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HEADER LIPASE 08-FEB-95 1CLE 1CLE 2
COMPND MOL_ID: 1; 1CLE 3
COMPND 2 MOLECULE: CHOLESTEROL ESTERASE; 1CLE 4
COMPND 3 CHAIN: A, B; 1CLE 5
COMPND 4 HETEROGEN: CHOLESTERYL LINOLEATE 1CLE 6
SOURCE MOL_ID: 1; 1CLE 7
SOURCE 2 ORGANISM_SCIENTIFIC: CANDIDA CYLINDRACEA 1CLE 8
KEYWDS ESTERASE, SUBSTRATE/PRODUCT-BOUND 1CLE 9
EXPDTA X-RAY DIFFRACTION 1CLE 10
AUTHOR D.GHOSH 1CLE 11
REVDAT 1 08-MAR-96 1CLE 0 1CLE 12
JRNL AUTH D.GHOSH,Z.WAWRZAK,V.Z.PLETNEV,N.LI,R.KAISER, 1CLE 13
JRNL AUTH 2 W.PANGBORN,H.JORNVALL,M.ERMAN,W.L.DUAX 1CLE 14
JRNL TITL STRUCTURE OF UNCOMPLEXED AND LINOLEATE-BOUND 1CLE 15
JRNL TITL 2 CANDIDA CYLINDRACEA CHOLESTEROL ESTERASE 1CLE 16
JRNL REF TO BE PUBLISHED REF NOW ASSIGNED AS 1CLE 17
JRNL REFN 0353 1CLE 18
REMARK 1 1CLE 19
REMARK 1 REFERENCE 1 1CLE 20
REMARK 1 AUTH R.KAISER,M.ERMAN,W.L.DUAX,D.GHOSH,H.JORNVALL 1CLE 21
REMARK 1 TITL MONOMERIC AND DIMERIC FORMS OF CHOLESTEROL ESTERASE 1CLE 22
REMARK 1 TITL 2 FROM CANDIDA CYLINDRACEA: PRIMARY STRUCTURE, 1CLE 23
REMARK 1 TITL 3 IDENTITY IN PEPTIDE PATTERNS, AND ADDITIONAL 1CLE 24
REMARK 1 TITL 4 MICROHETEROGENEITY 1CLE 25
REMARK 1 REF FEBS LETT. V. 337 123 1994 1CLE 26
REMARK 1 REFN ASTM FEBLAL NE ISSN 0014-5793 0165 1CLE 27
REMARK 1 REFERENCE 2 1CLE 28
REMARK 1 AUTH D.GHOSH,M.ERMAN,W.L.DUAX 1CLE 29
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY DIFFRACTION 1CLE 30
REMARK 1 TITL 2 ANALYSIS OF CHOLESTEROL ESTERASE FROM CANDIDA 1CLE 31
REMARK 1 TITL 3 CYLINDRACEA 1CLE 32
REMARK 1 REF J.STEROID BIOCHEM.MOL.BIOL. V. 38 663 1991 1CLE 33
REMARK 1 REFN ASTM JSBBEZ UK ISSN 0960-0760 2046 1CLE 34
REMARK 2 1CLE 35
REMARK 2 RESOLUTION. 2.00 ANGSTROMS. 1CLE 36
REMARK 3 1CLE 37
REMARK 3 REFINEMENT. 1CLE 38
REMARK 3 PROGRAM X-PLOR 3.1 1CLE 39
REMARK 3 AUTHORS BRUNGER 1CLE 40
REMARK 3 R VALUE 0.149 1CLE 41
REMARK 3 MEAN B VALUE 20.5 ANGSTROMS**2 1CLE 42
REMARK 3 ESTIMATED COORD. ERROR 0.18 ANGSTROMS 1CLE 43
REMARK 3 RMSD BOND DISTANCES 0.010 ANGSTROMS 1CLE 44
REMARK 3 RMSD BOND ANGLES 1.56 DEGREES 1CLE 45
REMARK 3 RMSD DIHEDRAL ANGLES 24.1 DEGREES 1CLE 46
REMARK 3 RMSD IMPROPER ANGLES 1.39 DEGREES 1CLE 47
REMARK 3 1CLE 48
REMARK 3 NUMBER OF REFLECTIONS 54351 1CLE 49
