HEADER VIRAL PROTEIN 19-MAR-18 6CS1
TITLE SARS SPIKE GLYCOPROTEIN, TRYPSIN-CLEAVED, STABILIZED VARIANT, TWO S1
TITLE 2 CTDS IN AN UPWARDS CONFORMATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SPIKE GLYCOPROTEIN,FIBRITIN;
COMPND 3 CHAIN: B, C, A;
COMPND 4 SYNONYM: S GLYCOPROTEIN,E2,PEPLOMER PROTEIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN SARS CORONAVIRUS, ENTEROBACTERIA PHAGE
SOURCE 3 T4;
SOURCE 4 ORGANISM_COMMON: SARS-COV, BACTERIOPHAGE T4;
SOURCE 5 ORGANISM_TAXID: 227859, 10665;
SOURCE 6 GENE: S, 2, WAC, T4TP161;
SOURCE 7 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293F;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS MEMBRANE FUSION, GLYCOPROTEIN, RECEPTOR BINDING, VIRAL PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR R.N.KIRCHDOERFER,N.WANG,J.PALLESEN,H.L.TURNER,C.A.COTTRELL,
AUTHOR 2 J.S.MCLELLAN,A.B.WARD
REVDAT 6 29-JUL-20 6CS1 1 COMPND REMARK HETNAM LINK
REVDAT 6 2 1 SITE ATOM
REVDAT 5 18-DEC-19 6CS1 1 SCALE
REVDAT 4 20-FEB-19 6CS1 1 REMARK
REVDAT 3 12-DEC-18 6CS1 1 JRNL
REVDAT 2 25-APR-18 6CS1 1 COMPND SOURCE DBREF SEQADV
REVDAT 1 11-APR-18 6CS1 0
JRNL AUTH R.N.KIRCHDOERFER,N.WANG,J.PALLESEN,D.WRAPP,H.L.TURNER,
JRNL AUTH 2 C.A.COTTRELL,K.S.CORBETT,B.S.GRAHAM,J.S.MCLELLAN,A.B.WARD
JRNL TITL STABILIZED CORONAVIRUS SPIKES ARE RESISTANT TO
JRNL TITL 2 CONFORMATIONAL CHANGES INDUCED BY RECEPTOR RECOGNITION OR
JRNL TITL 3 PROTEOLYSIS.
JRNL REF SCI REP V. 8 15701 2018
JRNL REFN ESSN 2045-2322
JRNL PMID 30356097
JRNL DOI 10.1038/S41598-018-34171-7
REMARK 2
REMARK 2 RESOLUTION. 4.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : LEGINON, GCTF, COOT, PHENIX, RELION,
REMARK 3 RELION, RELION, RELION
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : 5I08
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 4.600
REMARK 3 NUMBER OF PARTICLES : 15314
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 6CS1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAR-18.
