HEADER BETA-AMYLASE 08-JUN-93 1TML 1TML 2 COMPND ENDO-1,4-BETA-D-GLUCANASE (E.C.3.2.1.4) 1TML 3 SOURCE (THERMOMONOSPORA FUSCA, STRAIN YX) EXPRESSED IN 1TML 4 SOURCE 2 (STREPTOMYCES LIVIDANS) 1TML 5 AUTHOR M.SPEZIO,D.B.WILSON,P.A.KARPLUS 1TML 6 REVDAT 1 31-JAN-94 1TML 0 1TML 7 JRNL AUTH M.SPEZIO,D.B.WILSON,P.A.KARPLUS 1TML 8 JRNL TITL CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF A 1TML 9 JRNL TITL 2 THERMOPHILIC ENDOCELLULASE 1TML 10 JRNL REF BIOCHEMISTRY V. 32 9906 1993 1TML 11 JRNL REFN ASTM BICHAW US ISSN 0006-2960 033 1TML 12 REMARK 1 1TML 13 REMARK 1 REFERENCE 1 1TML 14 REMARK 1 AUTH M.SPEZIO,D.B.WILSON,P.A.KARPLUS 1TML 15 REMARK 1 TITL CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF A 1TML 16 REMARK 1 TITL 2 THERMOPHILIC ENDOCELLULASE 1TML 17 REMARK 1 REF TO BE PUBLISHED 1TML 18 REMARK 1 REFN 353 1TML 19 REMARK 2 1TML 20 REMARK 2 RESOLUTION. 1.8 ANGSTROMS. 1TML 21 REMARK 3 1TML 22 REMARK 3 REFINEMENT. 1TML 23 REMARK 3 PROGRAM X-PLOR 1TML 24 REMARK 3 AUTHORS BRUNGER 1TML 25 REMARK 3 R VALUE 0.184 1TML 26 REMARK 3 RMSD BOND DISTANCES 0.014 ANGSTROMS 1TML 27 REMARK 3 RMSD BOND ANGLES 2.8 DEGREES 1TML 28 REMARK 3 1TML 29 REMARK 3 NUMBER OF PROTEIN ATOMS 2140 1TML 30 REMARK 3 NUMBER OF SOLVENT ATOMS 73 1TML 31 REMARK 4 1TML 32 REMARK 4 ALL NON-GLYCINE RESIDUES FALL WITHIN THE FAVORABLE REGIONS 1TML 33 REMARK 4 OF A RAMACHANDRAN PLOT EXCEPT FOR ASP - 2, HIS - 83, AND 1TML 34 REMARK 4 TRP - 162. 1TML 35 REMARK 5 1TML 36 REMARK 5 MODEL INCLUDES: 286 PROTEIN RESIDUES, 73 WATER MOLECULES 1TML 37 REMARK 5 AND 1 SULFATE. 1TML 38 REMARK 6 1TML 39 REMARK 6 THE TRUE C-TERMINUS IS NOT KNOWN. IF THE PROTEIN EXTENDS 1TML 40 REMARK 6 BEYOND ALA - 286, THE ADDITIONAL RESIDUES ARE DISORDERED 1TML 41 REMARK 6 AND ARE NOT SEEN IN ELECTRON DENSITY MAPS. 1TML 42 REMARK 7 1TML 43 REMARK 7 THE SHEET PRESENTED AS *COR* ON SHEET RECORDS BELOW IS 1TML 44 REMARK 7 ACTUALLY AN EIGHT STRANDED BETA-BARREL. THIS IS 1TML 45 REMARK 7 REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST 1TML 46 REMARK 7 AND LAST STRANDS ARE IDENTICAL. IN ADDITION, STRAND 1 IS 1TML 47 REMARK 7 BIFURCATED THUS THE BARREL IS REPRESENTED BY TWO SETS OF 1TML 48 REMARK 7 SHEET RECORDS *COR* AND *BOR* WHERE STRANDS 2, 3, 4, 5, 6, 1TML 49 REMARK 7 7, AND 8 ARE IDENTICAL. 