HEADER HYDROLASE(O-GLYCOSYL) 17-MAY-94 1CEL 1CEL 2 COMPND 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE I (CELLULASE) 1CEL 3 COMPND 2 (E.C.3.2.1.91) 1CEL 4 SOURCE FUNGUS (TRICHODERMA REESEI) 1CEL 5 AUTHOR C.DIVNE,T.A.JONES 1CEL 6 REVDAT 1 01-NOV-94 1CEL 0 1CEL 7 JRNL AUTH C.DIVNE,J.STAHLBERG,T.REINIKAINEN,L.RUOHONEN, 1CEL 8 JRNL AUTH 2 G.PETTERSSON,J.K.C.KNOWLES,T.T.TEERI,T.A.JONES 1CEL 9 JRNL TITL THE THREE-DIMENSIONAL CRYSTAL STRUCTURE OF THE 1CEL 10 JRNL TITL 2 CATALYTIC CORE OF CELLOBIOHYDROLASE I FROM 1CEL 11 JRNL TITL 3 TRICHODERMA REESEI 1CEL 12 JRNL REF SCIENCE V. 265 524 1994 1CEL 13 JRNL REFN ASTM SCIEAS US ISSN 0036-8075 0038 1CEL 14 REMARK 1 1CEL 15 REMARK 1 REFERENCE 1 1CEL 16 REMARK 1 AUTH C.DIVNE,I.SINNING,J.STAHLBERG,G.PETTERSSON, 1CEL 17 REMARK 1 AUTH 2 M.BAILEY,M.SIIKA-AHO,E.MARGOLLES-CLARK,T.TEERI, 1CEL 18 REMARK 1 AUTH 3 T.A.JONES 1CEL 19 REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY STUDIES ON 1CEL 20 REMARK 1 TITL 2 THE CORE PROTEINS OF CELLOBIOHYDROLASE I AND 1CEL 21 REMARK 1 TITL 3 ENDOGLUCANASE I FROM TRICHODERMA REESEI 1CEL 22 REMARK 1 REF J.MOL.BIOL. V. 234 905 1993 1CEL 23 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070 1CEL 24 REMARK 2 1CEL 25 REMARK 2 RESOLUTION. 1.81 ANGSTROMS. 1CEL 26 REMARK 3 1CEL 27 REMARK 3 REFINEMENT. 1CEL 28 REMARK 3 PROGRAM X-PLOR 1CEL 29 REMARK 3 AUTHORS BRUNGER 1CEL 30 REMARK 3 R VALUE 0.181 1CEL 31 REMARK 3 RMSD BOND DISTANCES 0.008 ANGSTROMS 1CEL 32 REMARK 3 RMSD BOND ANGLES 1.7 DEGREES 1CEL 33 REMARK 3 RMSD DIHEDRAL ANGLES 27.2 DEGREES 1CEL 34 REMARK 3 RMSD IMPROPERS 1.4 DEGREES 1CEL 35 REMARK 3 1CEL 36 REMARK 3 NUMBER OF REFLECTIONS 63053 1CEL 37 REMARK 3 RESOLUTION RANGE 7.5 - 1.8 ANGSTROMS 1CEL 38 REMARK 3 DATA CUTOFF 2.0 SIGMA(F) 1CEL 39 REMARK 3 PERCENT COMPLETION 86.8 1CEL 40 REMARK 3 1CEL 41 REMARK 3 NUMBER OF PROTEIN ATOMS 6436 1CEL 42 REMARK 3 NUMBER OF NUCLEIC ACID ATOMS 0 1CEL 43 REMARK 3 NUMBER OF HETEROGEN ATOMS 69 1CEL 44 REMARK 3 NUMBER OF SOLVENT ATOMS 529 1CEL 45 REMARK 4 1CEL 46 REMARK 4 THE COORDINATES GIVEN DEFINE THE STRUCTURE OF ONLY THE 1CEL 47 REMARK 4 CATALYTIC DOMAIN OF CELLOBIOHYDROLASE I AND COMPRISES 1CEL 48 REMARK 4 RESIDUES 1 - 434 OF THE 497 RESIDUES IN THE MATURE PROTEIN. 1CEL 49 REMARK 4 THERE ARE TWO COPIES OF THE MOLECULE IN THE ASYMMETRIC UNIT 1CEL 50 REMARK 4 WITH CHAIN IDENTIFIERS A AND B. THE N-TERMINUS IN EACH 1CEL 51 REMARK 4 MOLECULE IS PROTECTED BY A PYROGLUTAMATE RESIDUE WHICH HAS 1CEL 52 REMARK 4 THE RESIDUE NAME PCA. 1CEL 53 REMARK 5 1CEL 54 REMARK 5 AN N-ACETYL-GLUCOSAMINE RESIDUE IS BOUND TO ASN 270 IN EACH 1CEL 55 REMARK 5 MOLECULE AND HAS THE RESIDUE NAME NAG. 1CEL 56 REMARK 6 1CEL 57 REMARK 6 A LIGAND O-IODO-BENZYL-1-THIO-B-D-GLUCOSE IS BOUND IN THE 1CEL 58 REMARK 6 ACTIVE SITE OF EACH MOLECULE AND HAS THE RESIDUE NAMES IBZ 1CEL 59 REMARK 6 AND GLC (I.E., IBZ FOR THE IODO-BENZYL GROUP AND GLC FOR 1CEL 60 REMARK 6 THE B-D-GLUCOSE UNIT). 