR MET

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MLG

OXYGEN STORAGE 15-JUN-94 :: MYOGLOBIN (DEOXY) MUTANT WITH INITIATOR MET, VAL 6

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MLH

OXYGEN STORAGE 15-JUN-94 :: MYOGLOBIN (MET) MUTANT WITH INITIATOR MET, VAL 68

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2SPL

OXYGEN STORAGE 25-AUG-93 :: MYOGLOBIN (CARBONMONOXY) MUTANT WITH INITIATOR MET

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2SPM

OXYGEN STORAGE 25-AUG-93 :: MYOGLOBIN (MET) MUTANT WITH INITIATOR MET, ASP 122

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2SPN

OXYGEN STORAGE 25-AUG-93 :: MYOGLOBIN (OXY) MUTANT WITH INITIATOR MET, LEU 29

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MGN

OXYGEN TRANSPORT 29-OCT-93 :: METMYOGLOBIN MUTANT WITH INITIATOR MET, ASP 122 RE

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MLJ

OXYGEN STORAGE 15-JUN-94 :: MYOGLOBIN (CARBONMONOXY) MUTANT WITH INITIATOR MET

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MLK

OXYGEN STORAGE 15-JUN-94 :: MYOGLOBIN (DEOXY) MUTANT WITH INITIATOR MET, VAL 6

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MLL

OXYGEN STORAGE 15-JUN-94 :: MYOGLOBIN (MET) MUTANT WITH INITIATOR MET, VAL 68

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MGC

OXYGEN STORAGE 10-MAY-93 :: MYOGLOBIN (CARBONMONOXY) MUTANT WITH INITIATOR MET

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MGD

OXYGEN STORAGE 10-MAY-93 :: MYOGLOBIN (DEOXY) MUTANT WITH INITIATOR MET, ASP 1

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MGE

OXYGEN STORAGE 10-MAY-93 :: MYOGLOBIN (MET) MUTANT WITH INITIATOR MET, ASP 122

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MGI

OXYGEN STORAGE 10-MAY-93 :: MYOGLOBIN (MET) MUTANT WITH INITIATOR MET, ASP 122

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MGJ

OXYGEN STORAGE 10-MAY-93 :: MYOGLOBIN (MET) MUTANT WITH INITIATOR MET, ASP 122

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MGA

OXYGEN STORAGE 10-MAY-93 :: MYOGLOBIN (CARBONMONOXY) MUTANT WITH INITIATOR MET

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MGB

OXYGEN STORAGE 10-MAY-93 :: MYOGLOBIN (MET) MUTANT WITH INITIATOR MET, HIS 64

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MYM

OXYGEN TRANSPORT 14-OCT-93 :: MYOGLOBIN (CARBONMONOXY) MUTANT WITH INITIATOR MET

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MLU

OXYGEN STORAGE 15-JUN-94 :: MYOGLOBIN (CARBONMONOXY) MUTANT WITH INITIATOR MET

DOMAIN 1: 0 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1YMB

OXYGEN TRANSPORT 27-SEP-93 :: METMYOGLOBIN (HORSE HEART)

DOMAIN 1: 1 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1YMC

OXYGEN TRANSPORT 27-SEP-93 :: CYANOMET-SULFMYOGLOBIN (HORSE HEART)

DOMAIN 1: 1 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MM1

OXYGEN TRANSPORT 19-FEB-91 :: MYOGLOBIN MUTANT WITH LYS 45 REPLACED BY ARG AND C

DOMAIN 1: 1 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MYH A

OXYGEN STORAGE 27-FEB-92 :: MYOGLOBIN (AQUOMET, PH 7.1) MUTANT WITH LYS 45 REP

DOMAIN 1: A 1 to A 152 ; The following residues NOT assigned to any domain: Chain "A" 153 - 153 The following residues NOT assigned to any domain: Chain "A" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MYH B

OXYGEN STORAGE 27-FEB-92 :: MYOGLOBIN (AQUOMET, PH 7.1) MUTANT WITH LYS 45 REP

DOMAIN 1: B 1 to B 152 ; The following residues NOT assigned to any domain: Chain "B" 1 - 153 The following residues NOT assigned to any domain: Chain "B" 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1YMA

OXYGEN TRANSPORT 27-SEP-93 :: MYOGLOBIN (HORSE HEART) MUTANT WITH HIS 64 REPLACE

DOMAIN 1: 1 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MYG A

OXYGEN STORAGE 27-FEB-92 :: MYOGLOBIN (AQUOMET, PH 7.1)

DOMAIN 1: A 1 to A 152 ; The following residues NOT assigned to any domain: Chain "A" 153 - 153 The following residues NOT assigned to any domain: Chain "A" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MYG B

OXYGEN STORAGE 27-FEB-92 :: MYOGLOBIN (AQUOMET, PH 7.1)

DOMAIN 1: B 1 to B 152 ; The following residues NOT assigned to any domain: Chain "B" 1 - 153 The following residues NOT assigned to any domain: Chain "B" 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PMB A

OXYGEN STORAGE 27-NOV-89 :: MYOGLOBIN (AQUOMET, $P*H 7.1)

DOMAIN 1: A 1 to A 152 ; The following residues NOT assigned to any domain: Chain "A" 153 - 153 The following residues NOT assigned to any domain: Chain "A" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PMB B

OXYGEN STORAGE 27-NOV-89 :: MYOGLOBIN (AQUOMET, $P*H 7.1)

DOMAIN 1: B 1 to B 152 ; The following residues NOT assigned to any domain: Chain "B" 1 - 153 The following residues NOT assigned to any domain: Chain "B" 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MYI A

OXYGEN STORAGE 27-FEB-92 :: MYOGLOBIN (AQUOMET, PH 7.1) MUTANT WITH LYS 45 REP

DOMAIN 1: A 1 to A 152 ; The following residues NOT assigned to any domain: Chain "A" 153 - 153 The following residues NOT assigned to any domain: Chain "A" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MYI B

OXYGEN STORAGE 27-FEB-92 :: MYOGLOBIN (AQUOMET, PH 7.1) MUTANT WITH LYS 45 REP

DOMAIN 1: B 1 to B 152 ; The following residues NOT assigned to any domain: Chain "B" 1 - 153 The following residues NOT assigned to any domain: Chain "B" 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1YCA A

OXYGEN STORAGE 10-AUG-93 :: MYOGLOBIN (CARBONMONOXY, PH 7.1) MUTANT WITH VAL 6

DOMAIN 1: A 1 to A 152 ; The following residues NOT assigned to any domain: Chain "A" 153 - 153 The following residues NOT assigned to any domain: Chain "A" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1YCA B

OXYGEN STORAGE 10-AUG-93 :: MYOGLOBIN (CARBONMONOXY, PH 7.1) MUTANT WITH VAL 6

DOMAIN 1: B 1 to B 152 ; The following residues NOT assigned to any domain: Chain "B" 1 - 153 The following residues NOT assigned to any domain: Chain "B" 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1YCB A

OXYGEN STORAGE 10-AUG-93 :: MYOGLOBIN (DEOXY, PH 7.1) MUTANT WITH VAL 68

DOMAIN 1: A 1 to A 152 ; The following residues NOT assigned to any domain: Chain "A" 153 - 153 The following residues NOT assigned to any domain: Chain "A" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1YCB B

OXYGEN STORAGE 10-AUG-93 :: MYOGLOBIN (DEOXY, PH 7.1) MUTANT WITH VAL 68

DOMAIN 1: B 1 to B 152 ; The following residues NOT assigned to any domain: Chain "B" 1 - 153 The following residues NOT assigned to any domain: Chain "B" 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MYJ A

OXYGEN STORAGE 27-FEB-92 :: MYOGLOBIN (AQUOMET, PH 7.1) MUTANT WITH VAL 68 REP

DOMAIN 1: A 1 to A 152 ; The following residues NOT assigned to any domain: Chain "A" 153 - 153 The following residues NOT assigned to any domain: Chain "A" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MYJ B

OXYGEN STORAGE 27-FEB-92 :: MYOGLOBIN (AQUOMET, PH 7.1) MUTANT WITH VAL 68 REP

DOMAIN 1: B 1 to B 152 ; The following residues NOT assigned to any domain: Chain "B" 1 - 153 The following residues NOT assigned to any domain: Chain "B" 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MBS

OXYGEN TRANSPORT 22-MAR-79 :: MYOGLOBIN (MET)

DOMAIN 1: 1 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MYT

OXYGEN TRANSPORT 06-MAY-91 :: MYOGLOBIN (MET)

DOMAIN 1: 5 to 152 ; The following residues NOT assigned to any domain: Chain " " 153 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PGH A

OXYGEN TRANSPORT 16-SEP-94 :: HEMOGLOBIN (AQUOMET)

DOMAIN 1: A 1 to A 141 ; The following residues NOT assigned to any domain: Chain "A" 1 - 146 The following residues NOT assigned to any domain: Chain "A" 1 - 141 The following residues NOT assigned to any domain: Chain "A" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PGH C

OXYGEN TRANSPORT 16-SEP-94 :: HEMOGLOBIN (AQUOMET)

DOMAIN 1: C 1 to C 141 ; The following residues NOT assigned to any domain: Chain "C" 1 - 141 The following residues NOT assigned to any domain: Chain "C" 1 - 146 The following residues NOT assigned to any domain: Chain "C" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MHB A

OXYGEN TRANSPORT 14-FEB-77 :: HEMOGLOBIN (HORSE, AQUO MET)

DOMAIN 1: A 1 to A 141 ; The following residues NOT assigned to any domain: Chain "A" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2DHB A

OXYGEN TRANSPORT 01-NOV-73 :: HEMOGLOBIN (HORSE,DEOXY)

DOMAIN 1: A 1 to A 141 ; The following residues NOT assigned to any domain: Chain "A" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HBA A

PRELIMINARY 07-JAN-92 :: HEMOGLOBIN ROTHSCHILD (DEOXY) MUTANT (BETA 37 *TRP

DOMAIN 1: A 1 to A 141 ; The following residues NOT assigned to any domain: Chain "A" 1 - 146 The following residues NOT assigned to any domain: Chain "A" 1 - 141 The following residues NOT assigned to any domain: Chain "A" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HBA C

PRELIMINARY 07-JAN-92 :: HEMOGLOBIN ROTHSCHILD (DEOXY) MUTANT (BETA 37 *TRP

DOMAIN 1: C 1 to C 141 ; The following residues NOT assigned to any domain: Chain "C" 1 - 141 The following residues NOT assigned to any domain: Chain "C" 1 - 146 The following residues NOT assigned to any domain: Chain "C" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HBB A

PRELIMINARY 07-JAN-92 :: HEMOGLOBIN A (DEOXY, LOW SALT, 100MM CL)

DOMAIN 1: A 1 to A 141 ; The following residues NOT assigned to any domain: Chain "A" 1 - 146 The following residues NOT assigned to any domain: Chain "A" 1 - 141 The following residues NOT assigned to any domain: Chain "A" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HBB C

PRELIMINARY 07-JAN-92 :: HEMOGLOBIN A (DEOXY, LOW SALT, 100MM CL)

DOMAIN 1: C 1 to C 141 ; The following residues NOT assigned to any domain: Chain "C" 1 - 141 The following residues NOT assigned to any domain: Chain "C" 1 - 146 The following residues NOT assigned to any domain: Chain "C" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BBB A

OXYGEN TRANSPORT 29-APR-92 :: HEMOGLOBIN A (CARBONMONOXY)

DOMAIN 1: A 1 to A 141 ; The following residues NOT assigned to any domain: Chain "A" 1 - 146 The following residues NOT assigned to any domain: Chain "A" 1 - 141 The following residues NOT assigned to any domain: Chain "A" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BBB C

OXYGEN TRANSPORT 29-APR-92 :: HEMOGLOBIN A (CARBONMONOXY)

DOMAIN 1: C 1 to C 141 ; The following residues NOT assigned to any domain: Chain "C" 1 - 141 The following residues NOT assigned to any domain: Chain "C" 1 - 146 The following residues NOT assigned to any domain: Chain "C" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HBS A

OXYGEN TRANSPORT 02-JUN-82 :: HEMOGLOBIN S (DEOXY)

DOMAIN 1: A 1 to A 141 ; The following residues NOT assigned to any domain: Chain "A" 1 - 146 The following residues NOT assigned to any domain: Chain "A" 1 - 141 The following residues NOT assigned to any domain: Chain "A" 1 - 146 The following residues NOT assigned to any domain: Chain "A" 1 - 141 The following residues NOT assigned to any domain: Chain "A" 1 - 146 The following residues NOT assigned to any domain: Chain "A" 1 - 141 The following residues NOT assigned to any domain: Chain "A" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HBS C

OXYGEN TRANSPORT 02-JUN-82 :: HEMOGLOBIN S (DEOXY)

DOMAIN 1: C 1 to C 141 ; The following residues NOT assigned to any domain: Chain "C" 1 - 141 The following residues NOT assigned to any domain: Chain "C" 1 - 146 The following residues NOT assigned to any domain: Chain "C" 1 - 146 The following residues NOT assigned to any domain: Chain "C" 1 - 141 The following residues NOT assigned to any domain: Chain "C" 1 - 146 The following residues NOT assigned to any domain: Chain "C" 1 - 141 The following residues NOT assigned to any domain: Chain "C" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HBS E

OXYGEN TRANSPORT 02-JUN-82 :: HEMOGLOBIN S (DEOXY)

DOMAIN 1: E 1 to E 141 ; The following residues NOT assigned to any domain: Chain "E" 1 - 141 The following residues NOT assigned to any domain: Chain "E" 1 - 146 The following residues NOT assigned to any domain: Chain "E" 1 - 141 The following residues NOT assigned to any domain: Chain "E" 1 - 146 The following residues NOT assigned to any domain: Chain "E" 1 - 146 The following residues NOT assigned to any domain: Chain "E" 1 - 141 The following residues NOT assigned to any domain: Chain "E" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HBS G

OXYGEN TRANSPORT 02-JUN-82 :: HEMOGLOBIN S (DEOXY)

DOMAIN 1: G 1 to G 141 ; The following residues NOT assigned to any domain: Chain "G" 1 - 141 The following residues NOT assigned to any domain: Chain "G" 1 - 146 The following residues NOT assigned to any domain: Chain "G" 1 - 141 The following residues NOT assigned to any domain: Chain "G" 1 - 146 The following residues NOT assigned to any domain: Chain "G" 1 - 141 The following residues NOT assigned to any domain: Chain "G" 1 - 146 The following residues NOT assigned to any domain: Chain "G" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HCO A

OXYGEN TRANSPORT 07-AUG-79 :: HEMOGLOBIN (CARBONMONOXY)

DOMAIN 1: A 1 to A 141 ; The following residues NOT assigned to any domain: Chain "A" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HDA A

OXYGEN TRANSPORT 06-MAY-93 :: HEMOGLOBIN (DEOXY)

DOMAIN 1: A 1 to A 141 ; The following residues NOT assigned to any domain: Chain "A" 2 - 146 The following residues NOT assigned to any domain: Chain "A" 1 - 141 The following residues NOT assigned to any domain: Chain "A" 2 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HDA C

OXYGEN TRANSPORT 06-MAY-93 :: HEMOGLOBIN (DEOXY)

DOMAIN 1: C 1 to C 141 ; The following residues NOT assigned to any domain: Chain "C" 1 - 141 The following residues NOT assigned to any domain: Chain "C" 2 - 146 The following residues NOT assigned to any domain: Chain "C" 2 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGA A

PRELIMINARY 31-OCT-91 :: HEMOGLOBIN (T STATE, DEOXYGENATED)

DOMAIN 1: A 1 to A 141 ; The following residues NOT assigned to any domain: Chain "A" 1 - 146 The following residues NOT assigned to any domain: Chain "A" 1 - 141 The following residues NOT assigned to any domain: Chain "A" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGA C

PRELIMINARY 31-OCT-91 :: HEMOGLOBIN (T STATE, DEOXYGENATED)

DOMAIN 1: C 1 to C 141 ; The following residues NOT assigned to any domain: Chain "C" 1 - 141 The following residues NOT assigned to any domain: Chain "C" 1 - 146 The following residues NOT assigned to any domain: Chain "C" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGB A

PRELIMINARY 31-OCT-91 :: HEMOGLOBIN (T STATE, AQUOMET)

DOMAIN 1: A 1 to A 141 ; The following residues NOT assigned to any domain: Chain "A" 1 - 146 The following residues NOT assigned to any domain: Chain "A" 1 - 141 The following residues NOT assigned to any domain: Chain "A" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGB C

PRELIMINARY 31-OCT-91 :: HEMOGLOBIN (T STATE, AQUOMET)

DOMAIN 1: C 1 to C 141 ; The following residues NOT assigned to any domain: Chain "C" 1 - 141 The following residues NOT assigned to any domain: Chain "C" 1 - 146 The following residues NOT assigned to any domain: Chain "C" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGC A

PRELIMINARY 31-OCT-91 :: HEMOGLOBIN (T STATE, ALPHA-OXY)

DOMAIN 1: A 1 to A 141 ; The following residues NOT assigned to any domain: Chain "A" 1 - 146 The following residues NOT assigned to any domain: Chain "A" 1 - 141 The following residues NOT assigned to any domain: Chain "A" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGC C

PRELIMINARY 31-OCT-91 :: HEMOGLOBIN (T STATE, ALPHA-OXY)

DOMAIN 1: C 1 to C 141 ; The following residues NOT assigned to any domain: Chain "C" 1 - 141 The following residues NOT assigned to any domain: Chain "C" 1 - 146 The following residues NOT assigned to any domain: Chain "C" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4HHB A

OXYGEN TRANSPORT 07-MAR-84 :: HEMOGLOBIN (DEOXY)

DOMAIN 1: A 1 to A 141 ; The following residues NOT assigned to any domain: Chain "A" 1 - 146 The following residues NOT assigned to any domain: Chain "A" 1 - 141 The following residues NOT assigned to any domain: Chain "A" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4HHB C

OXYGEN TRANSPORT 07-MAR-84 :: HEMOGLOBIN (DEOXY)

DOMAIN 1: C 1 to C 141 ; The following residues NOT assigned to any domain: Chain "C" 1 - 141 The following residues NOT assigned to any domain: Chain "C" 1 - 146 The following residues NOT assigned to any domain: Chain "C" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HHO A

OXYGEN TRANSPORT 10-JUN-83 :: HEMOGLOBIN A (OXY)

DOMAIN 1: A 1 to A 141 ; The following residues NOT assigned to any domain: Chain "A" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DXT A

OXYGEN TRANSPORT 06-MAY-92 :: HEMOGLOBIN (DEOXY) MUTANT WITH ADDITIONAL MET AT T

DOMAIN 1: A 1 to A 141 ; The following residues NOT assigned to any domain: Chain "A" 1 - 147 The following residues NOT assigned to any domain: Chain "A" 1 - 141 The following residues NOT assigned to any domain: Chain "A" 1 - 147
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DXT C

OXYGEN TRANSPORT 06-MAY-92 :: HEMOGLOBIN (DEOXY) MUTANT WITH ADDITIONAL MET AT T

DOMAIN 1: C 1 to C 141 ; The following residues NOT assigned to any domain: Chain "C" 1 - 141 The following residues NOT assigned to any domain: Chain "C" 1 - 147 The following residues NOT assigned to any domain: Chain "C" 1 - 147
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DXU A

OXYGEN TRANSPORT 06-MAY-92 :: HEMOGLOBIN (DEOXY) MUTANT WITH VAL 1 REPLACED BY M

DOMAIN 1: A 1 to A 141 ; The following residues NOT assigned to any domain: Chain "A" 1 - 146 The following residues NOT assigned to any domain: Chain "A" 1 - 141 The following residues NOT assigned to any domain: Chain "A" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DXU C

OXYGEN TRANSPORT 06-MAY-92 :: HEMOGLOBIN (DEOXY) MUTANT WITH VAL 1 REPLACED BY M

DOMAIN 1: C 1 to C 141 ; The following residues NOT assigned to any domain: Chain "C" 1 - 141 The following residues NOT assigned to any domain: Chain "C" 1 - 146 The following residues NOT assigned to any domain: Chain "C" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DXV A

OXYGEN TRANSPORT 06-MAY-92 :: HEMOGLOBIN (DEOXY) MUTANT WITH VAL 1 REPLACED BY A

DOMAIN 1: A 1 to A 141 ; The following residues NOT assigned to any domain: Chain "A" 1 - 146 The following residues NOT assigned to any domain: Chain "A" 1 - 141 The following residues NOT assigned to any domain: Chain "A" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DXV C

OXYGEN TRANSPORT 06-MAY-92 :: HEMOGLOBIN (DEOXY) MUTANT WITH VAL 1 REPLACED BY A

DOMAIN 1: C 1 to C 141 ; The following residues NOT assigned to any domain: Chain "C" 1 - 141 The following residues NOT assigned to any domain: Chain "C" 1 - 146 The following residues NOT assigned to any domain: Chain "C" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FDH A

OXYGEN TRANSPORT 18-AUG-76 :: HEMOGLOBIN (DEOXY, HUMAN FETAL F=/II$=)

DOMAIN 1: A 1 to A 141 ; The following residues NOT assigned to any domain: Chain "A" 0 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CMY A

OXYGEN TRANSPORT 18-SEP-92 :: HEMOGLOBIN YPSILANTI (CARBON MONOXY FORM)

DOMAIN 1: A 1 to A 141 ; The following residues NOT assigned to any domain: Chain "A" 1 - 146 The following residues NOT assigned to any domain: Chain "A" 1 - 141 The following residues NOT assigned to any domain: Chain "A" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CMY C

OXYGEN TRANSPORT 18-SEP-92 :: HEMOGLOBIN YPSILANTI (CARBON MONOXY FORM)

DOMAIN 1: C 1 to C 141 ; The following residues NOT assigned to any domain: Chain "C" 1 - 141 The following residues NOT assigned to any domain: Chain "C" 1 - 146 The following residues NOT assigned to any domain: Chain "C" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NIH A

OXYGEN TRANSPORT 14-MAR-90 :: ALPHA-NICKELOUS, BETA-FERROUS CARBONMONOXY HEMOGLO

DOMAIN 1: A 1 to A 141 ; The following residues NOT assigned to any domain: Chain "A" 1 - 146 The following residues NOT assigned to any domain: Chain "A" 1 - 141 The following residues NOT assigned to any domain: Chain "A" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NIH C

OXYGEN TRANSPORT 14-MAR-90 :: ALPHA-NICKELOUS, BETA-FERROUS CARBONMONOXY HEMOGLO

DOMAIN 1: C 1 to C 141 ; The following residues NOT assigned to any domain: Chain "C" 1 - 141 The following residues NOT assigned to any domain: Chain "C" 1 - 146 The following residues NOT assigned to any domain: Chain "C" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1COH A

OXYGEN TRANSPORT 13-JAN-89 :: ALPHA-FERROUS-CARBONMONOXY, BETA-COBALTOUS-DEOXY H

DOMAIN 1: A 1 to A 141 ; The following residues NOT assigned to any domain: Chain "A" 1 - 146 The following residues NOT assigned to any domain: Chain "A" 1 - 141 The following residues NOT assigned to any domain: Chain "A" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1COH C

OXYGEN TRANSPORT 13-JAN-89 :: ALPHA-FERROUS-CARBONMONOXY, BETA-COBALTOUS-DEOXY H

DOMAIN 1: C 1 to C 141 ; The following residues NOT assigned to any domain: Chain "C" 1 - 141 The following residues NOT assigned to any domain: Chain "C" 1 - 146 The following residues NOT assigned to any domain: Chain "C" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3HHB A

OXYGEN TRANSPORT 07-MAR-84 :: HEMOGLOBIN (DEOXY)

DOMAIN 1: A 1 to A 141 ; The following residues NOT assigned to any domain: Chain "A" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1THB A

OXYGEN TRANSPORT 23-JAN-90 :: HEMOGLOBIN (T STATE, PARTIALLY OXYGENATED)

DOMAIN 1: A 1 to A 141 ; The following residues NOT assigned to any domain: Chain "A" 1 - 146 The following residues NOT assigned to any domain: Chain "A" 1 - 141 The following residues NOT assigned to any domain: Chain "A" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1THB C

OXYGEN TRANSPORT 23-JAN-90 :: HEMOGLOBIN (T STATE, PARTIALLY OXYGENATED)

DOMAIN 1: C 1 to C 141 ; The following residues NOT assigned to any domain: Chain "C" 1 - 141 The following residues NOT assigned to any domain: Chain "C" 1 - 146 The following residues NOT assigned to any domain: Chain "C" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HCO A

OXYGEN TRANSPORT 07-AUG-79 :: HEMOGLOBIN (CARBONMONOXY)

DOMAIN 1: A 1 to A 141 ; The following residues NOT assigned to any domain: Chain "A" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HHB A

OXYGEN TRANSPORT 07-MAR-84 :: HEMOGLOBIN (DEOXY)

DOMAIN 1: A 1 to A 141 ; The following residues NOT assigned to any domain: Chain "A" 1 - 146 The following residues NOT assigned to any domain: Chain "A" 1 - 141 The following residues NOT assigned to any domain: Chain "A" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HHB C

OXYGEN TRANSPORT 07-MAR-84 :: HEMOGLOBIN (DEOXY)

DOMAIN 1: C 1 to C 141 ; The following residues NOT assigned to any domain: Chain "C" 1 - 141 The following residues NOT assigned to any domain: Chain "C" 1 - 146 The following residues NOT assigned to any domain: Chain "C" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BAB C

PRELIMINARY 06-MAY-92 :: HEMOGLOBIN THIONVILLE (ALPHA 1 VALINE TO GLUTAMIC

DOMAIN 1: C 1 to C 142 ; The following residues NOT assigned to any domain: Chain "C" 0 - 142 The following residues NOT assigned to any domain: Chain "C" 1 - 146 The following residues NOT assigned to any domain: Chain "C" 0 - 0 The following residues NOT assigned to any domain: Chain "C" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HDS A

OXYGEN TRANSPORT 01-OCT-79 :: HEMOGLOBIN (SICKLE CELL)

DOMAIN 1: A 1 to A 141 ; The following residues NOT assigned to any domain: Chain "A" 1 - 145 The following residues NOT assigned to any domain: Chain "A" 1 - 141 The following residues NOT assigned to any domain: Chain "A" 1 - 145
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HDS C

OXYGEN TRANSPORT 01-OCT-79 :: HEMOGLOBIN (SICKLE CELL)

DOMAIN 1: C 1 to C 141 ; The following residues NOT assigned to any domain: Chain "C" 1 - 141 The following residues NOT assigned to any domain: Chain "C" 1 - 145 The following residues NOT assigned to any domain: Chain "C" 1 - 145
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PBX A

OXYGEN TRANSPORT 04-NOV-91 :: HEMOGLOBIN (CARBONMONOXY)

DOMAIN 1: A 1 to A 142 ; The following residues NOT assigned to any domain: Chain "A" 0 - 0 The following residues NOT assigned to any domain: Chain "A" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FDH G

OXYGEN TRANSPORT 18-AUG-76 :: HEMOGLOBIN (DEOXY, HUMAN FETAL F=/II$=)

DOMAIN 1: G 1 to G 146 ; The following residues NOT assigned to any domain: Chain "G" 1 - 141 The following residues NOT assigned to any domain: Chain "G" 0 - 0
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MHB B

OXYGEN TRANSPORT 14-FEB-77 :: HEMOGLOBIN (HORSE, AQUO MET)

DOMAIN 1: B 1 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 1 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BAB D

PRELIMINARY 06-MAY-92 :: HEMOGLOBIN THIONVILLE (ALPHA 1 VALINE TO GLUTAMIC

DOMAIN 1: D 1 to D 146 ; The following residues NOT assigned to any domain: Chain "D" 0 - 142 The following residues NOT assigned to any domain: Chain "D" 1 - 146 The following residues NOT assigned to any domain: Chain "D" 0 - 142
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HBA B

PRELIMINARY 07-JAN-92 :: HEMOGLOBIN ROTHSCHILD (DEOXY) MUTANT (BETA 37 *TRP

DOMAIN 1: B 1 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HBA D

PRELIMINARY 07-JAN-92 :: HEMOGLOBIN ROTHSCHILD (DEOXY) MUTANT (BETA 37 *TRP

DOMAIN 1: D 1 to D 146 ; The following residues NOT assigned to any domain: Chain "D" 1 - 141 The following residues NOT assigned to any domain: Chain "D" 1 - 146 The following residues NOT assigned to any domain: Chain "D" 1 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HBB B

PRELIMINARY 07-JAN-92 :: HEMOGLOBIN A (DEOXY, LOW SALT, 100MM CL)

DOMAIN 1: B 1 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HBB D

PRELIMINARY 07-JAN-92 :: HEMOGLOBIN A (DEOXY, LOW SALT, 100MM CL)

DOMAIN 1: D 1 to D 146 ; The following residues NOT assigned to any domain: Chain "D" 1 - 141 The following residues NOT assigned to any domain: Chain "D" 1 - 146 The following residues NOT assigned to any domain: Chain "D" 1 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BBB B

OXYGEN TRANSPORT 29-APR-92 :: HEMOGLOBIN A (CARBONMONOXY)

DOMAIN 1: B 1 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BBB D

OXYGEN TRANSPORT 29-APR-92 :: HEMOGLOBIN A (CARBONMONOXY)

DOMAIN 1: D 1 to D 146 ; The following residues NOT assigned to any domain: Chain "D" 1 - 141 The following residues NOT assigned to any domain: Chain "D" 1 - 146 The following residues NOT assigned to any domain: Chain "D" 1 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HBS B

OXYGEN TRANSPORT 02-JUN-82 :: HEMOGLOBIN S (DEOXY)

DOMAIN 1: B 1 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 146 The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 146 The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HBS D

OXYGEN TRANSPORT 02-JUN-82 :: HEMOGLOBIN S (DEOXY)

DOMAIN 1: D 1 to D 146 ; The following residues NOT assigned to any domain: Chain "D" 1 - 141 The following residues NOT assigned to any domain: Chain "D" 1 - 146 The following residues NOT assigned to any domain: Chain "D" 1 - 141 The following residues NOT assigned to any domain: Chain "D" 1 - 141 The following residues NOT assigned to any domain: Chain "D" 1 - 146 The following residues NOT assigned to any domain: Chain "D" 1 - 141 The following residues NOT assigned to any domain: Chain "D" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HBS F

OXYGEN TRANSPORT 02-JUN-82 :: HEMOGLOBIN S (DEOXY)

DOMAIN 1: F 1 to F 146 ; The following residues NOT assigned to any domain: Chain "F" 1 - 141 The following residues NOT assigned to any domain: Chain "F" 1 - 146 The following residues NOT assigned to any domain: Chain "F" 1 - 141 The following residues NOT assigned to any domain: Chain "F" 1 - 146 The following residues NOT assigned to any domain: Chain "F" 1 - 141 The following residues NOT assigned to any domain: Chain "F" 1 - 141 The following residues NOT assigned to any domain: Chain "F" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HBS H

OXYGEN TRANSPORT 02-JUN-82 :: HEMOGLOBIN S (DEOXY)

DOMAIN 1: H 1 to H 146 ; The following residues NOT assigned to any domain: Chain "H" 1 - 141 The following residues NOT assigned to any domain: Chain "H" 1 - 146 The following residues NOT assigned to any domain: Chain "H" 1 - 141 The following residues NOT assigned to any domain: Chain "H" 1 - 146 The following residues NOT assigned to any domain: Chain "H" 1 - 141 The following residues NOT assigned to any domain: Chain "H" 1 - 146 The following residues NOT assigned to any domain: Chain "H" 1 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HCO B

OXYGEN TRANSPORT 07-AUG-79 :: HEMOGLOBIN (CARBONMONOXY)

DOMAIN 1: B 1 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 1 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGA B

PRELIMINARY 31-OCT-91 :: HEMOGLOBIN (T STATE, DEOXYGENATED)

DOMAIN 1: B 1 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGA D

PRELIMINARY 31-OCT-91 :: HEMOGLOBIN (T STATE, DEOXYGENATED)

DOMAIN 1: D 1 to D 146 ; The following residues NOT assigned to any domain: Chain "D" 1 - 141 The following residues NOT assigned to any domain: Chain "D" 1 - 146 The following residues NOT assigned to any domain: Chain "D" 1 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGB B

PRELIMINARY 31-OCT-91 :: HEMOGLOBIN (T STATE, AQUOMET)

DOMAIN 1: B 1 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGB D

PRELIMINARY 31-OCT-91 :: HEMOGLOBIN (T STATE, AQUOMET)

DOMAIN 1: D 1 to D 146 ; The following residues NOT assigned to any domain: Chain "D" 1 - 141 The following residues NOT assigned to any domain: Chain "D" 1 - 146 The following residues NOT assigned to any domain: Chain "D" 1 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGC B

PRELIMINARY 31-OCT-91 :: HEMOGLOBIN (T STATE, ALPHA-OXY)

DOMAIN 1: B 1 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGC D

PRELIMINARY 31-OCT-91 :: HEMOGLOBIN (T STATE, ALPHA-OXY)

DOMAIN 1: D 1 to D 146 ; The following residues NOT assigned to any domain: Chain "D" 1 - 141 The following residues NOT assigned to any domain: Chain "D" 1 - 146 The following residues NOT assigned to any domain: Chain "D" 1 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4HHB B

OXYGEN TRANSPORT 07-MAR-84 :: HEMOGLOBIN (DEOXY)

DOMAIN 1: B 1 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4HHB D

OXYGEN TRANSPORT 07-MAR-84 :: HEMOGLOBIN (DEOXY)

DOMAIN 1: D 1 to D 146 ; The following residues NOT assigned to any domain: Chain "D" 1 - 141 The following residues NOT assigned to any domain: Chain "D" 1 - 146 The following residues NOT assigned to any domain: Chain "D" 1 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HHO B

OXYGEN TRANSPORT 10-JUN-83 :: HEMOGLOBIN A (OXY)

DOMAIN 1: B 1 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 1 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DXU B

OXYGEN TRANSPORT 06-MAY-92 :: HEMOGLOBIN (DEOXY) MUTANT WITH VAL 1 REPLACED BY M

DOMAIN 1: B 1 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DXU D

OXYGEN TRANSPORT 06-MAY-92 :: HEMOGLOBIN (DEOXY) MUTANT WITH VAL 1 REPLACED BY M

DOMAIN 1: D 1 to D 146 ; The following residues NOT assigned to any domain: Chain "D" 1 - 141 The following residues NOT assigned to any domain: Chain "D" 1 - 146 The following residues NOT assigned to any domain: Chain "D" 1 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DXV B

OXYGEN TRANSPORT 06-MAY-92 :: HEMOGLOBIN (DEOXY) MUTANT WITH VAL 1 REPLACED BY A

DOMAIN 1: B 1 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DXV D

OXYGEN TRANSPORT 06-MAY-92 :: HEMOGLOBIN (DEOXY) MUTANT WITH VAL 1 REPLACED BY A

DOMAIN 1: D 1 to D 146 ; The following residues NOT assigned to any domain: Chain "D" 1 - 141 The following residues NOT assigned to any domain: Chain "D" 1 - 146 The following residues NOT assigned to any domain: Chain "D" 1 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CBL A

OXYGEN TRANSPORT 18-FEB-93 :: DEOXY-BETA=4= HEMOGLOBIN ("R-LIKE" QUATERNARY STRU

DOMAIN 1: A 1 to A 146 ; The following residues NOT assigned to any domain: Chain "A" 1 - 146 The following residues NOT assigned to any domain: Chain "A" 1 - 146 The following residues NOT assigned to any domain: Chain "A" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CBL B

OXYGEN TRANSPORT 18-FEB-93 :: DEOXY-BETA=4= HEMOGLOBIN ("R-LIKE" QUATERNARY STRU

DOMAIN 1: B 1 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 1 - 146 The following residues NOT assigned to any domain: Chain "B" 1 - 146 The following residues NOT assigned to any domain: Chain "B" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CBL C

OXYGEN TRANSPORT 18-FEB-93 :: DEOXY-BETA=4= HEMOGLOBIN ("R-LIKE" QUATERNARY STRU

DOMAIN 1: C 1 to C 146 ; The following residues NOT assigned to any domain: Chain "C" 1 - 146 The following residues NOT assigned to any domain: Chain "C" 1 - 146 The following residues NOT assigned to any domain: Chain "C" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CBL D

OXYGEN TRANSPORT 18-FEB-93 :: DEOXY-BETA=4= HEMOGLOBIN ("R-LIKE" QUATERNARY STRU

DOMAIN 1: D 1 to D 146 ; The following residues NOT assigned to any domain: Chain "D" 1 - 146 The following residues NOT assigned to any domain: Chain "D" 1 - 146 The following residues NOT assigned to any domain: Chain "D" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CBM A

OXYGEN TRANSPORT 18-FEB-93 :: CARBONMONOXY-BETA=4= HEMOGLOBIN

DOMAIN 1: A 1 to A 146 ; The following residues NOT assigned to any domain: Chain "A" 1 - 146 The following residues NOT assigned to any domain: Chain "A" 1 - 146 The following residues NOT assigned to any domain: Chain "A" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CBM B

OXYGEN TRANSPORT 18-FEB-93 :: CARBONMONOXY-BETA=4= HEMOGLOBIN

DOMAIN 1: B 1 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 1 - 146 The following residues NOT assigned to any domain: Chain "B" 1 - 146 The following residues NOT assigned to any domain: Chain "B" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CBM C

OXYGEN TRANSPORT 18-FEB-93 :: CARBONMONOXY-BETA=4= HEMOGLOBIN

DOMAIN 1: C 1 to C 146 ; The following residues NOT assigned to any domain: Chain "C" 1 - 146 The following residues NOT assigned to any domain: Chain "C" 1 - 146 The following residues NOT assigned to any domain: Chain "C" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CBM D

OXYGEN TRANSPORT 18-FEB-93 :: CARBONMONOXY-BETA=4= HEMOGLOBIN

DOMAIN 1: D 1 to D 146 ; The following residues NOT assigned to any domain: Chain "D" 1 - 146 The following residues NOT assigned to any domain: Chain "D" 1 - 146 The following residues NOT assigned to any domain: Chain "D" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NIH B

OXYGEN TRANSPORT 14-MAR-90 :: ALPHA-NICKELOUS, BETA-FERROUS CARBONMONOXY HEMOGLO

DOMAIN 1: B 1 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NIH D

OXYGEN TRANSPORT 14-MAR-90 :: ALPHA-NICKELOUS, BETA-FERROUS CARBONMONOXY HEMOGLO

DOMAIN 1: D 1 to D 146 ; The following residues NOT assigned to any domain: Chain "D" 1 - 141 The following residues NOT assigned to any domain: Chain "D" 1 - 146 The following residues NOT assigned to any domain: Chain "D" 1 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1COH B

OXYGEN TRANSPORT 13-JAN-89 :: ALPHA-FERROUS-CARBONMONOXY, BETA-COBALTOUS-DEOXY H

DOMAIN 1: B 1 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1COH D

OXYGEN TRANSPORT 13-JAN-89 :: ALPHA-FERROUS-CARBONMONOXY, BETA-COBALTOUS-DEOXY H

DOMAIN 1: D 1 to D 146 ; The following residues NOT assigned to any domain: Chain "D" 1 - 141 The following residues NOT assigned to any domain: Chain "D" 1 - 146 The following residues NOT assigned to any domain: Chain "D" 1 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3HHB B

OXYGEN TRANSPORT 07-MAR-84 :: HEMOGLOBIN (DEOXY)

DOMAIN 1: B 1 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 1 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1THB B

OXYGEN TRANSPORT 23-JAN-90 :: HEMOGLOBIN (T STATE, PARTIALLY OXYGENATED)

DOMAIN 1: B 1 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1THB D

OXYGEN TRANSPORT 23-JAN-90 :: HEMOGLOBIN (T STATE, PARTIALLY OXYGENATED)

DOMAIN 1: D 1 to D 146 ; The following residues NOT assigned to any domain: Chain "D" 1 - 141 The following residues NOT assigned to any domain: Chain "D" 1 - 146 The following residues NOT assigned to any domain: Chain "D" 1 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HCO B

OXYGEN TRANSPORT 07-AUG-79 :: HEMOGLOBIN (CARBONMONOXY)

DOMAIN 1: B 1 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 1 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HHB B

OXYGEN TRANSPORT 07-MAR-84 :: HEMOGLOBIN (DEOXY)

DOMAIN 1: B 1 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HHB D

OXYGEN TRANSPORT 07-MAR-84 :: HEMOGLOBIN (DEOXY)

DOMAIN 1: D 1 to D 146 ; The following residues NOT assigned to any domain: Chain "D" 1 - 141 The following residues NOT assigned to any domain: Chain "D" 1 - 146 The following residues NOT assigned to any domain: Chain "D" 1 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HDA B

OXYGEN TRANSPORT 06-MAY-93 :: HEMOGLOBIN (DEOXY)

DOMAIN 1: B 2 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 2 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HDA D

OXYGEN TRANSPORT 06-MAY-93 :: HEMOGLOBIN (DEOXY)

DOMAIN 1: D 2 to D 146 ; The following residues NOT assigned to any domain: Chain "D" 1 - 141 The following residues NOT assigned to any domain: Chain "D" 2 - 146 The following residues NOT assigned to any domain: Chain "D" 1 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DXT B

OXYGEN TRANSPORT 06-MAY-92 :: HEMOGLOBIN (DEOXY) MUTANT WITH ADDITIONAL MET AT T

DOMAIN 1: B 1 to B 147 ; The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 147
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DXT D

OXYGEN TRANSPORT 06-MAY-92 :: HEMOGLOBIN (DEOXY) MUTANT WITH ADDITIONAL MET AT T

DOMAIN 1: D 1 to D 147 ; The following residues NOT assigned to any domain: Chain "D" 1 - 141 The following residues NOT assigned to any domain: Chain "D" 1 - 147 The following residues NOT assigned to any domain: Chain "D" 1 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PGH B

OXYGEN TRANSPORT 16-SEP-94 :: HEMOGLOBIN (AQUOMET)

DOMAIN 1: B 1 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PGH D

OXYGEN TRANSPORT 16-SEP-94 :: HEMOGLOBIN (AQUOMET)

DOMAIN 1: D 1 to D 146 ; The following residues NOT assigned to any domain: Chain "D" 1 - 141 The following residues NOT assigned to any domain: Chain "D" 1 - 146 The following residues NOT assigned to any domain: Chain "D" 1 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CMY B

OXYGEN TRANSPORT 18-SEP-92 :: HEMOGLOBIN YPSILANTI (CARBON MONOXY FORM)

DOMAIN 1: B 1 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CMY D

OXYGEN TRANSPORT 18-SEP-92 :: HEMOGLOBIN YPSILANTI (CARBON MONOXY FORM)

DOMAIN 1: D 1 to D 146 ; The following residues NOT assigned to any domain: Chain "D" 1 - 141 The following residues NOT assigned to any domain: Chain "D" 1 - 146 The following residues NOT assigned to any domain: Chain "D" 1 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2DHB B

OXYGEN TRANSPORT 01-NOV-73 :: HEMOGLOBIN (HORSE,DEOXY)

DOMAIN 1: B 1 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 1 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HDS B

OXYGEN TRANSPORT 01-OCT-79 :: HEMOGLOBIN (SICKLE CELL)

DOMAIN 1: B 1 to B 145 ; The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 141 The following residues NOT assigned to any domain: Chain "B" 1 - 145
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HDS D

OXYGEN TRANSPORT 01-OCT-79 :: HEMOGLOBIN (SICKLE CELL)

DOMAIN 1: D 1 to D 145 ; The following residues NOT assigned to any domain: Chain "D" 1 - 141 The following residues NOT assigned to any domain: Chain "D" 1 - 145 The following residues NOT assigned to any domain: Chain "D" 1 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PBX B

OXYGEN TRANSPORT 04-NOV-91 :: HEMOGLOBIN (CARBONMONOXY)

DOMAIN 1: B 1 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 0 - 142
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5FD1

ELECTRON TRANSPORT(IRON-SULFUR) 29-JUN-93 :: FERREDOXIN (OXIDIZED) AT PH 8

DOMAIN 1: 1 to 106 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FDA

ELECTRON TRANSPORT(IRON-SULFUR) 29-JUN-93 :: FERREDOXIN (OXIDIZED) AT PH 6

DOMAIN 1: 1 to 106 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FDB

ELECTRON TRANSPORT(IRON-SULFUR) 29-JUN-93 :: FERREDOXIN (REDUCED) AT PH 6

DOMAIN 1: 1 to 106 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FDC

ELECTRON TRANSPORT(IRON-SULFUR) 29-JUN-93 :: FERREDOXIN (REDUCED) AT PH 8

DOMAIN 1: 1 to 106 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FER

ELECTRON TRANSFER(IRON-SULFUR PROTEIN) 02-SEP-92 :: FERREDOXIN I (PH 6.5)

DOMAIN 1: 1 to 106 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FRI

ELECTRON TRANSPORT 27-SEP-93 :: FERREDOXIN (FDI) MUTANT WITH ASP 23 REPLACED BY AS

DOMAIN 1: 1 to 106 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FRH

ELECTRON TRANSPORT 27-SEP-93 :: FERREDOXIN (FDI) MUTANT WITH PHE 2 REPLACED BY TYR

DOMAIN 1: 1 to 106 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FRM

ELECTRON TRANSPORT 27-SEP-93 :: FERREDOXIN (FDI) MUTANT WITH GLU 46 REPLACED BY AL

DOMAIN 1: 1 to 106 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FRL

ELECTRON TRANSPORT 27-SEP-93 :: FERREDOXIN (FDI) MUTANT WITH GLU 38 REPLACED BY SE

DOMAIN 1: 1 to 106 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FRK

ELECTRON TRANSPORT 27-SEP-93 :: FERREDOXIN (FDI) MUTANT WITH HIS 35 REPLACED BY AS

DOMAIN 1: 1 to 106 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FRJ

ELECTRON TRANSPORT 27-SEP-93 :: FERREDOXIN (FDI) MUTANT WITH PHE 25 REPLACED BY IL

DOMAIN 1: 1 to 106 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FRX

ELECTRON TRANSPORT 13-JUL-94 :: FERREDOXIN (FDI) MUTANT WITH CYS 20 REPLACED BY SE

DOMAIN 1: 1 to 106 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FD2

ELECTRON TRANSFER(IRON-SULFUR PROTEIN) 08-DEC-88 :: FERREDOXIN (MUTANT WITH CYS 20 REPLACED BY ALA) (/

DOMAIN 1: 1 to 106 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2FD2

ELECTRON TRANSFER(IRON-SULFUR PROTEIN) 20-AUG-90 :: FERREDOXIN (MUTANT WITH CYS 24 REPLACED BY ALA) (/

DOMAIN 1: 1 to 106 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FDN

ELECTRON TRANSPORT 31-MAR-94 :: FERREDOXIN

DOMAIN 1: 1 to 55 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FDX

ELECTRON TRANSPORT 01-AUG-76 :: FERREDOXIN

DOMAIN 1: 1 to 54 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HRS

IRON STORAGE 05-NOV-93 :: APOFERRITIN CO-CRYSTALLIZED WITH SN-PROTOPORPHYRIN

DOMAIN 1: 1 to 172 ; The following residues NOT assigned to any domain: Chain " " 173 - 174
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4FIS A

DNA-BINDING PROTEIN 12-AUG-91 :: FIS PROTEIN (FACTOR FOR INVERSION STIMULATION) MUT

DOMAIN 1: [Assigned by homology with 1FIAB]A 26 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 26 - 98
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4FIS B

DNA-BINDING PROTEIN 12-AUG-91 :: FIS PROTEIN (FACTOR FOR INVERSION STIMULATION) MUT

DOMAIN 1: [Assigned by homology with 1FIAB]B 26 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 26 - 98
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FIA A

DNA-BINDING PROTEIN 18-DEC-91 :: FIS PROTEIN (FACTOR FOR INVERSION STIMULATION)

DOMAIN 1: [Assigned by homology with 1FIAB]A 10 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 10 - 98
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3FIS A

DNA-BINDING PROTEIN 12-AUG-91 :: FIS PROTEIN (FACTOR FOR INVERSION STIMULATION)

DOMAIN 1: [Assigned by homology with 1FIAB]A 26 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 26 - 98
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3FIS B

DNA-BINDING PROTEIN 12-AUG-91 :: FIS PROTEIN (FACTOR FOR INVERSION STIMULATION)

DOMAIN 1: [Assigned by homology with 1FIAB]B 26 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 26 - 98
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HRA

DNA-BINDING RECEPTOR 25-JUL-93 :: RETINOIC ACID RECEPTOR (HUMAN) (BETA DNA-BINDING D

DOMAIN 1: [Assigned by homology with 1GLUA] 1 to 80 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GLU B

GLUCOCORTICOID RECEPTOR 30-AUG-92 :: GLUCOCORTICOID RECEPTOR (DNA-BINDING DOMAIN) COMPL

DOMAIN 1: [Assigned by homology with 1GLUA]B 434 to B 513 ; The following residues NOT assigned to any domain: Chain "B" 434 - 514 The following residues NOT assigned to any domain: Chain "B" 514 - 514 The following residues NOT assigned to any domain: Chain "B" -10 - 9 The following residues NOT assigned to any domain: Chain "B" -10 - 9
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GDC

GLUCOCORTICOID RECEPTOR 15-MAR-94 :: GLUCOCORTICOID RECEPTOR (DNA BINDING DOMAIN) GR-DB

DOMAIN 1: [Assigned by homology with 1GLUA] 1 to 72 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2GDA

GLUCOCORTICOID RECEPTOR 15-MAR-94 :: GLUCOCORTICOID RECEPTOR (DNA BINDING DOMAIN, GR-DB

DOMAIN 1: [Assigned by homology with 1GLUA] 1 to 72 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CSG A

CYTOKINE 23-NOV-92 :: GRANULOCYTE-MACROPHAGE COLONY-STIMULATING FACTOR (

DOMAIN 1: [Assigned by homology with 1GMFA]A 5 to A 123 ; The following residues NOT assigned to any domain: Chain "A" 124 - 124 The following residues NOT assigned to any domain: Chain "A" 5 - 124
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CSG B

CYTOKINE 23-NOV-92 :: GRANULOCYTE-MACROPHAGE COLONY-STIMULATING FACTOR (

DOMAIN 1: [Assigned by homology with 1GMFA]B 5 to B 123 ; The following residues NOT assigned to any domain: Chain "B" 5 - 124 The following residues NOT assigned to any domain: Chain "B" 124 - 124
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GMF B

GROWTH FACTOR 01-DEC-91 :: GRANULOCYTE-MACROPHAGE COLONY-STIMULATING FACTOR

DOMAIN 1: [Assigned by homology with 1GMFA]B 5 to B 123 ; The following residues NOT assigned to any domain: Chain "B" 5 - 123
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2SAR A

HYDROLASE (ENDORIBONUCLEASE) 13-DEC-90 :: RIBONUCLEASE SA (E.C.3.1.4.8) COMPLEX WITH 3'-*GUA

DOMAIN 1: [Assigned by homology with 1GMPA]A 1 to A 96 ; The following residues NOT assigned to any domain: Chain "A" 1 - 96
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2SAR B

HYDROLASE (ENDORIBONUCLEASE) 13-DEC-90 :: RIBONUCLEASE SA (E.C.3.1.4.8) COMPLEX WITH 3'-*GUA

DOMAIN 1: [Assigned by homology with 1GMPA]B 1 to B 96 ; The following residues NOT assigned to any domain: Chain "B" 1 - 96
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SAR A

HYDROLASE (ENDORIBONUCLEASE) 13-DEC-90 :: RIBONUCLEASE SA (E.C.3.1.4.8)

DOMAIN 1: [Assigned by homology with 1GMPA]A 1 to A 96 ; The following residues NOT assigned to any domain: Chain "A" 1 - 96
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SAR B

HYDROLASE (ENDORIBONUCLEASE) 13-DEC-90 :: RIBONUCLEASE SA (E.C.3.1.4.8)

DOMAIN 1: [Assigned by homology with 1GMPA]B 1 to B 96 ; The following residues NOT assigned to any domain: Chain "B" 1 - 96
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GMP B

HYDROLASE(GUANYLORIBONUCLEASE) 01-OCT-92 :: RIBONUCLEASE FROM STREPTOMYCES AUREOFACIENS (RNASE

DOMAIN 1: [Assigned by homology with 1GMPA]B 1 to B 96 ; The following residues NOT assigned to any domain: Chain "B" 1 - 96
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GMQ A

HYDROLASE(GUANYLORIBONUCLEASE) 01-OCT-92 :: RIBONUCLEASE FROM STREPTOMYCES AUREOFACIENS (RNASE

DOMAIN 1: [Assigned by homology with 1GMPA]A 1 to A 96 ; The following residues NOT assigned to any domain: Chain "A" 1 - 96
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GMQ B

HYDROLASE(GUANYLORIBONUCLEASE) 01-OCT-92 :: RIBONUCLEASE FROM STREPTOMYCES AUREOFACIENS (RNASE

DOMAIN 1: [Assigned by homology with 1GMPA]B 1 to B 96 ; The following residues NOT assigned to any domain: Chain "B" 1 - 96
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GMR A

HYDROLASE(GUANYLORIBONUCLEASE) 01-OCT-92 :: RIBONUCLEASE FROM STREPTOMYCES AUREOFACIENS (RNASE

DOMAIN 1: [Assigned by homology with 1GMPA]A 1 to A 96 ; The following residues NOT assigned to any domain: Chain "A" 1 - 96
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GMR B

HYDROLASE(GUANYLORIBONUCLEASE) 01-OCT-92 :: RIBONUCLEASE FROM STREPTOMYCES AUREOFACIENS (RNASE

DOMAIN 1: [Assigned by homology with 1GMPA]B 1 to B 96 ; The following residues NOT assigned to any domain: Chain "B" 1 - 96
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GPT

PLANT TOXIN 29-JUL-92 :: GAMMA-1-H THIONIN (NMR, 8 STRUCTURES)

DOMAIN 1: 1 to 47 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HFH

GLYCOPROTEIN 23-FEB-93 :: FACTOR H, 15TH AND 16TH C-MODULE PAIR (NMR, MINIMI

DOMAIN 1: 1 to 119 ; The following residues NOT assigned to any domain: Chain " " 120 - 120
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HFI

GLYCOPROTEIN 23-FEB-93 :: FACTOR H, 15TH C-MODULE PAIR (NMR, MINIMIZED AVERA

DOMAIN 1: 1 to 61 ; The following residues NOT assigned to any domain: Chain " " 62 - 62
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGD B

PRELIMINARY 01-NOV-91 :: HEMAGGLUTININ (BROMELAIN DIGESTED) CONTAINING GLY

DOMAIN 1: [Assigned by homology with 1HGEB]B 1 to B 175 ; The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 175 The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGD D

PRELIMINARY 01-NOV-91 :: HEMAGGLUTININ (BROMELAIN DIGESTED) CONTAINING GLY

DOMAIN 1: [Assigned by homology with 1HGEB]D 1 to D 175 ; The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 175 The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGD F

PRELIMINARY 01-NOV-91 :: HEMAGGLUTININ (BROMELAIN DIGESTED) CONTAINING GLY

DOMAIN 1: [Assigned by homology with 1HGEB]F 1 to F 175 ; The following residues NOT assigned to any domain: Chain "F" 1 - 328 The following residues NOT assigned to any domain: Chain "F" 1 - 175 The following residues NOT assigned to any domain: Chain "F" 1 - 328 The following residues NOT assigned to any domain: Chain "F" 1 - 175 The following residues NOT assigned to any domain: Chain "F" 1 - 328
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGE D

PRELIMINARY 01-NOV-91 :: HEMAGGLUTININ (BROMELAIN DIGESTED) CONTAINING *GLY

DOMAIN 1: [Assigned by homology with 1HGEB]D 1 to D 175 ; The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 175 The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGE F

PRELIMINARY 01-NOV-91 :: HEMAGGLUTININ (BROMELAIN DIGESTED) CONTAINING *GLY

DOMAIN 1: [Assigned by homology with 1HGEB]F 1 to F 175 ; The following residues NOT assigned to any domain: Chain "F" 1 - 328 The following residues NOT assigned to any domain: Chain "F" 1 - 175 The following residues NOT assigned to any domain: Chain "F" 1 - 328 The following residues NOT assigned to any domain: Chain "F" 1 - 175 The following residues NOT assigned to any domain: Chain "F" 1 - 328
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGF B

PRELIMINARY 01-NOV-91 :: HEMAGGLUTININ (BROMELAIN DIGESTED) UNCOMPLEXED

DOMAIN 1: [Assigned by homology with 1HGEB]B 1 to B 175 ; The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 175 The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGF D

PRELIMINARY 01-NOV-91 :: HEMAGGLUTININ (BROMELAIN DIGESTED) UNCOMPLEXED

DOMAIN 1: [Assigned by homology with 1HGEB]D 1 to D 175 ; The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 175 The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGF F

PRELIMINARY 01-NOV-91 :: HEMAGGLUTININ (BROMELAIN DIGESTED) UNCOMPLEXED

DOMAIN 1: [Assigned by homology with 1HGEB]F 1 to F 175 ; The following residues NOT assigned to any domain: Chain "F" 1 - 328 The following residues NOT assigned to any domain: Chain "F" 1 - 175 The following residues NOT assigned to any domain: Chain "F" 1 - 328 The following residues NOT assigned to any domain: Chain "F" 1 - 175 The following residues NOT assigned to any domain: Chain "F" 1 - 328
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGG B

PRELIMINARY 01-NOV-91 :: HEMAGGLUTININ (BROMELAIN DIGESTED) COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HGEB]B 1 to B 175 ; The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 175 The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGG D

PRELIMINARY 01-NOV-91 :: HEMAGGLUTININ (BROMELAIN DIGESTED) COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HGEB]D 1 to D 175 ; The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 175 The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGG F

PRELIMINARY 01-NOV-91 :: HEMAGGLUTININ (BROMELAIN DIGESTED) COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HGEB]F 1 to F 175 ; The following residues NOT assigned to any domain: Chain "F" 1 - 328 The following residues NOT assigned to any domain: Chain "F" 1 - 175 The following residues NOT assigned to any domain: Chain "F" 1 - 328 The following residues NOT assigned to any domain: Chain "F" 1 - 175 The following residues NOT assigned to any domain: Chain "F" 1 - 328
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGH B

PRELIMINARY 01-NOV-91 :: HEMAGGLUTININ (BROMELAIN DIGESTED) COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HGEB]B 1 to B 175 ; The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 175 The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGH D

PRELIMINARY 01-NOV-91 :: HEMAGGLUTININ (BROMELAIN DIGESTED) COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HGEB]D 1 to D 175 ; The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 175 The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGH F

PRELIMINARY 01-NOV-91 :: HEMAGGLUTININ (BROMELAIN DIGESTED) COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HGEB]F 1 to F 175 ; The following residues NOT assigned to any domain: Chain "F" 1 - 328 The following residues NOT assigned to any domain: Chain "F" 1 - 175 The following residues NOT assigned to any domain: Chain "F" 1 - 328 The following residues NOT assigned to any domain: Chain "F" 1 - 175 The following residues NOT assigned to any domain: Chain "F" 1 - 328
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGI B

PRELIMINARY 01-NOV-91 :: HEMAGGLUTININ (BROMELAIN DIGESTED) COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HGEB]B 1 to B 175 ; The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 175 The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGI D

PRELIMINARY 01-NOV-91 :: HEMAGGLUTININ (BROMELAIN DIGESTED) COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HGEB]D 1 to D 175 ; The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 175 The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGI F

PRELIMINARY 01-NOV-91 :: HEMAGGLUTININ (BROMELAIN DIGESTED) COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HGEB]F 1 to F 175 ; The following residues NOT assigned to any domain: Chain "F" 1 - 328 The following residues NOT assigned to any domain: Chain "F" 1 - 175 The following residues NOT assigned to any domain: Chain "F" 1 - 328 The following residues NOT assigned to any domain: Chain "F" 1 - 175 The following residues NOT assigned to any domain: Chain "F" 1 - 328
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGJ B

PRELIMINARY 01-NOV-91 :: HEMAGGLUTININ (BROMELAIN DIGESTED) COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HGEB]B 1 to B 175 ; The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 175 The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGJ D

PRELIMINARY 01-NOV-91 :: HEMAGGLUTININ (BROMELAIN DIGESTED) COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HGEB]D 1 to D 175 ; The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 175 The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGJ F

PRELIMINARY 01-NOV-91 :: HEMAGGLUTININ (BROMELAIN DIGESTED) COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HGEB]F 1 to F 175 ; The following residues NOT assigned to any domain: Chain "F" 1 - 328 The following residues NOT assigned to any domain: Chain "F" 1 - 175 The following residues NOT assigned to any domain: Chain "F" 1 - 328 The following residues NOT assigned to any domain: Chain "F" 1 - 175 The following residues NOT assigned to any domain: Chain "F" 1 - 328
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4HMG B

INFLUENZA VIRUS HEMAGGLUTININ 11-SEP-89 :: HEMAGGLUTININ (/L226(A)Q$) (BROMELAIN DIGESTED) (M

DOMAIN 1: [Assigned by homology with 1HGEB]B 1 to B 175 ; The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 175 The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4HMG D

INFLUENZA VIRUS HEMAGGLUTININ 11-SEP-89 :: HEMAGGLUTININ (/L226(A)Q$) (BROMELAIN DIGESTED) (M

DOMAIN 1: [Assigned by homology with 1HGEB]D 1 to D 175 ; The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 175 The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4HMG F

INFLUENZA VIRUS HEMAGGLUTININ 11-SEP-89 :: HEMAGGLUTININ (/L226(A)Q$) (BROMELAIN DIGESTED) (M

DOMAIN 1: [Assigned by homology with 1HGEB]F 1 to F 175 ; The following residues NOT assigned to any domain: Chain "F" 1 - 328 The following residues NOT assigned to any domain: Chain "F" 1 - 175 The following residues NOT assigned to any domain: Chain "F" 1 - 328 The following residues NOT assigned to any domain: Chain "F" 1 - 175 The following residues NOT assigned to any domain: Chain "F" 1 - 328
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3HMG B

INFLUENZA VIRUS HEMAGGLUTININ 11-SEP-89 :: HEMAGGLUTININ (/L226(A)Q$) (BROMELAIN DIGESTED) (M

DOMAIN 1: [Assigned by homology with 1HGEB]B 1 to B 175 ; The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 175 The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3HMG D

INFLUENZA VIRUS HEMAGGLUTININ 11-SEP-89 :: HEMAGGLUTININ (/L226(A)Q$) (BROMELAIN DIGESTED) (M

DOMAIN 1: [Assigned by homology with 1HGEB]D 1 to D 175 ; The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 175 The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3HMG F

INFLUENZA VIRUS HEMAGGLUTININ 11-SEP-89 :: HEMAGGLUTININ (/L226(A)Q$) (BROMELAIN DIGESTED) (M

DOMAIN 1: [Assigned by homology with 1HGEB]F 1 to F 175 ; The following residues NOT assigned to any domain: Chain "F" 1 - 328 The following residues NOT assigned to any domain: Chain "F" 1 - 175 The following residues NOT assigned to any domain: Chain "F" 1 - 328 The following residues NOT assigned to any domain: Chain "F" 1 - 175 The following residues NOT assigned to any domain: Chain "F" 1 - 328
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HMG B

INFLUENZA VIRUS HEMAGGLUTININ 11-SEP-89 :: HEMAGGLUTININ (/G146(A)D$) (BROMELAIN DIGESTED) (M

DOMAIN 1: [Assigned by homology with 1HGEB]B 1 to B 175 ; The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 175 The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HMG D

INFLUENZA VIRUS HEMAGGLUTININ 11-SEP-89 :: HEMAGGLUTININ (/G146(A)D$) (BROMELAIN DIGESTED) (M

DOMAIN 1: [Assigned by homology with 1HGEB]D 1 to D 175 ; The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 175 The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HMG F

INFLUENZA VIRUS HEMAGGLUTININ 11-SEP-89 :: HEMAGGLUTININ (/G146(A)D$) (BROMELAIN DIGESTED) (M

DOMAIN 1: [Assigned by homology with 1HGEB]F 1 to F 175 ; The following residues NOT assigned to any domain: Chain "F" 1 - 328 The following residues NOT assigned to any domain: Chain "F" 1 - 175 The following residues NOT assigned to any domain: Chain "F" 1 - 328 The following residues NOT assigned to any domain: Chain "F" 1 - 175 The following residues NOT assigned to any domain: Chain "F" 1 - 328
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5HMG B

INFLUENZA VIRUS HEMAGGLUTININ 11-SEP-89 :: HEMAGGLUTININ (/D112(B)G$) (BROMELAIN DIGESTED) (M

DOMAIN 1: [Assigned by homology with 1HGEB]B 1 to B 175 ; The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 175 The following residues NOT assigned to any domain: Chain "B" 1 - 328 The following residues NOT assigned to any domain: Chain "B" 1 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5HMG D

INFLUENZA VIRUS HEMAGGLUTININ 11-SEP-89 :: HEMAGGLUTININ (/D112(B)G$) (BROMELAIN DIGESTED) (M

DOMAIN 1: [Assigned by homology with 1HGEB]D 1 to D 175 ; The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 175 The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 328 The following residues NOT assigned to any domain: Chain "D" 1 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5HMG F

INFLUENZA VIRUS HEMAGGLUTININ 11-SEP-89 :: HEMAGGLUTININ (/D112(B)G$) (BROMELAIN DIGESTED) (M

DOMAIN 1: [Assigned by homology with 1HGEB]F 1 to F 175 ; The following residues NOT assigned to any domain: Chain "F" 1 - 328 The following residues NOT assigned to any domain: Chain "F" 1 - 175 The following residues NOT assigned to any domain: Chain "F" 1 - 328 The following residues NOT assigned to any domain: Chain "F" 1 - 175 The following residues NOT assigned to any domain: Chain "F" 1 - 328
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FVB H

IMMUNOGLOBULIN 09-APR-88 :: IG*A FV FRAGMENT (19.1.2, ANTI-ALPHA(1(RIGHT ARROW

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 119 ; The following residues NOT assigned to any domain: Chain "H" 1 - 106
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2FVB H

IMMUNOGLOBULIN 09-APR-88 :: IG*A FV FRAGMENT (19.1.2, ANTI-ALPHA(1(RIGHT ARROW

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 119 ; The following residues NOT assigned to any domain: Chain "H" 1 - 106
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1JHL H

COMPLEX(ANTIBODY-ANTIGEN) 04-MAY-93 :: FV FRAGMENT (LIGHT AND HEAVY VARIABLE DOMAINS

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 116 ; The following residues NOT assigned to any domain: Chain "H" 1 - 108 The following residues NOT assigned to any domain: Chain "H" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FGV H

IMMUNOGLOBULIN 01-NOV-93 :: FV FRAGMENT OF A HUMANIZED VERSION OF THE ANTI-CD1

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 124 ; The following residues NOT assigned to any domain: Chain "H" 1 - 107
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FVC B

IMMUNOGLOBULIN 20-OCT-92 :: FV FRAGMENT OF HUMANIZED ANTIBODY 4D5, VERSION 8

DOMAIN 1: [Assigned by homology with 1HILA]B 1 to B 120 ; The following residues NOT assigned to any domain: Chain "B" 1 - 109 The following residues NOT assigned to any domain: Chain "B" 1 - 108 The following residues NOT assigned to any domain: Chain "B" 1 - 120
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FVC D

IMMUNOGLOBULIN 20-OCT-92 :: FV FRAGMENT OF HUMANIZED ANTIBODY 4D5, VERSION 8

DOMAIN 1: [Assigned by homology with 1HILA]D 1 to D 120 ; The following residues NOT assigned to any domain: Chain "D" 1 - 109 The following residues NOT assigned to any domain: Chain "D" 1 - 120 The following residues NOT assigned to any domain: Chain "D" 1 - 108
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FVW H

IMMUNOGLOBULIN 09-APR-88 :: IG*A FV FRAGMENT (W3129, ANTI-ALPHA(1(RIGHT ARROW)

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 121 ; The following residues NOT assigned to any domain: Chain "H" 1 - 112
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2FVW H

IMMUNOGLOBULIN 09-APR-88 :: IG*A FV FRAGMENT (W3129, ANTI-ALPHA(1(RIGHT ARROW)

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 121 ; The following residues NOT assigned to any domain: Chain "H" 1 - 112
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IGM H

IMMUNOGLOBULIN 10-JUL-92 :: IMMUNOGLOBULIN M (IG-M) FV FRAGMENT

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 129 ; The following residues NOT assigned to any domain: Chain "H" 1 - 115
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MCP H

IMMUNOGLOBULIN 15-OCT-84 :: IMMUNOGLOBULIN MC/PC603$ FAB-PHOSPHOCHOLINE COMPLE

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 123 ; The following residues NOT assigned to any domain: Chain "H" 1 - 220 The following residues NOT assigned to any domain: Chain "H" 124 - 222
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCP H

IMMUNOGLOBULIN 09-JUL-84 :: IMMUNOGLOBULIN FAB FRAGMENT (MC/PC$603)

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 123 ; The following residues NOT assigned to any domain: Chain "H" 1 - 220 The following residues NOT assigned to any domain: Chain "H" 124 - 222
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AAG H

IMMUNOGLOBULIN 06-APR-92 :: CARCINOGENIC EMBRYO ANTIGEN ANTIBODY (THEORETICAL

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 113 ; The following residues NOT assigned to any domain: Chain "H" 1 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MIG H

IMMUNOGLOBULIN 12-NOV-93 :: FV FRAGMENT OF CATALYTIC ANTIBODY NPN43C9 COMPLEXE

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 112 ; The following residues NOT assigned to any domain: Chain "H" 1 - 107
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1VFA B

IMMUNOGLOBULIN 03-DEC-93 :: FV FRAGMENT OF MOUSE MONOCLONAL ANTIBODY D1.3

DOMAIN 1: [Assigned by homology with 1HILA]B 1 to B 116 ; The following residues NOT assigned to any domain: Chain "B" 1 - 108
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1VFB B

IMMUNOGLOBULIN/HYDROLASE(O-GLYCOSYL) 03-DEC-93 :: FV FRAGMENT OF MOUSE MONOCLONAL ANTIBODY D1.3 COMP

DOMAIN 1: [Assigned by homology with 1HILA]B 1 to B 116 ; The following residues NOT assigned to any domain: Chain "B" 1 - 107 The following residues NOT assigned to any domain: Chain "B" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HFM H

IMMUNOGLOBULIN 30-OCT-87 :: IG*G1 FV FRAGMENT (HY/HEL$-10) (THEORETICAL MODEL)

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 113 ; The following residues NOT assigned to any domain: Chain "H" 1 - 107
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HFM H

COMPLEX(ANTIBODY-ANTIGEN) 30-OCT-87 :: IG*G1 FV FRAGMENT (HY/HEL$-10) AND LYSOZYME (E.C.3

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 113 ; The following residues NOT assigned to any domain: Chain "H" 1 - 107 The following residues NOT assigned to any domain: Chain "H" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2RHE

IMMUNOGLOBULIN 13-JUN-83 :: BENCE-*JONES PROTEIN (LAMBDA, VARIABLE DOMAIN)

DOMAIN 1: [Assigned by homology with 1HILA] 1 to 114 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2IMN

IMUNOGLOBULIN 30-MAR-92 :: IMMUNOGLOBULIN VL DOMAIN (VARIABLE DOMAIN OF KAPPA

DOMAIN 1: [Assigned by homology with 1HILA] 1 to 108 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LVD

IMMUNOGLOBULIN 19-JUL-94 :: LEN, A VARIABLE DOMAIN FROM IMMUNOGLOBULIN LIGHT-C

DOMAIN 1: [Assigned by homology with 1HILA] 1 to 107 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2IMM

IMMUNOGLOBULIN 01-MAR-93 :: IMMUNOGLOBULIN VL DOMAIN (VARIABLE DOMAIN OF KAPPA

DOMAIN 1: [Assigned by homology with 1HILA] 1 to 108 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FVC A

IMMUNOGLOBULIN 20-OCT-92 :: FV FRAGMENT OF HUMANIZED ANTIBODY 4D5, VERSION 8

DOMAIN 1: [Assigned by homology with 1HILA]A 1 to A 109 ; The following residues NOT assigned to any domain: Chain "A" 1 - 120 The following residues NOT assigned to any domain: Chain "A" 1 - 108 The following residues NOT assigned to any domain: Chain "A" 1 - 120
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1REI A

IMMUNOGLOBULIN(PART)SEQUESTERS ANTIGENS 17-MAR-76 :: BENCE-*JONES IMMUNOGLOBULIN /REI$ VARIABLE PORTION

DOMAIN 1: [Assigned by homology with 1HILA]A 1 to A 107 ; The following residues NOT assigned to any domain: Chain "A" 1 - 107
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1REI B

IMMUNOGLOBULIN(PART)SEQUESTERS ANTIGENS 17-MAR-76 :: BENCE-*JONES IMMUNOGLOBULIN /REI$ VARIABLE PORTION

DOMAIN 1: [Assigned by homology with 1HILA]B 1 to B 107 ; The following residues NOT assigned to any domain: Chain "B" 1 - 107
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FVC C

IMMUNOGLOBULIN 20-OCT-92 :: FV FRAGMENT OF HUMANIZED ANTIBODY 4D5, VERSION 8

DOMAIN 1: [Assigned by homology with 1HILA]C 1 to C 108 ; The following residues NOT assigned to any domain: Chain "C" 1 - 109 The following residues NOT assigned to any domain: Chain "C" 1 - 120 The following residues NOT assigned to any domain: Chain "C" 1 - 120
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MIG L

IMMUNOGLOBULIN 12-NOV-93 :: FV FRAGMENT OF CATALYTIC ANTIBODY NPN43C9 COMPLEXE

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 107 ; The following residues NOT assigned to any domain: Chain "L" 1 - 112
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FGV L

IMMUNOGLOBULIN 01-NOV-93 :: FV FRAGMENT OF A HUMANIZED VERSION OF THE ANTI-CD1

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 107 ; The following residues NOT assigned to any domain: Chain "L" 1 - 124
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AAG L

IMMUNOGLOBULIN 06-APR-92 :: CARCINOGENIC EMBRYO ANTIGEN ANTIBODY (THEORETICAL

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; The following residues NOT assigned to any domain: Chain "L" 1 - 113
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FVB L

IMMUNOGLOBULIN 09-APR-88 :: IG*A FV FRAGMENT (19.1.2, ANTI-ALPHA(1(RIGHT ARROW

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 106 ; The following residues NOT assigned to any domain: Chain "L" 1 - 119
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2FVB L

IMMUNOGLOBULIN 09-APR-88 :: IG*A FV FRAGMENT (19.1.2, ANTI-ALPHA(1(RIGHT ARROW

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 106 ; The following residues NOT assigned to any domain: Chain "L" 1 - 119
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1WTL A

IMMUNOGLOBULIN 08-JUN-94 :: WAT, A VARIABLE DOMAIN FROM IMMUNOGLOBULIN LIGHT-C

DOMAIN 1: [Assigned by homology with 1HILA]A 1 to A 108 ; The following residues NOT assigned to any domain: Chain "A" 1 - 108
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1WTL B

IMMUNOGLOBULIN 08-JUN-94 :: WAT, A VARIABLE DOMAIN FROM IMMUNOGLOBULIN LIGHT-C

DOMAIN 1: [Assigned by homology with 1HILA]B 1 to B 108 ; The following residues NOT assigned to any domain: Chain "B" 1 - 108
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IGM L

IMMUNOGLOBULIN 10-JUL-92 :: IMMUNOGLOBULIN M (IG-M) FV FRAGMENT

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 115 ; The following residues NOT assigned to any domain: Chain "L" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FVW L

IMMUNOGLOBULIN 09-APR-88 :: IG*A FV FRAGMENT (W3129, ANTI-ALPHA(1(RIGHT ARROW)

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 112 ; The following residues NOT assigned to any domain: Chain "L" 1 - 121
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2FVW L

IMMUNOGLOBULIN 09-APR-88 :: IG*A FV FRAGMENT (W3129, ANTI-ALPHA(1(RIGHT ARROW)

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 112 ; The following residues NOT assigned to any domain: Chain "L" 1 - 121
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1VFB A

IMMUNOGLOBULIN/HYDROLASE(O-GLYCOSYL) 03-DEC-93 :: FV FRAGMENT OF MOUSE MONOCLONAL ANTIBODY D1.3 COMP

DOMAIN 1: [Assigned by homology with 1HILA]A 1 to A 107 ; The following residues NOT assigned to any domain: Chain "A" 1 - 116 The following residues NOT assigned to any domain: Chain "A" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1VFA A

IMMUNOGLOBULIN 03-DEC-93 :: FV FRAGMENT OF MOUSE MONOCLONAL ANTIBODY D1.3

DOMAIN 1: [Assigned by homology with 1HILA]A 1 to A 108 ; The following residues NOT assigned to any domain: Chain "A" 1 - 116
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MAJ

IMMUNOGLOBULIN 16-SEP-93 :: MURINE ANTIBODY 26-10 VL DOMAIN (NMR, 15 ENERGY MI

DOMAIN 1: [Assigned by homology with 1HILA] 1 to 113 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MAK

IMMUNOGLOBULIN 16-SEP-93 :: MURINE ANTIBODY 26-10 VL DOMAIN (NMR, 15 SIMULATED

DOMAIN 1: [Assigned by homology with 1HILA] 1 to 113 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1JHL L

COMPLEX(ANTIBODY-ANTIGEN) 04-MAY-93 :: FV FRAGMENT (LIGHT AND HEAVY VARIABLE DOMAINS

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 108 ; The following residues NOT assigned to any domain: Chain "L" 1 - 116 The following residues NOT assigned to any domain: Chain "L" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IVL A

IMMUNOGLOBULIN 04-MAY-94 :: IMMUNOGLOBULIN VL DOMAIN (VARIABLE DOMAIN OF KAPPA

DOMAIN 1: [Assigned by homology with 1HILA]A 1 to A 107 ; The following residues NOT assigned to any domain: Chain "A" 1 - 107
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IVL B

IMMUNOGLOBULIN 04-MAY-94 :: IMMUNOGLOBULIN VL DOMAIN (VARIABLE DOMAIN OF KAPPA

DOMAIN 1: [Assigned by homology with 1HILA]B 1 to B 107 ; The following residues NOT assigned to any domain: Chain "B" 1 - 107
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HFM L

IMMUNOGLOBULIN 30-OCT-87 :: IG*G1 FV FRAGMENT (HY/HEL$-10) (THEORETICAL MODEL)

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 107 ; The following residues NOT assigned to any domain: Chain "L" 1 - 113
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HFM L

COMPLEX(ANTIBODY-ANTIGEN) 30-OCT-87 :: IG*G1 FV FRAGMENT (HY/HEL$-10) AND LYSOZYME (E.C.3

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 107 ; The following residues NOT assigned to any domain: Chain "L" 1 - 113 The following residues NOT assigned to any domain: Chain "L" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4PHV A

HYDROLASE(ASPARTIC PROTEINASE) 04-OCT-91 :: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 (HIV-1) PROTEA

DOMAIN 1: [Assigned by homology with 1HIVA]A 1 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 99 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4PHV B

HYDROLASE(ASPARTIC PROTEINASE) 04-OCT-91 :: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 (HIV-1) PROTEA

DOMAIN 1: [Assigned by homology with 1HIVA]B 1 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 99 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5HVP A

HYDROLASE(ACID PROTEINASE) 30-APR-90 :: /HIV$-1 PROTEASE COMPLEX WITH ACETYL-PEPSTATIN

DOMAIN 1: [Assigned by homology with 1HIVA]A 1 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 99 - 99 The following residues NOT assigned to any domain: Chain "A" 201 - 299 The following residues NOT assigned to any domain: Chain "A" 1 - 5
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5HVP B

HYDROLASE(ACID PROTEINASE) 30-APR-90 :: /HIV$-1 PROTEASE COMPLEX WITH ACETYL-PEPSTATIN

DOMAIN 1: [Assigned by homology with 1HIVA]B 201 to B 298 ; The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 299 - 299 The following residues NOT assigned to any domain: Chain "B" 1 - 5
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SBG A

HYDROLASE(ACID PROTEASE) 24-MAY-94 :: HIV-1 PROTEASE COMPLEXED WITH THE INHIBITOR SB2033

DOMAIN 1: [Assigned by homology with 1HIVA]A 1 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 99 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SBG B

HYDROLASE(ACID PROTEASE) 24-MAY-94 :: HIV-1 PROTEASE COMPLEXED WITH THE INHIBITOR SB2033

DOMAIN 1: [Assigned by homology with 1HIVA]B 1 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 99 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

9HVP A

HYDROLASE(ACID PROTEINASE) 06-NOV-90 :: /HIV$-1 PROTEASE COMPLEX WITH A-74704

DOMAIN 1: [Assigned by homology with 1HIVA]A 1 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 99 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 99 The following residues NOT assigned to any domain: Chain "A" 2 - 4
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

9HVP B

HYDROLASE(ACID PROTEINASE) 06-NOV-90 :: /HIV$-1 PROTEASE COMPLEX WITH A-74704

DOMAIN 1: [Assigned by homology with 1HIVA]B 1 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 99 - 99 The following residues NOT assigned to any domain: Chain "B" 2 - 4
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HVP

HYDROLASE(ACID PROTEINASE) 10-APR-89 :: /HIV$-1 PROTEASE

DOMAIN 1: [Assigned by homology with 1HIVA] 6 to 98 ; The following residues NOT assigned to any domain: Chain " " 99 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HHP

HYDROLASE(ACID PROTEINASE) 27-MAY-92 :: HIV-1 PROTEASE (BRU ISOLATE)

DOMAIN 1: [Assigned by homology with 1HIVA] 1 to 98 ; The following residues NOT assigned to any domain: Chain " " 99 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HIV B

HYDROLASE(ACID PROTEINASE) 12-FEB-92 :: HIV-1 PROTEASE (HIV-1 PR) COMPLEX WITH U75875

DOMAIN 1: [Assigned by homology with 1HIVA]B 1 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 99 - 99 The following residues NOT assigned to any domain: Chain "B" 2 - 4
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HOS A

