HEADER OXYGEN TRANSPORT 07-MAR-79 1ECA 1ECA 3 COMPND HEMOGLOBIN (ERYTHROCRUORIN, AQUO MET) 1ECA 4 SOURCE (CHIRONOMOUS THUMMI THUMMI) (FRACTION III) 1ECA 5 AUTHOR W.STEIGEMANN,E.WEBER 1ECA 6 REVDAT 6 30-SEP-83 1ECAE 1 REVDAT 1ECAE 1 REVDAT 5 15-SEP-81 1ECAD 1 JRNL 1ECAE 2 REVDAT 4 20-APR-81 1ECAC 1 HELIX 1ECAE 3 REVDAT 3 07-MAY-80 1ECAB 1 REMARK 1ECAE 4 REVDAT 2 12-DEC-79 1ECAA 3 ATOM 1ECAE 5 REVDAT 1 05-JUL-79 1ECA 0 1ECAE 6 JRNL AUTH W.STEIGEMANN,E.WEBER 1ECA 7 JRNL TITL STRUCTURE OF ERYTHROCRUORIN IN DIFFERENT LIGAND 1ECA 8 JRNL TITL 2 STATES REFINED AT 1.4 ANGSTROMS RESOLUTION 1ECA 9 JRNL REF J.MOL.BIOL. V. 127 309 1979 1ECAD 1 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 1ECA 11 REMARK 1 1ECA 12 REMARK 1 REFERENCE 1 1ECA 13 REMARK 1 AUTH E.WEBER,W.STEIGEMANN,T.A.JONES,R.HUBER 1ECA 14 REMARK 1 TITL THE STRUCTURE OF OXY-*ERYTHROCRUORIN AT 1.4 1ECA 15 REMARK 1 TITL 2 ANGSTROMS RESOLUTION 1ECA 16 REMARK 1 REF J.MOL.BIOL. V. 120 327 1978 1ECAB 1 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1ECA 18 REMARK 1 REFERENCE 2 1ECA 19 REMARK 1 AUTH R.HUBER,O.EPP,W.STEIGEMANN,H.FORMANEK 1ECA 20 REMARK 1 TITL THE ATOMIC STRUCTURE OF ERYTHROCRUORIN IN THE LIGHT 1ECA 21 REMARK 1 TITL 2 OF THE CHEMICAL SEQUENCE AND ITS COMPARISON WITH 1ECA 22 REMARK 1 TITL 3 MYOGLOBIN 1ECA 23 REMARK 1 REF EUR.J.BIOCHEM. V. 19 42 1971 1ECA 24 REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 262 1ECA 25 REMARK 1 REFERENCE 3 1ECA 26 REMARK 1 AUTH R.HUBER,O.EPP,H.FORMANEK 1ECA 27 REMARK 1 TITL STRUCTURES OF DEOXY- AND CARBOMONOXY-ERYTHROCRUORIN 1ECA 28 REMARK 1 REF J.MOL.BIOL. V. 52 349 1970 1ECA 29 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1ECA 30 REMARK 2 1ECA 31 REMARK 2 RESOLUTION. 1.4 ANGSTROMS. 1ECA 32 REMARK 3 1ECA 33 REMARK 3 REFINEMENT. CYCLIC REAL-SPACE REFINEMENT WITH CHAIN 1ECA 34 REMARK 3 CONSTRAINT. SEE J.DEISENHOFER,W.STEIGEMANN, ACTA CRYST., 1ECA 35 REMARK 3 VOL. B31, P. 238, 1975. FREE TEMPERATURE FACTORS FOR 1ECA 36 REMARK 3 PROTEIN ATOMS, TEMPERATURE FACTORS AND OCCUPANCIES FOR 1ECA 37 REMARK 3 SOLVENT MOLECULES. 1ECA 38 REMARK 4 1ECA 39 REMARK 4 FOR OXYGEN TRANSPORT PROTEINS NORMALLY A RESIDUE 1ECA 40 REMARK 4 IDENTIFICATION SCHEME IS USED WHICH IS BASED ON THE 1ECA 41 REMARK 4 SECONDARY STRUCTURE. THIS SCHEME HAS ALSO BEEN APPLIED TO 1ECA 42 REMARK 4 THIS STRUCTURE. SINCE THE RESIDUES ARE NUMBERED 1ECA 43 REMARK 4 SEQUENTIALLY IN THE PROTEIN DATA BANK, THE FOLLOWING TABLE 1ECA 44 REMARK 4 GIVES THE RELATIONSHIP BETWEEN THESE TWO SCHEMES FOR THIS 1ECA 45 REMARK 4 STRUCTURE. 