REMARK 100 THE DEPOSITION ID IS D_1000232999.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : SARS SPIKE GLYCOPROTEIN,TRYPSIN
REMARK 245 -CLEAVED, STABILIZED VARIANT
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.35
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.50
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 2200.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 2.70
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 65.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 29000
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, A, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L, M, N, O, P, Q, R, S,
REMARK 350 AND CHAINS: T, U, V, W, X
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER B 14
REMARK 465 ASP B 15
REMARK 465 LEU B 16
REMARK 465 ASP B 17
REMARK 465 ALA B 241
REMARK 465 GLN B 242
REMARK 465 ASP B 243
REMARK 465 GLY B 368
REMARK 465 VAL B 369
REMARK 465 SER B 370
REMARK 465 LEU B 503
REMARK 465 LEU B 504
REMARK 465 ASN B 505
REMARK 465 ALA B 506
REMARK 465 PRO B 507
REMARK 465 ALA B 508
REMARK 465 SER B 664
REMARK 465 LEU B 665
REMARK 465 LEU B 666
REMARK 465 ARG B 667
REMARK 465 SER B 668
REMARK 465 THR B 669
REMARK 465 SER B 670
REMARK 465 GLN B 671
REMARK 465 LEU B 810
REMARK 465 ALA B 811
REMARK 465 ASP B 812
REMARK 465 ALA B 813
REMARK 465 GLY B 814
REMARK 465 PHE B 815
REMARK 465 MET B 816
REMARK 465 LYS B 817
REMARK 465 GLY B 824
REMARK 465 ASP B 825
REMARK 465 ILE B 826
REMARK 465 ASN B 827
REMARK 465 ALA B 828
REMARK 465 ARG B 829
REMARK 465 ASP B 830
REMARK 465 ASP B 1121
REMARK 465 PRO B 1122
REMARK 465 LEU B 1123
REMARK 465 GLN B 1124
REMARK 465 PRO B 1125
REMARK 465 GLU B 1126
REMARK 465 LEU B 1127
REMARK 465 ASP B 1128
REMARK 465 SER B 1129
REMARK 465 PHE B 1130
REMARK 465 LYS B 1131
REMARK 465 GLU B 1132
REMARK 465 GLU B 1133
REMARK 465 LEU B 1134
REMARK 465 ASP B 1135
REMARK 465 LYS B 1136
REMARK 465 TYR B 1137
REMARK 465 PHE B 1138
REMARK 465 LYS B 1139
REMARK 465 ASN B 1140
REMARK 465 HIS B 1141
REMARK 465 THR B 1142
REMARK 465 SER B 1143
REMARK 465 PRO B 1144
REMARK 465 ASP B 1145
REMARK 465 VAL B 1146
REMARK 465 ASP B 1147
REMARK 465 LEU B 1148
REMARK 465 GLY B 1149
REMARK 465 ASP B 1150
REMARK 465 ILE B 1151
REMARK 465 SER B 1152
REMARK 465 GLY B 1153
REMARK 465 ILE B 1154
REMARK 465 ASN B 1155
REMARK 465 ALA B 1156
REMARK 465 SER B 1157
REMARK 465 VAL B 1158
REMARK 465 VAL B 1159
REMARK 465 ASN B 1160
REMARK 465 ILE B 1161
REMARK 465 GLN B 1162
REMARK 465 LYS B 1163
REMARK 465 GLU B 1164
REMARK 465 ILE B 1165
REMARK 465 ASP B 1166
REMARK 465 ARG B 1167
REMARK 465 LEU B 1168
REMARK 465 ASN B 1169
REMARK 465 GLU B 1170
REMARK 465 VAL B 1171