HYDROLASE(ACID PROTEINASE) 06-APR-93 :: HIV-1 PROTEASE COMPLEX WITH SB204144

DOMAIN 1: [Assigned by homology with 1HIVA]A 1 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 99 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HOS B

HYDROLASE(ACID PROTEINASE) 06-APR-93 :: HIV-1 PROTEASE COMPLEX WITH SB204144

DOMAIN 1: [Assigned by homology with 1HIVA]B 1 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 99 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HPS A

HYDROLASE(ACID PROTEINASE) 24-MAY-94 :: HIV-1 PROTEASE COMPLEXED WITH SB206343

DOMAIN 1: [Assigned by homology with 1HIVA]A 1 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 99 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HPS B

HYDROLASE(ACID PROTEINASE) 24-MAY-94 :: HIV-1 PROTEASE COMPLEXED WITH SB206343

DOMAIN 1: [Assigned by homology with 1HIVA]B 1 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 99 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HTE A

HYDROLASE(ACID PROTEINASE) 29-APR-94 :: HIV-1 PROTEASE COMPLEXED WITH GR123976

DOMAIN 1: [Assigned by homology with 1HIVA]A 1 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 99 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 99 The following residues NOT assigned to any domain: Chain "A" 202 - 205
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HTE B

HYDROLASE(ACID PROTEINASE) 29-APR-94 :: HIV-1 PROTEASE COMPLEXED WITH GR123976

DOMAIN 1: [Assigned by homology with 1HIVA]B 1 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 99 - 99 The following residues NOT assigned to any domain: Chain "B" 202 - 205
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HTF A

HYDROLASE(ACID PROTEINASE) 29-APR-94 :: HIV-1 PROTEASE COMPLEXED WITH GR126045

DOMAIN 1: [Assigned by homology with 1HIVA]A 1 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 99 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HTF B

HYDROLASE(ACID PROTEINASE) 29-APR-94 :: HIV-1 PROTEASE COMPLEXED WITH GR126045

DOMAIN 1: [Assigned by homology with 1HIVA]B 1 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 99 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HTG A

HYDROLASE(ACID PROTEINASE) 29-APR-94 :: HIV-1 PROTEASE COMPLEXED WITH GR137615

DOMAIN 1: [Assigned by homology with 1HIVA]A 1 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 99 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HTG B

HYDROLASE(ACID PROTEINASE) 29-APR-94 :: HIV-1 PROTEASE COMPLEXED WITH GR137615

DOMAIN 1: [Assigned by homology with 1HIVA]B 1 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 99 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HVI A

HYDROLASE(ACID PROTEASE) 26-JAN-94 :: HIV-1 PROTEASE COMPLEXED WITH THE INHIBITOR A77003

DOMAIN 1: [Assigned by homology with 1HIVA]A 1 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 99 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HVI B

HYDROLASE(ACID PROTEASE) 26-JAN-94 :: HIV-1 PROTEASE COMPLEXED WITH THE INHIBITOR A77003

DOMAIN 1: [Assigned by homology with 1HIVA]B 1 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 99 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HVJ A

HYDROLASE(ACID PROTEASE) 26-JAN-94 :: HIV-1 PROTEASE COMPLEXED WITH THE INHIBITOR A78791

DOMAIN 1: [Assigned by homology with 1HIVA]A 1 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 99 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HVJ B

HYDROLASE(ACID PROTEASE) 26-JAN-94 :: HIV-1 PROTEASE COMPLEXED WITH THE INHIBITOR A78791

DOMAIN 1: [Assigned by homology with 1HIVA]B 1 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 99 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HVK A

HYDROLASE(ACID PROTEASE) 26-JAN-94 :: HIV-1 PROTEASE COMPLEXED WITH THE INHIBITOR A76928

DOMAIN 1: [Assigned by homology with 1HIVA]A 1 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 99 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HVK B

HYDROLASE(ACID PROTEASE) 26-JAN-94 :: HIV-1 PROTEASE COMPLEXED WITH THE INHIBITOR A76928

DOMAIN 1: [Assigned by homology with 1HIVA]B 1 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 99 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HVL A

HYDROLASE(ACID PROTEASE) 26-JAN-94 :: HIV-1 PROTEASE COMPLEXED WITH THE INHIBITOR A76889

DOMAIN 1: [Assigned by homology with 1HIVA]A 1 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 99 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HVL B

HYDROLASE(ACID PROTEASE) 26-JAN-94 :: HIV-1 PROTEASE COMPLEXED WITH THE INHIBITOR A76889

DOMAIN 1: [Assigned by homology with 1HIVA]B 1 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 99 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HVP A

HYDROLASE(ACID PROTEINASE) 14-MAR-89 :: /HIV$-1 PROTEASE COMPLEX WITH SUBSTRATE (THEORETIC

DOMAIN 1: [Assigned by homology with 1HIVA]A 1 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 99 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 7
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HVP B

HYDROLASE(ACID PROTEINASE) 14-MAR-89 :: /HIV$-1 PROTEASE COMPLEX WITH SUBSTRATE (THEORETIC

DOMAIN 1: [Assigned by homology with 1HIVA]B 1 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 99 - 99 The following residues NOT assigned to any domain: Chain "B" 1 - 7
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3PHV

HYDROLASE(ASPARTIC PROTEINASE) 04-NOV-91 :: /HIV$-1 PROTEASE (ISOLATE HXB2)

DOMAIN 1: [Assigned by homology with 1HIVA] 1 to 98 ; The following residues NOT assigned to any domain: Chain " " 99 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HVC

HYDROLASE(ACID PROTEASE) 22-JUN-94 :: HIV-1 PROTEASE (TETHERED DIMER LINKED BY

DOMAIN 1: [Assigned by homology with 1HIVA] 1 B to 98 A ; The following residues NOT assigned to any domain: Chain " " 99A - 99A
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AAQ A

HYDROLASE(ACID PROTEASE) 13-APR-92 :: HIV-1 PROTEASE COMPLEXED WITH HYDROXYETHYLENE ISOS

DOMAIN 1: [Assigned by homology with 1HIVA]A 1 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 99 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AAQ B

HYDROLASE(ACID PROTEASE) 13-APR-92 :: HIV-1 PROTEASE COMPLEXED WITH HYDROXYETHYLENE ISOS

DOMAIN 1: [Assigned by homology with 1HIVA]B 1 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 99 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HEF E

HYDROLASE(ACID PROTEINASE) 21-SEP-92 :: HIV-1 PROTEASE COMPLEXED WITH SKF 108738 (HEF)

DOMAIN 1: [Assigned by homology with 1HIVA]E 1 to E 98 ; The following residues NOT assigned to any domain: Chain "E" 99 - 99 The following residues NOT assigned to any domain: Chain "E" 201 - 206
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HEG E

HYDROLASE(ACID PROTEINASE) 21-SEP-92 :: HIV-1 PROTEASE COMPLEXED WITH SKF 107457 (HEG)

DOMAIN 1: [Assigned by homology with 1HIVA]E 1 to E 98 ; The following residues NOT assigned to any domain: Chain "E" 99 - 99 The following residues NOT assigned to any domain: Chain "E" 201 - 206
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4HVP A

HYDROLASE(ACID PROTEINASE) 08-AUG-89 :: /HIV$-1 PROTEASE (/HIV-1$ /PR$) COMPLEX WITH INHIB

DOMAIN 1: [Assigned by homology with 1HIVA]A 1 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 99 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 99 The following residues NOT assigned to any domain: Chain "A" 0 - 6
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4HVP B

HYDROLASE(ACID PROTEINASE) 08-AUG-89 :: /HIV$-1 PROTEASE (/HIV-1$ /PR$) COMPLEX WITH INHIB

DOMAIN 1: [Assigned by homology with 1HIVA]B 1 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 99 - 99 The following residues NOT assigned to any domain: Chain "B" 0 - 6
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7HVP A

HYDROLASE(ACID PROTEINASE) 13-SEP-90 :: /HIV$-1 PROTEASE (/HIV-1$ /PR$) COMPLEX WITH INHIB

DOMAIN 1: [Assigned by homology with 1HIVA]A 1 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 99 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 99 The following residues NOT assigned to any domain: Chain "A" 0 - 8
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7HVP B

HYDROLASE(ACID PROTEINASE) 13-SEP-90 :: /HIV$-1 PROTEASE (/HIV-1$ /PR$) COMPLEX WITH INHIB

DOMAIN 1: [Assigned by homology with 1HIVA]B 1 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 99 - 99 The following residues NOT assigned to any domain: Chain "B" 0 - 8
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8HVP A

HYDROLASE(ACID PROTEINASE) 26-OCT-90 :: HIV-1 PROTEASE (HIV-1 PR) COMPLEX WITH INHIBITOR

DOMAIN 1: [Assigned by homology with 1HIVA]A 1 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 99 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 8
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8HVP B

HYDROLASE(ACID PROTEINASE) 26-OCT-90 :: HIV-1 PROTEASE (HIV-1 PR) COMPLEX WITH INHIBITOR

DOMAIN 1: [Assigned by homology with 1HIVA]B 1 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 99 - 99 The following residues NOT assigned to any domain: Chain "B" 1 - 8
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3HVP

HYDROLASE(ACID PROTEINASE) 08-AUG-89 :: (/ABA$==67,95==)-/HIV$-1 PROTEASE (/SF2$ ISOLATE)

DOMAIN 1: [Assigned by homology with 1HIVA] 1 to 98 ; The following residues NOT assigned to any domain: Chain " " 99 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SIP

HYDROLASE(ACID PROTEINASE) 13-APR-94 :: SIMIAN IMMUNODEFICIENCY VIRUS (SIV) PROTEINASE

DOMAIN 1: [Assigned by homology with 1HIVA] 1 to 98 ; The following residues NOT assigned to any domain: Chain " " 99 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2SAM

HYDROLASE(ACID PROTEASE) 08-JUL-94 :: SIMIAN IMMUNODEFICIENCY VIRUS (SIV) PROTEASE MUTAN

DOMAIN 1: [Assigned by homology with 1HIVA] 1 to 98 ; The following residues NOT assigned to any domain: Chain " " 99 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SIV A

HYDROLASE(ACID PROTEINASE) 24-AUG-93 :: SIMIAN IMMUNODEFICIENCY VIRUS (SIV) PROTEASE COMPL

DOMAIN 1: [Assigned by homology with 1HIVA]A 1 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 99 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SIV B

HYDROLASE(ACID PROTEINASE) 24-AUG-93 :: SIMIAN IMMUNODEFICIENCY VIRUS (SIV) PROTEASE COMPL

DOMAIN 1: [Assigned by homology with 1HIVA]B 1 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 99 - 99
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MIP A

HYDROLASE(ACID PROTEINASE) 03-JUN-93 :: HUMAN IMMUNODEFICIENCY VIRUS TYPE 2 (HIV-2) PROTEA

DOMAIN 1: [Assigned by homology with 1HIVA]A 1 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 99 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 6 The following residues NOT assigned to any domain: Chain "A" 1 - 6 The following residues NOT assigned to any domain: Chain "A" 1 - 6 The following residues NOT assigned to any domain: Chain "A" 1 - 6
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MIP B

HYDROLASE(ACID PROTEINASE) 03-JUN-93 :: HUMAN IMMUNODEFICIENCY VIRUS TYPE 2 (HIV-2) PROTEA

DOMAIN 1: [Assigned by homology with 1HIVA]B 1 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 99 - 99 The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 1 - 6 The following residues NOT assigned to any domain: Chain "B" 1 - 6 The following residues NOT assigned to any domain: Chain "B" 1 - 6 The following residues NOT assigned to any domain: Chain "B" 1 - 6
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MIP C

HYDROLASE(ACID PROTEINASE) 03-JUN-93 :: HUMAN IMMUNODEFICIENCY VIRUS TYPE 2 (HIV-2) PROTEA

DOMAIN 1: [Assigned by homology with 1HIVA]C 1 to C 98 ; The following residues NOT assigned to any domain: Chain "C" 1 - 99 The following residues NOT assigned to any domain: Chain "C" 1 - 99 The following residues NOT assigned to any domain: Chain "C" 99 - 99 The following residues NOT assigned to any domain: Chain "C" 1 - 99 The following residues NOT assigned to any domain: Chain "C" 1 - 6 The following residues NOT assigned to any domain: Chain "C" 1 - 6 The following residues NOT assigned to any domain: Chain "C" 1 - 6 The following residues NOT assigned to any domain: Chain "C" 1 - 6
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MIP D

HYDROLASE(ACID PROTEINASE) 03-JUN-93 :: HUMAN IMMUNODEFICIENCY VIRUS TYPE 2 (HIV-2) PROTEA

DOMAIN 1: [Assigned by homology with 1HIVA]D 1 to D 98 ; The following residues NOT assigned to any domain: Chain "D" 1 - 99 The following residues NOT assigned to any domain: Chain "D" 1 - 99 The following residues NOT assigned to any domain: Chain "D" 1 - 99 The following residues NOT assigned to any domain: Chain "D" 99 - 99 The following residues NOT assigned to any domain: Chain "D" 1 - 6 The following residues NOT assigned to any domain: Chain "D" 1 - 6 The following residues NOT assigned to any domain: Chain "D" 1 - 6 The following residues NOT assigned to any domain: Chain "D" 1 - 6
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PHV A

HYDROLASE (ACID PROTEASE) 28-FEB-91 :: HIV-2 PROTEASE (HIV-2 PR) COMPLEX WITH RENIN INHIB

DOMAIN 1: [Assigned by homology with 1HIVA]A 1 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 99 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 8
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PHV B

HYDROLASE (ACID PROTEASE) 28-FEB-91 :: HIV-2 PROTEASE (HIV-2 PR) COMPLEX WITH RENIN INHIB

DOMAIN 1: [Assigned by homology with 1HIVA]B 1 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 99 - 99 The following residues NOT assigned to any domain: Chain "B" 1 - 8
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PHV A

HYDROLASE (ACID PROTEASE) 28-FEB-91 :: HIV-2 PROTEASE (HIV-2 PR) COMPLEX WITH INHIBITOR

DOMAIN 1: [Assigned by homology with 1HIVA]A 1 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 99 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 5
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PHV B

HYDROLASE (ACID PROTEASE) 28-FEB-91 :: HIV-2 PROTEASE (HIV-2 PR) COMPLEX WITH INHIBITOR

DOMAIN 1: [Assigned by homology with 1HIVA]B 1 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 99 - 99 The following residues NOT assigned to any domain: Chain "B" 1 - 5
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IVP A

HYDROLASE(ACID PROTEINASE) 18-MAR-93 :: HUMAN IMMUNODEFICIENCY VIRUS TYPE 2 PROTEASE MUTAN

DOMAIN 1: [Assigned by homology with 1HIVA]A 1 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 99 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 99 The following residues NOT assigned to any domain: Chain "A" 2 - 4
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IVP B

HYDROLASE(ACID PROTEINASE) 18-MAR-93 :: HUMAN IMMUNODEFICIENCY VIRUS TYPE 2 PROTEASE MUTAN

DOMAIN 1: [Assigned by homology with 1HIVA]B 1 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 99 - 99 The following residues NOT assigned to any domain: Chain "B" 2 - 4
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IVQ A

HYDROLASE(ACID PROTEINASE) 18-MAR-93 :: HUMAN IMMUNODEFICIENCY VIRUS TYPE 2 PROTEASE MUTAN

DOMAIN 1: [Assigned by homology with 1HIVA]A 1 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 99 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 99 The following residues NOT assigned to any domain: Chain "A" 2 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IVQ B

HYDROLASE(ACID PROTEINASE) 18-MAR-93 :: HUMAN IMMUNODEFICIENCY VIRUS TYPE 2 PROTEASE MUTAN

DOMAIN 1: [Assigned by homology with 1HIVA]B 1 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 99 - 99 The following residues NOT assigned to any domain: Chain "B" 2 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HPE A

HYDROLASE(ACID PROTEASE) 21-SEP-94 :: HIV-2 PROTEASE MUTANT WITH LYS 57 REPLACED BY LEU

DOMAIN 1: [Assigned by homology with 1HIVA]A 1 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 99 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 9
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HPE B

HYDROLASE(ACID PROTEASE) 21-SEP-94 :: HIV-2 PROTEASE MUTANT WITH LYS 57 REPLACED BY LEU

DOMAIN 1: [Assigned by homology with 1HIVA]B 1 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 99 - 99 The following residues NOT assigned to any domain: Chain "B" 1 - 9
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HPF A

HYDROLASE(ACID PROTEASE) 21-SEP-94 :: HIV-2 PROTEASE MUTANT WITH LYS 57 REPLACED BY LEU

DOMAIN 1: [Assigned by homology with 1HIVA]A 1 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 99 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 8
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HPF B

HYDROLASE(ACID PROTEASE) 21-SEP-94 :: HIV-2 PROTEASE MUTANT WITH LYS 57 REPLACED BY LEU

DOMAIN 1: [Assigned by homology with 1HIVA]B 1 to B 98 ; The following residues NOT assigned to any domain: Chain "B" 1 - 99 The following residues NOT assigned to any domain: Chain "B" 99 - 99 The following residues NOT assigned to any domain: Chain "B" 1 - 8
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EQI A

HYDROLASE(ACID PROTEINASE) 15-JUL-94 :: EQUINE INFECTIOUS ANEMIA VIRUS PROTEASE (THEORETIC

DOMAIN 1: [Assigned by homology with 1HIVA]A 1 to A 103 ; The following residues NOT assigned to any domain: Chain "A" 104 - 104 The following residues NOT assigned to any domain: Chain "A" 1 - 104 The following residues NOT assigned to any domain: Chain "A" 1 - 9
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EQI B

HYDROLASE(ACID PROTEINASE) 15-JUL-94 :: EQUINE INFECTIOUS ANEMIA VIRUS PROTEASE (THEORETIC

DOMAIN 1: [Assigned by homology with 1HIVA]B 1 to B 103 ; The following residues NOT assigned to any domain: Chain "B" 1 - 104 The following residues NOT assigned to any domain: Chain "B" 104 - 104 The following residues NOT assigned to any domain: Chain "B" 1 - 9
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HIF

CYTOKINE 07-JUN-94 :: INTERFERON BETA (THEORETICAL MODEL)

DOMAIN 1: 3 to 160 ; The following residues NOT assigned to any domain: Chain " " 161 - 161
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HIE

CYTOKINE 07-JUN-94 :: INTERFERON ALPHA-2B (THEORETICAL MODEL)

DOMAIN 1: 1 to 162 ; The following residues NOT assigned to any domain: Chain " " 163 - 165
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ISU B

PRELIMINARY 09-SEP-92 :: HIGH-POTENTIAL IRON-SULFUR PROTEIN (HIPIP)

DOMAIN 1: [Assigned by homology with 1ISUA]B 1 to B 62 ; The following residues NOT assigned to any domain: Chain "B" 1 - 62
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CCF

COAGULATION FACTOR 19-MAY-93 :: COAGULATION FACTOR X (THE CALCIUM FORM OF THE N-TE

DOMAIN 1: 45 to 83 ; The following residues NOT assigned to any domain: Chain " " 84 - 86
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1APO

PRELIMINARY 21-APR-92 :: THE N-TERMINAL EGF-LIKE MODULE OF BLOOD COAGULATIO

DOMAIN 1: 45 to 83 ; The following residues NOT assigned to any domain: Chain " " 84 - 86
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTA A

ENTEROTOXIN 15-SEP-93 :: HEAT-LABILE ENTEROTOXIN (LT) COMPLEX WITH GALACTOS

DOMAIN 1: [Assigned by homology with 1LTSA]A 1 to A 187 ; The following residues NOT assigned to any domain: Chain "A" 1 - 103 The following residues NOT assigned to any domain: Chain "A" 1 - 103 The following residues NOT assigned to any domain: Chain "A" 1 - 103 The following residues NOT assigned to any domain: Chain "A" 1 - 103 The following residues NOT assigned to any domain: Chain "A" 1 - 103 The following residues NOT assigned to any domain: Chain "A" 188 - 188 The following residues NOT assigned to any domain: Chain "A" 196 - 240
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTB A

ENTEROTOXIN 15-SEP-93 :: HEAT-LABILE ENTEROTOXIN (LT) (PARTIALLY ACTIVATED

DOMAIN 1: [Assigned by homology with 1LTSA]A 4 to A 187 ; The following residues NOT assigned to any domain: Chain "A" 1 - 103 The following residues NOT assigned to any domain: Chain "A" 1 - 103 The following residues NOT assigned to any domain: Chain "A" 1 - 103 The following residues NOT assigned to any domain: Chain "A" 1 - 103 The following residues NOT assigned to any domain: Chain "A" 1 - 103 The following residues NOT assigned to any domain: Chain "A" 188 - 188 The following residues NOT assigned to any domain: Chain "A" 196 - 236
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTT A

PRELIMINARY 15-JUL-92 :: HEAT-LABILE ENTEROTOXIN (LT); CHOLERA-LIKE TOXIN,

DOMAIN 1: [Assigned by homology with 1LTSA]A 4 to A 187 ; The following residues NOT assigned to any domain: Chain "A" 1 - 103 The following residues NOT assigned to any domain: Chain "A" 1 - 103 The following residues NOT assigned to any domain: Chain "A" 1 - 103 The following residues NOT assigned to any domain: Chain "A" 1 - 103 The following residues NOT assigned to any domain: Chain "A" 1 - 103 The following residues NOT assigned to any domain: Chain "A" 188 - 188 The following residues NOT assigned to any domain: Chain "A" 196 - 236
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTA C

ENTEROTOXIN 15-SEP-93 :: HEAT-LABILE ENTEROTOXIN (LT) COMPLEX WITH GALACTOS

DOMAIN 1: [Assigned by homology with 1LTSC]C 196 to C 236 ; The following residues NOT assigned to any domain: Chain "C" 1 - 103 The following residues NOT assigned to any domain: Chain "C" 1 - 103 The following residues NOT assigned to any domain: Chain "C" 1 - 103 The following residues NOT assigned to any domain: Chain "C" 1 - 103 The following residues NOT assigned to any domain: Chain "C" 1 - 103 The following residues NOT assigned to any domain: Chain "C" 1 - 188 The following residues NOT assigned to any domain: Chain "C" 237 - 240
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTB C

ENTEROTOXIN 15-SEP-93 :: HEAT-LABILE ENTEROTOXIN (LT) (PARTIALLY ACTIVATED

DOMAIN 1: [Assigned by homology with 1LTSC]C 196 to C 236 ; The following residues NOT assigned to any domain: Chain "C" 1 - 103 The following residues NOT assigned to any domain: Chain "C" 1 - 103 The following residues NOT assigned to any domain: Chain "C" 1 - 103 The following residues NOT assigned to any domain: Chain "C" 1 - 103 The following residues NOT assigned to any domain: Chain "C" 1 - 103 The following residues NOT assigned to any domain: Chain "C" 4 - 188
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTT C

PRELIMINARY 15-JUL-92 :: HEAT-LABILE ENTEROTOXIN (LT); CHOLERA-LIKE TOXIN,

DOMAIN 1: [Assigned by homology with 1LTSC]C 196 to C 236 ; The following residues NOT assigned to any domain: Chain "C" 1 - 103 The following residues NOT assigned to any domain: Chain "C" 1 - 103 The following residues NOT assigned to any domain: Chain "C" 1 - 103 The following residues NOT assigned to any domain: Chain "C" 1 - 103 The following residues NOT assigned to any domain: Chain "C" 1 - 103 The following residues NOT assigned to any domain: Chain "C" 4 - 188
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTA D

ENTEROTOXIN 15-SEP-93 :: HEAT-LABILE ENTEROTOXIN (LT) COMPLEX WITH GALACTOS

DOMAIN 1: [Assigned by homology with 1LTSD]D 1 to D 103 ; The following residues NOT assigned to any domain: Chain "D" 1 - 103 The following residues NOT assigned to any domain: Chain "D" 1 - 103 The following residues NOT assigned to any domain: Chain "D" 1 - 103 The following residues NOT assigned to any domain: Chain "D" 1 - 103 The following residues NOT assigned to any domain: Chain "D" 1 - 188 The following residues NOT assigned to any domain: Chain "D" 196 - 240
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTA E

ENTEROTOXIN 15-SEP-93 :: HEAT-LABILE ENTEROTOXIN (LT) COMPLEX WITH GALACTOS

DOMAIN 1: [Assigned by homology with 1LTSD]E 1 to E 103 ; The following residues NOT assigned to any domain: Chain "E" 1 - 103 The following residues NOT assigned to any domain: Chain "E" 1 - 103 The following residues NOT assigned to any domain: Chain "E" 1 - 103 The following residues NOT assigned to any domain: Chain "E" 1 - 103 The following residues NOT assigned to any domain: Chain "E" 1 - 188 The following residues NOT assigned to any domain: Chain "E" 196 - 240
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTA F

ENTEROTOXIN 15-SEP-93 :: HEAT-LABILE ENTEROTOXIN (LT) COMPLEX WITH GALACTOS

DOMAIN 1: [Assigned by homology with 1LTSD]F 1 to F 103 ; The following residues NOT assigned to any domain: Chain "F" 1 - 103 The following residues NOT assigned to any domain: Chain "F" 1 - 103 The following residues NOT assigned to any domain: Chain "F" 1 - 103 The following residues NOT assigned to any domain: Chain "F" 1 - 103 The following residues NOT assigned to any domain: Chain "F" 1 - 188 The following residues NOT assigned to any domain: Chain "F" 196 - 240
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTA G

ENTEROTOXIN 15-SEP-93 :: HEAT-LABILE ENTEROTOXIN (LT) COMPLEX WITH GALACTOS

DOMAIN 1: [Assigned by homology with 1LTSD]G 1 to G 103 ; The following residues NOT assigned to any domain: Chain "G" 1 - 103 The following residues NOT assigned to any domain: Chain "G" 1 - 103 The following residues NOT assigned to any domain: Chain "G" 1 - 103 The following residues NOT assigned to any domain: Chain "G" 1 - 103 The following residues NOT assigned to any domain: Chain "G" 1 - 188 The following residues NOT assigned to any domain: Chain "G" 196 - 240
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTA H

ENTEROTOXIN 15-SEP-93 :: HEAT-LABILE ENTEROTOXIN (LT) COMPLEX WITH GALACTOS

DOMAIN 1: [Assigned by homology with 1LTSD]H 1 to H 103 ; The following residues NOT assigned to any domain: Chain "H" 1 - 103 The following residues NOT assigned to any domain: Chain "H" 1 - 103 The following residues NOT assigned to any domain: Chain "H" 1 - 103 The following residues NOT assigned to any domain: Chain "H" 1 - 103 The following residues NOT assigned to any domain: Chain "H" 1 - 188 The following residues NOT assigned to any domain: Chain "H" 196 - 240
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTB D

ENTEROTOXIN 15-SEP-93 :: HEAT-LABILE ENTEROTOXIN (LT) (PARTIALLY ACTIVATED

DOMAIN 1: [Assigned by homology with 1LTSD]D 1 to D 103 ; The following residues NOT assigned to any domain: Chain "D" 1 - 103 The following residues NOT assigned to any domain: Chain "D" 1 - 103 The following residues NOT assigned to any domain: Chain "D" 1 - 103 The following residues NOT assigned to any domain: Chain "D" 1 - 103 The following residues NOT assigned to any domain: Chain "D" 4 - 188 The following residues NOT assigned to any domain: Chain "D" 196 - 236
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTB E

ENTEROTOXIN 15-SEP-93 :: HEAT-LABILE ENTEROTOXIN (LT) (PARTIALLY ACTIVATED

DOMAIN 1: [Assigned by homology with 1LTSD]E 1 to E 103 ; The following residues NOT assigned to any domain: Chain "E" 1 - 103 The following residues NOT assigned to any domain: Chain "E" 1 - 103 The following residues NOT assigned to any domain: Chain "E" 1 - 103 The following residues NOT assigned to any domain: Chain "E" 1 - 103 The following residues NOT assigned to any domain: Chain "E" 4 - 188 The following residues NOT assigned to any domain: Chain "E" 196 - 236
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTB F

ENTEROTOXIN 15-SEP-93 :: HEAT-LABILE ENTEROTOXIN (LT) (PARTIALLY ACTIVATED

DOMAIN 1: [Assigned by homology with 1LTSD]F 1 to F 103 ; The following residues NOT assigned to any domain: Chain "F" 1 - 103 The following residues NOT assigned to any domain: Chain "F" 1 - 103 The following residues NOT assigned to any domain: Chain "F" 1 - 103 The following residues NOT assigned to any domain: Chain "F" 1 - 103 The following residues NOT assigned to any domain: Chain "F" 4 - 188 The following residues NOT assigned to any domain: Chain "F" 196 - 236
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTB G

ENTEROTOXIN 15-SEP-93 :: HEAT-LABILE ENTEROTOXIN (LT) (PARTIALLY ACTIVATED

DOMAIN 1: [Assigned by homology with 1LTSD]G 1 to G 103 ; The following residues NOT assigned to any domain: Chain "G" 1 - 103 The following residues NOT assigned to any domain: Chain "G" 1 - 103 The following residues NOT assigned to any domain: Chain "G" 1 - 103 The following residues NOT assigned to any domain: Chain "G" 1 - 103 The following residues NOT assigned to any domain: Chain "G" 4 - 188 The following residues NOT assigned to any domain: Chain "G" 196 - 236
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTB H

ENTEROTOXIN 15-SEP-93 :: HEAT-LABILE ENTEROTOXIN (LT) (PARTIALLY ACTIVATED

DOMAIN 1: [Assigned by homology with 1LTSD]H 1 to H 103 ; The following residues NOT assigned to any domain: Chain "H" 1 - 103 The following residues NOT assigned to any domain: Chain "H" 1 - 103 The following residues NOT assigned to any domain: Chain "H" 1 - 103 The following residues NOT assigned to any domain: Chain "H" 1 - 103 The following residues NOT assigned to any domain: Chain "H" 4 - 188 The following residues NOT assigned to any domain: Chain "H" 196 - 236
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTS E

PRELIMINARY 15-JUL-92 :: HEAT-LABILE ENTEROTOXIN (LT); CHOLERA-LIKE TOXIN,

DOMAIN 1: [Assigned by homology with 1LTSD]E 1 to E 103 ; The following residues NOT assigned to any domain: Chain "E" 1 - 103 The following residues NOT assigned to any domain: Chain "E" 1 - 103 The following residues NOT assigned to any domain: Chain "E" 1 - 103 The following residues NOT assigned to any domain: Chain "E" 1 - 103 The following residues NOT assigned to any domain: Chain "E" 4 - 188 The following residues NOT assigned to any domain: Chain "E" 196 - 236
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTS F

PRELIMINARY 15-JUL-92 :: HEAT-LABILE ENTEROTOXIN (LT); CHOLERA-LIKE TOXIN,

DOMAIN 1: [Assigned by homology with 1LTSD]F 1 to F 103 ; The following residues NOT assigned to any domain: Chain "F" 1 - 103 The following residues NOT assigned to any domain: Chain "F" 1 - 103 The following residues NOT assigned to any domain: Chain "F" 1 - 103 The following residues NOT assigned to any domain: Chain "F" 1 - 103 The following residues NOT assigned to any domain: Chain "F" 4 - 188 The following residues NOT assigned to any domain: Chain "F" 196 - 236
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTS G

PRELIMINARY 15-JUL-92 :: HEAT-LABILE ENTEROTOXIN (LT); CHOLERA-LIKE TOXIN,

DOMAIN 1: [Assigned by homology with 1LTSD]G 1 to G 103 ; The following residues NOT assigned to any domain: Chain "G" 1 - 103 The following residues NOT assigned to any domain: Chain "G" 1 - 103 The following residues NOT assigned to any domain: Chain "G" 1 - 103 The following residues NOT assigned to any domain: Chain "G" 1 - 103 The following residues NOT assigned to any domain: Chain "G" 4 - 188 The following residues NOT assigned to any domain: Chain "G" 196 - 236
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTS H

PRELIMINARY 15-JUL-92 :: HEAT-LABILE ENTEROTOXIN (LT); CHOLERA-LIKE TOXIN,

DOMAIN 1: [Assigned by homology with 1LTSD]H 1 to H 103 ; The following residues NOT assigned to any domain: Chain "H" 1 - 103 The following residues NOT assigned to any domain: Chain "H" 1 - 103 The following residues NOT assigned to any domain: Chain "H" 1 - 103 The following residues NOT assigned to any domain: Chain "H" 1 - 103 The following residues NOT assigned to any domain: Chain "H" 4 - 188 The following residues NOT assigned to any domain: Chain "H" 196 - 236
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTT D

PRELIMINARY 15-JUL-92 :: HEAT-LABILE ENTEROTOXIN (LT); CHOLERA-LIKE TOXIN,

DOMAIN 1: [Assigned by homology with 1LTSD]D 1 to D 103 ; The following residues NOT assigned to any domain: Chain "D" 1 - 103 The following residues NOT assigned to any domain: Chain "D" 1 - 103 The following residues NOT assigned to any domain: Chain "D" 1 - 103 The following residues NOT assigned to any domain: Chain "D" 1 - 103 The following residues NOT assigned to any domain: Chain "D" 4 - 188 The following residues NOT assigned to any domain: Chain "D" 196 - 236
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTT E

PRELIMINARY 15-JUL-92 :: HEAT-LABILE ENTEROTOXIN (LT); CHOLERA-LIKE TOXIN,

DOMAIN 1: [Assigned by homology with 1LTSD]E 1 to E 103 ; The following residues NOT assigned to any domain: Chain "E" 1 - 103 The following residues NOT assigned to any domain: Chain "E" 1 - 103 The following residues NOT assigned to any domain: Chain "E" 1 - 103 The following residues NOT assigned to any domain: Chain "E" 1 - 103 The following residues NOT assigned to any domain: Chain "E" 4 - 188 The following residues NOT assigned to any domain: Chain "E" 196 - 236
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTT F

PRELIMINARY 15-JUL-92 :: HEAT-LABILE ENTEROTOXIN (LT); CHOLERA-LIKE TOXIN,

DOMAIN 1: [Assigned by homology with 1LTSD]F 1 to F 103 ; The following residues NOT assigned to any domain: Chain "F" 1 - 103 The following residues NOT assigned to any domain: Chain "F" 1 - 103 The following residues NOT assigned to any domain: Chain "F" 1 - 103 The following residues NOT assigned to any domain: Chain "F" 1 - 103 The following residues NOT assigned to any domain: Chain "F" 4 - 188 The following residues NOT assigned to any domain: Chain "F" 196 - 236
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTT G

PRELIMINARY 15-JUL-92 :: HEAT-LABILE ENTEROTOXIN (LT); CHOLERA-LIKE TOXIN,

DOMAIN 1: [Assigned by homology with 1LTSD]G 1 to G 103 ; The following residues NOT assigned to any domain: Chain "G" 1 - 103 The following residues NOT assigned to any domain: Chain "G" 1 - 103 The following residues NOT assigned to any domain: Chain "G" 1 - 103 The following residues NOT assigned to any domain: Chain "G" 1 - 103 The following residues NOT assigned to any domain: Chain "G" 4 - 188 The following residues NOT assigned to any domain: Chain "G" 196 - 236
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTT H

PRELIMINARY 15-JUL-92 :: HEAT-LABILE ENTEROTOXIN (LT); CHOLERA-LIKE TOXIN,

DOMAIN 1: [Assigned by homology with 1LTSD]H 1 to H 103 ; The following residues NOT assigned to any domain: Chain "H" 1 - 103 The following residues NOT assigned to any domain: Chain "H" 1 - 103 The following residues NOT assigned to any domain: Chain "H" 1 - 103 The following residues NOT assigned to any domain: Chain "H" 1 - 103 The following residues NOT assigned to any domain: Chain "H" 4 - 188 The following residues NOT assigned to any domain: Chain "H" 196 - 236
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CHB D

TOXIN/RECEPTOR COMPLEX 15-SEP-93 :: CHOLERA TOXIN B-PENTAMER (CHOLERAGEN) COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1LTSD]D 1 to D 103 ; The following residues NOT assigned to any domain: Chain "D" 1 - 103 The following residues NOT assigned to any domain: Chain "D" 1 - 103 The following residues NOT assigned to any domain: Chain "D" 1 - 103 The following residues NOT assigned to any domain: Chain "D" 1 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CHB E

TOXIN/RECEPTOR COMPLEX 15-SEP-93 :: CHOLERA TOXIN B-PENTAMER (CHOLERAGEN) COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1LTSD]E 1 to E 103 ; The following residues NOT assigned to any domain: Chain "E" 1 - 103 The following residues NOT assigned to any domain: Chain "E" 1 - 103 The following residues NOT assigned to any domain: Chain "E" 1 - 103 The following residues NOT assigned to any domain: Chain "E" 1 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CHB F

TOXIN/RECEPTOR COMPLEX 15-SEP-93 :: CHOLERA TOXIN B-PENTAMER (CHOLERAGEN) COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1LTSD]F 1 to F 103 ; The following residues NOT assigned to any domain: Chain "F" 1 - 103 The following residues NOT assigned to any domain: Chain "F" 1 - 103 The following residues NOT assigned to any domain: Chain "F" 1 - 103 The following residues NOT assigned to any domain: Chain "F" 1 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CHB G

TOXIN/RECEPTOR COMPLEX 15-SEP-93 :: CHOLERA TOXIN B-PENTAMER (CHOLERAGEN) COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1LTSD]G 1 to G 103 ; The following residues NOT assigned to any domain: Chain "G" 1 - 103 The following residues NOT assigned to any domain: Chain "G" 1 - 103 The following residues NOT assigned to any domain: Chain "G" 1 - 103 The following residues NOT assigned to any domain: Chain "G" 1 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CHB H

TOXIN/RECEPTOR COMPLEX 15-SEP-93 :: CHOLERA TOXIN B-PENTAMER (CHOLERAGEN) COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1LTSD]H 1 to H 103 ; The following residues NOT assigned to any domain: Chain "H" 1 - 103 The following residues NOT assigned to any domain: Chain "H" 1 - 103 The following residues NOT assigned to any domain: Chain "H" 1 - 103 The following residues NOT assigned to any domain: Chain "H" 1 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RIB A

REDUCTASE(ACTING ON CH2) 19-JAN-93 :: PROTEIN R2 OF RIBONUCLEOTIDE REDUCTASE (E.C.1.17.4

DOMAIN 1: [Assigned by homology with 1MRRA]A 1 to A 340 ; The following residues NOT assigned to any domain: Chain "A" 1 - 340
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RIB B

REDUCTASE(ACTING ON CH2) 19-JAN-93 :: PROTEIN R2 OF RIBONUCLEOTIDE REDUCTASE (E.C.1.17.4

DOMAIN 1: [Assigned by homology with 1MRRA]B 1 to B 340 ; The following residues NOT assigned to any domain: Chain "B" 1 - 340
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RNR A

REDUCTASE(ACTING ON CH2) 26-APR-93 :: PROTEIN R2 OF RIBONUCLEOTIDE REDUCTASE (E.C.1.17.4

DOMAIN 1: [Assigned by homology with 1MRRA]A 1 to A 340 ; The following residues NOT assigned to any domain: Chain "A" 1 - 340
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RNR B

REDUCTASE(ACTING ON CH2) 26-APR-93 :: PROTEIN R2 OF RIBONUCLEOTIDE REDUCTASE (E.C.1.17.4

DOMAIN 1: [Assigned by homology with 1MRRA]B 1 to B 340 ; The following residues NOT assigned to any domain: Chain "B" 1 - 340
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MRR B

REDUCTASE (ACTING ON CH2) 28-JUL-92 :: MANGANESE SUBSTITUTED PROTEIN R2 OF

DOMAIN 1: [Assigned by homology with 1MRRA]B 1 to B 340 ; The following residues NOT assigned to any domain: Chain "B" 1 - 340
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NIP A

IRON PROTEIN 29-SEP-92 :: NITROGENASE IRON PROTEIN

DOMAIN 1: [Assigned by homology with 1NIPB]A 1 to A 283 ; The following residues NOT assigned to any domain: Chain "A" 1 - 287
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NRC B

PRELIMINARY 12-MAR-92 :: N-TERMINAL FRAGMENT (RESIDUES 1-95) OF A PROTEIN F

DOMAIN 1: [Assigned by homology with 1NRCA]B 6 to B 88 ; The following residues NOT assigned to any domain: Chain "B" 6 - 90
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FLV

ELECTRON TRANSPORT 02-JUL-92 :: FLAVODOXIN

DOMAIN 1: 2 to 169 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2FCR

ELECTRON TRANSPORT 03-FEB-92 :: FLAVODOXIN

DOMAIN 1: 1 to 173 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PHO

OUTER MEMBRANE PROTEIN 15-JAN-93 :: PHOSPHOPORIN (PHOE)

DOMAIN 1: 1 to 340 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BOC

CALCIUM-BINDING PROTEIN 23-APR-93 :: CALBINDIN D9K MUTANT WITH ALA 15 REPLACED BY ASP,

DOMAIN 1: 0 to 72 ; The following residues NOT assigned to any domain: Chain " " 73 - 75
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4ICB

CALCIUM-BINDING PROTEIN 27-AUG-91 :: CALBINDIN D9K (MINOR A FORM)

DOMAIN 1: 0 to 72 ; The following residues NOT assigned to any domain: Chain " " 73 - 75
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3ICB

CALCIUM-BINDING PROTEIN 09-SEP-86 :: CALCIUM-BINDING PROTEIN (VITAMIN D-DEPENDENT, MINO

DOMAIN 1: 1 to 72 ; The following residues NOT assigned to any domain: Chain " " 73 - 75
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2BCA

CALCIUM-BINDING PROTEIN 18-AUG-93 :: CALBINDIN D9K (CALCIUM-LOADED FORM) MUTANT WITH PR

DOMAIN 1: 1 to 72 ; The following residues NOT assigned to any domain: Chain " " 73 - 75
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2BCB

CALCIUM-BINDING PROTEIN 18-AUG-93 :: CALBINDIN D9K (CALCIUM-LOADED FORM) MUTANT WITH PR

DOMAIN 1: 1 to 72 ; The following residues NOT assigned to any domain: Chain " " 73 - 75
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CB1

CALCIUM-BINDING PROTEIN 13-DEC-91 :: CALBINDIN D9K (INTACT FORM) (NMR, 13 STRUCTURES)

DOMAIN 1: -2 to 72 ; The following residues NOT assigned to any domain: Chain " " 73 - 75
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BOD

CALCIUM-BINDING PROTEIN 23-APR-93 :: CALBINDIN D9K MUTANT WITH ALA 14 DELETED, ALA 15 R

DOMAIN 1: 0 to 72 ; The following residues NOT assigned to any domain: Chain " " 73 - 75
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TRC A

CALCIUM BINDING PROTEIN 18-JAN-90 :: CALMODULIN (/TR=2=C$ FRAGMENT COMPRISING RESIDUES

DOMAIN 1: A 80 to A 147 ; The following residues NOT assigned to any domain: Chain "A" 80 - 147
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PZA

ELECTRON TRANSFER(CUPROPROTEIN) 06-SEP-94 :: PSEUDOAZURIN (PH 7.8)

DOMAIN 1: 1 to 120 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PZB

ELECTRON TRANSFER(CUPROPROTEIN) 03-AUG-94 :: PSEUDOAZURIN (PH 4.4)

DOMAIN 1: 1 to 120 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PAZ

ELECTRON TRANSFER(CUPROPROTEIN) 06-SEP-88 :: PSEUDOAZURIN (CUPREDOXIN)

DOMAIN 1: 1 to 120 ; The following residues NOT assigned to any domain: Chain " " 121 - 123
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PMY

ELECTRON TRANSFER(CUPROPROTEIN) 28-JAN-94 :: PSEUDOAZURIN (CUPREDOXIN)

DOMAIN 1: 1 to 120 ; The following residues NOT assigned to any domain: Chain " " 121 - 123
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4CP4

OXIDOREDUCTASE(OXYGENASE) 04-JUN-91 :: CYTOCHROME P450CAM (CAMPHOR MONOOXYGENASE) (E.C.1.

DOMAIN 1: 10 to 413 ; The following residues NOT assigned to any domain: Chain " " 414 - 414
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4CPP

OXIDOREDUCTASE(OXYGENASE) 18-MAY-90 :: CYTOCHROME P450CAM (CAMPHOR MONOOXYGENASE) (E.C.1.

DOMAIN 1: 10 to 413 ; The following residues NOT assigned to any domain: Chain " " 414 - 414
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5CPP

OXIDOREDUCTASE(OXYGENASE) 18-MAY-90 :: CYTOCHROME P450CAM (CAMPHOR MONOOXYGENASE) (E.C.1.

DOMAIN 1: 10 to 413 ; The following residues NOT assigned to any domain: Chain " " 414 - 414
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6CPP

OXIDOREDUCTASE(OXYGENASE) 18-MAY-90 :: CYTOCHROME P450CAM (CAMPHOR MONOOXYGENASE) (E.C.1.

DOMAIN 1: 10 to 413 ; The following residues NOT assigned to any domain: Chain " " 414 - 414
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CPP

OXIDOREDUCTASE(OXYGENASE) 06-APR-87 :: CYTOCHROME P450CAM (CAMPHOR MONOOXYGENASE) (E.C.1.

DOMAIN 1: 10 to 413 ; The following residues NOT assigned to any domain: Chain " " 414 - 414
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CP4

OXIDOREDUCTASE(OXYGENASE) 04-JUN-91 :: CYTOCHROME P450=CAM= (CAMPHOR MONOOXYGENASE) (E.C.

DOMAIN 1: 10 to 413 ; The following residues NOT assigned to any domain: Chain " " 414 - 414
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3CP4

OXIDOREDUCTASE(OXYGENASE) 04-JUN-91 :: CYTOCHROME P450CAM (CAMPHOR MONOOXYGENASE) (E.C.1.

DOMAIN 1: 10 to 413 ; The following residues NOT assigned to any domain: Chain " " 414 - 414
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7CPP

OXIDOREDUCTASE(OXYGENASE) 18-MAY-90 :: CYTOCHROME P450CAM (CAMPHOR MONOOXYGENASE) (E.C.1.

DOMAIN 1: 10 to 413 ; The following residues NOT assigned to any domain: Chain " " 414 - 414
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3CPP

OXIDOREDUCTASE(OXYGENASE) 05-JUL-89 :: CYTOCHROME P450CAM (CAMPHOR MONOOXYGENASE) (E.C.1.

DOMAIN 1: 10 to 413 ; The following residues NOT assigned to any domain: Chain " " 414 - 414
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8CPP

OXIDOREDUCTASE(OXYGENASE) 18-MAY-90 :: CYTOCHROME P450CAM (CAMPHOR MONOOXYGENASE) (E.C.1.

DOMAIN 1: 10 to 413 ; The following residues NOT assigned to any domain: Chain " " 414 - 414
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PHA

OXIDOREDUCTASE(OXYGENASE) 27-JUL-92 :: CYTOCHROME P450-CAM (E.C.1.14.15.1) (CAMPHOR 5-MON

DOMAIN 1: 10 to 413 ; The following residues NOT assigned to any domain: Chain " " 414 - 414
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PHC

OXIDOREDUCTASE(OXYGENASE) 27-JUL-92 :: CYTOCHROME P450-CAM (E.C.1.14.15.1) (CAMPHOR 5-MON

DOMAIN 1: 10 to 413 ; The following residues NOT assigned to any domain: Chain " " 414 - 414
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PHD

OXIDOREDUCTASE(OXYGENASE) 27-JUL-92 :: CYTOCHROME P450-CAM (E.C.1.14.15.1) (CAMPHOR 5-MON

DOMAIN 1: 10 to 413 ; The following residues NOT assigned to any domain: Chain " " 414 - 414
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PHE

OXIDOREDUCTASE(OXYGENASE) 27-JUL-92 :: CYTOCHROME P450-CAM (E.C.1.14.15.1) (CAMPHOR 5-MON

DOMAIN 1: 10 to 413 ; The following residues NOT assigned to any domain: Chain " " 414 - 414
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PHF

OXIDOREDUCTASE(OXYGENASE) 27-JUL-92 :: CYTOCHROME P450-CAM (E.C.1.14.15.1) (CAMPHOR 5-MON

DOMAIN 1: 10 to 413 ; The following residues NOT assigned to any domain: Chain " " 414 - 414
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PHG

OXIDOREDUCTASE(OXYGENASE) 27-JUL-92 :: CYTOCHROME P450-CAM (E.C.1.14.15.1) (CAMPHOR 5-MON

DOMAIN 1: 10 to 413 ; The following residues NOT assigned to any domain: Chain " " 414 - 414
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CP4

OXIDOREDUCTASE(OXYGENASE) 04-JUN-91 :: CYTOCHROME P450CAM (CAMPHOR MONOOXYGENASE) (E.C.1.

DOMAIN 1: 10 to 413 ; The following residues NOT assigned to any domain: Chain " " 414 - 414
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CPT

OXIDOREDUCTASE(OXYGENASE) 23-NOV-93 :: CYTOCHROME P450-TERP

DOMAIN 1: 1 to 428 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1POB A

HYDROLASE 07-SEP-92 :: PHOSPHOLIPASE A2 (E.C.3.1.1.4) COMPLEX WITH THE

DOMAIN 1: A 1 to A 118 ; The following residues NOT assigned to any domain: Chain "A" 1 - 118
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1POB B

HYDROLASE 07-SEP-92 :: PHOSPHOLIPASE A2 (E.C.3.1.1.4) COMPLEX WITH THE

DOMAIN 1: B 1 to B 118 ; The following residues NOT assigned to any domain: Chain "B" 1 - 118
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PSH A

CARBOXYLIC ESTER HYDROLASE 28-JUL-92 :: PHOSPHOLIPASE A=2= (E.C.3.1.1.4) (PHOSPHATIDYLCHOL

DOMAIN 1: A 1 to A 118 ; The following residues NOT assigned to any domain: Chain "A" 119 - 119 The following residues NOT assigned to any domain: Chain "A" 1 - 119 The following residues NOT assigned to any domain: Chain "A" 1 - 119
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PSH B

CARBOXYLIC ESTER HYDROLASE 28-JUL-92 :: PHOSPHOLIPASE A=2= (E.C.3.1.1.4) (PHOSPHATIDYLCHOL

DOMAIN 1: B 1 to B 118 ; The following residues NOT assigned to any domain: Chain "B" 1 - 119 The following residues NOT assigned to any domain: Chain "B" 119 - 119 The following residues NOT assigned to any domain: Chain "B" 1 - 119
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PSH C

CARBOXYLIC ESTER HYDROLASE 28-JUL-92 :: PHOSPHOLIPASE A=2= (E.C.3.1.1.4) (PHOSPHATIDYLCHOL

DOMAIN 1: C 1 to C 118 ; The following residues NOT assigned to any domain: Chain "C" 1 - 119 The following residues NOT assigned to any domain: Chain "C" 1 - 119 The following residues NOT assigned to any domain: Chain "C" 119 - 119
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5P2P A

HYDROLASE(CARBOXYLIC ESTER) 01-SEP-90 :: PHOSPHOLIPASE A=2= (PHOSPHATIDE-2-ACYL-HYDROLASE)

DOMAIN 1: A 1 to A 124 ; The following residues NOT assigned to any domain: Chain "A" 1 - 124
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5P2P B

HYDROLASE(CARBOXYLIC ESTER) 01-SEP-90 :: PHOSPHOLIPASE A=2= (PHOSPHATIDE-2-ACYL-HYDROLASE)

DOMAIN 1: B 1 to B 124 ; The following residues NOT assigned to any domain: Chain "B" 1 - 124
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3P2P A

HYDROLASE(CARBOXYL ESTER) 29-NOV-89 :: PHOSPHOLIPASE A=2= (PHOSPHATIDE-2-ACYL-HYDROLASE)

DOMAIN 1: A 1 to A 124 ; The following residues NOT assigned to any domain: Chain "A" 1 - 124
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3P2P B

HYDROLASE(CARBOXYL ESTER) 29-NOV-89 :: PHOSPHOLIPASE A=2= (PHOSPHATIDE-2-ACYL-HYDROLASE)

DOMAIN 1: B 1 to B 124 ; The following residues NOT assigned to any domain: Chain "B" 1 - 124
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4P2P

CARBOXYLIC ESTER HYDROLASE 22-OCT-91 :: PHOSPHOLIPASE A=2= (PHOSPHATIDE-2-ACYL HYDROLASE)

DOMAIN 1: 1 to 124 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PHI A

HYDROLASE (CARBOXYLIC ESTER) 08-APR-93 :: PHOSPHOLIPASE A=2= (PHOSPHATIDE-2-ACYL-HYDROLASE)

DOMAIN 1: A 1 to A 124 ; The following residues NOT assigned to any domain: Chain "A" 1 - 124
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PHI B

HYDROLASE (CARBOXYLIC ESTER) 08-APR-93 :: PHOSPHOLIPASE A=2= (PHOSPHATIDE-2-ACYL-HYDROLASE)

DOMAIN 1: B 1 to B 124 ; The following residues NOT assigned to any domain: Chain "B" 1 - 124
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1P2P

CARBOXYLIC ESTER HYDROLASE 27-JUN-83 :: PHOSPHOLIPASE A=2= (E.C.3.1.1.4) (PHOSPHATIDE

DOMAIN 1: 1 to 124 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3BP2

CARBOXYLIC ESTER HYDROLASE 27-JUN-83 :: PHOSPHOLIPASE A=2= (E.C.3.1.1.4) (PHOSPHATIDE

DOMAIN 1: 2 to 123 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BP2

HYDROLASE 06-APR-81 :: PHOSPHOLIPASE A=2= (E.C.3.1.1.4) (PHOSPHATIDE

DOMAIN 1: 1 to 123 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BPQ

CARBOXYLIC ESTER HYDROLASE 28-OCT-91 :: PHOSPHOLIPASE A2 (E.C.3.1.1.4) MUTANT WITH LYS 56

DOMAIN 1: 1 to 123 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2BP2

HYDROLASE ZYMOGEN 05-JUN-81 :: PROPHOSPHOLIPASE A=2=

DOMAIN 1: 1 to 123 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2BPP

CARBOXYLIC ESTER HYDROLASE 17-JAN-92 :: PHOSPHOLIPASE A2 (E.C.3.1.1.4)

DOMAIN 1: 1 to 123 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4BP2

CARBOXYLIC ESTER HYDROLASE ZYMOGEN 07-SEP-90 :: PROPHOSPHOLIPASE A=2= (PHOSPHATIDE-2-ACYL HYDROLAS

DOMAIN 1: 1 to 123 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PP2 R

HYDROLASE 10-MAR-86 :: CALCIUM-FREE PHOSPHOLIPASE A=2= (E.C.3.1.1.4)

DOMAIN 1: R 1 to R 133 ; The following residues NOT assigned to any domain: Chain "R" 1 - 133
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PP2 L

HYDROLASE 10-MAR-86 :: CALCIUM-FREE PHOSPHOLIPASE A=2= (E.C.3.1.1.4)

DOMAIN 1: L 1 to L 133 ; The following residues NOT assigned to any domain: Chain "L" 1 - 133
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1POD

HYDROLASE 07-SEP-92 :: PHOSPHOLIPASE A2 (E.C.3.1.1.4)

DOMAIN 1: 1 to 124 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1POE A

HYDROLASE 07-SEP-92 :: PHOSPHOLIPASE A2 (E.C.3.1.1.4) COMPLEX WITH THE

DOMAIN 1: A 1 to A 124 ; The following residues NOT assigned to any domain: Chain "A" 1 - 124
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1POE B

HYDROLASE 07-SEP-92 :: PHOSPHOLIPASE A2 (E.C.3.1.1.4) COMPLEX WITH THE

DOMAIN 1: B 1 to B 124 ; The following residues NOT assigned to any domain: Chain "B" 1 - 124
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BBC

CARBOXYLIC ESTER HYDROLASE 04-MAY-92 :: PHOSPHOLIPASE A2 (PHOSPHATIDYLCHOLINE 2-ACYLHYDROL

DOMAIN 1: 1 to 132 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CLP A

HYDROLASE 12-SEP-94 :: MYOTOXIN II (PHOSPHOLIPASE A2) (E.C.3.1.1.4) MUTAN

DOMAIN 1: A 1 to A 133 ; The following residues NOT assigned to any domain: Chain "A" 1 - 133
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CLP B

HYDROLASE 12-SEP-94 :: MYOTOXIN II (PHOSPHOLIPASE A2) (E.C.3.1.1.4) MUTAN

DOMAIN 1: B 1 to B 133 ; The following residues NOT assigned to any domain: Chain "B" 1 - 133
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PPA

PRELIMINARY 29-OCT-91 :: PHOSPHOLIPASE A=2= LYS 49 VARIANT COMPLEX WITH

DOMAIN 1: 1 to 133 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PRC L

PHOTOSYNTHETIC REACTION CENTER 04-FEB-88 :: PHOTOSYNTHETIC REACTION CENTER

DOMAIN 1: [Assigned by homology with 1PRCM]L 1 to L 273 ; The following residues NOT assigned to any domain: Chain "L" 1 - 333 The following residues NOT assigned to any domain: Chain "L" 1 - 323 The following residues NOT assigned to any domain: Chain "L" 0 - 258
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2RCR L

PHOTOSYNTHETIC REACTION CENTER 04-FEB-91 :: PHOTOSYNTHETIC REACTION CENTER FROM

DOMAIN 1: [Assigned by homology with 1PRCM]L 1 to L 278 ; The following residues NOT assigned to any domain: Chain "L" 1 - 303 The following residues NOT assigned to any domain: Chain "L" 1 - 255
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PSS L

PHOTOSYNTHETIC REACTION CENTER 13-DEC-93 :: PHOTOSYNTHETIC REACTION CENTER (WILD-TYPE)

DOMAIN 1: [Assigned by homology with 1PRCM]L 5 to L 270 ; The following residues NOT assigned to any domain: Chain "L" 6 - 301 The following residues NOT assigned to any domain: Chain "L" 12 - 248
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PST L

PHOTOSYNTHETIC REACTION CENTER 13-DEC-93 :: PHOTOSYNTHETIC REACTION CENTER MUTANT WITH HIS M 2

DOMAIN 1: [Assigned by homology with 1PRCM]L 5 to L 270 ; The following residues NOT assigned to any domain: Chain "L" 6 - 301 The following residues NOT assigned to any domain: Chain "L" 12 - 248
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4RCR L

PHOTOSYNTHETIC REACTION CENTER 09-SEP-91 :: PHOTOSYNTHETIC REACTION CENTER

DOMAIN 1: [Assigned by homology with 1PRCM]L 5 to L 270 ; The following residues NOT assigned to any domain: Chain "L" 6 - 301 The following residues NOT assigned to any domain: Chain "L" 12 - 248
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PSS M

PHOTOSYNTHETIC REACTION CENTER 13-DEC-93 :: PHOTOSYNTHETIC REACTION CENTER (WILD-TYPE)

DOMAIN 1: [Assigned by homology with 1PRCM]M 6 to M 301 ; The following residues NOT assigned to any domain: Chain "M" 5 - 270 The following residues NOT assigned to any domain: Chain "M" 12 - 248
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4RCR M

PHOTOSYNTHETIC REACTION CENTER 09-SEP-91 :: PHOTOSYNTHETIC REACTION CENTER

DOMAIN 1: [Assigned by homology with 1PRCM]M 6 to M 301 ; The following residues NOT assigned to any domain: Chain "M" 5 - 270 The following residues NOT assigned to any domain: Chain "M" 12 - 248
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2RCR M

PHOTOSYNTHETIC REACTION CENTER 04-FEB-91 :: PHOTOSYNTHETIC REACTION CENTER FROM

DOMAIN 1: [Assigned by homology with 1PRCM]M 1 to M 303 ; The following residues NOT assigned to any domain: Chain "M" 1 - 278 The following residues NOT assigned to any domain: Chain "M" 1 - 255
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PST M

PHOTOSYNTHETIC REACTION CENTER 13-DEC-93 :: PHOTOSYNTHETIC REACTION CENTER MUTANT WITH HIS M 2

DOMAIN 1: [Assigned by homology with 1PRCM]M 6 to M 301 ; The following residues NOT assigned to any domain: Chain "M" 5 - 270 The following residues NOT assigned to any domain: Chain "M" 12 - 248
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2INT

CYTOKINE 22-JUL-93 :: INTERLEUKIN-4

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ITL

CYTOKINE 08-FEB-92 :: INTERLEUKIN 4 (IL-4) MUTANT WITH ADDITIONAL MET AT

DOMAIN 1: 0 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ITM

CYTOKINE 28-FEB-94 :: INTERLEUKIN 4 (IL-4) (NMR, MINIMIZED AVERAGE STRUC

DOMAIN 1: 0 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CYK

CYTOKINE 16-AUG-94 :: INTERLEUKIN 4 (NMR, MINIMIZED AVERAGE STRUCTURE)

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CYL

CYTOKINE 21-FEB-94 :: INTERLEUKIN 4 (NMR, 20 STRUCTURES)

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BBN

CYTOKINE 01-MAY-92 :: INTERLEUKIN 4 (NMR, MINIMIZED AVERAGE STRUCTURE)

DOMAIN 1: 1 to 132 ; The following residues NOT assigned to any domain: Chain " " 133 - 133
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BCN

CYTOKINE 01-MAY-92 :: INTERLEUKIN 4 (NMR, 22 STRUCTURES)

DOMAIN 1: 1 to 132 ; The following residues NOT assigned to any domain: Chain " " 133 - 133
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ITI

CYTOKINE 12-APR-93 :: INTERLEUKIN-4 MUTANT WITH FOUR ADDITIONAL RESIDUES

DOMAIN 1: 1 to 132 ; The following residues NOT assigned to any domain: Chain " " 133 - 133
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RVE B

PRELIMINARY 24-FEB-92 :: ECO RV ENDONUCLEASE (E.C.3.1.21.4)

DOMAIN 1: [Assigned by homology with 1RVEA]B 2 to B 245 ; The following residues NOT assigned to any domain: Chain "B" 2 - 245
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4RVE A

ENDONUCLEASE 18-FEB-93 :: ECO RV ENDONUCLEASE COMPLEX WITH DNA

DOMAIN 1: [Assigned by homology with 1RVEA]A 2 to A 241 ; The following residues NOT assigned to any domain: Chain "A" 2 - 241 The following residues NOT assigned to any domain: Chain "A" 2 - 241 The following residues NOT assigned to any domain: Chain "A" 1 - 10 The following residues NOT assigned to any domain: Chain "A" 1 - 10 The following residues NOT assigned to any domain: Chain "A" 1 - 10
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4RVE B

ENDONUCLEASE 18-FEB-93 :: ECO RV ENDONUCLEASE COMPLEX WITH DNA

DOMAIN 1: [Assigned by homology with 1RVEA]B 2 to B 241 ; The following residues NOT assigned to any domain: Chain "B" 2 - 241 The following residues NOT assigned to any domain: Chain "B" 2 - 241 The following residues NOT assigned to any domain: Chain "B" 1 - 10 The following residues NOT assigned to any domain: Chain "B" 1 - 10 The following residues NOT assigned to any domain: Chain "B" 1 - 10
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4RVE C

ENDONUCLEASE 18-FEB-93 :: ECO RV ENDONUCLEASE COMPLEX WITH DNA

DOMAIN 1: [Assigned by homology with 1RVEA]C 2 to C 241 ; The following residues NOT assigned to any domain: Chain "C" 2 - 241 The following residues NOT assigned to any domain: Chain "C" 2 - 241 The following residues NOT assigned to any domain: Chain "C" 1 - 10 The following residues NOT assigned to any domain: Chain "C" 1 - 10 The following residues NOT assigned to any domain: Chain "C" 1 - 10
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2RVE A

ENDONUCLEASE 19-MAR-91 :: ECO RV ENDONUCLEASE COMPLEX WITH DNA

DOMAIN 1: [Assigned by homology with 1RVEA]A 2 to A 240 ; The following residues NOT assigned to any domain: Chain "A" 2 - 241 The following residues NOT assigned to any domain: Chain "A" 1 - 8 The following residues NOT assigned to any domain: Chain "A" 1 - 8 The following residues NOT assigned to any domain: Chain "A" 1 - 8 The following residues NOT assigned to any domain: Chain "A" 1 - 8
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2RVE B

ENDONUCLEASE 19-MAR-91 :: ECO RV ENDONUCLEASE COMPLEX WITH DNA

DOMAIN 1: [Assigned by homology with 1RVEA]B 2 to B 241 ; The following residues NOT assigned to any domain: Chain "B" 2 - 240 The following residues NOT assigned to any domain: Chain "B" 1 - 8 The following residues NOT assigned to any domain: Chain "B" 1 - 8 The following residues NOT assigned to any domain: Chain "B" 1 - 8 The following residues NOT assigned to any domain: Chain "B" 1 - 8
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SHB A

PHOSPHOTRANSFERASE 18-AUG-92 :: V-SRC TYROSINE KINASE TRANSFORMING PROTEIN (PHOSPH

DOMAIN 1: [Assigned by homology with 1SHAA]A 2 to A 103 ; The following residues NOT assigned to any domain: Chain "A" 104 - 104 The following residues NOT assigned to any domain: Chain "A" 201 - 205
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SPR A

TRANSFERASE(PHOSPHOTRANSFERASE) 05-MAR-93 :: SRC-SH2 (SRC HOMOLOGY (SH2) DOMAIN) (PEPTIDE FREE

DOMAIN 1: [Assigned by homology with 1SHAA]A 2 to A 103 ; The following residues NOT assigned to any domain: Chain "A" 104 - 104 The following residues NOT assigned to any domain: Chain "A" 1 - 104 The following residues NOT assigned to any domain: Chain "A" 2 - 104 The following residues NOT assigned to any domain: Chain "A" 2 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SPR C

TRANSFERASE(PHOSPHOTRANSFERASE) 05-MAR-93 :: SRC-SH2 (SRC HOMOLOGY (SH2) DOMAIN) (PEPTIDE FREE

DOMAIN 1: [Assigned by homology with 1SHAA]C 2 to C 103 ; The following residues NOT assigned to any domain: Chain "C" 2 - 104 The following residues NOT assigned to any domain: Chain "C" 1 - 104 The following residues NOT assigned to any domain: Chain "C" 104 - 104 The following residues NOT assigned to any domain: Chain "C" 2 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SPR D

TRANSFERASE(PHOSPHOTRANSFERASE) 05-MAR-93 :: SRC-SH2 (SRC HOMOLOGY (SH2) DOMAIN) (PEPTIDE FREE

DOMAIN 1: [Assigned by homology with 1SHAA]D 2 to D 103 ; The following residues NOT assigned to any domain: Chain "D" 2 - 104 The following residues NOT assigned to any domain: Chain "D" 1 - 104 The following residues NOT assigned to any domain: Chain "D" 2 - 104 The following residues NOT assigned to any domain: Chain "D" 104 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SPS A

TRANSFERASE(PHOSPHOTRANSFERASE) 05-MAR-93 :: SRC-SH2 (SRC HOMOLOGY (SH2) DOMAIN) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 1SHAA]A 2 to A 103 ; The following residues NOT assigned to any domain: Chain "A" 104 - 104 The following residues NOT assigned to any domain: Chain "A" -2 - 4 The following residues NOT assigned to any domain: Chain "A" 2 - 104 The following residues NOT assigned to any domain: Chain "A" -2 - 3 The following residues NOT assigned to any domain: Chain "A" 2 - 104 The following residues NOT assigned to any domain: Chain "A" -2 - 7
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SPS B

TRANSFERASE(PHOSPHOTRANSFERASE) 05-MAR-93 :: SRC-SH2 (SRC HOMOLOGY (SH2) DOMAIN) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 1SHAA]B 2 to B 103 ; The following residues NOT assigned to any domain: Chain "B" 2 - 104 The following residues NOT assigned to any domain: Chain "B" -2 - 4 The following residues NOT assigned to any domain: Chain "B" 104 - 104 The following residues NOT assigned to any domain: Chain "B" -2 - 3 The following residues NOT assigned to any domain: Chain "B" 2 - 104 The following residues NOT assigned to any domain: Chain "B" -2 - 7
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SPS C

TRANSFERASE(PHOSPHOTRANSFERASE) 05-MAR-93 :: SRC-SH2 (SRC HOMOLOGY (SH2) DOMAIN) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 1SHAA]C 2 to C 103 ; The following residues NOT assigned to any domain: Chain "C" 2 - 104 The following residues NOT assigned to any domain: Chain "C" -2 - 4 The following residues NOT assigned to any domain: Chain "C" 2 - 104 The following residues NOT assigned to any domain: Chain "C" -2 - 3 The following residues NOT assigned to any domain: Chain "C" 104 - 104 The following residues NOT assigned to any domain: Chain "C" -2 - 7
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SPR B

TRANSFERASE(PHOSPHOTRANSFERASE) 05-MAR-93 :: SRC-SH2 (SRC HOMOLOGY (SH2) DOMAIN) (PEPTIDE FREE

DOMAIN 1: [Assigned by homology with 1SHAA]B 1 to B 103 ; The following residues NOT assigned to any domain: Chain "B" 2 - 104 The following residues NOT assigned to any domain: Chain "B" 104 - 104 The following residues NOT assigned to any domain: Chain "B" 2 - 104 The following residues NOT assigned to any domain: Chain "B" 2 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SHF B

PHOSPHOTRANSFERASE 19-MAY-93 :: FYN PROTO-ONCOGENE TYROSINE KINASE (E.C.2.7.1.112)

DOMAIN 1: [Assigned by homology with 1SHFA]B 84 to B 142 ; The following residues NOT assigned to any domain: Chain "B" 84 - 142
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SRL

PHOSPHOTRANSFERASE 07-MAR-94 :: SRC TYROSINE KINASE TRANSFORMING PROTEIN (SH3 DOMA

DOMAIN 1: [Assigned by homology with 1SHFA] 9 to 64 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SRM

PHOSPHOTRANSFERASE 07-MAR-94 :: SRC TYROSINE KINASE TRANSFORMING PROTEIN (SH3 DOMA

DOMAIN 1: [Assigned by homology with 1SHFA] 9 to 64 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LYA A

LYSOSOMAL ASPARTIC PROTEASE 22-APR-93 :: CATHEPSIN D (E.C.3.4.23.5)

DOMAIN 1: [Assigned by homology with 1SMRA]A 2 to A 97 ; The following residues NOT assigned to any domain: Chain " " 1 - 97 The following residues NOT assigned to any domain: Chain " " 106 - 346 The following residues NOT assigned to any domain: Chain " " 1 - 97 The following residues NOT assigned to any domain: Chain " " 106 - 346
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LYA C

LYSOSOMAL ASPARTIC PROTEASE 22-APR-93 :: CATHEPSIN D (E.C.3.4.23.5)

DOMAIN 1: [Assigned by homology with 1SMRA]C 2 to C 97 ; The following residues NOT assigned to any domain: Chain " " 1 - 97 The following residues NOT assigned to any domain: Chain " " 106 - 346 The following residues NOT assigned to any domain: Chain " " 1 - 97 The following residues NOT assigned to any domain: Chain " " 106 - 346
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LYB A

LYSOSOMAL ASPARTIC PROTEASE 22-APR-93 :: CATHEPSIN D COMPLEX WITH PEPSTATIN A

DOMAIN 1: [Assigned by homology with 1SMRA]A 2 to A 97 ; The following residues NOT assigned to any domain: Chain " " 1 - 97 The following residues NOT assigned to any domain: Chain " " 106 - 346 The following residues NOT assigned to any domain: Chain " " 2 - 5 The following residues NOT assigned to any domain: Chain " " 1 - 97 The following residues NOT assigned to any domain: Chain " " 106 - 346 The following residues NOT assigned to any domain: Chain " " 12 - 15
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LYB C

LYSOSOMAL ASPARTIC PROTEASE 22-APR-93 :: CATHEPSIN D COMPLEX WITH PEPSTATIN A

DOMAIN 1: [Assigned by homology with 1SMRA]C 2 to C 97 ; The following residues NOT assigned to any domain: Chain " " 1 - 97 The following residues NOT assigned to any domain: Chain " " 106 - 346 The following residues NOT assigned to any domain: Chain " " 2 - 5 The following residues NOT assigned to any domain: Chain " " 1 - 97 The following residues NOT assigned to any domain: Chain " " 106 - 346 The following residues NOT assigned to any domain: Chain " " 12 - 15
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ENA

HYDROLASE(PHOSPHORIC DIESTER) 14-FEB-94 :: STAPHYLOCOCCAL NUCLEASE (E.C.3.1.31.1) MUTATION WI

DOMAIN 1: 7 to 140 ; The following residues NOT assigned to any domain: Chain " " 141 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ENC

HYDROLASE(PHOSPHORIC DIESTER) 14-FEB-94 :: STAPHYLOCOCCAL NUCLEASE (E.C.3.1.31.1) MUTANT WITH

DOMAIN 1: 7 to 140 ; The following residues NOT assigned to any domain: Chain " " 141 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2ENB

HYDROLASE(PHOSPHORIC DIESTER) 23-MAR-94 :: STAPHYLOCOCCAL NUCLEASE (E.C.3.1.31.1) MUTATION WI

DOMAIN 1: 7 to 140 ; The following residues NOT assigned to any domain: Chain " " 141 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1STN

HYDROLASE(PHOSPHORIC DIESTER) 17-FEB-93 :: STAPHYLOCOCCAL NUCLEASE (E.C.3.1.31.1)

DOMAIN 1: 6 to 140 ; The following residues NOT assigned to any domain: Chain " " 141 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SNM

HYDROLASE (PHOSPHORIC DIESTER) 15-FEB-90 :: STAPHYLOCOCCAL NUCLEASE (E.C.3.1.31.1) MUTANT (GLU

DOMAIN 1: 7 to 140 ; The following residues NOT assigned to any domain: Chain " " 141 - 142
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2SNS

HYDROLASE (PHOSPHORIC DIESTER) 14-MAY-82 :: STAPHYLOCOCCAL NUCLEASE (E.C.3.1.33.1) COMPLEX WIT

DOMAIN 1: 1 to 140 ; The following residues NOT assigned to any domain: Chain " " 141 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SYG

HYDROLASE(PHOSPHORIC DIESTER) 07-JAN-94 :: STAPHYLOCOCCAL NUCLEASE (E.C.3.1.31.1) MUTANT WITH

DOMAIN 1: 6 to 140 ; The following residues NOT assigned to any domain: Chain " " 141 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1KAA

HYDROLASE(PHOSPHORIC DIESTER) 18-DEC-92 :: STAPHYLOCOCCAL NUCLEASE (E.C.3.1.33.1) MUTANT WITH

DOMAIN 1: 6 to 140 ; The following residues NOT assigned to any domain: Chain " " 141 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SYE

HYDROLASE(PHOSPHORIC DIESTER) 07-JAN-94 :: STAPHYLOCOCCAL NUCLEASE (E.C.3.1.31.1) MUTANT WITH

DOMAIN 1: 6 to 140 ; The following residues NOT assigned to any domain: Chain " " 141 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SYF

HYDROLASE(PHOSPHORIC DIESTER) 07-JAN-94 :: STAPHYLOCOCCAL NUCLEASE (E.C.3.1.31.1) MUTANT WITH

DOMAIN 1: 6 to 140 ; The following residues NOT assigned to any domain: Chain " " 141 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1KAB

HYDROLASE(PHOSPHORIC DIESTER) 18-DEC-92 :: STAPHYLOCOCCAL NUCLEASE (E.C.3.1.33.1) MUTANT WITH

DOMAIN 1: 6 to 140 ; The following residues NOT assigned to any domain: Chain " " 141 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SYC

HYDROLASE(PHOSPHORIC DIESTER) 07-JAN-94 :: STAPHYLOCOCCAL NUCLEASE (E.C.3.1.31.1) MUTANT WITH

DOMAIN 1: 6 to 140 ; The following residues NOT assigned to any domain: Chain " " 141 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SYD

HYDROLASE(PHOSPHORIC DIESTER) 07-JAN-94 :: STAPHYLOCOCCAL NUCLEASE (E.C.3.1.31.1) MUTANT WITH

DOMAIN 1: 6 to 140 ; The following residues NOT assigned to any domain: Chain " " 141 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2SNM

HYDROLASE (PHOSPHORIC DIESTER) 03-APR-91 :: STAPHYLOCOCCAL NUCLEASE (E.C.3.1.31.1) MUTANT WITH

DOMAIN 1: 7 to 140 ; The following residues NOT assigned to any domain: Chain " " 141 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1STA

HYDROLASE(PHOSPHORIC DIESTER) 17-JAN-94 :: STAPHYLOCOCCAL NUCLEASE (E.C.3.1.31.1) DOUBLE INSE

DOMAIN 1: 7 to 140 ; The following residues NOT assigned to any domain: Chain " " 141 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1STY

HYDROLASE (PHOSPHORIC DIESTER) 18-FEB-93 :: STAPHYLOCOCCAL NUCLEASE (E.C.3.1.31.1) INSERTION M

DOMAIN 1: 6 to 140 ; The following residues NOT assigned to any domain: Chain " " 141 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SYB

HYDROLASE(PHOSPHORIC DIESTER) 07-JAN-94 :: STAPHYLOCOCCAL NUCLEASE (E.C.3.1.31.1) WITH RESIDU

DOMAIN 1: 6 to 140 ; The following residues NOT assigned to any domain: Chain " " 141 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1STB

HYDROLASE(PHOSPHORIC DIESTER) 17-JAN-94 :: STAPHYLOCOCCAL NUCLEASE (E.C.3.1.31.1) INSERTION M

DOMAIN 1: 6 to 140 ; The following residues NOT assigned to any domain: Chain " " 141 - 141
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BBI

SERINE PROTEASE INHIBITOR 19-SEP-91 :: TRYPSIN/CHYMOTRYPSIN BOWMAN-BIRK INHIBITOR (NMR, M

DOMAIN 1: [Assigned by homology with 1TABI] 1 to 62 ; The following residues NOT assigned to any domain: Chain " " 63 - 71
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2BBI

SERINE PROTEASE INHIBITOR 19-SEP-91 :: TRYPSIN/CHYMOTRYPSIN BOWMAN-BIRK INHIBITOR (NMR,

DOMAIN 1: [Assigned by homology with 1TABI] 1 to 62 ; The following residues NOT assigned to any domain: Chain " " 63 - 71
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PI2

SERINE PROTEINASE INHIBITOR 26-MAR-91 :: BOWMAN-*BIRK PROTEINASE INHIBITOR /PI-II$

DOMAIN 1: [Assigned by homology with 1TABI] 3 to 60 ; The following residues NOT assigned to any domain: Chain " " 61 - 63
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2TGI

GROWTH FACTOR 20-OCT-93 :: TRANSFORMING GROWTH FACTOR-BETA TWO (TGF-B2)

DOMAIN 1: 1 to 112 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PCE

PROTEINASE INHIBITOR(KAZAL TYPE) 22-FEB-94 :: PEC-60 (PEPTIDE WITH N-TERMINAL GLUTAMIC ACID, C-T

DOMAIN 1: [Assigned by homology with 1TGSI] 1 to 59 ; The following residues NOT assigned to any domain: Chain " " 60 - 60
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CGJ I

SERINE PROTEASE/INHIBITOR COMPLEX 08-OCT-91 :: ALPHA-CHYMOTRYPSINOGEN COMPLEX WITH HUMAN PANCREAT

DOMAIN 1: [Assigned by homology with 1TGSI]I 1 to I 55 ; The following residues NOT assigned to any domain: Chain "I" 1 - 245 The following residues NOT assigned to any domain: Chain "I" 56 - 56
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HPT

SERINE PROTEASE INHIBITOR 27-MAR-92 :: HUMAN PANCREATIC SECRETORY TRYPSIN INHIBITOR VARIA

DOMAIN 1: [Assigned by homology with 1TGSI] 1 to 55 ; The following residues NOT assigned to any domain: Chain " " 56 - 56
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CGI I

SERINE PROTEASE/INHIBITOR COMPLEX 08-OCT-91 :: ALPHA-CHYMOTRYPSINOGEN COMPLEX WITH HUMAN PANCREAT

DOMAIN 1: [Assigned by homology with 1TGSI]I 1 to I 55 ; The following residues NOT assigned to any domain: Chain "I" 1 - 245 The following residues NOT assigned to any domain: Chain "I" 56 - 56
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2TUN A

LYMPHOKINE 06-OCT-93 :: TUMOR NECROSIS FACTOR-ALPHA (CACHECTIN) MUTANT WIT

DOMAIN 1: [Assigned by homology with 1TNFA]A 7 to A 157 ; The following residues NOT assigned to any domain: Chain "A" 7 - 157 The following residues NOT assigned to any domain: Chain "A" 7 - 157 The following residues NOT assigned to any domain: Chain "A" 7 - 157 The following residues NOT assigned to any domain: Chain "A" 7 - 157 The following residues NOT assigned to any domain: Chain "A" 7 - 157
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2TUN B

LYMPHOKINE 06-OCT-93 :: TUMOR NECROSIS FACTOR-ALPHA (CACHECTIN) MUTANT WIT

DOMAIN 1: [Assigned by homology with 1TNFA]B 7 to B 157 ; The following residues NOT assigned to any domain: Chain "B" 7 - 157 The following residues NOT assigned to any domain: Chain "B" 7 - 157 The following residues NOT assigned to any domain: Chain "B" 7 - 157 The following residues NOT assigned to any domain: Chain "B" 7 - 157 The following residues NOT assigned to any domain: Chain "B" 7 - 157
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2TUN C

LYMPHOKINE 06-OCT-93 :: TUMOR NECROSIS FACTOR-ALPHA (CACHECTIN) MUTANT WIT

DOMAIN 1: [Assigned by homology with 1TNFA]C 7 to C 157 ; The following residues NOT assigned to any domain: Chain "C" 7 - 157 The following residues NOT assigned to any domain: Chain "C" 7 - 157 The following residues NOT assigned to any domain: Chain "C" 7 - 157 The following residues NOT assigned to any domain: Chain "C" 7 - 157 The following residues NOT assigned to any domain: Chain "C" 7 - 157
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2TUN D

LYMPHOKINE 06-OCT-93 :: TUMOR NECROSIS FACTOR-ALPHA (CACHECTIN) MUTANT WIT

DOMAIN 1: [Assigned by homology with 1TNFA]D 7 to D 157 ; The following residues NOT assigned to any domain: Chain "D" 7 - 157 The following residues NOT assigned to any domain: Chain "D" 7 - 157 The following residues NOT assigned to any domain: Chain "D" 7 - 157 The following residues NOT assigned to any domain: Chain "D" 7 - 157 The following residues NOT assigned to any domain: Chain "D" 7 - 157
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2TUN E