1ECA 46 REMARK 4 1ECA 47 REMARK 4 1 NA3 1ECA 48 REMARK 4 2 - 17 A1 - A16 1ECA 49 REMARK 4 18 AB1 1ECA 50 REMARK 4 19 - 30 B5 - B16 1ECA 51 REMARK 4 31 - 37 C1 - C7 1ECA 52 REMARK 4 38 - 44 CD1 - CD7 1ECA 53 REMARK 4 45 - 51 D1 - D7 1ECA 54 REMARK 4 52 - 71 E1 - E20 1ECA 55 REMARK 4 72 - 79 EF1 - EF8 1ECA 56 REMARK 4 80 - 88 F1 - F9 1ECA 57 REMARK 4 89 - 92 FG2 - FG5 1ECA 58 REMARK 4 93 - 111 G1 - G19 1ECA 59 REMARK 4 112 - 113 GH1 - GH2 1ECA 60 REMARK 4 114 - 115 GH5 - GH6 1ECA 61 REMARK 4 116 - 136 H2 - H22 1ECA 62 REMARK 5 1ECA 63 REMARK 5 ATOM CB OF RESIDUE ALA 115 (GH6) IS INVISIBLE IN THE 1ECA 64 REMARK 5 ELECTRON DENSITY. NO COORDINATES ARE GIVEN FOR THIS ATOM. 1ECA 65 REMARK 6 1ECAA 1 REMARK 6 CORRECTION. INSERT MISSING ALTERNATE LOCATION INDICATOR FOR 1ECAA 2 REMARK 6 ATOM OG OF SER 134. ALSO CORRECT OCCUPANCY AND REORDER 1ECAA 3 REMARK 6 TO MEET SPECIFICATIONS. 12-DEC-79. 1ECAA 4 REMARK 7 1ECAB 2 REMARK 7 CORRECTION. CORRECT FORMAT IN REFERENCE 1. 07-MAY-80. 1ECAB 3 REMARK 8 1ECAC 1 REMARK 8 CORRECTION. CORRECT RESIDUE IDENTIFICATION ON HELIX 8 1ECAC 2 REMARK 8 RECORD. 20-APR-81. 1ECAC 3 REMARK 9 1ECAD 2 REMARK 9 CORRECTION. CORRECT JOURNAL NAME ON JRNL REFERENCE. 1ECAD 3 REMARK 9 15-SEP-81. 1ECAD 4 REMARK 10 1ECAE 7 REMARK 10 CORRECTION. INSERT REVDAT RECORDS. 30-SEP-83. 1ECAE 8 SEQRES 1 136 LEU SER ALA ASP GLN ILE SER THR VAL GLN ALA SER PHE 1ECA 66 SEQRES 2 136 ASP LYS VAL LYS GLY ASP PRO VAL GLY ILE LEU TYR ALA 1ECA 67 SEQRES 3 136 VAL PHE LYS ALA ASP PRO SER ILE MET ALA LYS PHE THR 1ECA 68 SEQRES 4 136 GLN PHE ALA GLY LYS ASP LEU GLU SER ILE LYS GLY THR 1ECA 69 SEQRES 5 136 ALA PRO PHE GLU THR HIS ALA ASN ARG ILE VAL GLY PHE 1ECA 70 SEQRES 6 136 PHE SER LYS ILE ILE GLY GLU LEU PRO ASN ILE GLU ALA 1ECA 71 SEQRES 7 136 ASP VAL ASN THR PHE VAL ALA SER HIS LYS PRO ARG GLY 1ECA 72 SEQRES 8 136 VAL THR HIS ASP GLN LEU ASN ASN PHE ARG ALA GLY PHE 1ECA 73 SEQRES 9 136 VAL SER TYR MET LYS ALA HIS THR ASP PHE ALA GLY ALA 1ECA 74 SEQRES 10 136 GLU ALA ALA TRP GLY ALA THR LEU ASP THR PHE PHE GLY 1ECA 75 SEQRES 11 136 MET ILE PHE SER LYS MET 1ECA 76 FTNOTE 1 1ECA 77 FTNOTE 1 RESIDUE PRO 74 IS A CIS-PROLINE. 1ECA 78 FTNOTE 2 1ECA 79 FTNOTE 2 AN OCCUPANCY OF 0.0 DENOTES ATOMS THAT HAVE NOT BEEN 1ECA 80 FTNOTE 2 LOCALIZED IN THE ELECTRON DENSITY. 1ECA 81 HET HEM 1 44 PROTOPORPHYRIN IX WITH FE3+ AND WATER 1ECA 82 FORMUL 2 HEM C34 H32 N4 O4 FE1 +++ . 1ECA 83 FORMUL 2 HEM H2 O1 1ECA 84 FORMUL 3 HOH *94(H2 O1) 1ECA 85 HELIX 1 A SER 2 LYS 17 1 FROM SER 12 ON DISTORTED TO 5 1ECA 86 HELIX 2 B ASP 19 ASP 31 1 1ECA 87 HELIX 3 C ASP 31 PHE 38 5 1ECA 88 HELIX 4 D ASP 45 LYS 50 1 DISTORTION TO TYPE 5 1ECA 89 HELIX 5 E THR 52 GLU 72 1 1ECA 90 HELIX 6 F ILE 76 LYS 88 1 INCLUDES EF-REGION 1ECA 91 HELIX 7 FG HIS 87 GLY 91 5 1ECA 92 HELIX 8 G THR 93 THR 112 1 1ECAC 4 HELIX 9 H ALA 117 PHE 133 1 1ECA 94 CRYST1 54.300 54.300 35.600 90.00 90.00 120.00 P 32 3 1ECA 95 ORIGX1 1.000000 0.000000 0.000000 0.00000 1ECA 96 ORIGX2 0.000000 1.000000 0.000000 0.00000 1ECA 97 ORIGX3 0.000000 0.000000 1.000000 0.00000 1ECA 98 SCALE1 .018420 .010630 0.000000 0.00000 1ECA 99 SCALE2 0.000000 .021270 0.000000 0.00000 1ECA 100 SCALE3 0.000000 0.000000 .028090 0.00000 1ECA 101