REMARK 3 RESOLUTION RANGE 8.0 - 2.00 ANGSTROMS 1CLE 50
REMARK 3 DATA CUTOFF 1. SIGMA(F) 1CLE 51
REMARK 3 1CLE 52
REMARK 3 DATA COLLECTION. 1CLE 53
REMARK 3 NUMBER OF UNIQUE REFLECTIONS 119382 1CLE 54
REMARK 3 COMPLETENESS OF DATA 88. % 1CLE 55
REMARK 3 REJECTION CRITERIA 1. SIGMA(I) 1CLE 56
REMARK 3 1CLE 57
REMARK 3 NUMBER OF ATOMS USED IN REFINEMENT. 1CLE 58
REMARK 3 NUMBER OF PROTEIN ATOMS 8074 1CLE 59
REMARK 3 NUMBER OF NUCLEIC ACID ATOMS 0 1CLE 60
REMARK 3 NUMBER OF HETEROGEN ATOMS 188 1CLE 61
REMARK 3 NUMBER OF SOLVENT ATOMS 478 1CLE 62
REMARK 5 1CLE 63
REMARK 5 SITE 1CLE 64
REMARK 5 SITE_IDENTIFIER: CA 1CLE 65
REMARK 5 ONE TRIAD IN EACH MONOMER. 1CLE 66
REMARK 6 1CLE 67
REMARK 6 HET GROUP TRIVIAL NAME: CHOLESTERYL LINOLEATE 1CLE 68
REMARK 6 CAS REGISTRY NUMBER: [604-33-1] 1CLE 69
REMARK 6 EMPIRICAL FORMULA: C45 H76 O2 1CLE 70
REMARK 6 CHARGE: UNCHARGED 1CLE 71
REMARK 6 ADDITIONAL COMMENTS: ALTHOUGH THIS SUBSTRATE WAS MODELED AS 1CLE 72
REMARK 6 THE INTACT CHOLESTERYL LINOLEATE, IT IS LIKELY THAT THE 1CLE 73
REMARK 6 ACTUAL COMPOSITION MAY BE A MIXTURE OF THE INTACT SUBSTRATE 1CLE 74
REMARK 6 CHOLESTERYL LINOLEATE AND PRODUCT LINOLEIC ACID. 1CLE 75
REMARK 18 1CLE 76
REMARK 18 EXPERIMENTAL DETAILS. 1CLE 77
REMARK 18 DATE OF DATA COLLECTION : 1993 1CLE 78
REMARK 18 MONOCHROMATIC (Y/N) : Y 1CLE 79
REMARK 18 LAUE (Y/N) : N 1CLE 80
REMARK 18 WAVELENGTH OR RANGE (A) : 1.54 1CLE 81
REMARK 18 DETECTOR TYPE : R-AXISIIC IMAGE PLATE 1CLE 82
REMARK 18 DETECTOR MANUFACTURER : RIGAKU 1CLE 83
REMARK 18 INTENSITY-INTEGRATION SOFTWARE : RIGAKU 1CLE 84
REMARK 18 DATA REDUNDANCY : 1.9 1CLE 85
REMARK 18 MERGING R VALUE (INTENSITY) : 0.069 1CLE 86
REMARK 19 1CLE 87
REMARK 19 SOLVENT CONTENT (VS) : 45. % 1CLE 88
REMARK 999 1CLE 89
REMARK 999 BASED ON THE ELECTRON DENSITY, THE AUTHORS BELIEVE THAT 1CLE 90
REMARK 999 RESIDUE 344 IS VAL. 1CLE 91
DBREF 1CLE A 1 534 SWS P32947 LIP3_CANRU 16 549 1CLE 92
DBREF 1CLE B 1 534 SWS P32947 LIP3_CANRU 16 549 1CLE 93
SEQADV 1CLE VAL A 344 SWS P32947 ILE 359 CONFLICT 1CLE 94
SEQADV 1CLE VAL B 344 SWS P32947 ILE 359 CONFLICT 1CLE 95
SEQRES 1 A 534 ALA PRO THR ALA LYS LEU ALA ASN GLY ASP THR ILE THR 1CLE 96
SEQRES 2 A 534 GLY LEU ASN ALA ILE ILE ASN GLU ALA PHE LEU GLY ILE 1CLE 97