LYMPHOKINE 06-OCT-93 :: TUMOR NECROSIS FACTOR-ALPHA (CACHECTIN) MUTANT WIT

DOMAIN 1: [Assigned by homology with 1TNFA]E 7 to E 157 ; The following residues NOT assigned to any domain: Chain "E" 7 - 157 The following residues NOT assigned to any domain: Chain "E" 7 - 157 The following residues NOT assigned to any domain: Chain "E" 7 - 157 The following residues NOT assigned to any domain: Chain "E" 7 - 157 The following residues NOT assigned to any domain: Chain "E" 7 - 157
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2TUN F

LYMPHOKINE 06-OCT-93 :: TUMOR NECROSIS FACTOR-ALPHA (CACHECTIN) MUTANT WIT

DOMAIN 1: [Assigned by homology with 1TNFA]F 7 to F 157 ; The following residues NOT assigned to any domain: Chain "F" 7 - 157 The following residues NOT assigned to any domain: Chain "F" 7 - 157 The following residues NOT assigned to any domain: Chain "F" 7 - 157 The following residues NOT assigned to any domain: Chain "F" 7 - 157 The following residues NOT assigned to any domain: Chain "F" 7 - 157
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TNF B

LYMPHOKINE 25-AUG-89 :: TUMOR NECROSIS FACTOR-ALPHA (CACHECTIN)

DOMAIN 1: [Assigned by homology with 1TNFA]B 6 to B 157 ; The following residues NOT assigned to any domain: Chain "B" 6 - 157 The following residues NOT assigned to any domain: Chain "B" 6 - 157
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TNF C

LYMPHOKINE 25-AUG-89 :: TUMOR NECROSIS FACTOR-ALPHA (CACHECTIN)

DOMAIN 1: [Assigned by homology with 1TNFA]C 6 to C 157 ; The following residues NOT assigned to any domain: Chain "C" 6 - 157 The following residues NOT assigned to any domain: Chain "C" 6 - 157
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TNR A

COMPLEX(LYMPHOKINE/RECEPTOR) 09-MAY-94 :: TUMOR NECROSIS FACTOR RECEPTOR P55 (EXTRACELLULAR

DOMAIN 1: [Assigned by homology with 1TNFA]A 28 to A 171 ; The following residues NOT assigned to any domain: Chain "A" 15 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TTA A

TRANSPORT(THYROXINE) 02-NOV-92 :: TRANSTHYRETIN (FORMERLY PREALBUMIN)

DOMAIN 1: [Assigned by homology with 1TTBA]A 1 to A 127 ; The following residues NOT assigned to any domain: Chain "A" 1 - 127
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TTA B

TRANSPORT(THYROXINE) 02-NOV-92 :: TRANSTHYRETIN (FORMERLY PREALBUMIN)

DOMAIN 1: [Assigned by homology with 1TTBA]B 1 to B 127 ; The following residues NOT assigned to any domain: Chain "B" 1 - 127
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TTB B

TRANSPORT(THYROXINE) 02-NOV-92 :: TRANSTHYRETIN (FORMERLY PREALBUMIN) MUTANT WITH AL

DOMAIN 1: [Assigned by homology with 1TTBA]B 1 to B 127 ; The following residues NOT assigned to any domain: Chain "B" 1 - 127
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TTC A

TRANSPORT(THYROXINE) 02-NOV-92 :: TRANSTHYRETIN (FORMERLY PREALBUMIN) MUTANT WITH VA

DOMAIN 1: [Assigned by homology with 1TTBA]A 1 to A 127 ; The following residues NOT assigned to any domain: Chain "A" 1 - 127
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TTC B

TRANSPORT(THYROXINE) 02-NOV-92 :: TRANSTHYRETIN (FORMERLY PREALBUMIN) MUTANT WITH VA

DOMAIN 1: [Assigned by homology with 1TTBA]B 1 to B 127 ; The following residues NOT assigned to any domain: Chain "B" 1 - 127
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TLM A

TRANSPORT (THYROXINE,RETINOL) 22-DEC-92 :: TRANSTHYRETIN (ALSO CALLED PREALBUMIN) COMPLEX WIT

DOMAIN 1: [Assigned by homology with 1TTBA]A 5 to A 127 ; The following residues NOT assigned to any domain: Chain "A" 8 - 127
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TLM B

TRANSPORT (THYROXINE,RETINOL) 22-DEC-92 :: TRANSTHYRETIN (ALSO CALLED PREALBUMIN) COMPLEX WIT

DOMAIN 1: [Assigned by homology with 1TTBA]B 8 to B 127 ; The following residues NOT assigned to any domain: Chain "B" 5 - 127
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1THA A

PRELIMINARY 21-NOV-91 :: TRANSTHYRETIN - 3,3'-DIIODO-L-THYRONINE COMPLEX

DOMAIN 1: [Assigned by homology with 1TTBA]A 10 to A 127 ; The following residues NOT assigned to any domain: Chain "A" 10 - 125
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1THC A

TRANSPORT (THYROXINE,RETINOL) IN SERUM 20-APR-92 :: TRANSTHYRETIN (ALSO CALLED PREALBUMIN) COMPLEX WIT

DOMAIN 1: [Assigned by homology with 1TTBA]A 9 to A 126 ; The following residues NOT assigned to any domain: Chain "A" 10 - 124
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1THA B

PRELIMINARY 21-NOV-91 :: TRANSTHYRETIN - 3,3'-DIIODO-L-THYRONINE COMPLEX

DOMAIN 1: [Assigned by homology with 1TTBA]B 10 to B 125 ; The following residues NOT assigned to any domain: Chain "B" 10 - 127
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1THC B

TRANSPORT (THYROXINE,RETINOL) IN SERUM 20-APR-92 :: TRANSTHYRETIN (ALSO CALLED PREALBUMIN) COMPLEX WIT

DOMAIN 1: [Assigned by homology with 1TTBA]B 10 to B 124 ; The following residues NOT assigned to any domain: Chain "B" 9 - 126
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PAB A

TRANSPORT (THYROXINE,RETINOL) IN SERUM 16-SEP-77 :: PREALBUMIN (HUMAN PLASMA)

DOMAIN 1: [Assigned by homology with 1TTBA]A 10 to A 123 ; The following residues NOT assigned to any domain: Chain "A" 10 - 123
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PAB B

TRANSPORT (THYROXINE,RETINOL) IN SERUM 16-SEP-77 :: PREALBUMIN (HUMAN PLASMA)

DOMAIN 1: [Assigned by homology with 1TTBA]B 10 to B 123 ; The following residues NOT assigned to any domain: Chain "B" 10 - 123
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ULB

PENTOSYLTRANSFERASE 05-NOV-91 :: PURINE NUCLEOSIDE PHOSPHORYLASE (E.C.2.4.2.1) COMP

DOMAIN 1: 1 to 289 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2UTG A

STEROID BINDING 17-MAY-89 :: UTEROGLOBIN

DOMAIN 1: A 1 to A 69 ; The following residues NOT assigned to any domain: Chain "A" 70 - 70 The following residues NOT assigned to any domain: Chain "A" 1 - 70
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2UTG B

STEROID BINDING 17-MAY-89 :: UTEROGLOBIN

DOMAIN 1: B 1 to B 69 ; The following residues NOT assigned to any domain: Chain "B" 1 - 70 The following residues NOT assigned to any domain: Chain "B" 70 - 70
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CCD

PRELIMINARY 17-SEP-91 :: CLARA CELL 17 KDA PROTEIN

DOMAIN 1: -2 to 69 ; The following residues NOT assigned to any domain: Chain " " 70 - 75
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAP

ELECTRON TRANSPORT 25-AUG-92 :: REP A2 ISO-1-CYTOCHROME C (REDUCED STATE) MUTANT W

DOMAIN 1: -5 to 102 ; The following residues NOT assigned to any domain: Chain " " 103 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAQ

ELECTRON TRANSPORT 25-AUG-92 :: REP A2 ISO-1-CYTOCHROME C (REDUCED STATE) MUTANT W

DOMAIN 1: -5 to 102 ; The following residues NOT assigned to any domain: Chain " " 103 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PCC B

OXIDOREDUCTASE/ELECTRON TRANSPORT 14-APR-93 :: YEAST CYTOCHROME C PEROXIDASE (CCP) COMPLEX WITH

DOMAIN 1: B -5 to B 102 ; The following residues NOT assigned to any domain: Chain "B" 1 - 294 The following residues NOT assigned to any domain: Chain "B" 103 - 103 The following residues NOT assigned to any domain: Chain "B" 1 - 294 The following residues NOT assigned to any domain: Chain "B" -5 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PCC D

OXIDOREDUCTASE/ELECTRON TRANSPORT 14-APR-93 :: YEAST CYTOCHROME C PEROXIDASE (CCP) COMPLEX WITH

DOMAIN 1: D -5 to D 102 ; The following residues NOT assigned to any domain: Chain "D" 1 - 294 The following residues NOT assigned to any domain: Chain "D" -5 - 103 The following residues NOT assigned to any domain: Chain "D" 1 - 294 The following residues NOT assigned to any domain: Chain "D" 103 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CRH

ELECTRON TRANSPORT(CYTOCHROME) 06-AUG-93 :: CYTOCHROME C (ISOZYME 1) (REDUCED) MUTANT WITH ASN

DOMAIN 1: -5 to 102 ; The following residues NOT assigned to any domain: Chain " " 103 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2YCC

ELECTRON TRANSPORT (HEME PROTEIN) 29-JAN-91 :: CYTOCHROME $C (ISOZYME 1) (OXIDIZED) (MUTANT WITH

DOMAIN 1: -5 to 102 ; The following residues NOT assigned to any domain: Chain " " 103 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CHH

ELECTRON TRANSPORT(HEME PROTEIN) 01-JUN-94 :: CYTOCHROME C (ISOZYME 1) (REDUCED) MUTANT WITH PHE

DOMAIN 1: -5 to 102 ; The following residues NOT assigned to any domain: Chain " " 103 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CTY

ELECTRON TRANSPORT (HEME PROTEIN) 15-FEB-93 :: CYTOCHROME $C (ISOZYME 1) (OXIDIZED) MUTANT WITH T

DOMAIN 1: -5 to 102 ; The following residues NOT assigned to any domain: Chain " " 103 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CTZ

ELECTRON TRANSPORT (HEME PROTEIN) 15-FEB-93 :: CYTOCHROME $C (ISOZYME 1) (REDUCED) MUTANT WITH TY

DOMAIN 1: -5 to 102 ; The following residues NOT assigned to any domain: Chain " " 103 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CRG

ELECTRON TRANSPORT(HEME PROTEIN) 06-AUG-93 :: CYTOCHROME C (ISOZYME 1) (OXIDIZED) MUTANT WITH AS

DOMAIN 1: -5 to 102 ; The following residues NOT assigned to any domain: Chain " " 103 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CHJ

ELECTRON TRANSPORT(HEME PROTEIN) 01-JUN-94 :: CYTOCHROME C (ISOZYME 1) (REDUCED) MUTANT WITH LEU

DOMAIN 1: -5 to 102 ; The following residues NOT assigned to any domain: Chain " " 103 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CRI

ELECTRON TRANSPORT(CYTOCHROME) 06-AUG-93 :: CYTOCHROME C (ISOZYME 1) (OXIDIZED) MUTANT WITH AS

DOMAIN 1: -5 to 102 ; The following residues NOT assigned to any domain: Chain " " 103 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CRJ

ELECTRON TRANSPORT(CYTOCHROME) 06-AUG-93 :: CYTOCHROME C (ISOZYME 1) (REDUCED) MUTANT WITH ASN

DOMAIN 1: -5 to 102 ; The following residues NOT assigned to any domain: Chain " " 103 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CHI

ELECTRON TRANSPORT(HEME PROTEIN) 01-JUN-94 :: CYTOCHROME C (ISOZYME 1) (REDUCED) MUTANT WITH PHE

DOMAIN 1: -5 to 102 ; The following residues NOT assigned to any domain: Chain " " 103 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1YEB

ELECTRON TRANSPORT 29-OCT-91 :: CYTOCHROME C (B-2036 COMPOSITE, REDUCED STATE)

DOMAIN 1: -5 to 102 ; The following residues NOT assigned to any domain: Chain " " 103 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1YEA

ELECTRON TRANSPORT 29-OCT-91 :: CYTOCHROME C (ISO-2, REDUCED STATE)

DOMAIN 1: -9 to 102 ; The following residues NOT assigned to any domain: Chain " " 103 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CCR

ELECTRON TRANSPORT(CYTOCHROME) 14-MAR-83 :: CYTOCHROME $C

DOMAIN 1: 1 to 110 ; The following residues NOT assigned to any domain: Chain " " 0 - 0 Chain " " 111 - 111
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PCB B

OXIDOREDUCTASE/ELECTRON TRANSPORT 14-APR-93 :: YEAST CYTOCHROME C PEROXIDASE (CCP) COMPLEX WITH H

DOMAIN 1: B 1 to B 102 ; The following residues NOT assigned to any domain: Chain "B" 1 - 294 The following residues NOT assigned to any domain: Chain "B" 103 - 104 The following residues NOT assigned to any domain: Chain "B" 1 - 294
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HRC

ELECTRON TRANSPORT(CYTOCHROME) 16-AUG-94 :: CYTOCHROME C

DOMAIN 1: 1 to 102 ; The following residues NOT assigned to any domain: Chain " " 0 - 0 Chain " " 103 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FRC

ELECTRON TRANSPORT(CYTOCHROME) 29-MAR-94 :: CYTOCHROME C (REDUCED) (NMR, AVERAGE STRUCTURE)

DOMAIN 1: 1 to 102 ; The following residues NOT assigned to any domain: Chain " " 103 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CYC

ELECTRON TRANSPORT 01-AUG-76 :: FERROCYTOCHROME $C

DOMAIN 1: 1 to 102 ; The following residues NOT assigned to any domain: Chain " " 103 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5CYT R

ELECTRON TRANSPORT (HEME PROTEIN) 14-JAN-88 :: CYTOCHROME $C (REDUCED)

DOMAIN 1: R 1 to R 102 ; The following residues NOT assigned to any domain: Chain "R" 0 - 0 Chain "R" 103 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3CYT O

ELECTRON TRANSPORT (HEME PROTEIN) 01-JUL-80 :: CYTOCHROME $C (OXIDIZED)

DOMAIN 1: O 1 to O 102 ; The following residues NOT assigned to any domain: Chain "O" 0 - 0 Chain "O" 103 - 103 The following residues NOT assigned to any domain: Chain "O" 0 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3CYT I

ELECTRON TRANSPORT (HEME PROTEIN) 01-JUL-80 :: CYTOCHROME $C (OXIDIZED)

DOMAIN 1: I 1 to I 102 ; The following residues NOT assigned to any domain: Chain "I" 0 - 103 The following residues NOT assigned to any domain: Chain "I" 0 - 0 Chain "I" 103 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CRY

ELECTRON TRANSPORT(HEME PROTEIN) 27-DEC-93 :: CYTOCHROME C2

DOMAIN 1: 1 to 101 ; The following residues NOT assigned to any domain: Chain " " 102 - 107
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2C2C

ELECTRON TRANSPORT PROTEIN (CYTOCHROME) 03-NOV-83 :: CYTOCHROME $C=2= (OXIDIZED)

DOMAIN 1: 1 to 112 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3C2C

ELECTRON TRANSPORT PROTEIN (CYTOCHROME) 03-NOV-83 :: CYTOCHROME $C=2= (REDUCED)

DOMAIN 1: 1 to 112 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

155C

ELECTRON TRANSPORT 01-AUG-76 :: CYTOCHROME C550

DOMAIN 1: 1 to 118 ; The following residues NOT assigned to any domain: Chain " " 0 - 0 Chain " " 119 - 134
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1COT

ELECTRON TRANSPORT 06-JUL-94 :: CYTOCHROME C=2= (FORMERLY CYTOCHROME C=550=)

DOMAIN 1: 2 to 119 ; The following residues NOT assigned to any domain: Chain " " 120 - 122
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2AVI B

BIOTIN BINDING PROTEIN 23-APR-93 :: AVIDIN COMPLEX WITH BIOTIN

DOMAIN 1: [Assigned by homology with 2AVIA]B 3 to B 122 ; The following residues NOT assigned to any domain: Chain "B" 3 - 123 The following residues NOT assigned to any domain: Chain "B" 123 - 123
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AVD A

BIOTIN-BINDING PROTEIN 05-MAR-93 :: AVIDIN COMPLEX WITH BIOTIN

DOMAIN 1: [Assigned by homology with 2AVIA]A 3 to A 122 ; The following residues NOT assigned to any domain: Chain "A" 123 - 125 The following residues NOT assigned to any domain: Chain "A" 2 - 125
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AVE A

BIOTIN-BINDING PROTEIN 05-MAR-93 :: AVIDIN (APO FORM)

DOMAIN 1: [Assigned by homology with 2AVIA]A 3 to A 122 ; The following residues NOT assigned to any domain: Chain "A" 123 - 125 The following residues NOT assigned to any domain: Chain "A" 3 - 125
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AVE B

BIOTIN-BINDING PROTEIN 05-MAR-93 :: AVIDIN (APO FORM)

DOMAIN 1: [Assigned by homology with 2AVIA]B 3 to B 122 ; The following residues NOT assigned to any domain: Chain "B" 3 - 125 The following residues NOT assigned to any domain: Chain "B" 123 - 125
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AVD B

BIOTIN-BINDING PROTEIN 05-MAR-93 :: AVIDIN COMPLEX WITH BIOTIN

DOMAIN 1: [Assigned by homology with 2AVIA]B 2 to B 122 ; The following residues NOT assigned to any domain: Chain "B" 3 - 125 The following residues NOT assigned to any domain: Chain "B" 123 - 125
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AZN A

ELECTRON TRANSPORT(COPPER BINDING) 27-MAY-94 :: AZURIN MUTANT WITH PHE 114 REPLACED BY ALA (F114A)

DOMAIN 1: [Assigned by homology with 2AZAA]A 1 to A 128 ; The following residues NOT assigned to any domain: Chain "A" 1 - 128 The following residues NOT assigned to any domain: Chain "A" 1 - 128 The following residues NOT assigned to any domain: Chain "A" 1 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AZN B

ELECTRON TRANSPORT(COPPER BINDING) 27-MAY-94 :: AZURIN MUTANT WITH PHE 114 REPLACED BY ALA (F114A)

DOMAIN 1: [Assigned by homology with 2AZAA]B 1 to B 128 ; The following residues NOT assigned to any domain: Chain "B" 1 - 128 The following residues NOT assigned to any domain: Chain "B" 1 - 128 The following residues NOT assigned to any domain: Chain "B" 1 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AZN C

ELECTRON TRANSPORT(COPPER BINDING) 27-MAY-94 :: AZURIN MUTANT WITH PHE 114 REPLACED BY ALA (F114A)

DOMAIN 1: [Assigned by homology with 2AZAA]C 1 to C 128 ; The following residues NOT assigned to any domain: Chain "C" 1 - 128 The following residues NOT assigned to any domain: Chain "C" 1 - 128 The following residues NOT assigned to any domain: Chain "C" 1 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AZN D

ELECTRON TRANSPORT(COPPER BINDING) 27-MAY-94 :: AZURIN MUTANT WITH PHE 114 REPLACED BY ALA (F114A)

DOMAIN 1: [Assigned by homology with 2AZAA]D 1 to D 128 ; The following residues NOT assigned to any domain: Chain "D" 1 - 128 The following residues NOT assigned to any domain: Chain "D" 1 - 128 The following residues NOT assigned to any domain: Chain "D" 1 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4AZU A

ELECTRON TRANSPORT(COPPER BINDING) 23-JUN-93 :: AZURIN (PH 5.5)

DOMAIN 1: [Assigned by homology with 2AZAA]A 1 to A 128 ; The following residues NOT assigned to any domain: Chain "A" 1 - 128 The following residues NOT assigned to any domain: Chain "A" 1 - 128 The following residues NOT assigned to any domain: Chain "A" 1 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4AZU B

ELECTRON TRANSPORT(COPPER BINDING) 23-JUN-93 :: AZURIN (PH 5.5)

DOMAIN 1: [Assigned by homology with 2AZAA]B 1 to B 128 ; The following residues NOT assigned to any domain: Chain "B" 1 - 128 The following residues NOT assigned to any domain: Chain "B" 1 - 128 The following residues NOT assigned to any domain: Chain "B" 1 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4AZU C

ELECTRON TRANSPORT(COPPER BINDING) 23-JUN-93 :: AZURIN (PH 5.5)

DOMAIN 1: [Assigned by homology with 2AZAA]C 1 to C 128 ; The following residues NOT assigned to any domain: Chain "C" 1 - 128 The following residues NOT assigned to any domain: Chain "C" 1 - 128 The following residues NOT assigned to any domain: Chain "C" 1 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4AZU D

ELECTRON TRANSPORT(COPPER BINDING) 23-JUN-93 :: AZURIN (PH 5.5)

DOMAIN 1: [Assigned by homology with 2AZAA]D 1 to D 128 ; The following residues NOT assigned to any domain: Chain "D" 1 - 128 The following residues NOT assigned to any domain: Chain "D" 1 - 128 The following residues NOT assigned to any domain: Chain "D" 1 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5AZU A

ELECTRON TRANSPORT(COPPER BINDING) 23-JUN-93 :: AZURIN (PH 9.0)

DOMAIN 1: [Assigned by homology with 2AZAA]A 1 to A 128 ; The following residues NOT assigned to any domain: Chain "A" 1 - 128 The following residues NOT assigned to any domain: Chain "A" 1 - 128 The following residues NOT assigned to any domain: Chain "A" 1 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5AZU B

ELECTRON TRANSPORT(COPPER BINDING) 23-JUN-93 :: AZURIN (PH 9.0)

DOMAIN 1: [Assigned by homology with 2AZAA]B 1 to B 128 ; The following residues NOT assigned to any domain: Chain "B" 1 - 128 The following residues NOT assigned to any domain: Chain "B" 1 - 128 The following residues NOT assigned to any domain: Chain "B" 1 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5AZU C

ELECTRON TRANSPORT(COPPER BINDING) 23-JUN-93 :: AZURIN (PH 9.0)

DOMAIN 1: [Assigned by homology with 2AZAA]C 1 to C 128 ; The following residues NOT assigned to any domain: Chain "C" 1 - 128 The following residues NOT assigned to any domain: Chain "C" 1 - 128 The following residues NOT assigned to any domain: Chain "C" 1 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5AZU D

ELECTRON TRANSPORT(COPPER BINDING) 23-JUN-93 :: AZURIN (PH 9.0)

DOMAIN 1: [Assigned by homology with 2AZAA]D 1 to D 128 ; The following residues NOT assigned to any domain: Chain "D" 1 - 128 The following residues NOT assigned to any domain: Chain "D" 1 - 128 The following residues NOT assigned to any domain: Chain "D" 1 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AZR A

ELECTRON TRANSFER(CUPROPROTEIN) 04-MAR-93 :: AZURIN MUTANT WITH ASN 47 REPLACED BY ASP (/N47D$)

DOMAIN 1: [Assigned by homology with 2AZAA]A 1 to A 128 ; The following residues NOT assigned to any domain: Chain "A" 1 - 128 The following residues NOT assigned to any domain: Chain "A" 1 - 128 The following residues NOT assigned to any domain: Chain "A" 1 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AZR B

ELECTRON TRANSFER(CUPROPROTEIN) 04-MAR-93 :: AZURIN MUTANT WITH ASN 47 REPLACED BY ASP (/N47D$)

DOMAIN 1: [Assigned by homology with 2AZAA]B 1 to B 128 ; The following residues NOT assigned to any domain: Chain "B" 1 - 128 The following residues NOT assigned to any domain: Chain "B" 1 - 128 The following residues NOT assigned to any domain: Chain "B" 1 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AZR C

ELECTRON TRANSFER(CUPROPROTEIN) 04-MAR-93 :: AZURIN MUTANT WITH ASN 47 REPLACED BY ASP (/N47D$)

DOMAIN 1: [Assigned by homology with 2AZAA]C 1 to C 128 ; The following residues NOT assigned to any domain: Chain "C" 1 - 128 The following residues NOT assigned to any domain: Chain "C" 1 - 128 The following residues NOT assigned to any domain: Chain "C" 1 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AZR D

ELECTRON TRANSFER(CUPROPROTEIN) 04-MAR-93 :: AZURIN MUTANT WITH ASN 47 REPLACED BY ASP (/N47D$)

DOMAIN 1: [Assigned by homology with 2AZAA]D 1 to D 128 ; The following residues NOT assigned to any domain: Chain "D" 1 - 128 The following residues NOT assigned to any domain: Chain "D" 1 - 128 The following residues NOT assigned to any domain: Chain "D" 1 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3AZU A

ELECTRON TRANSFER(CUPROPROTEIN) 11-JAN-91 :: AZURIN MUTANT WITH HIS 35 REPLACED BY GLN (/H35Q$)

DOMAIN 1: [Assigned by homology with 2AZAA]A 1 to A 128 ; The following residues NOT assigned to any domain: Chain "A" 1 - 128 The following residues NOT assigned to any domain: Chain "A" 1 - 128 The following residues NOT assigned to any domain: Chain "A" 1 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3AZU B

ELECTRON TRANSFER(CUPROPROTEIN) 11-JAN-91 :: AZURIN MUTANT WITH HIS 35 REPLACED BY GLN (/H35Q$)

DOMAIN 1: [Assigned by homology with 2AZAA]B 1 to B 128 ; The following residues NOT assigned to any domain: Chain "B" 1 - 128 The following residues NOT assigned to any domain: Chain "B" 1 - 128 The following residues NOT assigned to any domain: Chain "B" 1 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3AZU C

ELECTRON TRANSFER(CUPROPROTEIN) 11-JAN-91 :: AZURIN MUTANT WITH HIS 35 REPLACED BY GLN (/H35Q$)

DOMAIN 1: [Assigned by homology with 2AZAA]C 1 to C 128 ; The following residues NOT assigned to any domain: Chain "C" 1 - 128 The following residues NOT assigned to any domain: Chain "C" 1 - 128 The following residues NOT assigned to any domain: Chain "C" 1 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3AZU D

ELECTRON TRANSFER(CUPROPROTEIN) 11-JAN-91 :: AZURIN MUTANT WITH HIS 35 REPLACED BY GLN (/H35Q$)

DOMAIN 1: [Assigned by homology with 2AZAA]D 1 to D 128 ; The following residues NOT assigned to any domain: Chain "D" 1 - 128 The following residues NOT assigned to any domain: Chain "D" 1 - 128 The following residues NOT assigned to any domain: Chain "D" 1 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AZU

ELECTRON TRANSPORT (COPPER BINDING) 04-AUG-80 :: AZURIN

DOMAIN 1: [Assigned by homology with 2AZAA] 3 to 128 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2AZU A

ELECTRON TRANSFER(CUPROPROTEIN) 11-JAN-91 :: AZURIN MUTANT WITH HIS 35 REPLACED BY LEU (/H35L$)

DOMAIN 1: [Assigned by homology with 2AZAA]A 1 to A 128 ; The following residues NOT assigned to any domain: Chain "A" 1 - 128 The following residues NOT assigned to any domain: Chain "A" 1 - 128 The following residues NOT assigned to any domain: Chain "A" 1 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2AZU B

ELECTRON TRANSFER(CUPROPROTEIN) 11-JAN-91 :: AZURIN MUTANT WITH HIS 35 REPLACED BY LEU (/H35L$)

DOMAIN 1: [Assigned by homology with 2AZAA]B 1 to B 128 ; The following residues NOT assigned to any domain: Chain "B" 1 - 128 The following residues NOT assigned to any domain: Chain "B" 1 - 128 The following residues NOT assigned to any domain: Chain "B" 1 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2AZU C

ELECTRON TRANSFER(CUPROPROTEIN) 11-JAN-91 :: AZURIN MUTANT WITH HIS 35 REPLACED BY LEU (/H35L$)

DOMAIN 1: [Assigned by homology with 2AZAA]C 1 to C 128 ; The following residues NOT assigned to any domain: Chain "C" 1 - 128 The following residues NOT assigned to any domain: Chain "C" 1 - 128 The following residues NOT assigned to any domain: Chain "C" 1 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2AZU D

ELECTRON TRANSFER(CUPROPROTEIN) 11-JAN-91 :: AZURIN MUTANT WITH HIS 35 REPLACED BY LEU (/H35L$)

DOMAIN 1: [Assigned by homology with 2AZAA]D 1 to D 128 ; The following residues NOT assigned to any domain: Chain "D" 1 - 128 The following residues NOT assigned to any domain: Chain "D" 1 - 128 The following residues NOT assigned to any domain: Chain "D" 1 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AIZ A

ELECTRON TRANSPORT(CADMIUM BINDING) 11-NOV-93 :: AZURIN (CADMIUM FORM) (CADMIUM-AZURIN)

DOMAIN 1: [Assigned by homology with 2AZAA]A 1 to A 129 ; The following residues NOT assigned to any domain: Chain "A" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AIZ B

ELECTRON TRANSPORT(CADMIUM BINDING) 11-NOV-93 :: AZURIN (CADMIUM FORM) (CADMIUM-AZURIN)

DOMAIN 1: [Assigned by homology with 2AZAA]B 1 to B 129 ; The following residues NOT assigned to any domain: Chain "B" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AZB A

ELECTRON TRANSPORT(COPPER) 16-DEC-92 :: AZURIN (COPPER-REMOVED)

DOMAIN 1: [Assigned by homology with 2AZAA]A 1 to A 129 ; The following residues NOT assigned to any domain: Chain "A" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AZB B

ELECTRON TRANSPORT(COPPER) 16-DEC-92 :: AZURIN (COPPER-REMOVED)

DOMAIN 1: [Assigned by homology with 2AZAA]B 1 to B 129 ; The following residues NOT assigned to any domain: Chain "B" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AZC A

ELECTRON TRANSPORT(COPPER) 16-DEC-92 :: AZURIN (APO FORM)

DOMAIN 1: [Assigned by homology with 2AZAA]A 1 to A 129 ; The following residues NOT assigned to any domain: Chain "A" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AZC B

ELECTRON TRANSPORT(COPPER) 16-DEC-92 :: AZURIN (APO FORM)

DOMAIN 1: [Assigned by homology with 2AZAA]B 1 to B 129 ; The following residues NOT assigned to any domain: Chain "B" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2AZA B

ELECTRON TRANSPORT PROTEIN(CUPROPROTEIN)14-OCT-86 :: AZURIN (OXIDIZED)

DOMAIN 1: [Assigned by homology with 2AZAA]B 1 to B 129 ; The following residues NOT assigned to any domain: Chain "B" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BDS

ANTI-HYPERTENSIVE, ANTI-VIRAL PROTEIN 14-NOV-88 :: /BDS-I$ (/NMR$, MINIMIZED MEAN STRUCTURE)

DOMAIN 1: 1 to 43 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CBH

HYDROLASE (O-GLYCOSYL) 30-MAY-89 :: C-TERMINAL DOMAIN OF CELLOBIOHYDROLASE I (/CT-CBH$

DOMAIN 1: 1 to 36 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CCY B

ELECTRON TRANSPORT (HEME PROTEIN) 27-AUG-85 :: CYTOCHROME $C(PRIME)

DOMAIN 1: [Assigned by homology with 2CCYA]B 2 to B 128 ; The following residues NOT assigned to any domain: Chain "B" 2 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CYM

ELECTRON TRANSPORT 29-SEP-93 :: CYTOCHROME C=3=

DOMAIN 1: 1 to 106 ; The following residues NOT assigned to any domain: Chain " " 107 - 107
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CTH A

ELECTRON TRANSPORT 16-MAR-93 :: CYTOCHROME C3

DOMAIN 1: A 1 to A 106 ; The following residues NOT assigned to any domain: Chain "A" 107 - 107 The following residues NOT assigned to any domain: Chain "A" 1 - 107
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CTH B

ELECTRON TRANSPORT 16-MAR-93 :: CYTOCHROME C3

DOMAIN 1: B 1 to B 106 ; The following residues NOT assigned to any domain: Chain "B" 1 - 107 The following residues NOT assigned to any domain: Chain "B" 107 - 107
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CYR

ELECTRON TRANSPORT(CYTOCHROME) 15-JUL-94 :: CYTOCHROME C3

DOMAIN 1: 1 to 106 ; The following residues NOT assigned to any domain: Chain " " 107 - 107
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CY3

ELECTRON TRANSPORT (HEME PROTEIN) 01-JUL-94 :: CYTOCHROME C=3=

DOMAIN 1: 1 to 115 ; The following residues NOT assigned to any domain: Chain " " 116 - 118
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CYH A

ISOMERASE(PEPTIDYL-PROLYL CIS-TRANS) 14-DEC-92 :: CYCLOPHILIN A

DOMAIN 1: A 2 to A 164 ; The following residues NOT assigned to any domain: Chain "A" 165 - 165 The following residues NOT assigned to any domain: Chain "A" 1 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3CYS A

ISOMERASE(PEPTIDYL-PROLYL CIS-TRANS) 28-FEB-94 :: CYCLOPHILIN A COMPLEXED WITH CYCLOSPORIN A

DOMAIN 1: A 1 to A 164 ; The following residues NOT assigned to any domain: Chain "A" 165 - 165 The following residues NOT assigned to any domain: Chain "A" 205 - 208
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1KST

PRELIMINARY 04-SEP-91 :: KISTRIN

DOMAIN 1: 1 to 68 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HHM B

HYDROLASE 20-OCT-92 :: HUMAN INOSITOL MONOPHOSPHATASE (E.C.3.1.3.25) DIME

DOMAIN 1: [Assigned by homology with 2HHMA]B 5 to B 276 ; The following residues NOT assigned to any domain: Chain "B" 5 - 276
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PIH

ELECTRON TRANSFER(IRON-SULFUR PROTEIN) 03-AUG-94 :: HIGH POTENTIAL IRON SULFUR PROTEIN INSERTION MUTAN

DOMAIN 1: [Assigned by homology with 2HIPA] 1 to 72 ; The following residues NOT assigned to any domain: Chain " " 73 - 73
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HIP B

ELECTRON TRANSFER (IRON-SULFUR PROTEIN) 24-JUN-91 :: HIGH POTENTIAL IRON SULFUR PROTEIN (HI/PIP$)

DOMAIN 1: [Assigned by homology with 2HIPA]B 1 to B 70 ; The following residues NOT assigned to any domain: Chain "B" 1 - 71 The following residues NOT assigned to any domain: Chain "B" 71 - 71
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2IFF Y

IMMUNOGLOBULIN/HYDROLASE(O-GLYCOSYL) 03-FEB-94 :: IGG1 FAB FRAGMENT (HYHEL-5) COMPLEXED WITH LYSOZYM

DOMAIN 1: Y 1 to Y 128 ; The following residues NOT assigned to any domain: Chain "Y" 1 - 212 The following residues NOT assigned to any domain: Chain "Y" 2 - 215 The following residues NOT assigned to any domain: Chain "Y" 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LMA

HYDROLASE(O-GLYCOSYL) 14-AUG-92 :: LYSOZYME (E.C.3.2.1.17) (88 PERCENT HUMIDITY)

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2LYM

HYDROLASE (O-GLYCOSYL) 08-JUN-87 :: LYSOZYME (E.C.3.2.1.17) (1 ATMOSPHERE, 1.4 M NA*CL

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2LYZ

HYDROLASE (O-GLYCOSYL) 01-FEB-75 :: LYSOZYME (E.C.3.2.1.17)

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2LZH

HYDROLASE (O-GLYCOSYL) 29-JUN-81 :: LYSOZYME (ORTHORHOMBIC) (E.C.3.2.1.17)

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HEL

HYDROLASE(O-GLYCOSYL) 10-JAN-92 :: HEN EGG-WHITE LYSOZYME (E.C.3.2.1.17) WILD TYPE

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2LZT

HYDROLASE(O-GLYCOSYL) 21-AUG-89 :: LYSOZYME (E.C.3.2.1.17), TRICLINIC CRYSTAL FORM

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LSA

HYDROLASE(O-GLYCOSYL) 05-JUL-94 :: LYSOZYME (E.C.3.2.1.17) (120 K)

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LSB

HYDROLASE(O-GLYCOSYL) 05-JUL-94 :: LYSOZYME (E.C.3.2.1.17) (180 K)

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LSC

HYDROLASE(O-GLYCOSYL) 05-JUL-94 :: LYSOZYME (E.C.3.2.1.17) (250 K)

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LSD

HYDROLASE(O-GLYCOSYL) 05-JUL-94 :: LYSOZYME (E.C.3.2.1.17) (280 K)

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LSE

HYDROLASE(O-GLYCOSYL) 05-JUL-94 :: LYSOZYME (E.C.3.2.1.17) (295 K)

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HEW

PRELIMINARY 20-JAN-92 :: LYSOZYME E.C.3.2.1.17 COMPLEXED WITH THE INHIBITOR

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LSF

HYDROLASE(O-GLYCOSYL) 05-JUL-94 :: LYSOZYME (E.C.3.2.1.17) (95 K)

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1VFB C

IMMUNOGLOBULIN/HYDROLASE(O-GLYCOSYL) 03-DEC-93 :: FV FRAGMENT OF MOUSE MONOCLONAL ANTIBODY D1.3 COMP

DOMAIN 1: C 1 to C 128 ; The following residues NOT assigned to any domain: Chain "C" 1 - 107 The following residues NOT assigned to any domain: Chain "C" 1 - 116 The following residues NOT assigned to any domain: Chain "C" 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LYM A

HYDROLASE(O-GLYCOSYL) 29-JUL-82 :: LYSOZYME (E.C.3.2.1.17)

DOMAIN 1: A 1 to A 128 ; The following residues NOT assigned to any domain: Chain "A" 129 - 129 The following residues NOT assigned to any domain: Chain "A" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LYM B

HYDROLASE(O-GLYCOSYL) 29-JUL-82 :: LYSOZYME (E.C.3.2.1.17)

DOMAIN 1: B 1 to B 128 ; The following residues NOT assigned to any domain: Chain "B" 1 - 129 The following residues NOT assigned to any domain: Chain "B" 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LYS A

HYDROLASE(O-GLYCOSYL) 03-DEC-93 :: LYSOZYME (E.C.3.2.1.17)

DOMAIN 1: A 1 to A 128 ; The following residues NOT assigned to any domain: Chain "A" 129 - 129 The following residues NOT assigned to any domain: Chain "A" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LYS B

HYDROLASE(O-GLYCOSYL) 03-DEC-93 :: LYSOZYME (E.C.3.2.1.17)

DOMAIN 1: B 1 to B 128 ; The following residues NOT assigned to any domain: Chain "B" 1 - 129 The following residues NOT assigned to any domain: Chain "B" 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LYZ

HYDROLASE (O-GLYCOSYL) 01-FEB-75 :: LYSOZYME (E.C.3.2.1.17)

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4LYM

HYDROLASE (O-GLYCOSYL) 30-JUL-90 :: LYSOZYME (MUCOPEPTIDE N-ACETYLMURAMYL HYDROLASE)

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4LYT A

HYDROLASE(O-GLYCOSYL) 20-MAR-92 :: LYSOZYME (E.C.3.2.1.17) (298 KELVIN)

DOMAIN 1: A 1 to A 128 ; The following residues NOT assigned to any domain: Chain "A" 129 - 129 The following residues NOT assigned to any domain: Chain "A" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4LYT B

HYDROLASE(O-GLYCOSYL) 20-MAR-92 :: LYSOZYME (E.C.3.2.1.17) (298 KELVIN)

DOMAIN 1: B 1 to B 128 ; The following residues NOT assigned to any domain: Chain "B" 1 - 129 The following residues NOT assigned to any domain: Chain "B" 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4LYZ

HYDROLASE (O-GLYCOSYL) 01-FEB-75 :: LYSOZYME (E.C.3.2.1.17)

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LZH A

HYDROLASE (O-GLYCOSYL) 29-JUN-81 :: LYSOZYME (MONOCLINIC) (E.C.3.2.1.17)

DOMAIN 1: A 1 to A 128 ; The following residues NOT assigned to any domain: Chain "A" 129 - 129 The following residues NOT assigned to any domain: Chain "A" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LZH B

HYDROLASE (O-GLYCOSYL) 29-JUN-81 :: LYSOZYME (MONOCLINIC) (E.C.3.2.1.17)

DOMAIN 1: B 1 to B 128 ; The following residues NOT assigned to any domain: Chain "B" 1 - 129 The following residues NOT assigned to any domain: Chain "B" 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LZT

HYDROLASE(O-GLYCOSYL) 01-APR-85 :: LYSOZYME (E.C.3.2.1.17), TRICLINIC CRYSTAL FORM

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RCM A

HYDROLASE(O-GLYCOSYL) 10-JAN-93 :: LYSOZYME (E.C.3.2.1.17) (PARTIALLY REDUCED,

DOMAIN 1: A 1 to A 128 ; The following residues NOT assigned to any domain: Chain "A" 129 - 129 The following residues NOT assigned to any domain: Chain "A" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RCM B

HYDROLASE(O-GLYCOSYL) 10-JAN-93 :: LYSOZYME (E.C.3.2.1.17) (PARTIALLY REDUCED,

DOMAIN 1: B 1 to B 128 ; The following residues NOT assigned to any domain: Chain "B" 1 - 129 The following residues NOT assigned to any domain: Chain "B" 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

132L

HYDROLASE(O-GLYCOSYL) 02-JUN-93 :: LYSOZYME (E.C.3.2.1.17)

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HWA

HYDROLASE(O-GLYCOSYL) 17-AUG-92 :: LYSOZYME (E.C.3.2.1.17) (NMR, MINIMIZED AVERAGE ST

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5LYT

HYDROLASE(O-GLYCOSYL) 20-MAR-92 :: LYSOZYME (E.C.3.2.1.17) (100 KELVIN)

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5LYZ

HYDROLASE (O-GLYCOSYL) 01-FEB-75 :: LYSOZYME (E.C.3.2.1.17)

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FDL Y

COMPLEX (ANTIBODY-ANTIGEN) 27-AUG-90 :: IG*G1 FAB FRAGMENT (ANTI-LYSOZYME ANTIBODY D1.3, K

DOMAIN 1: Y 1 to Y 128 ; The following residues NOT assigned to any domain: Chain "Y" 1 - 214 The following residues NOT assigned to any domain: Chain "Y" 1 - 218 The following residues NOT assigned to any domain: Chain "Y" 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6LYT

HYDROLASE(O-GLYCOSYL) 20-MAR-92 :: LYSOZYME (E.C.3.2.1.17) (298 KELVIN)

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6LYZ

HYDROLASE (O-GLYCOSYL) 01-FEB-75 :: LYSOZYME (E.C.3.2.1.17)

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7LYZ

HYDROLASE(O-GLYCOSYL) 06-MAY-77 :: LYSOZYME (E.C.3.2.1.17) TRICLINIC CRYSTAL FORM

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3HFM Y

COMPLEX(ANTIBODY-ANTIGEN) 11-AUG-88 :: IG*G1 FAB FRAGMENT (HY/HEL$-10) AND LYSOZYME (E.C.

DOMAIN 1: Y 1 to Y 128 ; The following residues NOT assigned to any domain: Chain "Y" 1 - 214 The following residues NOT assigned to any domain: Chain "Y" 1 - 215 The following residues NOT assigned to any domain: Chain "Y" 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8LYZ

HYDROLASE (O-GLYCOSYL) 16-SEP-77 :: LYSOZYME (E.C.3.2.1.17) IODINE-INACTIVATED

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3LYM

HYDROLASE (O-GLYCOSYL) 08-JUN-87 :: LYSOZYME (E.C.3.2.1.17) (1000 ATMOSPHERES, 1.4 M N

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3LYT A

HYDROLASE(O-GLYCOSYL) 20-MAR-92 :: LYSOZYME (E.C.3.2.1.17) (100 KELVIN)

DOMAIN 1: A 1 to A 128 ; The following residues NOT assigned to any domain: Chain "A" 129 - 129 The following residues NOT assigned to any domain: Chain "A" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3LYT B

HYDROLASE(O-GLYCOSYL) 20-MAR-92 :: LYSOZYME (E.C.3.2.1.17) (100 KELVIN)

DOMAIN 1: B 1 to B 128 ; The following residues NOT assigned to any domain: Chain "B" 1 - 129 The following residues NOT assigned to any domain: Chain "B" 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3LYZ

HYDROLASE (O-GLYCOSYL) 01-FEB-75 :: LYSOZYME (E.C.3.2.1.17)

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HFM Y

COMPLEX(ANTIBODY-ANTIGEN) 30-OCT-87 :: IG*G1 FV FRAGMENT (HY/HEL$-10) AND LYSOZYME (E.C.3

DOMAIN 1: Y 1 to Y 128 ; The following residues NOT assigned to any domain: Chain "Y" 1 - 107 The following residues NOT assigned to any domain: Chain "Y" 1 - 113 The following residues NOT assigned to any domain: Chain "Y" 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HEM

HYDROLASE(O-GLYCOSYL) 10-JAN-92 :: LYSOZYME (E.C.3.2.1.17) MUTANT WITH SER 91 REPLACE

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HER

HYDROLASE(O-GLYCOSYL) 10-JAN-92 :: LYSOZYME (E.C.3.2.1.17) MUTANT WITH THR 40 REPLACE

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HFL Y

COMPLEX(ANTIBODY-ANTIGEN) 17-AUG-87 :: IG*G1 FAB FRAGMENT (HY/HEL$-5) AND LYSOZYME (E.C.3

DOMAIN 1: Y 1 to Y 128 ; The following residues NOT assigned to any domain: Chain "Y" 1 - 212 The following residues NOT assigned to any domain: Chain "Y" 1 - 213 The following residues NOT assigned to any domain: Chain "Y" 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HEO

HYDROLASE(O-GLYCOSYL) 10-JAN-92 :: LYSOZYME (E.C.3.2.1.17) MUTANT WITH ILE 55 REPLACE

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HEQ

HYDROLASE(O-GLYCOSYL) 10-JAN-92 :: LYSOZYME (E.C.3.2.1.17) MUTANT WITH THR 40 REPLACE

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HEN

HYDROLASE(O-GLYCOSYL) 10-JAN-92 :: LYSOZYME (E.C.3.2.1.17) MUTANT WITH ILE 55 REPLACE

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LSN

HYDROLASE(O-GLYCOSYL) 13-SEP-94 :: LYSOZYME (E.C.3.2.1.17) MUTANT WITH SER 91 REPLACE

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HEP

HYDROLASE(O-GLYCOSYL) 10-JAN-92 :: LYSOZYME (E.C.3.2.1.17) MUTANT WITH THR 40 REPLACE

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LSM

HYDROLASE(O-GLYCOSYL) 13-SEP-94 :: LYSOZYME (E.C.3.2.1.17) MUTANT WITH ILE 55 REPLACE

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2LZ2

HYDROLASE (O-GLYCOSYL) 20-OCT-88 :: LYSOZYME (E.C.3.2.1.17)

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

135L

HYDROLASE(O-GLYCOSYL) 10-JUN-93 :: LYSOZYME (E.C.3.2.1.17)

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3LZ2

HYDROLASE(O-GLYCOSYL) 13-SEP-91 :: LYSOZYME (E.C.3.2.1.17)

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LZ3

HYDROLASE(O-GLYCOSYL) 13-NOV-91 :: LYSOZYME (E.C.3.2.1.17)

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HHL

HYDROLASE(O-GLYCOSYL) 04-MAY-93 :: LYSOZYME (E.C.3.2.1.17)

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LZ2

HYDROLASE (O-GLYCOSYL) 21-SEP-81 :: LYSOZYME

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GHL A

HYDROLASE(O-GLYCOSYL) 04-MAY-93 :: LYSOZYME (E.C.3.2.1.17)

DOMAIN 1: A 0 to A 128 ; The following residues NOT assigned to any domain: Chain "A" 129 - 129 The following residues NOT assigned to any domain: Chain "A" 0 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GHL B

HYDROLASE(O-GLYCOSYL) 04-MAY-93 :: LYSOZYME (E.C.3.2.1.17)

DOMAIN 1: B 0 to B 128 ; The following residues NOT assigned to any domain: Chain "B" 0 - 129 The following residues NOT assigned to any domain: Chain "B" 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1JHL A

COMPLEX(ANTIBODY-ANTIGEN) 04-MAY-93 :: FV FRAGMENT (LIGHT AND HEAVY VARIABLE DOMAINS

DOMAIN 1: A 1 to A 128 ; The following residues NOT assigned to any domain: Chain "A" 1 - 108 The following residues NOT assigned to any domain: Chain "A" 1 - 116 The following residues NOT assigned to any domain: Chain "A" 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LZ5

HYDROLASE(O-GLYCOSYL) 03-FEB-93 :: LYSOZYME (E.C.3.2.1.17) MUTANT WITH FOUR AMINO

DOMAIN 1: 1 to 129 ; The following residues NOT assigned to any domain: Chain " " 130 - 130
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LZ6

HYDROLASE(O-GLYCOSYL) 03-FEB-93 :: LYSOZYME (E.C.3.2.1.17) MUTANT WITH EIGHT AMINO AC

DOMAIN 1: 1 to 129 ; The following residues NOT assigned to any domain: Chain " " 130 - 130
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TDY

HYDROLASE (O-GLYCOSYL) 06-AUG-92 :: LYSOZYME (E.C.3.2.1.17) MUTANT WITH TYR 63 REPLACE

DOMAIN 1: 1 to 129 ; The following residues NOT assigned to any domain: Chain " " 130 - 130
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LHH

PRELIMINARY 27-MAR-92 :: LYSOZOME (E.C.3.2.1.17) MUTANT WITH VAL 110 REPLAC

DOMAIN 1: 1 to 129 ; The following residues NOT assigned to any domain: Chain " " 130 - 130
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LHI

PRELIMINARY 27-MAR-92 :: LYSOZOME (E.C.3.2.1.17) MUTANT WITH PRO 71 REPLACE

DOMAIN 1: 1 to 129 ; The following residues NOT assigned to any domain: Chain " " 130 - 130
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LHJ

PRELIMINARY 27-MAR-92 :: LYSOZOME (E.C.3.2.1.17) MUTANT WITH PRO 103 REPLAC

DOMAIN 1: 1 to 129 ; The following residues NOT assigned to any domain: Chain " " 130 - 130
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LHK

PRELIMINARY 27-MAR-92 :: LYSOZOME (E.C.3.2.1.17) MUTANT WITH ASP 91 REPLACE

DOMAIN 1: 1 to 129 ; The following residues NOT assigned to any domain: Chain " " 130 - 130
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LHM

HYDROLASE (O-GLYCOSYL) 02-OCT-91 :: LYSOZYME (E.C.3.2.1.17) (MUTANT WITH CYS 77 REPLAC

DOMAIN 1: 1 to 129 ; The following residues NOT assigned to any domain: Chain " " 130 - 130
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2LHM

HYDROLASE (O-GLYCOSYL) 02-OCT-91 :: LYSOZYME (E.C.3.2.1.17) (APO) (MUTANT WITH GLN 86

DOMAIN 1: 1 to 129 ; The following residues NOT assigned to any domain: Chain " " 130 - 130
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LZ1

HYDROLASE (O-GLYCOSYL) 12-OCT-84 :: LYSOZYME (E.C.3.2.1.17)

DOMAIN 1: 1 to 129 ; The following residues NOT assigned to any domain: Chain " " 130 - 130
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LZ4

HYDROLASE(O-GLYCOSYL) 03-FEB-93 :: LYSOZYME (E.C.3.2.1.17) MUTANT WITH CYS 77 REPLACE

DOMAIN 1: 1 to 129 ; The following residues NOT assigned to any domain: Chain " " 130 - 130
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

133L

HYDROLASE(O-GLYCOSYL) 01-JUN-93 :: LYSOZYME (E.C.3.2.1.17) MUTANT WITH ARG 115 REPLAC

DOMAIN 1: 1 to 129 ; The following residues NOT assigned to any domain: Chain " " 130 - 130
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

134L

HYDROLASE(O-GLYCOSYL) 01-JUN-93 :: LYSOZYME (E.C.3.2.1.17) MUTANT WITH ARG 115 REPLAC

DOMAIN 1: 1 to 129 ; The following residues NOT assigned to any domain: Chain " " 130 - 130
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TAY

HYDROLASE (O-GLYCOSYL) 06-AUG-92 :: LYSOZYME (E.C.3.2.1.17) MUTANT WITH TYR 63 REPLACE

DOMAIN 1: 1 to 129 ; The following residues NOT assigned to any domain: Chain " " 130 - 130
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TBY

HYDROLASE (O-GLYCOSYL) 06-AUG-92 :: LYSOZYME (E.C.3.2.1.17) MUTANT WITH TYR 63 REPLACE

DOMAIN 1: 1 to 129 ; The following residues NOT assigned to any domain: Chain " " 130 - 130
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TCY

HYDROLASE (O-GLYCOSYL) 06-AUG-92 :: LYSOZYME (E.C.3.2.1.17) MUTANT WITH TYR 63 REPLACE

DOMAIN 1: 1 to 129 ; The following residues NOT assigned to any domain: Chain " " 130 - 130
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3LHM

HYDROLASE (O-GLYCOSYL) 02-OCT-91 :: LYSOZYME (E.C.3.2.1.17) (HOLO) (MUTANT WITH GLN 86

DOMAIN 1: 1 to 129 ; The following residues NOT assigned to any domain: Chain " " 130 - 130
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LAA

HYDROLASE (O-GLYCOSYL) 24-JUN-92 :: LYSOZYME (E.C.3.2.1.17) MUTANT WITH ASP 53 REPLACE

DOMAIN 1: 1 to 129 ; The following residues NOT assigned to any domain: Chain " " 130 - 130
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LHL

PRELIMINARY 27-MAR-92 :: LYSOZOME (E.C.3.2.1.17) MUTANT WITH ALA 47 REPLACE

DOMAIN 1: 1 to 129 ; The following residues NOT assigned to any domain: Chain " " 130 - 130
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2EQL

HYDROLASE(O-GLYCOSYL) 27-MAY-94 :: LYSOZYME (APO FORM)

DOMAIN 1: 1 to 128 ; The following residues NOT assigned to any domain: Chain " " 129 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ALC

CALCIUM BINDING PROTEIN 14-AUG-89 :: ALPHA-*LACTALBUMIN

DOMAIN 1: 1 to 121 ; The following residues NOT assigned to any domain: Chain " " 122 - 122
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ITA

CYTOKINE 29-FEB-92 :: INTERLEUKIN 1 ALPHA (THEORETICAL MODEL)

DOMAIN 1: 9 to 156 ; The following residues NOT assigned to any domain: Chain " " 157 - 159
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LEM B

LECTIN 17-NOV-93 :: LECTIN (LENTIL) (HEXAGONAL CRYSTAL FORM)

DOMAIN 1: [Assigned by homology with 2LALA]B 1 to B 47 ; The following residues NOT assigned to any domain: Chain "B" 1 - 181
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LEN B

LECTIN 17-NOV-93 :: LECTIN (LENTIL) (MONOCLINIC CRYSTAL FORM)

DOMAIN 1: [Assigned by homology with 2LALA]B 1 to B 47 ; The following residues NOT assigned to any domain: Chain "B" 1 - 181 The following residues NOT assigned to any domain: Chain "B" 1 - 181 The following residues NOT assigned to any domain: Chain "B" 1 - 47
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LEN D

LECTIN 17-NOV-93 :: LECTIN (LENTIL) (MONOCLINIC CRYSTAL FORM)

DOMAIN 1: [Assigned by homology with 2LALA]D 1 to D 47 ; The following residues NOT assigned to any domain: Chain "D" 1 - 181 The following residues NOT assigned to any domain: Chain "D" 1 - 47 The following residues NOT assigned to any domain: Chain "D" 1 - 181
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2LAL B

LECTIN 10-JUN-93 :: LENTIL LECTIN

DOMAIN 1: [Assigned by homology with 2LALA]B 1 to B 47 ; The following residues NOT assigned to any domain: Chain "B" 1 - 181 The following residues NOT assigned to any domain: Chain "B" 1 - 181 The following residues NOT assigned to any domain: Chain "B" 1 - 47
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2LAL D

LECTIN 10-JUN-93 :: LENTIL LECTIN

DOMAIN 1: [Assigned by homology with 2LALA]D 1 to D 47 ; The following residues NOT assigned to any domain: Chain "D" 1 - 181 The following residues NOT assigned to any domain: Chain "D" 1 - 47 The following residues NOT assigned to any domain: Chain "D" 1 - 181
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RIN D

LECTIN 27-JAN-93 :: PEA LECTIN COMPLEX WITH METHYL-3,6-DI-O-

DOMAIN 1: [Assigned by homology with 2LALA]D 188 to D 236 ; The following residues NOT assigned to any domain: Chain "D" 1 - 180 The following residues NOT assigned to any domain: Chain "D" 188 - 234 The following residues NOT assigned to any domain: Chain "D" 1 - 180
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2LTN B

LECTIN 26-JUN-90 :: PEA LECTIN

DOMAIN 1: [Assigned by homology with 2LALA]B 1 to B 47 ; The following residues NOT assigned to any domain: Chain "B" 1 - 181 The following residues NOT assigned to any domain: Chain "B" 48 - 48 The following residues NOT assigned to any domain: Chain "B" 1 - 181 The following residues NOT assigned to any domain: Chain "B" 1 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2LTN D

LECTIN 26-JUN-90 :: PEA LECTIN

DOMAIN 1: [Assigned by homology with 2LALA]D 1 to D 47 ; The following residues NOT assigned to any domain: Chain "D" 1 - 181 The following residues NOT assigned to any domain: Chain "D" 1 - 48 The following residues NOT assigned to any domain: Chain "D" 1 - 181 The following residues NOT assigned to any domain: Chain "D" 48 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RIN B

LECTIN 27-JAN-93 :: PEA LECTIN COMPLEX WITH METHYL-3,6-DI-O-

DOMAIN 1: [Assigned by homology with 2LALA]B 188 to B 234 ; The following residues NOT assigned to any domain: Chain "B" 1 - 180 The following residues NOT assigned to any domain: Chain "B" 1 - 180 The following residues NOT assigned to any domain: Chain "B" 188 - 236
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LGB B

COMPLEX(LECTIN/TRANSFERRIN) 07-JAN-94 :: LEGUME ISOLECTIN II (LOL II) COMPLEXED WITH LACTOT

DOMAIN 1: [Assigned by homology with 2LALA]B 2 to B 47 ; The following residues NOT assigned to any domain: Chain "B" 1 - 181 The following residues NOT assigned to any domain: Chain "B" 48 - 48 The following residues NOT assigned to any domain: Chain "B" 91 - 249
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LGC B

LECTIN 07-JAN-94 :: LEGUME ISOLECTIN II (LOL II) COMPLEXED WITH A HUMA

DOMAIN 1: [Assigned by homology with 2LALA]B 1 to B 50 ; The following residues NOT assigned to any domain: Chain "B" 1 - 181 The following residues NOT assigned to any domain: Chain "B" 512 - 512 The following residues NOT assigned to any domain: Chain "B" 51 - 51 The following residues NOT assigned to any domain: Chain "B" 1 - 181 The following residues NOT assigned to any domain: Chain "B" 512 - 512 The following residues NOT assigned to any domain: Chain "B" 1 - 48 The following residues NOT assigned to any domain: Chain "B" 1 - 181 The following residues NOT assigned to any domain: Chain "B" 512 - 513 The following residues NOT assigned to any domain: Chain "B" 2 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LGC F

LECTIN 07-JAN-94 :: LEGUME ISOLECTIN II (LOL II) COMPLEXED WITH A HUMA

DOMAIN 1: [Assigned by homology with 2LALA]F 2 to F 47 ; The following residues NOT assigned to any domain: Chain "F" 1 - 181 The following residues NOT assigned to any domain: Chain "F" 512 - 512 The following residues NOT assigned to any domain: Chain "F" 1 - 51 The following residues NOT assigned to any domain: Chain "F" 1 - 181 The following residues NOT assigned to any domain: Chain "F" 512 - 512 The following residues NOT assigned to any domain: Chain "F" 1 - 48 The following residues NOT assigned to any domain: Chain "F" 1 - 181 The following residues NOT assigned to any domain: Chain "F" 512 - 513 The following residues NOT assigned to any domain: Chain "F" 48 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LGC D

LECTIN 07-JAN-94 :: LEGUME ISOLECTIN II (LOL II) COMPLEXED WITH A HUMA

DOMAIN 1: [Assigned by homology with 2LALA]D 1 to D 47 ; The following residues NOT assigned to any domain: Chain "D" 1 - 181 The following residues NOT assigned to any domain: Chain "D" 512 - 512 The following residues NOT assigned to any domain: Chain "D" 1 - 51 The following residues NOT assigned to any domain: Chain "D" 1 - 181 The following residues NOT assigned to any domain: Chain "D" 512 - 512 The following residues NOT assigned to any domain: Chain "D" 48 - 48 The following residues NOT assigned to any domain: Chain "D" 1 - 181 The following residues NOT assigned to any domain: Chain "D" 512 - 513 The following residues NOT assigned to any domain: Chain "D" 2 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOA B

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]B 1 to B 47 ; The following residues NOT assigned to any domain: Chain "B" 1 - 180 The following residues NOT assigned to any domain: Chain "B" 1 - 180 The following residues NOT assigned to any domain: Chain "B" 2 - 48 The following residues NOT assigned to any domain: Chain "B" 1 - 180 The following residues NOT assigned to any domain: Chain "B" 1 - 47 The following residues NOT assigned to any domain: Chain "B" 1 - 180 The following residues NOT assigned to any domain: Chain "B" 2 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOA D

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]D 2 to D 48 ; The following residues NOT assigned to any domain: Chain "D" 1 - 180 The following residues NOT assigned to any domain: Chain "D" 1 - 47 The following residues NOT assigned to any domain: Chain "D" 1 - 180 The following residues NOT assigned to any domain: Chain "D" 1 - 180 The following residues NOT assigned to any domain: Chain "D" 1 - 47 The following residues NOT assigned to any domain: Chain "D" 1 - 180 The following residues NOT assigned to any domain: Chain "D" 2 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOA F

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]F 1 to F 47 ; The following residues NOT assigned to any domain: Chain "F" 1 - 180 The following residues NOT assigned to any domain: Chain "F" 1 - 47 The following residues NOT assigned to any domain: Chain "F" 1 - 180 The following residues NOT assigned to any domain: Chain "F" 2 - 48 The following residues NOT assigned to any domain: Chain "F" 1 - 180 The following residues NOT assigned to any domain: Chain "F" 1 - 180 The following residues NOT assigned to any domain: Chain "F" 2 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOA H

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]H 2 to H 48 ; The following residues NOT assigned to any domain: Chain "H" 1 - 180 The following residues NOT assigned to any domain: Chain "H" 1 - 47 The following residues NOT assigned to any domain: Chain "H" 1 - 180 The following residues NOT assigned to any domain: Chain "H" 2 - 48 The following residues NOT assigned to any domain: Chain "H" 1 - 180 The following residues NOT assigned to any domain: Chain "H" 1 - 47 The following residues NOT assigned to any domain: Chain "H" 1 - 180
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOB B

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]B 1 to B 47 ; The following residues NOT assigned to any domain: Chain "B" 1 - 180 The following residues NOT assigned to any domain: Chain "B" 1 - 180 The following residues NOT assigned to any domain: Chain "B" 2 - 48 The following residues NOT assigned to any domain: Chain "B" 1 - 180 The following residues NOT assigned to any domain: Chain "B" 1 - 47 The following residues NOT assigned to any domain: Chain "B" 1 - 180 The following residues NOT assigned to any domain: Chain "B" 2 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOB D

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]D 2 to D 48 ; The following residues NOT assigned to any domain: Chain "D" 1 - 180 The following residues NOT assigned to any domain: Chain "D" 1 - 47 The following residues NOT assigned to any domain: Chain "D" 1 - 180 The following residues NOT assigned to any domain: Chain "D" 1 - 180 The following residues NOT assigned to any domain: Chain "D" 1 - 47 The following residues NOT assigned to any domain: Chain "D" 1 - 180 The following residues NOT assigned to any domain: Chain "D" 2 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOB F

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]F 1 to F 47 ; The following residues NOT assigned to any domain: Chain "F" 1 - 180 The following residues NOT assigned to any domain: Chain "F" 1 - 47 The following residues NOT assigned to any domain: Chain "F" 1 - 180 The following residues NOT assigned to any domain: Chain "F" 2 - 48 The following residues NOT assigned to any domain: Chain "F" 1 - 180 The following residues NOT assigned to any domain: Chain "F" 1 - 180 The following residues NOT assigned to any domain: Chain "F" 2 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOB H

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]H 2 to H 48 ; The following residues NOT assigned to any domain: Chain "H" 1 - 180 The following residues NOT assigned to any domain: Chain "H" 1 - 47 The following residues NOT assigned to any domain: Chain "H" 1 - 180 The following residues NOT assigned to any domain: Chain "H" 2 - 48 The following residues NOT assigned to any domain: Chain "H" 1 - 180 The following residues NOT assigned to any domain: Chain "H" 1 - 47 The following residues NOT assigned to any domain: Chain "H" 1 - 180
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOC B

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]B 1 to B 47 ; The following residues NOT assigned to any domain: Chain "B" 1 - 180 The following residues NOT assigned to any domain: Chain "B" 951 - 952 The following residues NOT assigned to any domain: Chain "B" 1 - 180 The following residues NOT assigned to any domain: Chain "B" 2 - 48 The following residues NOT assigned to any domain: Chain "B" 961 - 961 The following residues NOT assigned to any domain: Chain "B" 1 - 180 The following residues NOT assigned to any domain: Chain "B" 1 - 47 The following residues NOT assigned to any domain: Chain "B" 971 - 972 The following residues NOT assigned to any domain: Chain "B" 1 - 180 The following residues NOT assigned to any domain: Chain "B" 2 - 48 The following residues NOT assigned to any domain: Chain "B" 981 - 982
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOC D

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]D 2 to D 48 ; The following residues NOT assigned to any domain: Chain "D" 1 - 180 The following residues NOT assigned to any domain: Chain "D" 1 - 47 The following residues NOT assigned to any domain: Chain "D" 951 - 952 The following residues NOT assigned to any domain: Chain "D" 1 - 180 The following residues NOT assigned to any domain: Chain "D" 961 - 961 The following residues NOT assigned to any domain: Chain "D" 1 - 180 The following residues NOT assigned to any domain: Chain "D" 1 - 47 The following residues NOT assigned to any domain: Chain "D" 971 - 972 The following residues NOT assigned to any domain: Chain "D" 1 - 180 The following residues NOT assigned to any domain: Chain "D" 2 - 48 The following residues NOT assigned to any domain: Chain "D" 981 - 982
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOC F

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]F 1 to F 47 ; The following residues NOT assigned to any domain: Chain "F" 1 - 180 The following residues NOT assigned to any domain: Chain "F" 1 - 47 The following residues NOT assigned to any domain: Chain "F" 951 - 952 The following residues NOT assigned to any domain: Chain "F" 1 - 180 The following residues NOT assigned to any domain: Chain "F" 2 - 48 The following residues NOT assigned to any domain: Chain "F" 961 - 961 The following residues NOT assigned to any domain: Chain "F" 1 - 180 The following residues NOT assigned to any domain: Chain "F" 971 - 972 The following residues NOT assigned to any domain: Chain "F" 1 - 180 The following residues NOT assigned to any domain: Chain "F" 2 - 48 The following residues NOT assigned to any domain: Chain "F" 981 - 982
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOC H

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]H 2 to H 48 ; The following residues NOT assigned to any domain: Chain "H" 1 - 180 The following residues NOT assigned to any domain: Chain "H" 1 - 47 The following residues NOT assigned to any domain: Chain "H" 951 - 952 The following residues NOT assigned to any domain: Chain "H" 1 - 180 The following residues NOT assigned to any domain: Chain "H" 2 - 48 The following residues NOT assigned to any domain: Chain "H" 961 - 961 The following residues NOT assigned to any domain: Chain "H" 1 - 180 The following residues NOT assigned to any domain: Chain "H" 1 - 47 The following residues NOT assigned to any domain: Chain "H" 971 - 972 The following residues NOT assigned to any domain: Chain "H" 1 - 180 The following residues NOT assigned to any domain: Chain "H" 981 - 982
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOD B

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]B 1 to B 47 ; The following residues NOT assigned to any domain: Chain "B" 1 - 180 The following residues NOT assigned to any domain: Chain "B" 1 - 180 The following residues NOT assigned to any domain: Chain "B" 2 - 48 The following residues NOT assigned to any domain: Chain "B" 1 - 180 The following residues NOT assigned to any domain: Chain "B" 1 - 47 The following residues NOT assigned to any domain: Chain "B" 1 - 180 The following residues NOT assigned to any domain: Chain "B" 2 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOD D

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]D 2 to D 48 ; The following residues NOT assigned to any domain: Chain "D" 1 - 180 The following residues NOT assigned to any domain: Chain "D" 1 - 47 The following residues NOT assigned to any domain: Chain "D" 1 - 180 The following residues NOT assigned to any domain: Chain "D" 1 - 180 The following residues NOT assigned to any domain: Chain "D" 1 - 47 The following residues NOT assigned to any domain: Chain "D" 1 - 180 The following residues NOT assigned to any domain: Chain "D" 2 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOD F

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]F 1 to F 47 ; The following residues NOT assigned to any domain: Chain "F" 1 - 180 The following residues NOT assigned to any domain: Chain "F" 1 - 47 The following residues NOT assigned to any domain: Chain "F" 1 - 180 The following residues NOT assigned to any domain: Chain "F" 2 - 48 The following residues NOT assigned to any domain: Chain "F" 1 - 180 The following residues NOT assigned to any domain: Chain "F" 1 - 180 The following residues NOT assigned to any domain: Chain "F" 2 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOD H

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]H 2 to H 48 ; The following residues NOT assigned to any domain: Chain "H" 1 - 180 The following residues NOT assigned to any domain: Chain "H" 1 - 47 The following residues NOT assigned to any domain: Chain "H" 1 - 180 The following residues NOT assigned to any domain: Chain "H" 2 - 48 The following residues NOT assigned to any domain: Chain "H" 1 - 180 The following residues NOT assigned to any domain: Chain "H" 1 - 47 The following residues NOT assigned to any domain: Chain "H" 1 - 180
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOE B

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I)

DOMAIN 1: [Assigned by homology with 2LALA]B 2 to B 47 ; The following residues NOT assigned to any domain: Chain "B" 1 - 180 The following residues NOT assigned to any domain: Chain "B" 1 - 181 The following residues NOT assigned to any domain: Chain "B" 1 - 47
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOE D

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I)

DOMAIN 1: [Assigned by homology with 2LALA]D 1 to D 47 ; The following residues NOT assigned to any domain: Chain "D" 1 - 180 The following residues NOT assigned to any domain: Chain "D" 2 - 47 The following residues NOT assigned to any domain: Chain "D" 1 - 181
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOF B

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]B 1 to B 47 ; The following residues NOT assigned to any domain: Chain "B" 1 - 181 The following residues NOT assigned to any domain: Chain "B" 1 - 180 The following residues NOT assigned to any domain: Chain "B" 1 - 52
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOF D

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]D 1 to D 52 ; The following residues NOT assigned to any domain: Chain "D" 1 - 181 The following residues NOT assigned to any domain: Chain "D" 1 - 47 The following residues NOT assigned to any domain: Chain "D" 1 - 180
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOG B

LECTIN 27-JAN-94 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH A TRIS

DOMAIN 1: [Assigned by homology with 2LALA]B 2 to B 47 ; The following residues NOT assigned to any domain: Chain "B" 1 - 180 The following residues NOT assigned to any domain: Chain "B" 1 - 181 The following residues NOT assigned to any domain: Chain "B" 1 - 51
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOG D

LECTIN 27-JAN-94 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH A TRIS

DOMAIN 1: [Assigned by homology with 2LALA]D 1 to D 51 ; The following residues NOT assigned to any domain: Chain "D" 1 - 180 The following residues NOT assigned to any domain: Chain "D" 2 - 47 The following residues NOT assigned to any domain: Chain "D" 1 - 181
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CN1 A

LECTIN (AGGLUTININ) 21-DEC-81 :: CONCANAVALIN A (DEMETALLIZED)

DOMAIN 1: [Assigned by homology with 2LALA]A 1 to A 227 ; The following residues NOT assigned to any domain: Chain "A" 228 - 237 The following residues NOT assigned to any domain: Chain "A" 1 - 237
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CN1 B

LECTIN (AGGLUTININ) 21-DEC-81 :: CONCANAVALIN A (DEMETALLIZED)

DOMAIN 1: [Assigned by homology with 2LALA]B 1 to B 227 ; The following residues NOT assigned to any domain: Chain "B" 1 - 237 The following residues NOT assigned to any domain: Chain "B" 228 - 237
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CNA

LECTIN (AGGLUTININ) 01-APR-75 :: CONCANAVALIN A

DOMAIN 1: [Assigned by homology with 2LALA] 1 to 227 ; The following residues NOT assigned to any domain: Chain " " 228 - 237
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3CNA

LECTIN (AGGLUTININ) 15-SEP-76 :: CONCANAVALIN A

DOMAIN 1: [Assigned by homology with 2LALA] 1 to 227 ; The following residues NOT assigned to any domain: Chain " " 228 - 237
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5CNA A

LECTIN(AGGLUTININ) 11-FEB-94 :: CONCANAVALIN A COMPLEXED WITH ALPHA-METHYL-D-MANNO

DOMAIN 1: [Assigned by homology with 2LALA]A 1 to A 227 ; The following residues NOT assigned to any domain: Chain "A" 228 - 237 The following residues NOT assigned to any domain: Chain "A" 1 - 237 The following residues NOT assigned to any domain: Chain "A" 1 - 237 The following residues NOT assigned to any domain: Chain "A" 1 - 237
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5CNA B

LECTIN(AGGLUTININ) 11-FEB-94 :: CONCANAVALIN A COMPLEXED WITH ALPHA-METHYL-D-MANNO

DOMAIN 1: [Assigned by homology with 2LALA]B 1 to B 227 ; The following residues NOT assigned to any domain: Chain "B" 1 - 237 The following residues NOT assigned to any domain: Chain "B" 228 - 237 The following residues NOT assigned to any domain: Chain "B" 1 - 237 The following residues NOT assigned to any domain: Chain "B" 1 - 237
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5CNA C

LECTIN(AGGLUTININ) 11-FEB-94 :: CONCANAVALIN A COMPLEXED WITH ALPHA-METHYL-D-MANNO

DOMAIN 1: [Assigned by homology with 2LALA]C 1 to C 227 ; The following residues NOT assigned to any domain: Chain "C" 1 - 237 The following residues NOT assigned to any domain: Chain "C" 1 - 237 The following residues NOT assigned to any domain: Chain "C" 228 - 237 The following residues NOT assigned to any domain: Chain "C" 1 - 237
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5CNA D

LECTIN(AGGLUTININ) 11-FEB-94 :: CONCANAVALIN A COMPLEXED WITH ALPHA-METHYL-D-MANNO

DOMAIN 1: [Assigned by homology with 2LALA]D 1 to D 227 ; The following residues NOT assigned to any domain: Chain "D" 1 - 237 The following residues NOT assigned to any domain: Chain "D" 1 - 237 The following residues NOT assigned to any domain: Chain "D" 1 - 237 The following residues NOT assigned to any domain: Chain "D" 228 - 237
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SCR

LECTIN(AGGLUTININ) 06-DEC-93 :: CONCANAVALIN A (NICKEL SUBSTITUTED FOR MANGANESE)

DOMAIN 1: [Assigned by homology with 2LALA] 1 to 227 ; The following residues NOT assigned to any domain: Chain " " 228 - 237
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SCS

LECTIN(AGGLUTININ) 06-DEC-93 :: CONCANAVALIN A (COBALT SUBSTITUTED FOR MANGANESE)

DOMAIN 1: [Assigned by homology with 2LALA] 1 to 227 ; The following residues NOT assigned to any domain: Chain " " 228 - 237
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CON A

PRELIMINARY 16-MAR-93 :: CONCANAVALIN A CADMIUM SUBSTITUTED FOR MANGANESE

DOMAIN 1: [Assigned by homology with 2LALA]A 1 to A 227 ; The following residues NOT assigned to any domain: Chain " " 1 - 237
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CTV A

LECTIN 10-AUG-93 :: CONCANAVALIN A (NATIVE)

DOMAIN 1: [Assigned by homology with 2LALA]A 1 to A 227 ; The following residues NOT assigned to any domain: Chain "A" 228 - 237
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LEC

PRELIMINARY 17-DEC-92 :: FOURTH LECTIN ISOLATED FROM GRIFFONIA SIMPLICIFOLI

DOMAIN 1: [Assigned by homology with 2LALA] 1 to 243 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LED

PRELIMINARY 17-DEC-92 :: COMPLEX OF GS4 WITH LEWIS B HUMAN BLOOD GROUP DETE

DOMAIN 1: [Assigned by homology with 2LALA] 1 to 243 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LTE

PRELIMINARY 25-JUN-91 :: LECTIN COMPLEX WITH LACTOSE

DOMAIN 1: [Assigned by homology with 2LALA] 1 to 230 ; The following residues NOT assigned to any domain: Chain " " 231 - 239
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LGC E

LECTIN 07-JAN-94 :: LEGUME ISOLECTIN II (LOL II) COMPLEXED WITH A HUMA

DOMAIN 1: [Assigned by homology with 2LALA]E 1 to E 180 ; The following residues NOT assigned to any domain: Chain "E" 1 - 181 The following residues NOT assigned to any domain: Chain "E" 512 - 512 The following residues NOT assigned to any domain: Chain "E" 1 - 51 The following residues NOT assigned to any domain: Chain "E" 1 - 181 The following residues NOT assigned to any domain: Chain "E" 512 - 512 The following residues NOT assigned to any domain: Chain "E" 1 - 48 The following residues NOT assigned to any domain: Chain "E" 181 - 181 The following residues NOT assigned to any domain: Chain "E" 512 - 513 The following residues NOT assigned to any domain: Chain "E" 2 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RIN A

LECTIN 27-JAN-93 :: PEA LECTIN COMPLEX WITH METHYL-3,6-DI-O-

DOMAIN 1: [Assigned by homology with 2LALA]A 1 to A 180 ; The following residues NOT assigned to any domain: Chain "A" 188 - 234 The following residues NOT assigned to any domain: Chain "A" 1 - 180 The following residues NOT assigned to any domain: Chain "A" 188 - 236
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RIN C

LECTIN 27-JAN-93 :: PEA LECTIN COMPLEX WITH METHYL-3,6-DI-O-

DOMAIN 1: [Assigned by homology with 2LALA]C 1 to C 180 ; The following residues NOT assigned to any domain: Chain "C" 1 - 180 The following residues NOT assigned to any domain: Chain "C" 188 - 234 The following residues NOT assigned to any domain: Chain "C" 188 - 236
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2LTN A

LECTIN 26-JUN-90 :: PEA LECTIN

DOMAIN 1: [Assigned by homology with 2LALA]A 1 to A 180 ; The following residues NOT assigned to any domain: Chain "A" 181 - 181 The following residues NOT assigned to any domain: Chain "A" 1 - 48 The following residues NOT assigned to any domain: Chain "A" 1 - 181 The following residues NOT assigned to any domain: Chain "A" 1 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2LTN C

LECTIN 26-JUN-90 :: PEA LECTIN

DOMAIN 1: [Assigned by homology with 2LALA]C 1 to C 180 ; The following residues NOT assigned to any domain: Chain "C" 1 - 181 The following residues NOT assigned to any domain: Chain "C" 1 - 48 The following residues NOT assigned to any domain: Chain "C" 181 - 181 The following residues NOT assigned to any domain: Chain "C" 1 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOA A

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]A 1 to A 180 ; The following residues NOT assigned to any domain: Chain "A" 1 - 47 The following residues NOT assigned to any domain: Chain "A" 1 - 180 The following residues NOT assigned to any domain: Chain "A" 2 - 48 The following residues NOT assigned to any domain: Chain "A" 1 - 180 The following residues NOT assigned to any domain: Chain "A" 1 - 47 The following residues NOT assigned to any domain: Chain "A" 1 - 180 The following residues NOT assigned to any domain: Chain "A" 2 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOA C

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]C 1 to C 180 ; The following residues NOT assigned to any domain: Chain "C" 1 - 180 The following residues NOT assigned to any domain: Chain "C" 1 - 47 The following residues NOT assigned to any domain: Chain "C" 2 - 48 The following residues NOT assigned to any domain: Chain "C" 1 - 180 The following residues NOT assigned to any domain: Chain "C" 1 - 47 The following residues NOT assigned to any domain: Chain "C" 1 - 180 The following residues NOT assigned to any domain: Chain "C" 2 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOA E

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]E 1 to E 180 ; The following residues NOT assigned to any domain: Chain "E" 1 - 180 The following residues NOT assigned to any domain: Chain "E" 1 - 47 The following residues NOT assigned to any domain: Chain "E" 1 - 180 The following residues NOT assigned to any domain: Chain "E" 2 - 48 The following residues NOT assigned to any domain: Chain "E" 1 - 47 The following residues NOT assigned to any domain: Chain "E" 1 - 180 The following residues NOT assigned to any domain: Chain "E" 2 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOA G

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]G 1 to G 180 ; The following residues NOT assigned to any domain: Chain "G" 1 - 180 The following residues NOT assigned to any domain: Chain "G" 1 - 47 The following residues NOT assigned to any domain: Chain "G" 1 - 180 The following residues NOT assigned to any domain: Chain "G" 2 - 48 The following residues NOT assigned to any domain: Chain "G" 1 - 180 The following residues NOT assigned to any domain: Chain "G" 1 - 47 The following residues NOT assigned to any domain: Chain "G" 2 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOB A

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]A 1 to A 180 ; The following residues NOT assigned to any domain: Chain "A" 1 - 47 The following residues NOT assigned to any domain: Chain "A" 1 - 180 The following residues NOT assigned to any domain: Chain "A" 2 - 48 The following residues NOT assigned to any domain: Chain "A" 1 - 180 The following residues NOT assigned to any domain: Chain "A" 1 - 47 The following residues NOT assigned to any domain: Chain "A" 1 - 180 The following residues NOT assigned to any domain: Chain "A" 2 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOB C