1CEL 61 REMARK 7 1CEL 62 REMARK 7 THERE IS A CALCIUM (+II) ION COORDINATED BY GLU 295 AND GLU 1CEL 63 REMARK 7 325 FROM ONE MOLECULE (CHAIN A) AND GLU 295 AND GLU 325 1CEL 64 REMARK 7 FROM A NON-CRYSTALLOGRAPHICALLY RELATED B MOLECULE. IN 1CEL 65 REMARK 7 ADDITION, ONE WATER MOLECULE IS BOUND TO THE CALCIUM ION. 1CEL 66 REMARK 7 THE COORDINATION IS DISTORTED PENTAGONAL BIPYRAMIDAL. 1CEL 67 REMARK 8 1CEL 68 REMARK 8 THE PUTATIVE ACTIVE SITE RESIDUES ARE GLU 212, ASP 214, GLU 1CEL 69 REMARK 8 217, AND HIS 228 IN EACH MOLECULES. THESE ARE PRESENTED AS 1CEL 70 REMARK 8 SITES CTA AND CTB IN THIS ENTRY. 1CEL 71 REMARK 9 1CEL 72 REMARK 9 EACH CHAIN CONTAINS TWO LARGE ANTI-PARALLEL BETA SHEETS 1CEL 73 REMARK 9 THAT STACK FACE-TO-FACE TO FORM A BETA SANDWICH. EACH 1CEL 74 REMARK 9 SHEET IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN 1CEL 75 REMARK 9 THE SHEET RECORDS BELOW, TWO SHEETS ARE PRESENTED FOR EACH 1CEL 76 REMARK 9 SHEET WHICH HAVE ONE OR MORE IDENTICAL STRANDS. SHEET 1 1CEL 77 REMARK 9 OF THE SANDWICH IS PRESENTED AS SHEETS *A1A* AND *A1B* FOR 1CEL 78 REMARK 9 CHAIN A AND SHEETS *B1A* AND *B1B* FOR CHAIN B. SHEET 2 1CEL 79 REMARK 9 OF THE SANDWICH IS PRESENTED AS SHEETS *A2A* AND *A2B* FOR 1CEL 80 REMARK 9 CHAIN A AND SHEETS *B2A* AND *B2B* FOR CHAIN B. THE 1CEL 81 REMARK 9 FOLLOWING B-STRANDS ARE DISJOINT IN THE TWO SHEETS OF THE 1CEL 82 REMARK 9 B-SANDWICH: STRAND 2 OF SHEET 1 IS DISJOINT CONSISTING OF 1CEL 83 REMARK 9 TWO STRANDS (RESIDUES 24 - 26 AND RESIDUES 84 - 87) THAT 1CEL 84 REMARK 9 RUN IN OPPOSITE DIRECTIONS; STRAND 3 OF SHEET 1 IS 1CEL 85 REMARK 9 DISJOINT CONSISTING OF TWO STRANDS (RESIDUES 17 - 20 AND 1CEL 86 REMARK 9 RESIDUES 90 - 95) THAT RUN IN OPPOSITE DIRECTIONS; STRAND 1CEL 87 REMARK 9 8 OF SHEET 1 IS DISJOINT CONSISTING OF TWO STRANDS 1CEL 88 REMARK 9 (RESIDUES 309 - 313 AND RESIDUES 325 - 327) THAT RUN IN THE 1CEL 89 REMARK 9 SAME DIRECTION; STRAND 2 OF SHEET 2 IS DISJOINT CONSISTING 1CEL 90 REMARK 9 OF TWO STRANDS (RESIDUES 107 - 111 AND RESIDUES 119 - 121) 1CEL 91 REMARK 9 THAT RUN IN THE SAME DIRECTION. 1CEL 92 REMARK 10 1CEL 93 REMARK 10 SEQUENCE ADVISORY NOTICE 1CEL 94 REMARK 10 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. 