SEQRES 3 A 534 PRO PHE ALA GLU PRO PRO VAL GLY ASN LEU ARG PHE LYS 1CLE 98
SEQRES 4 A 534 ASP PRO VAL PRO TYR SER GLY SER LEU ASN GLY GLN LYS 1CLE 99
SEQRES 5 A 534 PHE THR SER TYR GLY PRO SER CYS MET GLN GLN ASN PRO 1CLE 100
SEQRES 6 A 534 GLU GLY THR PHE GLU GLU ASN LEU GLY LYS THR ALA LEU 1CLE 101
SEQRES 7 A 534 ASP LEU VAL MET GLN SER LYS VAL PHE GLN ALA VAL LEU 1CLE 102
SEQRES 8 A 534 PRO GLN SER GLU ASP CYS LEU THR ILE ASN VAL VAL ARG 1CLE 103
SEQRES 9 A 534 PRO PRO GLY THR LYS ALA GLY ALA ASN LEU PRO VAL MET 1CLE 104
SEQRES 10 A 534 LEU TRP ILE PHE GLY GLY GLY PHE GLU ILE GLY SER PRO 1CLE 105
SEQRES 11 A 534 THR ILE PHE PRO PRO ALA GLN MET VAL THR LYS SER VAL 1CLE 106
SEQRES 12 A 534 LEU MET GLY LYS PRO ILE ILE HIS VAL ALA VAL ASN TYR 1CLE 107
SEQRES 13 A 534 ARG VAL ALA SER TRP GLY PHE LEU ALA GLY ASP ASP ILE 1CLE 108
SEQRES 14 A 534 LYS ALA GLU GLY SER GLY ASN ALA GLY LEU LYS ASP GLN 1CLE 109
SEQRES 15 A 534 ARG LEU GLY MET GLN TRP VAL ALA ASP ASN ILE ALA GLY 1CLE 110
SEQRES 16 A 534 PHE GLY GLY ASP PRO SER LYS VAL THR ILE PHE GLY GLU 1CLE 111
SEQRES 17 A 534 SER ALA GLY SER MET SER VAL LEU CYS HIS LEU ILE TRP 1CLE 112
SEQRES 18 A 534 ASN ASP GLY ASP ASN THR TYR LYS GLY LYS PRO LEU PHE 1CLE 113
SEQRES 19 A 534 ARG ALA GLY ILE MET GLN SER GLY ALA MET VAL PRO SER 1CLE 114
SEQRES 20 A 534 ASP PRO VAL ASP GLY THR TYR GLY ASN GLU ILE TYR ASP 1CLE 115
SEQRES 21 A 534 LEU PHE VAL SER SER ALA GLY CYS GLY SER ALA SER ASP 1CLE 116
SEQRES 22 A 534 LYS LEU ALA CYS LEU ARG SER ALA SER SER ASP THR LEU 1CLE 117
SEQRES 23 A 534 LEU ASP ALA THR ASN ASN THR PRO GLY PHE LEU ALA TYR 1CLE 118
SEQRES 24 A 534 SER SER LEU ARG LEU SER TYR LEU PRO ARG PRO ASP GLY 1CLE 119
SEQRES 25 A 534 LYS ASN ILE THR ASP ASP MET TYR LYS LEU VAL ARG ASP 1CLE 120
SEQRES 26 A 534 GLY LYS TYR ALA SER VAL PRO VAL ILE ILE GLY ASP GLN 1CLE 121
SEQRES 27 A 534 ASN ASP GLU GLY THR VAL PHE GLY LEU SER SER LEU ASN 1CLE 122
SEQRES 28 A 534 VAL THR THR ASN ALA GLN ALA ARG ALA TYR PHE LYS GLN 1CLE 123
SEQRES 29 A 534 SER PHE ILE HIS ALA SER ASP ALA GLU ILE ASP THR LEU 1CLE 124
SEQRES 30 A 534 MET ALA ALA TYR PRO GLN ASP ILE THR GLN GLY SER PRO 1CLE 125
SEQRES 31 A 534 PHE ASP THR GLY ILE PHE ASN ALA ILE THR PRO GLN PHE 1CLE 126