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]C 1 to C 180 ; The following residues NOT assigned to any domain: Chain "C" 1 - 180 The following residues NOT assigned to any domain: Chain "C" 1 - 47 The following residues NOT assigned to any domain: Chain "C" 2 - 48 The following residues NOT assigned to any domain: Chain "C" 1 - 180 The following residues NOT assigned to any domain: Chain "C" 1 - 47 The following residues NOT assigned to any domain: Chain "C" 1 - 180 The following residues NOT assigned to any domain: Chain "C" 2 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOB E

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]E 1 to E 180 ; The following residues NOT assigned to any domain: Chain "E" 1 - 180 The following residues NOT assigned to any domain: Chain "E" 1 - 47 The following residues NOT assigned to any domain: Chain "E" 1 - 180 The following residues NOT assigned to any domain: Chain "E" 2 - 48 The following residues NOT assigned to any domain: Chain "E" 1 - 47 The following residues NOT assigned to any domain: Chain "E" 1 - 180 The following residues NOT assigned to any domain: Chain "E" 2 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOB G

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]G 1 to G 180 ; The following residues NOT assigned to any domain: Chain "G" 1 - 180 The following residues NOT assigned to any domain: Chain "G" 1 - 47 The following residues NOT assigned to any domain: Chain "G" 1 - 180 The following residues NOT assigned to any domain: Chain "G" 2 - 48 The following residues NOT assigned to any domain: Chain "G" 1 - 180 The following residues NOT assigned to any domain: Chain "G" 1 - 47 The following residues NOT assigned to any domain: Chain "G" 2 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOC A

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]A 1 to A 180 ; The following residues NOT assigned to any domain: Chain "A" 1 - 47 The following residues NOT assigned to any domain: Chain "A" 951 - 952 The following residues NOT assigned to any domain: Chain "A" 1 - 180 The following residues NOT assigned to any domain: Chain "A" 2 - 48 The following residues NOT assigned to any domain: Chain "A" 961 - 961 The following residues NOT assigned to any domain: Chain "A" 1 - 180 The following residues NOT assigned to any domain: Chain "A" 1 - 47 The following residues NOT assigned to any domain: Chain "A" 971 - 972 The following residues NOT assigned to any domain: Chain "A" 1 - 180 The following residues NOT assigned to any domain: Chain "A" 2 - 48 The following residues NOT assigned to any domain: Chain "A" 981 - 982
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOC C

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]C 1 to C 180 ; The following residues NOT assigned to any domain: Chain "C" 1 - 180 The following residues NOT assigned to any domain: Chain "C" 1 - 47 The following residues NOT assigned to any domain: Chain "C" 951 - 952 The following residues NOT assigned to any domain: Chain "C" 2 - 48 The following residues NOT assigned to any domain: Chain "C" 961 - 961 The following residues NOT assigned to any domain: Chain "C" 1 - 180 The following residues NOT assigned to any domain: Chain "C" 1 - 47 The following residues NOT assigned to any domain: Chain "C" 971 - 972 The following residues NOT assigned to any domain: Chain "C" 1 - 180 The following residues NOT assigned to any domain: Chain "C" 2 - 48 The following residues NOT assigned to any domain: Chain "C" 981 - 982
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOC E

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]E 1 to E 180 ; The following residues NOT assigned to any domain: Chain "E" 1 - 180 The following residues NOT assigned to any domain: Chain "E" 1 - 47 The following residues NOT assigned to any domain: Chain "E" 951 - 952 The following residues NOT assigned to any domain: Chain "E" 1 - 180 The following residues NOT assigned to any domain: Chain "E" 2 - 48 The following residues NOT assigned to any domain: Chain "E" 961 - 961 The following residues NOT assigned to any domain: Chain "E" 1 - 47 The following residues NOT assigned to any domain: Chain "E" 971 - 972 The following residues NOT assigned to any domain: Chain "E" 1 - 180 The following residues NOT assigned to any domain: Chain "E" 2 - 48 The following residues NOT assigned to any domain: Chain "E" 981 - 982
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOC G

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]G 1 to G 180 ; The following residues NOT assigned to any domain: Chain "G" 1 - 180 The following residues NOT assigned to any domain: Chain "G" 1 - 47 The following residues NOT assigned to any domain: Chain "G" 951 - 952 The following residues NOT assigned to any domain: Chain "G" 1 - 180 The following residues NOT assigned to any domain: Chain "G" 2 - 48 The following residues NOT assigned to any domain: Chain "G" 961 - 961 The following residues NOT assigned to any domain: Chain "G" 1 - 180 The following residues NOT assigned to any domain: Chain "G" 1 - 47 The following residues NOT assigned to any domain: Chain "G" 971 - 972 The following residues NOT assigned to any domain: Chain "G" 2 - 48 The following residues NOT assigned to any domain: Chain "G" 981 - 982
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOD A

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]A 1 to A 180 ; The following residues NOT assigned to any domain: Chain "A" 1 - 47 The following residues NOT assigned to any domain: Chain "A" 1 - 180 The following residues NOT assigned to any domain: Chain "A" 2 - 48 The following residues NOT assigned to any domain: Chain "A" 1 - 180 The following residues NOT assigned to any domain: Chain "A" 1 - 47 The following residues NOT assigned to any domain: Chain "A" 1 - 180 The following residues NOT assigned to any domain: Chain "A" 2 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOD C

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]C 1 to C 180 ; The following residues NOT assigned to any domain: Chain "C" 1 - 180 The following residues NOT assigned to any domain: Chain "C" 1 - 47 The following residues NOT assigned to any domain: Chain "C" 2 - 48 The following residues NOT assigned to any domain: Chain "C" 1 - 180 The following residues NOT assigned to any domain: Chain "C" 1 - 47 The following residues NOT assigned to any domain: Chain "C" 1 - 180 The following residues NOT assigned to any domain: Chain "C" 2 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOD E

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]E 1 to E 180 ; The following residues NOT assigned to any domain: Chain "E" 1 - 180 The following residues NOT assigned to any domain: Chain "E" 1 - 47 The following residues NOT assigned to any domain: Chain "E" 1 - 180 The following residues NOT assigned to any domain: Chain "E" 2 - 48 The following residues NOT assigned to any domain: Chain "E" 1 - 47 The following residues NOT assigned to any domain: Chain "E" 1 - 180 The following residues NOT assigned to any domain: Chain "E" 2 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOD G

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]G 1 to G 180 ; The following residues NOT assigned to any domain: Chain "G" 1 - 180 The following residues NOT assigned to any domain: Chain "G" 1 - 47 The following residues NOT assigned to any domain: Chain "G" 1 - 180 The following residues NOT assigned to any domain: Chain "G" 2 - 48 The following residues NOT assigned to any domain: Chain "G" 1 - 180 The following residues NOT assigned to any domain: Chain "G" 1 - 47 The following residues NOT assigned to any domain: Chain "G" 2 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOE A

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I)

DOMAIN 1: [Assigned by homology with 2LALA]A 1 to A 180 ; The following residues NOT assigned to any domain: Chain "A" 2 - 47 The following residues NOT assigned to any domain: Chain "A" 1 - 181 The following residues NOT assigned to any domain: Chain "A" 1 - 47
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOF C

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]C 1 to C 180 ; The following residues NOT assigned to any domain: Chain "C" 1 - 181 The following residues NOT assigned to any domain: Chain "C" 1 - 47 The following residues NOT assigned to any domain: Chain "C" 1 - 52
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOG A

LECTIN 27-JAN-94 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH A TRIS

DOMAIN 1: [Assigned by homology with 2LALA]A 1 to A 180 ; The following residues NOT assigned to any domain: Chain "A" 2 - 47 The following residues NOT assigned to any domain: Chain "A" 1 - 181 The following residues NOT assigned to any domain: Chain "A" 1 - 51
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LEM A

LECTIN 17-NOV-93 :: LECTIN (LENTIL) (HEXAGONAL CRYSTAL FORM)

DOMAIN 1: [Assigned by homology with 2LALA]A 1 to A 180 ; The following residues NOT assigned to any domain: Chain "A" 181 - 181 The following residues NOT assigned to any domain: Chain "A" 1 - 47
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LEN A

LECTIN 17-NOV-93 :: LECTIN (LENTIL) (MONOCLINIC CRYSTAL FORM)

DOMAIN 1: [Assigned by homology with 2LALA]A 1 to A 180 ; The following residues NOT assigned to any domain: Chain "A" 181 - 181 The following residues NOT assigned to any domain: Chain "A" 1 - 47 The following residues NOT assigned to any domain: Chain "A" 1 - 181 The following residues NOT assigned to any domain: Chain "A" 1 - 47
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LEN C

LECTIN 17-NOV-93 :: LECTIN (LENTIL) (MONOCLINIC CRYSTAL FORM)

DOMAIN 1: [Assigned by homology with 2LALA]C 1 to C 180 ; The following residues NOT assigned to any domain: Chain "C" 1 - 181 The following residues NOT assigned to any domain: Chain "C" 1 - 47 The following residues NOT assigned to any domain: Chain "C" 181 - 181 The following residues NOT assigned to any domain: Chain "C" 1 - 47
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LGB A

COMPLEX(LECTIN/TRANSFERRIN) 07-JAN-94 :: LEGUME ISOLECTIN II (LOL II) COMPLEXED WITH LACTOT

DOMAIN 1: [Assigned by homology with 2LALA]A 1 to A 180 ; The following residues NOT assigned to any domain: Chain "A" 181 - 181 The following residues NOT assigned to any domain: Chain "A" 2 - 48 The following residues NOT assigned to any domain: Chain "A" 91 - 249
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LGC A

LECTIN 07-JAN-94 :: LEGUME ISOLECTIN II (LOL II) COMPLEXED WITH A HUMA

DOMAIN 1: [Assigned by homology with 2LALA]A 1 to A 180 ; The following residues NOT assigned to any domain: Chain "A" 181 - 181 The following residues NOT assigned to any domain: Chain "A" 512 - 512 The following residues NOT assigned to any domain: Chain "A" 1 - 51 The following residues NOT assigned to any domain: Chain "A" 1 - 181 The following residues NOT assigned to any domain: Chain "A" 512 - 512 The following residues NOT assigned to any domain: Chain "A" 1 - 48 The following residues NOT assigned to any domain: Chain "A" 1 - 181 The following residues NOT assigned to any domain: Chain "A" 512 - 513 The following residues NOT assigned to any domain: Chain "A" 2 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LGC C

LECTIN 07-JAN-94 :: LEGUME ISOLECTIN II (LOL II) COMPLEXED WITH A HUMA

DOMAIN 1: [Assigned by homology with 2LALA]C 1 to C 180 ; The following residues NOT assigned to any domain: Chain "C" 1 - 181 The following residues NOT assigned to any domain: Chain "C" 512 - 512 The following residues NOT assigned to any domain: Chain "C" 1 - 51 The following residues NOT assigned to any domain: Chain "C" 181 - 181 The following residues NOT assigned to any domain: Chain "C" 512 - 512 The following residues NOT assigned to any domain: Chain "C" 1 - 48 The following residues NOT assigned to any domain: Chain "C" 1 - 181 The following residues NOT assigned to any domain: Chain "C" 512 - 513 The following residues NOT assigned to any domain: Chain "C" 2 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2LAL C

LECTIN 10-JUN-93 :: LENTIL LECTIN

DOMAIN 1: [Assigned by homology with 2LALA]C 1 to C 180 ; The following residues NOT assigned to any domain: Chain "C" 1 - 181 The following residues NOT assigned to any domain: Chain "C" 1 - 47 The following residues NOT assigned to any domain: Chain "C" 181 - 181 The following residues NOT assigned to any domain: Chain "C" 1 - 47
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOE C

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I)

DOMAIN 1: [Assigned by homology with 2LALA]C 1 to C 180 ; The following residues NOT assigned to any domain: Chain "C" 1 - 180 The following residues NOT assigned to any domain: Chain "C" 2 - 47 The following residues NOT assigned to any domain: Chain "C" 181 - 181 The following residues NOT assigned to any domain: Chain "C" 1 - 47
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOF A

LECTIN 27-JAN-93 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 2LALA]A 1 to A 180 ; The following residues NOT assigned to any domain: Chain "A" 181 - 181 The following residues NOT assigned to any domain: Chain "A" 1 - 47 The following residues NOT assigned to any domain: Chain "A" 1 - 180 The following residues NOT assigned to any domain: Chain "A" 1 - 52
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LOG C

LECTIN 27-JAN-94 :: LECTIN (LEGUME, ISOLECTIN I) COMPLEXED WITH A TRIS

DOMAIN 1: [Assigned by homology with 2LALA]C 1 to C 180 ; The following residues NOT assigned to any domain: Chain "C" 1 - 180 The following residues NOT assigned to any domain: Chain "C" 2 - 47 The following residues NOT assigned to any domain: Chain "C" 181 - 181 The following residues NOT assigned to any domain: Chain "C" 1 - 51
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HRB

OXYGEN TRANSPORT 23-JUN-76 :: HEMERYTHRIN B

DOMAIN 1: 1 to 113 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HMD A

OXYGEN TRANSPORT 18-OCT-90 :: HEMERYTHRIN (DEOXY)

DOMAIN 1: A 1 to A 113 ; The following residues NOT assigned to any domain: Chain "A" 1 - 113 The following residues NOT assigned to any domain: Chain "A" 1 - 113 The following residues NOT assigned to any domain: Chain "A" 1 - 113
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HMD B

OXYGEN TRANSPORT 18-OCT-90 :: HEMERYTHRIN (DEOXY)

DOMAIN 1: B 1 to B 113 ; The following residues NOT assigned to any domain: Chain "B" 1 - 113 The following residues NOT assigned to any domain: Chain "B" 1 - 113 The following residues NOT assigned to any domain: Chain "B" 1 - 113
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HMD C

OXYGEN TRANSPORT 18-OCT-90 :: HEMERYTHRIN (DEOXY)

DOMAIN 1: C 1 to C 113 ; The following residues NOT assigned to any domain: Chain "C" 1 - 113 The following residues NOT assigned to any domain: Chain "C" 1 - 113 The following residues NOT assigned to any domain: Chain "C" 1 - 113
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HMD D

OXYGEN TRANSPORT 18-OCT-90 :: HEMERYTHRIN (DEOXY)

DOMAIN 1: D 1 to D 113 ; The following residues NOT assigned to any domain: Chain "D" 1 - 113 The following residues NOT assigned to any domain: Chain "D" 1 - 113 The following residues NOT assigned to any domain: Chain "D" 1 - 113
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HMO A

OXYGEN TRANSPORT 18-OCT-90 :: HEMERYTHRIN (OXY)

DOMAIN 1: A 1 to A 113 ; The following residues NOT assigned to any domain: Chain "A" 1 - 113 The following residues NOT assigned to any domain: Chain "A" 1 - 113 The following residues NOT assigned to any domain: Chain "A" 1 - 113
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HMO B

OXYGEN TRANSPORT 18-OCT-90 :: HEMERYTHRIN (OXY)

DOMAIN 1: B 1 to B 113 ; The following residues NOT assigned to any domain: Chain "B" 1 - 113 The following residues NOT assigned to any domain: Chain "B" 1 - 113 The following residues NOT assigned to any domain: Chain "B" 1 - 113
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HMO C

OXYGEN TRANSPORT 18-OCT-90 :: HEMERYTHRIN (OXY)

DOMAIN 1: C 1 to C 113 ; The following residues NOT assigned to any domain: Chain "C" 1 - 113 The following residues NOT assigned to any domain: Chain "C" 1 - 113 The following residues NOT assigned to any domain: Chain "C" 1 - 113
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HMO D

OXYGEN TRANSPORT 18-OCT-90 :: HEMERYTHRIN (OXY)

DOMAIN 1: D 1 to D 113 ; The following residues NOT assigned to any domain: Chain "D" 1 - 113 The following residues NOT assigned to any domain: Chain "D" 1 - 113 The following residues NOT assigned to any domain: Chain "D" 1 - 113
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HMQ A

OXYGEN TRANSPORT 18-OCT-90 :: HEMERYTHRIN (MET)

DOMAIN 1: A 1 to A 113 ; The following residues NOT assigned to any domain: Chain "A" 1 - 113 The following residues NOT assigned to any domain: Chain "A" 1 - 113 The following residues NOT assigned to any domain: Chain "A" 1 - 113
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HMQ B

OXYGEN TRANSPORT 18-OCT-90 :: HEMERYTHRIN (MET)

DOMAIN 1: B 1 to B 113 ; The following residues NOT assigned to any domain: Chain "B" 1 - 113 The following residues NOT assigned to any domain: Chain "B" 1 - 113 The following residues NOT assigned to any domain: Chain "B" 1 - 113
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HMQ C

OXYGEN TRANSPORT 18-OCT-90 :: HEMERYTHRIN (MET)

DOMAIN 1: C 1 to C 113 ; The following residues NOT assigned to any domain: Chain "C" 1 - 113 The following residues NOT assigned to any domain: Chain "C" 1 - 113 The following residues NOT assigned to any domain: Chain "C" 1 - 113
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HMQ D

OXYGEN TRANSPORT 18-OCT-90 :: HEMERYTHRIN (MET)

DOMAIN 1: D 1 to D 113 ; The following residues NOT assigned to any domain: Chain "D" 1 - 113 The following residues NOT assigned to any domain: Chain "D" 1 - 113 The following residues NOT assigned to any domain: Chain "D" 1 - 113
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HMZ A

OXYGEN TRANSPORT 18-OCT-90 :: HEMERYTHRIN (ADIZOMET)

DOMAIN 1: A 1 to A 113 ; The following residues NOT assigned to any domain: Chain "A" 1 - 113 The following residues NOT assigned to any domain: Chain "A" 1 - 113 The following residues NOT assigned to any domain: Chain "A" 1 - 113
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HMZ B

OXYGEN TRANSPORT 18-OCT-90 :: HEMERYTHRIN (ADIZOMET)

DOMAIN 1: B 1 to B 113 ; The following residues NOT assigned to any domain: Chain "B" 1 - 113 The following residues NOT assigned to any domain: Chain "B" 1 - 113 The following residues NOT assigned to any domain: Chain "B" 1 - 113
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HMZ C

OXYGEN TRANSPORT 18-OCT-90 :: HEMERYTHRIN (ADIZOMET)

DOMAIN 1: C 1 to C 113 ; The following residues NOT assigned to any domain: Chain "C" 1 - 113 The following residues NOT assigned to any domain: Chain "C" 1 - 113 The following residues NOT assigned to any domain: Chain "C" 1 - 113
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HMZ D

OXYGEN TRANSPORT 18-OCT-90 :: HEMERYTHRIN (ADIZOMET)

DOMAIN 1: D 1 to D 113 ; The following residues NOT assigned to any domain: Chain "D" 1 - 113 The following residues NOT assigned to any domain: Chain "D" 1 - 113 The following residues NOT assigned to any domain: Chain "D" 1 - 113
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MSB B

LECTIN 28-JUL-92 :: MANNOSE-BINDING PROTEIN A (LECTIN DOMAIN) COMPLEX

DOMAIN 1: [Assigned by homology with 2MSBA]B 109 to B 219 ; The following residues NOT assigned to any domain: Chain "B" 109 - 220 The following residues NOT assigned to any domain: Chain "B" 220 - 221
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MSB A

HEPATIC LECTIN 23-SEP-91 :: MANNOSE BINDING PROTEIN *A (LECTIN DOMAIN) COMPLEX

DOMAIN 1: [Assigned by homology with 2MSBA]A 107 to A 219 ; The following residues NOT assigned to any domain: Chain "A" 220 - 221 The following residues NOT assigned to any domain: Chain "A" 107 - 221
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MSB B

HEPATIC LECTIN 23-SEP-91 :: MANNOSE BINDING PROTEIN *A (LECTIN DOMAIN) COMPLEX

DOMAIN 1: [Assigned by homology with 2MSBA]B 107 to B 219 ; The following residues NOT assigned to any domain: Chain "B" 107 - 221 The following residues NOT assigned to any domain: Chain "B" 220 - 221
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HLJ

PRELIMINARY 18-JUN-93 :: MURINE LOW-AFFINITY IGE RECEPTOR (FCERII/CD23) LEC

DOMAIN 1: [Assigned by homology with 2MSBA] 173 to 284 ; The following residues NOT assigned to any domain: Chain " " 285 - 285
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HLI

PRELIMINARY 18-JUN-93 :: HUMAN LOW-AFFINITY IGE RECEPTOR (FCERII/CD23) LECT

DOMAIN 1: [Assigned by homology with 2MSBA] 173 to 284 ; The following residues NOT assigned to any domain: Chain " " 285 - 285
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3POR

INTEGRAL MEMBRANE PROTEIN PORIN 09-NOV-92 :: PORIN (CRYSTAL FORM A')

DOMAIN 1: 1 to 301 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2SCP B

BINDING PROTEIN 22-AUG-91 :: SARCOPLASMIC CALCIUM-BINDING PROTEIN

DOMAIN 1: [Assigned by homology with 2SCPA]B 1 to B 174 ; The following residues NOT assigned to any domain: Chain "B" 1 - 174
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1VTM P

VIRUS 30-MAR-92 :: TOBACCO MOSAIC VIRUS, STRAIN U2 (FIBER DIFFRACTION

DOMAIN 1: [Assigned by homology with 2TMVP]P 1 to P 154 ; The following residues NOT assigned to any domain: Chain "P" 155 - 158 The following residues NOT assigned to any domain: Chain "P" 1 - 3
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CGM E

VIRUS 17-NOV-93 :: CUCUMBER GREEN MOTTLE MOSAIC VIRUS (CGMMV), WATERM

DOMAIN 1: [Assigned by homology with 2TMVP]E 1 to E 154 ; The following residues NOT assigned to any domain: Chain "E" 0 - 0 Chain "E" 155 - 160 The following residues NOT assigned to any domain: Chain "E" 1 - 3
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CHN

SIGNAL TRANSDUCTION PROTEIN 20-APR-94 :: CHEY COMPLEXED WITH MG2+ IN THE ACTIVE SITE

DOMAIN 1: 4 to 129 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CHE

SIGNAL TRANSDUCTION PROTEIN 17-JAN-94 :: CHEY COMPLEXED WITH MG2+

DOMAIN 1: 2 to 129 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CHF

SIGNAL TRANSDUCTION PROTEIN 17-JAN-94 :: CHEY

DOMAIN 1: 2 to 129 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CHY

SIGNAL TRANSDUCTION PROTEIN 17-MAY-90 :: CHE*Y (MUTANT WITH SER 56 REPLACED BY CYS) (/S56C$

DOMAIN 1: 2 to 129 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4CLA

TRANSFERASE (ACYLTRANSFERASE) 23-OCT-90 :: TYPE /III$ CHLORAMPHENICOL ACETYLTRANSFERASE (/CAT

DOMAIN 1: 6 to 219 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CLA

TRANSFERASE (ACYLTRANSFERASE) 16-OCT-89 :: TYPE /III$ CHLORAMPHENICOL ACETYLTRANSFERASE (/CAT

DOMAIN 1: 6 to 219 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CLA

TRANSFERASE (ACYLTRANSFERASE) 05-APR-90 :: CHLORAMPHENICOL ACETYLTRANSFERASE (E.C.2.3.1.28)

DOMAIN 1: 6 to 219 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CIA

TRANSFERASE(ACYLTRANSFERASE) 19-JUL-93 :: CHLORAMPHENICOL ACETYLTRANSFERASE (TYPE III) (E.C.

DOMAIN 1: 6 to 219 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CGP A

GENE-REGULATORY PROTEIN 12-AUG-91 :: CATABOLITE GENE ACTIVATOR PROTEIN COMPLEX WITH DNA

DOMAIN 1: [Assigned by homology with 3GAPA]A 9 to A 205 ; The following residues NOT assigned to any domain: Chain "A" 9 - 205 The following residues NOT assigned to any domain: Chain "A" 3 - 33 The following residues NOT assigned to any domain: Chain "A" 3 - 33
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CGP B

GENE-REGULATORY PROTEIN 12-AUG-91 :: CATABOLITE GENE ACTIVATOR PROTEIN COMPLEX WITH DNA

DOMAIN 1: [Assigned by homology with 3GAPA]B 9 to B 205 ; The following residues NOT assigned to any domain: Chain "B" 9 - 205 The following residues NOT assigned to any domain: Chain "B" 3 - 33 The following residues NOT assigned to any domain: Chain "B" 3 - 33
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2GAP A

GENE REGULATORY PROTEIN 06-MAR-86 :: CATABOLITE GENE ACTIVATOR PROTEIN - DNA COMPLEX (T

DOMAIN 1: [Assigned by homology with 3GAPA]A 1 to A 208 ; The following residues NOT assigned to any domain: Chain "A" 1 - 205 The following residues NOT assigned to any domain: Chain "A" 1 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3GAP B

GENE REGULATORY PROTEIN 15-APR-87 :: CATABOLITE GENE ACTIVATOR PROTEIN - CYCLIC /AMP$ C

DOMAIN 1: [Assigned by homology with 3GAPA]B 1 to B 205 ; The following residues NOT assigned to any domain: Chain "B" 1 - 208
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2GAP B

GENE REGULATORY PROTEIN 06-MAR-86 :: CATABOLITE GENE ACTIVATOR PROTEIN - DNA COMPLEX (T

DOMAIN 1: [Assigned by homology with 3GAPA]B 1 to B 205 ; The following residues NOT assigned to any domain: Chain "B" 1 - 208 The following residues NOT assigned to any domain: Chain "B" 1 - 48
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RBL M

LYASE(CARBON-CARBON) 12-MAY-93 :: RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE/OXYGENASE

DOMAIN 1: [Assigned by homology with 3RUBS]M 2 to M 122 ; The following residues NOT assigned to any domain: Chain "M" 9 - 475
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8RUB S

LYASE(CARBON-CARBON) 13-NOV-90 :: RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE(SLASH)OXYGEN

DOMAIN 1: [Assigned by homology with 3RUBS]S 1 to S 122 ; The following residues NOT assigned to any domain: Chain "S" 123 - 123 The following residues NOT assigned to any domain: Chain "S" 9 - 475
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RLC S

LYASE(CARBON-CARBON) 04-AUG-93 :: RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE (R

DOMAIN 1: [Assigned by homology with 3RUBS]S 1 to S 122 ; The following residues NOT assigned to any domain: Chain "S" 22 - 467 The following residues NOT assigned to any domain: Chain "S" 123 - 123
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RLD S

LYASE(CARBON-CARBON) 10-DEC-93 :: RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE (R

DOMAIN 1: [Assigned by homology with 3RUBS]S 501 to S 622 ; The following residues NOT assigned to any domain: Chain "S" 22 - 467 The following residues NOT assigned to any domain: Chain "S" 623 - 623 The following residues NOT assigned to any domain: Chain "S" 22 - 467 The following residues NOT assigned to any domain: Chain "S" 501 - 623
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RLD T

LYASE(CARBON-CARBON) 10-DEC-93 :: RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE (R

DOMAIN 1: [Assigned by homology with 3RUBS]T 501 to T 622 ; The following residues NOT assigned to any domain: Chain "T" 22 - 467 The following residues NOT assigned to any domain: Chain "T" 501 - 623 The following residues NOT assigned to any domain: Chain "T" 22 - 467 The following residues NOT assigned to any domain: Chain "T" 623 - 623
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4RUB S

LYASE(CARBON-CARBON) 25-MAY-90 :: RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE(SLASH)OXYGEN

DOMAIN 1: [Assigned by homology with 3RUBS]S 1 to S 122 ; The following residues NOT assigned to any domain: Chain "S" 9 - 473 The following residues NOT assigned to any domain: Chain "S" 123 - 123 The following residues NOT assigned to any domain: Chain "S" 9 - 473 The following residues NOT assigned to any domain: Chain "S" 1 - 123 The following residues NOT assigned to any domain: Chain "S" 9 - 473 The following residues NOT assigned to any domain: Chain "S" 1 - 123 The following residues NOT assigned to any domain: Chain "S" 9 - 473 The following residues NOT assigned to any domain: Chain "S" 1 - 123
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4RUB T

LYASE(CARBON-CARBON) 25-MAY-90 :: RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE(SLASH)OXYGEN

DOMAIN 1: [Assigned by homology with 3RUBS]T 1 to T 122 ; The following residues NOT assigned to any domain: Chain "T" 9 - 473 The following residues NOT assigned to any domain: Chain "T" 1 - 123 The following residues NOT assigned to any domain: Chain "T" 9 - 473 The following residues NOT assigned to any domain: Chain "T" 123 - 123 The following residues NOT assigned to any domain: Chain "T" 9 - 473 The following residues NOT assigned to any domain: Chain "T" 1 - 123 The following residues NOT assigned to any domain: Chain "T" 9 - 473 The following residues NOT assigned to any domain: Chain "T" 1 - 123
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4RUB U

LYASE(CARBON-CARBON) 25-MAY-90 :: RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE(SLASH)OXYGEN

DOMAIN 1: [Assigned by homology with 3RUBS]U 1 to U 122 ; The following residues NOT assigned to any domain: Chain "U" 9 - 473 The following residues NOT assigned to any domain: Chain "U" 1 - 123 The following residues NOT assigned to any domain: Chain "U" 9 - 473 The following residues NOT assigned to any domain: Chain "U" 1 - 123 The following residues NOT assigned to any domain: Chain "U" 9 - 473 The following residues NOT assigned to any domain: Chain "U" 123 - 123 The following residues NOT assigned to any domain: Chain "U" 9 - 473 The following residues NOT assigned to any domain: Chain "U" 1 - 123
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4RUB V

LYASE(CARBON-CARBON) 25-MAY-90 :: RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE(SLASH)OXYGEN

DOMAIN 1: [Assigned by homology with 3RUBS]V 1 to V 122 ; The following residues NOT assigned to any domain: Chain "V" 9 - 473 The following residues NOT assigned to any domain: Chain "V" 1 - 123 The following residues NOT assigned to any domain: Chain "V" 9 - 473 The following residues NOT assigned to any domain: Chain "V" 1 - 123 The following residues NOT assigned to any domain: Chain "V" 9 - 473 The following residues NOT assigned to any domain: Chain "V" 1 - 123 The following residues NOT assigned to any domain: Chain "V" 9 - 473 The following residues NOT assigned to any domain: Chain "V" 123 - 123
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PPF I

PRELIMINARY 24-OCT-91 :: HUMAN LEUKOCYTE ELASTASE, ALSO CALLED NEUTROPHIL E

DOMAIN 1: [Assigned by homology with 3SGBI]I 1 to I 55 ; The following residues NOT assigned to any domain: Chain "I" 16 - 243 The following residues NOT assigned to any domain: Chain "I" 56 - 56
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TUR

SERINE PROTEINASE INHIBITOR 06-JUL-94 :: OVOMUCOID (THIRD DOMAIN) (NMR, 12 STRUCTURES)

DOMAIN 1: [Assigned by homology with 3SGBI] 1 to 55 ; The following residues NOT assigned to any domain: Chain " " 56 - 56
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TUS

SERINE PROTEINASE INHIBITOR 06-JUL-94 :: OVOMUCOID (REACTIVE-SITE HYDROLYZED THIRD DOMAIN)

DOMAIN 1: [Assigned by homology with 3SGBI] 1 to 55 ; The following residues NOT assigned to any domain: Chain " " 56 - 56
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CHO I

COMPLEX(SERINE PROTEINASE-INHIBITOR) 04-MAR-88 :: ALPHA-CHYMOTRYPSIN (E.C.3.4.21.1) COMPLEX WITH TUR

DOMAIN 1: [Assigned by homology with 3SGBI]I 4 to I 55 ; The following residues NOT assigned to any domain: Chain "I" 1 - 146 The following residues NOT assigned to any domain: Chain "I" 149 - 245 The following residues NOT assigned to any domain: Chain "I" 56 - 56
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4OVO

PROTEINASE INHIBITOR (KAZAL) 13-MAY-91 :: OVOMUCOID THIRD DOMAIN CLEAVED RDI

DOMAIN 1: [Assigned by homology with 3SGBI] 1 to 55 ; The following residues NOT assigned to any domain: Chain " " 56 - 56
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2OVO

PROTEINASE INHIBITOR (KAZAL) 11-JUN-85 :: OVOMUCOID THIRD DOMAIN

DOMAIN 1: [Assigned by homology with 3SGBI] 1 to 55 ; The following residues NOT assigned to any domain: Chain " " 56 - 56
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1OVO A

PROTEINASE INHIBITOR (KAZAL) 18-JAN-82 :: OVOMUCOID THIRD DOMAIN

DOMAIN 1: [Assigned by homology with 3SGBI]A 1 to A 55 ; The following residues NOT assigned to any domain: Chain "A" 56 - 56 The following residues NOT assigned to any domain: Chain "A" 1 - 56 The following residues NOT assigned to any domain: Chain "A" 1 - 56 The following residues NOT assigned to any domain: Chain "A" 1 - 56
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1OVO B

PROTEINASE INHIBITOR (KAZAL) 18-JAN-82 :: OVOMUCOID THIRD DOMAIN

DOMAIN 1: [Assigned by homology with 3SGBI]B 1 to B 55 ; The following residues NOT assigned to any domain: Chain "B" 1 - 56 The following residues NOT assigned to any domain: Chain "B" 56 - 56 The following residues NOT assigned to any domain: Chain "B" 1 - 56 The following residues NOT assigned to any domain: Chain "B" 1 - 56
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1OVO C

PROTEINASE INHIBITOR (KAZAL) 18-JAN-82 :: OVOMUCOID THIRD DOMAIN

DOMAIN 1: [Assigned by homology with 3SGBI]C 1 to C 55 ; The following residues NOT assigned to any domain: Chain "C" 1 - 56 The following residues NOT assigned to any domain: Chain "C" 1 - 56 The following residues NOT assigned to any domain: Chain "C" 56 - 56 The following residues NOT assigned to any domain: Chain "C" 1 - 56
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1OVO D

PROTEINASE INHIBITOR (KAZAL) 18-JAN-82 :: OVOMUCOID THIRD DOMAIN

DOMAIN 1: [Assigned by homology with 3SGBI]D 1 to D 55 ; The following residues NOT assigned to any domain: Chain "D" 1 - 56 The following residues NOT assigned to any domain: Chain "D" 1 - 56 The following residues NOT assigned to any domain: Chain "D" 1 - 56 The following residues NOT assigned to any domain: Chain "D" 56 - 56
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3OVO

PROTEINASE INHIBITOR (KAZAL) 13-MAY-91 :: OVOMUCOID THIRD DOMAIN CLEAVED RDI

DOMAIN 1: [Assigned by homology with 3SGBI] 1 to 55 ; The following residues NOT assigned to any domain: Chain " " 56 - 56
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BUS

PROTEINASE INHIBITOR 14-MAY-90 :: PROTEINASE INHIBITOR /IIA$ (/BUSI$ /IIA$) (/NMR$,

DOMAIN 1: [Assigned by homology with 3SGBI] 1 to 56 ; The following residues NOT assigned to any domain: Chain " " 57 - 57
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2BUS

PROTEINASE INHIBITOR 14-MAY-90 :: PROTEINASE INHIBITOR /IIA$ (/BUSI$ /IIA$) (/NMR$,

DOMAIN 1: [Assigned by homology with 3SGBI] 1 to 56 ; The following residues NOT assigned to any domain: Chain " " 57 - 57
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2SIC I

COMPLEX (PROTEINASE/INHIBITOR) 01-APR-91 :: SUBTILISIN /BPN$' (E.C.3.4.21.14) COMPLEX WITH

DOMAIN 1: [Assigned by homology with 3SICI]I 7 to I 112 ; The following residues NOT assigned to any domain: Chain "I" 1 - 275 The following residues NOT assigned to any domain: Chain "I" 113 - 113
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2SSI

PROTEINASE INHIBITOR (SUBTILISIN BPN*) 15-APR-80 :: STREPTOMYCES SUBTILISIN INHIBITOR

DOMAIN 1: [Assigned by homology with 3SICI] 7 to 112 ; The following residues NOT assigned to any domain: Chain " " 113 - 113
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5SIC I

PRELIMINARY 18-NOV-91 :: SUBTILISIN /BPN$' (E.C.3.4.21.14) COMPLEXED WITH A

DOMAIN 1: [Assigned by homology with 3SICI]I 7 to I 112 ; The following residues NOT assigned to any domain: Chain "I" 1 - 275 The following residues NOT assigned to any domain: Chain "I" 113 - 113
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2TLD I

PROTEINASE INHIBITOR (TRYPSIN) 16-SEP-91 :: BOVINE TRYPSIN (E.C.3.4.21.4) COMPLEX WITH A

DOMAIN 1: [Assigned by homology with 3SICI]I 4 to I 112 ; The following residues NOT assigned to any domain: Chain "I" 16 - 245 The following residues NOT assigned to any domain: Chain "I" 113 - 113
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2BLM A

HYDROLASE(ACTING IN CYCLIC AMIDES) 02-FEB-90 :: BETA-LACTAMASE (PENICILLINASE) (E.C.3.5.2.6)

DOMAIN 1: [Assigned by homology with 4BLMA]A 31 to A 291 ; The following residues NOT assigned to any domain: Chain "A" 292 - 295 The following residues NOT assigned to any domain: Chain "A" 31 - 295
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2BLM B

HYDROLASE(ACTING IN CYCLIC AMIDES) 02-FEB-90 :: BETA-LACTAMASE (PENICILLINASE) (E.C.3.5.2.6)

DOMAIN 1: [Assigned by homology with 4BLMA]B 31 to B 291 ; The following residues NOT assigned to any domain: Chain "B" 31 - 295 The following residues NOT assigned to any domain: Chain "B" 292 - 295
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4BLM B

HYDROLASE(ACTING IN CYCLIC AMIDES) 28-MAY-91 :: BETA-*LACTAMASE (E.C.3.5.2.6) (PENICILLINASE)

DOMAIN 1: [Assigned by homology with 4BLMA]B 31 to B 291 ; The following residues NOT assigned to any domain: Chain "B" 31 - 291
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MBL A

17-AUG-92 :: BETA-LACTAMASE (E.C. 3.5.2.6)MUTANT GLU-166-ALA A.

DOMAIN 1: [Assigned by homology with 4BLMA]A 31 to A 291 ; The following residues NOT assigned to any domain: Chain "A" 31 - 291
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MBL B

17-AUG-92 :: BETA-LACTAMASE (E.C. 3.5.2.6)MUTANT GLU-166-ALA A.

DOMAIN 1: [Assigned by homology with 4BLMA]B 31 to B 291 ; The following residues NOT assigned to any domain: Chain "B" 31 - 291
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BLC

HYDROLASE(ACTING IN CYCLIC AMIDES) 27-SEP-93 :: BETA-LACTAMASE (E.C.3.5.2.6) COMPLEX WITH DEGRADAT

DOMAIN 1: [Assigned by homology with 4BLMA] 31 to 290 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BLH

HYDROLASE(BETA-LACTAMASE) 30-SEP-93 :: BETA-LACTAMASE (E.C.3.5.2.6) COMPLEXED WITH

DOMAIN 1: [Assigned by homology with 4BLMA] 31 to 290 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3BLM

HYDROLASE 03-DEC-90 :: BETA-*LACTAMASE (E.C.3.5.2.6)

DOMAIN 1: [Assigned by homology with 4BLMA] 31 to 290 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BLP

HYDROLASE(ACTING ON CYCLIC AMIDES) 23-SEP-93 :: BETA-LACTAMASE (E.C.3.5.2.6) P54 MUTANT WITH ASP 1

DOMAIN 1: [Assigned by homology with 4BLMA] 31 to 290 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ELS

CARBON-OXYGEN LYASE 05-APR-94 :: ENOLASE (E.C.4.2.1.11) (2-PHOSPHO-D-GLYCERATE HYDR

DOMAIN 1: 1 to 436 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5ENL

CARBON-OXYGEN LYASE 13-NOV-90 :: ENOLASE (E.C.4.2.1.11) (2-PHOSPHO-*D-GLYCERATE HYD

DOMAIN 1: 1 to 436 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NEL

CARBON-OXYGEN LYASE 20-AUG-93 :: ENOLASE (E.C.4.2.1.11) (2-PHOSPHO-D-GLYCERATE HYDR

DOMAIN 1: 1 to 436 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6ENL

CARBON-OXYGEN LYASE 13-NOV-90 :: ENOLASE (E.C.4.2.1.11) (2-PHOSPHO-*D-GLYCERATE HYD

DOMAIN 1: 1 to 436 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7ENL

CARBON-OXYGEN LYASE 13-NOV-90 :: ENOLASE (E.C.4.2.1.11) (2-PHOSPHO-*D-GLYCERATE HYD

DOMAIN 1: 1 to 436 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3ENL

CARBON-OXYGEN LYASE 13-NOV-90 :: ENOLASE (E.C.4.2.1.11) (2-PHOSPHO-*D-GLYCERATE HYD

DOMAIN 1: 1 to 436 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3FXN

ELECTRON TRANSPORT 16-DEC-77 :: FLAVODOXIN (OXIDIZED FORM)

DOMAIN 1: 1 to 138 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4HIR

COAGULATION INHIBITOR 19-DEC-88 :: HIRUDIN (MUTANT WITH LYS 47 REPLACED BY GLU) (/K47

DOMAIN 1: [Assigned by homology with 4HTCI] 1 to 49 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6HIR

COAGULATION INHIBITOR 09-JAN-90 :: HIRUDIN (MUTANT WITH LYS 47 REPLACED BY GLU) (/K47

DOMAIN 1: [Assigned by homology with 4HTCI] 1 to 49 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HRT I

HYDROLASE(SERINE PROTEINASE) 25-FEB-93 :: ALPHA-THROMBIN (E.C.3.4.21.5) COMPLEX WITH HIRUDIN

DOMAIN 1: [Assigned by homology with 4HTCI]I 1 to I 65 ; The following residues NOT assigned to any domain: Chain "I" 1H - 15 The following residues NOT assigned to any domain: Chain "I" 16 - 247
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5HIR

COAGULATION INHIBITOR 09-JAN-90 :: HIRUDIN (WILD-TYPE)

DOMAIN 1: [Assigned by homology with 4HTCI] 1 to 49 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HIR

COAGULATION INHIBITOR 19-DEC-88 :: HIRUDIN (WILD-TYPE)

DOMAIN 1: [Assigned by homology with 4HTCI] 1 to 49 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HIC

HIRUDIN 30-APR-92 :: HIRUDIN VARIANT 1 (RESIDUES 1 - 51) (NMR, 20 STRUC

DOMAIN 1: [Assigned by homology with 4HTCI] 1 to 51 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3HTC I

HYDROLASE (SERINE PROTEINASE) 11-JUN-93 :: ALPHA-THROMBIN (E.C.3.4.21.5) COMPLEX WITH RECOMBI

DOMAIN 1: [Assigned by homology with 4HTCI]I 1 to I 65 ; The following residues NOT assigned to any domain: Chain "I" 1F - 15 The following residues NOT assigned to any domain: Chain "I" 16 - 245
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4SBV C

COAT PROTEIN (VIRAL) 01-APR-85 :: SOUTHERN BEAN MOSAIC VIRUS COAT PROTEIN

DOMAIN 1: [Assigned by homology with 4SBVA]C 39 to C 259 ; The following residues NOT assigned to any domain: Chain "C" 62 - 260 The following residues NOT assigned to any domain: Chain "C" 62 - 260 The following residues NOT assigned to any domain: Chain "C" 260 - 260
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4SBV B

COAT PROTEIN (VIRAL) 01-APR-85 :: SOUTHERN BEAN MOSAIC VIRUS COAT PROTEIN

DOMAIN 1: [Assigned by homology with 4SBVA]B 62 to B 259 ; The following residues NOT assigned to any domain: Chain "B" 62 - 260 The following residues NOT assigned to any domain: Chain "B" 260 - 260 The following residues NOT assigned to any domain: Chain "B" 39 - 260
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3TGF

GROWTH FACTOR 23-JAN-91 :: TRANSFORMING GROWTH FACTOR-ALPHA (NMR, 4 STRUCTURE

DOMAIN 1: 1 to 50 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2TGF

GROWTH FACTOR 23-JAN-91 :: TRANSFORMING GROWTH FACTOR-ALPHA (NMR, MINIMIZED A

DOMAIN 1: 1 to 50 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8API B

PROTEINASE INHIBITOR 08-SEP-88 :: MODIFIED ALPHA=1=-*ANTITRYPSIN

DOMAIN 1: [Assigned by homology with 7APIB]B 359 to B 394 ; The following residues NOT assigned to any domain: Chain "B" 19 - 358 The following residues NOT assigned to any domain: Chain "B" 395 - 395
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

9API B

PROTEINASE INHIBITOR 08-SEP-88 :: MODIFIED ALPHA=1=-*ANTITRYPSIN

DOMAIN 1: [Assigned by homology with 7APIB]B 359 to B 394 ; The following residues NOT assigned to any domain: Chain "B" 20 - 358 The following residues NOT assigned to any domain: Chain "B" 395 - 395
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RDG

ELECTRON TRANSFER(IRON-SULFUR PROTEIN) 17-MAR-88 :: RUBREDOXIN

DOMAIN 1: [Assigned by homology with 8RXNA] 1 to 52 ; The following residues NOT assigned to any domain: Chain " " 0 - 0
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7RXN

ELECTRON TRANSFER(IRON-SULFUR PROTEIN) 11-MAY-90 :: RUBREDOXIN

DOMAIN 1: [Assigned by homology with 8RXNA] 1 to 52 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4RXN

ELECTRON TRANSFER(IRON-SULFUR PROTEIN) 15-OCT-84 :: RUBREDOXIN (OXIDIZED, FE(/III$)) (UNCONSTRAINED MO

DOMAIN 1: [Assigned by homology with 8RXNA] 1 to 52 ; The following residues NOT assigned to any domain: Chain " " 53 - 54
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5RXN

ELECTRON TRANSFER(IRON-SULFUR PROTEIN) 15-OCT-84 :: RUBREDOXIN (OXIDIZED, FE(/III$)) (CONSTRAINED MODE

DOMAIN 1: [Assigned by homology with 8RXNA] 1 to 52 ; The following residues NOT assigned to any domain: Chain " " 53 - 54
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CAA

ELECTRON TRANSPORT 18-MAY-92 :: RUBREDOXIN (OXIDIZED)

DOMAIN 1: [Assigned by homology with 8RXNA] 1 to 51 ; The following residues NOT assigned to any domain: Chain " " 52 - 53
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CAD

ELECTRON TRANSPORT 18-MAY-92 :: RUBREDOXIN (REDUCED)

DOMAIN 1: [Assigned by homology with 8RXNA] 1 to 51 ; The following residues NOT assigned to any domain: Chain " " 52 - 53
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ZRP

ELECTRON TRANSPORT 10-JUL-92 :: RUBREDOXIN (ZN-SUBSTITUTED) (NMR, 40 STRUCTURES)

DOMAIN 1: [Assigned by homology with 8RXNA] 1 to 51 ; The following residues NOT assigned to any domain: Chain " " 52 - 53
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6RXN

ELECTRON TRANSFER(IRON-SULFUR PROTEIN) 16-JAN-90 :: RUBREDOXIN

DOMAIN 1: [Assigned by homology with 8RXNA] 1 to 52 ; The following residues NOT assigned to any domain: Chain " " 0 - 0
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TRP A

HYDROLASE(ENDORIBONUCLEASE) 06-JUL-93 :: RIBONUCLEASE T1 (E.C.3.1.27.3) (LYS 25 ISOFORM) MU

DOMAIN 1: A 1 to A 103 ; The following residues NOT assigned to any domain: Chain "A" 104 - 104 The following residues NOT assigned to any domain: Chain "A" 201 - 304
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TRP B

HYDROLASE(ENDORIBONUCLEASE) 06-JUL-93 :: RIBONUCLEASE T1 (E.C.3.1.27.3) (LYS 25 ISOFORM) MU

DOMAIN 1: B 201 to B 303 ; The following residues NOT assigned to any domain: Chain "B" 1 - 104 The following residues NOT assigned to any domain: Chain "B" 304 - 304
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7RNT

HYDROLASE(ENDORIBONUCLEASE) 20-AUG-91 :: RIBONUCLEASE T=1= (E.C.3.1.27.3) MUTANT WITH TYR 4

DOMAIN 1: 1 to 103 ; The following residues NOT assigned to any domain: Chain " " 104 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TRQ A

HYDROLASE(ENDORIBONUCLEASE) 06-JUL-93 :: RIBONUCLEASE T1 (E.C.3.1.27.3) (LYS 25 ISOFORM) MU

DOMAIN 1: A 1 to A 103 ; The following residues NOT assigned to any domain: Chain "A" 104 - 104 The following residues NOT assigned to any domain: Chain "A" 201 - 304
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TRQ B

HYDROLASE(ENDORIBONUCLEASE) 06-JUL-93 :: RIBONUCLEASE T1 (E.C.3.1.27.3) (LYS 25 ISOFORM) MU

DOMAIN 1: B 201 to B 303 ; The following residues NOT assigned to any domain: Chain "B" 1 - 104 The following residues NOT assigned to any domain: Chain "B" 304 - 304
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RGA

HYDROLASE(ENDORIBONUCLEASE) 07-JUN-93 :: RIBONUCLEASE T1 (E.C.3.1.27.3) ISOZYME COMPLEX WIT

DOMAIN 1: 1 to 103 ; The following residues NOT assigned to any domain: Chain " " 104 - 104 The following residues NOT assigned to any domain: Chain " " 106 - 106
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RGC A

HYDROLASE(ENDORIBONUCLEASE) 12-MAY-93 :: RIBONUCLEASE T1 (E.C.3.1.27.3) MUTANT WITH GLN 25

DOMAIN 1: A 1 to A 103 ; The following residues NOT assigned to any domain: Chain "A" 104 - 104 The following residues NOT assigned to any domain: Chain "A" 1 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RGC B

HYDROLASE(ENDORIBONUCLEASE) 12-MAY-93 :: RIBONUCLEASE T1 (E.C.3.1.27.3) MUTANT WITH GLN 25

DOMAIN 1: B 1 to B 103 ; The following residues NOT assigned to any domain: Chain "B" 1 - 104 The following residues NOT assigned to any domain: Chain "B" 104 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RNT

HYDROLASE(ENDORIBONUCLEASE) 10-JUL-87 :: RIBONUCLEASE T=1=(E.C.3.1.27.3) ISOZYME-2(PRIME)-G

DOMAIN 1: 1 to 103 ; The following residues NOT assigned to any domain: Chain " " 104 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2RNT

HYDROLASE(ENDORIBONUCLEASE) 06-JUL-88 :: LYS 25-RIBONUCLEASE T=1= (LYS 25-/RN$ASE T=1=)

DOMAIN 1: 1 to 103 ; The following residues NOT assigned to any domain: Chain " " 104 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5RNT

HYDROLASE(ENDORIBONUCLEASE) 28-MAR-91 :: RIBONUCLEASE T=1= (E.C.3.1.27.3) COMPLEX WITH

DOMAIN 1: 1 to 103 ; The following residues NOT assigned to any domain: Chain " " 104 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6RNT

HYDROLASE(ENDORIBONUCLEASE) 20-AUG-91 :: RIBONUCLEASE T=1= (E.C.3.1.27.3) COMPLEX WITH 2'-A

DOMAIN 1: 1 to 103 ; The following residues NOT assigned to any domain: Chain " " 104 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8RNT

HYDROLASE(ENDORIBONUCLEASE) 23-SEP-91 :: RIBONUCLEASE T=1= (E.C.3.1.27.3) COMPLEX WITH ZN==

DOMAIN 1: 1 to 103 ; The following residues NOT assigned to any domain: Chain " " 104 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3RNT

HYDROLASE(ENDORIBONUCLEASE) 31-MAY-89 :: LYS 25-RIBONUCLEASE T=1= (LYS 25-/RN$ASE T=1=)

DOMAIN 1: 1 to 103 ; The following residues NOT assigned to any domain: Chain " " 104 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RGK

HYDROLASE(ENDORIBONUCLEASE) 19-FEB-92 :: RIBONUCLEASE T=1= (E.C.3.1.27.3) MUTANT WITH GLU 4

DOMAIN 1: 1 to 103 ; The following residues NOT assigned to any domain: Chain " " 104 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RGL

HYDROLASE(ENDORIBONUCLEASE) 19-FEB-92 :: RIBONUCLEASE T=1= (E.C.3.1.27.3) MUTANT WITH GLU 4

DOMAIN 1: 1 to 103 ; The following residues NOT assigned to any domain: Chain " " 104 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LRA

HYDROLASE(ENDORIBONUCLEASE) 01-OCT-93 :: RIBONUCLEASE T1 (RNASE T1) (E.C.3.1.27.3) MUTANT W

DOMAIN 1: 1 to 103 ; The following residues NOT assigned to any domain: Chain " " 104 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RLS

HYDROLASE(ENDORIBONUCLEASE) 29-MAR-94 :: RIBONUCLEASE T1 (E.C.3.1.27.3) COMPLEXED WITH 3'-G

DOMAIN 1: 1 to 103 ; The following residues NOT assigned to any domain: Chain " " 104 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RN1 C

PRELIMINARY 22-NOV-91 :: GLN(25) RIBONUCLEASE T=1= (E.C. 3.1.27.3)

DOMAIN 1: C 1 to C 103 ; The following residues NOT assigned to any domain: Chain " " 1 - 104 The following residues NOT assigned to any domain: Chain " " 106 - 208 The following residues NOT assigned to any domain: Chain " " 209 - 312
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RN1 B

PRELIMINARY 22-NOV-91 :: GLN(25) RIBONUCLEASE T=1= (E.C. 3.1.27.3)

DOMAIN 1: B 2 to B 103 ; The following residues NOT assigned to any domain: Chain " " 1 - 104 The following residues NOT assigned to any domain: Chain " " 106 - 208 The following residues NOT assigned to any domain: Chain " " 209 - 312
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2AAD A

PRELIMINARY 15-SEP-92 :: RIBONUCLEASE T=1= (E.C.3.1.27.3) ISOZYME 2' MUTANT

DOMAIN 1: A 1 to A 103 ; The following residues NOT assigned to any domain: Chain "A" 104 - 104 The following residues NOT assigned to any domain: Chain "A" 1 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2AAD B

PRELIMINARY 15-SEP-92 :: RIBONUCLEASE T=1= (E.C.3.1.27.3) ISOZYME 2' MUTANT

DOMAIN 1: B 1 to B 103 ; The following residues NOT assigned to any domain: Chain "B" 1 - 104 The following residues NOT assigned to any domain: Chain "B" 104 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2AAE

PRELIMINARY 15-SEP-92 :: RIBONUCLEASE T=1= MUTANT WITH HIS 40 REPLACED BY L

DOMAIN 1: 1 to 103 ; The following residues NOT assigned to any domain: Chain " " 104 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4RNT

HYDROLASE(ENDORIBONUCLEASE) 13-FEB-90 :: RIBONUCLEASE T1 (E.C.3.1.27.3) (/H92A$) (MUTANT WI

DOMAIN 1: 1 to 103 ; The following residues NOT assigned to any domain: Chain " " 104 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RN4

HYDROLASE(ENDORIBONUCLEASE) 07-NOV-91 :: RIBONUCLEASE T=1= (E.C.3.1.27.3) MUTANT WITH HISTI

DOMAIN 1: 1 to 103 ; The following residues NOT assigned to any domain: Chain " " 104 - 104
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RN1 A

PRELIMINARY 22-NOV-91 :: GLN(25) RIBONUCLEASE T=1= (E.C. 3.1.27.3)

DOMAIN 1: A 1 to A 103 ; The following residues NOT assigned to any domain: Chain "A" 104 - 104 The following residues NOT assigned to any domain: Chain "A" 106 - 208 The following residues NOT assigned to any domain: Chain "A" 209 - 312
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RDS

HYDROLASE(ENDORIBONUCLEASE) 14-MAY-93 :: RIBONUCLEASE MS (E.C.3.1.27.3) COMPLEX WITH

DOMAIN 1: 1 to 102 ; The following residues NOT assigned to any domain: Chain " " 103 - 105
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RMS

HYDROLASE(ENDORIBONUCLEASE) 02-DEC-91 :: RIBONUCLEASE MS (E.C.3.1.4.23) COMPLEXED WITH 3'-G

DOMAIN 1: 1 to 102 ; The following residues NOT assigned to any domain: Chain " " 103 - 105
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RCK

HYDROLASE(ENDORIBONUCLEASE) 08-AUG-94 :: RIBONUCLEASE F1 (E.C.3.1.27.3) (NMR, 42 STRUCTURES

DOMAIN 1: 1 to 102 ; The following residues NOT assigned to any domain: Chain " " 103 - 106
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RCL

HYDROLASE(ENDORIBONUCLEASE) 08-AUG-94 :: RIBONUCLEASE F1 (E.C.3.1.27.3)

DOMAIN 1: 1 to 102 ; The following residues NOT assigned to any domain: Chain " " 103 - 106
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FUS

HYDROLASE(ENDORIBONUCLEASE) 18-JAN-93 :: RIBONUCLEASE F1 (E.C.3.1.27.3)

DOMAIN 1: 1 to 103 ; The following residues NOT assigned to any domain: Chain " " 104 - 107
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FUT

HYDROLASE(ENDORIBONUCLEASE) 18-JAN-93 :: RIBONUCLEASE F1 (E.C.3.1.27.3) COMPLEX WITH

DOMAIN 1: 1 to 103 ; The following residues NOT assigned to any domain: Chain " " 104 - 107
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HEV

PRELIMINARY 14-JAN-93 :: HEVEIN

DOMAIN 1: [Assigned by homology with 9WGAA] 1 to 43 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]
AUTHOR ASSIGNMENTS - 2 DOMAIN STRUCTURES

AUTHOR ASSIGNMENTS - 2 DOMAIN STRUCTURES


1ABH

PHOSPHOTRANSFERASE 23-APR-92 :: PHOSPHATE-BINDING PROTEIN COMPLEX WITH PHOSPHATE

DOMAIN 1: 1 to 78 ; 210 to 321 ; DOMAIN 2: 79 to 209 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ABK

ENDONUCLEASE 15-SEP-92 :: ENDONUCLEASE III (E.C.4.2.99.18) (ACS REG 60184-90

DOMAIN 1: 1 to 21 ; 133 to 211 ; DOMAIN 2: 22 to 132 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ABM A

OXIDOREDUCTASE 27-AUG-92 :: MANGANESE SUPEROXIDE DISMUTASE (E.C.1.15.1.1)

DOMAIN 1: A 1 to A 84 ; DOMAIN 2: A 85 to A 198 ; The following residues NOT assigned to any domain: Chain "A" 1 - 198
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ARB

HYDROLASE(SERINE PROTEASE) 15-APR-93 :: ACHROMOBACTER PROTEASE I (E.C.3.4.21.50)

DOMAIN 1: 1 to 139 ; 229 to 263 ; DOMAIN 2: 140 to 228 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BAA

ANTI-FUNGAL PROTEIN 18-NOV-92 :: ENDOCHITINASE (26 KD)

DOMAIN 1: 1 to 84 ; 148 to 243 ; DOMAIN 2: 85 to 147 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BAB B

PRELIMINARY 06-MAY-92 :: HEMOGLOBIN THIONVILLE (ALPHA 1 VALINE TO GLUTAMIC

DOMAIN 1: B 1 to B 146 ; DOMAIN 2: B 1 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 0 - 142 The following residues NOT assigned to any domain: Chain "B" 0 - 142 The following residues NOT assigned to any domain: Chain "B" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BBO

DNA-BINDING PROTEIN 01-MAY-92 :: HUMAN ENHANCER-BINDING PROTEIN MBP-1 MUTANT WITH C

DOMAIN 1: 1 to 25 ; DOMAIN 2: 29 to 57 ; The following residues NOT assigned to any domain: Chain " " 26 - 28
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CAU B

SEED STORAGE PROTEIN 08-JUL-93 :: CANAVALIN (JACK BEAN 7S VICILIN)

DOMAIN 1: B 241 to B 379 ; DOMAIN 2: B 380 to B 424 ; The following residues NOT assigned to any domain: Chain "B" 44 - 224
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CID

T-CELL SURFACE GLYCOPROTEIN 28-JAN-93 :: CD4 (DOMAINS 3 AND 4)

DOMAIN 1: 1 to 105 ; DOMAIN 2: 106 to 177 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CPC A

LIGHT HARVESTING PROTEIN 11-OCT-90 :: C-PHYCOCYANIN

DOMAIN 1: A 1 to A 34 ; DOMAIN 2: A 35 to A 174 ; The following residues NOT assigned to any domain: Chain "A" 1 - 174 The following residues NOT assigned to any domain: Chain "A" 1 - 174 The following residues NOT assigned to any domain: Chain "A" 1 - 174
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CPC L

LIGHT HARVESTING PROTEIN 11-OCT-90 :: C-PHYCOCYANIN

DOMAIN 1: L 1 to L 35 ; DOMAIN 2: L 36 to L 174 ; The following residues NOT assigned to any domain: Chain "L" 1 - 174 The following residues NOT assigned to any domain: Chain "L" 1 - 174 The following residues NOT assigned to any domain: Chain "L" 1 - 174
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DPI

NUCLEOTIDYLTRANSFERASE 11-AUG-87 :: /DNA$ POLYMERASE I (KLENOW FRAGMENT) (E.C.2.7.7.7)

DOMAIN 1: 326 to 517 ; DOMAIN 2: 520 to 928 ; The following residues NOT assigned to any domain: Chain " " 518 - 519
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DRI

BINDING PROTEIN 12-FEB-92 :: D-RIBOSE-BINDING PROTEIN

DOMAIN 1: 1 to 103 ; 236 to 264 ; DOMAIN 2: 104 to 235 ; 265 to 271 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EPS

TRANSFERASE 05-APR-91 :: 5-ENOL-PYRUVYL-3-PHOSPHATE SYNTHASE (E.C.2.5.1.9)

DOMAIN 1: 1 to 19 ; 239 to 427 ; DOMAIN 2: 20 to 238 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EZM

HYDROLASE 13-JAN-92 :: ELASTASE (E.C.3.4.24.26) (ZINC METALLOPROTEASE)

DOMAIN 1: 1 to 134 ; DOMAIN 2: 135 to 298 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FNR

OXIDOREDUCTASE(NADP+(A),FERREDOXIN(A)) 21-JUN-90 :: FERREDOXIN:/NADP==+==$ OXIDOREDUCTASE (FERREDOXIN

DOMAIN 1: 19 to 161 ; DOMAIN 2: 162 to 314 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GLA G

PHOSPHOTRANSFERASE 28-OCT-92 :: GLYCEROL KINASE (E.C.2.7.1.30) COMPLEX WITH GLYCER

DOMAIN 1: G 5 to G 253 ; DOMAIN 2: G 254 to G 501 ; The following residues NOT assigned to any domain: Chain " " 1 - 168 The following residues NOT assigned to any domain: Chain " " 4 - 4 Chain " " 254 - 499
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GPB

GLYCOGEN PHOSPHORYLASE 04-JUN-90 :: GLYCOGEN PHOSPHORYLASE $B (E.C.2.4.1.1) (T STATE)

DOMAIN 1: 19 to 489 ; DOMAIN 2: 490 to 841 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GRC A

TRANSFERASE(FORMYL) 21-JUL-92 :: GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE (E.C.2.1

DOMAIN 1: A 1 to A 100 ; DOMAIN 2: A 104 to A 209 ; The following residues NOT assigned to any domain: Chain "A" 101 - 103 The following residues NOT assigned to any domain: Chain "A" 1 - 209
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GSS A

TRANSFERASE(GLUTATHIONE) 28-MAY-92 :: GLUTATHIONE S-TRANSFERASE (E.C.2.5.1.18) (CLASS PI

DOMAIN 1: A 1 to A 74 ; DOMAIN 2: A 81 to A 207 ; The following residues NOT assigned to any domain: Chain "A" 75 - 80 The following residues NOT assigned to any domain: Chain "A" 1 - 3 The following residues NOT assigned to any domain: Chain "A" 1 - 207 The following residues NOT assigned to any domain: Chain "A" 1 - 3
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HIL A

PRELIMINARY 08-JUL-92 :: IGG2A FAB FRAGMENT (FAB 17/9)

DOMAIN 1: A 1 to A 104 ; DOMAIN 2: A 110 to A 211 ; The following residues NOT assigned to any domain: Chain "A" 105 - 109 The following residues NOT assigned to any domain: Chain "A" 1 - 228 The following residues NOT assigned to any domain: Chain "A" 1 - 211 The following residues NOT assigned to any domain: Chain "A" 1 - 228
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1L92

HYDROLASE(O-GLYCOSYL) 21-JAN-92 :: LYSOZYME (E.C.3.2.1.17) MUTANT WITH CYS 54 REPLACE

DOMAIN 1: 1 to 73 ; DOMAIN 2: 74 to 162 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LAP

HYDROLASE(ALPHA-AMINOACYLPEPTIDE) 01-AUG-90 :: LEUCINE AMINOPEPTIDASE (E.C.3.4.11.1)

DOMAIN 1: 1 to 150 ; DOMAIN 2: 171 to 487 ; The following residues NOT assigned to any domain: Chain " " 151 - 484
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LGA A

OXIDOREDUCTASE 08-DEC-92 :: LIGNIN PEROXIDASE (LIP) (E.C.1.11.1.-) (FERRIC)

DOMAIN 1: A 1 to A 145 ; A 269 to A 292 ; DOMAIN 2: A 146 to A 268 ; A 293 to A 338 ; The following residues NOT assigned to any domain: Chain "A" 339 - 343 The following residues NOT assigned to any domain: Chain "A" 1 - 341
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NRD

OXIDOREDUCTASE(NITRIC OXIDE(A)) 08-APR-91 :: NITRITE REDUCTASE (E.C.1.7.99.3)

DOMAIN 1: 8 to 160 ; DOMAIN 2: 161 to 340 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1OMP

PRELIMINARY 14-SEP-92 :: D-MALTODEXTRIN-BINDING PROTEIN

DOMAIN 1: 1 to 109 ; 261 to 313 ; DOMAIN 2: 114 to 258 ; 316 to 370 ; The following residues NOT assigned to any domain: Chain " " 110 - 113 Chain " " 259 - 260 Chain " " 314 - 315
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1OSA

CALCIUM-BINDING PROTEIN 11-AUG-93 :: CALMODULIN

DOMAIN 1: 1 to 68 ; DOMAIN 2: 93 to 148 ; The following residues NOT assigned to any domain: Chain " " 69 - 92
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PFK A

TRANSFERASE(PHOSPHOTRANSFERASE) 25-JAN-88 :: PHOSPHOFRUCTOKINASE (E.C.2.7.1.11) (R-STATE) COMPL

DOMAIN 1: A 0 to A 138 ; A 251 to A 301 ; DOMAIN 2: A 139 to A 250 ; A 302 to A 319 ; The following residues NOT assigned to any domain: Chain "A" 0 - 319
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PHB

OXIDOREDUCTASE(OXYGENASE) 27-JUL-92 :: CYTOCHROME P450-CAM (E.C.1.14.15.1) (CAMPHOR 5-MON

DOMAIN 1: 10 to 85 ; 295 to 326 ; DOMAIN 2: 86 to 294 ; 327 to 414 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PHH

OXIDOREDUCTASE 04-NOV-87 :: $P-*HYDROXYBENZOATE HYDROXYLASE (/PHBH$) (E.C.1.14

DOMAIN 1: 1 to 74 ; 97 to 181 ; 269 to 391 ; DOMAIN 2: 75 to 96 ; 182 to 268 ; The following residues NOT assigned to any domain: Chain " " 392 - 394
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PPF E

PRELIMINARY 24-OCT-91 :: HUMAN LEUKOCYTE ELASTASE, ALSO CALLED NEUTROPHIL E

DOMAIN 1: E 16 to E 23 ; E 125 to E 243 ; DOMAIN 2: E 26 to E 121 ; The following residues NOT assigned to any domain: Chain "E" 24 - 25 Chain "E" 122 - 124 The following residues NOT assigned to any domain: Chain "E" 1 - 56
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PPN

PRELIMINARY 25-OCT-91 :: PAPAIN CYS-25 WITH BOUND ATOM

DOMAIN 1: 1 to 10 ; 112 to 208 ; DOMAIN 2: 21 to 111 ; 209 to 212 ; The following residues NOT assigned to any domain: Chain " " 11 - 20
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1REA

SELF-CLEAVAGE STIMULATION 19-DEC-91 :: REC A PROTEIN (E.C.3.4.99.37) COMPLEX WITH ADENOSI

DOMAIN 1: 3 to 268 ; DOMAIN 2: 269 to 328 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RHD

TRANSFERASE(THIOSULFATE,CYANIDE SULFUR) 23-NOV-77 :: RHODANESE (E.C.2.8.1.1)

DOMAIN 1: 1 to 158 ; DOMAIN 2: 159 to 293 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SBP

BINDING PROTEIN 19-JUL-93 :: SULFATE-BINDING PROTEIN

DOMAIN 1: 1 to 93 ; 220 to 273 ; DOMAIN 2: 94 to 219 ; 274 to 309 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SGT

HYDROLASE (SERINE PROTEINASE) 13-APR-88 :: TRYPSIN (/SGT$) (E.C.3.4.21.4)

DOMAIN 1: 22 to 123 ; 234 to 245 ; DOMAIN 2: 129 to 233 ; The following residues NOT assigned to any domain: Chain " " 16 - 21 Chain " " 124 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SMR A

PRELIMINARY 11-MAR-92 :: MOUSE SUBMAXILLARY RENIN (EC 3.4.23.15) COMPLEXED

DOMAIN 1: A 2 to A 174 ; DOMAIN 2: A 175 to A 326 ; The following residues NOT assigned to any domain: Chain "A" -2 - 1 The following residues NOT assigned to any domain: Chain "A" 2 - 9
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1VSG A

GLYCOPROTEIN 22-OCT-90 :: VARIANT SURFACE GLYCOPROTEIN (N-TERMINAL DOMAIN)

DOMAIN 1: A 1 to A 29 ; A 92 to A 251 ; DOMAIN 2: A 42 to A 75 ; A 266 to A 362 ; The following residues NOT assigned to any domain: Chain "A" 30 - 41 Chain "A" 76 - 91 Chain "A" 252 - 265 The following residues NOT assigned to any domain: Chain "A" 1 - 362
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1WSY B

LYASE(CARBON-OXYGEN) 19-SEP-88 :: TRYPTOPHAN SYNTHASE (E.C.4.2.1.20)

DOMAIN 1: B 9 to B 52 ; B 86 to B 204 ; DOMAIN 2: B 53 to B 85 ; B 205 to B 397 ; The following residues NOT assigned to any domain: Chain " " 1 - 265 The following residues NOT assigned to any domain: Chain " " 205 - 393
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CTS

OXO-ACID-LYASE 27-JAN-84 :: CITRATE SYNTHASE (E.C.4.1.3.7) - (CO*A, CITRATE) C

DOMAIN 1: 1 to 274 ; 381 to 437 ; DOMAIN 2: 275 to 380 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CYP

OXIDOREDUCTASE (H2O2(A)) 27-AUG-85 :: CYTOCHROME $C PEROXIDASE (E.C.1.11.1.5) (FERROCYTO

DOMAIN 1: 3 to 145 ; 266 to 294 ; DOMAIN 2: 164 to 265 ; The following residues NOT assigned to any domain: Chain " " 2 - 2 Chain " " 146 - 163
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2GLS A

LIGASE(AMIDE SYNTHETASE) 19-MAY-89 :: GLUTAMINE SYNTHETASE (E.C.6.3.1.2)

DOMAIN 1: A 1 to A 102 ; DOMAIN 2: A 103 to A 468 ; The following residues NOT assigned to any domain: Chain "A" 1 - 468 The following residues NOT assigned to any domain: Chain "A" 1 - 468 The following residues NOT assigned to any domain: Chain "A" 1 - 468 The following residues NOT assigned to any domain: Chain "A" 1 - 468 The following residues NOT assigned to any domain: Chain "A" 1 - 468 The following residues NOT assigned to any domain: Chain "A" 1 - 468 The following residues NOT assigned to any domain: Chain "A" 1 - 468 The following residues NOT assigned to any domain: Chain "A" 1 - 468 The following residues NOT assigned to any domain: Chain "A" 1 - 468 The following residues NOT assigned to any domain: Chain "A" 1 - 468 The following residues NOT assigned to any domain: Chain "A" 1 - 468
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HAD

DEHALOGENASE 07-AUG-92 :: HALOALKANE DEHALOGENASE ($P*H 6.2)

DOMAIN 1: 1 to 155 ; 230 to 310 ; DOMAIN 2: 156 to 229 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HHM A

HYDROLASE 20-OCT-92 :: HUMAN INOSITOL MONOPHOSPHATASE (E.C.3.1.3.25) DIME

DOMAIN 1: A 5 to A 144 ; DOMAIN 2: A 145 to A 276 ; The following residues NOT assigned to any domain: Chain "A" 5 - 276
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HHR C

HORMONE 12-OCT-92 :: HUMAN GROWTH HORMONE COMPLEX WITH ITS RECEPTOR

DOMAIN 1: C 32 to C 124 ; DOMAIN 2: C 129 to C 236 ; The following residues NOT assigned to any domain: Chain "C" 1 - 190 The following residues NOT assigned to any domain: Chain "C" 32 - 234 The following residues NOT assigned to any domain: Chain "C" 125 - 128
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HPD A

OXIDOREDUCTASE(OXYGENASE) 16-SEP-93 :: CYTOCHROME P450 (BM-3) (E.C.1.14.14.1) (HEMOPROTEI

DOMAIN 1: A 1 to A 70 ; A 329 to A 361 ; DOMAIN 2: A 72 to A 325 ; A 390 to A 457 ; The following residues NOT assigned to any domain: Chain "A" 71 - 71 Chain "A" 326 - 328 Chain "A" 362 - 389 The following residues NOT assigned to any domain: Chain "A" 1 - 457
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2LIV

PERIPLASMIC BINDING PROTEIN 10-APR-89 :: LEUCINE(SLASH)*ISOLEUCINE(SLASH)*VALINE-BINDING PR

DOMAIN 1: 1 to 118 ; 253 to 326 ; DOMAIN 2: 124 to 247 ; 332 to 344 ; The following residues NOT assigned to any domain: Chain " " 119 - 123 Chain " " 248 - 252 Chain " " 327 - 331
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2SGA

HYDROLASE (SERINE PROTEINASE) 21-JAN-83 :: PROTEINASE A (COMPONENT OF THE EXTRACELLULAR FILTR

DOMAIN 1: 16 to 126 ; DOMAIN 2: 127 to 242 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2SNV

COAT PROTEIN 17-JUL-92 :: SINDBIS VIRUS CAPSID PROTEIN (CHYMOTRYPSIN-LIKE SE

DOMAIN 1: 114 to 177 ; DOMAIN 2: 180 to 264 ; The following residues NOT assigned to any domain: Chain " " 178 - 179
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2TBV A

VIRUS 22-JUN-84 :: TOMATO BUSHY STUNT VIRUS

DOMAIN 1: A 102 to A 271 ; DOMAIN 2: A 272 to A 387 ; The following residues NOT assigned to any domain: Chain "A" 101 - 101 The following residues NOT assigned to any domain: Chain "A" 101 - 387 The following residues NOT assigned to any domain: Chain "A" 67 - 387
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3CD4

T-CELL SURFACE GLYCOPROTEIN 30-JUL-92 :: CD4 (N-TERMINAL FRAGMENT CONSISTING OF RESIDUES 1-

DOMAIN 1: 1 to 98 ; DOMAIN 2: 99 to 182 ; The following residues NOT assigned to any domain: Chain " " 99 - 178
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3COX

OXIDOREDUCTASE(OXYGEN RECEPTOR) 14-JUN-93 :: CHOLESTEROL OXIDASE (E.C.1.1.3.6)

DOMAIN 1: 5 to 44 ; 226 to 316 ; 462 to 506 ; DOMAIN 2: 45 to 225 ; 317 to 461 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3DPA

CHAPERONE PROTEIN 09-OCT-91 :: PAP*D

DOMAIN 1: 1 to 121 ; DOMAIN 2: 122 to 218 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3GAP A

GENE REGULATORY PROTEIN 15-APR-87 :: CATABOLITE GENE ACTIVATOR PROTEIN - CYCLIC /AMP$ C

DOMAIN 1: A 1 to A 137 ; DOMAIN 2: A 138 to A 208 ; The following residues NOT assigned to any domain: Chain "A" 1 - 205
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3PGK

PHOSPHOTRANSFERASE(CARBOXYL AS ACCEPTOR)15-JUL-82 :: PHOSPHOGLYCERATE KINASE (E.C.2.7.2.3) COMPLEX WITH

DOMAIN 1: 1 to 185 ; 403 to 416 ; DOMAIN 2: 200 to 392 ; The following residues NOT assigned to any domain: Chain " " 0 - 0 Chain " " 186 - 199 Chain " " 393 - 415
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4ENL

CARBON-OXYGEN LYASE 13-NOV-90 :: ENOLASE (E.C.4.2.1.11) (2-PHOSPHO-*D-GLYCERATE HYD

DOMAIN 1: 1 to 128 ; DOMAIN 2: 129 to 436 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4GCR

EYE LENS PROTEIN 02-APR-92 :: GAMMA-B CRYSTALLIN (PREVIOUSLY GAMMA-II CRYSTALLIN

DOMAIN 1: 1 to 83 ; DOMAIN 2: 84 to 174 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4GPD 1

OXIDOREDUCTASE(ALDEHYDE(D)-NAD(A)) 04-JAN-88 :: APO-D-GYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE

DOMAIN 1: 1 1 to 1 148 ; DOMAIN 2: 1 149 to 1 333 ; The following residues NOT assigned to any domain: Chain "1" 1 - 333 The following residues NOT assigned to any domain: Chain "1" 1 - 333 The following residues NOT assigned to any domain: Chain "1" 1 - 333
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4RCR H

PHOTOSYNTHETIC REACTION CENTER 09-SEP-91 :: PHOTOSYNTHETIC REACTION CENTER

DOMAIN 1: H 12 to H 39 ; DOMAIN 2: H 40 to H 248 ; The following residues NOT assigned to any domain: Chain "H" 5 - 270 The following residues NOT assigned to any domain: Chain "H" 6 - 301
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4TMS

TRANSFERASE (METHYLTRANFERASE) 07-JAN-92 :: THYMIDYLATE SYNTHASE (E.C.2.1.1.45)

DOMAIN 1: 1 to 69 ; 143 to 316 ; DOMAIN 2: 70 to 142 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4TS1 A

LIGASE (SYNTHETASE) 29-JUN-89 :: DES-(ILE 318-ARG 417)-TYROSYL-TRANSFER /RNA$ SYNTH

DOMAIN 1: A 1 to A 220 ; DOMAIN 2: A 248 to A 319 ; The following residues NOT assigned to any domain: Chain "A" 221 - 247 The following residues NOT assigned to any domain: Chain "A" 1 - 1 The following residues NOT assigned to any domain: Chain "A" 1 - 313 The following residues NOT assigned to any domain: Chain "A" 1 - 1
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5FBP A

HYDROLASE (PHOSPHORIC MONOESTER) 11-FEB-91 :: FRUCTOSE-1,6-BISPHOSPHATASE (*FRU-1,6-*PASE)

DOMAIN 1: A 6 to A 201 ; DOMAIN 2: A 202 to A 335 ; The following residues NOT assigned to any domain: Chain "A" 5 - 335
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6LDH

OXIDOREDUCTASE(CHOH(D)-NAD(A)) 25-NOV-87 :: M=4= APO-*LACTATE DEHYDROGENASE (E.C.1.1.1.27)

DOMAIN 1: 20 to 164 ; DOMAIN 2: 165 to 329 ; The following residues NOT assigned to any domain: Chain " " 0 - 19
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7AAT A

TRANSFERASE(AMINOTRANSFERASE) 02-DEC-91 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) COMPLEX W

DOMAIN 1: A 3 to A 47 ; A 326 to A 410 ; DOMAIN 2: A 48 to A 325 ; The following residues NOT assigned to any domain: Chain "A" 3 - 410
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8ABP

BINDING PROTEINS 25-APR-91 :: L-*ARABINOSE-BINDING PROTEIN (MUTANT WITH MET 108

DOMAIN 1: 2 to 109 ; 255 to 284 ; DOMAIN 2: 110 to 254 ; 285 to 306 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8ADH

OXIDOREDUCTASE(NAD(A)-CHOH(D)) 20-APR-89 :: APO-LIVER ALCOHOL DEHYDROGENASE (E.C.1.1.99.8)

DOMAIN 1: 1 to 175 ; 319 to 374 ; DOMAIN 2: 176 to 318 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8ATC A

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 25-AUG-89 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: A 1 to A 137 ; A 288 to A 310 ; DOMAIN 2: A 144 to A 283 ; The following residues NOT assigned to any domain: Chain "A" 138 - 143 Chain "A" 284 - 287 The following residues NOT assigned to any domain: Chain "A" 8 - 153 The following residues NOT assigned to any domain: Chain "A" 1 - 310 The following residues NOT assigned to any domain: Chain "A" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8ATC B

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 25-AUG-89 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: B 8 to B 97 ; DOMAIN 2: B 101 to B 152 ; The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 98 - 100 Chain "B" 153 - 153 The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

9RUB B

LYASE(CARBON-CARBON) 28-NOV-90 :: RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE(SLASH)OXYGLU

DOMAIN 1: B 2 to B 138 ; DOMAIN 2: B 139 to B 459 ; The following residues NOT assigned to any domain: Chain "B" 2 - 460
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2RNP A

NUCLEOTIDYLTRANSFERASE 11-AUG-93 :: DNA-DIRECTED RNA POLYMERASE (E.C.2.7.7.6)

DOMAIN 1: A 1 to A 448 ; DOMAIN 2: A 449 to A 883 ; The following residues NOT assigned to any domain: Chain "A" 1 - 883 The following residues NOT assigned to any domain: Chain "A" 1 - 883
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3GLY

HYDROLASE 03-JUN-94 :: GLUCOAMYLASE-471 (1,4-ALPHA-D-GLUCAN GLUCOHYDROLAS

DOMAIN 1: 1 to 440 ; DOMAIN 2: 441 to 471 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GPH 1

TRANSFERASE(GLUTAMINE AMIDOTRANSFERASE) 20-APR-94 :: GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP)

DOMAIN 1: 1 1 to 1 230 ; DOMAIN 2: 1 231 to 1 456 ; The following residues NOT assigned to any domain: Chain "1" 457 - 465 The following residues NOT assigned to any domain: Chain "1" 1 - 465 The following residues NOT assigned to any domain: Chain "1" 1 - 465 The following residues NOT assigned to any domain: Chain "1" 1 - 465
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PII

PRELIMINARY 21-JUN-91 :: N-(5'PHOSPORIBOSYL)ANTHRANILATE ISOMERASE (E.C.5.3

DOMAIN 1: 1 to 255 ; DOMAIN 2: 256 to 452 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HPL A

HYDROLASE(CARBOXYLIC ESTERASE) 27-JAN-93 :: LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE)

DOMAIN 1: A 1 to A 335 ; DOMAIN 2: A 336 to A 449 ; The following residues NOT assigned to any domain: Chain "A" 1 - 449
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SES A

LIGASE(SYNTHETASE) 21-FEB-94 :: SERYL-TRNA SYNTHETASE (E.C.6.1.1.11) (SERINE-TRNA

DOMAIN 1: A 1 to A 98 ; DOMAIN 2: A 99 to A 421 ; The following residues NOT assigned to any domain: Chain "A" 1 - 421
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CHM A

CREATINASE 19-JUL-93 :: CREATINE AMIDINOHYDROLASE (E.C.3.5.3.3)

DOMAIN 1: A 2 to A 162 ; DOMAIN 2: A 163 to A 402 ; The following residues NOT assigned to any domain: Chain "A" 2 - 402
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3MDD A

OXIDOREDUCTASE 13-JUL-94 :: MEDIUM CHAIN ACYL-COA DEHYDROGENASE (MCAD) (E.C.1.