1TML 50 REMARK 8 1TML 51 REMARK 8 D1 AND F1 OF THE HELIX ARE SMALL AND ARE NOT EXACTLY 1TML 52 REMARK 8 CONSERVED BETWEEN THIS STRUCTURE AND CELLOBIOHYDROLASE II. 1TML 53 REMARK 9 1TML 54 REMARK 9 SEQUENCE ADVISORY NOTICE: 1TML 55 REMARK 9 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. 1TML 56 REMARK 9 1TML 57 REMARK 9 SWISS-PROT ENTRY NAME: GUN2_THEFU 1TML 58 REMARK 9 1TML 59 REMARK 9 SWISS-PROT RESIDUE PDB ATOM RECORDS 1TML 60 REMARK 9 NAME NUMBER NAME CHAIN SEQ/INSERT CODE 1TML 61 REMARK 9 SER 162 TRP 162 1TML 62 REMARK 9 ASP 163 HIS 163 1TML 63 REMARK 9 GLN 166 ALA 166 1TML 64 SEQRES 1 286 ASN ASP SER PRO PHE TYR VAL ASN PRO ASN MET SER SER 1TML 65 SEQRES 2 286 ALA GLU TRP VAL ARG ASN ASN PRO ASN ASP PRO ARG THR 1TML 66 SEQRES 3 286 PRO VAL ILE ARG ASP ARG ILE ALA SER VAL PRO GLN GLY 1TML 67 SEQRES 4 286 THR TRP PHE ALA HIS HIS ASN PRO GLY GLN ILE THR GLY 1TML 68 SEQRES 5 286 GLN VAL ASP ALA LEU MET SER ALA ALA GLN ALA ALA GLY 1TML 69 SEQRES 6 286 LYS ILE PRO ILE LEU VAL VAL TYR ASN ALA PRO GLY ARG 1TML 70 SEQRES 7 286 ASP CYS GLY ASN HIS SER SER GLY GLY ALA PRO SER HIS 1TML 71 SEQRES 8 286 SER ALA TYR ARG SER TRP ILE ASP GLU PHE ALA ALA GLY 1TML 72 SEQRES 9 286 LEU LYS ASN ARG PRO ALA TYR ILE ILE VAL GLU PRO ASP 1TML 73 SEQRES 10 286 LEU ILE SER LEU MET SER SER CYS MET GLN HIS VAL GLN 1TML 74 SEQRES 11 286 GLN GLU VAL LEU GLU THR MET ALA TYR ALA GLY LYS ALA 1TML 75 SEQRES 12 286 LEU LYS ALA GLY SER SER GLN ALA ARG ILE TYR PHE ASP 1TML 76 SEQRES 13 286 ALA GLY HIS SER ALA TRP HIS SER PRO ALA GLN MET ALA 1TML 77 SEQRES 14 286 SER TRP LEU GLN GLN ALA ASP ILE SER ASN SER ALA HIS 1TML 78 SEQRES 15 286 GLY ILE ALA THR ASN THR SER ASN TYR ARG TRP THR ALA 1TML 79 SEQRES 16 286 ASP GLU VAL ALA TYR ALA LYS ALA VAL LEU SER ALA ILE 1TML 80 SEQRES 17 286 GLY ASN PRO SER LEU ARG ALA VAL ILE ASP THR SER ARG 1TML 81 SEQRES 18 286 ASN GLY ASN GLY PRO ALA GLY ASN GLU TRP CYS ASP PRO 1TML 82 SEQRES 19 286 SER GLY ARG ALA ILE GLY THR PRO SER THR THR ASN THR 1TML 83 SEQRES 20 286 GLY ASP PRO MET ILE ASP ALA PHE LEU TRP ILE LYS LEU 1TML 84 SEQRES 21 286 PRO GLY GLU ALA ASP GLY CYS ILE ALA GLY ALA GLY GLN 1TML 85 SEQRES 22 286 PHE VAL PRO GLN ALA ALA TYR GLU MET ALA ILE ALA ALA 1TML 86 FTNOTE 1 1TML 87 FTNOTE 1 RESIDUES ASN 1 AND ASP 2 ARE NOT WELL ORDERED AND HAVE VERY 1TML 88 FTNOTE 1 WEAK ELECTRON DENSITY. 