SEQRES 32 A 534 LYS ARG ILE SER ALA VAL LEU GLY ASP LEU ALA PHE ILE 1CLE 127
SEQRES 33 A 534 HIS ALA ARG ARG TYR PHE LEU ASN HIS PHE GLN GLY GLY 1CLE 128
SEQRES 34 A 534 THR LYS TYR SER PHE LEU SER LYS GLN LEU SER GLY LEU 1CLE 129
SEQRES 35 A 534 PRO ILE MET GLY THR PHE HIS ALA ASN ASP ILE VAL TRP 1CLE 130
SEQRES 36 A 534 GLN ASP TYR LEU LEU GLY SER GLY SER VAL ILE TYR ASN 1CLE 131
SEQRES 37 A 534 ASN ALA PHE ILE ALA PHE ALA THR ASP LEU ASP PRO ASN 1CLE 132
SEQRES 38 A 534 THR ALA GLY LEU LEU VAL ASN TRP PRO LYS TYR THR SER 1CLE 133
SEQRES 39 A 534 SER SER GLN SER GLY ASN ASN LEU MET MET ILE ASN ALA 1CLE 134
SEQRES 40 A 534 LEU GLY LEU TYR THR GLY LYS ASP ASN PHE ARG THR ALA 1CLE 135
SEQRES 41 A 534 GLY TYR ASP ALA LEU MET THR ASN PRO SER SER PHE PHE 1CLE 136
SEQRES 42 A 534 VAL 1CLE 137
SEQRES 1 B 534 ALA PRO THR ALA LYS LEU ALA ASN GLY ASP THR ILE THR 1CLE 138
SEQRES 2 B 534 GLY LEU ASN ALA ILE ILE ASN GLU ALA PHE LEU GLY ILE 1CLE 139
SEQRES 3 B 534 PRO PHE ALA GLU PRO PRO VAL GLY ASN LEU ARG PHE LYS 1CLE 140
SEQRES 4 B 534 ASP PRO VAL PRO TYR SER GLY SER LEU ASN GLY GLN LYS 1CLE 141
SEQRES 5 B 534 PHE THR SER TYR GLY PRO SER CYS MET GLN GLN ASN PRO 1CLE 142
SEQRES 6 B 534 GLU GLY THR PHE GLU GLU ASN LEU GLY LYS THR ALA LEU 1CLE 143
SEQRES 7 B 534 ASP LEU VAL MET GLN SER LYS VAL PHE GLN ALA VAL LEU 1CLE 144
SEQRES 8 B 534 PRO GLN SER GLU ASP CYS LEU THR ILE ASN VAL VAL ARG 1CLE 145
SEQRES 9 B 534 PRO PRO GLY THR LYS ALA GLY ALA ASN LEU PRO VAL MET 1CLE 146
SEQRES 10 B 534 LEU TRP ILE PHE GLY GLY GLY PHE GLU ILE GLY SER PRO 1CLE 147
SEQRES 11 B 534 THR ILE PHE PRO PRO ALA GLN MET VAL THR LYS SER VAL 1CLE 148
SEQRES 12 B 534 LEU MET GLY LYS PRO ILE ILE HIS VAL ALA VAL ASN TYR 1CLE 149
SEQRES 13 B 534 ARG VAL ALA SER TRP GLY PHE LEU ALA GLY ASP ASP ILE 1CLE 150
SEQRES 14 B 534 LYS ALA GLU GLY SER GLY ASN ALA GLY LEU LYS ASP GLN 1CLE 151
SEQRES 15 B 534 ARG LEU GLY MET GLN TRP VAL ALA ASP ASN ILE ALA GLY 1CLE 152
SEQRES 16 B 534 PHE GLY GLY ASP PRO SER LYS VAL THR ILE PHE GLY GLU 1CLE 153
SEQRES 17 B 534 SER ALA GLY SER MET SER VAL LEU CYS HIS LEU ILE TRP 1CLE 154
SEQRES 18 B 534 ASN ASP GLY ASP ASN THR TYR LYS GLY LYS PRO LEU PHE 1CLE 155
SEQRES 19 B 534 ARG ALA GLY ILE MET GLN SER GLY ALA MET VAL PRO SER 1CLE 156