1CEL 95 REMARK 10 1CEL 96 REMARK 10 SWISS-PROT ENTRY NAME: GUX1_TRIRE 1CEL 97 REMARK 10 1CEL 98 REMARK 10 SWISS-PROT RESIDUE PDB SEQRES 1CEL 99 REMARK 10 1CEL 100 REMARK 10 NAME NUMBER NAME CHAIN SEQ/INSERT CODE 1CEL 101 REMARK 10 GLN 18 PCA A 1 1CEL 102 REMARK 10 GLN 18 PCA B 1 1CEL 103 REMARK 11 1CEL 104 REMARK 11 THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL 1CEL 105 REMARK 11 YIELD APPROXIMATE COORDINATES FOR CHAIN *B* WHEN APPLIED TO 1CEL 106 REMARK 11 CHAIN *A*. 1CEL 107 SEQRES 1 A 434 PCA SER ALA CYS THR LEU GLN SER GLU THR HIS PRO PRO 1CEL 108 SEQRES 2 A 434 LEU THR TRP GLN LYS CYS SER SER GLY GLY THR CYS THR 1CEL 109 SEQRES 3 A 434 GLN GLN THR GLY SER VAL VAL ILE ASP ALA ASN TRP ARG 1CEL 110 SEQRES 4 A 434 TRP THR HIS ALA THR ASN SER SER THR ASN CYS TYR ASP 1CEL 111 SEQRES 5 A 434 GLY ASN THR TRP SER SER THR LEU CYS PRO ASP ASN GLU 1CEL 112 SEQRES 6 A 434 THR CYS ALA LYS ASN CYS CYS LEU ASP GLY ALA ALA TYR 1CEL 113 SEQRES 7 A 434 ALA SER THR TYR GLY VAL THR THR SER GLY ASN SER LEU 1CEL 114 SEQRES 8 A 434 SER ILE GLY PHE VAL THR GLN SER ALA GLN LYS ASN VAL 1CEL 115 SEQRES 9 A 434 GLY ALA ARG LEU TYR LEU MET ALA SER ASP THR THR TYR 1CEL 116 SEQRES 10 A 434 GLN GLU PHE THR LEU LEU GLY ASN GLU PHE SER PHE ASP 1CEL 117 SEQRES 11 A 434 VAL ASP VAL SER GLN LEU PRO CYS GLY LEU ASN GLY ALA 1CEL 118 SEQRES 12 A 434 LEU TYR PHE VAL SER MET ASP ALA ASP GLY GLY VAL SER 1CEL 119 SEQRES 13 A 434 LYS TYR PRO THR ASN THR ALA GLY ALA LYS TYR GLY THR 1CEL 120 SEQRES 14 A 434 GLY TYR CYS ASP SER GLN CYS PRO ARG ASP LEU LYS PHE 1CEL 121 SEQRES 15 A 434 ILE ASN GLY GLN ALA ASN VAL GLU GLY TRP GLU PRO SER 1CEL 122 SEQRES 16 A 434 SER ASN ASN ALA ASN THR GLY ILE GLY GLY HIS GLY SER 1CEL 123 SEQRES 17 A 434 CYS CYS SER GLU MET ASP ILE TRP GLU ALA ASN SER ILE 1CEL 124 SEQRES 18 A 434 SER GLU ALA LEU THR PRO HIS PRO CYS THR THR VAL GLY 1CEL 125 SEQRES 19 A 434 GLN GLU ILE CYS GLU GLY ASP GLY CYS GLY GLY THR TYR 1CEL 126 SEQRES 20 A 434 SER ASP ASN ARG TYR GLY GLY THR CYS ASP PRO ASP GLY 1CEL 127 SEQRES 21 A 434 CYS ASP TRP ASN PRO TYR ARG LEU GLY ASN THR SER PHE 1CEL 128 SEQRES 22 A 434 TYR GLY PRO GLY SER SER PHE THR LEU ASP THR THR LYS 1CEL 129 SEQRES 23 A 434 LYS LEU THR VAL VAL THR GLN PHE GLU THR SER GLY ALA 1CEL 130 SEQRES 24 A 434 ILE ASN ARG TYR TYR VAL GLN ASN GLY VAL THR PHE GLN 1CEL 131 SEQRES 25 A 434 GLN PRO ASN ALA GLU LEU GLY SER TYR SER GLY ASN GLU 1CEL 132 SEQRES 26 A 434 LEU ASN ASP ASP TYR CYS THR ALA GLU GLU ALA GLU PHE 1CEL 133 SEQRES 27 A 434 GLY GLY SER SER PHE SER ASP LYS GLY GLY LEU THR GLN 1CEL 134 SEQRES 28 A 434 PHE LYS LYS ALA THR SER GLY GLY MET VAL LEU VAL MET 1CEL 135 SEQRES 29 A 434 SER LEU TRP ASP ASP TYR TYR ALA ASN MET LEU TRP LEU 1CEL 136 SEQRES 30 A 434 ASP SER THR TYR PRO THR ASN GLU THR SER SER THR PRO 1CEL 