REMARK 465 ALA B 1172
REMARK 465 LYS B 1173
REMARK 465 ASN B 1174
REMARK 465 LEU B 1175
REMARK 465 ASN B 1176
REMARK 465 GLU B 1177
REMARK 465 SER B 1178
REMARK 465 LEU B 1179
REMARK 465 ILE B 1180
REMARK 465 ASP B 1181
REMARK 465 LEU B 1182
REMARK 465 GLN B 1183
REMARK 465 GLU B 1184
REMARK 465 LEU B 1185
REMARK 465 GLY B 1186
REMARK 465 LYS B 1187
REMARK 465 TYR B 1188
REMARK 465 GLU B 1189
REMARK 465 GLN B 1190
REMARK 465 GLY B 1191
REMARK 465 SER B 1192
REMARK 465 GLY B 1193
REMARK 465 TYR B 1194
REMARK 465 ILE B 1195
REMARK 465 PRO B 1196
REMARK 465 GLU B 1197
REMARK 465 ALA B 1198
REMARK 465 PRO B 1199
REMARK 465 ARG B 1200
REMARK 465 ASP B 1201
REMARK 465 GLY B 1202
REMARK 465 GLN B 1203
REMARK 465 ALA B 1204
REMARK 465 TYR B 1205
REMARK 465 VAL B 1206
REMARK 465 ARG B 1207
REMARK 465 LYS B 1208
REMARK 465 ASP B 1209
REMARK 465 GLY B 1210
REMARK 465 GLU B 1211
REMARK 465 TRP B 1212
REMARK 465 VAL B 1213
REMARK 465 LEU B 1214
REMARK 465 LEU B 1215
REMARK 465 SER B 1216
REMARK 465 THR B 1217
REMARK 465 PHE B 1218
REMARK 465 LEU B 1219
REMARK 465 GLY B 1220
REMARK 465 ARG B 1221
REMARK 465 SER B 1222
REMARK 465 LEU B 1223
REMARK 465 GLU B 1224
REMARK 465 VAL B 1225
REMARK 465 LEU B 1226
REMARK 465 PHE B 1227
REMARK 465 GLN B 1228
REMARK 465 SER C 14
REMARK 465 ASP C 15
REMARK 465 LEU C 16
REMARK 465 ASP C 17
REMARK 465 ALA C 241
REMARK 465 GLN C 242
REMARK 465 ASP C 243
REMARK 465 GLY C 368
REMARK 465 VAL C 369
REMARK 465 SER C 370
REMARK 465 LEU C 503
REMARK 465 LEU C 504
REMARK 465 ASN C 505
REMARK 465 ALA C 506
REMARK 465 PRO C 507
REMARK 465 ALA C 508
REMARK 465 VAL C 663
REMARK 465 SER C 664
REMARK 465 LEU C 665
REMARK 465 LEU C 666
REMARK 465 ARG C 667
REMARK 465 SER C 668
REMARK 465 THR C 669
REMARK 465 SER C 670
REMARK 465 GLN C 671
REMARK 465 LEU C 810
REMARK 465 ALA C 811
REMARK 465 ASP C 812
REMARK 465 ALA C 813
REMARK 465 GLY C 814
REMARK 465 PHE C 815
REMARK 465 MET C 816
REMARK 465 LYS C 817
REMARK 465 ASP C 825
REMARK 465 ILE C 826
REMARK 465 ASN C 827
REMARK 465 ALA C 828
REMARK 465 ARG C 829
REMARK 465 ASP C 830
REMARK 465 ASP C 1121
REMARK 465 PRO C 1122
REMARK 465 LEU C 1123
REMARK 465 GLN C 1124
REMARK 465 PRO C 1125
REMARK 465 GLU C 1126
REMARK 465 LEU C 1127
REMARK 465 ASP C 1128
REMARK 465 SER C 1129
REMARK 465 PHE C 1130
REMARK 465 LYS C 1131
REMARK 465 GLU C 1132
REMARK 465 GLU C 1133
REMARK 465 LEU C 1134
REMARK 465 ASP C 1135
REMARK 465 LYS C 1136
REMARK 465 TYR C 1137
REMARK 465 PHE C 1138
REMARK 465 LYS C 1139
REMARK 465 ASN C 1140
REMARK 465 HIS C 1141
REMARK 465 THR C 1142
REMARK 465 SER C 1143
REMARK 465 PRO C 1144
REMARK 465 ASP C 1145
REMARK 465 VAL C 1146
REMARK 465 ASP C 1147