SEQRES 20 B 534 ASP PRO VAL ASP GLY THR TYR GLY ASN GLU ILE TYR ASP 1CLE 157
SEQRES 21 B 534 LEU PHE VAL SER SER ALA GLY CYS GLY SER ALA SER ASP 1CLE 158
SEQRES 22 B 534 LYS LEU ALA CYS LEU ARG SER ALA SER SER ASP THR LEU 1CLE 159
SEQRES 23 B 534 LEU ASP ALA THR ASN ASN THR PRO GLY PHE LEU ALA TYR 1CLE 160
SEQRES 24 B 534 SER SER LEU ARG LEU SER TYR LEU PRO ARG PRO ASP GLY 1CLE 161
SEQRES 25 B 534 LYS ASN ILE THR ASP ASP MET TYR LYS LEU VAL ARG ASP 1CLE 162
SEQRES 26 B 534 GLY LYS TYR ALA SER VAL PRO VAL ILE ILE GLY ASP GLN 1CLE 163
SEQRES 27 B 534 ASN ASP GLU GLY THR VAL PHE GLY LEU SER SER LEU ASN 1CLE 164
SEQRES 28 B 534 VAL THR THR ASN ALA GLN ALA ARG ALA TYR PHE LYS GLN 1CLE 165
SEQRES 29 B 534 SER PHE ILE HIS ALA SER ASP ALA GLU ILE ASP THR LEU 1CLE 166
SEQRES 30 B 534 MET ALA ALA TYR PRO GLN ASP ILE THR GLN GLY SER PRO 1CLE 167
SEQRES 31 B 534 PHE ASP THR GLY ILE PHE ASN ALA ILE THR PRO GLN PHE 1CLE 168
SEQRES 32 B 534 LYS ARG ILE SER ALA VAL LEU GLY ASP LEU ALA PHE ILE 1CLE 169
SEQRES 33 B 534 HIS ALA ARG ARG TYR PHE LEU ASN HIS PHE GLN GLY GLY 1CLE 170
SEQRES 34 B 534 THR LYS TYR SER PHE LEU SER LYS GLN LEU SER GLY LEU 1CLE 171
SEQRES 35 B 534 PRO ILE MET GLY THR PHE HIS ALA ASN ASP ILE VAL TRP 1CLE 172
SEQRES 36 B 534 GLN ASP TYR LEU LEU GLY SER GLY SER VAL ILE TYR ASN 1CLE 173
SEQRES 37 B 534 ASN ALA PHE ILE ALA PHE ALA THR ASP LEU ASP PRO ASN 1CLE 174
SEQRES 38 B 534 THR ALA GLY LEU LEU VAL ASN TRP PRO LYS TYR THR SER 1CLE 175
SEQRES 39 B 534 SER SER GLN SER GLY ASN ASN LEU MET MET ILE ASN ALA 1CLE 176
SEQRES 40 B 534 LEU GLY LEU TYR THR GLY LYS ASP ASN PHE ARG THR ALA 1CLE 177
SEQRES 41 B 534 GLY TYR ASP ALA LEU MET THR ASN PRO SER SER PHE PHE 1CLE 178
SEQRES 42 B 534 VAL 1CLE 179
FTNOTE 1 1CLE 180
FTNOTE 1 CIS PROLINE - PRO A 390 1CLE 181
FTNOTE 2 1CLE 182
FTNOTE 2 CIS PROLINE - PRO B 390 1CLE 183
HET NAG A 535 14 N-ACETYL-D-GLUCOSAMINE 1CLE 184
HET NAG A 537 14 N-ACETYL-D-GLUCOSAMINE 1CLE 185
HET NAG A 538 14 N-ACETYL-D-GLUCOSAMINE 1CLE 186
HET PO4 A 601 5 PHOSPHATE ION 1CLE 187
HET CLL A 801 47 CHOLESTERYL LINOLEATE 1CLE 188
HET NAG B 535 14 N-ACETYL-D-GLUCOSAMINE 1CLE 189
HET NAG B 537 14 N-ACETYL-D-GLUCOSAMINE 1CLE 190
HET NAG B 538 14 N-ACETYL-D-GLUCOSAMINE 1CLE 191