137 SEQRES 31 A 434 GLY ALA VAL ARG GLY SER CYS SER THR SER SER GLY VAL 1CEL 138 SEQRES 32 A 434 PRO ALA GLN VAL GLU SER GLN SER PRO ASN ALA LYS VAL 1CEL 139 SEQRES 33 A 434 THR PHE SER ASN ILE LYS PHE GLY PRO ILE GLY SER THR 1CEL 140 SEQRES 34 A 434 GLY ASN PRO SER GLY 1CEL 141 SEQRES 1 B 434 PCA SER ALA CYS THR LEU GLN SER GLU THR HIS PRO PRO 1CEL 142 SEQRES 2 B 434 LEU THR TRP GLN LYS CYS SER SER GLY GLY THR CYS THR 1CEL 143 SEQRES 3 B 434 GLN GLN THR GLY SER VAL VAL ILE ASP ALA ASN TRP ARG 1CEL 144 SEQRES 4 B 434 TRP THR HIS ALA THR ASN SER SER THR ASN CYS TYR ASP 1CEL 145 SEQRES 5 B 434 GLY ASN THR TRP SER SER THR LEU CYS PRO ASP ASN GLU 1CEL 146 SEQRES 6 B 434 THR CYS ALA LYS ASN CYS CYS LEU ASP GLY ALA ALA TYR 1CEL 147 SEQRES 7 B 434 ALA SER THR TYR GLY VAL THR THR SER GLY ASN SER LEU 1CEL 148 SEQRES 8 B 434 SER ILE GLY PHE VAL THR GLN SER ALA GLN LYS ASN VAL 1CEL 149 SEQRES 9 B 434 GLY ALA ARG LEU TYR LEU MET ALA SER ASP THR THR TYR 1CEL 150 SEQRES 10 B 434 GLN GLU PHE THR LEU LEU GLY ASN GLU PHE SER PHE ASP 1CEL 151 SEQRES 11 B 434 VAL ASP VAL SER GLN LEU PRO CYS GLY LEU ASN GLY ALA 1CEL 152 SEQRES 12 B 434 LEU TYR PHE VAL SER MET ASP ALA ASP GLY GLY VAL SER 1CEL 153 SEQRES 13 B 434 LYS TYR PRO THR ASN THR ALA GLY ALA LYS TYR GLY THR 1CEL 154 SEQRES 14 B 434 GLY TYR CYS ASP SER GLN CYS PRO ARG ASP LEU LYS PHE 1CEL 155 SEQRES 15 B 434 ILE ASN GLY GLN ALA ASN VAL GLU GLY TRP GLU PRO SER 1CEL 156 SEQRES 16 B 434 SER ASN ASN ALA ASN THR GLY ILE GLY GLY HIS GLY SER 1CEL 157 SEQRES 17 B 434 CYS CYS SER GLU MET ASP ILE TRP GLU ALA ASN SER ILE 1CEL 158 SEQRES 18 B 434 SER GLU ALA LEU THR PRO HIS PRO CYS THR THR VAL GLY 1CEL 159 SEQRES 19 B 434 GLN GLU ILE CYS GLU GLY ASP GLY CYS GLY GLY THR TYR 1CEL 160 SEQRES 20 B 434 SER ASP ASN ARG TYR GLY GLY THR CYS ASP PRO ASP GLY 1CEL 161 SEQRES 21 B 434 CYS ASP TRP ASN PRO TYR ARG LEU GLY ASN THR SER PHE 1CEL 162 SEQRES 22 B 434 TYR GLY PRO GLY SER SER PHE THR LEU ASP THR THR LYS 1CEL 163 SEQRES 23 B 434 LYS LEU THR VAL VAL THR GLN PHE GLU THR SER GLY ALA 1CEL 164 SEQRES 24 B 434 ILE ASN ARG TYR TYR VAL GLN ASN GLY VAL THR PHE GLN 1CEL 165 SEQRES 25 B 434 GLN PRO ASN ALA GLU LEU GLY SER TYR SER GLY ASN GLU 1CEL 166 SEQRES 26 B 434 LEU ASN ASP ASP TYR CYS THR ALA GLU GLU ALA GLU PHE 1CEL 167 SEQRES 27 B 434 GLY GLY SER SER PHE SER ASP LYS GLY GLY LEU THR GLN 1CEL 168 SEQRES 28 B 434 PHE LYS LYS ALA THR SER GLY GLY MET VAL LEU VAL MET 1CEL 169 SEQRES 29 B 434 SER LEU TRP ASP ASP TYR TYR ALA ASN MET LEU TRP LEU 1CEL 170 SEQRES 30 B 434 ASP SER THR TYR PRO THR ASN GLU THR SER SER THR PRO 1CEL 171 SEQRES 31 B 434 GLY ALA VAL ARG GLY SER CYS SER THR SER SER