REMARK 465 LEU C 1148
REMARK 465 GLY C 1149
REMARK 465 ASP C 1150
REMARK 465 ILE C 1151
REMARK 465 SER C 1152
REMARK 465 GLY C 1153
REMARK 465 ILE C 1154
REMARK 465 ASN C 1155
REMARK 465 ALA C 1156
REMARK 465 SER C 1157
REMARK 465 VAL C 1158
REMARK 465 VAL C 1159
REMARK 465 ASN C 1160
REMARK 465 ILE C 1161
REMARK 465 GLN C 1162
REMARK 465 LYS C 1163
REMARK 465 GLU C 1164
REMARK 465 ILE C 1165
REMARK 465 ASP C 1166
REMARK 465 ARG C 1167
REMARK 465 LEU C 1168
REMARK 465 ASN C 1169
REMARK 465 GLU C 1170
REMARK 465 VAL C 1171
REMARK 465 ALA C 1172
REMARK 465 LYS C 1173
REMARK 465 ASN C 1174
REMARK 465 LEU C 1175
REMARK 465 ASN C 1176
REMARK 465 GLU C 1177
REMARK 465 SER C 1178
REMARK 465 LEU C 1179
REMARK 465 ILE C 1180
REMARK 465 ASP C 1181
REMARK 465 LEU C 1182
REMARK 465 GLN C 1183
REMARK 465 GLU C 1184
REMARK 465 LEU C 1185
REMARK 465 GLY C 1186
REMARK 465 LYS C 1187
REMARK 465 TYR C 1188
REMARK 465 GLU C 1189
REMARK 465 GLN C 1190
REMARK 465 GLY C 1191
REMARK 465 SER C 1192
REMARK 465 GLY C 1193
REMARK 465 TYR C 1194
REMARK 465 ILE C 1195
REMARK 465 PRO C 1196
REMARK 465 GLU C 1197
REMARK 465 ALA C 1198
REMARK 465 PRO C 1199
REMARK 465 ARG C 1200
REMARK 465 ASP C 1201
REMARK 465 GLY C 1202
REMARK 465 GLN C 1203
REMARK 465 ALA C 1204
REMARK 465 TYR C 1205
REMARK 465 VAL C 1206
REMARK 465 ARG C 1207
REMARK 465 LYS C 1208
REMARK 465 ASP C 1209
REMARK 465 GLY C 1210
REMARK 465 GLU C 1211
REMARK 465 TRP C 1212
REMARK 465 VAL C 1213
REMARK 465 LEU C 1214
REMARK 465 LEU C 1215
REMARK 465 SER C 1216
REMARK 465 THR C 1217
REMARK 465 PHE C 1218
REMARK 465 LEU C 1219
REMARK 465 GLY C 1220
REMARK 465 ARG C 1221
REMARK 465 SER C 1222
REMARK 465 LEU C 1223
REMARK 465 GLU C 1224
REMARK 465 VAL C 1225
REMARK 465 LEU C 1226
REMARK 465 PHE C 1227
REMARK 465 GLN C 1228
REMARK 465 SER A 14
REMARK 465 ASP A 15
REMARK 465 LEU A 16
REMARK 465 ASP A 17
REMARK 465 ALA A 241
REMARK 465 GLN A 242
REMARK 465 ASP A 243
REMARK 465 GLY A 368
REMARK 465 VAL A 369
REMARK 465 SER A 370
REMARK 465 LEU A 503
REMARK 465 LEU A 504
REMARK 465 ASN A 505
REMARK 465 ALA A 506
REMARK 465 PRO A 507
REMARK 465 ALA A 508
REMARK 465 VAL A 663
REMARK 465 SER A 664
REMARK 465 LEU A 665
REMARK 465 LEU A 666
REMARK 465 ARG A 667
REMARK 465 SER A 668
REMARK 465 THR A 669
REMARK 465 SER A 670
REMARK 465 GLN A 671
REMARK 465 LEU A 810
REMARK 465 ALA A 811
REMARK 465 ASP A 812
REMARK 465 ALA A 813
REMARK 465 GLY A 814
REMARK 465 PHE A 815
REMARK 465 MET A 816
REMARK 465 LYS A 817
REMARK 465 GLY A 824
REMARK 465 ASP A 825
REMARK 465 ILE A 826
REMARK 465 ASN A 827
REMARK 465 ALA A 828
REMARK 465 ARG A 829
REMARK 465 ASP A 830
REMARK 465 LEU A 831
REMARK 465 ASP A 1121
REMARK 465 PRO A 1122