DOMAIN 1: A 11 to A 128 ; A 254 to A 395 ; DOMAIN 2: A 129 to A 253 ; The following residues NOT assigned to any domain: Chain "A" 11 - 395
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BMV 2

VIRUS 09-OCT-89 :: BEAN POD MOTTLE VIRUS (MIDDLE COMPONENT)

DOMAIN 1: 2 2189 to 2 3014 ; DOMAIN 2: 2 3014 to 2 3181 ; The following residues NOT assigned to any domain: Chain "2" 1001 - 1185 The following residues NOT assigned to any domain: Chain "2" 3001 - 3013 Chain "2" 2190 - 2192 The following residues NOT assigned to any domain: Chain "2" 1 - 11
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RPA

HYDROLASE(PHOSPHORIC MONOESTER) 12-JUN-93 :: PROSTATIC ACID PHOSPHATASE (E.C.3.1.3.2) COMPLEXED

DOMAIN 1: 1 to 126 ; 227 to 342 ; DOMAIN 2: 127 to 226 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1APM E

TRANSFERASE(PHOSPHOTRANSFERASE) 18-JAN-93 :: $C-/AMP$-DEPENDENT PROTEIN KINASE (E.C.2.7.1.37) (

DOMAIN 1: E 10 to E 32 ; E 128 to E 316 ; DOMAIN 2: E 33 to E 127 ; E 317 to E 350 ; The following residues NOT assigned to any domain: Chain "E" 5 - 24
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1UDP A

ISOMERASE 20-JUL-92 :: URIDINE DIPHOSPHOGALACTOSE 4-EPIMERASE (E.C.5.1.3.

DOMAIN 1: A 1 to A 179 ; A 234 to A 262 ; DOMAIN 2: A 180 to A 233 ; A 263 to A 338 ; The following residues NOT assigned to any domain: Chain "A" 1 - 338
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BGT

TRANSFERASE(GLYCOSYLTRANSFERASE) 09-JUN-94 :: BETA-GLUCOSYLTRANSFERASE (E.C.2.4.1.27) (ALPHA-CAR

DOMAIN 1: 1 to 162 ; 339 to 351 ; DOMAIN 2: 163 to 338 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HGE A

PRELIMINARY 01-NOV-91 :: HEMAGGLUTININ (BROMELAIN DIGESTED) CONTAINING *GLY

DOMAIN 1: A 1 to A 94 ; A 260 to A 328 ; DOMAIN 2: A 95 to A 259 ; The following residues NOT assigned to any domain: Chain "A" 1 - 175 The following residues NOT assigned to any domain: Chain "A" 1 - 328 The following residues NOT assigned to any domain: Chain "A" 1 - 175 The following residues NOT assigned to any domain: Chain "A" 1 - 328 The following residues NOT assigned to any domain: Chain "A" 1 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HMY

TRANSFERASE(METHYLTRANSFERASE) 05-AUG-93 :: HHAI DNA (CYTOSINE-C5-)-METHYLTRANSFERASE (E.C.2.1

DOMAIN 1: 1 to 187 ; 304 to 327 ; DOMAIN 2: 188 to 303 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3ECA A

HYDROLASE 02-JUL-93 :: ASPARAGINASE TYPE II (E.C.3.5.1.1) (ECA)

DOMAIN 1: A 1 to A 208 ; DOMAIN 2: A 209 to A 326 ; The following residues NOT assigned to any domain: Chain "A" 327 - 327 The following residues NOT assigned to any domain: Chain "A" 1 - 326 The following residues NOT assigned to any domain: Chain "A" 327 - 327 The following residues NOT assigned to any domain: Chain "A" 1 - 326 The following residues NOT assigned to any domain: Chain "A" 327 - 327 The following residues NOT assigned to any domain: Chain "A" 1 - 326 The following residues NOT assigned to any domain: Chain "A" 327 - 327
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GDH A

OXIDOREDUCTASE(CHOH (D)-NAD(P)+ (A)) 22-SEP-93 :: D-GLYCERATE DEHYDROGENASE (APO FORM) (E.C.1.1.1.29

DOMAIN 1: A 2 to A 99 ; A 291 to A 321 ; DOMAIN 2: A 100 to A 290 ; The following residues NOT assigned to any domain: Chain "A" 2 - 321
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BDM A

OXIDOREDUCTASE(NAD(A)-CHOH(D)) 16-FEB-93 :: MALATE DEHYDROGENASE (E.C.1.1.1.37) MUTANT WITH TH

DOMAIN 1: A 0 to A 156 ; DOMAIN 2: A 157 to A 329 ; The following residues NOT assigned to any domain: Chain "A" 330 - 332 The following residues NOT assigned to any domain: Chain "A" 0 - 332
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EMD

OXIDOREDUCTASE(NAD(A)-CHOH(D)) 25-MAR-93 :: MALATE DEHYDROGENASE (E.C.1.1.1.37)

DOMAIN 1: 1 to 148 ; DOMAIN 2: 149 to 309 ; The following residues NOT assigned to any domain: Chain " " 310 - 312
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GIA

SIGNAL TRANSDUCTION PROTEIN 20-JUL-94 :: GI ALPHA 1 (ACTIVE FORM WITH BOUND GTP-GAMMA-S)

DOMAIN 1: 34 to 60 ; 177 to 343 ; DOMAIN 2: 61 to 176 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PNG

HYDROLASE 02-JUN-94 :: PEPTIDE-N(4)-(N-ACETYL-BETA-D-GLUCOSAMINYL) ASPARA

DOMAIN 1: 5 to 140 ; DOMAIN 2: 141 to 314 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MAT

HYDROLASE(ALPHA-AMINOACYLPEPTIDE) 02-DEC-92 :: METHIONINE AMINOPEPTIDASE (E.C.3.4.11.18)

DOMAIN 1: 11 to 118 ; DOMAIN 2: 119 to 241 ; The following residues NOT assigned to any domain: Chain " " 2 - 10 Chain " " 242 - 264
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2AAI B

GLYCOSIDASE 07-SEP-93 :: RICIN (E.C.3.2.2.22)

DOMAIN 1: B 10 to B 138 ; DOMAIN 2: B 139 to B 262 ; The following residues NOT assigned to any domain: Chain "B" 1 - 267 The following residues NOT assigned to any domain: Chain "B" 1 - 9
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CND

OXIDOREDUCTASE(NITROGENOUS ACCEPTOR) 25-JUL-94 :: NITRATE REDUCTASE (C-TERMINAL FRAGMENT) (E.C.1.6.6

DOMAIN 1: 11 to 118 ; DOMAIN 2: 119 to 270 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1WHT A

SERINE CARBOXYPEPTIDASE 07-MAR-94 :: SERINE CARBOXYPEPTIDASE II (E.C.3.4.16.1) COMPLEXE

DOMAIN 1: B * to B * ; A -5 to A 181 ; DOMAIN 2: A 182 to A 248 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1KAN A

NUCLEOTIDYLTRANSFERASE 13-AUG-93 :: KANAMYCIN NUCLEOTIDYLTRANSFERASE (E.C.2.7.7.-) MUT

DOMAIN 1: A 1 to A 126 ; DOMAIN 2: A 127 to A 253 ; The following residues NOT assigned to any domain: Chain "A" 1 - 253
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CTM

ELECTRON TRANSPORT(CYTOCHROME) 02-JAN-94 :: CYTOCHROME F (REDUCED)

DOMAIN 1: 1 to 168 ; 232 to 250 ; DOMAIN 2: 169 to 231 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AHC

GLYCOSIDASE 07-JAN-94 :: ALPHA-MOMORCHARIN (E.C.3.2.2.22) (TYPE I RIBOSOME-

DOMAIN 1: 1 to 181 ; DOMAIN 2: 182 to 246 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2LAO

AMINO-ACID BINDING PROTEIN 25-FEB-93 :: LYSINE-, ARGININE-, ORNITHINE-BINDING PROTEIN (LAO

DOMAIN 1: 1 to 90 ; 191 to 238 ; DOMAIN 2: 91 to 190 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CFB

NEURAL ADHESION MOLECULE 27-AUG-94 :: DROSOPHILA NEUROGLIAN (CHYMOTRYPTIC FRAGMENT CONTA

DOMAIN 1: 610 to 710 ; DOMAIN 2: 711 to 814 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IAG

METALLOPROTEASE 09-MAY-94 :: ADAMALYSIN II (PROTEINASE II) (E.C.3.4.24.46)

DOMAIN 1: 2 to 149 ; DOMAIN 2: 150 to 202 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IAA

ZINC ENDOPEPTIDASE 09-MAY-94 :: ASTACIN (E.C.3.4.24.21) WITH ZINC REPLACED BY COPP

DOMAIN 1: 1 to 101 ; 180 to 200 ; DOMAIN 2: 102 to 181 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3HHR B

HORMONE/RECEPTOR 30-DEC-93 :: HUMAN GROWTH HORMONE COMPLEXED WITH ITS RECEPTOR

DOMAIN 1: B 32 to B 125 ; DOMAIN 2: B 126 to B 234 ; The following residues NOT assigned to any domain: Chain "B" 1 - 190 The following residues NOT assigned to any domain: Chain "B" 32 - 236
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TSS A

TOXIN 29-OCT-93 :: TOXIC SHOCK SYNDROME TOXIN 1

DOMAIN 1: A 1 to A 16 ; A 90 to A 194 ; DOMAIN 2: A 17 to A 89 ; The following residues NOT assigned to any domain: Chain "A" 1 - 194 The following residues NOT assigned to any domain: Chain "A" 1 - 194
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DSB A

DISULFIDE OXIDOREDUCTASE 24-MAY-93 :: DSBA (DISULFIDE BOND FORMATION PROTEIN)

DOMAIN 1: A 1 to A 62 ; A 139 to A 188 ; DOMAIN 2: A 63 to A 138 ; The following residues NOT assigned to any domain: Chain "A" 1 - 188
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1REC

CALCIUM-BINDING PROTEIN 29-OCT-93 :: RECOVERIN (CALCIUM SENSOR IN VISION)

DOMAIN 1: 9 to 96 ; DOMAIN 2: 97 to 198 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2SAS

CALCIUM-BINDING PROTEIN 30-JUL-93 :: SARCOPLASMIC CALCIUM-BINDING PROTEIN (ISO TYPE II)

DOMAIN 1: 1 to 100 ; DOMAIN 2: 101 to 185 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TBP A

BINDING PROTEIN 02-AUG-93 :: TATA-BINDING PROTEIN (TBP, C-TERMINAL 179 AMINO AC

DOMAIN 1: A 61 to A 71 ; A 159 to A 240 ; DOMAIN 2: A 68 to A 158 ; The following residues NOT assigned to any domain: Chain "A" 61 - 240
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FCD C

ELECTRON TRANSPORT(FLAVOCYTOCHROME) 18-AUG-94 :: FLAVOCYTOCHROME C SULFIDE DEHYDROGENASE (FCSD)

DOMAIN 1: C 1 to C 82 ; DOMAIN 2: C 83 to C 174 ; The following residues NOT assigned to any domain: Chain "C" 1 - 401 The following residues NOT assigned to any domain: Chain "C" 1 - 401 The following residues NOT assigned to any domain: Chain "C" 1 - 174
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PRR

BINDING PROTEIN 25-MAR-94 :: DEVELOPMENT-SPECIFIC PROTEIN S (SPORE COAT PROTEIN

DOMAIN 1: 1 to 89 ; DOMAIN 2: 90 to 173 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ESL

CELL ADHESION PROTEIN 03-JUN-94 :: E-SELECTIN (LECTIN AND EGF DOMAINS, RESIDUES 1 - 1

DOMAIN 1: 1 to 120 ; DOMAIN 2: 121 to 157 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PKP

RIBOSOMAL PROTEIN 30-AUG-93 :: RIBOSOMAL PROTEIN S5 (PROKARYOTIC)

DOMAIN 1: 4 to 75 ; DOMAIN 2: 76 to 148 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BAB A

PRELIMINARY 06-MAY-92 :: HEMOGLOBIN THIONVILLE (ALPHA 1 VALINE TO GLUTAMIC

DOMAIN 1: A * to A * ; DOMAIN 2: A 1 to A 142 ; The following residues NOT assigned to any domain: Chain "A" 1 - 146 The following residues NOT assigned to any domain: Chain "A" 0 - 142 The following residues NOT assigned to any domain: Chain "A" 1 - 146
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PSP A

SPASMOLYTIC PROTEIN 05-JAN-94 :: PANCREATIC SPASMOLYTIC POLYPEPTIDE (PSP)

DOMAIN 1: A 1 to A 56 ; A 99 to A 106 ; DOMAIN 2: A 57 to A 98 ; The following residues NOT assigned to any domain: Chain "A" 1 - 106
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BN2 1

HORMONE 07-AUG-90 :: BOVINE NEUROPHYSIN /II$ COMPLEX WITH P-IODO-PHE-TY

DOMAIN 1: 1 1 to 1 58 ; DOMAIN 2: 1 59 to 1 86 ; The following residues NOT assigned to any domain: Chain "1" 1 - 86 The following residues NOT assigned to any domain: Chain "1" 1 - 86 The following residues NOT assigned to any domain: Chain "1" 1 - 86 The following residues NOT assigned to any domain: Chain "1" 1 - 2 The following residues NOT assigned to any domain: Chain "1" 1 - 2 The following residues NOT assigned to any domain: Chain "1" 1 - 2 The following residues NOT assigned to any domain: Chain "1" 1 - 2 The following residues NOT assigned to any domain: Chain "1" 1 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2DRP A

COMPLEX(TRANSCRIPTION REGULATION/DNA) 06-JUN-94 :: TRAMTRACK PROTEIN (TWO ZINC-FINGER PEPTIDE) COMPLE

DOMAIN 1: A 103 to A 138 ; DOMAIN 2: A 139 to A 165 ; The following residues NOT assigned to any domain: Chain "A" 1 - 19 The following residues NOT assigned to any domain: Chain "A" 21 - 39 The following residues NOT assigned to any domain: Chain "A" 102 - 166 The following residues NOT assigned to any domain: Chain "A" 1 - 19 The following residues NOT assigned to any domain: Chain "A" 21 - 39
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4MT2

METALLOTHIONEIN 26-FEB-93 :: METALLOTHIONEIN ISOFORM II

DOMAIN 1: 1 to 31 ; DOMAIN 2: 32 to 61 ; The following residues NOT assigned to any domain: Chain " " 0 - 0
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PBP

PHOSPHATE TRANSPORT 20-JUL-94 :: TITLE: PHOSPHATE-BINDING PROTEIN (MUTANT WITH THR

DOMAIN 1: 1 to 78 ; 210 to 321 ; DOMAIN 2: 79 to 209 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ARC

HYDROLASE(SERINE PROTEASE) 15-APR-93 :: ACHROMOBACTER PROTEASE I (E.C.3.4.21.50) COMPLEX W

DOMAIN 1: 1 to 139 ; 229 to 263 ; DOMAIN 2: 140 to 228 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PHL A

PLANT SEED STORAGE PROTEIN(VICILIN) 07-JUL-94 :: PHASEOLIN

DOMAIN 1: [Assigned by homology with 1CAUB]A 11 to A 148 ; DOMAIN 2: [Assigned by homology with 1CAUB]A 149 to A 279 ; The following residues NOT assigned to any domain: Chain "A" 280 - 381 The following residues NOT assigned to any domain: Chain "A" 11 - 381 The following residues NOT assigned to any domain: Chain "A" 10 - 381
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PHL B

PLANT SEED STORAGE PROTEIN(VICILIN) 07-JUL-94 :: PHASEOLIN

DOMAIN 1: [Assigned by homology with 1CAUB]B 11 to B 148 ; DOMAIN 2: [Assigned by homology with 1CAUB]B 149 to B 279 ; The following residues NOT assigned to any domain: Chain "B" 11 - 381 The following residues NOT assigned to any domain: Chain "B" 280 - 381 The following residues NOT assigned to any domain: Chain "B" 10 - 381
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PHL C

PLANT SEED STORAGE PROTEIN(VICILIN) 07-JUL-94 :: PHASEOLIN

DOMAIN 1: [Assigned by homology with 1CAUB]C 10 to C 148 ; DOMAIN 2: [Assigned by homology with 1CAUB]C 149 to C 279 ; The following residues NOT assigned to any domain: Chain "C" 11 - 381 The following residues NOT assigned to any domain: Chain "C" 11 - 381 The following residues NOT assigned to any domain: Chain "C" 280 - 381
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PHS

PLANT SEED STORAGE PROTEIN (VICILIN) 21-MAR-90 :: PHASEOLIN

DOMAIN 1: [Assigned by homology with 1CAUB] 11 to 148 ; DOMAIN 2: [Assigned by homology with 1CAUB] 149 to 279 ; The following residues NOT assigned to any domain: Chain " " 280 - 381
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CAV B

SEED STORAGE PROTEIN 27-MAY-93 :: CANAVALIN (JACK BEAN 7S VICILIN)

DOMAIN 1: [Assigned by homology with 1CAUB]B 241 to B 379 ; DOMAIN 2: [Assigned by homology with 1CAUB]B 380 to B 424 ; The following residues NOT assigned to any domain: Chain "B" 44 - 224
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CAW B

SEED STORAGE PROTEIN 02-JUN-93 :: CANAVALIN (JACK BEAN 7S VICILIN)

DOMAIN 1: [Assigned by homology with 1CAUB]B 241 to B 379 ; DOMAIN 2: [Assigned by homology with 1CAUB]B 380 to B 424 ; The following residues NOT assigned to any domain: Chain "B" 44 - 224
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CAX B

SEED STORAGE PROTEIN 10-JUN-93 :: CANAVALIN (JACK BEAN 7S VICILIN)

DOMAIN 1: [Assigned by homology with 1CAUB]B 241 to B 379 ; DOMAIN 2: [Assigned by homology with 1CAUB]B 380 to B 424 ; The following residues NOT assigned to any domain: Chain "B" 44 - 224 The following residues NOT assigned to any domain: Chain "B" 44 - 224 The following residues NOT assigned to any domain: Chain "B" 241 - 424 The following residues NOT assigned to any domain: Chain "B" 44 - 224 The following residues NOT assigned to any domain: Chain "B" 241 - 424
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CAX D

SEED STORAGE PROTEIN 10-JUN-93 :: CANAVALIN (JACK BEAN 7S VICILIN)

DOMAIN 1: [Assigned by homology with 1CAUB]D 241 to D 379 ; DOMAIN 2: [Assigned by homology with 1CAUB]D 380 to D 424 ; The following residues NOT assigned to any domain: Chain "D" 44 - 224 The following residues NOT assigned to any domain: Chain "D" 241 - 424 The following residues NOT assigned to any domain: Chain "D" 44 - 224 The following residues NOT assigned to any domain: Chain "D" 44 - 224 The following residues NOT assigned to any domain: Chain "D" 241 - 424
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CAX F

SEED STORAGE PROTEIN 10-JUN-93 :: CANAVALIN (JACK BEAN 7S VICILIN)

DOMAIN 1: [Assigned by homology with 1CAUB]F 241 to F 379 ; DOMAIN 2: [Assigned by homology with 1CAUB]F 380 to F 424 ; The following residues NOT assigned to any domain: Chain "F" 44 - 224 The following residues NOT assigned to any domain: Chain "F" 241 - 424 The following residues NOT assigned to any domain: Chain "F" 44 - 224 The following residues NOT assigned to any domain: Chain "F" 241 - 424 The following residues NOT assigned to any domain: Chain "F" 44 - 224
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CAU A

SEED STORAGE PROTEIN 08-JUL-93 :: CANAVALIN (JACK BEAN 7S VICILIN)

DOMAIN 1: [Assigned by homology with 1CAUB]A 44 to A 177 ; DOMAIN 2: [Assigned by homology with 1CAUB]A 178 to A 224 ; The following residues NOT assigned to any domain: Chain "A" 241 - 424
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CAV A

SEED STORAGE PROTEIN 27-MAY-93 :: CANAVALIN (JACK BEAN 7S VICILIN)

DOMAIN 1: [Assigned by homology with 1CAUB]A 44 to A 177 ; DOMAIN 2: [Assigned by homology with 1CAUB]A 178 to A 224 ; The following residues NOT assigned to any domain: Chain "A" 241 - 424
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CAW A

SEED STORAGE PROTEIN 02-JUN-93 :: CANAVALIN (JACK BEAN 7S VICILIN)

DOMAIN 1: [Assigned by homology with 1CAUB]A 44 to A 177 ; DOMAIN 2: [Assigned by homology with 1CAUB]A 178 to A 224 ; The following residues NOT assigned to any domain: Chain "A" 241 - 424
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CAX A

SEED STORAGE PROTEIN 10-JUN-93 :: CANAVALIN (JACK BEAN 7S VICILIN)

DOMAIN 1: [Assigned by homology with 1CAUB]A 44 to A 177 ; DOMAIN 2: [Assigned by homology with 1CAUB]A 178 to A 224 ; The following residues NOT assigned to any domain: Chain "A" 241 - 424 The following residues NOT assigned to any domain: Chain "A" 44 - 224 The following residues NOT assigned to any domain: Chain "A" 241 - 424 The following residues NOT assigned to any domain: Chain "A" 44 - 224 The following residues NOT assigned to any domain: Chain "A" 241 - 424
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CAX C

SEED STORAGE PROTEIN 10-JUN-93 :: CANAVALIN (JACK BEAN 7S VICILIN)

DOMAIN 1: [Assigned by homology with 1CAUB]C 44 to C 177 ; DOMAIN 2: [Assigned by homology with 1CAUB]C 178 to C 224 ; The following residues NOT assigned to any domain: Chain "C" 44 - 224 The following residues NOT assigned to any domain: Chain "C" 241 - 424 The following residues NOT assigned to any domain: Chain "C" 241 - 424 The following residues NOT assigned to any domain: Chain "C" 44 - 224 The following residues NOT assigned to any domain: Chain "C" 241 - 424
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CAX E

SEED STORAGE PROTEIN 10-JUN-93 :: CANAVALIN (JACK BEAN 7S VICILIN)

DOMAIN 1: [Assigned by homology with 1CAUB]E 44 to E 177 ; DOMAIN 2: [Assigned by homology with 1CAUB]E 178 to E 224 ; The following residues NOT assigned to any domain: Chain "E" 44 - 224 The following residues NOT assigned to any domain: Chain "E" 241 - 424 The following residues NOT assigned to any domain: Chain "E" 44 - 224 The following residues NOT assigned to any domain: Chain "E" 241 - 424 The following residues NOT assigned to any domain: Chain "E" 241 - 424
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CPC K

LIGHT HARVESTING PROTEIN 11-OCT-90 :: C-PHYCOCYANIN

DOMAIN 1: [Assigned by homology with 1CPCA]K 1 to K 34 ; DOMAIN 2: [Assigned by homology with 1CPCA]K 35 to K 174 ; The following residues NOT assigned to any domain: Chain "K" 1 - 174 The following residues NOT assigned to any domain: Chain "K" 1 - 174 The following residues NOT assigned to any domain: Chain "K" 1 - 174
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CPC B

LIGHT HARVESTING PROTEIN 11-OCT-90 :: C-PHYCOCYANIN

DOMAIN 1: [Assigned by homology with 1CPCL]B 1 to B 35 ; DOMAIN 2: [Assigned by homology with 1CPCL]B 36 to B 174 ; The following residues NOT assigned to any domain: Chain "B" 1 - 174 The following residues NOT assigned to any domain: Chain "B" 1 - 174 The following residues NOT assigned to any domain: Chain "B" 1 - 174
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1KFD

NUCLEOTIDYLTRANSFERASE 23-SEP-93 :: DNA POLYMERASE I (KLENOW FRAGMENT) (E.C.2.7.7.7) C

DOMAIN 1: 324 to 516 ; DOMAIN 2: 519 to 927 ; The following residues NOT assigned to any domain: Chain " " 517 - 518 Chain " " 928 - 928
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1KLN A

NUCLEOTIDYLTRANSFERASE 24-MAY-94 :: DNA POLYMERASE I (KLENOW FRAGMENT) (E.C.2.7.7.7) M

DOMAIN 1: A 324 to A 516 ; DOMAIN 2: A 519 to A 927 ; The following residues NOT assigned to any domain: Chain "A" 517 - 518 Chain "A" 928 - 928 The following residues NOT assigned to any domain: Chain "A" 2 - 29
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DBP

BINDING PROTEIN 31-JAN-94 :: D-RIBOSE-BINDING PROTEIN MUTANT WITH GLY 72 REPLAC

DOMAIN 1: 1 to 102 ; 235 to 263 ; DOMAIN 2: 103 to 234 ; 264 to 270 ; The following residues NOT assigned to any domain: Chain " " 271 - 271
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3GBP

PERIPLASMIC BINDING PROTEIN 25-JAN-90 :: GALACTOSE-BINDING PROTEIN COMPLEX WITH GLUCOSE

DOMAIN 1: 3 to 109 ; 256 to 286 ; DOMAIN 2: 110 to 255 ; 287 to 300 ; The following residues NOT assigned to any domain: Chain " " 301 - 307
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GCA

GALACTOSE-BINDING PROTEIN 13-MAY-93 :: GLUCOSE/GALACTOSE-BINDING PROTEIN COMPLEX WITH GAL

DOMAIN 1: 1 to 109 ; 256 to 286 ; DOMAIN 2: 110 to 255 ; 287 to 300 ; The following residues NOT assigned to any domain: Chain " " 301 - 309
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GCG

GALACTOSE-BINDING PROTEIN 03-FEB-94 :: GALACTOSE/GLUCOSE-BINDING PROTEIN (CLOSED, UNLIGAN

DOMAIN 1: 1 to 109 ; 256 to 286 ; DOMAIN 2: 110 to 255 ; 287 to 300 ; The following residues NOT assigned to any domain: Chain " " 301 - 309
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2GBP

PERIPLASMIC BINDING PROTEIN 23-FEB-89 :: D-*GALACTOSE/D-*GLUCOSE BINDING PROTEIN (/GGBP$)

DOMAIN 1: 1 to 109 ; 256 to 286 ; DOMAIN 2: 110 to 255 ; 287 to 300 ; The following residues NOT assigned to any domain: Chain " " 301 - 309
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GLG

GALACTOSE-BINDING PROTEIN 27-DEC-93 :: GALACTOSE/GLUCOSE-BINDING PROTEIN COMPLEXED WITH D

DOMAIN 1: 1 to 109 ; 256 to 286 ; DOMAIN 2: 110 to 255 ; 287 to 300 ; The following residues NOT assigned to any domain: Chain " " 301 - 309
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3TMN E

HYDROLASE (METALLOPROTEINASE) 29-JUN-87 :: THERMOLYSIN (E.C.3.4.24.27) COMPLEX WITH VAL-TRP (

DOMAIN 1: E 1 to E 135 ; DOMAIN 2: E 137 to E 316 ; The following residues NOT assigned to any domain: Chain "E" 136 - 136 The following residues NOT assigned to any domain: Chain "E" 1 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4TLN

HYDROLASE (METALLOPROTEINASE) 08-FEB-82 :: THERMOLYSIN (E.C.3.4.24.27) COMPLEX WITH

DOMAIN 1: 1 to 135 ; DOMAIN 2: 137 to 316 ; The following residues NOT assigned to any domain: Chain " " 136 - 136
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4TMN E

HYDROLASE (METALLOPROTEINASE) 29-JUN-87 :: THERMOLYSIN (E.C.3.4.24.27) COMPLEX WITH

DOMAIN 1: E 1 to E 135 ; DOMAIN 2: E 137 to E 316 ; The following residues NOT assigned to any domain: Chain "E" 136 - 136 The following residues NOT assigned to any domain: Chain "E" 3 - 4
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HYT

HYDROLASE(METALLOPROTEINASE) 04-MAY-94 :: THERMOLYSIN (E.C.3.4.24.27) COMPLEXED WITH BENZYLS

DOMAIN 1: 1 to 135 ; DOMAIN 2: 137 to 316 ; The following residues NOT assigned to any domain: Chain " " 136 - 136
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5TLN

HYDROLASE (METALLOPROTEINASE) 08-FEB-82 :: THERMOLYSIN (E.C.3.4.24.27) COMPLEX WITH

DOMAIN 1: 1 to 135 ; DOMAIN 2: 137 to 316 ; The following residues NOT assigned to any domain: Chain " " 136 - 136
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5TMN E

HYDROLASE (METALLOPROTEINASE) 29-JUN-87 :: THERMOLYSIN (E.C.3.4.24.27) COMPLEX WITH

DOMAIN 1: E 1 to E 135 ; DOMAIN 2: E 137 to E 316 ; The following residues NOT assigned to any domain: Chain "E" 136 - 136 The following residues NOT assigned to any domain: Chain "E" 3 - 4
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2TMN E

HYDROLASE (METALLOPROTEINASE) 29-JUN-87 :: THERMOLYSIN (E.C.3.4.24.27) COMPLEX WITH

DOMAIN 1: E 1 to E 135 ; DOMAIN 2: E 137 to E 316 ; The following residues NOT assigned to any domain: Chain "E" 136 - 136 The following residues NOT assigned to any domain: Chain "E" 2 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6TMN E

HYDROLASE (METALLOPROTEINASE) 29-JUN-87 :: THERMOLYSIN (E.C.3.4.24.27) COMPLEX WITH

DOMAIN 1: E 1 to E 135 ; DOMAIN 2: E 137 to E 316 ; The following residues NOT assigned to any domain: Chain "E" 136 - 136 The following residues NOT assigned to any domain: Chain "E" 4 - 4
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7TLN

HYDROLASE (METALLOPROTEINASE) 27-JAN-83 :: THERMOLYSIN (E.C.3.4.24.27) COMPLEX WITH CH2CO(N-O

DOMAIN 1: 1 to 135 ; DOMAIN 2: 137 to 316 ; The following residues NOT assigned to any domain: Chain " " 136 - 136
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1THL

HYDROLASE(METALLOPROTEINASE) 17-NOV-93 :: THERMOLYSIN (E.C.3.4.24.27) COMPLEXED WITH A NOVEL

DOMAIN 1: 1 to 135 ; DOMAIN 2: 137 to 322 ; The following residues NOT assigned to any domain: Chain " " 136 - 136
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8TLN E

HYDROLASE(METALLOPROTEINASE) 01-SEP-93 :: THERMOLYSIN (E.C.3.4.24.27) COMPLEXED WITH VAL-LYS

DOMAIN 1: E 1 to E 135 ; DOMAIN 2: E 137 to E 316 ; The following residues NOT assigned to any domain: Chain "E" 136 - 136 The following residues NOT assigned to any domain: Chain "E" 322 - 323
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TLP E

HYDROLASE (METALLOPROTEINASE) 29-JUN-87 :: THERMOLYSIN (E.C.3.4.24.27) COMPLEX WITH PHOSPHORA

DOMAIN 1: E 1 to E 135 ; DOMAIN 2: E 137 to E 316 ; The following residues NOT assigned to any domain: Chain "E" 136 - 136 The following residues NOT assigned to any domain: Chain "E" 2 - 3
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TMN E

HYDROLASE (METALLOPROTEINASE) 29-JUN-87 :: THERMOLYSIN (E.C.3.4.24.27) COMPLEX WITH

DOMAIN 1: E 1 to E 135 ; DOMAIN 2: E 137 to E 316 ; The following residues NOT assigned to any domain: Chain "E" 136 - 136 The following residues NOT assigned to any domain: Chain "E" 2 - 3
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NPC

HYDROLASE(METALLOPROTEINASE) 08-JAN-92 :: NEUTRAL PROTEASE (E.C.3.4.24.27)

DOMAIN 1: 1 to 136 ; DOMAIN 2: 138 to 317 ; The following residues NOT assigned to any domain: Chain " " 137 - 137
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2FNR

OXIDOREDUCTASE(NADP+(A),FERREDOXIN(A)) 21-JUN-90 :: FERREDOXIN:/NADP==+==$ OXIDOREDUCTASE (FERREDOXIN

DOMAIN 1: 19 to 161 ; DOMAIN 2: 162 to 314 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GLB G

PHOSPHOTRANSFERASE 28-OCT-92 :: GLYCEROL KINASE (E.C.2.7.1.30) COMPLEX WITH GLYCER

DOMAIN 1: [Assigned by homology with 1GLAG]G 5 to G 253 ; DOMAIN 2: [Assigned by homology with 1GLAG]G 254 to G 4 ; The following residues NOT assigned to any domain: Chain "G" 1 - 168 The following residues NOT assigned to any domain: Chain "G" 255 - 499
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GLC G

PHOSPHOTRANSFERASE 07-MAR-94 :: GLYCEROL KINASE (E.C.2.7.1.30) COMPLEXED WITH THE

DOMAIN 1: [Assigned by homology with 1GLAG]G 5 to G 253 ; DOMAIN 2: [Assigned by homology with 1GLAG]G 254 to G 4 ; The following residues NOT assigned to any domain: Chain "G" 1 - 168 The following residues NOT assigned to any domain: Chain "G" 255 - 499
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GLD G

PHOSPHOTRANSFERASE 07-MAR-94 :: GLYCEROL KINASE (E.C.2.7.1.30) COMPLEXED WITH THE

DOMAIN 1: [Assigned by homology with 1GLAG]G 5 to G 253 ; DOMAIN 2: [Assigned by homology with 1GLAG]G 254 to G 4 ; The following residues NOT assigned to any domain: Chain "G" 1 - 168 The following residues NOT assigned to any domain: Chain "G" 255 - 499
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GLE G

PHOSPHOTRANSFERASE 07-MAR-94 :: GLYCEROL KINASE (E.C.2.7.1.30) COMPLEXED WITH THE

DOMAIN 1: [Assigned by homology with 1GLAG]G 5 to G 253 ; DOMAIN 2: [Assigned by homology with 1GLAG]G 254 to G 4 ; The following residues NOT assigned to any domain: Chain "G" 1 - 168 The following residues NOT assigned to any domain: Chain "G" 255 - 499
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PYG A

PRELIMINARY 07-JUL-92 :: PYRIDOXAL-5'-PYROPHOSPHORYL DERIVATIVE OF GLYCOGEN

DOMAIN 1: A 10 to A 488 ; DOMAIN 2: A 489 to A 836 ; The following residues NOT assigned to any domain: Chain "A" 20 - 836 The following residues NOT assigned to any domain: Chain "A" 10 - 836 The following residues NOT assigned to any domain: Chain "A" 10 - 836
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PYG C

PRELIMINARY 07-JUL-92 :: PYRIDOXAL-5'-PYROPHOSPHORYL DERIVATIVE OF GLYCOGEN

DOMAIN 1: C 10 to C 488 ; DOMAIN 2: C 489 to C 836 ; The following residues NOT assigned to any domain: Chain "C" 10 - 836 The following residues NOT assigned to any domain: Chain "C" 20 - 836 The following residues NOT assigned to any domain: Chain "C" 10 - 836
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PYG D

PRELIMINARY 07-JUL-92 :: PYRIDOXAL-5'-PYROPHOSPHORYL DERIVATIVE OF GLYCOGEN

DOMAIN 1: D 10 to D 488 ; DOMAIN 2: D 489 to D 836 ; The following residues NOT assigned to any domain: Chain "D" 10 - 836 The following residues NOT assigned to any domain: Chain "D" 20 - 836 The following residues NOT assigned to any domain: Chain "D" 10 - 836
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PYG B

PRELIMINARY 07-JUL-92 :: PYRIDOXAL-5'-PYROPHOSPHORYL DERIVATIVE OF GLYCOGEN

DOMAIN 1: B 20 to B 488 ; DOMAIN 2: B 489 to B 836 ; The following residues NOT assigned to any domain: Chain "B" 10 - 836 The following residues NOT assigned to any domain: Chain "B" 10 - 836 The following residues NOT assigned to any domain: Chain "B" 10 - 836
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GPY

GLYCOGEN PHOSPHORYLASE 31-MAR-93 :: GLYCOGEN PHOSPHORYLASE B (E.C.2.4.1.1) (T STATE) C

DOMAIN 1: 14 to 488 ; DOMAIN 2: 489 to 840 ; The following residues NOT assigned to any domain: Chain " " 841 - 841
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4GPB

GLYCOGEN PHOSPHORYLASE 04-JUN-90 :: GLYCOGEN PHOSPHORYLASE $B (E.C.2.4.1.1) (T STATE)

DOMAIN 1: 10 to 488 ; DOMAIN 2: 489 to 840 ; The following residues NOT assigned to any domain: Chain " " 841 - 842
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5GPB

GLYCOGEN PHOSPHORYLASE 04-JUN-90 :: GLYCOGEN PHOSPHORYLASE $B (E.C.2.4.1.1) (T STATE)

DOMAIN 1: 10 to 488 ; DOMAIN 2: 489 to 840 ; The following residues NOT assigned to any domain: Chain " " 841 - 842
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ABB A

GLYCOGEN PHOSPHORYLASE 09-APR-92 :: GLYCOGEN PHOSPHORYLASE (E.C.2.4.1.1) COMPLEX WITH

DOMAIN 1: A 10 to A 488 ; DOMAIN 2: A 489 to A 837 ; The following residues NOT assigned to any domain: Chain "A" 10 - 837 The following residues NOT assigned to any domain: Chain "A" 10 - 837 The following residues NOT assigned to any domain: Chain "A" 10 - 837
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ABB B

GLYCOGEN PHOSPHORYLASE 09-APR-92 :: GLYCOGEN PHOSPHORYLASE (E.C.2.4.1.1) COMPLEX WITH

DOMAIN 1: B 10 to B 488 ; DOMAIN 2: B 489 to B 837 ; The following residues NOT assigned to any domain: Chain "B" 10 - 837 The following residues NOT assigned to any domain: Chain "B" 10 - 837 The following residues NOT assigned to any domain: Chain "B" 10 - 837
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ABB C

GLYCOGEN PHOSPHORYLASE 09-APR-92 :: GLYCOGEN PHOSPHORYLASE (E.C.2.4.1.1) COMPLEX WITH

DOMAIN 1: C 10 to C 488 ; DOMAIN 2: C 489 to C 837 ; The following residues NOT assigned to any domain: Chain "C" 10 - 837 The following residues NOT assigned to any domain: Chain "C" 10 - 837 The following residues NOT assigned to any domain: Chain "C" 10 - 837
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ABB D

GLYCOGEN PHOSPHORYLASE 09-APR-92 :: GLYCOGEN PHOSPHORYLASE (E.C.2.4.1.1) COMPLEX WITH

DOMAIN 1: D 10 to D 488 ; DOMAIN 2: D 489 to D 837 ; The following residues NOT assigned to any domain: Chain "D" 10 - 837 The following residues NOT assigned to any domain: Chain "D" 10 - 837 The following residues NOT assigned to any domain: Chain "D" 10 - 837
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6GPB

GLYCOGEN PHOSPHORYLASE 04-JUN-90 :: GLYCOGEN PHOSPHORYLASE $B (E.C.2.4.1.1) (T STATE)

DOMAIN 1: 14 to 488 ; DOMAIN 2: 489 to 840 ; The following residues NOT assigned to any domain: Chain " " 841 - 841
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7GPB A

GLYCOGEN PHOSPHORYLASE 13-NOV-90 :: GLYCOGEN PHOSPHORYLASE $B (E.C.2.4.1.1) (R STATE)

DOMAIN 1: A 10 to A 488 ; DOMAIN 2: A 489 to A 837 ; The following residues NOT assigned to any domain: Chain "A" 10 - 837 The following residues NOT assigned to any domain: Chain "A" 10 - 837 The following residues NOT assigned to any domain: Chain "A" 10 - 837
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7GPB B

GLYCOGEN PHOSPHORYLASE 13-NOV-90 :: GLYCOGEN PHOSPHORYLASE $B (E.C.2.4.1.1) (R STATE)

DOMAIN 1: B 10 to B 488 ; DOMAIN 2: B 489 to B 837 ; The following residues NOT assigned to any domain: Chain "B" 10 - 837 The following residues NOT assigned to any domain: Chain "B" 10 - 837 The following residues NOT assigned to any domain: Chain "B" 10 - 837
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7GPB C

GLYCOGEN PHOSPHORYLASE 13-NOV-90 :: GLYCOGEN PHOSPHORYLASE $B (E.C.2.4.1.1) (R STATE)

DOMAIN 1: C 10 to C 488 ; DOMAIN 2: C 489 to C 837 ; The following residues NOT assigned to any domain: Chain "C" 10 - 837 The following residues NOT assigned to any domain: Chain "C" 10 - 837 The following residues NOT assigned to any domain: Chain "C" 10 - 837
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7GPB D

GLYCOGEN PHOSPHORYLASE 13-NOV-90 :: GLYCOGEN PHOSPHORYLASE $B (E.C.2.4.1.1) (R STATE)

DOMAIN 1: D 10 to D 488 ; DOMAIN 2: D 489 to D 837 ; The following residues NOT assigned to any domain: Chain "D" 10 - 837 The following residues NOT assigned to any domain: Chain "D" 10 - 837 The following residues NOT assigned to any domain: Chain "D" 10 - 837
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3GPB

GLYCOGEN PHOSPHORYLASE 04-JUN-90 :: GLYCOGEN PHOSPHORYLASE $B (E.C.2.4.1.1) (T STATE)

DOMAIN 1: 10 to 488 ; DOMAIN 2: 489 to 840 ; The following residues NOT assigned to any domain: Chain " " 841 - 842
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8GPB

GLYCOGEN PHOSPHORYLASE 13-NOV-90 :: GLYCOGEN PHOSPHORYLASE $B (E.C.2.4.1.1) (T STATE)

DOMAIN 1: 11 to 488 ; DOMAIN 2: 489 to 840 ; The following residues NOT assigned to any domain: Chain " " 841 - 842
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2GPB

GLYCOGEN PHOSPHORYLASE 04-JUN-90 :: GLYCOGEN PHOSPHORYLASE $B (E.C.2.4.1.1) (T STATE)

DOMAIN 1: 12 to 488 ; DOMAIN 2: 489 to 840 ; The following residues NOT assigned to any domain: Chain " " 841 - 842
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

9GPB A

GLYCOGEN PHOSPHORYLASE 17-DEC-90 :: GLYCOGEN PHOSPHORYLASE $B (E.C.2.4.1.1) (R STATE)

DOMAIN 1: A 10 to A 488 ; DOMAIN 2: A 489 to A 837 ; The following residues NOT assigned to any domain: Chain "A" 10 - 837 The following residues NOT assigned to any domain: Chain "A" 10 - 837 The following residues NOT assigned to any domain: Chain "A" 10 - 837
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

9GPB B

GLYCOGEN PHOSPHORYLASE 17-DEC-90 :: GLYCOGEN PHOSPHORYLASE $B (E.C.2.4.1.1) (R STATE)

DOMAIN 1: B 10 to B 488 ; DOMAIN 2: B 489 to B 837 ; The following residues NOT assigned to any domain: Chain "B" 10 - 837 The following residues NOT assigned to any domain: Chain "B" 10 - 837 The following residues NOT assigned to any domain: Chain "B" 10 - 837
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

9GPB C

GLYCOGEN PHOSPHORYLASE 17-DEC-90 :: GLYCOGEN PHOSPHORYLASE $B (E.C.2.4.1.1) (R STATE)

DOMAIN 1: C 10 to C 488 ; DOMAIN 2: C 489 to C 837 ; The following residues NOT assigned to any domain: Chain "C" 10 - 837 The following residues NOT assigned to any domain: Chain "C" 10 - 837 The following residues NOT assigned to any domain: Chain "C" 10 - 837
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

9GPB D

GLYCOGEN PHOSPHORYLASE 17-DEC-90 :: GLYCOGEN PHOSPHORYLASE $B (E.C.2.4.1.1) (R STATE)

DOMAIN 1: D 10 to D 488 ; DOMAIN 2: D 489 to D 837 ; The following residues NOT assigned to any domain: Chain "D" 10 - 837 The following residues NOT assigned to any domain: Chain "D" 10 - 837 The following residues NOT assigned to any domain: Chain "D" 10 - 837
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GPA A

GLYCOGEN PHOSPHORYLASE 13-NOV-90 :: GLYCOGEN PHOSPHORYLASE $A (E.C.2.4.1.1) (R STATE)

DOMAIN 1: A 10 to A 488 ; DOMAIN 2: A 489 to A 837 ; The following residues NOT assigned to any domain: Chain "A" 10 - 839 The following residues NOT assigned to any domain: Chain "A" 10 - 837 The following residues NOT assigned to any domain: Chain "A" 10 - 837
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GPA B

GLYCOGEN PHOSPHORYLASE 13-NOV-90 :: GLYCOGEN PHOSPHORYLASE $A (E.C.2.4.1.1) (R STATE)

DOMAIN 1: B 10 to B 488 ; DOMAIN 2: B 489 to B 839 ; The following residues NOT assigned to any domain: Chain "B" 10 - 837 The following residues NOT assigned to any domain: Chain "B" 10 - 837 The following residues NOT assigned to any domain: Chain "B" 10 - 837
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GPA C

GLYCOGEN PHOSPHORYLASE 13-NOV-90 :: GLYCOGEN PHOSPHORYLASE $A (E.C.2.4.1.1) (R STATE)

DOMAIN 1: C 10 to C 488 ; DOMAIN 2: C 489 to C 837 ; The following residues NOT assigned to any domain: Chain "C" 10 - 837 The following residues NOT assigned to any domain: Chain "C" 10 - 839 The following residues NOT assigned to any domain: Chain "C" 10 - 837
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GPA D

GLYCOGEN PHOSPHORYLASE 13-NOV-90 :: GLYCOGEN PHOSPHORYLASE $A (E.C.2.4.1.1) (R STATE)

DOMAIN 1: D 10 to D 488 ; DOMAIN 2: D 489 to D 837 ; The following residues NOT assigned to any domain: Chain "D" 10 - 837 The following residues NOT assigned to any domain: Chain "D" 10 - 839 The following residues NOT assigned to any domain: Chain "D" 10 - 837
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2IFF H

IMMUNOGLOBULIN/HYDROLASE(O-GLYCOSYL) 03-FEB-94 :: IGG1 FAB FRAGMENT (HYHEL-5) COMPLEXED WITH LYSOZYM

DOMAIN 1: [Assigned by homology with 1HILA]H 2 to H 111 ; DOMAIN 2: [Assigned by homology with 1HILA]H 117 to H 214 ; The following residues NOT assigned to any domain: Chain "H" 1 - 212 The following residues NOT assigned to any domain: Chain "H" 112 - 116 Chain "H" 215 - 215 The following residues NOT assigned to any domain: Chain "H" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HFL H

COMPLEX(ANTIBODY-ANTIGEN) 17-AUG-87 :: IG*G1 FAB FRAGMENT (HY/HEL$-5) AND LYSOZYME (E.C.3

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 111 ; DOMAIN 2: [Assigned by homology with 1HILA]H 117 to H 213 ; The following residues NOT assigned to any domain: Chain "H" 1 - 212 The following residues NOT assigned to any domain: Chain "H" 112 - 116 The following residues NOT assigned to any domain: Chain "H" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CGS H

IMMUNOGLOBULIN 06-OCT-93 :: IGG2B (KAPPA) FAB FRAGMENT AGAINST ANTIGEN

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 111 ; DOMAIN 2: [Assigned by homology with 1HILA]H 117 to H 214 ; The following residues NOT assigned to any domain: Chain "H" 1 - 219 The following residues NOT assigned to any domain: Chain "H" 112 - 116
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CGR H

IMMUNOGLOBULIN 23-NOV-93 :: IGG2B (KAPPA) FAB FRAGMENT COMPLEXED WITH ANTIGEN

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 111 ; DOMAIN 2: [Assigned by homology with 1HILA]H 117 to H 214 ; The following residues NOT assigned to any domain: Chain "H" 1 - 219 The following residues NOT assigned to any domain: Chain "H" 112 - 116
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FOR H

IMMUNOGLOBULIN 24-MAY-94 :: IGG2A FAB FRAGMENT (FAB17-IA) (ORTHORHOMBIC CRYSTA

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 114 ; DOMAIN 2: [Assigned by homology with 1HILA]H 120 to H 217 ; The following residues NOT assigned to any domain: Chain "H" 1 - 210 The following residues NOT assigned to any domain: Chain "H" 115 - 119 Chain "H" 218 - 219
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TET H

IMMUNOGLOBULIN 21-JUN-93 :: IGG1 MONOCLONAL FAB FRAGMENT (TE33) COMPLEX WITH C

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 108 ; DOMAIN 2: [Assigned by homology with 1HILA]H 114 to H 211 ; The following residues NOT assigned to any domain: Chain "H" 1 - 211 The following residues NOT assigned to any domain: Chain "H" 109 - 113 Chain "H" 212 - 213 The following residues NOT assigned to any domain: Chain "H" 3 - 14
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EAP B

CATALYTIC ANTIBODY 10-AUG-94 :: 17E8 COMPLEXED WITH PHENYL [1-(1-N-SUCCINYLAMINO)P

DOMAIN 1: [Assigned by homology with 1HILA]B 1 to B 119 ; DOMAIN 2: [Assigned by homology with 1HILA]B 125 to B 221 ; The following residues NOT assigned to any domain: Chain "B" 1 - 214 The following residues NOT assigned to any domain: Chain "B" 120 - 124
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FAI H

IMMUNOGLOBULIN 27-MAY-92 :: FAB FRAGMENT FROM A MONOCLONAL ANTI-ARSONATE ANTIB

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 119 ; DOMAIN 2: [Assigned by homology with 1HILA]H 125 to H 221 ; The following residues NOT assigned to any domain: Chain "H" 1 - 214 The following residues NOT assigned to any domain: Chain "H" 120 - 124
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2F19 H

IMMUNOGLOBULIN 27-MAY-92 :: FAB FRAGMENT FROM A MONOCLONAL ANTI-ARSONATE ANTIB

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 119 ; DOMAIN 2: [Assigned by homology with 1HILA]H 125 to H 221 ; The following residues NOT assigned to any domain: Chain "H" 1 - 214 The following residues NOT assigned to any domain: Chain "H" 120 - 124
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MFB H

IMMUNOGLOBULIN 25-OCT-93 :: FAB FRAGMENT (MURINE SE155-4) COMPLEX WITH HEPTASA

DOMAIN 1: [Assigned by homology with 1HILA]H 251 to H 363 ; DOMAIN 2: [Assigned by homology with 1HILA]H 369 to H 466 ; The following residues NOT assigned to any domain: Chain "H" 1 - 212 The following residues NOT assigned to any domain: Chain "H" 364 - 368 Chain "H" 467 - 468
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MFC H

IMMUNOGLOBULIN 25-OCT-93 :: FAB FRAGMENT (MURINE SE155-4) COMPLEX WITH HEPTASA

DOMAIN 1: [Assigned by homology with 1HILA]H 251 to H 363 ; DOMAIN 2: [Assigned by homology with 1HILA]H 369 to H 466 ; The following residues NOT assigned to any domain: Chain "H" 1 - 212 The following residues NOT assigned to any domain: Chain "H" 364 - 368 Chain "H" 467 - 468
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MFD H

IMMUNOGLOBULIN 25-OCT-93 :: FAB FRAGMENT (MURINE SE155-4) COMPLEX WITH THE

DOMAIN 1: [Assigned by homology with 1HILA]H 251 to H 363 ; DOMAIN 2: [Assigned by homology with 1HILA]H 369 to H 466 ; The following residues NOT assigned to any domain: Chain "H" 1 - 212 The following residues NOT assigned to any domain: Chain "H" 364 - 368 Chain "H" 467 - 468
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6FAB H

IMMUNOGLOBULIN 17-JAN-91 :: ANTIGEN-BINDING FRAGMENT OF THE MURINE ANTI-PHENYL

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 116 ; DOMAIN 2: [Assigned by homology with 1HILA]H 122 to H 219 ; The following residues NOT assigned to any domain: Chain "H" 1 - 214 The following residues NOT assigned to any domain: Chain "H" 117 - 121 Chain "H" 220 - 222
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1JEL H

IMMUNOGLOBULIN 02-APR-93 :: FAB JE142 MONOCLONAL ANTIBODY COMPLEXED WITH HISTI

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 108 ; DOMAIN 2: [Assigned by homology with 1HILA]H 114 to H 210 ; The following residues NOT assigned to any domain: Chain "H" 1 - 212 The following residues NOT assigned to any domain: Chain "H" 109 - 113 The following residues NOT assigned to any domain: Chain "H" 1 - 85
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BBD H

PRELIMINARY 05-MAY-92 :: FAB FRAGMENT FROM 8F5 ANTIBODY AGAINST HRV2

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 113 ; DOMAIN 2: [Assigned by homology with 1HILA]H 119 to H 216 ; The following residues NOT assigned to any domain: Chain "H" 1 - 219 The following residues NOT assigned to any domain: Chain "H" 114 - 118 Chain "H" 217 - 218
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FDL H

COMPLEX (ANTIBODY-ANTIGEN) 27-AUG-90 :: IG*G1 FAB FRAGMENT (ANTI-LYSOZYME ANTIBODY D1.3, K

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 111 ; DOMAIN 2: [Assigned by homology with 1HILA]H 117 to H 214 ; The following residues NOT assigned to any domain: Chain "H" 1 - 214 The following residues NOT assigned to any domain: Chain "H" 112 - 116 Chain "H" 215 - 218 The following residues NOT assigned to any domain: Chain "H" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IGI H

IMMUNOGLOBULIN 19-FEB-93 :: FAB (IGG2A,KAPPA) FRAGMENT (26-10)

DOMAIN 1: [Assigned by homology with 1HILA]H 2 to H 108 ; DOMAIN 2: [Assigned by homology with 1HILA]H 114 to H 226 ; The following residues NOT assigned to any domain: Chain "H" 1 - 213 The following residues NOT assigned to any domain: Chain "H" 109 - 113 Chain "H" 227 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IGJ B

IMMUNOGLOBULIN 19-FEB-93 :: FAB (IGG2A,KAPPA) FRAGMENT (26-10) COMPLEX WITH DI

DOMAIN 1: [Assigned by homology with 1HILA]B 2 to B 108 ; DOMAIN 2: [Assigned by homology with 1HILA]B 114 to B 226 ; The following residues NOT assigned to any domain: Chain "B" 1 - 211 The following residues NOT assigned to any domain: Chain "B" 109 - 113 Chain "B" 227 - 227 The following residues NOT assigned to any domain: Chain "B" 1 - 211 The following residues NOT assigned to any domain: Chain "B" 2 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IGJ D

IMMUNOGLOBULIN 19-FEB-93 :: FAB (IGG2A,KAPPA) FRAGMENT (26-10) COMPLEX WITH DI

DOMAIN 1: [Assigned by homology with 1HILA]D 2 to D 108 ; DOMAIN 2: [Assigned by homology with 1HILA]D 114 to D 226 ; The following residues NOT assigned to any domain: Chain "D" 1 - 211 The following residues NOT assigned to any domain: Chain "D" 2 - 227 The following residues NOT assigned to any domain: Chain "D" 1 - 211 The following residues NOT assigned to any domain: Chain "D" 109 - 113 Chain "D" 227 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FIG H

IMMUNOGLOBULIN 07-JAN-94 :: IMMUNOGLOBULIN G1 (KAPPA LIGHT CHAIN) FAB' FRAGMEN

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 108 ; DOMAIN 2: [Assigned by homology with 1HILA]H 114 to H 223 ; The following residues NOT assigned to any domain: Chain "H" 1 - 214 The following residues NOT assigned to any domain: Chain "H" 109 - 113
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NCB H

PRELIMINARY 21-JAN-92 :: N9 NEURAMINIDASE MUTANT WITH ASN 329 REPLACED BY A

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 108 ; DOMAIN 2: [Assigned by homology with 1HILA]H 114 to H 224 ; The following residues NOT assigned to any domain: Chain "H" 81 - 468 The following residues NOT assigned to any domain: Chain "H" 1 - 214 The following residues NOT assigned to any domain: Chain "H" 109 - 113 Chain "H" 225 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NCD H

PRELIMINARY 21-JAN-92 :: N9 NEURAMINIDASE-/NC$41 FAB COMPLEX (E.C.3.2.1.18)

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 108 ; DOMAIN 2: [Assigned by homology with 1HILA]H 114 to H 224 ; The following residues NOT assigned to any domain: Chain "H" 81 - 468 The following residues NOT assigned to any domain: Chain "H" 1 - 214 The following residues NOT assigned to any domain: Chain "H" 109 - 113 Chain "H" 225 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NCA H

PRELIMINARY 21-JAN-92 :: N9 NEURAMINIDASE-/NC$41 FAB COMPLEX (E.C.3.2.1.18)

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 108 ; DOMAIN 2: [Assigned by homology with 1HILA]H 114 to H 224 ; The following residues NOT assigned to any domain: Chain "H" 81 - 468 The following residues NOT assigned to any domain: Chain "H" 1 - 214 The following residues NOT assigned to any domain: Chain "H" 109 - 113 Chain "H" 225 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NCC H

PRELIMINARY 21-JAN-92 :: N9 NEURAMINIDASE MUTANT WITH ILE 368 REPLACED BY A

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 108 ; DOMAIN 2: [Assigned by homology with 1HILA]H 114 to H 224 ; The following residues NOT assigned to any domain: Chain "H" 81 - 468 The following residues NOT assigned to any domain: Chain "H" 1 - 214 The following residues NOT assigned to any domain: Chain "H" 109 - 113 Chain "H" 225 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2IGF H

IMMUNOGLOBULIN 21-MAR-91 :: IGG1 FAB' FRAGMENT (B13I2) COMPLEX WITH PEPTIDE

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 108 ; DOMAIN 2: [Assigned by homology with 1HILA]H 114 to H 226 ; The following residues NOT assigned to any domain: Chain "H" 1 - 214 The following residues NOT assigned to any domain: Chain "H" 109 - 113 Chain "H" 227 - 233 The following residues NOT assigned to any domain: Chain "H" 69 - 75
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IGF H

IMMUNOGLOBULIN 21-MAR-91 :: IGG1 FAB' FRAGMENT (B13I2)

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 108 ; DOMAIN 2: [Assigned by homology with 1HILA]H 114 to H 226 ; The following residues NOT assigned to any domain: Chain "H" 1 - 214 The following residues NOT assigned to any domain: Chain "H" 109 - 113 Chain "H" 227 - 227 The following residues NOT assigned to any domain: Chain "H" 1 - 214 The following residues NOT assigned to any domain: Chain "H" 1 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IGF J

IMMUNOGLOBULIN 21-MAR-91 :: IGG1 FAB' FRAGMENT (B13I2)

DOMAIN 1: [Assigned by homology with 1HILA]J 1 to J 108 ; DOMAIN 2: [Assigned by homology with 1HILA]J 114 to J 226 ; The following residues NOT assigned to any domain: Chain "J" 1 - 214 The following residues NOT assigned to any domain: Chain "J" 1 - 227 The following residues NOT assigned to any domain: Chain "J" 1 - 214 The following residues NOT assigned to any domain: Chain "J" 109 - 113 Chain "J" 227 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ACY H

COMPLEX(ANTIBODY/HIV-1 FRAGMENT) 10-FEB-94 :: IGG1 FAB FRAGMENT (59.1) COMPLEXED WITH HIV-1 GP12

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 108 ; DOMAIN 2: [Assigned by homology with 1HILA]H 114 to H 224 ; The following residues NOT assigned to any domain: Chain "H" 1 - 211 The following residues NOT assigned to any domain: Chain "H" 109 - 113 Chain "H" 225 - 226 The following residues NOT assigned to any domain: Chain "H" 315 - 326
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4FAB H

IMMUNOGLOBULIN 10-APR-89 :: 4-4-20 (IG*G2A=KAPPA=) FAB FRAGMENT - FLUORESCEIN

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 113 ; DOMAIN 2: [Assigned by homology with 1HILA]H 119 to H 216 ; The following residues NOT assigned to any domain: Chain "H" 1 - 219 The following residues NOT assigned to any domain: Chain "H" 114 - 118
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DBA H

IMMUNOGLOBULIN 10-NOV-92 :: FAB' FRAGMENT OF THE DB3 ANTI-STEROID MONOCLONAL A

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 108 ; DOMAIN 2: [Assigned by homology with 1HILA]H 114 to H 226 ; The following residues NOT assigned to any domain: Chain "H" 1 - 211 The following residues NOT assigned to any domain: Chain "H" 109 - 113 Chain "H" 227 - 228
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DBB H

IMMUNOGLOBULIN 11-NOV-92 :: FAB' FRAGMENT OF THE DB3 ANTI-STEROID MONOCLONAL A

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 108 ; DOMAIN 2: [Assigned by homology with 1HILA]H 114 to H 226 ; The following residues NOT assigned to any domain: Chain "H" 1 - 211 The following residues NOT assigned to any domain: Chain "H" 109 - 113 Chain "H" 227 - 228
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DBJ H

IMMUNOGLOBULIN 24-AUG-93 :: FAB' FRAGMENT OF MONOCLONAL ANTIBODY DB3

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 108 ; DOMAIN 2: [Assigned by homology with 1HILA]H 114 to H 226 ; The following residues NOT assigned to any domain: Chain "H" 1 - 211 The following residues NOT assigned to any domain: Chain "H" 109 - 113 Chain "H" 227 - 228
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DBK H

IMMUNOGLOBULIN 24-AUG-93 :: FAB' FRAGMENT OF MONOCLONAL ANTIBODY DB3

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 108 ; DOMAIN 2: [Assigned by homology with 1HILA]H 114 to H 226 ; The following residues NOT assigned to any domain: Chain "H" 1 - 211 The following residues NOT assigned to any domain: Chain "H" 109 - 113 Chain "H" 227 - 228
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DBM H

IMMUNOGLOBULIN 24-AUG-93 :: FAB' FRAGMENT OF MONOCLONAL ANTIBODY DB3

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 108 ; DOMAIN 2: [Assigned by homology with 1HILA]H 114 to H 226 ; The following residues NOT assigned to any domain: Chain "H" 1 - 211 The following residues NOT assigned to any domain: Chain "H" 109 - 113 Chain "H" 227 - 228
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2DBL H

IMMUNOGLOBULIN 08-FEB-94 :: FAB' FRAGMENT OF MONOCLONAL ANTIBODY DB3

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 108 ; DOMAIN 2: [Assigned by homology with 1HILA]H 114 to H 226 ; The following residues NOT assigned to any domain: Chain "H" 1 - 211 The following residues NOT assigned to any domain: Chain "H" 109 - 113 Chain "H" 227 - 228
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2FGW H

IMMUNOGLOBULIN 16-JAN-94 :: FAB FRAGMENT OF A HUMANIZED VERSION OF THE ANTI-CD

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 119 ; DOMAIN 2: [Assigned by homology with 1HILA]H 125 to H 223 ; The following residues NOT assigned to any domain: Chain "H" 1 - 214 The following residues NOT assigned to any domain: Chain "H" 120 - 124 Chain "H" 224 - 228
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3HFM H

COMPLEX(ANTIBODY-ANTIGEN) 11-AUG-88 :: IG*G1 FAB FRAGMENT (HY/HEL$-10) AND LYSOZYME (E.C.

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 108 ; DOMAIN 2: [Assigned by homology with 1HILA]H 114 to H 211 ; The following residues NOT assigned to any domain: Chain "H" 1 - 214 The following residues NOT assigned to any domain: Chain "H" 109 - 113 Chain "H" 212 - 215 The following residues NOT assigned to any domain: Chain "H" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GIG H

IMMUNOGLOBULIN 20-JAN-93 :: IGG1 FAB FRAGMENT (HC19)

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 117 ; DOMAIN 2: [Assigned by homology with 1HILA]H 123 to H 220 ; The following residues NOT assigned to any domain: Chain "H" 1 - 210 The following residues NOT assigned to any domain: Chain "H" 118 - 122 Chain "H" 221 - 221
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BAF H

PRELIMINARY 16-JAN-92 :: AN02 FAB FRAGMENT

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 110 ; DOMAIN 2: [Assigned by homology with 1HILA]H 116 to H 213 ; The following residues NOT assigned to any domain: Chain "H" 1 - 214 The following residues NOT assigned to any domain: Chain "H" 111 - 115 Chain "H" 214 - 217
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BBJ H

PRELIMINARY 30-APR-92 :: B72.3, FAB' FRAGMENT OF CHIMAERIC MONOCLONAL ANTIB

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 109 ; DOMAIN 2: [Assigned by homology with 1HILA]H 115 to H 212 ; The following residues NOT assigned to any domain: Chain "H" 1 - 211 The following residues NOT assigned to any domain: Chain "H" 110 - 114
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FVE B

IMMUNOGLOBULIN 20-OCT-92 :: FAB FRAGMENT OF HUMANIZED ANTIBODY 4D5, VERSION 7

DOMAIN 1: [Assigned by homology with 1HILA]B 1 to B 115 ; DOMAIN 2: [Assigned by homology with 1HILA]B 121 to B 219 ; The following residues NOT assigned to any domain: Chain "B" 1 - 214 The following residues NOT assigned to any domain: Chain "B" 116 - 120 Chain "B" 220 - 223 The following residues NOT assigned to any domain: Chain "B" 1 - 214 The following residues NOT assigned to any domain: Chain "B" 1 - 223
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FVE D

IMMUNOGLOBULIN 20-OCT-92 :: FAB FRAGMENT OF HUMANIZED ANTIBODY 4D5, VERSION 7

DOMAIN 1: [Assigned by homology with 1HILA]D 1 to D 115 ; DOMAIN 2: [Assigned by homology with 1HILA]D 121 to D 219 ; The following residues NOT assigned to any domain: Chain "D" 1 - 214 The following residues NOT assigned to any domain: Chain "D" 1 - 223 The following residues NOT assigned to any domain: Chain "D" 1 - 214 The following residues NOT assigned to any domain: Chain "D" 116 - 120 Chain "D" 220 - 223
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IND H

IMMUNOGLOBULIN 14-JUN-93 :: CHA255 IMMUNOGLOBULIN FAB' FRAGMENT (IGG1-LAMBDA)

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 109 ; DOMAIN 2: [Assigned by homology with 1HILA]H 114 to H 211 ; The following residues NOT assigned to any domain: Chain "H" 2 - 212 The following residues NOT assigned to any domain: Chain "H" 110 - 113 Chain "H" 212 - 213
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1INE H

IMMUNOGLOBULIN 14-JUN-93 :: CHA255 IMMUNOGLOBULIN FAB' FRAGMENT (IGG1-LAMBDA)

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 109 ; DOMAIN 2: [Assigned by homology with 1HILA]H 114 to H 211 ; The following residues NOT assigned to any domain: Chain "H" 2 - 212 The following residues NOT assigned to any domain: Chain "H" 110 - 113 Chain "H" 212 - 213
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FVD B

IMMUNOGLOBULIN 20-OCT-92 :: FAB FRAGMENT OF HUMANIZED ANTIBODY 4D5, VERSION 4

DOMAIN 1: [Assigned by homology with 1HILA]B 1 to B 115 ; DOMAIN 2: [Assigned by homology with 1HILA]B 121 to B 219 ; The following residues NOT assigned to any domain: Chain "B" 1 - 214 The following residues NOT assigned to any domain: Chain "B" 116 - 120 Chain "B" 220 - 223 The following residues NOT assigned to any domain: Chain "B" 1 - 214 The following residues NOT assigned to any domain: Chain "B" 1 - 223
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FVD D

IMMUNOGLOBULIN 20-OCT-92 :: FAB FRAGMENT OF HUMANIZED ANTIBODY 4D5, VERSION 4

DOMAIN 1: [Assigned by homology with 1HILA]D 1 to D 115 ; DOMAIN 2: [Assigned by homology with 1HILA]D 121 to D 219 ; The following residues NOT assigned to any domain: Chain "D" 1 - 214 The following residues NOT assigned to any domain: Chain "D" 1 - 223 The following residues NOT assigned to any domain: Chain "D" 1 - 214 The following residues NOT assigned to any domain: Chain "D" 116 - 120 Chain "D" 220 - 223
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HIL D

PRELIMINARY 08-JUL-92 :: IGG2A FAB FRAGMENT (FAB 17/9)

DOMAIN 1: [Assigned by homology with 1HILA]D 1 to D 108 ; DOMAIN 2: [Assigned by homology with 1HILA]D 114 to D 226 ; The following residues NOT assigned to any domain: Chain "D" 1 - 211 The following residues NOT assigned to any domain: Chain "D" 1 - 228 The following residues NOT assigned to any domain: Chain "D" 1 - 211 The following residues NOT assigned to any domain: Chain "D" 109 - 113 Chain "D" 227 - 228
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HIL B

PRELIMINARY 08-JUL-92 :: IGG2A FAB FRAGMENT (FAB 17/9)

DOMAIN 1: [Assigned by homology with 1HILA]B 1 to B 108 ; DOMAIN 2: [Assigned by homology with 1HILA]B 114 to B 226 ; The following residues NOT assigned to any domain: Chain "B" 1 - 211 The following residues NOT assigned to any domain: Chain "B" 109 - 113 Chain "B" 227 - 228 The following residues NOT assigned to any domain: Chain "B" 1 - 211 The following residues NOT assigned to any domain: Chain "B" 1 - 228
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HIM L

PRELIMINARY 08-JUL-92 :: IGG2A FAB FRAGMENT (FAB 17/9) COMPLEX WITH A SYNTH

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 108 ; DOMAIN 2: [Assigned by homology with 1HILA]L 114 to L 226 ; The following residues NOT assigned to any domain: Chain " " 1 - 211 The following residues NOT assigned to any domain: Chain " " 1 - 228 The following residues NOT assigned to any domain: Chain " " 100 - 107 The following residues NOT assigned to any domain: Chain " " 1 - 211 The following residues NOT assigned to any domain: Chain " " 1 - 228 The following residues NOT assigned to any domain: Chain " " 100 - 108
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HIM M

PRELIMINARY 08-JUL-92 :: IGG2A FAB FRAGMENT (FAB 17/9) COMPLEX WITH A SYNTH

DOMAIN 1: [Assigned by homology with 1HILA]M 1 to M 108 ; DOMAIN 2: [Assigned by homology with 1HILA]M 114 to M 226 ; The following residues NOT assigned to any domain: Chain " " 1 - 211 The following residues NOT assigned to any domain: Chain " " 1 - 228 The following residues NOT assigned to any domain: Chain " " 100 - 107 The following residues NOT assigned to any domain: Chain " " 1 - 211 The following residues NOT assigned to any domain: Chain " " 1 - 228 The following residues NOT assigned to any domain: Chain " " 100 - 108
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IFH H

IMMUNOGLOBULIN 06-MAY-93 :: IGG2A FAB FRAGMENT (FAB 17/9) COMPLEX WITH PEPTIDE

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 108 ; DOMAIN 2: [Assigned by homology with 1HILA]H 114 to H 226 ; The following residues NOT assigned to any domain: Chain "H" 1 - 212 The following residues NOT assigned to any domain: Chain "H" 109 - 113 Chain "H" 227 - 228 The following residues NOT assigned to any domain: Chain "H" 100 - 107
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HIN H

IMMUNOGLOBULIN 08-JUL-92 :: IGG2A FAB FRAGMENT (FAB 17/9) COMPLEXED WITH PEPTI

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 108 ; DOMAIN 2: [Assigned by homology with 1HILA]H 114 to H 226 ; The following residues NOT assigned to any domain: Chain "H" 1 - 211 The following residues NOT assigned to any domain: Chain "H" 109 - 113 Chain "H" 227 - 228 The following residues NOT assigned to any domain: Chain "H" 100 - 107
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GGB H

IMMUNOGLOBULIN 19-JUL-93 :: IGG2A FAB FRAGMENT (50.1)

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 108 ; DOMAIN 2: [Assigned by homology with 1HILA]H 114 to H 226 ; The following residues NOT assigned to any domain: Chain "H" 1 - 211 The following residues NOT assigned to any domain: Chain "H" 109 - 113 Chain "H" 227 - 228
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GGC H

IMMUNOGLOBULIN 19-JUL-93 :: IGG2A FAB FRAGMENT (50.1)

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 108 ; DOMAIN 2: [Assigned by homology with 1HILA]H 114 to H 226 ; The following residues NOT assigned to any domain: Chain "H" 1 - 211 The following residues NOT assigned to any domain: Chain "H" 109 - 113 Chain "H" 227 - 228
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GGI H

IMMUNOGLOBULIN 02-APR-93 :: IGG2A FAB FRAGMENT (50.1) COMPLEX WITH 16-RESIDUE

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 108 ; DOMAIN 2: [Assigned by homology with 1HILA]H 114 to H 226 ; The following residues NOT assigned to any domain: Chain "H" 1 - 211 The following residues NOT assigned to any domain: Chain "H" 109 - 113 Chain "H" 227 - 228 The following residues NOT assigned to any domain: Chain "H" 311 - 321 The following residues NOT assigned to any domain: Chain "H" 1 - 211 The following residues NOT assigned to any domain: Chain "H" 1 - 228 The following residues NOT assigned to any domain: Chain "H" 311 - 321
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GGI J

IMMUNOGLOBULIN 02-APR-93 :: IGG2A FAB FRAGMENT (50.1) COMPLEX WITH 16-RESIDUE

DOMAIN 1: [Assigned by homology with 1HILA]J 1 to J 108 ; DOMAIN 2: [Assigned by homology with 1HILA]J 114 to J 226 ; The following residues NOT assigned to any domain: Chain "J" 1 - 211 The following residues NOT assigned to any domain: Chain "J" 1 - 228 The following residues NOT assigned to any domain: Chain "J" 311 - 321 The following residues NOT assigned to any domain: Chain "J" 1 - 211 The following residues NOT assigned to any domain: Chain "J" 109 - 113 Chain "J" 227 - 228 The following residues NOT assigned to any domain: Chain "J" 311 - 321
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DFB H

IMMUNOGLOBULIN 27-MAR-92 :: 3D6 FAB

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 121 ; DOMAIN 2: [Assigned by homology with 1HILA]H 127 to H 225 ; The following residues NOT assigned to any domain: Chain "H" 1 - 212 The following residues NOT assigned to any domain: Chain "H" 122 - 126 Chain "H" 226 - 229
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2GFB B

IMMUNOGLOBULIN 07-JUL-94 :: IGG2A FAB FRAGMENT (CNJ206)

DOMAIN 1: [Assigned by homology with 1HILA]B 1 to B 108 ; DOMAIN 2: [Assigned by homology with 1HILA]B 113 to B 224 ; The following residues NOT assigned to any domain: Chain "B" 1 - 214 The following residues NOT assigned to any domain: Chain "B" 109 - 112 Chain "B" 225 - 227 The following residues NOT assigned to any domain: Chain "B" 1 - 214 The following residues NOT assigned to any domain: Chain "B" 1 - 227 The following residues NOT assigned to any domain: Chain "B" 1 - 214 The following residues NOT assigned to any domain: Chain "B" 1 - 227 The following residues NOT assigned to any domain: Chain "B" 1 - 214 The following residues NOT assigned to any domain: Chain "B" 1 - 227 The following residues NOT assigned to any domain: Chain "B" 1 - 214 The following residues NOT assigned to any domain: Chain "B" 1 - 227 The following residues NOT assigned to any domain: Chain "B" 1 - 214 The following residues NOT assigned to any domain: Chain "B" 1 - 227 The following residues NOT assigned to any domain: Chain "B" 1 - 214 The following residues NOT assigned to any domain: Chain "B" 1 - 227 The following residues NOT assigned to any domain: Chain "B" 1 - 214 The following residues NOT assigned to any domain: Chain "B" 1 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2GFB D

IMMUNOGLOBULIN 07-JUL-94 :: IGG2A FAB FRAGMENT (CNJ206)

DOMAIN 1: [Assigned by homology with 1HILA]D 1 to D 108 ; DOMAIN 2: [Assigned by homology with 1HILA]D 113 to D 224 ; The following residues NOT assigned to any domain: Chain "D" 1 - 214 The following residues NOT assigned to any domain: Chain "D" 1 - 227 The following residues NOT assigned to any domain: Chain "D" 1 - 214 The following residues NOT assigned to any domain: Chain "D" 109 - 112 Chain "D" 225 - 227 The following residues NOT assigned to any domain: Chain "D" 1 - 214 The following residues NOT assigned to any domain: Chain "D" 1 - 227 The following residues NOT assigned to any domain: Chain "D" 1 - 214 The following residues NOT assigned to any domain: Chain "D" 1 - 227 The following residues NOT assigned to any domain: Chain "D" 1 - 214 The following residues NOT assigned to any domain: Chain "D" 1 - 227 The following residues NOT assigned to any domain: Chain "D" 1 - 214 The following residues NOT assigned to any domain: Chain "D" 1 - 227 The following residues NOT assigned to any domain: Chain "D" 1 - 214 The following residues NOT assigned to any domain: Chain "D" 1 - 227 The following residues NOT assigned to any domain: Chain "D" 1 - 214 The following residues NOT assigned to any domain: Chain "D" 1 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2GFB F

IMMUNOGLOBULIN 07-JUL-94 :: IGG2A FAB FRAGMENT (CNJ206)

DOMAIN 1: [Assigned by homology with 1HILA]F 1 to F 108 ; DOMAIN 2: [Assigned by homology with 1HILA]F 113 to F 224 ; The following residues NOT assigned to any domain: Chain "F" 1 - 214 The following residues NOT assigned to any domain: Chain "F" 1 - 227 The following residues NOT assigned to any domain: Chain "F" 1 - 214 The following residues NOT assigned to any domain: Chain "F" 1 - 227 The following residues NOT assigned to any domain: Chain "F" 1 - 214 The following residues NOT assigned to any domain: Chain "F" 109 - 112 Chain "F" 225 - 227 The following residues NOT assigned to any domain: Chain "F" 1 - 214 The following residues NOT assigned to any domain: Chain "F" 1 - 227 The following residues NOT assigned to any domain: Chain "F" 1 - 214 The following residues NOT assigned to any domain: Chain "F" 1 - 227 The following residues NOT assigned to any domain: Chain "F" 1 - 214 The following residues NOT assigned to any domain: Chain "F" 1 - 227 The following residues NOT assigned to any domain: Chain "F" 1 - 214 The following residues NOT assigned to any domain: Chain "F" 1 - 227 The following residues NOT assigned to any domain: Chain "F" 1 - 214 The following residues NOT assigned to any domain: Chain "F" 1 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2GFB H

IMMUNOGLOBULIN 07-JUL-94 :: IGG2A FAB FRAGMENT (CNJ206)

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 108 ; DOMAIN 2: [Assigned by homology with 1HILA]H 113 to H 224 ; The following residues NOT assigned to any domain: Chain "H" 1 - 214 The following residues NOT assigned to any domain: Chain "H" 1 - 227 The following residues NOT assigned to any domain: Chain "H" 1 - 214 The following residues NOT assigned to any domain: Chain "H" 1 - 227 The following residues NOT assigned to any domain: Chain "H" 1 - 214 The following residues NOT assigned to any domain: Chain "H" 1 - 227 The following residues NOT assigned to any domain: Chain "H" 1 - 214 The following residues NOT assigned to any domain: Chain "H" 109 - 112 Chain "H" 225 - 227 The following residues NOT assigned to any domain: Chain "H" 1 - 214 The following residues NOT assigned to any domain: Chain "H" 1 - 227 The following residues NOT assigned to any domain: Chain "H" 1 - 214 The following residues NOT assigned to any domain: Chain "H" 1 - 227 The following residues NOT assigned to any domain: Chain "H" 1 - 214 The following residues NOT assigned to any domain: Chain "H" 1 - 227 The following residues NOT assigned to any domain: Chain "H" 1 - 214 The following residues NOT assigned to any domain: Chain "H" 1 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2GFB J

IMMUNOGLOBULIN 07-JUL-94 :: IGG2A FAB FRAGMENT (CNJ206)

DOMAIN 1: [Assigned by homology with 1HILA]J 1 to J 108 ; DOMAIN 2: [Assigned by homology with 1HILA]J 113 to J 224 ; The following residues NOT assigned to any domain: Chain "J" 1 - 214 The following residues NOT assigned to any domain: Chain "J" 1 - 227 The following residues NOT assigned to any domain: Chain "J" 1 - 214 The following residues NOT assigned to any domain: Chain "J" 1 - 227 The following residues NOT assigned to any domain: Chain "J" 1 - 214 The following residues NOT assigned to any domain: Chain "J" 1 - 227 The following residues NOT assigned to any domain: Chain "J" 1 - 214 The following residues NOT assigned to any domain: Chain "J" 1 - 227 The following residues NOT assigned to any domain: Chain "J" 1 - 214 The following residues NOT assigned to any domain: Chain "J" 109 - 112 Chain "J" 225 - 227 The following residues NOT assigned to any domain: Chain "J" 1 - 214 The following residues NOT assigned to any domain: Chain "J" 1 - 227 The following residues NOT assigned to any domain: Chain "J" 1 - 214 The following residues NOT assigned to any domain: Chain "J" 1 - 227 The following residues NOT assigned to any domain: Chain "J" 1 - 214 The following residues NOT assigned to any domain: Chain "J" 1 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2GFB L