GLY VAL 1CEL 172 SEQRES 32 B 434 PRO ALA GLN VAL GLU SER GLN SER PRO ASN ALA LYS VAL 1CEL 173 SEQRES 33 B 434 THR PHE SER ASN ILE LYS PHE GLY PRO ILE GLY SER THR 1CEL 174 SEQRES 34 B 434 GLY ASN PRO SER GLY 1CEL 175 FTNOTE 1 1CEL 176 FTNOTE 1 CIS PROLINE - PRO A 382 1CEL 177 FTNOTE 2 1CEL 178 FTNOTE 2 CIS PROLINE - PRO B 382 1CEL 179 HET NAG A 435 14 N-ACETYL-D-GLUCOSAMINE 1CEL 180 HET IBZ A 436 9 2-IODOBENZYLTHIO GROUP 1CEL 181 HET GLC A 437 11 GLUCOSE 1CEL 182 HET NAG B 435 14 N-ACETYL-D-GLUCOSAMINE 1CEL 183 HET IBZ B 436 9 2-IODOBENZYLTHIO GROUP 1CEL 184 HET GLC B 437 11 GLUCOSE 1CEL 185 HET CA 440 1 CALCIUM +2 COUNTER ION 1CEL 186 FORMUL 3 NAG 2(C8 H15 N1 O6) 1CEL 187 FORMUL 4 IBZ 2(C7 H6 I1 S1) 1CEL 188 FORMUL 5 GLC 2(C6 H12 O6) 1CEL 189 FORMUL 6 CA CA1 ++ 1CEL 190 FORMUL 7 HOH *529(H2 O1) 1CEL 191 HELIX 1 AA1 ASN A 64 ASN A 70 1 1CEL 192 HELIX 2 AA2 TYR A 78 TYR A 82 1 1CEL 193 HELIX 3 AA3 ASP A 328 PHE A 338 1 1CEL 194 HELIX 4 AA4 SER A 342 ASP A 345 1 1CEL 195 HELIX 5 AA5 GLY A 348 THR A 356 1 1CEL 196 HELIX 6 AA6 LEU A 375 ASP A 378 1 1CEL 197 HELIX 7 AA7 PRO A 404 GLN A 410 1 1CEL 198 HELIX 8 AG1 ALA A 36 TRP A 38 5 1CEL 199 HELIX 9 AG2 ALA A 165 TYR A 167 5 1CEL 200 HELIX 10 AG3 ASP A 241 CYS A 243 5 1CEL 201 HELIX 11 BA1 ASN B 64 ASN B 70 1 1CEL 202 HELIX 12 BA2 TYR B 78 TYR B 82 1 1CEL 203 HELIX 13 BA3 ASP B 328 PHE B 338 1 1CEL 204 HELIX 14 BA4 SER B 342 ASP B 345 1 1CEL 205 HELIX 15 BA5 GLY B 348 THR B 356 1 1CEL 206 HELIX 16 BA6 LEU B 375 ASP B 378 1 1CEL 207 HELIX 17 BA7 PRO B 404 GLN B 410 1 1CEL 208 HELIX 18 BG1 ALA B 36 TRP B 38 5 1CEL 209 HELIX 19 BG2 ALA B 165 TYR B 167 5 1CEL 210 HELIX 20 BG3 ASP B 241 CYS B 243 5 1CEL 211 SHEET 1 A1A 8 PRO A 12 TRP A 16 0 1CEL 212 SHEET 2 A1A 8 VAL A 84 GLY A 88 1 O GLY A 88 N THR A 15 1CEL 213 SHEET 3 A1A 8 SER A 90 PHE A 95 -1 N SER A 92 O THR A 85 1CEL 214 SHEET 4 A1A 8 ALA A 414 GLY A 424 -1 N VAL A 416 O ILE A 93 1CEL 215 SHEET 5 A1A 8 ASN A 125 ASP A 132 -1 N ASP A 130 O SER A 419 1CEL 216 SHEET 6 A1A 8 LEU A 288 GLU A 295 -1 N THR A 292 O PHE A 127 1CEL 217 SHEET 7 A1A 8 ALA A 299 ASN A 307 -1 N ASN A 301 O GLN A 293 1CEL 218 SHEET 8 A1A 8 VAL A 309 GLN A 313 -1 N PHE A 311 O TYR A 304 1CEL 219 SHEET 1 A1B 7 THR A 24 THR A 26 0 1CEL 220 SHEET 2 A1B 7 GLN A 17 SER A 20 -1 N SER A 20 O THR A 24 1CEL 221 SHEET 3 A1B 7 ALA A 414 GLY A 424 1 O PHE A 423 N CYS A 19 1CEL 222 SHEET 4 A1B 7 ASN A 125 ASP A 132 -1 N ASP A 130 O SER A 419 1CEL 223 SHEET 5 A1B 7 LEU A 288 GLU A 295 -1 N THR A 292 O PHE A 127 1CEL 224 SHEET 6 A1B 7 ALA A 299 ASN A 307 -1 N ASN A 301 O GLN A 293 1CEL 225 SHEET 7 A1B 7 GLU A 325 ASN A 327 -1 N LEU A 326 O ILE A 