HET PO4 B 601 5 PHOSPHATE ION 1CLE 192
HET CLL B 802 47 CHOLESTERYL LINOLEATE 1CLE 193
FORMUL 3 NAG 6(C8 H15 N1 O6) 1CLE 194
FORMUL 4 PO4 2(O4 P1 3-) 1CLE 195
FORMUL 5 CLL 2(C45 H76 O2) 1CLE 196
FORMUL 6 HOH *478(H2 O1) 1CLE 197
HELIX 1 1 GLY A 34 LEU A 36 5 1CLE 198
HELIX 2 2 LEU A 73 MET A 82 1 1CLE 199
HELIX 3 3 LYS A 85 VAL A 90 1 1CLE 200
HELIX 4 4 PRO A 130 ILE A 132 5 1CLE 201
HELIX 5 5 ALA A 136 LEU A 144 1 1CLE 202
HELIX 6 6 ALA A 159 PHE A 163 1 1CLE 203
HELIX 7 7 ASP A 167 GLU A 172 1 1CLE 204
HELIX 8 8 ALA A 177 PHE A 196 1 1CLE 205
HELIX 9 9 SER A 209 GLY A 224 5 1CLE 206
HELIX 10 10 THR A 253 ALA A 266 1 1CLE 207
HELIX 11 11 LYS A 274 ARG A 279 1 1CLE 208
HELIX 12 12 SER A 283 ASN A 292 1 1CLE 209
HELIX 13 13 MET A 319 ARG A 324 1 1CLE 210
HELIX 14 14 GLU A 341 THR A 343 5 1CLE 211
HELIX 15 15 PHE A 345 SER A 349 5 1CLE 212
HELIX 16 16 ASN A 355 SER A 365 1 1CLE 213
HELIX 17 17 ASP A 371 ALA A 380 1 1CLE 214
HELIX 18 18 PHE A 403 ALA A 414 1 1CLE 215
HELIX 19 19 ILE A 416 HIS A 425 1 1CLE 216
HELIX 20 20 ASN A 451 ASP A 457 1 1CLE 217
HELIX 21 21 SER A 462 TYR A 467 5 1CLE 218
HELIX 22 22 ASN A 469 ASP A 477 1 1CLE 219
HELIX 23 23 PRO A 480 ALA A 483 5 1CLE 220
HELIX 24 24 THR A 519 MET A 526 1 1CLE 221
HELIX 25 25 PRO A 529 PHE A 532 5 1CLE 222
HELIX 26 26 GLY B 34 LEU B 36 5 1CLE 223
HELIX 27 27 LEU B 73 GLN B 83 1 1CLE 224
HELIX 28 28 LYS B 85 VAL B 90 1 1CLE 225
HELIX 29 29 PRO B 130 ILE B 132 5 1CLE 226
HELIX 30 30 ALA B 136 LEU B 144 1 1CLE 227
HELIX 31 31 ALA B 159 PHE B 163 1 1CLE 228
HELIX 32 32 ASP B 167 GLU B 172 1 1CLE 229
HELIX 33 33 ALA B 177 PHE B 196 1 1CLE 230
HELIX 34 34 SER B 209 GLY B 224 5 1CLE 231
HELIX 35 35 THR B 253 SER B 265 1 1CLE 232
HELIX 36 36 LYS B 274 LEU B 278 1 1CLE 233
HELIX 37 37 SER B 283 ASN B 292 1 1CLE 234
HELIX 38 38 MET B 319 ARG B 324 1 1CLE 235
HELIX 39 39 THR B 343 SER B 349 1 1CLE 236
HELIX 40 40 ASN B 355 SER B 365 1 1CLE 237
HELIX 41 41 ASP B 371 ALA B 380 1 1CLE 238
HELIX 42 42 ILE B 385 GLN B 387 5 1CLE 239
HELIX 43 43 PHE B 403 ALA B 414 1 1CLE 240
HELIX 44 44 ILE B 416 HIS B 425 1 1CLE 241
HELIX 45 45 ASN B 451 ASP B 457 1 1CLE 242
HELIX 46 46 SER B 462 TYR B 467 5 1CLE 243
HELIX 47 47 ASN B 469 ASP B 477 1 1CLE 244