IMMUNOGLOBULIN 07-JUL-94 :: IGG2A FAB FRAGMENT (CNJ206)

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 108 ; DOMAIN 2: [Assigned by homology with 1HILA]L 113 to L 224 ; The following residues NOT assigned to any domain: Chain "L" 1 - 214 The following residues NOT assigned to any domain: Chain "L" 1 - 227 The following residues NOT assigned to any domain: Chain "L" 1 - 214 The following residues NOT assigned to any domain: Chain "L" 1 - 227 The following residues NOT assigned to any domain: Chain "L" 1 - 214 The following residues NOT assigned to any domain: Chain "L" 1 - 227 The following residues NOT assigned to any domain: Chain "L" 1 - 214 The following residues NOT assigned to any domain: Chain "L" 1 - 227 The following residues NOT assigned to any domain: Chain "L" 1 - 214 The following residues NOT assigned to any domain: Chain "L" 1 - 227 The following residues NOT assigned to any domain: Chain "L" 1 - 214 The following residues NOT assigned to any domain: Chain "L" 109 - 112 Chain "L" 225 - 227 The following residues NOT assigned to any domain: Chain "L" 1 - 214 The following residues NOT assigned to any domain: Chain "L" 1 - 227 The following residues NOT assigned to any domain: Chain "L" 1 - 214 The following residues NOT assigned to any domain: Chain "L" 1 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2GFB N

IMMUNOGLOBULIN 07-JUL-94 :: IGG2A FAB FRAGMENT (CNJ206)

DOMAIN 1: [Assigned by homology with 1HILA]N 1 to N 108 ; DOMAIN 2: [Assigned by homology with 1HILA]N 113 to N 224 ; The following residues NOT assigned to any domain: Chain "N" 1 - 214 The following residues NOT assigned to any domain: Chain "N" 1 - 227 The following residues NOT assigned to any domain: Chain "N" 1 - 214 The following residues NOT assigned to any domain: Chain "N" 1 - 227 The following residues NOT assigned to any domain: Chain "N" 1 - 214 The following residues NOT assigned to any domain: Chain "N" 1 - 227 The following residues NOT assigned to any domain: Chain "N" 1 - 214 The following residues NOT assigned to any domain: Chain "N" 1 - 227 The following residues NOT assigned to any domain: Chain "N" 1 - 214 The following residues NOT assigned to any domain: Chain "N" 1 - 227 The following residues NOT assigned to any domain: Chain "N" 1 - 214 The following residues NOT assigned to any domain: Chain "N" 1 - 227 The following residues NOT assigned to any domain: Chain "N" 1 - 214 The following residues NOT assigned to any domain: Chain "N" 109 - 112 Chain "N" 225 - 227 The following residues NOT assigned to any domain: Chain "N" 1 - 214 The following residues NOT assigned to any domain: Chain "N" 1 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2GFB P

IMMUNOGLOBULIN 07-JUL-94 :: IGG2A FAB FRAGMENT (CNJ206)

DOMAIN 1: [Assigned by homology with 1HILA]P 1 to P 108 ; DOMAIN 2: [Assigned by homology with 1HILA]P 113 to P 224 ; The following residues NOT assigned to any domain: Chain "P" 1 - 214 The following residues NOT assigned to any domain: Chain "P" 1 - 227 The following residues NOT assigned to any domain: Chain "P" 1 - 214 The following residues NOT assigned to any domain: Chain "P" 1 - 227 The following residues NOT assigned to any domain: Chain "P" 1 - 214 The following residues NOT assigned to any domain: Chain "P" 1 - 227 The following residues NOT assigned to any domain: Chain "P" 1 - 214 The following residues NOT assigned to any domain: Chain "P" 1 - 227 The following residues NOT assigned to any domain: Chain "P" 1 - 214 The following residues NOT assigned to any domain: Chain "P" 1 - 227 The following residues NOT assigned to any domain: Chain "P" 1 - 214 The following residues NOT assigned to any domain: Chain "P" 1 - 227 The following residues NOT assigned to any domain: Chain "P" 1 - 214 The following residues NOT assigned to any domain: Chain "P" 1 - 227 The following residues NOT assigned to any domain: Chain "P" 1 - 214 The following residues NOT assigned to any domain: Chain "P" 109 - 112 Chain "P" 225 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8FAB D

IMMUNOGLOBULIN 23-MAR-92 :: FAB FRAGMENT FROM HUMAN IMMUNOGLOBULIN IGG1 (LAMBD

DOMAIN 1: [Assigned by homology with 1HILA]D 1 to D 116 ; DOMAIN 2: [Assigned by homology with 1HILA]D 122 to D 220 ; The following residues NOT assigned to any domain: Chain "D" 3 - 208 The following residues NOT assigned to any domain: Chain "D" 1 - 223 The following residues NOT assigned to any domain: Chain "D" 3 - 208 The following residues NOT assigned to any domain: Chain "D" 117 - 121 Chain "D" 221 - 222
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FRG H

IMMUNOGLOBULIN/VIRUS HEMAGGLUTININ 17-JAN-94 :: IGG2A FAB FRAGMENT (FAB 26/9) COMPLEXED WITH INFLU

DOMAIN 1: [Assigned by homology with 1HILA]H 218 to H 332 ; DOMAIN 2: [Assigned by homology with 1HILA]H 338 to H 435 ; The following residues NOT assigned to any domain: Chain "H" 1 - 217 The following residues NOT assigned to any domain: Chain "H" 333 - 337 Chain "H" 436 - 437 The following residues NOT assigned to any domain: Chain "H" 1 - 9
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CBV H

IMMUNOGLOBULIN 16-MAR-93 :: FAB (BV04-01) AUTOANTIBODY BINDING SINGLE-STRANDED

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 116 ; DOMAIN 2: [Assigned by homology with 1HILA]H 122 to H 219 ; The following residues NOT assigned to any domain: Chain "H" 1 - 219 The following residues NOT assigned to any domain: Chain "H" 117 - 121 The following residues NOT assigned to any domain: Chain "H" 1 - 3
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NBV H

IMMUNOGLOBULIN 16-MAR-93 :: FAB (BV04-01) AUTOANTIBODY BINDING SINGLE-STRANDED

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 116 ; DOMAIN 2: [Assigned by homology with 1HILA]H 122 to H 219 ; The following residues NOT assigned to any domain: Chain "H" 1 - 219 The following residues NOT assigned to any domain: Chain "H" 117 - 121
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MAM H

IMMUNOGLOBULIN 14-JAN-92 :: ANTIGEN-BINDING FRAGMENT (FAB) (IGG2B, KAPPA)

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 114 ; DOMAIN 2: [Assigned by homology with 1HILA]H 120 to H 217 ; The following residues NOT assigned to any domain: Chain "H" 1 - 214 The following residues NOT assigned to any domain: Chain "H" 115 - 119
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2FB4 H

IMMUNOGLOBULIN 18-APR-89 :: IMMUNOGLOBULIN FAB

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 113 ; DOMAIN 2: [Assigned by homology with 1HILA]H 119 to H 217 ; The following residues NOT assigned to any domain: Chain "H" 1 - 214 The following residues NOT assigned to any domain: Chain "H" 114 - 118 Chain "H" 218 - 221
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2IG2 H

IMMUNOGLOBULIN 18-APR-89 :: IMMUNOGLOBULIN G1

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 113 ; DOMAIN 2: [Assigned by homology with 1HILA]H 119 to H 217 ; The following residues NOT assigned to any domain: Chain "H" 1 - 214 The following residues NOT assigned to any domain: Chain "H" 114 - 118 Chain "H" 218 - 231
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MFE H

IMMUNOGLOBULIN 25-OCT-93 :: FAB FRAGMENT (MURINE SE155-4) COMPLEX WITH DODECAS

DOMAIN 1: [Assigned by homology with 1HILA]H 251 to H 363 ; DOMAIN 2: [Assigned by homology with 1HILA]H 369 to H 466 ; The following residues NOT assigned to any domain: Chain "H" 1 - 211 The following residues NOT assigned to any domain: Chain "H" 364 - 368 Chain "H" 467 - 468
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MFA

IMMUNOGLOBULIN 25-OCT-93 :: FV FRAGMENT (MURINE SE155-4) COMPLEX WITH THE TRIS

DOMAIN 1: [Assigned by homology with 1HILA] 1 L to 252 H ; DOMAIN 2: [Assigned by homology with 1HILA] 258 H to 362 H ; The following residues NOT assigned to any domain: Chain " " 253H - 257H Chain " " 363H - 367H
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCO H

PRELIMINARY 25-FEB-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER (IGG1) WITH

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 320 ; DOMAIN 2: [Assigned by homology with 1HILA]H 326 to H 426 ; The following residues NOT assigned to any domain: Chain "H" 1 - 216 The following residues NOT assigned to any domain: Chain "H" 321 - 325 Chain "H" 427 - 428
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8FAB B

IMMUNOGLOBULIN 23-MAR-92 :: FAB FRAGMENT FROM HUMAN IMMUNOGLOBULIN IGG1 (LAMBD

DOMAIN 1: [Assigned by homology with 1HILA]B 1 to B 116 ; DOMAIN 2: [Assigned by homology with 1HILA]B 122 to B 220 ; The following residues NOT assigned to any domain: Chain "B" 3 - 208 The following residues NOT assigned to any domain: Chain "B" 117 - 121 Chain "B" 221 - 223 The following residues NOT assigned to any domain: Chain "B" 3 - 208 The following residues NOT assigned to any domain: Chain "B" 1 - 222
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7FAB H

PRELIMINARY 20-NOV-91 :: LAMBDA IMMUNOGLOBULIN FAB(PRIME) - NEW

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 112 ; DOMAIN 2: [Assigned by homology with 1HILA]H 118 to H 216 ; The following residues NOT assigned to any domain: Chain "H" 1 - 204 The following residues NOT assigned to any domain: Chain "H" 113 - 117 Chain "H" 217 - 217
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2FBJ H

IMMUNOGLOBULIN 18-AUG-89 :: IG*A FAB FRAGMENT (J539) (GALACTAN-BINDING)

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 113 ; DOMAIN 2: [Assigned by homology with 1HILA]H 119 to H 218 ; The following residues NOT assigned to any domain: Chain "H" 1 - 213 The following residues NOT assigned to any domain: Chain "H" 114 - 118 Chain "H" 219 - 220
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7FAB L

PRELIMINARY 20-NOV-91 :: LAMBDA IMMUNOGLOBULIN FAB(PRIME) - NEW

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 98 ; DOMAIN 2: [Assigned by homology with 1HILA]L 104 to L 203 ; The following residues NOT assigned to any domain: Chain "L" 99 - 103 Chain "L" 204 - 204 The following residues NOT assigned to any domain: Chain "L" 1 - 217
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8FAB A

IMMUNOGLOBULIN 23-MAR-92 :: FAB FRAGMENT FROM HUMAN IMMUNOGLOBULIN IGG1 (LAMBD

DOMAIN 1: [Assigned by homology with 1HILA]A 3 to A 102 ; DOMAIN 2: [Assigned by homology with 1HILA]A 108 to A 207 ; The following residues NOT assigned to any domain: Chain "A" 103 - 107 Chain "A" 208 - 208 The following residues NOT assigned to any domain: Chain "A" 1 - 223 The following residues NOT assigned to any domain: Chain "A" 3 - 208 The following residues NOT assigned to any domain: Chain "A" 1 - 222
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8FAB C

IMMUNOGLOBULIN 23-MAR-92 :: FAB FRAGMENT FROM HUMAN IMMUNOGLOBULIN IGG1 (LAMBD

DOMAIN 1: [Assigned by homology with 1HILA]C 3 to C 102 ; DOMAIN 2: [Assigned by homology with 1HILA]C 108 to C 207 ; The following residues NOT assigned to any domain: Chain "C" 3 - 208 The following residues NOT assigned to any domain: Chain "C" 1 - 223 The following residues NOT assigned to any domain: Chain "C" 103 - 107 Chain "C" 208 - 208 The following residues NOT assigned to any domain: Chain "C" 1 - 222
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BJL 1

IMMUNOGLOBULIN 11-MAR-91 :: BENCE-*JONES PROTEIN LOC (CRYSTALLIZED FROM AMMONI

DOMAIN 1: [Assigned by homology with 1HILA]1 1 to 1 107 ; DOMAIN 2: [Assigned by homology with 1HILA]1 113 to 1 212 ; The following residues NOT assigned to any domain: Chain "1" 108 - 112 Chain "1" 213 - 217 The following residues NOT assigned to any domain: Chain "1" 1 - 217
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BJL 2

IMMUNOGLOBULIN 11-MAR-91 :: BENCE-*JONES PROTEIN LOC (CRYSTALLIZED FROM AMMONI

DOMAIN 1: [Assigned by homology with 1HILA]2 1 to 2 107 ; DOMAIN 2: [Assigned by homology with 1HILA]2 113 to 2 212 ; The following residues NOT assigned to any domain: Chain "2" 1 - 217 The following residues NOT assigned to any domain: Chain "2" 108 - 112 Chain "2" 213 - 217
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2IG2 L

IMMUNOGLOBULIN 18-APR-89 :: IMMUNOGLOBULIN G1

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 104 ; DOMAIN 2: [Assigned by homology with 1HILA]L 110 to L 209 ; The following residues NOT assigned to any domain: Chain "L" 105 - 109 Chain "L" 210 - 214 The following residues NOT assigned to any domain: Chain "L" 1 - 231
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2FB4 L

IMMUNOGLOBULIN 18-APR-89 :: IMMUNOGLOBULIN FAB

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 104 ; DOMAIN 2: [Assigned by homology with 1HILA]L 110 to L 209 ; The following residues NOT assigned to any domain: Chain "L" 105 - 109 Chain "L" 210 - 214 The following residues NOT assigned to any domain: Chain "L" 1 - 221
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2BJL 1

IMMUNOGLOBULIN 11-MAR-91 :: BENCE-*JONES PROTEIN LOC (CRYSTALLIZED FROM DISTIL

DOMAIN 1: [Assigned by homology with 1HILA]1 1 to 1 107 ; DOMAIN 2: [Assigned by homology with 1HILA]1 113 to 1 212 ; The following residues NOT assigned to any domain: Chain "1" 108 - 112 Chain "1" 213 - 217 The following residues NOT assigned to any domain: Chain "1" 1 - 217
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2BJL 2

IMMUNOGLOBULIN 11-MAR-91 :: BENCE-*JONES PROTEIN LOC (CRYSTALLIZED FROM DISTIL

DOMAIN 1: [Assigned by homology with 1HILA]2 1 to 2 107 ; DOMAIN 2: [Assigned by homology with 1HILA]2 113 to 2 212 ; The following residues NOT assigned to any domain: Chain "2" 1 - 217 The following residues NOT assigned to any domain: Chain "2" 108 - 112 Chain "2" 213 - 217
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MCG 1

IMMUNOGLOBULIN 09-MAY-89 :: IMMUNOGLOBULIN LAMBDA LIGHT CHAIN DIMER (/MCG$)

DOMAIN 1: [Assigned by homology with 1HILA]1 1 to 1 106 ; DOMAIN 2: [Assigned by homology with 1HILA]1 112 to 1 211 ; The following residues NOT assigned to any domain: Chain "1" 107 - 111 Chain "1" 212 - 216 The following residues NOT assigned to any domain: Chain "1" 1 - 216
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MCG 2

IMMUNOGLOBULIN 09-MAY-89 :: IMMUNOGLOBULIN LAMBDA LIGHT CHAIN DIMER (/MCG$)

DOMAIN 1: [Assigned by homology with 1HILA]2 1 to 2 106 ; DOMAIN 2: [Assigned by homology with 1HILA]2 112 to 2 211 ; The following residues NOT assigned to any domain: Chain "2" 1 - 216 The following residues NOT assigned to any domain: Chain "2" 107 - 111 Chain "2" 212 - 216
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCB A

PRELIMINARY 25-JAN-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]A 1 to A 106 ; DOMAIN 2: [Assigned by homology with 1HILA]A 112 to A 211 ; The following residues NOT assigned to any domain: Chain "A" 107 - 111 Chain "A" 212 - 216 The following residues NOT assigned to any domain: Chain "A" 1 - 216 The following residues NOT assigned to any domain: Chain "A" 1 - 4
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCB B

PRELIMINARY 25-JAN-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]B 1 to B 106 ; DOMAIN 2: [Assigned by homology with 1HILA]B 112 to B 211 ; The following residues NOT assigned to any domain: Chain "B" 1 - 216 The following residues NOT assigned to any domain: Chain "B" 107 - 111 Chain "B" 212 - 216 The following residues NOT assigned to any domain: Chain "B" 1 - 4
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCC A

PRELIMINARY 25-JAN-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]A 1 to A 106 ; DOMAIN 2: [Assigned by homology with 1HILA]A 112 to A 211 ; The following residues NOT assigned to any domain: Chain "A" 107 - 111 Chain "A" 212 - 216 The following residues NOT assigned to any domain: Chain "A" 1 - 216 The following residues NOT assigned to any domain: Chain "A" 0 - 4
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCC B

PRELIMINARY 25-JAN-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]B 1 to B 106 ; DOMAIN 2: [Assigned by homology with 1HILA]B 112 to B 211 ; The following residues NOT assigned to any domain: Chain "B" 1 - 216 The following residues NOT assigned to any domain: Chain "B" 107 - 111 Chain "B" 212 - 216 The following residues NOT assigned to any domain: Chain "B" 0 - 4
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCD A

PRELIMINARY 25-JAN-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]A 1 to A 106 ; DOMAIN 2: [Assigned by homology with 1HILA]A 112 to A 211 ; The following residues NOT assigned to any domain: Chain "A" 107 - 111 Chain "A" 212 - 216 The following residues NOT assigned to any domain: Chain "A" 1 - 216 The following residues NOT assigned to any domain: Chain "A" 0 - 4
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCD B

PRELIMINARY 25-JAN-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]B 1 to B 106 ; DOMAIN 2: [Assigned by homology with 1HILA]B 112 to B 211 ; The following residues NOT assigned to any domain: Chain "B" 1 - 216 The following residues NOT assigned to any domain: Chain "B" 107 - 111 Chain "B" 212 - 216 The following residues NOT assigned to any domain: Chain "B" 0 - 4
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCE A

PRELIMINARY 25-JAN-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]A 1 to A 106 ; DOMAIN 2: [Assigned by homology with 1HILA]A 112 to A 211 ; The following residues NOT assigned to any domain: Chain "A" 107 - 111 Chain "A" 212 - 216 The following residues NOT assigned to any domain: Chain "A" 1 - 216 The following residues NOT assigned to any domain: Chain "A" 0 - 5
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCE B

PRELIMINARY 25-JAN-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]B 1 to B 106 ; DOMAIN 2: [Assigned by homology with 1HILA]B 112 to B 211 ; The following residues NOT assigned to any domain: Chain "B" 1 - 216 The following residues NOT assigned to any domain: Chain "B" 107 - 111 Chain "B" 212 - 216 The following residues NOT assigned to any domain: Chain "B" 0 - 5
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCF A

PRELIMINARY 25-JAN-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]A 1 to A 106 ; DOMAIN 2: [Assigned by homology with 1HILA]A 112 to A 211 ; The following residues NOT assigned to any domain: Chain "A" 107 - 111 Chain "A" 212 - 216 The following residues NOT assigned to any domain: Chain "A" 1 - 216 The following residues NOT assigned to any domain: Chain "A" 0 - 6
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCF B

PRELIMINARY 25-JAN-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]B 1 to B 106 ; DOMAIN 2: [Assigned by homology with 1HILA]B 112 to B 211 ; The following residues NOT assigned to any domain: Chain "B" 1 - 216 The following residues NOT assigned to any domain: Chain "B" 107 - 111 Chain "B" 212 - 216 The following residues NOT assigned to any domain: Chain "B" 0 - 6
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCH A

PRELIMINARY 25-JAN-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]A 1 to A 106 ; DOMAIN 2: [Assigned by homology with 1HILA]A 112 to A 211 ; The following residues NOT assigned to any domain: Chain "A" 107 - 111 Chain "A" 212 - 216 The following residues NOT assigned to any domain: Chain "A" 1 - 216 The following residues NOT assigned to any domain: Chain "A" 0 - 6
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCH B

PRELIMINARY 25-JAN-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]B 1 to B 106 ; DOMAIN 2: [Assigned by homology with 1HILA]B 112 to B 211 ; The following residues NOT assigned to any domain: Chain "B" 1 - 216 The following residues NOT assigned to any domain: Chain "B" 107 - 111 Chain "B" 212 - 216 The following residues NOT assigned to any domain: Chain "B" 0 - 6
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCI A

PRELIMINARY 25-JAN-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]A 1 to A 106 ; DOMAIN 2: [Assigned by homology with 1HILA]A 112 to A 211 ; The following residues NOT assigned to any domain: Chain "A" 107 - 111 Chain "A" 212 - 216 The following residues NOT assigned to any domain: Chain "A" 1 - 216 The following residues NOT assigned to any domain: Chain "A" 0 - 3
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCI B

PRELIMINARY 25-JAN-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]B 1 to B 106 ; DOMAIN 2: [Assigned by homology with 1HILA]B 112 to B 211 ; The following residues NOT assigned to any domain: Chain "B" 1 - 216 The following residues NOT assigned to any domain: Chain "B" 107 - 111 Chain "B" 212 - 216 The following residues NOT assigned to any domain: Chain "B" 0 - 3
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCJ A

PRELIMINARY 25-JAN-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]A 1 to A 106 ; DOMAIN 2: [Assigned by homology with 1HILA]A 112 to A 211 ; The following residues NOT assigned to any domain: Chain "A" 107 - 111 Chain "A" 212 - 216 The following residues NOT assigned to any domain: Chain "A" 1 - 216 The following residues NOT assigned to any domain: Chain "A" 0 - 3
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCJ B

PRELIMINARY 25-JAN-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]B 1 to B 106 ; DOMAIN 2: [Assigned by homology with 1HILA]B 112 to B 211 ; The following residues NOT assigned to any domain: Chain "B" 1 - 216 The following residues NOT assigned to any domain: Chain "B" 107 - 111 Chain "B" 212 - 216 The following residues NOT assigned to any domain: Chain "B" 0 - 3
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCK A

PRELIMINARY 25-FEB-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]A 1 to A 106 ; DOMAIN 2: [Assigned by homology with 1HILA]A 112 to A 211 ; The following residues NOT assigned to any domain: Chain "A" 107 - 111 Chain "A" 212 - 216 The following residues NOT assigned to any domain: Chain "A" 1 - 216 The following residues NOT assigned to any domain: Chain "A" 0 - 3
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCK B

PRELIMINARY 25-FEB-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]B 1 to B 106 ; DOMAIN 2: [Assigned by homology with 1HILA]B 112 to B 211 ; The following residues NOT assigned to any domain: Chain "B" 1 - 216 The following residues NOT assigned to any domain: Chain "B" 107 - 111 Chain "B" 212 - 216 The following residues NOT assigned to any domain: Chain "B" 0 - 3
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCL A

PRELIMINARY 25-FEB-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]A 1 to A 106 ; DOMAIN 2: [Assigned by homology with 1HILA]A 112 to A 211 ; The following residues NOT assigned to any domain: Chain "A" 107 - 111 Chain "A" 212 - 216 The following residues NOT assigned to any domain: Chain "A" 1 - 216 The following residues NOT assigned to any domain: Chain "A" 0 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCL B

PRELIMINARY 25-FEB-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]B 1 to B 106 ; DOMAIN 2: [Assigned by homology with 1HILA]B 112 to B 211 ; The following residues NOT assigned to any domain: Chain "B" 1 - 216 The following residues NOT assigned to any domain: Chain "B" 107 - 111 Chain "B" 212 - 216 The following residues NOT assigned to any domain: Chain "B" 0 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCN A

PRELIMINARY 25-FEB-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]A 1 to A 106 ; DOMAIN 2: [Assigned by homology with 1HILA]A 112 to A 211 ; The following residues NOT assigned to any domain: Chain "A" 107 - 111 Chain "A" 212 - 216 The following residues NOT assigned to any domain: Chain "A" 1 - 216 The following residues NOT assigned to any domain: Chain "A" 0 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCN B

PRELIMINARY 25-FEB-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]B 1 to B 106 ; DOMAIN 2: [Assigned by homology with 1HILA]B 112 to B 211 ; The following residues NOT assigned to any domain: Chain "B" 1 - 216 The following residues NOT assigned to any domain: Chain "B" 107 - 111 Chain "B" 212 - 216 The following residues NOT assigned to any domain: Chain "B" 0 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCQ A

PRELIMINARY 25-FEB-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]A 1 to A 106 ; DOMAIN 2: [Assigned by homology with 1HILA]A 112 to A 211 ; The following residues NOT assigned to any domain: Chain "A" 107 - 111 Chain "A" 212 - 216 The following residues NOT assigned to any domain: Chain "A" 1 - 216 The following residues NOT assigned to any domain: Chain "A" 0 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCQ B

PRELIMINARY 25-FEB-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]B 1 to B 106 ; DOMAIN 2: [Assigned by homology with 1HILA]B 112 to B 211 ; The following residues NOT assigned to any domain: Chain "B" 1 - 216 The following residues NOT assigned to any domain: Chain "B" 107 - 111 Chain "B" 212 - 216 The following residues NOT assigned to any domain: Chain "B" 0 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCR A

PRELIMINARY 25-FEB-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]A 1 to A 106 ; DOMAIN 2: [Assigned by homology with 1HILA]A 112 to A 211 ; The following residues NOT assigned to any domain: Chain "A" 107 - 111 Chain "A" 212 - 216 The following residues NOT assigned to any domain: Chain "A" 1 - 216 The following residues NOT assigned to any domain: Chain "A" 0 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCR B

PRELIMINARY 25-FEB-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]B 1 to B 106 ; DOMAIN 2: [Assigned by homology with 1HILA]B 112 to B 211 ; The following residues NOT assigned to any domain: Chain "B" 1 - 216 The following residues NOT assigned to any domain: Chain "B" 107 - 111 Chain "B" 212 - 216 The following residues NOT assigned to any domain: Chain "B" 0 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCS A

PRELIMINARY 25-FEB-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]A 1 to A 106 ; DOMAIN 2: [Assigned by homology with 1HILA]A 112 to A 211 ; The following residues NOT assigned to any domain: Chain "A" 107 - 111 Chain "A" 212 - 216 The following residues NOT assigned to any domain: Chain "A" 1 - 216 The following residues NOT assigned to any domain: Chain "A" 0 - 4
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCS B

PRELIMINARY 25-FEB-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1HILA]B 1 to B 106 ; DOMAIN 2: [Assigned by homology with 1HILA]B 112 to B 211 ; The following residues NOT assigned to any domain: Chain "B" 1 - 216 The following residues NOT assigned to any domain: Chain "B" 107 - 111 Chain "B" 212 - 216 The following residues NOT assigned to any domain: Chain "B" 0 - 4
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCW M

IMMUNOGLOBULIN 09-MAY-89 :: IMMUNOGLOBULIN HETEROLOGOUS LIGHT CHAIN DIMER

DOMAIN 1: [Assigned by homology with 1HILA]M 1 to M 106 ; DOMAIN 2: [Assigned by homology with 1HILA]M 112 to M 211 ; The following residues NOT assigned to any domain: Chain "M" 1 - 216 The following residues NOT assigned to any domain: Chain "M" 107 - 111 Chain "M" 212 - 216
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3MCG 1

IMMUNOGLOBULIN 09-MAY-89 :: IMMUNOGLOBULIN LAMBDA LIGHT CHAIN DIMER (/MCG$)

DOMAIN 1: [Assigned by homology with 1HILA]1 1 to 1 106 ; DOMAIN 2: [Assigned by homology with 1HILA]1 112 to 1 211 ; The following residues NOT assigned to any domain: Chain "1" 107 - 111 Chain "1" 212 - 216 The following residues NOT assigned to any domain: Chain "1" 1 - 216
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3MCG 2

IMMUNOGLOBULIN 09-MAY-89 :: IMMUNOGLOBULIN LAMBDA LIGHT CHAIN DIMER (/MCG$)

DOMAIN 1: [Assigned by homology with 1HILA]2 1 to 2 106 ; DOMAIN 2: [Assigned by homology with 1HILA]2 112 to 2 211 ; The following residues NOT assigned to any domain: Chain "2" 1 - 216 The following residues NOT assigned to any domain: Chain "2" 107 - 111 Chain "2" 212 - 216
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCO L

PRELIMINARY 25-FEB-93 :: IMMUNOGLOBIN LAMBDA LIGHT CHAIN DIMER (IGG1) WITH

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 106 ; DOMAIN 2: [Assigned by homology with 1HILA]L 112 to L 211 ; The following residues NOT assigned to any domain: Chain "L" 107 - 111 Chain "L" 212 - 216 The following residues NOT assigned to any domain: Chain "L" 1 - 428
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCW W

IMMUNOGLOBULIN 09-MAY-89 :: IMMUNOGLOBULIN HETEROLOGOUS LIGHT CHAIN DIMER

DOMAIN 1: [Assigned by homology with 1HILA]W 1 to W 106 ; DOMAIN 2: [Assigned by homology with 1HILA]W 112 to W 211 ; The following residues NOT assigned to any domain: Chain "W" 107 - 111 Chain "W" 212 - 216 The following residues NOT assigned to any domain: Chain "W" 1 - 216
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GIG L

IMMUNOGLOBULIN 20-JAN-93 :: IGG1 FAB FRAGMENT (HC19)

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 105 ; DOMAIN 2: [Assigned by homology with 1HILA]L 111 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 106 - 110 The following residues NOT assigned to any domain: Chain "L" 1 - 221
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IND L

IMMUNOGLOBULIN 14-JUN-93 :: CHA255 IMMUNOGLOBULIN FAB' FRAGMENT (IGG1-LAMBDA)

DOMAIN 1: [Assigned by homology with 1HILA]L 2 to L 105 ; DOMAIN 2: [Assigned by homology with 1HILA]L 111 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 106 - 110 Chain "L" 211 - 212 The following residues NOT assigned to any domain: Chain "L" 1 - 213
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1INE L

IMMUNOGLOBULIN 14-JUN-93 :: CHA255 IMMUNOGLOBULIN FAB' FRAGMENT (IGG1-LAMBDA)

DOMAIN 1: [Assigned by homology with 1HILA]L 2 to L 105 ; DOMAIN 2: [Assigned by homology with 1HILA]L 111 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 106 - 110 Chain "L" 211 - 212 The following residues NOT assigned to any domain: Chain "L" 1 - 213
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MFE L

IMMUNOGLOBULIN 25-OCT-93 :: FAB FRAGMENT (MURINE SE155-4) COMPLEX WITH DODECAS

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 105 ; DOMAIN 2: [Assigned by homology with 1HILA]L 111 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 106 - 110 Chain "L" 211 - 211 The following residues NOT assigned to any domain: Chain "L" 251 - 468
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MFB L

IMMUNOGLOBULIN 25-OCT-93 :: FAB FRAGMENT (MURINE SE155-4) COMPLEX WITH HEPTASA

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 105 ; DOMAIN 2: [Assigned by homology with 1HILA]L 111 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 106 - 110 Chain "L" 211 - 212 The following residues NOT assigned to any domain: Chain "L" 251 - 468
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MFC L

IMMUNOGLOBULIN 25-OCT-93 :: FAB FRAGMENT (MURINE SE155-4) COMPLEX WITH HEPTASA

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 105 ; DOMAIN 2: [Assigned by homology with 1HILA]L 111 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 106 - 110 Chain "L" 211 - 212 The following residues NOT assigned to any domain: Chain "L" 251 - 468
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MFD L

IMMUNOGLOBULIN 25-OCT-93 :: FAB FRAGMENT (MURINE SE155-4) COMPLEX WITH THE

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 105 ; DOMAIN 2: [Assigned by homology with 1HILA]L 111 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 106 - 110 Chain "L" 211 - 212 The following residues NOT assigned to any domain: Chain "L" 251 - 468
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2FBJ L

IMMUNOGLOBULIN 18-AUG-89 :: IG*A FAB FRAGMENT (J539) (GALACTAN-BINDING)

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 102 ; DOMAIN 2: [Assigned by homology with 1HILA]L 108 to L 209 ; The following residues NOT assigned to any domain: Chain "L" 103 - 107 Chain "L" 210 - 213 The following residues NOT assigned to any domain: Chain "L" 1 - 220
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BAF L

PRELIMINARY 16-JAN-92 :: AN02 FAB FRAGMENT

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 214 The following residues NOT assigned to any domain: Chain "L" 1 - 217
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FIG L

IMMUNOGLOBULIN 07-JAN-94 :: IMMUNOGLOBULIN G1 (KAPPA LIGHT CHAIN) FAB' FRAGMEN

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 214 The following residues NOT assigned to any domain: Chain "L" 1 - 223
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HIL C

PRELIMINARY 08-JUL-92 :: IGG2A FAB FRAGMENT (FAB 17/9)

DOMAIN 1: [Assigned by homology with 1HILA]C 1 to C 103 ; DOMAIN 2: [Assigned by homology with 1HILA]C 109 to C 210 ; The following residues NOT assigned to any domain: Chain "C" 1 - 211 The following residues NOT assigned to any domain: Chain "C" 1 - 228 The following residues NOT assigned to any domain: Chain "C" 104 - 108 Chain "C" 211 - 211 The following residues NOT assigned to any domain: Chain "C" 1 - 228
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HIM H

PRELIMINARY 08-JUL-92 :: IGG2A FAB FRAGMENT (FAB 17/9) COMPLEX WITH A SYNTH

DOMAIN 1: [Assigned by homology with 1HILA]H 1 to H 103 ; DOMAIN 2: [Assigned by homology with 1HILA]H 109 to H 210 ; The following residues NOT assigned to any domain: Chain " " 1 - 211 The following residues NOT assigned to any domain: Chain " " 1 - 228 The following residues NOT assigned to any domain: Chain " " 100 - 107 The following residues NOT assigned to any domain: Chain " " 1 - 211 The following residues NOT assigned to any domain: Chain " " 1 - 228 The following residues NOT assigned to any domain: Chain " " 100 - 108
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HIM J

PRELIMINARY 08-JUL-92 :: IGG2A FAB FRAGMENT (FAB 17/9) COMPLEX WITH A SYNTH

DOMAIN 1: [Assigned by homology with 1HILA]J 1 to J 103 ; DOMAIN 2: [Assigned by homology with 1HILA]J 109 to J 210 ; The following residues NOT assigned to any domain: Chain " " 1 - 211 The following residues NOT assigned to any domain: Chain " " 1 - 228 The following residues NOT assigned to any domain: Chain " " 100 - 107 The following residues NOT assigned to any domain: Chain " " 1 - 211 The following residues NOT assigned to any domain: Chain " " 1 - 228 The following residues NOT assigned to any domain: Chain " " 100 - 108
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HIN L

IMMUNOGLOBULIN 08-JUL-92 :: IGG2A FAB FRAGMENT (FAB 17/9) COMPLEXED WITH PEPTI

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 211 The following residues NOT assigned to any domain: Chain "L" 1 - 228 The following residues NOT assigned to any domain: Chain "L" 100 - 107
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IFH L

IMMUNOGLOBULIN 06-MAY-93 :: IGG2A FAB FRAGMENT (FAB 17/9) COMPLEX WITH PEPTIDE

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 212 The following residues NOT assigned to any domain: Chain "L" 1 - 228 The following residues NOT assigned to any domain: Chain "L" 100 - 107
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FRG L

IMMUNOGLOBULIN/VIRUS HEMAGGLUTININ 17-JAN-94 :: IGG2A FAB FRAGMENT (FAB 26/9) COMPLEXED WITH INFLU

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 109 ; DOMAIN 2: [Assigned by homology with 1HILA]L 115 to L 216 ; The following residues NOT assigned to any domain: Chain "L" 110 - 114 Chain "L" 217 - 217 The following residues NOT assigned to any domain: Chain "L" 218 - 437 The following residues NOT assigned to any domain: Chain "L" 1 - 9
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BBD L

PRELIMINARY 05-MAY-92 :: FAB FRAGMENT FROM 8F5 ANTIBODY AGAINST HRV2

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 109 ; DOMAIN 2: [Assigned by homology with 1HILA]L 115 to L 216 ; The following residues NOT assigned to any domain: Chain "L" 110 - 114 Chain "L" 217 - 219 The following residues NOT assigned to any domain: Chain "L" 1 - 218
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CBV L

IMMUNOGLOBULIN 16-MAR-93 :: FAB (BV04-01) AUTOANTIBODY BINDING SINGLE-STRANDED

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 108 ; DOMAIN 2: [Assigned by homology with 1HILA]L 114 to L 215 ; The following residues NOT assigned to any domain: Chain "L" 109 - 113 Chain "L" 216 - 219 The following residues NOT assigned to any domain: Chain "L" 1 - 219 The following residues NOT assigned to any domain: Chain "L" 1 - 3
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CGS L

IMMUNOGLOBULIN 06-OCT-93 :: IGG2B (KAPPA) FAB FRAGMENT AGAINST ANTIGEN

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 108 ; DOMAIN 2: [Assigned by homology with 1HILA]L 114 to L 215 ; The following residues NOT assigned to any domain: Chain "L" 109 - 113 Chain "L" 216 - 219 The following residues NOT assigned to any domain: Chain "L" 1 - 214
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NBV L

IMMUNOGLOBULIN 16-MAR-93 :: FAB (BV04-01) AUTOANTIBODY BINDING SINGLE-STRANDED

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 108 ; DOMAIN 2: [Assigned by homology with 1HILA]L 114 to L 215 ; The following residues NOT assigned to any domain: Chain "L" 109 - 113 Chain "L" 216 - 219 The following residues NOT assigned to any domain: Chain "L" 1 - 219
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CGR L

IMMUNOGLOBULIN 23-NOV-93 :: IGG2B (KAPPA) FAB FRAGMENT COMPLEXED WITH ANTIGEN

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 108 ; DOMAIN 2: [Assigned by homology with 1HILA]L 114 to L 215 ; The following residues NOT assigned to any domain: Chain "L" 109 - 113 Chain "L" 216 - 219 The following residues NOT assigned to any domain: Chain "L" 1 - 214
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FOR L

IMMUNOGLOBULIN 24-MAY-94 :: IGG2A FAB FRAGMENT (FAB17-IA) (ORTHORHOMBIC CRYSTA

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 102 ; DOMAIN 2: [Assigned by homology with 1HILA]L 108 to L 209 ; The following residues NOT assigned to any domain: Chain "L" 103 - 107 Chain "L" 210 - 210 The following residues NOT assigned to any domain: Chain "L" 1 - 219
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2IFF L

IMMUNOGLOBULIN/HYDROLASE(O-GLYCOSYL) 03-FEB-94 :: IGG1 FAB FRAGMENT (HYHEL-5) COMPLEXED WITH LYSOZYM

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 101 ; DOMAIN 2: [Assigned by homology with 1HILA]L 107 to L 208 ; The following residues NOT assigned to any domain: Chain "L" 102 - 106 Chain "L" 209 - 212 The following residues NOT assigned to any domain: Chain "L" 2 - 215 The following residues NOT assigned to any domain: Chain "L" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HFL L

COMPLEX(ANTIBODY-ANTIGEN) 17-AUG-87 :: IG*G1 FAB FRAGMENT (HY/HEL$-5) AND LYSOZYME (E.C.3

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 101 ; DOMAIN 2: [Assigned by homology with 1HILA]L 107 to L 208 ; The following residues NOT assigned to any domain: Chain "L" 102 - 106 Chain "L" 209 - 212 The following residues NOT assigned to any domain: Chain "L" 1 - 213 The following residues NOT assigned to any domain: Chain "L" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FAI L

IMMUNOGLOBULIN 27-MAY-92 :: FAB FRAGMENT FROM A MONOCLONAL ANTI-ARSONATE ANTIB

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 214 The following residues NOT assigned to any domain: Chain "L" 1 - 221
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NCA L

PRELIMINARY 21-JAN-92 :: N9 NEURAMINIDASE-/NC$41 FAB COMPLEX (E.C.3.2.1.18)

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 81 - 468 The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 214 The following residues NOT assigned to any domain: Chain "L" 1 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NCB L

PRELIMINARY 21-JAN-92 :: N9 NEURAMINIDASE MUTANT WITH ASN 329 REPLACED BY A

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 81 - 468 The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 214 The following residues NOT assigned to any domain: Chain "L" 1 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NCC L

PRELIMINARY 21-JAN-92 :: N9 NEURAMINIDASE MUTANT WITH ILE 368 REPLACED BY A

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 81 - 468 The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 214 The following residues NOT assigned to any domain: Chain "L" 1 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NCD L

PRELIMINARY 21-JAN-92 :: N9 NEURAMINIDASE-/NC$41 FAB COMPLEX (E.C.3.2.1.18)

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 81 - 468 The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 214 The following residues NOT assigned to any domain: Chain "L" 1 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FDL L

COMPLEX (ANTIBODY-ANTIGEN) 27-AUG-90 :: IG*G1 FAB FRAGMENT (ANTI-LYSOZYME ANTIBODY D1.3, K

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 214 The following residues NOT assigned to any domain: Chain "L" 1 - 218 The following residues NOT assigned to any domain: Chain "L" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6FAB L

IMMUNOGLOBULIN 17-JAN-91 :: ANTIGEN-BINDING FRAGMENT OF THE MURINE ANTI-PHENYL

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 214 The following residues NOT assigned to any domain: Chain "L" 1 - 222
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2F19 L

IMMUNOGLOBULIN 27-MAY-92 :: FAB FRAGMENT FROM A MONOCLONAL ANTI-ARSONATE ANTIB

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 214 The following residues NOT assigned to any domain: Chain "L" 1 - 221
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ACY L

COMPLEX(ANTIBODY/HIV-1 FRAGMENT) 10-FEB-94 :: IGG1 FAB FRAGMENT (59.1) COMPLEXED WITH HIV-1 GP12

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 211 The following residues NOT assigned to any domain: Chain "L" 1 - 226 The following residues NOT assigned to any domain: Chain "L" 315 - 326
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GGB L

IMMUNOGLOBULIN 19-JUL-93 :: IGG2A FAB FRAGMENT (50.1)

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 211 The following residues NOT assigned to any domain: Chain "L" 1 - 228
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GGC L

IMMUNOGLOBULIN 19-JUL-93 :: IGG2A FAB FRAGMENT (50.1)

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 211 The following residues NOT assigned to any domain: Chain "L" 1 - 228
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GGI L

IMMUNOGLOBULIN 02-APR-93 :: IGG2A FAB FRAGMENT (50.1) COMPLEX WITH 16-RESIDUE

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 211 The following residues NOT assigned to any domain: Chain "L" 1 - 228 The following residues NOT assigned to any domain: Chain "L" 311 - 321 The following residues NOT assigned to any domain: Chain "L" 1 - 211 The following residues NOT assigned to any domain: Chain "L" 1 - 228 The following residues NOT assigned to any domain: Chain "L" 311 - 321
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GGI M

IMMUNOGLOBULIN 02-APR-93 :: IGG2A FAB FRAGMENT (50.1) COMPLEX WITH 16-RESIDUE

DOMAIN 1: [Assigned by homology with 1HILA]M 1 to M 103 ; DOMAIN 2: [Assigned by homology with 1HILA]M 109 to M 210 ; The following residues NOT assigned to any domain: Chain "M" 1 - 211 The following residues NOT assigned to any domain: Chain "M" 1 - 228 The following residues NOT assigned to any domain: Chain "M" 311 - 321 The following residues NOT assigned to any domain: Chain "M" 104 - 108 Chain "M" 211 - 211 The following residues NOT assigned to any domain: Chain "M" 1 - 228 The following residues NOT assigned to any domain: Chain "M" 311 - 321
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IGJ A

IMMUNOGLOBULIN 19-FEB-93 :: FAB (IGG2A,KAPPA) FRAGMENT (26-10) COMPLEX WITH DI

DOMAIN 1: [Assigned by homology with 1HILA]A 1 to A 103 ; DOMAIN 2: [Assigned by homology with 1HILA]A 109 to A 210 ; The following residues NOT assigned to any domain: Chain "A" 104 - 108 Chain "A" 211 - 211 The following residues NOT assigned to any domain: Chain "A" 2 - 227 The following residues NOT assigned to any domain: Chain "A" 1 - 211 The following residues NOT assigned to any domain: Chain "A" 2 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IGJ C

IMMUNOGLOBULIN 19-FEB-93 :: FAB (IGG2A,KAPPA) FRAGMENT (26-10) COMPLEX WITH DI

DOMAIN 1: [Assigned by homology with 1HILA]C 1 to C 103 ; DOMAIN 2: [Assigned by homology with 1HILA]C 109 to C 210 ; The following residues NOT assigned to any domain: Chain "C" 1 - 211 The following residues NOT assigned to any domain: Chain "C" 2 - 227 The following residues NOT assigned to any domain: Chain "C" 104 - 108 Chain "C" 211 - 211 The following residues NOT assigned to any domain: Chain "C" 2 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TET L

IMMUNOGLOBULIN 21-JUN-93 :: IGG1 MONOCLONAL FAB FRAGMENT (TE33) COMPLEX WITH C

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 211 The following residues NOT assigned to any domain: Chain "L" 1 - 213 The following residues NOT assigned to any domain: Chain "L" 3 - 14
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IGI L

IMMUNOGLOBULIN 19-FEB-93 :: FAB (IGG2A,KAPPA) FRAGMENT (26-10)

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 213 The following residues NOT assigned to any domain: Chain "L" 2 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2IGF L

IMMUNOGLOBULIN 21-MAR-91 :: IGG1 FAB' FRAGMENT (B13I2) COMPLEX WITH PEPTIDE

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 214 The following residues NOT assigned to any domain: Chain "L" 1 - 233 The following residues NOT assigned to any domain: Chain "L" 69 - 75
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4FAB L

IMMUNOGLOBULIN 10-APR-89 :: 4-4-20 (IG*G2A=KAPPA=) FAB FRAGMENT - FLUORESCEIN

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 108 ; DOMAIN 2: [Assigned by homology with 1HILA]L 114 to L 215 ; The following residues NOT assigned to any domain: Chain "L" 109 - 113 Chain "L" 216 - 219 The following residues NOT assigned to any domain: Chain "L" 1 - 216
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IGF L

IMMUNOGLOBULIN 21-MAR-91 :: IGG1 FAB' FRAGMENT (B13I2)

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 214 The following residues NOT assigned to any domain: Chain "L" 1 - 227 The following residues NOT assigned to any domain: Chain "L" 1 - 214 The following residues NOT assigned to any domain: Chain "L" 1 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IGF M

IMMUNOGLOBULIN 21-MAR-91 :: IGG1 FAB' FRAGMENT (B13I2)

DOMAIN 1: [Assigned by homology with 1HILA]M 1 to M 103 ; DOMAIN 2: [Assigned by homology with 1HILA]M 109 to M 210 ; The following residues NOT assigned to any domain: Chain "M" 1 - 214 The following residues NOT assigned to any domain: Chain "M" 1 - 227 The following residues NOT assigned to any domain: Chain "M" 104 - 108 Chain "M" 211 - 214 The following residues NOT assigned to any domain: Chain "M" 1 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MCP L

IMMUNOGLOBULIN 15-OCT-84 :: IMMUNOGLOBULIN MC/PC603$ FAB-PHOSPHOCHOLINE COMPLE

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 109 ; DOMAIN 2: [Assigned by homology with 1HILA]L 115 to L 216 ; The following residues NOT assigned to any domain: Chain "L" 110 - 114 Chain "L" 217 - 220 The following residues NOT assigned to any domain: Chain "L" 1 - 222
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MCP L

IMMUNOGLOBULIN 09-JUL-84 :: IMMUNOGLOBULIN FAB FRAGMENT (MC/PC$603)

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 109 ; DOMAIN 2: [Assigned by homology with 1HILA]L 115 to L 216 ; The following residues NOT assigned to any domain: Chain "L" 110 - 114 Chain "L" 217 - 220 The following residues NOT assigned to any domain: Chain "L" 1 - 222
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2GFB A

IMMUNOGLOBULIN 07-JUL-94 :: IGG2A FAB FRAGMENT (CNJ206)

DOMAIN 1: [Assigned by homology with 1HILA]A 1 to A 103 ; DOMAIN 2: [Assigned by homology with 1HILA]A 109 to A 210 ; The following residues NOT assigned to any domain: Chain "A" 104 - 108 Chain "A" 211 - 214 The following residues NOT assigned to any domain: Chain "A" 1 - 227 The following residues NOT assigned to any domain: Chain "A" 1 - 214 The following residues NOT assigned to any domain: Chain "A" 1 - 227 The following residues NOT assigned to any domain: Chain "A" 1 - 214 The following residues NOT assigned to any domain: Chain "A" 1 - 227 The following residues NOT assigned to any domain: Chain "A" 1 - 214 The following residues NOT assigned to any domain: Chain "A" 1 - 227 The following residues NOT assigned to any domain: Chain "A" 1 - 214 The following residues NOT assigned to any domain: Chain "A" 1 - 227 The following residues NOT assigned to any domain: Chain "A" 1 - 214 The following residues NOT assigned to any domain: Chain "A" 1 - 227 The following residues NOT assigned to any domain: Chain "A" 1 - 214 The following residues NOT assigned to any domain: Chain "A" 1 - 227 The following residues NOT assigned to any domain: Chain "A" 1 - 214 The following residues NOT assigned to any domain: Chain "A" 1 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2GFB C

IMMUNOGLOBULIN 07-JUL-94 :: IGG2A FAB FRAGMENT (CNJ206)

DOMAIN 1: [Assigned by homology with 1HILA]C 1 to C 103 ; DOMAIN 2: [Assigned by homology with 1HILA]C 109 to C 210 ; The following residues NOT assigned to any domain: Chain "C" 1 - 214 The following residues NOT assigned to any domain: Chain "C" 1 - 227 The following residues NOT assigned to any domain: Chain "C" 104 - 108 Chain "C" 211 - 214 The following residues NOT assigned to any domain: Chain "C" 1 - 227 The following residues NOT assigned to any domain: Chain "C" 1 - 214 The following residues NOT assigned to any domain: Chain "C" 1 - 227 The following residues NOT assigned to any domain: Chain "C" 1 - 214 The following residues NOT assigned to any domain: Chain "C" 1 - 227 The following residues NOT assigned to any domain: Chain "C" 1 - 214 The following residues NOT assigned to any domain: Chain "C" 1 - 227 The following residues NOT assigned to any domain: Chain "C" 1 - 214 The following residues NOT assigned to any domain: Chain "C" 1 - 227 The following residues NOT assigned to any domain: Chain "C" 1 - 214 The following residues NOT assigned to any domain: Chain "C" 1 - 227 The following residues NOT assigned to any domain: Chain "C" 1 - 214 The following residues NOT assigned to any domain: Chain "C" 1 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2GFB E

IMMUNOGLOBULIN 07-JUL-94 :: IGG2A FAB FRAGMENT (CNJ206)

DOMAIN 1: [Assigned by homology with 1HILA]E 1 to E 103 ; DOMAIN 2: [Assigned by homology with 1HILA]E 109 to E 210 ; The following residues NOT assigned to any domain: Chain "E" 1 - 214 The following residues NOT assigned to any domain: Chain "E" 1 - 227 The following residues NOT assigned to any domain: Chain "E" 1 - 214 The following residues NOT assigned to any domain: Chain "E" 1 - 227 The following residues NOT assigned to any domain: Chain "E" 104 - 108 Chain "E" 211 - 214 The following residues NOT assigned to any domain: Chain "E" 1 - 227 The following residues NOT assigned to any domain: Chain "E" 1 - 214 The following residues NOT assigned to any domain: Chain "E" 1 - 227 The following residues NOT assigned to any domain: Chain "E" 1 - 214 The following residues NOT assigned to any domain: Chain "E" 1 - 227 The following residues NOT assigned to any domain: Chain "E" 1 - 214 The following residues NOT assigned to any domain: Chain "E" 1 - 227 The following residues NOT assigned to any domain: Chain "E" 1 - 214 The following residues NOT assigned to any domain: Chain "E" 1 - 227 The following residues NOT assigned to any domain: Chain "E" 1 - 214 The following residues NOT assigned to any domain: Chain "E" 1 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2GFB G

IMMUNOGLOBULIN 07-JUL-94 :: IGG2A FAB FRAGMENT (CNJ206)

DOMAIN 1: [Assigned by homology with 1HILA]G 1 to G 103 ; DOMAIN 2: [Assigned by homology with 1HILA]G 109 to G 210 ; The following residues NOT assigned to any domain: Chain "G" 1 - 214 The following residues NOT assigned to any domain: Chain "G" 1 - 227 The following residues NOT assigned to any domain: Chain "G" 1 - 214 The following residues NOT assigned to any domain: Chain "G" 1 - 227 The following residues NOT assigned to any domain: Chain "G" 1 - 214 The following residues NOT assigned to any domain: Chain "G" 1 - 227 The following residues NOT assigned to any domain: Chain "G" 104 - 108 Chain "G" 211 - 214 The following residues NOT assigned to any domain: Chain "G" 1 - 227 The following residues NOT assigned to any domain: Chain "G" 1 - 214 The following residues NOT assigned to any domain: Chain "G" 1 - 227 The following residues NOT assigned to any domain: Chain "G" 1 - 214 The following residues NOT assigned to any domain: Chain "G" 1 - 227 The following residues NOT assigned to any domain: Chain "G" 1 - 214 The following residues NOT assigned to any domain: Chain "G" 1 - 227 The following residues NOT assigned to any domain: Chain "G" 1 - 214 The following residues NOT assigned to any domain: Chain "G" 1 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2GFB I

IMMUNOGLOBULIN 07-JUL-94 :: IGG2A FAB FRAGMENT (CNJ206)

DOMAIN 1: [Assigned by homology with 1HILA]I 1 to I 103 ; DOMAIN 2: [Assigned by homology with 1HILA]I 109 to I 210 ; The following residues NOT assigned to any domain: Chain "I" 1 - 214 The following residues NOT assigned to any domain: Chain "I" 1 - 227 The following residues NOT assigned to any domain: Chain "I" 1 - 214 The following residues NOT assigned to any domain: Chain "I" 1 - 227 The following residues NOT assigned to any domain: Chain "I" 1 - 214 The following residues NOT assigned to any domain: Chain "I" 1 - 227 The following residues NOT assigned to any domain: Chain "I" 1 - 214 The following residues NOT assigned to any domain: Chain "I" 1 - 227 The following residues NOT assigned to any domain: Chain "I" 104 - 108 Chain "I" 211 - 214 The following residues NOT assigned to any domain: Chain "I" 1 - 227 The following residues NOT assigned to any domain: Chain "I" 1 - 214 The following residues NOT assigned to any domain: Chain "I" 1 - 227 The following residues NOT assigned to any domain: Chain "I" 1 - 214 The following residues NOT assigned to any domain: Chain "I" 1 - 227 The following residues NOT assigned to any domain: Chain "I" 1 - 214 The following residues NOT assigned to any domain: Chain "I" 1 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2GFB K

IMMUNOGLOBULIN 07-JUL-94 :: IGG2A FAB FRAGMENT (CNJ206)

DOMAIN 1: [Assigned by homology with 1HILA]K 1 to K 103 ; DOMAIN 2: [Assigned by homology with 1HILA]K 109 to K 210 ; The following residues NOT assigned to any domain: Chain "K" 1 - 214 The following residues NOT assigned to any domain: Chain "K" 1 - 227 The following residues NOT assigned to any domain: Chain "K" 1 - 214 The following residues NOT assigned to any domain: Chain "K" 1 - 227 The following residues NOT assigned to any domain: Chain "K" 1 - 214 The following residues NOT assigned to any domain: Chain "K" 1 - 227 The following residues NOT assigned to any domain: Chain "K" 1 - 214 The following residues NOT assigned to any domain: Chain "K" 1 - 227 The following residues NOT assigned to any domain: Chain "K" 1 - 214 The following residues NOT assigned to any domain: Chain "K" 1 - 227 The following residues NOT assigned to any domain: Chain "K" 104 - 108 Chain "K" 211 - 214 The following residues NOT assigned to any domain: Chain "K" 1 - 227 The following residues NOT assigned to any domain: Chain "K" 1 - 214 The following residues NOT assigned to any domain: Chain "K" 1 - 227 The following residues NOT assigned to any domain: Chain "K" 1 - 214 The following residues NOT assigned to any domain: Chain "K" 1 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2GFB M

IMMUNOGLOBULIN 07-JUL-94 :: IGG2A FAB FRAGMENT (CNJ206)

DOMAIN 1: [Assigned by homology with 1HILA]M 1 to M 103 ; DOMAIN 2: [Assigned by homology with 1HILA]M 109 to M 210 ; The following residues NOT assigned to any domain: Chain "M" 1 - 214 The following residues NOT assigned to any domain: Chain "M" 1 - 227 The following residues NOT assigned to any domain: Chain "M" 1 - 214 The following residues NOT assigned to any domain: Chain "M" 1 - 227 The following residues NOT assigned to any domain: Chain "M" 1 - 214 The following residues NOT assigned to any domain: Chain "M" 1 - 227 The following residues NOT assigned to any domain: Chain "M" 1 - 214 The following residues NOT assigned to any domain: Chain "M" 1 - 227 The following residues NOT assigned to any domain: Chain "M" 1 - 214 The following residues NOT assigned to any domain: Chain "M" 1 - 227 The following residues NOT assigned to any domain: Chain "M" 1 - 214 The following residues NOT assigned to any domain: Chain "M" 1 - 227 The following residues NOT assigned to any domain: Chain "M" 104 - 108 Chain "M" 211 - 214 The following residues NOT assigned to any domain: Chain "M" 1 - 227 The following residues NOT assigned to any domain: Chain "M" 1 - 214 The following residues NOT assigned to any domain: Chain "M" 1 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2GFB O

IMMUNOGLOBULIN 07-JUL-94 :: IGG2A FAB FRAGMENT (CNJ206)

DOMAIN 1: [Assigned by homology with 1HILA]O 1 to O 103 ; DOMAIN 2: [Assigned by homology with 1HILA]O 109 to O 210 ; The following residues NOT assigned to any domain: Chain "O" 1 - 214 The following residues NOT assigned to any domain: Chain "O" 1 - 227 The following residues NOT assigned to any domain: Chain "O" 1 - 214 The following residues NOT assigned to any domain: Chain "O" 1 - 227 The following residues NOT assigned to any domain: Chain "O" 1 - 214 The following residues NOT assigned to any domain: Chain "O" 1 - 227 The following residues NOT assigned to any domain: Chain "O" 1 - 214 The following residues NOT assigned to any domain: Chain "O" 1 - 227 The following residues NOT assigned to any domain: Chain "O" 1 - 214 The following residues NOT assigned to any domain: Chain "O" 1 - 227 The following residues NOT assigned to any domain: Chain "O" 1 - 214 The following residues NOT assigned to any domain: Chain "O" 1 - 227 The following residues NOT assigned to any domain: Chain "O" 1 - 214 The following residues NOT assigned to any domain: Chain "O" 1 - 227 The following residues NOT assigned to any domain: Chain "O" 104 - 108 Chain "O" 211 - 214 The following residues NOT assigned to any domain: Chain "O" 1 - 227
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DBA L

IMMUNOGLOBULIN 10-NOV-92 :: FAB' FRAGMENT OF THE DB3 ANTI-STEROID MONOCLONAL A

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 211 The following residues NOT assigned to any domain: Chain "L" 1 - 228
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DBB L

IMMUNOGLOBULIN 11-NOV-92 :: FAB' FRAGMENT OF THE DB3 ANTI-STEROID MONOCLONAL A

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 211 The following residues NOT assigned to any domain: Chain "L" 1 - 228
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DBJ L

IMMUNOGLOBULIN 24-AUG-93 :: FAB' FRAGMENT OF MONOCLONAL ANTIBODY DB3

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 211 The following residues NOT assigned to any domain: Chain "L" 1 - 228
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DBK L

IMMUNOGLOBULIN 24-AUG-93 :: FAB' FRAGMENT OF MONOCLONAL ANTIBODY DB3

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 211 The following residues NOT assigned to any domain: Chain "L" 1 - 228
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DBM L

IMMUNOGLOBULIN 24-AUG-93 :: FAB' FRAGMENT OF MONOCLONAL ANTIBODY DB3

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 211 The following residues NOT assigned to any domain: Chain "L" 1 - 228
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2DBL L

IMMUNOGLOBULIN 08-FEB-94 :: FAB' FRAGMENT OF MONOCLONAL ANTIBODY DB3

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 211 The following residues NOT assigned to any domain: Chain "L" 1 - 228
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MAM L

IMMUNOGLOBULIN 14-JAN-92 :: ANTIGEN-BINDING FRAGMENT (FAB) (IGG2B, KAPPA)

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 214 The following residues NOT assigned to any domain: Chain "L" 1 - 217
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1JEL L

IMMUNOGLOBULIN 02-APR-93 :: FAB JE142 MONOCLONAL ANTIBODY COMPLEXED WITH HISTI

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 212 The following residues NOT assigned to any domain: Chain "L" 1 - 210 The following residues NOT assigned to any domain: Chain "L" 1 - 85
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EAP A

CATALYTIC ANTIBODY 10-AUG-94 :: 17E8 COMPLEXED WITH PHENYL [1-(1-N-SUCCINYLAMINO)P

DOMAIN 1: [Assigned by homology with 1HILA]A 1 to A 103 ; DOMAIN 2: [Assigned by homology with 1HILA]A 109 to A 210 ; The following residues NOT assigned to any domain: Chain "A" 104 - 108 Chain "A" 211 - 214 The following residues NOT assigned to any domain: Chain "A" 1 - 221
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BBJ L

PRELIMINARY 30-APR-92 :: B72.3, FAB' FRAGMENT OF CHIMAERIC MONOCLONAL ANTIB

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 211 The following residues NOT assigned to any domain: Chain "L" 1 - 212
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DFB L

IMMUNOGLOBULIN 27-MAR-92 :: 3D6 FAB

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 101 ; DOMAIN 2: [Assigned by homology with 1HILA]L 107 to L 208 ; The following residues NOT assigned to any domain: Chain "L" 102 - 106 Chain "L" 209 - 212 The following residues NOT assigned to any domain: Chain "L" 1 - 229
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FVD A

IMMUNOGLOBULIN 20-OCT-92 :: FAB FRAGMENT OF HUMANIZED ANTIBODY 4D5, VERSION 4

DOMAIN 1: [Assigned by homology with 1HILA]A 1 to A 103 ; DOMAIN 2: [Assigned by homology with 1HILA]A 109 to A 210 ; The following residues NOT assigned to any domain: Chain "A" 104 - 108 Chain "A" 211 - 214 The following residues NOT assigned to any domain: Chain "A" 1 - 223 The following residues NOT assigned to any domain: Chain "A" 1 - 214 The following residues NOT assigned to any domain: Chain "A" 1 - 223
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FVD C

IMMUNOGLOBULIN 20-OCT-92 :: FAB FRAGMENT OF HUMANIZED ANTIBODY 4D5, VERSION 4

DOMAIN 1: [Assigned by homology with 1HILA]C 1 to C 103 ; DOMAIN 2: [Assigned by homology with 1HILA]C 109 to C 210 ; The following residues NOT assigned to any domain: Chain "C" 1 - 214 The following residues NOT assigned to any domain: Chain "C" 1 - 223 The following residues NOT assigned to any domain: Chain "C" 104 - 108 Chain "C" 211 - 214 The following residues NOT assigned to any domain: Chain "C" 1 - 223
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FVE A

IMMUNOGLOBULIN 20-OCT-92 :: FAB FRAGMENT OF HUMANIZED ANTIBODY 4D5, VERSION 7

DOMAIN 1: [Assigned by homology with 1HILA]A 1 to A 103 ; DOMAIN 2: [Assigned by homology with 1HILA]A 109 to A 210 ; The following residues NOT assigned to any domain: Chain "A" 104 - 108 Chain "A" 211 - 214 The following residues NOT assigned to any domain: Chain "A" 1 - 223 The following residues NOT assigned to any domain: Chain "A" 1 - 214 The following residues NOT assigned to any domain: Chain "A" 1 - 223
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FVE C

IMMUNOGLOBULIN 20-OCT-92 :: FAB FRAGMENT OF HUMANIZED ANTIBODY 4D5, VERSION 7

DOMAIN 1: [Assigned by homology with 1HILA]C 1 to C 103 ; DOMAIN 2: [Assigned by homology with 1HILA]C 109 to C 210 ; The following residues NOT assigned to any domain: Chain "C" 1 - 214 The following residues NOT assigned to any domain: Chain "C" 1 - 223 The following residues NOT assigned to any domain: Chain "C" 104 - 108 Chain "C" 211 - 214 The following residues NOT assigned to any domain: Chain "C" 1 - 223
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2FGW L

IMMUNOGLOBULIN 16-JAN-94 :: FAB FRAGMENT OF A HUMANIZED VERSION OF THE ANTI-CD

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 214 The following residues NOT assigned to any domain: Chain "L" 1 - 228
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3HFM L

COMPLEX(ANTIBODY-ANTIGEN) 11-AUG-88 :: IG*G1 FAB FRAGMENT (HY/HEL$-10) AND LYSOZYME (E.C.

DOMAIN 1: [Assigned by homology with 1HILA]L 1 to L 103 ; DOMAIN 2: [Assigned by homology with 1HILA]L 109 to L 210 ; The following residues NOT assigned to any domain: Chain "L" 104 - 108 Chain "L" 211 - 214 The following residues NOT assigned to any domain: Chain "L" 1 - 215 The following residues NOT assigned to any domain: Chain "L" 1 - 129
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2IGE A

IMMUNOGLOBULIN 02-OCT-90 :: FC FRAGMENT (IGE'CL) (THEORETICAL MODEL)

DOMAIN 1: [Assigned by homology with 1HILA]A 229 to A 396 ; DOMAIN 2: [Assigned by homology with 1HILA]A 438 to A 542 ; The following residues NOT assigned to any domain: Chain "A" 397 - 437 Chain "A" 543 - 547 The following residues NOT assigned to any domain: Chain "A" 229 - 547
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2IGE B

IMMUNOGLOBULIN 02-OCT-90 :: FC FRAGMENT (IGE'CL) (THEORETICAL MODEL)

DOMAIN 1: [Assigned by homology with 1HILA]B 229 to B 396 ; DOMAIN 2: [Assigned by homology with 1HILA]B 438 to B 542 ; The following residues NOT assigned to any domain: Chain "B" 229 - 547 The following residues NOT assigned to any domain: Chain "B" 397 - 437 Chain "B" 543 - 547
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IGE A

IMMUNOGLOBULIN 14-JAN-85 :: FC FRAGMENT (IGE'CL) (THEORETICAL MODEL)

DOMAIN 1: [Assigned by homology with 1HILA]A 1 to A 171 ; DOMAIN 2: [Assigned by homology with 1HILA]A 213 to A 317 ; The following residues NOT assigned to any domain: Chain "A" 172 - 212 Chain "A" 318 - 322 The following residues NOT assigned to any domain: Chain "A" 1 - 322
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IGE B

IMMUNOGLOBULIN 14-JAN-85 :: FC FRAGMENT (IGE'CL) (THEORETICAL MODEL)

DOMAIN 1: [Assigned by homology with 1HILA]B 1 to B 171 ; DOMAIN 2: [Assigned by homology with 1HILA]B 213 to B 317 ; The following residues NOT assigned to any domain: Chain "B" 1 - 322 The following residues NOT assigned to any domain: Chain "B" 172 - 212 Chain "B" 318 - 322
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FC1 A

IMMUNOGLOBULIN 21-MAY-81 :: FC FRAGMENT (IGG1 CLASS)

DOMAIN 1: [Assigned by homology with 1HILA]A 238 to A 335 ; DOMAIN 2: [Assigned by homology with 1HILA]A 341 to A 441 ; The following residues NOT assigned to any domain: Chain "A" 336 - 340 Chain "A" 442 - 444 The following residues NOT assigned to any domain: Chain "A" 238 - 444
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FC1 B

IMMUNOGLOBULIN 21-MAY-81 :: FC FRAGMENT (IGG1 CLASS)

DOMAIN 1: [Assigned by homology with 1HILA]B 238 to B 335 ; DOMAIN 2: [Assigned by homology with 1HILA]B 341 to B 441 ; The following residues NOT assigned to any domain: Chain "B" 238 - 444 The following residues NOT assigned to any domain: Chain "B" 336 - 340 Chain "B" 442 - 444
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FC2 D

IMMUNOGLOBULIN 21-MAY-81 :: IMMUNOGLOBULIN FC AND FRAGMENT B OF PROTEIN A COMP

DOMAIN 1: [Assigned by homology with 1HILA]D 238 to D 335 ; DOMAIN 2: [Assigned by homology with 1HILA]D 341 to D 441 ; The following residues NOT assigned to any domain: Chain "D" 124 - 167 The following residues NOT assigned to any domain: Chain "D" 336 - 340 Chain "D" 442 - 444
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PFC

IMMUNOGLOBULIN 28-OCT-81 :: $P/F$C(PRIME) FRAGMENT OF AN IG*G1

DOMAIN 1: [Assigned by homology with 1HILA] 334 to 409 ; DOMAIN 2: [Assigned by homology with 1HILA] 415 to 441 ; The following residues NOT assigned to any domain: Chain " " 410 - 414 Chain " " 442 - 446
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MBP

PRELIMINARY 14-SEP-92 :: D-MALTODEXTRIN-BINDING PROTEIN COMPLEXED WITH D-MA

DOMAIN 1: 1 to 109 ; 261 to 313 ; DOMAIN 2: 114 to 258 ; 316 to 370 ; The following residues NOT assigned to any domain: Chain " " 110 - 113 Chain " " 259 - 260 Chain " " 314 - 315
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DMB

SUGAR TRANSPORT 10-JUN-93 :: D-MALTODEXTRIN-BINDING PROTEIN

DOMAIN 1: 1 to 109 ; 261 to 313 ; DOMAIN 2: 114 to 258 ; 316 to 370 ; The following residues NOT assigned to any domain: Chain " " 110 - 113 Chain " " 259 - 260 Chain " " 314 - 315
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MDQ

SUGAR TRANSPORT 10-AUG-94 :: MALTODEXTRIN-BINDING PROTEIN (MALE322)

DOMAIN 1: 1 to 109 ; 261 to 314 ; DOMAIN 2: 114 to 258 ; 317 to 371 ; The following residues NOT assigned to any domain: Chain " " 110 - 113 Chain " " 259 - 260 Chain " " 315 - 316
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MDP 1

SUGAR TRANSPORT 10-AUG-94 :: MALTODEXTRIN-BINDING PROTEIN (MALE178 MUTANT)

DOMAIN 1: 1 1 to 1 109 ; 1 261 to 1 313 ; DOMAIN 2: 1 114 to 1 258 ; 1 316 to 1 370 ; The following residues NOT assigned to any domain: Chain "1" 110 - 113 Chain "1" 259 - 260 Chain "1" 314 - 315 The following residues NOT assigned to any domain: Chain "1" 1 - 370
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MDP 2

SUGAR TRANSPORT 10-AUG-94 :: MALTODEXTRIN-BINDING PROTEIN (MALE178 MUTANT)

DOMAIN 1: 2 1 to 2 109 ; 2 261 to 2 313 ; DOMAIN 2: 2 114 to 2 258 ; 2 316 to 2 370 ; The following residues NOT assigned to any domain: Chain "2" 1 - 370 The following residues NOT assigned to any domain: Chain "2" 110 - 113 Chain "2" 259 - 260 Chain "2" 314 - 315
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CTR

CALCIUM-BINDING PROTEIN 21-SEP-94 :: CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:1 COM

DOMAIN 1: 1 to 67 ; DOMAIN 2: 92 to 147 ; The following residues NOT assigned to any domain: Chain " " 68 - 91
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CLM

CALCIUM-BINDING PROTEIN 23-JAN-93 :: CALMODULIN (PARAMECIUM TETRAURELIA) (WILD TYPE)

DOMAIN 1: 4 to 67 ; DOMAIN 2: 92 to 147 ; The following residues NOT assigned to any domain: Chain " " 68 - 91
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DEG

CALCIUM-BINDING PROTEIN 07-JUN-93 :: CALMODULIN MUTANT WITH GLU 84 DELETED (DEL E84)

DOMAIN 1: 5 to 67 ; DOMAIN 2: 92 to 147 ; The following residues NOT assigned to any domain: Chain " " 68 - 91
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CDL A

CALCIUM-BINDING PROTEIN 08-OCT-93 :: CALMODULIN COMPLEXED WITH CALMODULIN-BINDING PEPTI

DOMAIN 1: A 5 to A 67 ; DOMAIN 2: A 92 to A 146 ; The following residues NOT assigned to any domain: Chain "A" 68 - 91 The following residues NOT assigned to any domain: Chain "A" 797 - 815 The following residues NOT assigned to any domain: Chain "A" 5 - 146 The following residues NOT assigned to any domain: Chain "A" 797 - 815 The following residues NOT assigned to any domain: Chain "A" 5 - 146 The following residues NOT assigned to any domain: Chain "A" 796 - 815 The following residues NOT assigned to any domain: Chain "A" 5 - 146 The following residues NOT assigned to any domain: Chain "A" 798 - 815
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CDL B

CALCIUM-BINDING PROTEIN 08-OCT-93 :: CALMODULIN COMPLEXED WITH CALMODULIN-BINDING PEPTI

DOMAIN 1: B 5 to B 67 ; DOMAIN 2: B 92 to B 146 ; The following residues NOT assigned to any domain: Chain "B" 5 - 146 The following residues NOT assigned to any domain: Chain "B" 797 - 815 The following residues NOT assigned to any domain: Chain "B" 68 - 91 The following residues NOT assigned to any domain: Chain "B" 797 - 815 The following residues NOT assigned to any domain: Chain "B" 5 - 146 The following residues NOT assigned to any domain: Chain "B" 796 - 815 The following residues NOT assigned to any domain: Chain "B" 5 - 146 The following residues NOT assigned to any domain: Chain "B" 798 - 815
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CDL C

CALCIUM-BINDING PROTEIN 08-OCT-93 :: CALMODULIN COMPLEXED WITH CALMODULIN-BINDING PEPTI

DOMAIN 1: C 5 to C 67 ; DOMAIN 2: C 92 to C 146 ; The following residues NOT assigned to any domain: Chain "C" 5 - 146 The following residues NOT assigned to any domain: Chain "C" 797 - 815 The following residues NOT assigned to any domain: Chain "C" 5 - 146 The following residues NOT assigned to any domain: Chain "C" 797 - 815 The following residues NOT assigned to any domain: Chain "C" 68 - 91 The following residues NOT assigned to any domain: Chain "C" 796 - 815 The following residues NOT assigned to any domain: Chain "C" 5 - 146 The following residues NOT assigned to any domain: Chain "C" 798 - 815
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CDL D

CALCIUM-BINDING PROTEIN 08-OCT-93 :: CALMODULIN COMPLEXED WITH CALMODULIN-BINDING PEPTI

DOMAIN 1: D 5 to D 67 ; DOMAIN 2: D 92 to D 146 ; The following residues NOT assigned to any domain: Chain "D" 5 - 146 The following residues NOT assigned to any domain: Chain "D" 797 - 815 The following residues NOT assigned to any domain: Chain "D" 5 - 146 The following residues NOT assigned to any domain: Chain "D" 797 - 815 The following residues NOT assigned to any domain: Chain "D" 5 - 146 The following residues NOT assigned to any domain: Chain "D" 796 - 815 The following residues NOT assigned to any domain: Chain "D" 68 - 91 The following residues NOT assigned to any domain: Chain "D" 798 - 815
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3CLN

CALCIUM BINDING PROTEIN 11-MAY-88 :: CALMODULIN

DOMAIN 1: 5 to 67 ; DOMAIN 2: 92 to 147 ; The following residues NOT assigned to any domain: Chain " " 68 - 91
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CLL

CALCIUM-BINDING PROTEIN 29-SEP-92 :: CALMODULIN (VERTEBRATE)

DOMAIN 1: 4 to 67 ; DOMAIN 2: 92 to 147 ; The following residues NOT assigned to any domain: Chain " " 68 - 91
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CLN

CALCIUM BINDING PROTEIN 03-FEB-88 :: N==Z115== TRIMETHYLCALMODULIN COMPLEX WITH TRIFLUO

DOMAIN 1: 1 to 67 ; DOMAIN 2: 92 to 147 ; The following residues NOT assigned to any domain: Chain " " 68 - 91 Chain " " 148 - 148
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4CLN

CALCIUM BINDING PROTEIN 24-JUN-91 :: CALMODULIN

DOMAIN 1: 1 to 67 ; DOMAIN 2: 92 to 147 ; The following residues NOT assigned to any domain: Chain " " 68 - 91 Chain " " 148 - 148
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2BBM A

PRELIMINARY 16-JUL-92 :: CALCIUM-BOUND CALMODULIN COMPLEX WITH CALMODULIN B

DOMAIN 1: A 1 to A 67 ; DOMAIN 2: A 92 to A 147 ; The following residues NOT assigned to any domain: Chain "A" 68 - 91 Chain "A" 148 - 148 The following residues NOT assigned to any domain: Chain "A" 1 - 26
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2BBN A

CALCIUM-BINDING PROTEIN 16-JUL-92 :: CALMODULIN (CALCIUM-BOUND) COMPLEXED WITH RABBIT S

DOMAIN 1: A 1 to A 67 ; DOMAIN 2: A 92 to A 147 ; The following residues NOT assigned to any domain: Chain "A" 68 - 91 Chain "A" 148 - 148 The following residues NOT assigned to any domain: Chain "A" 1 - 26
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CDM A

CALCIUM-BINDING PROTEIN 08-OCT-93 :: CALMODULIN COMPLEXED WITH CALMODULIN-BINDING DOMAI

DOMAIN 1: A 4 to A 67 ; DOMAIN 2: A 92 to A 146 ; The following residues NOT assigned to any domain: Chain "A" 68 - 91 The following residues NOT assigned to any domain: Chain "A" 293 - 310
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4PFK

TRANSFERASE(PHOSPHOTRANSFERASE) 25-JAN-88 :: PHOSPHOFRUCTOKINASE (E.C.2.7.1.11) COMPLEX WITH

DOMAIN 1: [Assigned by homology with 1PFKA] 1 to 138 ; 251 to 301 ; DOMAIN 2: [Assigned by homology with 1PFKA] 139 to 250 ; 303 to 320 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5PFK

TRANSFERASE 25-JAN-88 :: PHOSPHOFRUCTOKINASE (E.C.2.7.1.11) (INHIBITED T-ST

DOMAIN 1: [Assigned by homology with 1PFKA] 1 to 138 ; 251 to 301 ; DOMAIN 2: [Assigned by homology with 1PFKA] 139 to 250 ; 303 to 320 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3PFK

TRANSFERASE(PHOSPHOTRANSFERASE) 25-JAN-88 :: PHOSPHOFRUCTOKINASE (E.C.2.7.1.11)

DOMAIN 1: [Assigned by homology with 1PFKA] 1 to 138 ; 251 to 301 ; DOMAIN 2: [Assigned by homology with 1PFKA] 139 to 250 ; 303 to 320 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PFK D

TRANSFERASE(PHOSPHOTRANSFERASE) 25-JAN-88 :: PHOSPHOFRUCTOKINASE (E.C.2.7.1.11)

DOMAIN 1: [Assigned by homology with 1PFKA]D 0 to D 138 ; D 251 to D 301 ; DOMAIN 2: [Assigned by homology with 1PFKA]D 139 to D 250 ; D 302 to D 304 ; The following residues NOT assigned to any domain: Chain "D" 0 - 300 The following residues NOT assigned to any domain: Chain "D" 0 - 300 The following residues NOT assigned to any domain: Chain "D" 0 - 301
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PFK B

TRANSFERASE(PHOSPHOTRANSFERASE) 25-JAN-88 :: PHOSPHOFRUCTOKINASE (E.C.2.7.1.11) (R-STATE) COMPL

DOMAIN 1: [Assigned by homology with 1PFKA]B 0 to B 138 ; B 251 to B 301 ; DOMAIN 2: [Assigned by homology with 1PFKA]B 139 to B 250 ; B 302 to B 319 ; The following residues NOT assigned to any domain: Chain "B" 0 - 319
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PFK A

TRANSFERASE(PHOSPHOTRANSFERASE) 25-JAN-88 :: PHOSPHOFRUCTOKINASE (E.C.2.7.1.11)

DOMAIN 1: [Assigned by homology with 1PFKA]A 0 to A 138 ; A 251 to A 300 ; DOMAIN 2: [Assigned by homology with 1PFKA]A 139 to A 250 ; A 300 to A 300 ; The following residues NOT assigned to any domain: Chain "A" 0 - 300 The following residues NOT assigned to any domain: Chain "A" 0 - 301 The following residues NOT assigned to any domain: Chain "A" 0 - 304
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PFK B

TRANSFERASE(PHOSPHOTRANSFERASE) 25-JAN-88 :: PHOSPHOFRUCTOKINASE (E.C.2.7.1.11)

DOMAIN 1: [Assigned by homology with 1PFKA]B 0 to B 138 ; B 251 to B 300 ; DOMAIN 2: [Assigned by homology with 1PFKA]B 139 to B 250 ; B 300 to B 300 ; The following residues NOT assigned to any domain: Chain "B" 0 - 300 The following residues NOT assigned to any domain: Chain "B" 0 - 301 The following residues NOT assigned to any domain: Chain "B" 0 - 304
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PFK C

TRANSFERASE(PHOSPHOTRANSFERASE) 25-JAN-88 :: PHOSPHOFRUCTOKINASE (E.C.2.7.1.11)

DOMAIN 1: [Assigned by homology with 1PFKA]C 0 to C 138 ; C 251 to C 300 ; DOMAIN 2: [Assigned by homology with 1PFKA]C 139 to C 250 ; C 300 to C 300 ; The following residues NOT assigned to any domain: Chain "C" 0 - 300 The following residues NOT assigned to any domain: Chain "C" 0 - 300 The following residues NOT assigned to any domain: Chain "C" 301 - 301 The following residues NOT assigned to any domain: Chain "C" 0 - 304
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BBS

ASPARTIC PROTEINASE 21-MAY-92 :: RENIN (E.C.3.4.23.15)

DOMAIN 1: [Assigned by homology with 1SMRA] 1 to 173 ; DOMAIN 2: [Assigned by homology with 1SMRA] 174 to 325 ; The following residues NOT assigned to any domain: Chain " " -1 - -1 Chain " " 326 - 326
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RNE

HYDROLASE(ACID PROTEINASE) 12-DEC-91 :: RENIN (ACTIVATED, GLYCOSYLATED, INHIBITED) (E.C.3.