300 1CEL 226 SHEET 1 A2A 7 GLN A 27 ASP A 35 0 1CEL 227 SHEET 2 A2A 7 ARG A 107 MET A 111 -1 O TYR A 109 N VAL A 33 1CEL 228 SHEET 3 A2A 7 MET A 360 TRP A 367 -1 O MET A 364 N LEU A 108 1CEL 229 SHEET 4 A2A 7 ASN A 141 SER A 148 -1 N TYR A 145 O VAL A 363 1CEL 230 SHEET 5 A2A 7 SER A 211 ASN A 219 -1 N TRP A 216 O LEU A 144 1CEL 231 SHEET 6 A2A 7 SER A 222 HIS A 228 -1 N THR A 226 O ASP A 214 1CEL 232 SHEET 7 A2A 7 CYS A 261 TRP A 263 -1 N CYS A 261 O PRO A 227 1CEL 233 SHEET 1 A2B 6 GLU A 119 THR A 121 0 1CEL 234 SHEET 2 A2B 6 MET A 360 TRP A 367 -1 O MET A 360 N PHE A 120 1CEL 235 SHEET 3 A2B 6 ASN A 141 SER A 148 -1 N TYR A 145 O VAL A 363 1CEL 236 SHEET 4 A2B 6 SER A 211 ASN A 219 -1 N TRP A 216 O LEU A 144 1CEL 237 SHEET 5 A2B 6 SER A 222 HIS A 228 -1 N THR A 226 O ASP A 214 1CEL 238 SHEET 6 A2B 6 CYS A 261 TRP A 263 -1 N CYS A 261 O PRO A 227 1CEL 239 SHEET 1 B1A 8 PRO B 12 TRP B 16 0 1CEL 240 SHEET 2 B1A 8 VAL B 84 GLY B 88 1 O GLY B 88 N THR B 15 1CEL 241 SHEET 3 B1A 8 SER B 90 PHE B 95 -1 N SER B 92 O THR B 85 1CEL 242 SHEET 4 B1A 8 ALA B 414 GLY B 424 -1 N VAL B 416 O ILE B 93 1CEL 243 SHEET 5 B1A 8 ASN B 125 ASP B 132 -1 N ASP B 130 O SER B 419 1CEL 244 SHEET 6 B1A 8 LEU B 288 GLU B 295 -1 N THR B 292 O PHE B 127 1CEL 245 SHEET 7 B1A 8 ALA B 299 ASN B 307 -1 N ASN B 301 O GLN B 293 1CEL 246 SHEET 8 B1A 8 VAL B 309 GLN B 313 -1 N PHE B 311 O TYR B 304 1CEL 247 SHEET 1 B1B 7 THR B 24 THR B 26 0 1CEL 248 SHEET 2 B1B 7 GLN B 17 SER B 20 -1 N SER B 20 O THR B 24 1CEL 249 SHEET 3 B1B 7 ALA B 414 GLY B 424 1 O PHE B 423 N CYS B 19 1CEL 250 SHEET 4 B1B 7 ASN B 125 ASP B 132 -1 N ASP B 130 O SER B 419 1CEL 251 SHEET 5 B1B 7 LEU B 288 GLU B 295 -1 N THR B 292 O PHE B 127 1CEL 252 SHEET 6 B1B 7 ALA B 299 ASN B 307 -1 N ASN B 301 O GLN B 293 1CEL 253 SHEET 7 B1B 7 GLU B 325 ASN B 327 -1 N LEU B 326 O ILE B 300 1CEL 254 SHEET 1 B2A 7 GLN B 27 ASP B 35 0 1CEL 255 SHEET 2 B2A 7 ARG B 107 MET B 111 -1 O TYR B 109 N VAL B 33 1CEL 256 SHEET 3 B2A 7 MET B 360 TRP B 367 -1 O MET B 364 N LEU B 108 1CEL 257 SHEET 4 B2A 7 ASN B 141 SER B 148 -1 N TYR B 145 O VAL B 363 1CEL 258 SHEET 5 B2A 7 SER B 211 ASN B 219 -1 N TRP B 216 O LEU B 144 1CEL 259 SHEET 6 B2A 7 SER B 222 HIS B 228 -1 N THR B 226 O ASP B 214 1CEL 260 SHEET 7 B2A 7 CYS B 261 TRP B 263 -1 N CYS B 261 O PRO B 227 1CEL 261 SHEET 1 B2B 6 GLU B 119 THR B 121 0 1CEL 262 SHEET 2 B2B 6 MET B 360 TRP B 367 -1 O MET B 360 N PHE B 120 1CEL 263 SHEET 3 B2B 6 ASN B 141 SER B 148 -1 N TYR B 145 O VAL B 363 1CEL 264 SHEET 4 B2B 6 SER B 211 ASN B 219 -1 N TRP B 216 O LEU B 144 1CEL 265 SHEET 5 B2B 6 SER B 222 HIS B 228 -1 N THR B 226 O ASP B 214 1CEL 266 SHEET 