HELIX 48 48 PRO B 480 ALA B 483 5 1CLE 245
HELIX 49 49 THR B 519 MET B 526 1 1CLE 246
HELIX 50 50 PRO B 529 PHE B 532 5 1CLE 247
SHEET 1 A 2 THR A 3 LYS A 5 0 1CLE 248
SHEET 2 A 2 THR A 11 THR A 13 -1 N ILE A 12 O ALA A 4 1CLE 249
SHEET 1 B10 ASN A 20 PHE A 23 0 1CLE 250
SHEET 2 B10 ILE A 100 PRO A 105 -1 N ARG A 104 O GLU A 21 1CLE 251
SHEET 3 B10 ILE A 149 VAL A 154 -1 N ALA A 153 O ASN A 101 1CLE 252
SHEET 4 B10 PRO A 115 ILE A 120 1 N PRO A 115 O ILE A 150 1CLE 253
SHEET 5 B10 VAL A 203 GLU A 208 1 N THR A 204 O VAL A 116 1CLE 254
SHEET 6 B10 ALA A 236 GLN A 240 1 N ALA A 236 O ILE A 205 1CLE 255
SHEET 7 B10 PRO A 332 GLN A 338 1 N PRO A 332 O GLY A 237 1CLE 256
SHEET 8 B10 LYS A 431 SER A 436 1 N TYR A 432 O VAL A 333 1CLE 257
SHEET 9 B10 LEU A 502 ILE A 505 1 N MET A 503 O LEU A 435 1CLE 258
SHEET 10 B10 LEU A 510 GLY A 513 -1 N GLY A 513 O LEU A 502 1CLE 259
SHEET 1 C 2 THR B 3 LYS B 5 0 1CLE 260
SHEET 2 C 2 THR B 11 THR B 13 -1 N ILE B 12 O ALA B 4 1CLE 261
SHEET 1 D10 GLU B 21 PHE B 23 0 1CLE 262
SHEET 2 D10 ILE B 100 ARG B 104 -1 N ARG B 104 O GLU B 21 1CLE 263
SHEET 3 D10 ILE B 149 VAL B 154 -1 N ALA B 153 O ASN B 101 1CLE 264
SHEET 4 D10 PRO B 115 ILE B 120 1 N PRO B 115 O ILE B 150 1CLE 265
SHEET 5 D10 VAL B 203 GLU B 208 1 N THR B 204 O VAL B 116 1CLE 266
SHEET 6 D10 ALA B 236 GLN B 240 1 N ALA B 236 O ILE B 205 1CLE 267
SHEET 7 D10 PRO B 332 GLN B 338 1 N PRO B 332 O GLY B 237 1CLE 268
SHEET 8 D10 LYS B 431 SER B 436 1 N TYR B 432 O VAL B 333 1CLE 269
SHEET 9 D10 LEU B 502 ASN B 506 1 N MET B 503 O LEU B 435 1CLE 270
SHEET 10 D10 GLY B 509 GLY B 513 -1 N GLY B 513 O LEU B 502 1CLE 271
SSBOND 1 CYS A 60 CYS A 97 1CLE 272
SSBOND 2 CYS A 268 CYS A 277 1CLE 273
SSBOND 3 CYS B 60 CYS B 97 1CLE 274
SSBOND 4 CYS B 268 CYS B 277 1CLE 275
SITE 1 CAT 6 SER A 209 GLU A 341 HIS A 449 SER B 209 1CLE 276
SITE 2 CAT 6 GLU B 341 HIS B 449 1CLE 277
CRYST1 58.790 90.920 58.790 93.39 105.74 97.22 P 1 2 1CLE 278
ORIGX1 1.000000 0.000000 0.000000 0.00000 1CLE 279
ORIGX2 0.000000 1.000000 0.000000 0.00000 1CLE 280
ORIGX3 0.000000 0.000000 1.000000 0.00000 1CLE 281
SCALE1 0.017010 0.002155 0.005028 0.00000 1CLE 282
SCALE2 0.000000 0.011087 0.001088 0.00000 1CLE 283
SCALE3 0.000000 0.000000 0.017757 0.00000 1CLE 284 |