DOMAIN 1: [Assigned by homology with 1SMRA] 1 to 173 ; DOMAIN 2: [Assigned by homology with 1SMRA] 174 to 325 ; The following residues NOT assigned to any domain: Chain " " -1 - 0 Chain " " 326 - 326
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2REN

PRELIMINARY 05-FEB-92 :: RENIN (E.C.3.4.23.15)

DOMAIN 1: [Assigned by homology with 1SMRA] 7 to 184 ; DOMAIN 2: [Assigned by homology with 1SMRA] 185 to 339 ; The following residues NOT assigned to any domain: Chain " " 4 - 6 Chain " " 340 - 340
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LYA B

LYSOSOMAL ASPARTIC PROTEASE 22-APR-93 :: CATHEPSIN D (E.C.3.4.23.5)

DOMAIN 1: [Assigned by homology with 1SMRA]B 106 to B 189 ; DOMAIN 2: [Assigned by homology with 1SMRA]B 190 to B 345 ; The following residues NOT assigned to any domain: Chain " " 1 - 97 The following residues NOT assigned to any domain: Chain " " 106 - 346 The following residues NOT assigned to any domain: Chain " " 1 - 97 The following residues NOT assigned to any domain: Chain " " 106 - 346
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LYA D

LYSOSOMAL ASPARTIC PROTEASE 22-APR-93 :: CATHEPSIN D (E.C.3.4.23.5)

DOMAIN 1: [Assigned by homology with 1SMRA]D 106 to D 189 ; DOMAIN 2: [Assigned by homology with 1SMRA]D 190 to D 345 ; The following residues NOT assigned to any domain: Chain " " 1 - 97 The following residues NOT assigned to any domain: Chain " " 106 - 346 The following residues NOT assigned to any domain: Chain " " 1 - 97 The following residues NOT assigned to any domain: Chain " " 106 - 346
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LYB B

LYSOSOMAL ASPARTIC PROTEASE 22-APR-93 :: CATHEPSIN D COMPLEX WITH PEPSTATIN A

DOMAIN 1: [Assigned by homology with 1SMRA]B 106 to B 189 ; DOMAIN 2: [Assigned by homology with 1SMRA]B 190 to B 345 ; The following residues NOT assigned to any domain: Chain " " 1 - 97 The following residues NOT assigned to any domain: Chain " " 106 - 346 The following residues NOT assigned to any domain: Chain " " 2 - 5 The following residues NOT assigned to any domain: Chain " " 1 - 97 The following residues NOT assigned to any domain: Chain " " 106 - 346 The following residues NOT assigned to any domain: Chain " " 12 - 15
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LYB D

LYSOSOMAL ASPARTIC PROTEASE 22-APR-93 :: CATHEPSIN D COMPLEX WITH PEPSTATIN A

DOMAIN 1: [Assigned by homology with 1SMRA]D 106 to D 189 ; DOMAIN 2: [Assigned by homology with 1SMRA]D 190 to D 345 ; The following residues NOT assigned to any domain: Chain " " 1 - 97 The following residues NOT assigned to any domain: Chain " " 106 - 346 The following residues NOT assigned to any domain: Chain " " 2 - 5 The following residues NOT assigned to any domain: Chain " " 1 - 97 The following residues NOT assigned to any domain: Chain " " 106 - 346 The following residues NOT assigned to any domain: Chain " " 12 - 15
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PSA A

HYDROLASE (ACID PROTEINASE) 22-OCT-91 :: PEPSIN HYDROLASE (ACID PROTEINASE) (E.C.3.4.23.1)

DOMAIN 1: [Assigned by homology with 1SMRA]A 1 to A 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]A 174 to A 325 ; The following residues NOT assigned to any domain: Chain "A" 326 - 326 The following residues NOT assigned to any domain: Chain "A" 2 - 3 The following residues NOT assigned to any domain: Chain "A" 1 - 326 The following residues NOT assigned to any domain: Chain "A" 2 - 3
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PSA B

HYDROLASE (ACID PROTEINASE) 22-OCT-91 :: PEPSIN HYDROLASE (ACID PROTEINASE) (E.C.3.4.23.1)

DOMAIN 1: [Assigned by homology with 1SMRA]B 1 to B 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]B 174 to B 325 ; The following residues NOT assigned to any domain: Chain "B" 1 - 326 The following residues NOT assigned to any domain: Chain "B" 2 - 3 The following residues NOT assigned to any domain: Chain "B" 326 - 326 The following residues NOT assigned to any domain: Chain "B" 2 - 3
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4PEP

HYDROLASE (ACID PROTEINASE) 18-DEC-89 :: PEPSIN (E.C.3.4.23.1)

DOMAIN 1: [Assigned by homology with 1SMRA] 1 to 173 ; DOMAIN 2: [Assigned by homology with 1SMRA] 174 to 325 ; The following residues NOT assigned to any domain: Chain " " 326 - 326
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5PEP

HYDROLASE(ACID PROTEINASE) 30-MAY-90 :: PEPSIN (E.C.3.4.23.1)

DOMAIN 1: [Assigned by homology with 1SMRA] 1 to 173 ; DOMAIN 2: [Assigned by homology with 1SMRA] 174 to 326 ; The following residues NOT assigned to any domain: Chain " " 327 - 327
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3PEP

HYDROLASE (ACID PROTEINASE) 24-OCT-89 :: PEPSIN (E.C.3.4.23.1)

DOMAIN 1: [Assigned by homology with 1SMRA] 1 to 173 ; DOMAIN 2: [Assigned by homology with 1SMRA] 174 to 325 ; The following residues NOT assigned to any domain: Chain " " 326 - 326
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3PSG

HYDROLASE(ACID PROTEINASE ZYMOGEN) 03-SEP-91 :: PEPSINOGEN

DOMAIN 1: [Assigned by homology with 1SMRA] 1 to 173 ; DOMAIN 2: [Assigned by homology with 1SMRA] 174 to 325 ; The following residues NOT assigned to any domain: Chain " " 1P - 44P Chain " " 326 - 326
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PSG

HYDROLASE(ACID PROTEINASE ZYMOGEN) 23-JAN-91 :: PEPSINOGEN

DOMAIN 1: [Assigned by homology with 1SMRA] 1 to 173 ; DOMAIN 2: [Assigned by homology with 1SMRA] 174 to 325 ; The following residues NOT assigned to any domain: Chain " " 1P - 44P Chain " " 326 - 326 The following residues NOT assigned to any domain: Chain " " 68 - 68
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4CMS

HYDROLASE (ACID PROTEINASE) 01-NOV-91 :: CHYMOSIN B (FORMERLY KNOWN AS RENNIN) (E.C.3.4.23.

DOMAIN 1: [Assigned by homology with 1SMRA] 1 to 173 ; DOMAIN 2: [Assigned by homology with 1SMRA] 174 to 325 ; The following residues NOT assigned to any domain: Chain " " -2 - -1 Chain " " 326 - 326
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3CMS

HYDROLASE (ACID PROTEINASE) 26-FEB-90 :: CHYMOSIN B (FORMERLY KNOWN AS RENNIN) (E.C.3.4.23.

DOMAIN 1: [Assigned by homology with 1SMRA] 1 to 173 ; DOMAIN 2: [Assigned by homology with 1SMRA] 174 to 325 ; The following residues NOT assigned to any domain: Chain " " -2 - -1 Chain " " 326 - 326
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CMS

HYDROLASE(ACID PROTEINASE) 12-OCT-89 :: CHYMOSIN B (FORMERLY KNOWN AS RENNIN) (E.C.3.4.23.

DOMAIN 1: [Assigned by homology with 1SMRA] 3 to 174 ; DOMAIN 2: [Assigned by homology with 1SMRA] 175 to 322 ; The following residues NOT assigned to any domain: Chain " " 1 - 2 Chain " " 323 - 323
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ASI

ASPARTIC PROTEINASE 12-SEP-94 :: ASPARTIC PROTEINASE FROM RHIZOMUCOR MIEHEI (RENNIL

DOMAIN 1: [Assigned by homology with 1SMRA] 6 to 190 ; DOMAIN 2: [Assigned by homology with 1SMRA] 191 to 354 ; The following residues NOT assigned to any domain: Chain " " 355 - 361
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MPP

HYDROLASE(ACID PROTEINASE) 19-FEB-92 :: PEPSIN (RENIN) (E.C.3.4.23.23)

DOMAIN 1: [Assigned by homology with 1SMRA] 1 to 173 ; DOMAIN 2: [Assigned by homology with 1SMRA] 174 to 325 ; The following residues NOT assigned to any domain: Chain " " -1 - -1 Chain " " 326 - 332
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4APR E

HYDROLASE (ACID PROTEINASE) 03-AUG-89 :: ACID PROTEINASE (RHIZOPUSPEPSIN) (E.C.3.4.23.6) CO

DOMAIN 1: [Assigned by homology with 1SMRA]E 3 to E 177 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 178 to E 323 ; The following residues NOT assigned to any domain: Chain "E" 1 - 2 Chain "E" 324 - 325 The following residues NOT assigned to any domain: Chain "E" 3 - 7
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5APR E

HYDROLASE (ACID PROTEINASE) 03-AUG-89 :: ACID PROTEINASE (RHIZOPUSPEPSIN) (E.C.3.4.23.6) CO

DOMAIN 1: [Assigned by homology with 1SMRA]E 3 to E 177 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 178 to E 323 ; The following residues NOT assigned to any domain: Chain "E" 1 - 2 Chain "E" 324 - 325 The following residues NOT assigned to any domain: Chain "E" 3 - 8
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2APR

HYDROLASE (ASPARTIC PROTEINASE) 19-MAR-87 :: ACID PROTEINASE (RHIZOPUSPEPSIN) (E.C.3.4.23.6)

DOMAIN 1: [Assigned by homology with 1SMRA] 3 to 177 ; DOMAIN 2: [Assigned by homology with 1SMRA] 178 to 323 ; The following residues NOT assigned to any domain: Chain " " 1 - 2 Chain " " 324 - 325
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6APR E

HYDROLASE (ACID PROTEINASE) 03-AUG-89 :: ACID PROTEINASE (RHIZOPUSPEPSIN) (E.C.3.4.23.6) CO

DOMAIN 1: [Assigned by homology with 1SMRA]E 3 to E 177 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 178 to E 323 ; The following residues NOT assigned to any domain: Chain "E" 1 - 2 Chain "E" 324 - 325 The following residues NOT assigned to any domain: Chain "E" 2 - 5
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3APR E

HYDROLASE (ASPARTIC PROTEINASE) 22-JUN-87 :: ACID PROTEINASE (RHIZOPUSPEPSIN) (E.C.3.4.23.6) CO

DOMAIN 1: [Assigned by homology with 1SMRA]E 3 to E 177 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 178 to E 323 ; The following residues NOT assigned to any domain: Chain "E" 1 - 2 Chain "E" 324 - 325 The following residues NOT assigned to any domain: Chain "E" 2 - 8
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PPK E

HYDROLASE(ACID PROTEINASE) 20-JAN-94 :: ACID PROTEINASE (PENICILLOPEPSIN) (E.C.3.4.23.20)

DOMAIN 1: [Assigned by homology with 1SMRA]E 5 to E 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 174 to E 322 ; The following residues NOT assigned to any domain: Chain "E" 1 - 4 Chain "E" 323 - 323 The following residues NOT assigned to any domain: Chain "E" 3 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PPL E

HYDROLASE(ACID PROTEINASE) 01-JUN-92 :: ACID PROTEINASE (PENICILLOPEPSIN) (E.C.3.4.23.20)

DOMAIN 1: [Assigned by homology with 1SMRA]E 5 to E 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 174 to E 322 ; The following residues NOT assigned to any domain: Chain "E" 1 - 4 Chain "E" 323 - 323 The following residues NOT assigned to any domain: Chain "E" 325 - 326
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PPM E

HYDROLASE(ACID PROTEINASE) 01-JUN-92 :: ACID PROTEINASE (PENICILLOPEPSIN) (E.C.3.4.23.20)

DOMAIN 1: [Assigned by homology with 1SMRA]E 5 to E 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 174 to E 322 ; The following residues NOT assigned to any domain: Chain "E" 1 - 4 Chain "E" 323 - 323 The following residues NOT assigned to any domain: Chain "E" 325 - 326
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3APP

HYDROLASE (ACID PROTEINASE) 27-NOV-90 :: ACID PROTEINASE (PENICILLOPEPSIN) (E.C.3.4.23.20)

DOMAIN 1: [Assigned by homology with 1SMRA] 5 to 173 ; DOMAIN 2: [Assigned by homology with 1SMRA] 174 to 322 ; The following residues NOT assigned to any domain: Chain " " 1 - 4 Chain " " 323 - 323
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1APT E

PRELIMINARY 16-DEC-91 :: ACID PROTEINASE (PENICILLOPEPSIN) (E.C.3.4.23.7) C

DOMAIN 1: [Assigned by homology with 1SMRA]E 5 to E 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 174 to E 322 ; The following residues NOT assigned to any domain: Chain " " 1 - 323 The following residues NOT assigned to any domain: Chain " " 3 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1APU E

PRELIMINARY 16-DEC-91 :: ACID PROTEINASE (PENICILLOPEPSIN) (E.C.3.4.23.7) C

DOMAIN 1: [Assigned by homology with 1SMRA]E 5 to E 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 174 to E 322 ; The following residues NOT assigned to any domain: Chain " " 1 - 323 The following residues NOT assigned to any domain: Chain " " 3 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1APV E

PRELIMINARY 16-DEC-91 :: ACID PROTEINASE (PENICILLOPEPSIN) (E.C.3.4.23.7) C

DOMAIN 1: [Assigned by homology with 1SMRA]E 5 to E 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 174 to E 322 ; The following residues NOT assigned to any domain: Chain " " 1 - 323 The following residues NOT assigned to any domain: Chain " " 3 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1APW E

PRELIMINARY 16-DEC-91 :: ACID PROTEINASE (PENICILLOPEPSIN) (E.C.3.4.23.7) C

DOMAIN 1: [Assigned by homology with 1SMRA]E 5 to E 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 174 to E 322 ; The following residues NOT assigned to any domain: Chain " " 1 - 323 The following residues NOT assigned to any domain: Chain " " 3 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4APE

HYDROLASE (ACID PROTEINASE) 09-JUN-86 :: ACID PROTEINASE (E.C.3.4.23.10), ENDOTHIAPEPSIN

DOMAIN 1: [Assigned by homology with 1SMRA] 1 to 173 ; DOMAIN 2: [Assigned by homology with 1SMRA] 174 to 326 ; The following residues NOT assigned to any domain: Chain " " -2 - 0
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4ER1 E

HYDROLASE (ACID PROTEINASE) 14-OCT-90 :: ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN)

DOMAIN 1: [Assigned by homology with 1SMRA]E 1 to E 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 174 to E 326 ; The following residues NOT assigned to any domain: Chain "E" -2 - 0 The following residues NOT assigned to any domain: Chain "E" 2 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4ER2 E

HYDROLASE (ACID PROTEINASE) 20-OCT-90 :: ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN)

DOMAIN 1: [Assigned by homology with 1SMRA]E 1 to E 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 174 to E 326 ; The following residues NOT assigned to any domain: Chain "E" -2 - 0 The following residues NOT assigned to any domain: Chain "E" 2 - 5
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4ER4 E

HYDROLASE (ACID PROTEINASE) 05-JAN-91 :: ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN)

DOMAIN 1: [Assigned by homology with 1SMRA]E 1 to E 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 174 to E 326 ; The following residues NOT assigned to any domain: Chain "E" -2 - 0 The following residues NOT assigned to any domain: Chain "E" 1 - 10
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EED P

PRELIMINARY 15-JUN-92 :: ENDOTHIAPEPSIN-PD125754 COMPLEX (E.C.3.4.23.6)

DOMAIN 1: [Assigned by homology with 1SMRA]P 1 to P 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]P 174 to P 326 ; The following residues NOT assigned to any domain: Chain " " 22 - 326
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5ER1 E

HYDROLASE (ACID PROTEINASE) 07-NOV-90 :: ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN)

DOMAIN 1: [Assigned by homology with 1SMRA]E 1 to E 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 174 to E 326 ; The following residues NOT assigned to any domain: Chain "E" -2 - 0 The following residues NOT assigned to any domain: Chain "E" 3 - 5
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5ER2 E

HYDROLASE (ACID PROTEINASE) 02-JAN-91 :: ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN)

DOMAIN 1: [Assigned by homology with 1SMRA]E 1 to E 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 174 to E 326 ; The following residues NOT assigned to any domain: Chain "E" -2 - 0 The following residues NOT assigned to any domain: Chain "E" 2 - 6
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EPL E

HYDROLASE(ACID PROTEINASE) 27-JUL-94 :: ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN)

DOMAIN 1: [Assigned by homology with 1SMRA]E 1 to E 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 174 to E 326 ; The following residues NOT assigned to any domain: Chain "E" -2 - 0 The following residues NOT assigned to any domain: Chain "E" 4 - 3'
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EPM E

HYDROLASE(ACID PROTEINASE) 27-JUL-94 :: ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN)

DOMAIN 1: [Assigned by homology with 1SMRA]E 1 to E 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 174 to E 326 ; The following residues NOT assigned to any domain: Chain "E" -2 - 0 The following residues NOT assigned to any domain: Chain "E" 5 - 4'
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EPN E

HYDROLASE(ACID PROTEINASE) 27-JUL-94 :: ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN)

DOMAIN 1: [Assigned by homology with 1SMRA]E 1 to E 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 174 to E 326 ; The following residues NOT assigned to any domain: Chain "E" -2 - 0 The following residues NOT assigned to any domain: Chain "E" 3 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EPO E

HYDROLASE(ACID PROTEINASE) 27-JUL-94 :: ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN)

DOMAIN 1: [Assigned by homology with 1SMRA]E 1 to E 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 174 to E 326 ; The following residues NOT assigned to any domain: Chain "E" -2 - 0 The following residues NOT assigned to any domain: Chain "E" 3 - 3
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EPP E

HYDROLASE(ACID PROTEINASE) 27-JUL-94 :: ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN)

DOMAIN 1: [Assigned by homology with 1SMRA]E 1 to E 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 174 to E 326 ; The following residues NOT assigned to any domain: Chain "E" -2 - 0 The following residues NOT assigned to any domain: Chain "E" 3 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EPQ E

HYDROLASE(ACID PROTEINASE) 27-JUL-94 :: ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN)

DOMAIN 1: [Assigned by homology with 1SMRA]E 1 to E 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 174 to E 326 ; The following residues NOT assigned to any domain: Chain "E" -2 - 0 The following residues NOT assigned to any domain: Chain "E" 3 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EPR E

HYDROLASE(ACID PROTEINASE) 27-JUL-94 :: ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN)

DOMAIN 1: [Assigned by homology with 1SMRA]E 1 to E 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 174 to E 326 ; The following residues NOT assigned to any domain: Chain "E" -2 - 0 The following residues NOT assigned to any domain: Chain "E" 2 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ER8 E

HYDROLASE (ACID PROTEINASE) 16-OCT-89 :: ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN)

DOMAIN 1: [Assigned by homology with 1SMRA]E 1 to E 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 174 to E 326 ; The following residues NOT assigned to any domain: Chain "E" -2 - 0 The following residues NOT assigned to any domain: Chain "E" 1 - 8
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3ER3 E

HYDROLASE (ACID PROTEINASE) 02-JAN-91 :: ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN)

DOMAIN 1: [Assigned by homology with 1SMRA]E 1 to E 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 174 to E 326 ; The following residues NOT assigned to any domain: Chain "E" -2 - 0 The following residues NOT assigned to any domain: Chain "E" 2 - 5
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3ER5 E

HYDROLASE (ACID PROTEINASE) 05-JAN-91 :: ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN)

DOMAIN 1: [Assigned by homology with 1SMRA]E 1 to E 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 174 to E 326 ; The following residues NOT assigned to any domain: Chain "E" -2 - 0 The following residues NOT assigned to any domain: Chain "E" 1 - 10
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2ER0 E

HYDROLASE (ACID PROTEINASE) 20-OCT-90 :: ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN)

DOMAIN 1: [Assigned by homology with 1SMRA]E 1 to E 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 174 to E 326 ; The following residues NOT assigned to any domain: Chain "E" -2 - 0 The following residues NOT assigned to any domain: Chain "E" 2 - 8
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2ER6 E

HYDROLASE (ACID PROTEINASE) 13-OCT-90 :: ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN)

DOMAIN 1: [Assigned by homology with 1SMRA]E 1 to E 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 174 to E 326 ; The following residues NOT assigned to any domain: Chain "E" -2 - 0 The following residues NOT assigned to any domain: Chain "E" 1 - 7
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2ER7 E

HYDROLASE (ACID PROTEINASE) 12-NOV-90 :: ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN)

DOMAIN 1: [Assigned by homology with 1SMRA]E 1 to E 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 174 to E 326 ; The following residues NOT assigned to any domain: Chain "E" -2 - 0 The following residues NOT assigned to any domain: Chain "E" 2 - 8
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2ER9 E

HYDROLASE (ACID PROTEINASE) 20-OCT-90 :: ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN)

DOMAIN 1: [Assigned by homology with 1SMRA]E 1 to E 173 ; DOMAIN 2: [Assigned by homology with 1SMRA]E 174 to E 326 ; The following residues NOT assigned to any domain: Chain "E" -2 - 0 The following residues NOT assigned to any domain: Chain "E" 2 - 8
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1VSG B

GLYCOPROTEIN 22-OCT-90 :: VARIANT SURFACE GLYCOPROTEIN (N-TERMINAL DOMAIN)

DOMAIN 1: [Assigned by homology with 1VSGA]B 1 to B 29 ; B 92 to B 251 ; DOMAIN 2: [Assigned by homology with 1VSGA]B 42 to B 75 ; B 266 to B 362 ; The following residues NOT assigned to any domain: Chain "B" 1 - 362 The following residues NOT assigned to any domain: Chain "B" 30 - 41 Chain "B" 76 - 91 Chain "B" 252 - 265
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4CSC

OXO-ACID-LYASE 07-MAY-90 :: CITRATE SYNTHASE (E.C.4.1.3.7)- D-MALATE - ACETYL

DOMAIN 1: 1 to 274 ; 381 to 433 ; DOMAIN 2: 275 to 380 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5CTS

OXO-ACID-LYASE 16-NOV-89 :: CITRATE SYNTHASE (E.C.4.1.3.7)- OXALOACETATE - CAR

DOMAIN 1: 1 to 274 ; 381 to 433 ; DOMAIN 2: 275 to 380 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6CTS

OXO-ACID-LYASE 16-NOV-89 :: CITRATE SYNTHASE (E.C.4.1.3.7) - CITRYLTHIOETHER -

DOMAIN 1: 1 to 274 ; 381 to 433 ; DOMAIN 2: 275 to 380 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CSC

OXO-ACID-LYASE 07-MAY-90 :: CITRATE SYNTHASE (E.C.4.1.3.7)- D-MALATE - CARBOXY

DOMAIN 1: 1 to 274 ; 381 to 433 ; DOMAIN 2: 275 to 380 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CSC

OXO-ACID-LYASE 07-MAY-90 :: CITRATE SYNTHASE (E.C.4.1.3.7)- L-MALATE - CARBOXY

DOMAIN 1: 1 to 274 ; 381 to 433 ; DOMAIN 2: 275 to 380 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3CSC

OXO-ACID-LYASE 07-MAY-90 :: CITRATE SYNTHASE (E.C.4.1.3.7)- L-MALATE - ACETYL

DOMAIN 1: 1 to 274 ; 381 to 433 ; DOMAIN 2: 275 to 380 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5CSC A

OXO-ACID-LYASE 07-MAY-90 :: CITRATE SYNTHASE (E.C.4.1.3.7)

DOMAIN 1: A 1 to A 274 ; A 381 to A 433 ; DOMAIN 2: A 275 to A 380 ; The following residues NOT assigned to any domain: Chain "A" 1 - 433
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5CSC B

OXO-ACID-LYASE 07-MAY-90 :: CITRATE SYNTHASE (E.C.4.1.3.7)

DOMAIN 1: B 1 to B 274 ; B 381 to B 433 ; DOMAIN 2: B 275 to B 380 ; The following residues NOT assigned to any domain: Chain "B" 1 - 433
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4CTS A

OXO-ACID-LYASE 27-JAN-84 :: CITRATE SYNTHASE (E.C.4.1.3.7) - OXALOACETATE COMP

DOMAIN 1: A 1 to A 274 ; A 381 to A 437 ; DOMAIN 2: A 275 to A 380 ; The following residues NOT assigned to any domain: Chain "A" 1 - 437
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4CTS B

OXO-ACID-LYASE 27-JAN-84 :: CITRATE SYNTHASE (E.C.4.1.3.7) - OXALOACETATE COMP

DOMAIN 1: B 1 to B 274 ; B 381 to B 437 ; DOMAIN 2: B 275 to B 380 ; The following residues NOT assigned to any domain: Chain "B" 1 - 437
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CTS

OXO-ACID-LYASE 27-JAN-84 :: CITRATE SYNTHASE (E.C.4.1.3.7) - CITRATE COMPLEX

DOMAIN 1: 1 to 274 ; 381 to 437 ; DOMAIN 2: 275 to 380 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CSH

LYASE(OXO-ACID) 07-MAR-94 :: CITRATE SYNTHASE (E.C.4.1.3.7) COMPLEXED WITH OXAL

DOMAIN 1: 3 to 274 ; 381 to 437 ; DOMAIN 2: 275 to 380 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CSI

LYASE(OXO-ACID) 07-MAR-94 :: CITRATE SYNTHASE (E.C.4.1.3.7) COMPLEXED WITH OXAL

DOMAIN 1: 3 to 274 ; 381 to 437 ; DOMAIN 2: 275 to 380 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3CCP

OXIDOREDUCTASE (H2O2 (A)) 28-FEB-90 :: YEAST CYTOCHROME $C PEROXIDASE (E.C.1.11.1.5) MUTA

DOMAIN 1: 2 to 144 ; 265 to 293 ; DOMAIN 2: 163 to 264 ; The following residues NOT assigned to any domain: Chain " " 145 - 162 Chain " " 294 - 294
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DCC

OXIDOREDUCTASE(H2O2(A)) 01-JUN-94 :: CYTOCHROME C PEROXIDASE (E.C.1.11.1.5) MUTANT WITH

DOMAIN 1: 4 to 144 ; 265 to 293 ; DOMAIN 2: 163 to 264 ; The following residues NOT assigned to any domain: Chain " " 145 - 162 Chain " " 294 - 294
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PCB A

OXIDOREDUCTASE/ELECTRON TRANSPORT 14-APR-93 :: YEAST CYTOCHROME C PEROXIDASE (CCP) COMPLEX WITH H

DOMAIN 1: A 2 to A 144 ; A 265 to A 293 ; DOMAIN 2: A 163 to A 264 ; The following residues NOT assigned to any domain: Chain "A" 1 - 1 Chain "A" 145 - 162 Chain "A" 294 - 294 The following residues NOT assigned to any domain: Chain "A" 1 - 104 The following residues NOT assigned to any domain: Chain "A" 1 - 294
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PCB C

OXIDOREDUCTASE/ELECTRON TRANSPORT 14-APR-93 :: YEAST CYTOCHROME C PEROXIDASE (CCP) COMPLEX WITH H

DOMAIN 1: C 2 to C 144 ; C 265 to C 293 ; DOMAIN 2: C 163 to C 264 ; The following residues NOT assigned to any domain: Chain "C" 1 - 294 The following residues NOT assigned to any domain: Chain "C" 1 - 104 The following residues NOT assigned to any domain: Chain "C" 1 - 1 Chain "C" 145 - 162 Chain "C" 294 - 294
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PCC A

OXIDOREDUCTASE/ELECTRON TRANSPORT 14-APR-93 :: YEAST CYTOCHROME C PEROXIDASE (CCP) COMPLEX WITH

DOMAIN 1: A 2 to A 144 ; A 265 to A 293 ; DOMAIN 2: A 163 to A 264 ; The following residues NOT assigned to any domain: Chain "A" 1 - 1 Chain "A" 145 - 162 Chain "A" 294 - 294 The following residues NOT assigned to any domain: Chain "A" -5 - 103 The following residues NOT assigned to any domain: Chain "A" 1 - 294 The following residues NOT assigned to any domain: Chain "A" -5 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PCC C

OXIDOREDUCTASE/ELECTRON TRANSPORT 14-APR-93 :: YEAST CYTOCHROME C PEROXIDASE (CCP) COMPLEX WITH

DOMAIN 1: C 2 to C 144 ; C 265 to C 293 ; DOMAIN 2: C 163 to C 264 ; The following residues NOT assigned to any domain: Chain "C" 1 - 294 The following residues NOT assigned to any domain: Chain "C" -5 - 103 The following residues NOT assigned to any domain: Chain "C" 1 - 1 Chain "C" 145 - 162 Chain "C" 294 - 294 The following residues NOT assigned to any domain: Chain "C" -5 - 103
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CCP

OXIDOREDUCTASE (H2O2 (A)) 28-FEB-90 :: YEAST CYTOCHROME $C PEROXIDASE (E.C.1.11.1.5)

DOMAIN 1: 2 to 144 ; 265 to 293 ; DOMAIN 2: 163 to 264 ; The following residues NOT assigned to any domain: Chain " " 145 - 162 Chain " " 294 - 294
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CCA

OXIDOREDUCTASE 04-JAN-93 :: CYTOCHROME C PEROXIDASE (CCP-MKT) (E.C.1.11.1.5) W

DOMAIN 1: 4 to 144 ; 265 to 293 ; DOMAIN 2: 163 to 264 ; The following residues NOT assigned to any domain: Chain " " 145 - 162 Chain " " 294 - 294
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CCB

OXIDOREDUCTASE 04-JAN-93 :: CYTOCHROME C PEROXIDASE (CCP-MKT) (E.C.1.11.1.5) M

DOMAIN 1: 4 to 144 ; 265 to 293 ; DOMAIN 2: 163 to 264 ; The following residues NOT assigned to any domain: Chain " " 145 - 162 Chain " " 294 - 294
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CCP

OXIDOREDUCTASE (H2O2 (A)) 28-FEB-90 :: YEAST CYTOCHROME $C PEROXIDASE (E.C.1.11.1.5) MUTA

DOMAIN 1: 2 to 144 ; 265 to 293 ; DOMAIN 2: 163 to 264 ; The following residues NOT assigned to any domain: Chain " " 145 - 162 Chain " " 294 - 294
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6CCP

OXIDOREDUCTASE(H2O2(A)) 07-JUN-93 :: CYTOCHROME C PEROXIDASE (E.C.1.11.1.5) MUTANT WITH

DOMAIN 1: 4 to 144 ; 265 to 293 ; DOMAIN 2: 163 to 264 ; The following residues NOT assigned to any domain: Chain " " 145 - 162 Chain " " 294 - 294
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CMP

OXIDOREDUCTASE(H2O2(A)) 23-NOV-93 :: CYTOCHROME C PEROXIDASE (RECOMBINANT YEAST, CCP-MK

DOMAIN 1: 4 to 144 ; 265 to 293 ; DOMAIN 2: 163 to 264 ; The following residues NOT assigned to any domain: Chain " " 145 - 162 Chain " " 294 - 294
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CMQ

OXIDOREDUCTASE(H2O2(A)) 23-NOV-93 :: CYTOCHROME C PEROXIDASE (RECOMBINANT YEAST, CCP-MK

DOMAIN 1: 4 to 144 ; 265 to 293 ; DOMAIN 2: 163 to 264 ; The following residues NOT assigned to any domain: Chain " " 145 - 162 Chain " " 294 - 294
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CPD

OXIDOREDUCTASE(H2O2(A)) 18-AUG-94 :: CYTOCHROME C PEROXIDASE (E.C.1.11.1.5) MUTANT WITH

DOMAIN 1: 4 to 144 ; 265 to 293 ; DOMAIN 2: 163 to 264 ; The following residues NOT assigned to any domain: Chain " " 145 - 162 Chain " " 294 - 294
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CPE

OXIDOREDUCTASE(H2O2(A)) 18-AUG-94 :: CYTOCHROME C PEROXIDASE (E.C.1.11.1.5) MUTANT WITH

DOMAIN 1: 4 to 144 ; 265 to 293 ; DOMAIN 2: 163 to 264 ; The following residues NOT assigned to any domain: Chain " " 145 - 162 Chain " " 294 - 294
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CPF

OXIDOREDUCTASE(H2O2(A)) 18-AUG-94 :: CYTOCHROME C PEROXIDASE (E.C.1.11.1.5) MUTANT WITH

DOMAIN 1: 4 to 144 ; 265 to 293 ; DOMAIN 2: 163 to 264 ; The following residues NOT assigned to any domain: Chain " " 145 - 162 Chain " " 294 - 294
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CCC

OXIDOREDUCTASE 04-JAN-93 :: CYTOCHROME C PEROXIDASE (CCP-MKT) (E.C.1.11.1.5) M

DOMAIN 1: 4 to 144 ; 265 to 293 ; DOMAIN 2: 163 to 264 ; The following residues NOT assigned to any domain: Chain " " 145 - 162 Chain " " 294 - 294
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CPG

OXIDOREDUCTASE(H2O2(A)) 18-AUG-94 :: CYTOCHROME C PEROXIDASE (E.C.1.11.1.5) MUTANT WITH

DOMAIN 1: 4 to 144 ; 265 to 293 ; DOMAIN 2: 163 to 264 ; The following residues NOT assigned to any domain: Chain " " 145 - 162 Chain " " 294 - 294
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CEP

OXIDOREDUCTASE(H2O2(A)) 31-MAY-94 :: CYTOCHROME C PEROXIDASE (E.C.1.11.1.5) MUTANT WITH

DOMAIN 1: 2 to 144 ; 265 to 293 ; DOMAIN 2: 163 to 264 ; The following residues NOT assigned to any domain: Chain " " 145 - 162 Chain " " 294 - 294
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5CCP

OXIDOREDUCTASE(H2O2(A)) 07-JUN-93 :: CYTOCHROME C PEROXIDASE (E.C.1.11.1.5) MUTANT WITH

DOMAIN 1: 4 to 144 ; 265 to 293 ; DOMAIN 2: 163 to 264 ; The following residues NOT assigned to any domain: Chain " " 145 - 162 Chain " " 294 - 294
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7CCP

OXIDOREDUCTASE(H2O2(A)) 07-JUN-93 :: CYTOCHROME C PEROXIDASE (E.C.1.11.1.5) MUTANT WITH

DOMAIN 1: 4 to 144 ; 265 to 293 ; DOMAIN 2: 163 to 264 ; The following residues NOT assigned to any domain: Chain " " 145 - 162 Chain " " 294 - 294
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CCE

OXIDOREDUCTASE(H2O2(A)) 04-MAY-94 :: CYTOCHROME C PEROXIDASE (E.C.1.11.1.5) (CCP-MKT) M

DOMAIN 1: 4 to 144 ; 265 to 293 ; DOMAIN 2: 163 to 264 ; The following residues NOT assigned to any domain: Chain " " 145 - 162 Chain " " 294 - 294
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CCG

OXIDOREDUCTASE(H2O2(A)) 04-MAY-94 :: CYTOCHROME C PEROXIDASE (E.C.1.11.1.5) (CCP-MKT) M

DOMAIN 1: 4 to 144 ; 265 to 293 ; DOMAIN 2: 163 to 264 ; The following residues NOT assigned to any domain: Chain " " 145 - 162 Chain " " 294 - 294
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4CCP

OXIDOREDUCTASE (H2O2 (A)) 28-FEB-90 :: YEAST CYTOCHROME $C PEROXIDASE (E.C.1.11.1.5) MUTA

DOMAIN 1: 2 to 144 ; 265 to 293 ; DOMAIN 2: 163 to 264 ; The following residues NOT assigned to any domain: Chain " " 145 - 162 Chain " " 294 - 294
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EDB

DEHALOGENASE 13-MAY-93 :: HALOALKANE DEHALOGENASE (E.C.3.8.1.5) COMPLEX WITH

DOMAIN 1: 1 to 155 ; 230 to 310 ; DOMAIN 2: 156 to 229 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EDD

DEHALOGENASE 13-MAY-93 :: HALOALKANE DEHALOGENASE (E.C.3.8.1.5) COMPLEX WITH

DOMAIN 1: 1 to 155 ; 230 to 310 ; DOMAIN 2: 156 to 229 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1EDE

DEHALOGENASE 13-MAY-93 :: HALOALKANE DEHALOGENASE (E.C.3.8.1.5) AT PH 8.2

DOMAIN 1: 1 to 155 ; 230 to 310 ; DOMAIN 2: 156 to 229 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2DHC

DEHALOGENASE 08-SEP-93 :: HALOALKANE DEHALOGENASE (E.C.3.8.1.5) COMPLEXED WI

DOMAIN 1: 1 to 155 ; 230 to 310 ; DOMAIN 2: 156 to 229 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2DHD

DEHALOGENASE 08-SEP-93 :: HALOALKANE DEHALOGENASE (E.C.3.8.1.5) COMPLEXED WI

DOMAIN 1: 1 to 155 ; 230 to 310 ; DOMAIN 2: 156 to 229 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2DHE

DEHALOGENASE 24-JUN-93 :: HALOALKANE DEHALOGENASE (E.C.3.8.1.5)

DOMAIN 1: 1 to 155 ; 230 to 310 ; DOMAIN 2: 156 to 229 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2EDA

DEHALOGENASE 30-AUG-93 :: HALOALKANE DEHALOGENASE (E.C.3.8.1.5) COMPLEX WITH

DOMAIN 1: 1 to 155 ; 230 to 310 ; DOMAIN 2: 156 to 229 ; The following residues NOT assigned to any domain: Chain " " 700 - 700
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2EDC

DEHALOGENASE 31-AUG-93 :: HALOALKANE DEHALOGENASE (E.C.3.8.1.5)

DOMAIN 1: 1 to 155 ; 230 to 310 ; DOMAIN 2: 156 to 229 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2BMH A

OXIDOREDUCTASE(OXYGENASE) 17-MAY-94 :: CYTOCHROME P450 (BM-3) (E.C.1.14.14.1) (HEMOPROTEI

DOMAIN 1: [Assigned by homology with 2HPDA]A 1 to A 70 ; A 329 to A 361 ; DOMAIN 2: [Assigned by homology with 2HPDA]A 72 to A 325 ; A 390 to A 455 ; The following residues NOT assigned to any domain: Chain "A" 71 - 71 Chain "A" 326 - 328 Chain "A" 362 - 389 The following residues NOT assigned to any domain: Chain "A" 1 - 455
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2BMH B

OXIDOREDUCTASE(OXYGENASE) 17-MAY-94 :: CYTOCHROME P450 (BM-3) (E.C.1.14.14.1) (HEMOPROTEI

DOMAIN 1: [Assigned by homology with 2HPDA]B 1 to B 70 ; B 329 to B 361 ; DOMAIN 2: [Assigned by homology with 2HPDA]B 72 to B 325 ; B 390 to B 455 ; The following residues NOT assigned to any domain: Chain "B" 1 - 455 The following residues NOT assigned to any domain: Chain "B" 71 - 71 Chain "B" 326 - 328 Chain "B" 362 - 389
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HPD B

OXIDOREDUCTASE(OXYGENASE) 16-SEP-93 :: CYTOCHROME P450 (BM-3) (E.C.1.14.14.1) (HEMOPROTEI

DOMAIN 1: [Assigned by homology with 2HPDA]B 1 to B 70 ; B 329 to B 361 ; DOMAIN 2: [Assigned by homology with 2HPDA]B 72 to B 325 ; B 390 to B 457 ; The following residues NOT assigned to any domain: Chain "B" 1 - 457 The following residues NOT assigned to any domain: Chain "B" 71 - 71 Chain "B" 326 - 328 Chain "B" 362 - 389
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2LBP

PERIPLASMIC BINDING PROTEIN 10-APR-89 :: LEUCINE-BINDING PROTEIN (/LBP$)

DOMAIN 1: 1 to 118 ; 253 to 328 ; DOMAIN 2: 124 to 247 ; 334 to 346 ; The following residues NOT assigned to any domain: Chain " " 119 - 123 Chain " " 248 - 252 Chain " " 329 - 333
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3SGA E

HYDROLASE (SERINE PROTEINASE) 29-MAY-90 :: PROTEINASE *A (COMPONENT OF THE EXTRACELLULAR FILT

DOMAIN 1: E 16 to E 125 ; DOMAIN 2: E 126 to E 241 ; The following residues NOT assigned to any domain: Chain "E" 242 - 242 The following residues NOT assigned to any domain: Chain "E" 5 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4SGA E

HYDROLASE (SERINE PROTEINASE) 29-MAY-90 :: PROTEINASE *A (COMPONENT OF THE EXTRACELLULAR FILT

DOMAIN 1: E 16 to E 125 ; DOMAIN 2: E 126 to E 241 ; The following residues NOT assigned to any domain: Chain "E" 242 - 242 The following residues NOT assigned to any domain: Chain "E" 5 - 1
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5SGA E

HYDROLASE (SERINE PROTEINASE) 29-MAY-90 :: PROTEINASE *A (COMPONENT OF THE EXTRACELLULAR FILT

DOMAIN 1: E 16 to E 125 ; DOMAIN 2: E 126 to E 241 ; The following residues NOT assigned to any domain: Chain "E" 242 - 242 The following residues NOT assigned to any domain: Chain "E" 5 - 1
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SGC

HYDROLASE (SERINE PROTEINASE) 18-APR-86 :: PROTEINASE *A COMPLEX WITH CHYMOSTATIN

DOMAIN 1: 16 to 125 ; DOMAIN 2: 126 to 241 ; The following residues NOT assigned to any domain: Chain " " 242 - 242
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3SGB E

COMPLEX(SERINE PROTEINASE-INHIBITOR) 21-JAN-83 :: PROTEINASE B FROM STREPTOMYCES GRISEUS (/SGPB$)

DOMAIN 1: E 16 to E 125 ; DOMAIN 2: E 126 to E 241 ; The following residues NOT assigned to any domain: Chain "E" 242 - 242 The following residues NOT assigned to any domain: Chain "E" 7 - 56
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4SGB E

COMPLEX(SERINE PROTEINASE-INHIBITOR) 21-SEP-89 :: SERINE PROTEINASE B COMPLEX WITH THE POTATO INHIBI

DOMAIN 1: E 16 to E 122 ; DOMAIN 2: E 123 to E 242 ; The following residues NOT assigned to any domain: Chain "E" 243 - 243 The following residues NOT assigned to any domain: Chain "E" 1 - 51
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2LPR A

HYDROLASE (SERINE PROTEINASE) 05-AUG-91 :: ALPHA-LYTIC PROTEASE (E.C.3.4.21.12) (MUTANT WITH

DOMAIN 1: A 15 A to A 125 ; DOMAIN 2: A 126 to A 241 ; The following residues NOT assigned to any domain: Chain "A" 242 - 244 The following residues NOT assigned to any domain: Chain "A" 4 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LPR A

HYDROLASE (SERINE PROTEINASE) 05-AUG-91 :: ALPHA-LYTIC PROTEASE (E.C.3.4.21.12) (MUTANT WITH

DOMAIN 1: A 15 A to A 125 ; DOMAIN 2: A 126 to A 241 ; The following residues NOT assigned to any domain: Chain "A" 242 - 244 The following residues NOT assigned to any domain: Chain "A" 4 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4LPR A

HYDROLASE (SERINE PROTEINASE) 05-AUG-91 :: ALPHA-LYTIC PROTEASE (E.C.3.4.21.12) (MUTANT WITH

DOMAIN 1: A 15 A to A 125 ; DOMAIN 2: A 126 to A 241 ; The following residues NOT assigned to any domain: Chain "A" 242 - 244 The following residues NOT assigned to any domain: Chain "A" 4 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2P07

HYDROLASE (SERINE PROTEINASE) 26-OCT-90 :: ALPHA-*LYTIC PROTEASE (E.C.3.4.21.12) MUTANT WITH

DOMAIN 1: 15 A to 125 ; DOMAIN 2: 126 to 241 ; The following residues NOT assigned to any domain: Chain " " 242 - 244
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1P08 A

HYDROLASE (SERINE PROTEINASE) 24-APR-89 :: ALPHA-LYTIC PROTEASE (E.C.3.4.21.12) (MUTANT WITH

DOMAIN 1: A 15 A to A 125 ; DOMAIN 2: A 126 to A 241 ; The following residues NOT assigned to any domain: Chain "A" 242 - 244 The following residues NOT assigned to any domain: Chain "A" 4 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3LPR A

HYDROLASE (SERINE PROTEINASE) 05-AUG-91 :: ALPHA-LYTIC PROTEASE (E.C.3.4.21.12) (MUTANT WITH

DOMAIN 1: A 15 A to A 125 ; DOMAIN 2: A 126 to A 241 ; The following residues NOT assigned to any domain: Chain "A" 242 - 244 The following residues NOT assigned to any domain: Chain "A" 4 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2ALP

HYDROLASE (SERINE PROTEINASE) 07-MAR-85 :: ALPHA-LYTIC PROTEASE (E.C.3.4.21.12)

DOMAIN 1: 15 A to 122 ; DOMAIN 2: 123 to 242 ; The following residues NOT assigned to any domain: Chain " " 243 - 245
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5LPR A

HYDROLASE (SERINE PROTEINASE) 05-AUG-91 :: ALPHA-LYTIC PROTEASE (E.C.3.4.21.12) (MUTANT WITH

DOMAIN 1: A 15 A to A 125 ; DOMAIN 2: A 126 to A 241 ; The following residues NOT assigned to any domain: Chain "A" 242 - 244 The following residues NOT assigned to any domain: Chain "A" 4 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6LPR A

HYDROLASE (SERINE PROTEINASE) 05-AUG-91 :: ALPHA-LYTIC PROTEASE (E.C.3.4.21.12) (MUTANT WITH

DOMAIN 1: A 15 A to A 125 ; DOMAIN 2: A 126 to A 241 ; The following residues NOT assigned to any domain: Chain "A" 242 - 244 The following residues NOT assigned to any domain: Chain "A" 4 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1P01 A

HYDROLASE (SERINE PROTEINASE) 24-APR-89 :: ALPHA-LYTIC PROTEASE (E.C.3.4.21.12) COMPLEX WITH

DOMAIN 1: A 15 A to A 125 ; DOMAIN 2: A 126 to A 241 ; The following residues NOT assigned to any domain: Chain "A" 242 - 244 The following residues NOT assigned to any domain: Chain "A" 3 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1P02 A

HYDROLASE (SERINE PROTEINASE) 24-APR-89 :: ALPHA-LYTIC PROTEASE (E.C.3.4.21.12) COMPLEX WITH

DOMAIN 1: A 15 A to A 125 ; DOMAIN 2: A 126 to A 241 ; The following residues NOT assigned to any domain: Chain "A" 242 - 244 The following residues NOT assigned to any domain: Chain "A" 4 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1P03 A

HYDROLASE (SERINE PROTEINASE) 24-APR-89 :: ALPHA-LYTIC PROTEASE (E.C.3.4.21.12) COMPLEX WITH

DOMAIN 1: A 15 A to A 125 ; DOMAIN 2: A 126 to A 241 ; The following residues NOT assigned to any domain: Chain "A" 242 - 244 The following residues NOT assigned to any domain: Chain "A" 4 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1P04 A

HYDROLASE (SERINE PROTEINASE) 24-APR-89 :: ALPHA-LYTIC PROTEASE (E.C.3.4.21.12) COMPLEX WITH

DOMAIN 1: A 15 A to A 125 ; DOMAIN 2: A 126 to A 241 ; The following residues NOT assigned to any domain: Chain "A" 242 - 244 The following residues NOT assigned to any domain: Chain "A" 4 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1P05 A

HYDROLASE (SERINE PROTEINASE) 24-APR-89 :: ALPHA-LYTIC PROTEASE (E.C.3.4.21.12) COMPLEX WITH

DOMAIN 1: A 15 A to A 125 ; DOMAIN 2: A 126 to A 241 ; The following residues NOT assigned to any domain: Chain "A" 242 - 244 The following residues NOT assigned to any domain: Chain "A" 4 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1P06 A

HYDROLASE (SERINE PROTEINASE) 24-APR-89 :: ALPHA-LYTIC PROTEASE (E.C.3.4.21.12) COMPLEX WITH

DOMAIN 1: A 15 A to A 125 ; DOMAIN 2: A 126 to A 241 ; The following residues NOT assigned to any domain: Chain "A" 242 - 244 The following residues NOT assigned to any domain: Chain "A" 4 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7LPR A

HYDROLASE (SERINE PROTEINASE) 05-AUG-91 :: ALPHA-LYTIC PROTEASE (E.C.3.4.21.12) (MUTANT WITH

DOMAIN 1: A 15 A to A 125 ; DOMAIN 2: A 126 to A 241 ; The following residues NOT assigned to any domain: Chain "A" 242 - 244 The following residues NOT assigned to any domain: Chain "A" 4 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1P09 A

HYDROLASE (SERINE PROTEINASE) 24-APR-89 :: ALPHA-LYTIC PROTEASE (E.C.3.4.21.12) (MUTANT WITH

DOMAIN 1: A 15 A to A 125 ; DOMAIN 2: A 126 to A 241 ; The following residues NOT assigned to any domain: Chain "A" 242 - 244
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1P10 A

HYDROLASE (SERINE PROTEINASE) 24-APR-89 :: ALPHA-LYTIC PROTEASE (E.C.3.4.21.12) (MUTANT WITH

DOMAIN 1: A 15 A to A 125 ; DOMAIN 2: A 126 to A 241 ; The following residues NOT assigned to any domain: Chain "A" 242 - 244 The following residues NOT assigned to any domain: Chain "A" 4 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1P11 E

HYDROLASE (SERINE PROTEINASE) 26-OCT-90 :: ALPHA-*LYTIC PROTEASE (E.C.3.4.21.12) COMPLEX WITH

DOMAIN 1: E 15 A to E 125 ; DOMAIN 2: E 126 to E 241 ; The following residues NOT assigned to any domain: Chain "E" 242 - 244 The following residues NOT assigned to any domain: Chain "E" 4 - -2 The following residues NOT assigned to any domain: Chain "E" 4 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1P12 E

HYDROLASE (SERINE PROTEINASE) 26-OCT-90 :: ALPHA-*LYTIC PROTEASE (E.C.3.4.21.12) COMPLEX WITH

DOMAIN 1: E 15 A to E 125 ; DOMAIN 2: E 126 to E 241 ; The following residues NOT assigned to any domain: Chain "E" 242 - 244 The following residues NOT assigned to any domain: Chain "E" 4 - -2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8LPR A

HYDROLASE (SERINE PROTEINASE) 05-AUG-91 :: ALPHA-LYTIC PROTEASE (E.C.3.4.21.12) (MUTANT WITH

DOMAIN 1: A 15 A to A 125 ; DOMAIN 2: A 126 to A 241 ; The following residues NOT assigned to any domain: Chain "A" 242 - 244 The following residues NOT assigned to any domain: Chain "A" 4 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

9LPR A

HYDROLASE (SERINE PROTEINASE) 05-AUG-91 :: ALPHA-LYTIC PROTEASE (E.C.3.4.21.12) COMPLEX WITH

DOMAIN 1: A 15 A to A 125 ; DOMAIN 2: A 126 to A 241 ; The following residues NOT assigned to any domain: Chain "A" 242 - 244 The following residues NOT assigned to any domain: Chain "A" 4 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SNW A

PRELIMINARY 17-JUL-92 :: SINDBIS VIRUS CAPSID PROTEIN (CHYMOTRYPSIN-LIKE SE

DOMAIN 1: A 114 to A 177 ; DOMAIN 2: A 180 to A 264 ; The following residues NOT assigned to any domain: Chain "A" 178 - 179 The following residues NOT assigned to any domain: Chain "A" 114 - 264
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SNW B

PRELIMINARY 17-JUL-92 :: SINDBIS VIRUS CAPSID PROTEIN (CHYMOTRYPSIN-LIKE SE

DOMAIN 1: B 114 to B 177 ; DOMAIN 2: B 180 to B 264 ; The following residues NOT assigned to any domain: Chain "B" 114 - 264 The following residues NOT assigned to any domain: Chain "B" 178 - 179
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2TBV C

VIRUS 22-JUN-84 :: TOMATO BUSHY STUNT VIRUS

DOMAIN 1: [Assigned by homology with 2TBVA]C 67 to C 270 ; DOMAIN 2: [Assigned by homology with 2TBVA]C 271 to C 386 ; The following residues NOT assigned to any domain: Chain "C" 101 - 387 The following residues NOT assigned to any domain: Chain "C" 101 - 387 The following residues NOT assigned to any domain: Chain "C" 387 - 387
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2TBV B

VIRUS 22-JUN-84 :: TOMATO BUSHY STUNT VIRUS

DOMAIN 1: [Assigned by homology with 2TBVA]B 102 to B 270 ; DOMAIN 2: [Assigned by homology with 2TBVA]B 271 to B 386 ; The following residues NOT assigned to any domain: Chain "B" 101 - 387 The following residues NOT assigned to any domain: Chain "B" 101 - 101 Chain "B" 387 - 387 The following residues NOT assigned to any domain: Chain "B" 67 - 387
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1COY

OXIDOREDUCTASE(OXYGEN RECEPTOR) 14-JUN-93 :: CHOLESTEROL OXIDASE (E.C.1.1.3.6) COMPLEX WITH

DOMAIN 1: 4 to 43 ; 225 to 315 ; 461 to 505 ; DOMAIN 2: 44 to 224 ; 316 to 460 ; The following residues NOT assigned to any domain: Chain " " 506 - 506
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BLB A

EYE LENS PROTEIN 22-DEC-93 :: BETA B2 CRYSTALLIN TETRAMER

DOMAIN 1: A -6 to A 82 ; DOMAIN 2: A 83 to A 173 ; The following residues NOT assigned to any domain: Chain "A" 174 - 175 The following residues NOT assigned to any domain: Chain "A" -2 - 175 The following residues NOT assigned to any domain: Chain "A" -8 - 175 The following residues NOT assigned to any domain: Chain "A" -4 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BLB C

EYE LENS PROTEIN 22-DEC-93 :: BETA B2 CRYSTALLIN TETRAMER

DOMAIN 1: C -8 to C 82 ; DOMAIN 2: C 83 to C 173 ; The following residues NOT assigned to any domain: Chain "C" -6 - 175 The following residues NOT assigned to any domain: Chain "C" -2 - 175 The following residues NOT assigned to any domain: Chain "C" 174 - 175 The following residues NOT assigned to any domain: Chain "C" -4 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BLB D

EYE LENS PROTEIN 22-DEC-93 :: BETA B2 CRYSTALLIN TETRAMER

DOMAIN 1: D -4 to D 82 ; DOMAIN 2: D 83 to D 173 ; The following residues NOT assigned to any domain: Chain "D" -6 - 175 The following residues NOT assigned to any domain: Chain "D" -2 - 175 The following residues NOT assigned to any domain: Chain "D" -8 - 175 The following residues NOT assigned to any domain: Chain "D" 174 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BLB B

EYE LENS PROTEIN 22-DEC-93 :: BETA B2 CRYSTALLIN TETRAMER

DOMAIN 1: B -2 to B 82 ; DOMAIN 2: B 83 to B 173 ; The following residues NOT assigned to any domain: Chain "B" -6 - 175 The following residues NOT assigned to any domain: Chain "B" 174 - 175 The following residues NOT assigned to any domain: Chain "B" -8 - 175 The following residues NOT assigned to any domain: Chain "B" -4 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2BB2

EYE LENS PROTEIN 21-SEP-92 :: BETA-B2-CRYSTALLIN

DOMAIN 1: -2 to 82 ; DOMAIN 2: 83 to 173 ; The following residues NOT assigned to any domain: Chain " " 174 - 175
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GCS

EYE LENS PROTEIN 27-JAN-94 :: GAMMA-B CRYSTALLIN (PREVIOUSLY CALLED GAMMA-II CRY

DOMAIN 1: 1 to 82 ; DOMAIN 2: 83 to 173 ; The following residues NOT assigned to any domain: Chain " " 174 - 174
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2GCR

EYE LENS PROTEIN 23-MAY-89 :: GAMMA /IV$A-CRYSTALLIN

DOMAIN 1: 1 to 82 ; DOMAIN 2: 82 to 173 ; The following residues NOT assigned to any domain: Chain " " 174 - 174
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2LDB

OXIDOREDUCTASE(CHOH(D)-NAD(A)) 27-MAR-89 :: L-*LACTATE DEHYDROGENASE (E.C.1.1.1.27) COMPLEX WI

DOMAIN 1: 15 to 164 ; DOMAIN 2: 165 to 331 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LDB

OXIDOREDUCTASE(CHOH(D)-NAD(A)) 27-MAR-89 :: APO-*L-*LACTATE DEHYDROGENASE (E.C.1.1.1.27)

DOMAIN 1: 15 to 164 ; DOMAIN 2: 165 to 331 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LDN A

PRELIMINARY 19-NOV-91 :: L-LACTATE DEHYDROGENASE (E.C.1.1.1.27) COMPLEX WIT

DOMAIN 1: A 15 to A 164 ; DOMAIN 2: A 165 to A 330 ; The following residues NOT assigned to any domain: Chain "A" 15 - 330 The following residues NOT assigned to any domain: Chain "A" 15 - 330 The following residues NOT assigned to any domain: Chain "A" 15 - 330 The following residues NOT assigned to any domain: Chain "A" 15 - 330 The following residues NOT assigned to any domain: Chain "A" 15 - 330 The following residues NOT assigned to any domain: Chain "A" 15 - 330 The following residues NOT assigned to any domain: Chain "A" 15 - 330
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LDN B

PRELIMINARY 19-NOV-91 :: L-LACTATE DEHYDROGENASE (E.C.1.1.1.27) COMPLEX WIT

DOMAIN 1: B 15 to B 164 ; DOMAIN 2: B 165 to B 330 ; The following residues NOT assigned to any domain: Chain "B" 15 - 330 The following residues NOT assigned to any domain: Chain "B" 15 - 330 The following residues NOT assigned to any domain: Chain "B" 15 - 330 The following residues NOT assigned to any domain: Chain "B" 15 - 330 The following residues NOT assigned to any domain: Chain "B" 15 - 330 The following residues NOT assigned to any domain: Chain "B" 15 - 330 The following residues NOT assigned to any domain: Chain "B" 15 - 330
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LDN C

PRELIMINARY 19-NOV-91 :: L-LACTATE DEHYDROGENASE (E.C.1.1.1.27) COMPLEX WIT

DOMAIN 1: C 15 to C 164 ; DOMAIN 2: C 165 to C 330 ; The following residues NOT assigned to any domain: Chain "C" 15 - 330 The following residues NOT assigned to any domain: Chain "C" 15 - 330 The following residues NOT assigned to any domain: Chain "C" 15 - 330 The following residues NOT assigned to any domain: Chain "C" 15 - 330 The following residues NOT assigned to any domain: Chain "C" 15 - 330 The following residues NOT assigned to any domain: Chain "C" 15 - 330 The following residues NOT assigned to any domain: Chain "C" 15 - 330
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LDN D

PRELIMINARY 19-NOV-91 :: L-LACTATE DEHYDROGENASE (E.C.1.1.1.27) COMPLEX WIT

DOMAIN 1: D 15 to D 164 ; DOMAIN 2: D 165 to D 330 ; The following residues NOT assigned to any domain: Chain "D" 15 - 330 The following residues NOT assigned to any domain: Chain "D" 15 - 330 The following residues NOT assigned to any domain: Chain "D" 15 - 330 The following residues NOT assigned to any domain: Chain "D" 15 - 330 The following residues NOT assigned to any domain: Chain "D" 15 - 330 The following residues NOT assigned to any domain: Chain "D" 15 - 330 The following residues NOT assigned to any domain: Chain "D" 15 - 330
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LDN E

PRELIMINARY 19-NOV-91 :: L-LACTATE DEHYDROGENASE (E.C.1.1.1.27) COMPLEX WIT

DOMAIN 1: E 15 to E 164 ; DOMAIN 2: E 165 to E 330 ; The following residues NOT assigned to any domain: Chain "E" 15 - 330 The following residues NOT assigned to any domain: Chain "E" 15 - 330 The following residues NOT assigned to any domain: Chain "E" 15 - 330 The following residues NOT assigned to any domain: Chain "E" 15 - 330 The following residues NOT assigned to any domain: Chain "E" 15 - 330 The following residues NOT assigned to any domain: Chain "E" 15 - 330 The following residues NOT assigned to any domain: Chain "E" 15 - 330
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LDN F

PRELIMINARY 19-NOV-91 :: L-LACTATE DEHYDROGENASE (E.C.1.1.1.27) COMPLEX WIT

DOMAIN 1: F 15 to F 164 ; DOMAIN 2: F 165 to F 330 ; The following residues NOT assigned to any domain: Chain "F" 15 - 330 The following residues NOT assigned to any domain: Chain "F" 15 - 330 The following residues NOT assigned to any domain: Chain "F" 15 - 330 The following residues NOT assigned to any domain: Chain "F" 15 - 330 The following residues NOT assigned to any domain: Chain "F" 15 - 330 The following residues NOT assigned to any domain: Chain "F" 15 - 330 The following residues NOT assigned to any domain: Chain "F" 15 - 330
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LDN G

PRELIMINARY 19-NOV-91 :: L-LACTATE DEHYDROGENASE (E.C.1.1.1.27) COMPLEX WIT

DOMAIN 1: G 15 to G 164 ; DOMAIN 2: G 165 to G 330 ; The following residues NOT assigned to any domain: Chain "G" 15 - 330 The following residues NOT assigned to any domain: Chain "G" 15 - 330 The following residues NOT assigned to any domain: Chain "G" 15 - 330 The following residues NOT assigned to any domain: Chain "G" 15 - 330 The following residues NOT assigned to any domain: Chain "G" 15 - 330 The following residues NOT assigned to any domain: Chain "G" 15 - 330 The following residues NOT assigned to any domain: Chain "G" 15 - 330
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LDN H

PRELIMINARY 19-NOV-91 :: L-LACTATE DEHYDROGENASE (E.C.1.1.1.27) COMPLEX WIT

DOMAIN 1: H 15 to H 164 ; DOMAIN 2: H 165 to H 330 ; The following residues NOT assigned to any domain: Chain "H" 15 - 330 The following residues NOT assigned to any domain: Chain "H" 15 - 330 The following residues NOT assigned to any domain: Chain "H" 15 - 330 The following residues NOT assigned to any domain: Chain "H" 15 - 330 The following residues NOT assigned to any domain: Chain "H" 15 - 330 The following residues NOT assigned to any domain: Chain "H" 15 - 330 The following residues NOT assigned to any domain: Chain "H" 15 - 330
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LLC

OXIDOREDUCTASE(CHOH(D)-NAD(A)) 21-NOV-88 :: L-*LACTATE DEHYDROGENASE (E.C.1.1.1.27) COMPLEX WI

DOMAIN 1: 13 to 166 ; DOMAIN 2: 167 to 331 ; The following residues NOT assigned to any domain: Chain " " 332 - 334
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LLD A

PRELIMINARY 08-JUN-92 :: OXIDOREDUCTASE(CHOH (D)-NAD (A))

DOMAIN 1: A 7 to A 151 ; DOMAIN 2: A 152 to A 319 ; The following residues NOT assigned to any domain: Chain "A" 7 - 319
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LLD B

PRELIMINARY 08-JUN-92 :: OXIDOREDUCTASE(CHOH (D)-NAD (A))

DOMAIN 1: B 7 to B 151 ; DOMAIN 2: B 152 to B 319 ; The following residues NOT assigned to any domain: Chain "B" 7 - 319
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

9LDB A

OXIDOREDUCTASE(CHOH(D)-NAD+(A)) 26-NOV-91 :: LACTATE DEHYDROGENASE (E.C.1.1.1.27) COMPLEX WITH

DOMAIN 1: A 1 to A 166 ; DOMAIN 2: A 167 to A 331 ; The following residues NOT assigned to any domain: Chain "A" 0 - 0 The following residues NOT assigned to any domain: Chain "A" 0 - 331
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

9LDB B

OXIDOREDUCTASE(CHOH(D)-NAD+(A)) 26-NOV-91 :: LACTATE DEHYDROGENASE (E.C.1.1.1.27) COMPLEX WITH

DOMAIN 1: B 1 to B 166 ; DOMAIN 2: B 167 to B 331 ; The following residues NOT assigned to any domain: Chain "B" 0 - 331 The following residues NOT assigned to any domain: Chain "B" 0 - 0
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

9LDT A

OXIDOREDUCTASE(CHOH(D)-NAD+(A)) 26-NOV-91 :: LACTATE DEHYDROGENASE (E.C.1.1.1.27) COMPLEX WITH

DOMAIN 1: A 1 to A 166 ; DOMAIN 2: A 167 to A 331 ; The following residues NOT assigned to any domain: Chain "A" 0 - 0 The following residues NOT assigned to any domain: Chain "A" 0 - 331
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

9LDT B

OXIDOREDUCTASE(CHOH(D)-NAD+(A)) 26-NOV-91 :: LACTATE DEHYDROGENASE (E.C.1.1.1.27) COMPLEX WITH

DOMAIN 1: B 1 to B 166 ; DOMAIN 2: B 167 to B 331 ; The following residues NOT assigned to any domain: Chain "B" 0 - 331 The following residues NOT assigned to any domain: Chain "B" 0 - 0
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2LDX

OXIDOREDUCTASE(CHOH(D)-NAD(A)) 25-NOV-87 :: APO-LACTATE DEHYDROGENASE (E.C.1.1.1.27), ISOENZYM

DOMAIN 1: 1 to 163 ; DOMAIN 2: 164 to 331 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5LDH

OXIDOREDUCTASE, CHOH DONOR, NAD ACCEPTR 29-OCT-80 :: LACTATE DEHYDROGENASE H=4= AND S-$LAC-/NAD$==+== C

DOMAIN 1: 1 to 166 ; DOMAIN 2: 167 to 330 B ; The following residues NOT assigned to any domain: Chain " " 0 - 0 Chain " " 331 - 331
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8LDH

OXIDOREDUCTASE(CHOH(D)-NAD(A)) 04-JAN-88 :: M=4= APO-*LACTATE DEHYDROGENASE (E.C.1.1.1.27) COM

DOMAIN 1: 1 to 164 ; DOMAIN 2: 165 to 329 ; The following residues NOT assigned to any domain: Chain " " 0 - 0
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LDM

OXIDOREDUCTASE(CHOH(D)-NAD(A)) 25-NOV-87 :: M=4= LACTATE DEHYDROGENASE (E.C.1.1.1.27) TERNARY

DOMAIN 1: 1 to 164 ; DOMAIN 2: 165 to 329 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3LDH

OXIDOREDUCTASE, CHOH DONOR, NAD ACCEPTR 06-JUN-74 :: LACTATE DEHYDROGENASE (E.C.1.1.1.27) M4 ENZYME,

DOMAIN 1: 1 to 166 ; DOMAIN 2: 167 to 331 ; The following residues NOT assigned to any domain: Chain " " 0 - 0
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MAP

AMINOTRANSFERASE 10-SEP-93 :: ASPARTATE AMINOTRANSFERASE (MASPAT) (E.C.2.6.1.1)

DOMAIN 1: [Assigned by homology with 7AATA] 3 to 46 ; 325 to 409 ; DOMAIN 2: [Assigned by homology with 7AATA] 47 to 324 ; The following residues NOT assigned to any domain: Chain " " 410 - 410
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MAQ

AMINOTRANSFERASE 10-SEP-93 :: ASPARTATE AMINOTRANSFERASE (MASPAT) (E.C.2.6.1.1)

DOMAIN 1: [Assigned by homology with 7AATA] 3 to 46 ; 325 to 409 ; DOMAIN 2: [Assigned by homology with 7AATA] 47 to 324 ; The following residues NOT assigned to any domain: Chain " " 410 - 410
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7AAT B

TRANSFERASE(AMINOTRANSFERASE) 02-DEC-91 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) COMPLEX W

DOMAIN 1: [Assigned by homology with 7AATA]B 3 to B 46 ; B 325 to B 409 ; DOMAIN 2: [Assigned by homology with 7AATA]B 47 to B 324 ; The following residues NOT assigned to any domain: Chain "B" 3 - 410 The following residues NOT assigned to any domain: Chain "B" 410 - 410
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TAR A

AMINOTRANSFERASE 04-OCT-93 :: ASPARTATE AMINOTRANSFERASE (MASPAT) (E.C.2.6.1.1)

DOMAIN 1: [Assigned by homology with 7AATA]A 3 to A 46 ; A 325 to A 409 ; DOMAIN 2: [Assigned by homology with 7AATA]A 47 to A 324 ; The following residues NOT assigned to any domain: Chain "A" 410 - 410 The following residues NOT assigned to any domain: Chain "A" 3 - 410
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TAR B

AMINOTRANSFERASE 04-OCT-93 :: ASPARTATE AMINOTRANSFERASE (MASPAT) (E.C.2.6.1.1)

DOMAIN 1: [Assigned by homology with 7AATA]B 3 to B 46 ; B 325 to B 409 ; DOMAIN 2: [Assigned by homology with 7AATA]B 47 to B 324 ; The following residues NOT assigned to any domain: Chain "B" 3 - 410 The following residues NOT assigned to any domain: Chain "B" 410 - 410
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TAS A

AMINOTRANSFERASE 04-OCT-93 :: ASPARTATE AMINOTRANSFERASE (MASPAT) (E.C.2.6.1.1)

DOMAIN 1: [Assigned by homology with 7AATA]A 3 to A 46 ; A 325 to A 409 ; DOMAIN 2: [Assigned by homology with 7AATA]A 47 to A 324 ; The following residues NOT assigned to any domain: Chain "A" 410 - 410 The following residues NOT assigned to any domain: Chain "A" 3 - 410
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TAS B

AMINOTRANSFERASE 04-OCT-93 :: ASPARTATE AMINOTRANSFERASE (MASPAT) (E.C.2.6.1.1)

DOMAIN 1: [Assigned by homology with 7AATA]B 3 to B 46 ; B 325 to B 409 ; DOMAIN 2: [Assigned by homology with 7AATA]B 47 to B 324 ; The following residues NOT assigned to any domain: Chain "B" 3 - 410 The following residues NOT assigned to any domain: Chain "B" 410 - 410
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TAT A

AMINOTRANSFERASE 04-OCT-93 :: ASPARTATE AMINOTRANSFERASE (MASPAT) (E.C.2.6.1.1)

DOMAIN 1: [Assigned by homology with 7AATA]A 3 to A 46 ; A 325 to A 409 ; DOMAIN 2: [Assigned by homology with 7AATA]A 47 to A 324 ; The following residues NOT assigned to any domain: Chain "A" 410 - 410 The following residues NOT assigned to any domain: Chain "A" 3 - 410
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TAT B

AMINOTRANSFERASE 04-OCT-93 :: ASPARTATE AMINOTRANSFERASE (MASPAT) (E.C.2.6.1.1)

DOMAIN 1: [Assigned by homology with 7AATA]B 3 to B 46 ; B 325 to B 409 ; DOMAIN 2: [Assigned by homology with 7AATA]B 47 to B 324 ; The following residues NOT assigned to any domain: Chain "B" 3 - 410 The following residues NOT assigned to any domain: Chain "B" 410 - 410
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AMA

TRANSFERASE(AMINOTRANSFERASE) 05-FEB-92 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) COMPLEX W

DOMAIN 1: [Assigned by homology with 7AATA] 3 to 46 ; 325 to 409 ; DOMAIN 2: [Assigned by homology with 7AATA] 47 to 324 ; The following residues NOT assigned to any domain: Chain " " 410 - 410
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8AAT A

TRANSFERASE(AMINOTRANSFERASE) 02-DEC-91 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) COMPLEX W

DOMAIN 1: [Assigned by homology with 7AATA]A 3 to A 46 ; A 325 to A 409 ; DOMAIN 2: [Assigned by homology with 7AATA]A 47 to A 324 ; The following residues NOT assigned to any domain: Chain "A" 410 - 410 The following residues NOT assigned to any domain: Chain "A" 3 - 410
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8AAT B

TRANSFERASE(AMINOTRANSFERASE) 02-DEC-91 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) COMPLEX W

DOMAIN 1: [Assigned by homology with 7AATA]B 3 to B 46 ; B 325 to B 409 ; DOMAIN 2: [Assigned by homology with 7AATA]B 47 to B 324 ; The following residues NOT assigned to any domain: Chain "B" 3 - 410 The following residues NOT assigned to any domain: Chain "B" 410 - 410
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

9AAT A

TRANSFERASE(AMINOTRANSFERASE) 02-DEC-91 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) COMPLEX W

DOMAIN 1: [Assigned by homology with 7AATA]A 3 to A 46 ; A 325 to A 409 ; DOMAIN 2: [Assigned by homology with 7AATA]A 47 to A 324 ; The following residues NOT assigned to any domain: Chain "A" 410 - 410 The following residues NOT assigned to any domain: Chain "A" 3 - 410
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

9AAT B

TRANSFERASE(AMINOTRANSFERASE) 02-DEC-91 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) COMPLEX W

DOMAIN 1: [Assigned by homology with 7AATA]B 3 to B 46 ; B 325 to B 409 ; DOMAIN 2: [Assigned by homology with 7AATA]B 47 to B 324 ; The following residues NOT assigned to any domain: Chain "B" 3 - 410 The following residues NOT assigned to any domain: Chain "B" 410 - 410
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AKA A

TRANSFERASE(AMINOTRANSFERASE) 28-FEB-94 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) MUTANT WI

DOMAIN 1: [Assigned by homology with 7AATA]A 3 to A 46 ; A 325 to A 409 ; DOMAIN 2: [Assigned by homology with 7AATA]A 47 to A 324 ; The following residues NOT assigned to any domain: Chain "A" 410 - 410 The following residues NOT assigned to any domain: Chain "A" 3 - 410
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AKA B

TRANSFERASE(AMINOTRANSFERASE) 28-FEB-94 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) MUTANT WI

DOMAIN 1: [Assigned by homology with 7AATA]B 3 to B 46 ; B 325 to B 409 ; DOMAIN 2: [Assigned by homology with 7AATA]B 47 to B 324 ; The following residues NOT assigned to any domain: Chain "B" 3 - 410 The following residues NOT assigned to any domain: Chain "B" 410 - 410
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AKB A

TRANSFERASE(AMINOTRANSFERASE) 28-FEB-94 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) MUTANT WI

DOMAIN 1: [Assigned by homology with 7AATA]A 3 to A 46 ; A 325 to A 409 ; DOMAIN 2: [Assigned by homology with 7AATA]A 47 to A 324 ; The following residues NOT assigned to any domain: Chain "A" 410 - 410
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AKC A

TRANSFERASE(AMINOTRANSFERASE) 28-FEB-94 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) MUTANT WI

DOMAIN 1: [Assigned by homology with 7AATA]A 3 to A 46 ; A 325 to A 409 ; DOMAIN 2: [Assigned by homology with 7AATA]A 47 to A 324 ; The following residues NOT assigned to any domain: Chain "A" 410 - 410
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CST A

TRANSFERASE(AMINOTRANSFERASE) 06-SEP-94 :: ASPARTATE AMINOTRANSFERASE (CASPAT) (E.C.2.6.1.1)

DOMAIN 1: [Assigned by homology with 7AATA]A 2 to A 46 ; A 325 to A 409 ; DOMAIN 2: [Assigned by homology with 7AATA]A 47 to A 324 ; The following residues NOT assigned to any domain: Chain "A" 410 - 412 The following residues NOT assigned to any domain: Chain "A" 2 - 412
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CST B

TRANSFERASE(AMINOTRANSFERASE) 06-SEP-94 :: ASPARTATE AMINOTRANSFERASE (CASPAT) (E.C.2.6.1.1)

DOMAIN 1: [Assigned by homology with 7AATA]B 2 to B 46 ; B 325 to B 409 ; DOMAIN 2: [Assigned by homology with 7AATA]B 47 to B 324 ; The following residues NOT assigned to any domain: Chain "B" 2 - 412 The following residues NOT assigned to any domain: Chain "B" 410 - 412
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AAT

AMINOTRANSFERASE 23-APR-82 :: CYTOSOLIC ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1)

DOMAIN 1: [Assigned by homology with 7AATA] 2 to 46 ; 325 to 409 ; DOMAIN 2: [Assigned by homology with 7AATA] 47 to 324 ; The following residues NOT assigned to any domain: Chain " " 410 - 412
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2AAT

TRANSFERASE(AMINOTRANSFERASE) 30-MAY-89 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) MUTANT K2

DOMAIN 1: [Assigned by homology with 7AATA] 13 to 54 ; 325 to 408 ; DOMAIN 2: [Assigned by homology with 7AATA] 55 to 324 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AAM

AMINOTRANSFERASE 13-JUL-93 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) MUTANT WI

DOMAIN 1: [Assigned by homology with 7AATA] 13 to 54 ; 325 to 408 ; DOMAIN 2: [Assigned by homology with 7AATA] 55 to 324 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AAW

AMINOTRANSFERASE 13-JUL-93 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) WILD TYPE

DOMAIN 1: [Assigned by homology with 7AATA] 13 to 54 ; 325 to 408 ; DOMAIN 2: [Assigned by homology with 7AATA] 55 to 324 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1SPA

TRANSFERASE(AMINOTRANSFERASE) 26-JAN-93 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) MUTANT WI

DOMAIN 1: [Assigned by homology with 7AATA] 5 to 46 ; 325 to 409 ; DOMAIN 2: [Assigned by homology with 7AATA] 47 to 324 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3AAT

TRANSFERASE(AMINOTRANSFERASE) 06-DEC-90 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) (MUTANT W

DOMAIN 1: [Assigned by homology with 7AATA] 5 to 46 ; 325 to 409 ; DOMAIN 2: [Assigned by homology with 7AATA] 47 to 324 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AIA A

TRANSFERASE(AMINOTRANSFERASE) 10-MAY-94 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) (HOLO FOR

DOMAIN 1: [Assigned by homology with 7AATA]A 5 to A 46 ; A 325 to A 409 ; DOMAIN 2: [Assigned by homology with 7AATA]A 47 to A 324 ; The following residues NOT assigned to any domain: Chain "A" 5 - 409
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AIA B

TRANSFERASE(AMINOTRANSFERASE) 10-MAY-94 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) (HOLO FOR

DOMAIN 1: [Assigned by homology with 7AATA]B 5 to B 46 ; B 325 to B 409 ; DOMAIN 2: [Assigned by homology with 7AATA]B 47 to B 324 ; The following residues NOT assigned to any domain: Chain "B" 5 - 409
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AIB A

TRANSFERASE(AMINOTRANSFERASE) 10-MAY-94 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) MUTANT WI

DOMAIN 1: [Assigned by homology with 7AATA]A 5 to A 46 ; A 325 to A 409 ; DOMAIN 2: [Assigned by homology with 7AATA]A 47 to A 324 ; The following residues NOT assigned to any domain: Chain "A" 5 - 409
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AIB B

TRANSFERASE(AMINOTRANSFERASE) 10-MAY-94 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) MUTANT WI

DOMAIN 1: [Assigned by homology with 7AATA]B 5 to B 46 ; B 325 to B 409 ; DOMAIN 2: [Assigned by homology with 7AATA]B 47 to B 324 ; The following residues NOT assigned to any domain: Chain "B" 5 - 409
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AIC A

TRANSFERASE(AMINOTRANSFERASE) 10-MAY-94 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) MUTANT WI

DOMAIN 1: [Assigned by homology with 7AATA]A 5 to A 46 ; A 325 to A 409 ; DOMAIN 2: [Assigned by homology with 7AATA]A 47 to A 324 ; The following residues NOT assigned to any domain: Chain "A" 5 - 409
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AIC B

TRANSFERASE(AMINOTRANSFERASE) 10-MAY-94 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) MUTANT WI

DOMAIN 1: [Assigned by homology with 7AATA]B 5 to B 46 ; B 325 to B 409 ; DOMAIN 2: [Assigned by homology with 7AATA]B 47 to B 324 ; The following residues NOT assigned to any domain: Chain "B" 5 - 409
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AMQ

TRANSFERASE(AMINOTRANSFERASE) 01-JUL-94 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) COMPLEXED

DOMAIN 1: [Assigned by homology with 7AATA] 5 to 46 ; 325 to 409 ; DOMAIN 2: [Assigned by homology with 7AATA] 47 to 324 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AMR

TRANSFERASE(AMINOTRANSFERASE) 01-JUL-94 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) COMPLEXED

DOMAIN 1: [Assigned by homology with 7AATA] 5 to 46 ; 325 to 409 ; DOMAIN 2: [Assigned by homology with 7AATA] 47 to 324 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AMS

TRANSFERASE(AMINOTRANSFERASE) 01-JUL-94 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) COMPLEXED

DOMAIN 1: [Assigned by homology with 7AATA] 5 to 46 ; 325 to 409 ; DOMAIN 2: [Assigned by homology with 7AATA] 47 to 324 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ARS

TRANSFERASE(AMINOTRANSFERASE) 02-AUG-93 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) COMPLEXED

DOMAIN 1: [Assigned by homology with 7AATA] 5 to 46 ; 325 to 409 ; DOMAIN 2: [Assigned by homology with 7AATA] 47 to 324 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ASA