6 B2B 6 CYS B 261 TRP B 263 -1 N CYS B 261 O PRO B 227 1CEL 267 TURN 1 A1 SER A 20 GLY A 23 TYPE I (III) 1CEL 268 TURN 2 A2 ALA A 43 SER A 46 TYPE I 1CEL 269 TURN 3 A3 ASP A 52 THR A 55 TYPE IV (II') 1CEL 270 TURN 4 AI1 ALA A 76 TYR A 78 TYPE INVERSE GAMMA BEND 1CEL 271 TURN 5 A4 SER A 87 SER A 90 TYPE II' 1CEL 272 TURN 6 A5 SER A 113 THR A 116 TYPE I 1CEL 273 TURN 7 A6 LEU A 122 ASN A 125 TYPE II 1CEL 274 TURN 8 A7 VAL A 133 GLN A 135 TYPE I 1CEL 275 TURN 9 A8 PRO A 137 LEU A 140 TYPE II 1CEL 276 TURN 10 AI2 VAL A 147 MET A 149 TYPE INVERSE GAMMA BEND 1CEL 277 TURN 11 A9 ASP A 150 GLY A 153 TYPE I 1CEL 278 TURN 12 A10 GLY A 154 LYS A 157 TYPE III (I) 1CEL 279 TURN 13 A11 TYR A 158 ASN A 161 TYPE I (III) 1CEL 280 TURN 14 A12 ASP A 173 CYS A 176 TYPE I (III) 1CEL 281 TURN 15 A13 ILE A 183 GLN A 186 TYPE I' (III') 1CEL 282 TURN 16 A14 VAL A 189 TRP A 192 TYPE II 1CEL 283 TURN 17 A15 ASN A 198 THR A 201 TYPE I 1CEL 284 TURN 18 A16 GLY A 245 SER A 248 TYPE I 1CEL 285 TURN 19 A17 ASN A 250 GLY A 253 TYPE I 1CEL 286 TURN 20 A18 TYR A 266 GLY A 269 TYPE I 1CEL 287 TURN 21 AI3 GLY A 269 THR A 271 TYPE INVERSE GAMMA BEND 1CEL 288 TURN 22 A19 ASN A 270 PHE A 273 TYPE I 1CEL 289 TURN 23 A20 GLY A 277 PHE A 280 TYPE I 1CEL 290 TURN 24 A21 ASP A 283 LYS A 286 TYPE I (III) 1CEL 291 TURN 25 A22 GLU A 295 GLY A 298 TYPE III (I) 1CEL 292 TURN 26 A23 GLN A 306 VAL A 309 TYPE I' 1CEL 293 TURN 27 A24 LEU A 318 TYR A 321 TYPE II' 1CEL 294 TURN 28 AI4 GLU A 325 ASN A 327 TYPE INVERSE GAMMA BEND 1CEL 295 TURN 29 A25 ALA A 372 LEU A 375 TYPE III' (I') 1CEL 296 TURN 30 A26 PRO A 382 GLU A 385 TYPE I (III) 1CEL 297 TURN 31 A27 THR A 386 THR A 389 TYPE III (I) 1CEL 298 TURN 32 A28 THR A 389 ALA A 392 TYPE II 1CEL 299 TURN 33 A29 SER A 398 SER A 401 TYPE I 1CEL 300 TURN 34 A30 SER A 411 ALA A 414 TYPE I 1CEL 301 TURN 35 A31 PRO A 425 SER A 428 TYPE II 1CEL 302 TURN 36 A32 SER A 428 ASN A 431 TYPE I 1CEL 303 TURN 37 B1 SER B 20 GLY B 23 TYPE I (III) 1CEL 304 TURN 38 B2 ALA B 43 SER B 46 TYPE I 1CEL 305 TURN 39 B3 ASP B 52 THR B 55 TYPE IV (II') 1CEL 306 TURN 40 BI1 ALA B 76 TYR B 78 TYPE INVERSE GAMMA BEND 1CEL 307 TURN 41 B4 SER B 87 SER B 90 TYPE II' 1CEL 308 TURN 42 B5 SER B 113 THR B 116 TYPE I 1CEL 309 TURN 43 B6 LEU B 122 ASN B 125 TYPE II 1CEL 310 TURN 44 B7 VAL B 133 GLN B 135 TYPE I 1CEL 311 TURN 45 B8 PRO B 137 LEU B 140 TYPE II 1CEL 312 TURN 46 BI2 VAL B 147 MET B 149 TYPE INVERSE GAMMA BEND 1CEL 313 TURN 47 B9 ASP B 150 GLY B 153 TYPE I 1CEL 314 TURN 48 B10 GLY B 154 LYS B 157 TYPE III (I) 1CEL 315 TURN 49 B11 TYR B 158 ASN B 161 TYPE I (III) 1CEL 316 TURN 50 B12 ASP B 173 CYS B 176 TYPE I (III) 1CEL 317 TURN 51 