1TML 89 FTNOTE 2 1TML 90 FTNOTE 2 RESIDUE TRP 162, IN THE ACTIVE SITE CLEFT, IS WELL ORDERED 1TML 91 FTNOTE 2 AND HAS STRONG DENSITY EVEN THOUGH ITS MAIN CHAIN TORSION 1TML 92 FTNOTE 2 ANGLES ARE OUTSIDE THE FAVORABLE REGIONS OF A RAMACHANDRAN 1TML 93 FTNOTE 2 PLOT. 1TML 94 HET SO4 360 5 SULFATE 1TML 95 FORMUL 2 SO4 O4 S1 1TML 96 FORMUL 3 HOH *73(H2 O1) 1TML 97 HELIX 1 A SER 12 ASN 19 1 1TML 98 HELIX 2 B THR 26 ARG 32 1 1TML 99 HELIX 3 C PRO 47 ALA 64 1 1TML 100 HELIX 4 D HIS 91 ALA 103 1 1TML 101 HELIX 5 E GLN 127 GLY 147 1 1TML 102 HELIX 6 F PRO 165 GLN 174 1 1TML 103 HELIX 7 G THR 194 ILE 208 1 1TML 104 HELIX 8 H PRO 276 ILE 284 1 1TML 105 HELIX 9 D1 LEU 118 MET 122 1 1TML 106 HELIX 10 F1 ILE 177 SER 180 1 1TML 107 SHEET 1 COR 9 PRO 4 TYR 6 0 1TML 108 SHEET 2 COR 9 ILE 67 VAL 72 1 1TML 109 SHEET 3 COR 9 TYR 111 VAL 114 1 1TML 110 SHEET 4 COR 9 ARG 152 ASP 156 1 1TML 111 SHEET 5 COR 9 GLY 183 THR 186 1 1TML 112 SHEET 6 COR 9 ARG 214 ASP 218 1 1TML 113 SHEET 7 COR 9 ILE 252 TRP 257 1 1TML 114 SHEET 8 COR 9 SER 243 THR 245 -1 1TML 115 SHEET 9 COR 9 PRO 4 TYR 6 -1 1TML 116 SHEET 1 BOR 9 GLN 38 PHE 42 0 1TML 117 SHEET 2 BOR 9 ILE 67 VAL 72 1 1TML 118 SHEET 3 BOR 9 TYR 111 VAL 114 1 1TML 119 SHEET 4 BOR 9 ARG 152 ASP 156 1 1TML 120 SHEET 5 BOR 9 GLY 183 THR 186 1 1TML 121 SHEET 6 BOR 9 ARG 214 ASP 218 1 1TML 122 SHEET 7 BOR 9 ILE 252 TRP 257 1 1TML 123 SHEET 8 BOR 9 SER 243 THR 245 -1 1TML 124 SHEET 9 BOR 9 GLN 38 PHE 42 -1 1TML 125 SSBOND 1 CYS 80 CYS 125 1TML 126 SSBOND 2 CYS 232 CYS 267 1TML 127 CRYST1 43.350 65.940 43.410 90.00 90.00 90.00 P 21 2 1TML 128 ORIGX1 1.000000 0.000000 0.000000 0.00000 1TML 129 ORIGX2 0.000000 1.000000 0.000000 0.00000 1TML 130 ORIGX3 0.000000 0.000000 1.000000 0.00000 1TML 131 SCALE1 0.023068 0.000000 0.000000 0.00000 1TML 132 SCALE2 0.000000 0.015165 0.000000 0.00000 1TML 133 SCALE3 0.000000 0.000000 0.023036 0.00000 1TML 134