AMINOTRANSFERASE 27-AUG-93 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) WILD TYPE

DOMAIN 1: [Assigned by homology with 7AATA] 13 to 54 ; 325 to 408 ; DOMAIN 2: [Assigned by homology with 7AATA] 55 to 324 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ASB

AMINOTRANSFERASE 27-AUG-93 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) MUTANT WI

DOMAIN 1: [Assigned by homology with 7AATA] 13 to 54 ; 325 to 408 ; DOMAIN 2: [Assigned by homology with 7AATA] 55 to 324 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ASC

AMINOTRANSFERASE 27-AUG-93 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) MUTANT WI

DOMAIN 1: [Assigned by homology with 7AATA] 13 to 54 ; 325 to 408 ; DOMAIN 2: [Assigned by homology with 7AATA] 55 to 324 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ASD

AMINOTRANSFERASE 27-AUG-93 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) WILD TYPE

DOMAIN 1: [Assigned by homology with 7AATA] 13 to 54 ; 325 to 408 ; DOMAIN 2: [Assigned by homology with 7AATA] 55 to 324 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ASE

AMINOTRANSFERASE 27-AUG-93 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) WILD TYPE

DOMAIN 1: [Assigned by homology with 7AATA] 13 to 54 ; 325 to 408 ; DOMAIN 2: [Assigned by homology with 7AATA] 55 to 324 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ASF

AMINOTRANSFERASE 27-AUG-93 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) MUTANT WI

DOMAIN 1: [Assigned by homology with 7AATA] 13 to 54 ; 325 to 408 ; DOMAIN 2: [Assigned by homology with 7AATA] 55 to 324 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ASG

AMINOTRANSFERASE 27-AUG-93 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) MUTANT WI

DOMAIN 1: [Assigned by homology with 7AATA] 13 to 54 ; 325 to 408 ; DOMAIN 2: [Assigned by homology with 7AATA] 55 to 324 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ASL A

AMINOTRANSFERASE 16-SEP-93 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) (WILD TYP

DOMAIN 1: [Assigned by homology with 7AATA]A 5 to A 46 ; A 325 to A 409 ; DOMAIN 2: [Assigned by homology with 7AATA]A 47 to A 324 ; The following residues NOT assigned to any domain: Chain "A" 5 - 409
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ASL B

AMINOTRANSFERASE 16-SEP-93 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) (WILD TYP

DOMAIN 1: [Assigned by homology with 7AATA]B 5 to B 46 ; B 325 to B 409 ; DOMAIN 2: [Assigned by homology with 7AATA]B 47 to B 324 ; The following residues NOT assigned to any domain: Chain "B" 5 - 409
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ASM A

AMINOTRANSFERASE 16-SEP-93 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) (WILD TYP

DOMAIN 1: [Assigned by homology with 7AATA]A 5 to A 46 ; A 325 to A 409 ; DOMAIN 2: [Assigned by homology with 7AATA]A 47 to A 324 ; The following residues NOT assigned to any domain: Chain "A" 5 - 409
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ASM B

AMINOTRANSFERASE 16-SEP-93 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) (WILD TYP

DOMAIN 1: [Assigned by homology with 7AATA]B 5 to B 46 ; B 325 to B 409 ; DOMAIN 2: [Assigned by homology with 7AATA]B 47 to B 324 ; The following residues NOT assigned to any domain: Chain "B" 5 - 409
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ASN A

AMINOTRANSFERASE 16-SEP-93 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) (WILD TYP

DOMAIN 1: [Assigned by homology with 7AATA]A 5 to A 46 ; A 325 to A 409 ; DOMAIN 2: [Assigned by homology with 7AATA]A 47 to A 324 ; The following residues NOT assigned to any domain: Chain "A" 5 - 409
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ASN B

AMINOTRANSFERASE 16-SEP-93 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) (WILD TYP

DOMAIN 1: [Assigned by homology with 7AATA]B 5 to B 46 ; B 325 to B 409 ; DOMAIN 2: [Assigned by homology with 7AATA]B 47 to B 324 ; The following residues NOT assigned to any domain: Chain "B" 5 - 409
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ART

TRANSFERASE(AMINOTRANSFERASE) 02-AUG-93 :: ASPARTATE AMINOTRANSFERASE (E.C.2.6.1.1) COMPLEXED

DOMAIN 1: [Assigned by homology with 7AATA] 5 to 46 ; 325 to 414 ; DOMAIN 2: [Assigned by homology with 7AATA] 47 to 324 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BAP

BINDING PROTEINS 15-NOV-91 :: L-*ARABINOSE-BINDING PROTEIN (MUTANT WITH PRO 254

DOMAIN 1: 2 to 109 ; 255 to 284 ; DOMAIN 2: 110 to 254 ; 285 to 306 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1APB

BINDING PROTEINS 15-NOV-91 :: L-*ARABINOSE-BINDING PROTEIN (MUTANT WITH PRO 254

DOMAIN 1: 2 to 109 ; 255 to 284 ; DOMAIN 2: 110 to 254 ; 285 to 306 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

9ABP

BINDING PROTEINS 15-NOV-91 :: L-*ARABINOSE-BINDING PROTEIN (MUTANT WITH PRO 254

DOMAIN 1: 2 to 109 ; 255 to 284 ; DOMAIN 2: 110 to 254 ; 285 to 306 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5ABP

BINDING PROTEIN 26-DEC-90 :: L-ARABINOSE-BINDING PROTEIN COMPLEX WITH D-GALACTO

DOMAIN 1: 2 to 109 ; 255 to 284 ; DOMAIN 2: 110 to 254 ; 285 to 306 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ABE

BINDING PROTEIN 23-APR-92 :: L-ARABINOSE-BINDING PROTEIN COMPLEX WITH L-ARABINO

DOMAIN 1: 2 to 109 ; 255 to 284 ; DOMAIN 2: 110 to 254 ; 285 to 306 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ABF

BINDING PROTEIN 23-APR-92 :: L-ARABINOSE-BINDING PROTEIN COMPLEX WITH D-FUCOSE

DOMAIN 1: 2 to 109 ; 255 to 284 ; DOMAIN 2: 110 to 254 ; 285 to 306 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6ABP

BINDING PROTEINS 25-APR-91 :: L-*ARABINOSE-BINDING PROTEIN (MUTANT WITH MET 108

DOMAIN 1: 2 to 109 ; 255 to 284 ; DOMAIN 2: 110 to 254 ; 285 to 306 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7ABP

BINDING PROTEINS 25-APR-91 :: L-*ARABINOSE-BINDING PROTEIN (MUTANT WITH MET 108

DOMAIN 1: 2 to 109 ; 255 to 284 ; DOMAIN 2: 110 to 254 ; 285 to 306 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4AT1 A

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 26-APR-90 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCA]A 1 to A 137 ; A 288 to A 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]A 144 to A 283 ; The following residues NOT assigned to any domain: Chain "A" 138 - 143 Chain "A" 284 - 287 The following residues NOT assigned to any domain: Chain "A" 8 - 153 The following residues NOT assigned to any domain: Chain "A" 1 - 310 The following residues NOT assigned to any domain: Chain "A" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4AT1 C

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 26-APR-90 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCA]C 1 to C 137 ; C 288 to C 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]C 144 to C 283 ; The following residues NOT assigned to any domain: Chain "C" 1 - 310 The following residues NOT assigned to any domain: Chain "C" 8 - 153 The following residues NOT assigned to any domain: Chain "C" 138 - 143 Chain "C" 284 - 287 The following residues NOT assigned to any domain: Chain "C" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5AT1 A

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 26-APR-90 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCA]A 1 to A 137 ; A 288 to A 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]A 144 to A 283 ; The following residues NOT assigned to any domain: Chain "A" 138 - 143 Chain "A" 284 - 287 The following residues NOT assigned to any domain: Chain "A" 8 - 153 The following residues NOT assigned to any domain: Chain "A" 1 - 310 The following residues NOT assigned to any domain: Chain "A" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5AT1 C

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 26-APR-90 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCA]C 1 to C 137 ; C 288 to C 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]C 144 to C 283 ; The following residues NOT assigned to any domain: Chain "C" 1 - 310 The following residues NOT assigned to any domain: Chain "C" 8 - 153 The following residues NOT assigned to any domain: Chain "C" 138 - 143 Chain "C" 284 - 287 The following residues NOT assigned to any domain: Chain "C" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2AT1 A

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 22-SEP-89 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCA]A 1 to A 137 ; A 288 to A 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]A 144 to A 283 ; The following residues NOT assigned to any domain: Chain "A" 138 - 143 Chain "A" 284 - 287 The following residues NOT assigned to any domain: Chain "A" 8 - 153 The following residues NOT assigned to any domain: Chain "A" 1 - 310 The following residues NOT assigned to any domain: Chain "A" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2AT1 C

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 22-SEP-89 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCA]C 1 to C 137 ; C 288 to C 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]C 144 to C 283 ; The following residues NOT assigned to any domain: Chain "C" 1 - 310 The following residues NOT assigned to any domain: Chain "C" 8 - 153 The following residues NOT assigned to any domain: Chain "C" 138 - 143 Chain "C" 284 - 287 The following residues NOT assigned to any domain: Chain "C" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6AT1 A

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 26-APR-90 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCA]A 1 to A 137 ; A 288 to A 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]A 144 to A 283 ; The following residues NOT assigned to any domain: Chain "A" 138 - 143 Chain "A" 284 - 287 The following residues NOT assigned to any domain: Chain "A" 8 - 153 The following residues NOT assigned to any domain: Chain "A" 1 - 310 The following residues NOT assigned to any domain: Chain "A" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6AT1 C

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 26-APR-90 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCA]C 1 to C 137 ; C 288 to C 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]C 144 to C 283 ; The following residues NOT assigned to any domain: Chain "C" 1 - 310 The following residues NOT assigned to any domain: Chain "C" 8 - 153 The following residues NOT assigned to any domain: Chain "C" 138 - 143 Chain "C" 284 - 287 The following residues NOT assigned to any domain: Chain "C" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3AT1 A

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 22-SEP-89 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCA]A 1 to A 137 ; A 288 to A 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]A 144 to A 283 ; The following residues NOT assigned to any domain: Chain "A" 138 - 143 Chain "A" 284 - 287 The following residues NOT assigned to any domain: Chain "A" 8 - 153 The following residues NOT assigned to any domain: Chain "A" 1 - 310 The following residues NOT assigned to any domain: Chain "A" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3AT1 C

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 22-SEP-89 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCA]C 1 to C 137 ; C 288 to C 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]C 144 to C 283 ; The following residues NOT assigned to any domain: Chain "C" 1 - 310 The following residues NOT assigned to any domain: Chain "C" 8 - 153 The following residues NOT assigned to any domain: Chain "C" 138 - 143 Chain "C" 284 - 287 The following residues NOT assigned to any domain: Chain "C" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7AT1 A

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 22-SEP-89 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCA]A 1 to A 137 ; A 288 to A 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]A 144 to A 283 ; The following residues NOT assigned to any domain: Chain "A" 138 - 143 Chain "A" 284 - 287 The following residues NOT assigned to any domain: Chain "A" 8 - 153 The following residues NOT assigned to any domain: Chain "A" 1 - 310 The following residues NOT assigned to any domain: Chain "A" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7AT1 C

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 22-SEP-89 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCA]C 1 to C 137 ; C 288 to C 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]C 144 to C 283 ; The following residues NOT assigned to any domain: Chain "C" 1 - 310 The following residues NOT assigned to any domain: Chain "C" 8 - 153 The following residues NOT assigned to any domain: Chain "C" 138 - 143 Chain "C" 284 - 287 The following residues NOT assigned to any domain: Chain "C" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8AT1 A

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 22-SEP-89 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCA]A 1 to A 137 ; A 288 to A 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]A 144 to A 283 ; The following residues NOT assigned to any domain: Chain "A" 138 - 143 Chain "A" 284 - 287 The following residues NOT assigned to any domain: Chain "A" 8 - 153 The following residues NOT assigned to any domain: Chain "A" 1 - 310 The following residues NOT assigned to any domain: Chain "A" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8AT1 C

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 22-SEP-89 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCA]C 1 to C 137 ; C 288 to C 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]C 144 to C 283 ; The following residues NOT assigned to any domain: Chain "C" 1 - 310 The following residues NOT assigned to any domain: Chain "C" 8 - 153 The following residues NOT assigned to any domain: Chain "C" 138 - 143 Chain "C" 284 - 287 The following residues NOT assigned to any domain: Chain "C" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8ATC C

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 25-AUG-89 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCA]C 1 to C 137 ; C 288 to C 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]C 144 to C 283 ; The following residues NOT assigned to any domain: Chain "C" 1 - 310 The following residues NOT assigned to any domain: Chain "C" 8 - 153 The following residues NOT assigned to any domain: Chain "C" 138 - 143 Chain "C" 284 - 287 The following residues NOT assigned to any domain: Chain "C" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AT1 A

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 22-SEP-89 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCA]A 1 to A 137 ; A 288 to A 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]A 144 to A 283 ; The following residues NOT assigned to any domain: Chain "A" 138 - 143 Chain "A" 284 - 287 The following residues NOT assigned to any domain: Chain "A" 8 - 153 The following residues NOT assigned to any domain: Chain "A" 1 - 310 The following residues NOT assigned to any domain: Chain "A" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AT1 C

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 22-SEP-89 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCA]C 1 to C 137 ; C 288 to C 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]C 144 to C 283 ; The following residues NOT assigned to any domain: Chain "C" 1 - 310 The following residues NOT assigned to any domain: Chain "C" 8 - 153 The following residues NOT assigned to any domain: Chain "C" 138 - 143 Chain "C" 284 - 287 The following residues NOT assigned to any domain: Chain "C" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ACM A

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 08-JUL-92 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCA]A 1 to A 137 ; A 288 to A 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]A 144 to A 283 ; The following residues NOT assigned to any domain: Chain "A" 138 - 143 Chain "A" 284 - 287 The following residues NOT assigned to any domain: Chain "A" 8 - 153 The following residues NOT assigned to any domain: Chain "A" 1 - 310 The following residues NOT assigned to any domain: Chain "A" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ACM C

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 08-JUL-92 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCA]C 1 to C 137 ; C 288 to C 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]C 144 to C 283 ; The following residues NOT assigned to any domain: Chain "C" 1 - 310 The following residues NOT assigned to any domain: Chain "C" 8 - 153 The following residues NOT assigned to any domain: Chain "C" 138 - 143 Chain "C" 284 - 287 The following residues NOT assigned to any domain: Chain "C" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAA A

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCA]A 1 to A 137 ; A 288 to A 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]A 144 to A 283 ; The following residues NOT assigned to any domain: Chain "A" 138 - 143 Chain "A" 284 - 287 The following residues NOT assigned to any domain: Chain "A" 1 - 153 The following residues NOT assigned to any domain: Chain "A" 1 - 310 The following residues NOT assigned to any domain: Chain "A" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAA C

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCA]C 1 to C 137 ; C 288 to C 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]C 144 to C 283 ; The following residues NOT assigned to any domain: Chain "C" 1 - 310 The following residues NOT assigned to any domain: Chain "C" 1 - 153 The following residues NOT assigned to any domain: Chain "C" 138 - 143 Chain "C" 284 - 287 The following residues NOT assigned to any domain: Chain "C" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAB A

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCA]A 1 to A 137 ; A 288 to A 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]A 144 to A 283 ; The following residues NOT assigned to any domain: Chain "A" 138 - 143 Chain "A" 284 - 287 The following residues NOT assigned to any domain: Chain "A" 1 - 153 The following residues NOT assigned to any domain: Chain "A" 1 - 310 The following residues NOT assigned to any domain: Chain "A" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAB C

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCA]C 1 to C 137 ; C 288 to C 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]C 144 to C 283 ; The following residues NOT assigned to any domain: Chain "C" 1 - 310 The following residues NOT assigned to any domain: Chain "C" 1 - 153 The following residues NOT assigned to any domain: Chain "C" 138 - 143 Chain "C" 284 - 287 The following residues NOT assigned to any domain: Chain "C" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAC A

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCA]A 1 to A 137 ; A 288 to A 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]A 144 to A 283 ; The following residues NOT assigned to any domain: Chain "A" 138 - 143 Chain "A" 284 - 287 The following residues NOT assigned to any domain: Chain "A" 1 - 153 The following residues NOT assigned to any domain: Chain "A" 1 - 310 The following residues NOT assigned to any domain: Chain "A" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAC C

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCA]C 1 to C 137 ; C 288 to C 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]C 144 to C 283 ; The following residues NOT assigned to any domain: Chain "C" 1 - 310 The following residues NOT assigned to any domain: Chain "C" 1 - 153 The following residues NOT assigned to any domain: Chain "C" 138 - 143 Chain "C" 284 - 287 The following residues NOT assigned to any domain: Chain "C" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAD A

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCA]A 1 to A 137 ; A 288 to A 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]A 144 to A 283 ; The following residues NOT assigned to any domain: Chain "A" 138 - 143 Chain "A" 284 - 287 The following residues NOT assigned to any domain: Chain "A" 1 - 153 The following residues NOT assigned to any domain: Chain "A" 1 - 310 The following residues NOT assigned to any domain: Chain "A" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAD C

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCA]C 1 to C 137 ; C 288 to C 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]C 144 to C 283 ; The following residues NOT assigned to any domain: Chain "C" 1 - 310 The following residues NOT assigned to any domain: Chain "C" 1 - 153 The following residues NOT assigned to any domain: Chain "C" 138 - 143 Chain "C" 284 - 287 The following residues NOT assigned to any domain: Chain "C" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAE A

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCA]A 1 to A 137 ; A 288 to A 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]A 144 to A 283 ; The following residues NOT assigned to any domain: Chain " " 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAE C

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCA]C 1 to C 137 ; C 288 to C 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]C 144 to C 283 ; The following residues NOT assigned to any domain: Chain " " 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAF A

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCA]A 1 to A 137 ; A 288 to A 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]A 144 to A 283 ; The following residues NOT assigned to any domain: Chain "A" 138 - 143 Chain "A" 284 - 287 The following residues NOT assigned to any domain: Chain "A" 1 - 153 The following residues NOT assigned to any domain: Chain "A" 1 - 310 The following residues NOT assigned to any domain: Chain "A" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAF C

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCA]C 1 to C 137 ; C 288 to C 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]C 144 to C 283 ; The following residues NOT assigned to any domain: Chain "C" 1 - 310 The following residues NOT assigned to any domain: Chain "C" 1 - 153 The following residues NOT assigned to any domain: Chain "C" 138 - 143 Chain "C" 284 - 287 The following residues NOT assigned to any domain: Chain "C" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAG A

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCA]A 1 to A 137 ; A 288 to A 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]A 144 to A 283 ; The following residues NOT assigned to any domain: Chain "A" 138 - 143 Chain "A" 284 - 287 The following residues NOT assigned to any domain: Chain "A" 1 - 153 The following residues NOT assigned to any domain: Chain "A" 1 - 310 The following residues NOT assigned to any domain: Chain "A" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAG C

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCA]C 1 to C 137 ; C 288 to C 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]C 144 to C 283 ; The following residues NOT assigned to any domain: Chain "C" 1 - 310 The following residues NOT assigned to any domain: Chain "C" 1 - 153 The following residues NOT assigned to any domain: Chain "C" 138 - 143 Chain "C" 284 - 287 The following residues NOT assigned to any domain: Chain "C" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAH A

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCA]A 1 to A 137 ; A 288 to A 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]A 144 to A 283 ; The following residues NOT assigned to any domain: Chain "A" 138 - 143 Chain "A" 284 - 287 The following residues NOT assigned to any domain: Chain "A" 1 - 153 The following residues NOT assigned to any domain: Chain "A" 1 - 310 The following residues NOT assigned to any domain: Chain "A" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAH C

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCA]C 1 to C 137 ; C 288 to C 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]C 144 to C 283 ; The following residues NOT assigned to any domain: Chain "C" 1 - 310 The following residues NOT assigned to any domain: Chain "C" 1 - 153 The following residues NOT assigned to any domain: Chain "C" 138 - 143 Chain "C" 284 - 287 The following residues NOT assigned to any domain: Chain "C" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAI A

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCA]A 1 to A 137 ; A 288 to A 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]A 144 to A 283 ; The following residues NOT assigned to any domain: Chain "A" 138 - 143 Chain "A" 284 - 287 The following residues NOT assigned to any domain: Chain "A" 1 - 153 The following residues NOT assigned to any domain: Chain "A" 1 - 310 The following residues NOT assigned to any domain: Chain "A" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAI C

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCA]C 1 to C 137 ; C 288 to C 310 ; DOMAIN 2: [Assigned by homology with 8ATCA]C 144 to C 283 ; The following residues NOT assigned to any domain: Chain "C" 1 - 310 The following residues NOT assigned to any domain: Chain "C" 1 - 153 The following residues NOT assigned to any domain: Chain "C" 138 - 143 Chain "C" 284 - 287 The following residues NOT assigned to any domain: Chain "C" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2ATC A

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 24-MAR-82 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCA]A 1 to A 137 ; A 283 to A 305 ; DOMAIN 2: [Assigned by homology with 8ATCA]A 144 to A 278 ; The following residues NOT assigned to any domain: Chain "A" 138 - 143 Chain "A" 279 - 282 The following residues NOT assigned to any domain: Chain "A" 1 - 152
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2AT2 A

PRELIMINARY 20-JUL-92 :: ASPARTATE TRANSCARBAMOYLASE (E.C.2.1.3.2) (ASPARTA

DOMAIN 1: [Assigned by homology with 8ATCA]A 1 to A 130 ; A 273 to A 295 ; DOMAIN 2: [Assigned by homology with 8ATCA]A 137 to A 268 ; The following residues NOT assigned to any domain: Chain "A" 131 - 136 Chain "A" 269 - 272 The following residues NOT assigned to any domain: Chain "A" 1 - 295 The following residues NOT assigned to any domain: Chain "A" 1 - 295
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2AT2 B

PRELIMINARY 20-JUL-92 :: ASPARTATE TRANSCARBAMOYLASE (E.C.2.1.3.2) (ASPARTA

DOMAIN 1: [Assigned by homology with 8ATCA]B 1 to B 130 ; B 273 to B 295 ; DOMAIN 2: [Assigned by homology with 8ATCA]B 137 to B 268 ; The following residues NOT assigned to any domain: Chain "B" 1 - 295 The following residues NOT assigned to any domain: Chain "B" 131 - 136 Chain "B" 269 - 272 The following residues NOT assigned to any domain: Chain "B" 1 - 295
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2AT2 C

PRELIMINARY 20-JUL-92 :: ASPARTATE TRANSCARBAMOYLASE (E.C.2.1.3.2) (ASPARTA

DOMAIN 1: [Assigned by homology with 8ATCA]C 1 to C 130 ; C 273 to C 295 ; DOMAIN 2: [Assigned by homology with 8ATCA]C 137 to C 268 ; The following residues NOT assigned to any domain: Chain "C" 1 - 295 The following residues NOT assigned to any domain: Chain "C" 1 - 295 The following residues NOT assigned to any domain: Chain "C" 131 - 136 Chain "C" 269 - 272
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4AT1 B

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 26-APR-90 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCB]B 8 to B 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]B 100 to B 151 ; The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 97 - 99 Chain "B" 152 - 153 The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4AT1 D

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 26-APR-90 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCB]D 8 to D 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]D 100 to D 151 ; The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 8 - 153 The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 97 - 99 Chain "D" 152 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5AT1 B

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 26-APR-90 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCB]B 8 to B 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]B 100 to B 151 ; The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 97 - 99 Chain "B" 152 - 153 The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5AT1 D

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 26-APR-90 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCB]D 8 to D 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]D 100 to D 151 ; The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 8 - 153 The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 97 - 99 Chain "D" 152 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2AT1 B

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 22-SEP-89 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCB]B 8 to B 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]B 100 to B 151 ; The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 97 - 99 Chain "B" 152 - 153 The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2AT1 D

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 22-SEP-89 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCB]D 8 to D 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]D 100 to D 151 ; The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 8 - 153 The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 97 - 99 Chain "D" 152 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6AT1 B

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 26-APR-90 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCB]B 8 to B 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]B 100 to B 151 ; The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 97 - 99 Chain "B" 152 - 153 The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6AT1 D

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 26-APR-90 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCB]D 8 to D 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]D 100 to D 151 ; The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 8 - 153 The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 97 - 99 Chain "D" 152 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ACM B

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 08-JUL-92 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCB]B 8 to B 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]B 100 to B 151 ; The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 97 - 99 Chain "B" 152 - 153 The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ACM D

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 08-JUL-92 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCB]D 8 to D 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]D 100 to D 151 ; The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 8 - 153 The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 97 - 99 Chain "D" 152 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3AT1 B

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 22-SEP-89 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCB]B 8 to B 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]B 100 to B 151 ; The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 97 - 99 Chain "B" 152 - 153 The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3AT1 D

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 22-SEP-89 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCB]D 8 to D 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]D 100 to D 151 ; The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 8 - 153 The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 97 - 99 Chain "D" 152 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7AT1 B

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 22-SEP-89 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCB]B 8 to B 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]B 100 to B 151 ; The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 97 - 99 Chain "B" 152 - 153 The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7AT1 D

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 22-SEP-89 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCB]D 8 to D 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]D 100 to D 151 ; The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 8 - 153 The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 97 - 99 Chain "D" 152 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8AT1 B

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 22-SEP-89 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCB]B 8 to B 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]B 100 to B 151 ; The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 97 - 99 Chain "B" 152 - 153 The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8AT1 D

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 22-SEP-89 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCB]D 8 to D 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]D 100 to D 151 ; The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 8 - 153 The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 97 - 99 Chain "D" 152 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8ATC D

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 25-AUG-89 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCB]D 8 to D 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]D 100 to D 151 ; The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 8 - 153 The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 97 - 99 Chain "D" 152 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AT1 B

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 22-SEP-89 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCB]B 8 to B 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]B 100 to B 151 ; The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 97 - 99 Chain "B" 152 - 153 The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AT1 D

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 22-SEP-89 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCB]D 8 to D 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]D 100 to D 151 ; The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 8 - 153 The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 97 - 99 Chain "D" 152 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAA B

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCB]B 1 to B 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]B 100 to B 151 ; The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 97 - 99 Chain "B" 152 - 153 The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAA D

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCB]D 1 to D 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]D 100 to D 151 ; The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 1 - 153 The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 97 - 99 Chain "D" 152 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAB B

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCB]B 1 to B 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]B 100 to B 151 ; The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 97 - 99 Chain "B" 152 - 153 The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAB D

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCB]D 1 to D 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]D 100 to D 151 ; The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 1 - 153 The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 97 - 99 Chain "D" 152 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAC B

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCB]B 1 to B 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]B 100 to B 151 ; The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 97 - 99 Chain "B" 152 - 153 The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAC D

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCB]D 1 to D 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]D 100 to D 151 ; The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 1 - 153 The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 97 - 99 Chain "D" 152 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAD B

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCB]B 1 to B 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]B 100 to B 151 ; The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 97 - 99 Chain "B" 152 - 153 The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAD D

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCB]D 1 to D 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]D 100 to D 151 ; The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 1 - 153 The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 97 - 99 Chain "D" 152 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAE B

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCB]B 1 to B 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]B 100 to B 151 ; The following residues NOT assigned to any domain: Chain " " 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAE D

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCB]D 1 to D 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]D 100 to D 151 ; The following residues NOT assigned to any domain: Chain " " 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAF B

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCB]B 1 to B 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]B 100 to B 151 ; The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 97 - 99 Chain "B" 152 - 153 The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAF D

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCB]D 1 to D 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]D 100 to D 151 ; The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 1 - 153 The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 97 - 99 Chain "D" 152 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAG B

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCB]B 1 to B 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]B 100 to B 151 ; The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 97 - 99 Chain "B" 152 - 153 The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAG D

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCB]D 1 to D 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]D 100 to D 151 ; The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 1 - 153 The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 97 - 99 Chain "D" 152 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAH B

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCB]B 1 to B 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]B 100 to B 151 ; The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 97 - 99 Chain "B" 152 - 153 The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 1 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAH D

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCB]D 1 to D 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]D 100 to D 151 ; The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 1 - 153 The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 97 - 99 Chain "D" 152 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAI B

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCB]B 1 to B 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]B 100 to B 151 ; The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 97 - 99 Chain "B" 152 - 153 The following residues NOT assigned to any domain: Chain "B" 1 - 310 The following residues NOT assigned to any domain: Chain "B" 8 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1RAI D

PRELIMINARY 14-AUG-92 :: ASPARTATE TRANSCARBAMOYLASE (ASPARTATE CARBAMOYLTR

DOMAIN 1: [Assigned by homology with 8ATCB]D 8 to D 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]D 100 to D 151 ; The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 1 - 153 The following residues NOT assigned to any domain: Chain "D" 1 - 310 The following residues NOT assigned to any domain: Chain "D" 97 - 99 Chain "D" 152 - 153
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2ATC B

TRANSFERASE (CARBAMOYL-P,ASPARTATE) 24-MAR-82 :: ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCAR

DOMAIN 1: [Assigned by homology with 8ATCB]B 1 to B 96 ; DOMAIN 2: [Assigned by homology with 8ATCB]B 100 to B 150 ; The following residues NOT assigned to any domain: Chain "B" 1 - 305 The following residues NOT assigned to any domain: Chain "B" 97 - 99 Chain "B" 151 - 152
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]
AUTHOR ASSIGNMENTS - 3 DOMAIN STRUCTURES

AUTHOR ASSIGNMENTS - 3 DOMAIN STRUCTURES


1AOZ A

OXIDOREDUCTASE(OXYGEN ACCEPTOR) 08-JAN-92 :: ASCORBATE OXIDASE (E.C.1.10.3.3)

DOMAIN 1: A 1 to A 123 ; DOMAIN 2: A 130 to A 317 ; DOMAIN 3: A 337 to A 524 ; The following residues NOT assigned to any domain: Chain "A" 124 - 129 Chain "A" 318 - 336 Chain "A" 525 - 552 The following residues NOT assigned to any domain: Chain "A" 1 - 552
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GLT

PRELIMINARY 12-MAR-93 :: GLUTATHIONE SYNTHASE

DOMAIN 1: 1 to 121 ; DOMAIN 2: 122 to 133 ; 207 to 316 ; DOMAIN 3: 134 to 201 ; The following residues NOT assigned to any domain: Chain " " 202 - 206
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HSB A

HISTOCOMPATIBILITY ANTIGEN 30-MAR-93 :: CLASS I HISTOCOMPATIBILITY ANTIGEN AW68.1 (LEUCOCY

DOMAIN 1: A 1 to A 90 ; DOMAIN 2: A 91 to A 182 ; DOMAIN 3: A 183 to A 270 ; The following residues NOT assigned to any domain: Chain "A" 1 - 99 The following residues NOT assigned to any domain: Chain "A" 1 - 3 The following residues NOT assigned to any domain: Chain "A" 1 - 2
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MIN A

MOLYBDENUM-IRON PROTEIN 23-JAN-93 :: NITROGENASE MOLYBDENUM-IRON PROTEIN

DOMAIN 1: A 5 to A 60 ; A 334 to A 481 ; DOMAIN 2: A 61 to A 212 ; DOMAIN 3: A 213 to A 333 ; The following residues NOT assigned to any domain: Chain "A" 2 - 523 The following residues NOT assigned to any domain: Chain "A" 5 - 481 The following residues NOT assigned to any domain: Chain "A" 2 - 523
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MIN B

MOLYBDENUM-IRON PROTEIN 23-JAN-93 :: NITROGENASE MOLYBDENUM-IRON PROTEIN

DOMAIN 1: B 69 to B 209 ; DOMAIN 2: B 223 to B 336 ; DOMAIN 3: B 365 to B 523 ; The following residues NOT assigned to any domain: Chain "B" 5 - 481 The following residues NOT assigned to any domain: Chain "B" 2 - 68 Chain "B" 210 - 222 Chain "B" 337 - 364 The following residues NOT assigned to any domain: Chain "B" 5 - 481 The following residues NOT assigned to any domain: Chain "B" 2 - 523
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PDA

LYASE(PORPHYRIN) 17-NOV-92 :: PORPHOBILINOGEN DEAMINASE (E.C.4.3.1.8)

DOMAIN 1: 3 to 99 ; 200 to 217 ; DOMAIN 2: 105 to 193 ; DOMAIN 3: 222 to 307 ; The following residues NOT assigned to any domain: Chain " " 100 - 104 Chain " " 194 - 199 Chain " " 218 - 221
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TMD

PRELIMINARY 07-JAN-92 :: TRIMETHYLAMINE DEHYDROGENASE (E.C.1.5.99.7)

DOMAIN 1: 1 to 383 ; DOMAIN 2: 384 to 494 ; 649 to 696 ; DOMAIN 3: 495 to 648 ; The following residues NOT assigned to any domain: Chain " " 697 - 729
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TPT

THYMIDINE PHOSPHORYLASE 14-JUN-90 :: THYMIDINE PHOSPHORYLASE (E.C.2.4.2.4)

DOMAIN 1: 1 to 69 ; 159 to 196 ; DOMAIN 2: 70 to 158 ; 197 to 335 ; 430 to 440 ; DOMAIN 3: 336 to 429 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TRB

PRELIMINARY 07-SEP-91 :: THIOREDOXIN REDUCTASE /NADPH$: OXIDIZED-THIOREDOXI

DOMAIN 1: 1 to 116 ; 245 to 316 ; DOMAIN 2: 117 to 244 ; DOMAIN 3: 245 to 316 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2AAA

GLYCOSIDASE 27-FEB-91 :: ACID $ALPHA-AMYLASE (E.C.3.2.1.1)

DOMAIN 1: 1 to 100 ; 169 to 407 ; DOMAIN 2: 101 to 168 ; DOMAIN 3: 408 to 496 ; The following residues NOT assigned to any domain: Chain " " 408 - 476
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2MNR

RACEMASE 06-JUL-93 :: MANDELATE RACEMASE (E.C.5.1.2.2)

DOMAIN 1: 3 to 126 ; DOMAIN 2: 134 to 319 ; DOMAIN 3: 331 to 359 ; The following residues NOT assigned to any domain: Chain " " 127 - 133 Chain " " 320 - 330
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PIA

REDUCTASE 15-FEB-93 :: PHTHALATE DIOXYGENASE REDUCTASE (E.C.1.18.1.)

DOMAIN 1: 1 to 102 ; DOMAIN 2: 112 to 226 ; DOMAIN 3: 236 to 321 ; The following residues NOT assigned to any domain: Chain " " 103 - 111 Chain " " 227 - 235
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3GRS

OXIDOREDUCTASE (FLAVOENZYME) 05-FEB-88 :: GLUTATHIONE REDUCTASE (E.C.1.6.4.2), OXIDIZED FORM

DOMAIN 1: 18 to 157 ; 294 to 364 ; DOMAIN 2: 158 to 293 ; DOMAIN 3: 365 to 478 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4ICD

OXIDOREDUCTASE (NAD(A)-CHOH(D)) 28-DEC-89 :: PHOSPHORYLATED ISOCITRATE DEHYDROGENASE (E.C.1.1.1

DOMAIN 1: 3 to 124 ; 318 to 416 ; DOMAIN 2: 125 to 157 ; 203 to 317 ; DOMAIN 3: 158 to 202 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TRK A

TRANSFERASE(KETONE RESIDUES) 22-NOV-93 :: TRANSKETOLASE (E.C.2.2.1.1)

DOMAIN 1: A 3 to A 322 ; DOMAIN 2: A 323 to A 538 ; DOMAIN 3: A 539 to A 680 ; The following residues NOT assigned to any domain: Chain "A" 3 - 680
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GOF

OXIDOREDUCTASE(OXYGEN(A)) 30-SEP-93 :: GALACTOSE OXIDASE (E.C.1.1.3.9) (PH 4.5)

DOMAIN 1: 1 to 152 ; DOMAIN 2: 153 to 532 ; DOMAIN 3: 542 to 639 ; The following residues NOT assigned to any domain: Chain " " 533 - 541
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LLA

PRELIMINARY 07-SEP-92 :: LIMULUS POLYPHEMUS SUBUNIT II HEMOCYANIN

DOMAIN 1: 2 to 120 ; DOMAIN 2: 155 to 380 ; DOMAIN 3: 381 to 628 ; The following residues NOT assigned to any domain: Chain " " 121 - 154
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1POX A

OXIDOREDUCTASE(OXYGEN AS ACCEPTOR) 09-NOV-93 :: PYRUVATE OXIDASE (E.C.1.2.3.3) MUTANT WITH PRO 178

DOMAIN 1: A 9 to A 191 ; DOMAIN 2: A 192 to A 342 ; DOMAIN 3: A 342 to A 593 ; The following residues NOT assigned to any domain: Chain "A" 9 - 593
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DLC

TOXIN 22-JUN-94 :: DELTA-ENDOTOXIN CRYIIIA (BT13)

DOMAIN 1: 61 to 292 ; DOMAIN 2: 293 to 300 ; 497 to 644 ; DOMAIN 3: 301 to 496 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GAL

OXIDOREDUCTASE(FLAVOPROTEIN) 27-AUG-92 :: GLUCOSE OXIDASE (E.C.1.1.3.4)

DOMAIN 1: 3 to 56 ; 228 to 323 ; 521 to 583 ; DOMAIN 2: 56 to 228 ; DOMAIN 3: 324 to 520 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PYD A

LYASE(CARBON-CARBON) 23-MAR-93 :: PYRUVATE DECARBOXYLASE (PDC) (E.C.4.1.1.1)

DOMAIN 1: A 2 to A 191 ; DOMAIN 2: A 192 to A 354 ; DOMAIN 3: A 355 to A 556 ; The following residues NOT assigned to any domain: Chain "A" 2 - 556
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1DDT

TOXIN 01-MAR-94 :: DIPHTHERIA TOXIN (DIMERIC)

DOMAIN 1: 1 to 187 ; DOMAIN 2: 200 to 380 ; DOMAIN 3: 381 to 535 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1OLB A

BINDING PROTEIN 26-APR-94 :: OLIGO-PEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WIT

DOMAIN 1: A 1 to A 44 ; A 169 to A 270 ; A 487 to A 517 ; DOMAIN 2: A 45 to A 168 ; DOMAIN 3: A 271 to A 486 ; The following residues NOT assigned to any domain: Chain "A" 1 - 3
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HKG

TRANSFERASE 22-DEC-80 :: HEXOKINASE A AND GLUCOSE COMPLEX (E.C.2.7.1.1)

DOMAIN 1: 2 to 24 ; 253 to 370 ; DOMAIN 2: 24 to 50 ; 191 to 252 ; 371 to 432 ; DOMAIN 3: 51 to 190 ; 433 to 458 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NPX

PRELIMINARY 02-AUG-91 :: NADH PEROXIDASE (E.C.1.11.1.1) NON-NATIVE CYS 42 O

DOMAIN 1: 1 to 115 ; 242 to 325 ; DOMAIN 2: 116 to 241 ; DOMAIN 3: 326 to 447 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2DKB

LYASE(DECARBOXYLASE) 12-JUL-94 :: 2,2-DIALKYLGLYCINE DECARBOXYLASE (PYRUVATE) (DGD)

DOMAIN 1: 3 to 49 ; DOMAIN 2: 50 to 325 ; DOMAIN 3: 326 to 433 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TPL A

LYASE(CARBON-CARBON) 25-NOV-92 :: TYROSINE PHENOL-LYASE (E.C.4.1.99.2)

DOMAIN 1: A 19 to A 48 ; A 333 to A 456 ; DOMAIN 2: A 49 to A 56 ; A 311 to A 332 ; DOMAIN 3: A 57 to A 310 ; The following residues NOT assigned to any domain: Chain "A" 1 - 18 The following residues NOT assigned to any domain: Chain "A" 1 - 456
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1FCD A

ELECTRON TRANSPORT(FLAVOCYTOCHROME) 18-AUG-94 :: FLAVOCYTOCHROME C SULFIDE DEHYDROGENASE (FCSD)

DOMAIN 1: A 1 to A 107 ; A 256 to A 328 ; DOMAIN 2: A 108 to A 255 ; DOMAIN 3: A 328 to A 401 ; The following residues NOT assigned to any domain: Chain "A" 1 - 174 The following residues NOT assigned to any domain: Chain "A" 1 - 401 The following residues NOT assigned to any domain: Chain "A" 1 - 174
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2POL A

PRELIMINARY 13-NOV-92 :: BETA SUBUNIT OF POL III (E.C.2.7.7.7)

DOMAIN 1: A 1 to A 121 ; DOMAIN 2: A 121 to A 249 ; DOMAIN 3: A 250 to A 366 ; The following residues NOT assigned to any domain: Chain "A" 1 - 366
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PXT A

THIOLASE 04-JUL-94 :: PEROXISOMAL 3-KETOACYL-COA THIOLASE (E.C.2.3.1.16)

DOMAIN 1: A 28 to A 153 ; A 276 to A 298 ; DOMAIN 2: A 154 to A 275 ; DOMAIN 3: A 299 to A 417 ; The following residues NOT assigned to any domain: Chain "A" 28 - 417
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TAH B

HYDROLASE(CARBOXYLIC ESTERASE) 21-DEC-93 :: LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE)

DOMAIN 1: B 2 to B 117 ; B 166 to B 213 ; B 272 to B 319 ; DOMAIN 2: B 118 to B 165 ; DOMAIN 3: B 214 to B 271 ; The following residues NOT assigned to any domain: Chain "B" 2 - 319 The following residues NOT assigned to any domain: Chain "B" 2 - 319 The following residues NOT assigned to any domain: Chain "B" 2 - 319
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BIA

TRANSCRIPTION REGULATION 06-JUL-92 :: BIRA BIFUNCTIONAL PROTEIN (ACTS AS BIOTIN OPERON R

DOMAIN 1: 1 to 64 ; DOMAIN 2: 66 to 270 ; DOMAIN 3: 271 to 317 ; The following residues NOT assigned to any domain: Chain " " 65 - 65
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1BPB

NUCLEOTIDYLTRANSFERASE 12-APR-94 :: DNA POLYMERASE BETA (BETA POLYMERASE) (E.C.2.7.7.7

DOMAIN 1: 91 to 147 ; DOMAIN 2: 148 to 272 ; DOMAIN 3: 263 to 335 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ZAA C

DNA-BINDING PROTEIN 17-SEP-92 :: ZIF268 IMMEDIATE EARLY GENE (KROX-24) COMPLEX WITH

DOMAIN 1: C 3 to C 31 ; DOMAIN 2: C 32 to C 60 ; DOMAIN 3: C 61 to C 87 ; The following residues NOT assigned to any domain: Chain "C" 1 - 11 The following residues NOT assigned to any domain: Chain "C" 1 - 11
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GLV

PRELIMINARY 12-MAR-93 :: GLUTATHIONE SYNTHASE, LOOPLESS MUTANT (DEL)

DOMAIN 1: 1 to 121 ; DOMAIN 2: 122 to 133 ; 207 to 316 ; DOMAIN 3: 134 to 201 ; The following residues NOT assigned to any domain: Chain " " 202 - 206
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MIN C

MOLYBDENUM-IRON PROTEIN 23-JAN-93 :: NITROGENASE MOLYBDENUM-IRON PROTEIN

DOMAIN 1: [Assigned by homology with 1MINA]C 5 to C 60 ; C 334 to C 481 ; DOMAIN 2: [Assigned by homology with 1MINA]C 61 to C 212 ; DOMAIN 3: [Assigned by homology with 1MINA]C 213 to C 333 ; The following residues NOT assigned to any domain: Chain "C" 5 - 481 The following residues NOT assigned to any domain: Chain "C" 2 - 523 The following residues NOT assigned to any domain: Chain "C" 2 - 523
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MIO A

MOLYBDENUM-IRON PROTEIN 24-MAR-93 :: NITROGENASE MOLYBDENUM-IRON PROTEIN

DOMAIN 1: [Assigned by homology with 1MINA]A 2 to A 51 ; A 322 to A 521 ; DOMAIN 2: [Assigned by homology with 1MINA]A 52 to A 203 ; DOMAIN 3: [Assigned by homology with 1MINA]A 204 to A 321 ; The following residues NOT assigned to any domain: Chain "A" 522 - 526 The following residues NOT assigned to any domain: Chain "A" 2 - 458 The following residues NOT assigned to any domain: Chain "A" 2 - 526 The following residues NOT assigned to any domain: Chain "A" 2 - 458
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MIO C

MOLYBDENUM-IRON PROTEIN 24-MAR-93 :: NITROGENASE MOLYBDENUM-IRON PROTEIN

DOMAIN 1: [Assigned by homology with 1MINA]C 2 to C 51 ; C 322 to C 521 ; DOMAIN 2: [Assigned by homology with 1MINA]C 52 to C 203 ; DOMAIN 3: [Assigned by homology with 1MINA]C 204 to C 321 ; The following residues NOT assigned to any domain: Chain "C" 2 - 526 The following residues NOT assigned to any domain: Chain "C" 2 - 458 The following residues NOT assigned to any domain: Chain "C" 522 - 526 The following residues NOT assigned to any domain: Chain "C" 2 - 458
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MIN D

MOLYBDENUM-IRON PROTEIN 23-JAN-93 :: NITROGENASE MOLYBDENUM-IRON PROTEIN

DOMAIN 1: [Assigned by homology with 1MINB]D 69 to D 209 ; DOMAIN 2: [Assigned by homology with 1MINB]D 223 to D 336 ; DOMAIN 3: [Assigned by homology with 1MINB]D 365 to D 523 ; The following residues NOT assigned to any domain: Chain "D" 5 - 481 The following residues NOT assigned to any domain: Chain "D" 2 - 523 The following residues NOT assigned to any domain: Chain "D" 5 - 481 The following residues NOT assigned to any domain: Chain "D" 2 - 68 Chain "D" 210 - 222 Chain "D" 337 - 364
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MIO B

MOLYBDENUM-IRON PROTEIN 24-MAR-93 :: NITROGENASE MOLYBDENUM-IRON PROTEIN

DOMAIN 1: [Assigned by homology with 1MINB]B 22 to B 160 ; DOMAIN 2: [Assigned by homology with 1MINB]B 171 to B 284 ; DOMAIN 3: [Assigned by homology with 1MINB]B 313 to B 458 ; The following residues NOT assigned to any domain: Chain "B" 2 - 526 The following residues NOT assigned to any domain: Chain "B" 2 - 21 Chain "B" 161 - 170 Chain "B" 285 - 312 The following residues NOT assigned to any domain: Chain "B" 2 - 526 The following residues NOT assigned to any domain: Chain "B" 2 - 458
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MIO D

MOLYBDENUM-IRON PROTEIN 24-MAR-93 :: NITROGENASE MOLYBDENUM-IRON PROTEIN

DOMAIN 1: [Assigned by homology with 1MINB]D 22 to D 160 ; DOMAIN 2: [Assigned by homology with 1MINB]D 171 to D 284 ; DOMAIN 3: [Assigned by homology with 1MINB]D 313 to D 458 ; The following residues NOT assigned to any domain: Chain "D" 2 - 526 The following residues NOT assigned to any domain: Chain "D" 2 - 458 The following residues NOT assigned to any domain: Chain "D" 2 - 526 The following residues NOT assigned to any domain: Chain "D" 2 - 21 Chain "D" 161 - 170 Chain "D" 285 - 312
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TDF

OXIDOREDUCTASE(FLAVOENZYME) 14-JAN-94 :: THIOREDOXIN REDUCTASE (E.C.1.6.4.5) MUTANT WITH CY

DOMAIN 1: 1 to 116 ; DOMAIN 2: 117 to 244 ; DOMAIN 3: 245 to 316 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TDE

OXIDOREDUCTASE(FLAVOENZYME) 14-JAN-94 :: THIOREDOXIN REDUCTASE (E.C.1.6.4.5) (WILD TYPE)

DOMAIN 1: 1 to 116 ; DOMAIN 2: 117 to 244 ; DOMAIN 3: 245 to 316 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MDR

RACEMASE 19-NOV-93 :: MANDELATE RACEMASE (E.C.5.1.2.2)

DOMAIN 1: 3 to 125 ; DOMAIN 2: 133 to 318 ; DOMAIN 3: 330 to 358 ; The following residues NOT assigned to any domain: Chain " " 126 - 132 Chain " " 319 - 329 Chain " " 359 - 359
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MNS

RACEMASE 06-JUL-93 :: MANDELATE RACEMASE (E.C.5.1.2.2)

DOMAIN 1: 3 to 125 ; DOMAIN 2: 133 to 318 ; DOMAIN 3: 330 to 358 ; The following residues NOT assigned to any domain: Chain " " 126 - 132 Chain " " 319 - 329 Chain " " 359 - 359
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1MLE

ISOMERASE(INTRAMOLECULAR LYASE) 09-OCT-90 :: MUCONATE LACTONIZING ENZYME (CIS,CIS MUCONATE

DOMAIN 1: 2 to 126 ; DOMAIN 2: 134 to 331 ; DOMAIN 3: 343 to 371 ; The following residues NOT assigned to any domain: Chain " " 127 - 133 Chain " " 332 - 342 Chain " " 372 - 373
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CHR A

ISOMERASE 20-AUG-93 :: CHLOROMUCONATE CYCLOISOMERASE (E.C.5.5.1.7)

DOMAIN 1: A 1 to A 122 ; DOMAIN 2: A 130 to A 327 ; DOMAIN 3: A 339 to A 367 ; The following residues NOT assigned to any domain: Chain "A" 123 - 129 Chain "A" 328 - 338 Chain "A" 368 - 370 The following residues NOT assigned to any domain: Chain "A" 1 - 370
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1CHR B

ISOMERASE 20-AUG-93 :: CHLOROMUCONATE CYCLOISOMERASE (E.C.5.5.1.7)

DOMAIN 1: B 1 to B 122 ; DOMAIN 2: B 130 to B 327 ; DOMAIN 3: B 339 to B 367 ; The following residues NOT assigned to any domain: Chain "B" 1 - 370 The following residues NOT assigned to any domain: Chain "B" 123 - 129 Chain "B" 328 - 338 Chain "B" 368 - 370
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TYP A

PRELIMINARY 29-JUN-92 :: TRYPANOTHIONE REDUCTASE (E.C.1.6.4.8)

DOMAIN 1: A 1 to A 160 ; A 289 to A 358 ; DOMAIN 2: A 161 to A 288 ; DOMAIN 3: A 359 to A 471 ; The following residues NOT assigned to any domain: Chain "A" 472 - 487 The following residues NOT assigned to any domain: Chain "A" 2 - 487 The following residues NOT assigned to any domain: Chain "A" 496 - 501 The following residues NOT assigned to any domain: Chain "A" 496 - 501
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TYP B

PRELIMINARY 29-JUN-92 :: TRYPANOTHIONE REDUCTASE (E.C.1.6.4.8)

DOMAIN 1: B 2 to B 160 ; B 289 to B 358 ; DOMAIN 2: B 161 to B 288 ; DOMAIN 3: B 359 to B 471 ; The following residues NOT assigned to any domain: Chain "B" 1 - 487 The following residues NOT assigned to any domain: Chain "B" 472 - 487 The following residues NOT assigned to any domain: Chain "B" 496 - 501 The following residues NOT assigned to any domain: Chain "B" 496 - 501
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TYT A

OXIDOREDUCTASE 10-JUN-93 :: TRYPANOTHIONE REDUCTASE (E.C.1.6.4.8) (OXIDIZED FO

DOMAIN 1: A 1 to A 160 ; A 289 to A 358 ; DOMAIN 2: A 161 to A 288 ; DOMAIN 3: A 359 to A 471 ; The following residues NOT assigned to any domain: Chain "A" 472 - 487 The following residues NOT assigned to any domain: Chain "A" 2 - 487
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TYT B

OXIDOREDUCTASE 10-JUN-93 :: TRYPANOTHIONE REDUCTASE (E.C.1.6.4.8) (OXIDIZED FO

DOMAIN 1: B 2 to B 160 ; B 289 to B 358 ; DOMAIN 2: B 161 to B 288 ; DOMAIN 3: B 359 to B 471 ; The following residues NOT assigned to any domain: Chain "B" 1 - 487 The following residues NOT assigned to any domain: Chain "B" 472 - 487
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2TPR A

OXIDOREDUCTASE 22-AUG-91 :: TRYPANOTHIONE REDUCTASE (E.C.1.6.4.8)

DOMAIN 1: A 1 to A 159 ; A 288 to A 357 ; DOMAIN 2: A 160 to A 287 ; DOMAIN 3: A 358 to A 470 ; The following residues NOT assigned to any domain: Chain "A" 471 - 482 The following residues NOT assigned to any domain: Chain "A" 1 - 482
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2TPR B

OXIDOREDUCTASE 22-AUG-91 :: TRYPANOTHIONE REDUCTASE (E.C.1.6.4.8)

DOMAIN 1: B 1 to B 159 ; B 288 to B 357 ; DOMAIN 2: B 160 to B 287 ; DOMAIN 3: B 358 to B 470 ; The following residues NOT assigned to any domain: Chain "B" 1 - 482 The following residues NOT assigned to any domain: Chain "B" 471 - 482
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NDA A

OXIDOREDUCTASE 02-JUL-93 :: TRYPANOTHIONE OXIDOREDUCTASE (E.C.1.6.4.8) (OXIDIZ

DOMAIN 1: A 4 to A 160 ; A 289 to A 357 ; DOMAIN 2: A 161 to A 288 ; DOMAIN 3: A 358 to A 470 ; The following residues NOT assigned to any domain: Chain "A" 471 - 484 The following residues NOT assigned to any domain: Chain "A" 4 - 484
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NDA B

OXIDOREDUCTASE 02-JUL-93 :: TRYPANOTHIONE OXIDOREDUCTASE (E.C.1.6.4.8) (OXIDIZ

DOMAIN 1: B 4 to B 160 ; B 289 to B 357 ; DOMAIN 2: B 161 to B 288 ; DOMAIN 3: B 358 to B 470 ; The following residues NOT assigned to any domain: Chain "B" 4 - 484 The following residues NOT assigned to any domain: Chain "B" 471 - 484
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GER A

OXIDOREDUCTASE(FLAVOENZYME) 18-JAN-94 :: GLUTATHIONE REDUCTASE (E.C.1.6.4.2) COMPLEXED WITH

DOMAIN 1: A 3 to A 139 ; A 265 to A 335 ; DOMAIN 2: A 140 to A 264 ; DOMAIN 3: A 336 to A 449 ; The following residues NOT assigned to any domain: Chain "A" 450 - 450 The following residues NOT assigned to any domain: Chain "A" 2 - 450
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GES A

OXIDOREDUCTASE(FLAVOENZYME) 18-JAN-94 :: GLUTATHIONE REDUCTASE (E.C.1.6.4.2) NAD MUTANT WIT

DOMAIN 1: A 3 to A 139 ; A 265 to A 335 ; DOMAIN 2: A 140 to A 264 ; DOMAIN 3: A 336 to A 449 ; The following residues NOT assigned to any domain: Chain "A" 450 - 450 The following residues NOT assigned to any domain: Chain "A" 2 - 450
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GET A

OXIDOREDUCTASE(FLAVOENZYME) 18-JAN-94 :: GLUTATHIONE REDUCTASE (E.C.1.6.4.2) WILD-TYPE COMP

DOMAIN 1: A 3 to A 139 ; A 265 to A 335 ; DOMAIN 2: A 140 to A 264 ; DOMAIN 3: A 336 to A 449 ; The following residues NOT assigned to any domain: Chain "A" 450 - 450 The following residues NOT assigned to any domain: Chain "A" 2 - 450
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GEU A

OXIDOREDUCTASE(FLAVOENZYME) 18-JAN-94 :: GLUTATHIONE REDUCTASE (E.C.1.6.4.2) NAD MUTANT WIT

DOMAIN 1: A 3 to A 139 ; A 265 to A 335 ; DOMAIN 2: A 140 to A 264 ; DOMAIN 3: A 336 to A 449 ; The following residues NOT assigned to any domain: Chain "A" 450 - 450 The following residues NOT assigned to any domain: Chain "A" 2 - 450
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GER B

OXIDOREDUCTASE(FLAVOENZYME) 18-JAN-94 :: GLUTATHIONE REDUCTASE (E.C.1.6.4.2) COMPLEXED WITH

DOMAIN 1: B 2 to B 139 ; B 265 to B 335 ; DOMAIN 2: B 140 to B 264 ; DOMAIN 3: B 336 to B 449 ; The following residues NOT assigned to any domain: Chain "B" 3 - 450 The following residues NOT assigned to any domain: Chain "B" 450 - 450
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GES B

OXIDOREDUCTASE(FLAVOENZYME) 18-JAN-94 :: GLUTATHIONE REDUCTASE (E.C.1.6.4.2) NAD MUTANT WIT

DOMAIN 1: B 2 to B 139 ; B 265 to B 335 ; DOMAIN 2: B 140 to B 264 ; DOMAIN 3: B 336 to B 449 ; The following residues NOT assigned to any domain: Chain "B" 3 - 450 The following residues NOT assigned to any domain: Chain "B" 450 - 450
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GET B

OXIDOREDUCTASE(FLAVOENZYME) 18-JAN-94 :: GLUTATHIONE REDUCTASE (E.C.1.6.4.2) WILD-TYPE COMP

DOMAIN 1: B 2 to B 139 ; B 265 to B 335 ; DOMAIN 2: B 140 to B 264 ; DOMAIN 3: B 336 to B 449 ; The following residues NOT assigned to any domain: Chain "B" 3 - 450 The following residues NOT assigned to any domain: Chain "B" 450 - 450
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GEU B

OXIDOREDUCTASE(FLAVOENZYME) 18-JAN-94 :: GLUTATHIONE REDUCTASE (E.C.1.6.4.2) NAD MUTANT WIT

DOMAIN 1: B 2 to B 139 ; B 265 to B 335 ; DOMAIN 2: B 140 to B 264 ; DOMAIN 3: B 336 to B 449 ; The following residues NOT assigned to any domain: Chain "B" 3 - 450 The following residues NOT assigned to any domain: Chain "B" 450 - 450
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

4GR1

OXIDOREDUCTASE (FLAVOENZYME) 26-MAR-90 :: GLUTATHIONE REDUCTASE (E.C.1.6.4.2) OXIDIZED FORM

DOMAIN 1: 18 to 156 ; 293 to 363 ; DOMAIN 2: 157 to 292 ; DOMAIN 3: 364 to 477 ; The following residues NOT assigned to any domain: Chain " " 478 - 478
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GRA

PRELIMINARY 15-DEC-92 :: GLUTATHIONE REDUCTASE,NADPH:GSSG OXIDOREDUCTASE,EC

DOMAIN 1: 18 to 156 ; 293 to 363 ; DOMAIN 2: 157 to 292 ; DOMAIN 3: 364 to 477 ; The following residues NOT assigned to any domain: Chain " " 478 - 478 The following residues NOT assigned to any domain: Chain " " 482 - 486
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GRB

PRELIMINARY 15-DEC-92 :: GLUTATHIONE REDUCTASE,NADPH:GSSG OXIDOREDUCTASE,EC

DOMAIN 1: 18 to 156 ; 293 to 363 ; DOMAIN 2: 157 to 292 ; DOMAIN 3: 364 to 477 ; The following residues NOT assigned to any domain: Chain " " 478 - 478
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GRE

PRELIMINARY 15-DEC-92 :: GLUTATHIONE REDUCTASE,NADPH:GSSG OXIDOREDUCTASE,EC

DOMAIN 1: 18 to 156 ; 293 to 363 ; DOMAIN 2: 157 to 292 ; DOMAIN 3: 364 to 477 ; The following residues NOT assigned to any domain: Chain " " 478 - 478 The following residues NOT assigned to any domain: Chain " " 482 - 486
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GRF

PRELIMINARY 15-DEC-92 :: GLUTATHIONE REDUCTASE,NADPH:GSSG OXIDOREDUCTASE,EC

DOMAIN 1: 18 to 156 ; 293 to 363 ; DOMAIN 2: 157 to 292 ; DOMAIN 3: 364 to 477 ; The following residues NOT assigned to any domain: Chain " " 478 - 478
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1GRG

OXIDOREDUCTASE(FLAVOENZYME) 15-DEC-92 :: GLUTATHIONE REDUCTASE (E.C.1.6.4.2) MODIFIED BY BC

DOMAIN 1: 18 to 156 ; 293 to 363 ; DOMAIN 2: 157 to 292 ; DOMAIN 3: 364 to 477 ; The following residues NOT assigned to any domain: Chain " " 478 - 478
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LVL

PRELIMINARY 16-DEC-92 :: DIHYDROLIPOAMIDE DEHYDROGENASE(E.C.1.8.1.4)/NAD+

DOMAIN 1: 1 to 142 ; 268 to 335 ; DOMAIN 2: 143 to 267 ; DOMAIN 3: 336 to 449 ; The following residues NOT assigned to any domain: Chain " " 450 - 458
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3LAD A

PRELIMINARY 12-DEC-91 :: DIHYDROLIPOAMIDE DEHYDROGENASE (E.C.1.8.1.4)

DOMAIN 1: A 1 to A 150 ; A 280 to A 348 ; DOMAIN 2: A 151 to A 279 ; DOMAIN 3: A 349 to A 462 ; The following residues NOT assigned to any domain: Chain "A" 463 - 472 The following residues NOT assigned to any domain: Chain "A" 1 - 472
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3LAD B

PRELIMINARY 12-DEC-91 :: DIHYDROLIPOAMIDE DEHYDROGENASE (E.C.1.8.1.4)

DOMAIN 1: B 1 to B 150 ; B 280 to B 348 ; DOMAIN 2: B 151 to B 279 ; DOMAIN 3: B 349 to B 462 ; The following residues NOT assigned to any domain: Chain "B" 1 - 472 The following residues NOT assigned to any domain: Chain "B" 463 - 472
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LPF A

PRELIMINARY 26-OCT-92 :: LIPOAMIDE DEHYDROGENASE (E.C. 1.8.1.6)

DOMAIN 1: A 1 to A 150 ; A 280 to A 348 ; DOMAIN 2: A 151 to A 279 ; DOMAIN 3: A 349 to A 462 ; The following residues NOT assigned to any domain: Chain "A" 463 - 472 The following residues NOT assigned to any domain: Chain "A" 501 - 972
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1LPF B

PRELIMINARY 26-OCT-92 :: LIPOAMIDE DEHYDROGENASE (E.C. 1.8.1.6)

DOMAIN 1: B 1 to B 150 ; B 280 to B 348 ; DOMAIN 2: B 151 to B 279 ; DOMAIN 3: B 349 to B 462 ; The following residues NOT assigned to any domain: Chain " " 1 - 472 The following residues NOT assigned to any domain: Chain " " 501 - 972
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1HEX

OXIDOREDUCTASE 09-SEP-94 :: 3-ISOPROPYLMALATE DEHYDROGENASE (E.C.1.1.1.85) COM

DOMAIN 1: 1 to 90 ; 252 to 344 ; DOMAIN 2: 91 to 120 ; 159 to 251 ; DOMAIN 3: 121 to 158 ; The following residues NOT assigned to any domain: Chain " " 345 - 345
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IPD

OXIDOREDUCTASE 29-JAN-92 :: 3-ISOPROPYLMALATE DEHYDROGENASE (E.C.1.1.1.85)

DOMAIN 1: 1 to 90 ; 252 to 344 ; DOMAIN 2: 91 to 120 ; 159 to 251 ; DOMAIN 3: 121 to 158 ; The following residues NOT assigned to any domain: Chain " " 345 - 345
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5ICD

OXIDOREDUCTASE (NAD(A)-CHOH(D)) 30-MAY-90 :: ISOCITRATE DEHYDROGENASE (E.C.1.1.1.42) COMPLEX WI

DOMAIN 1: 3 to 124 ; 318 to 416 ; DOMAIN 2: 125 to 157 ; 203 to 317 ; DOMAIN 3: 158 to 202 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IKA

OXIDOREDUCTASE(NAD(A)-CHOH(D)) 15-JUN-93 :: ISOCITRATE DEHYDROGENASE (E.C.1.1.1.42) COMPLEXED

DOMAIN 1: 3 to 124 ; 318 to 416 ; DOMAIN 2: 125 to 157 ; 203 to 317 ; DOMAIN 3: 158 to 202 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1IKB

OXIDOREDUCTASE(NAD(A)-CHOH(D)) 15-JUN-93 :: ISOCITRATE DEHYDROGENASE (E.C.1.1.1.42) COMPLEXED

DOMAIN 1: 3 to 124 ; 318 to 416 ; DOMAIN 2: 125 to 157 ; 203 to 317 ; DOMAIN 3: 158 to 202 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6ICD

OXIDOREDUCTASE (NAD(A)-CHOH(D)) 30-MAY-90 :: ISOCITRATE DEHYDROGENASE (E.C.1.1.1.42) (MUTANT WI

DOMAIN 1: 3 to 124 ; 318 to 416 ; DOMAIN 2: 125 to 157 ; 203 to 317 ; DOMAIN 3: 158 to 202 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7ICD

OXIDOREDUCTASE (NAD(A)-CHOH(D)) 30-MAY-90 :: ISOCITRATE DEHYDROGENASE (E.C.1.1.1.42) (MUTANT WI

DOMAIN 1: 3 to 124 ; 318 to 416 ; DOMAIN 2: 125 to 157 ; 203 to 317 ; DOMAIN 3: 158 to 202 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8ICD

OXIDOREDUCTASE (NAD(A)-CHOH(D)) 30-MAY-90 :: ISOCITRATE DEHYDROGENASE (E.C.1.1.1.42) (MUTANT WI

DOMAIN 1: 3 to 124 ; 318 to 416 ; DOMAIN 2: 125 to 157 ; 203 to 317 ; DOMAIN 3: 158 to 202 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

3ICD

OXIDOREDUCTASE (NAD(A)-CHOH(D)) 28-DEC-89 :: ISOCITRATE DEHYDROGENASE (E.C.1.1.1.42)

DOMAIN 1: 3 to 124 ; 318 to 416 ; DOMAIN 2: 125 to 157 ; 203 to 317 ; DOMAIN 3: 158 to 202 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

9ICD

OXIDOREDUCTASE (NAD(A)-CHOH(D)) 29-JUL-91 :: ISOCITRATE DEHYDROGENASE (E.C.1.1.1.42) COMPLEX WI

DOMAIN 1: 3 to 124 ; 318 to 416 ; DOMAIN 2: 125 to 157 ; 203 to 317 ; DOMAIN 3: 158 to 202 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]
AUTHOR ASSIGNMENTS - 4 DOMAIN STRUCTURES

AUTHOR ASSIGNMENTS - 4 DOMAIN STRUCTURES


1ATN A

ENDODEOXYRIBONUCLEASE 08-MAR-91 :: DEOXYRIBONUCLEASE I COMPLEX WITH ACTIN

DOMAIN 1: A 1 to A 32 ; A 70 to A 144 ; DOMAIN 2: A 33 to A 69 ; DOMAIN 3: A 145 to A 180 ; A 270 to A 337 ; DOMAIN 4: A 181 to A 269 ; The following residues NOT assigned to any domain: Chain "A" 0 - 0 Chain "A" 338 - 372 The following residues NOT assigned to any domain: Chain "A" 1 - 260
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1AVH A

PRELIMINARY 17-OCT-91 :: ANNEXIN V (HEXAGONAL)

DOMAIN 1: A 3 to A 87 ; DOMAIN 2: A 88 to A 167 ; DOMAIN 3: A 168 to A 246 ; DOMAIN 4: A 247 to A 320 ; The following residues NOT assigned to any domain: Chain "A" 3 - 320
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PMG A

PHOSPHOTRANSFERASE 05-AUG-92 :: PHOSPHOGLUCOMUTASE (E.C.5.4.2.2)

DOMAIN 1: A 1 to A 188 ; DOMAIN 2: A 192 to A 315 ; DOMAIN 3: A 325 to A 403 ; DOMAIN 4: A 408 to A 561 ; The following residues NOT assigned to any domain: Chain "A" 189 - 191 Chain "A" 316 - 324 Chain "A" 404 - 407 The following residues NOT assigned to any domain: Chain "A" 1 - 561
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8ACN

LYASE(CARBON-OXYGEN) 15-MAY-91 :: ACONITASE (E.C.4.2.1.3) COMPLEX WITH NITROISOCITRA

DOMAIN 1: 2 to 200 ; DOMAIN 2: 201 to 317 ; DOMAIN 3: 320 to 513 ; DOMAIN 4: 538 to 754 ; The following residues NOT assigned to any domain: Chain " " 318 - 319 Chain " " 514 - 537
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8CAT A

OXIDOREDUCTASE (H2O2 ACCEPTOR) 15-NOV-84 :: CATALASE (E.C.1.11.1.6)

DOMAIN 1: A 3 to A 75 ; DOMAIN 2: A 76 to A 320 ; DOMAIN 3: A 321 to A 436 ; DOMAIN 4: A 437 to A 500 ; The following residues NOT assigned to any domain: Chain "A" 3 - 500
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

9WGA A

LECTIN (AGGLUTININ) 20-APR-90 :: WHEAT GERM AGGLUTININ (ISOLECTIN 2)

DOMAIN 1: A 2 to A 43 ; DOMAIN 2: A 44 to A 83 ; DOMAIN 3: A 84 to A 120 ; DOMAIN 4: A 121 to A 171 ; The following residues NOT assigned to any domain: Chain "A" 1 - 1 The following residues NOT assigned to any domain: Chain "A" 1 - 171
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1PGD

OXIDOREDUCTASE(CHOH(D)-NADP+(A)) 21-AUG-91 :: 6-PHOSPHOGLUCONATE DEHYDROGENASE (6-PGDH) (E.C.1.1

DOMAIN 1: 1 to 176 ; DOMAIN 2: 177 to 303 ; DOMAIN 3: 304 to 432 ; DOMAIN 4: 433 to 469 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1TNR R

COMPLEX(LYMPHOKINE/RECEPTOR) 09-MAY-94 :: TUMOR NECROSIS FACTOR RECEPTOR P55 (EXTRACELLULAR

DOMAIN 1: R 15 to R 52 ; DOMAIN 2: R 53 to R 97 ; DOMAIN 3: R 98 to R 137 ; DOMAIN 4: R 138 to R 153 ; The following residues NOT assigned to any domain: Chain "R" 28 - 171
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2PMG B

PHOSPHOTRANSFERASE 05-AUG-92 :: PHOSPHOGLUCOMUTASE (E.C.5.4.2.2)

DOMAIN 1: [Assigned by homology with 2PMGA]B 1 to B 188 ; DOMAIN 2: [Assigned by homology with 2PMGA]B 192 to B 315 ; DOMAIN 3: [Assigned by homology with 2PMGA]B 325 to B 403 ; DOMAIN 4: [Assigned by homology with 2PMGA]B 408 to B 561 ; The following residues NOT assigned to any domain: Chain "B" 1 - 561 The following residues NOT assigned to any domain: Chain "B" 189 - 191 Chain "B" 316 - 324 Chain "B" 404 - 407
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

5ACN

LYASE(CARBON-OXYGEN) 16-JAN-90 :: ACONITASE (E.C.4.2.1.3) (INACTIVE (3FE-4S) CLUSTER

DOMAIN 1: 1 to 199 ; DOMAIN 2: 200 to 316 ; DOMAIN 3: 319 to 512 ; DOMAIN 4: 537 to 753 ; The following residues NOT assigned to any domain: Chain " " 317 - 318 Chain " " 513 - 536 Chain " " 754 - 754
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

6ACN

LYASE(CARBON-OXYGEN) 16-JAN-90 :: ACONITASE (E.C.4.2.1.3) (ACTIVATED (4FE-4S) CLUSTE

DOMAIN 1: 1 to 199 ; DOMAIN 2: 200 to 316 ; DOMAIN 3: 319 to 512 ; DOMAIN 4: 537 to 753 ; The following residues NOT assigned to any domain: Chain " " 317 - 318 Chain " " 513 - 536 Chain " " 754 - 754
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7ACN

LYASE(CARBON-OXYGEN) 15-MAY-91 :: ACONITASE (E.C.4.2.1.3) COMPLEX WITH ISOCITRATE

DOMAIN 1: 2 to 199 ; DOMAIN 2: 200 to 316 ; DOMAIN 3: 319 to 512 ; DOMAIN 4: 537 to 753 ; The following residues NOT assigned to any domain: Chain " " 317 - 318 Chain " " 513 - 536 Chain " " 754 - 754
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1ACO

LYASE(CARBON-OXYGEN) 17-JAN-93 :: ACONITASE (MITOCHONDRIAL) (E.C.4.2.1.3) COMPLEX WI

DOMAIN 1: 2 to 199 ; DOMAIN 2: 200 to 316 ; DOMAIN 3: 319 to 512 ; DOMAIN 4: 537 to 753 ; The following residues NOT assigned to any domain: Chain " " 317 - 318 Chain " " 513 - 536 Chain " " 754 - 754
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NIS

LYASE(CARBON-OXYGEN) 17-JAN-93 :: ACONITASE (E.C.4.2.1.3) COMPLEX WITH NITROCITRATE

DOMAIN 1: 2 to 199 ; DOMAIN 2: 200 to 316 ; DOMAIN 3: 319 to 512 ; DOMAIN 4: 537 to 753 ; The following residues NOT assigned to any domain: Chain " " 317 - 318 Chain " " 513 - 536 Chain " " 754 - 754
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1NIT

LYASE(CARBON-OXYGEN) 17-JAN-93 :: ACONITASE (E.C.4.2.1.3) COMPLEX WITH SULFATE (MINO

DOMAIN 1: 2 to 199 ; DOMAIN 2: 200 to 316 ; DOMAIN 3: 319 to 512 ; DOMAIN 4: 537 to 753 ; The following residues NOT assigned to any domain: Chain " " 317 - 318 Chain " " 513 - 536 Chain " " 754 - 754
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7CAT A

OXIDOREDUCTASE (H2O2 ACCEPTOR) 15-NOV-84 :: CATALASE (E.C.1.11.1.6)

DOMAIN 1: [Assigned by homology with 8CATA]A 3 to A 75 ; DOMAIN 2: [Assigned by homology with 8CATA]A 76 to A 320 ; DOMAIN 3: [Assigned by homology with 8CATA]A 321 to A 436 ; DOMAIN 4: [Assigned by homology with 8CATA]A 437 to A 500 ;
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

8CAT B

OXIDOREDUCTASE (H2O2 ACCEPTOR) 15-NOV-84 :: CATALASE (E.C.1.11.1.6)

DOMAIN 1: [Assigned by homology with 8CATA]B 3 to B 75 ; DOMAIN 2: [Assigned by homology with 8CATA]B 76 to B 320 ; DOMAIN 3: [Assigned by homology with 8CATA]B 321 to B 436 ; DOMAIN 4: [Assigned by homology with 8CATA]B 437 to B 500 ; The following residues NOT assigned to any domain: Chain "B" 3 - 500
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1WGC A

LECTIN (AGGLUTININ) 03-APR-90 :: WHEAT GERM AGGLUTININ (ISOLECTIN 1) COMPLEX WITH

DOMAIN 1: [Assigned by homology with 9WGAA]A 2 to A 43 ; DOMAIN 2: [Assigned by homology with 9WGAA]A 44 to A 83 ; DOMAIN 3: [Assigned by homology with 9WGAA]A 84 to A 120 ; DOMAIN 4: [Assigned by homology with 9WGAA]A 121 to A 171 ; The following residues NOT assigned to any domain: Chain "A" 1 - 1 The following residues NOT assigned to any domain: Chain "A" 1 - 171
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

1WGC B

LECTIN (AGGLUTININ) 03-APR-90 :: WHEAT GERM AGGLUTININ (ISOLECTIN 1) COMPLEX WITH

DOMAIN 1: [Assigned by homology with 9WGAA]B 2 to B 43 ; DOMAIN 2: [Assigned by homology with 9WGAA]B 44 to B 83 ; DOMAIN 3: [Assigned by homology with 9WGAA]B 84 to B 120 ; DOMAIN 4: [Assigned by homology with 9WGAA]B 121 to B 171 ; The following residues NOT assigned to any domain: Chain "B" 1 - 171 The following residues NOT assigned to any domain: Chain "B" 1 - 1
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CWG A

PRELIMINARY 08-JAN-93 :: WHEAT GERM AGGLUTININ ISOLECTIN 1 COMPLEX WITH T5

DOMAIN 1: [Assigned by homology with 9WGAA]A 2 to A 43 ; DOMAIN 2: [Assigned by homology with 9WGAA]A 44 to A 83 ; DOMAIN 3: [Assigned by homology with 9WGAA]A 84 to A 120 ; DOMAIN 4: [Assigned by homology with 9WGAA]A 121 to A 171 ; The following residues NOT assigned to any domain: Chain "A" 176 - 183 The following residues NOT assigned to any domain: Chain "A" 2 - 171 The following residues NOT assigned to any domain: Chain "A" 476 - 478
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2CWG B

PRELIMINARY 08-JAN-93 :: WHEAT GERM AGGLUTININ ISOLECTIN 1 COMPLEX WITH T5

DOMAIN 1: [Assigned by homology with 9WGAA]B 2 to B 43 ; DOMAIN 2: [Assigned by homology with 9WGAA]B 44 to B 83 ; DOMAIN 3: [Assigned by homology with 9WGAA]B 84 to B 120 ; DOMAIN 4: [Assigned by homology with 9WGAA]B 121 to B 171 ; The following residues NOT assigned to any domain: Chain "B" 2 - 171 The following residues NOT assigned to any domain: Chain "B" 176 - 183 The following residues NOT assigned to any domain: Chain "B" 476 - 478
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7WGA A

LECTIN (AGGLUTININ) 03-APR-90 :: WHEAT GERM AGGLUTININ (ISOLECTIN 1)

DOMAIN 1: [Assigned by homology with 9WGAA]A 2 to A 43 ; DOMAIN 2: [Assigned by homology with 9WGAA]A 44 to A 83 ; DOMAIN 3: [Assigned by homology with 9WGAA]A 84 to A 120 ; DOMAIN 4: [Assigned by homology with 9WGAA]A 121 to A 171 ; The following residues NOT assigned to any domain: Chain "A" 1 - 1 The following residues NOT assigned to any domain: Chain "A" 1 - 171
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

7WGA B

LECTIN (AGGLUTININ) 03-APR-90 :: WHEAT GERM AGGLUTININ (ISOLECTIN 1)

DOMAIN 1: [Assigned by homology with 9WGAA]B 2 to B 43 ; DOMAIN 2: [Assigned by homology with 9WGAA]B 44 to B 83 ; DOMAIN 3: [Assigned by homology with 9WGAA]B 84 to B 120 ; DOMAIN 4: [Assigned by homology with 9WGAA]B 121 to B 171 ; The following residues NOT assigned to any domain: Chain "B" 1 - 171 The following residues NOT assigned to any domain: Chain "B" 1 - 1
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2WGC A

LECTIN (AGGLUTININ) 03-APR-90 :: WHEAT GERM AGGLUTININ (ISOLECTIN 2) COMPLEX WITH

DOMAIN 1: [Assigned by homology with 9WGAA]A 2 to A 43 ; DOMAIN 2: [Assigned by homology with 9WGAA]A 44 to A 83 ; DOMAIN 3: [Assigned by homology with 9WGAA]A 84 to A 120 ; DOMAIN 4: [Assigned by homology with 9WGAA]A 121 to A 171 ; The following residues NOT assigned to any domain: Chain "A" 1 - 1 The following residues NOT assigned to any domain: Chain "A" 1 - 171
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2WGC B

LECTIN (AGGLUTININ) 03-APR-90 :: WHEAT GERM AGGLUTININ (ISOLECTIN 2) COMPLEX WITH

DOMAIN 1: [Assigned by homology with 9WGAA]B 2 to B 43 ; DOMAIN 2: [Assigned by homology with 9WGAA]B 44 to B 83 ; DOMAIN 3: [Assigned by homology with 9WGAA]B 84 to B 120 ; DOMAIN 4: [Assigned by homology with 9WGAA]B 121 to B 171 ; The following residues NOT assigned to any domain: Chain "B" 1 - 171 The following residues NOT assigned to any domain: Chain "B" 1 - 1
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

9WGA B

LECTIN (AGGLUTININ) 20-APR-90 :: WHEAT GERM AGGLUTININ (ISOLECTIN 2)

DOMAIN 1: [Assigned by homology with 9WGAA]B 2 to B 43 ; DOMAIN 2: [Assigned by homology with 9WGAA]B 44 to B 83 ; DOMAIN 3: [Assigned by homology with 9WGAA]B 84 to B 120 ; DOMAIN 4: [Assigned by homology with 9WGAA]B 121 to B 171 ; The following residues NOT assigned to any domain: Chain "B" 1 - 171 The following residues NOT assigned to any domain: Chain "B" 1 - 1
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]
AUTHOR ASSIGNMENTS - 5 DOMAIN STRUCTURES

AUTHOR ASSIGNMENTS - 5 DOMAIN STRUCTURES


1GSG P

COMPLEX (LIGASE-T/RNA$) 03-APR-90 :: GLUTAMINYL-T/RNA$ SYNTHETASE (GLN/RS$) COMPLEX WIT

DOMAIN 1: P 8 to P 100 ; P 211 to P 260 ; DOMAIN 2: P 101 to P 210 ; DOMAIN 3: P 260 to P 339 ; DOMAIN 4: P 340 to P 348 ; P 465 to P 547 ; DOMAIN 5: P 349 to P 464 ; The following residues NOT assigned to any domain: Chain "P" 1 - 76
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]

2HSC

HYDROLASE(ACTING ON ACID ANHYDRIDES) 18-MAY-94 :: HEAT-SHOCK COGNATE 7OKD PROTEIN (44KD ATPASE N-TER

DOMAIN 1: 3 to 38 ; 116 to 175 ; 366 to 383 ; DOMAIN 2: 39 to 69 ; DOMAIN 3: 70 to 115 ; DOMAIN 4: 176 to 229 ; 308 to 365 ; DOMAIN 5: 230 to 307 ; The following residues NOT assigned to any domain: Chain " " 384 - 384
[PDB Header] [PREPI] [RASMOL] [NCBI ENTREZ] [SCOP]
AUTHOR ASSIGNMENTS - 6 DOMAIN STRUCTURES

AUTHOR ASSIGNMENTS - 6 DOMAIN STRUCTURES