B13 ILE B 183 GLN B 186 TYPE I' (III') 1CEL 318 TURN 52 B14 VAL B 189 TRP B 192 TYPE II 1CEL 319 TURN 53 B15 ASN B 198 THR B 201 TYPE I 1CEL 320 TURN 54 B16 GLY B 245 SER B 248 TYPE I 1CEL 321 TURN 55 B17 ASN B 250 GLY B 253 TYPE I 1CEL 322 TURN 56 B18 TYR B 266 GLY B 269 TYPE I 1CEL 323 TURN 57 BI3 GLY B 269 THR B 271 TYPE INVERSE GAMMA BEND 1CEL 324 TURN 58 B19 ASN B 270 PHE B 273 TYPE I 1CEL 325 TURN 59 B20 GLY B 277 PHE B 280 TYPE I 1CEL 326 TURN 60 B21 ASP B 283 LYS B 286 TYPE I (III) 1CEL 327 TURN 61 B22 GLU B 295 GLY B 298 TYPE III (I) 1CEL 328 TURN 62 B23 GLN B 306 VAL B 309 TYPE I' 1CEL 329 TURN 63 B24 LEU B 318 TYR B 321 TYPE II' 1CEL 330 TURN 64 BI4 GLU B 325 ASN B 327 TYPE INVERSE GAMMA BEND 1CEL 331 TURN 65 B25 ALA B 372 LEU B 375 TYPE III' (I') 1CEL 332 TURN 66 B26 PRO B 382 GLU B 385 TYPE I (III) 1CEL 333 TURN 67 B27 THR B 386 THR B 389 TYPE III (I) 1CEL 334 TURN 68 B28 THR B 389 ALA B 392 TYPE II 1CEL 335 TURN 69 B29 SER B 398 SER B 401 TYPE I 1CEL 336 TURN 70 B30 SER B 411 ALA B 414 TYPE I 1CEL 337 TURN 71 B31 PRO B 425 SER B 428 TYPE II 1CEL 338 TURN 72 B32 SER B 428 ASN B 431 TYPE I 1CEL 339 SSBOND 1 CYS A 4 CYS A 72 1CEL 340 SSBOND 2 CYS A 19 CYS A 25 1CEL 341 SSBOND 3 CYS A 50 CYS A 71 1CEL 342 SSBOND 4 CYS A 61 CYS A 67 1CEL 343 SSBOND 5 CYS A 138 CYS A 397 1CEL 344 SSBOND 6 CYS A 172 CYS A 210 1CEL 345 SSBOND 7 CYS A 176 CYS A 209 1CEL 346 SSBOND 8 CYS A 230 CYS A 256 1CEL 347 SSBOND 9 CYS A 238 CYS A 243 1CEL 348 SSBOND 10 CYS A 261 CYS A 331 1CEL 349 SSBOND 11 CYS B 4 CYS B 72 1CEL 350 SSBOND 12 CYS B 19 CYS B 25 1CEL 351 SSBOND 13 CYS B 50 CYS B 71 1CEL 352 SSBOND 14 CYS B 61 CYS B 67 1CEL 353 SSBOND 15 CYS B 138 CYS B 397 1CEL 354 SSBOND 16 CYS B 172 CYS B 210 1CEL 355 SSBOND 17 CYS B 176 CYS B 209 1CEL 356 SSBOND 18 CYS B 230 CYS B 256 1CEL 357 SSBOND 19 CYS B 238 CYS B 243 1CEL 358 SSBOND 20 CYS B 261 CYS B 331 1CEL 359 SITE 1 CTA 4 GLU A 212 ASP A 214 GLU A 217 HIS A 228 1CEL 360 SITE 1 CAA 5 GLU A 295 GLU A 325 GLU B 295 GLU B 325 1CEL 361 SITE 2 CAA 5 HOH 441 1CEL 362 SITE 1 CTB 4 GLU B 212 ASP B 214 GLU B 217 HIS B 228 1CEL 363 CRYST1 84.000 86.200 111.800 90.00 90.00 90.00 P 21 21 2 8 1CEL 364 ORIGX1 1.000000 0.000000 0.000000 0.00000 1CEL 365 ORIGX2 0.000000 1.000000 0.000000 0.00000 1CEL 366 ORIGX3 0.000000 0.000000 1.000000 0.00000 1CEL 367 SCALE1 0.011905 0.000000 0.000000 0.00000 1CEL 368 SCALE2 0.000000 0.011601 0.000000 0.00000 1CEL 369 SCALE3 0.000000 0.000000 0.008945 0.00000 1CEL 370 MTRIX1 1 1.000000 0.000000 0.000000 -38.09200 1 1CEL 371 MTRIX2 1 0.000000 1.000000 0.000000 -43.10800 1 1CEL 372 MTRIX3 1 0.000000 0.000000 1.000000 -56.39300 1 1CEL 373