REMARK 465 LEU A 1123
REMARK 465 GLN A 1124
REMARK 465 PRO A 1125
REMARK 465 GLU A 1126
REMARK 465 LEU A 1127
REMARK 465 ASP A 1128
REMARK 465 SER A 1129
REMARK 465 PHE A 1130
REMARK 465 LYS A 1131
REMARK 465 GLU A 1132
REMARK 465 GLU A 1133
REMARK 465 LEU A 1134
REMARK 465 ASP A 1135
REMARK 465 LYS A 1136
REMARK 465 TYR A 1137
REMARK 465 PHE A 1138
REMARK 465 LYS A 1139
REMARK 465 ASN A 1140
REMARK 465 HIS A 1141
REMARK 465 THR A 1142
REMARK 465 SER A 1143
REMARK 465 PRO A 1144
REMARK 465 ASP A 1145
REMARK 465 VAL A 1146
REMARK 465 ASP A 1147
REMARK 465 LEU A 1148
REMARK 465 GLY A 1149
REMARK 465 ASP A 1150
REMARK 465 ILE A 1151
REMARK 465 SER A 1152
REMARK 465 GLY A 1153
REMARK 465 ILE A 1154
REMARK 465 ASN A 1155
REMARK 465 ALA A 1156
REMARK 465 SER A 1157
REMARK 465 VAL A 1158
REMARK 465 VAL A 1159
REMARK 465 ASN A 1160
REMARK 465 ILE A 1161
REMARK 465 GLN A 1162
REMARK 465 LYS A 1163
REMARK 465 GLU A 1164
REMARK 465 ILE A 1165
REMARK 465 ASP A 1166
REMARK 465 ARG A 1167
REMARK 465 LEU A 1168
REMARK 465 ASN A 1169
REMARK 465 GLU A 1170
REMARK 465 VAL A 1171
REMARK 465 ALA A 1172
REMARK 465 LYS A 1173
REMARK 465 ASN A 1174
REMARK 465 LEU A 1175
REMARK 465 ASN A 1176
REMARK 465 GLU A 1177
REMARK 465 SER A 1178
REMARK 465 LEU A 1179
REMARK 465 ILE A 1180
REMARK 465 ASP A 1181
REMARK 465 LEU A 1182
REMARK 465 GLN A 1183
REMARK 465 GLU A 1184
REMARK 465 LEU A 1185
REMARK 465 GLY A 1186
REMARK 465 LYS A 1187
REMARK 465 TYR A 1188
REMARK 465 GLU A 1189
REMARK 465 GLN A 1190
REMARK 465 GLY A 1191
REMARK 465 SER A 1192
REMARK 465 GLY A 1193
REMARK 465 TYR A 1194
REMARK 465 ILE A 1195
REMARK 465 PRO A 1196
REMARK 465 GLU A 1197
REMARK 465 ALA A 1198
REMARK 465 PRO A 1199
REMARK 465 ARG A 1200
REMARK 465 ASP A 1201
REMARK 465 GLY A 1202
REMARK 465 GLN A 1203
REMARK 465 ALA A 1204
REMARK 465 TYR A 1205
REMARK 465 VAL A 1206
REMARK 465 ARG A 1207
REMARK 465 LYS A 1208
REMARK 465 ASP A 1209
REMARK 465 GLY A 1210
REMARK 465 GLU A 1211
REMARK 465 TRP A 1212
REMARK 465 VAL A 1213
REMARK 465 LEU A 1214
REMARK 465 LEU A 1215
REMARK 465 SER A 1216
REMARK 465 THR A 1217
REMARK 465 PHE A 1218
REMARK 465 LEU A 1219
REMARK 465 GLY A 1220
REMARK 465 ARG A 1221
REMARK 465 SER A 1222
REMARK 465 LEU A 1223
REMARK 465 GLU A 1224
REMARK 465 VAL A 1225
REMARK 465 LEU A 1226
REMARK 465 PHE A 1227
REMARK 465 GLN A 1228
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER B 35 34.93 -89.64
REMARK 500 TYR B 63 16.21 57.78
REMARK 500 LYS B 84 -29.92 70.39
REMARK 500 ASP B 85 -27.02 -148.14
REMARK 500 SER B 105 -60.96 -103.52
REMARK 500 MET B 107 -14.03 73.47
REMARK 500 ASN B 109 49.25 -82.18
REMARK 500 SER B 120 -0.71 66.10
REMARK 500 ILE B 152 -60.80 -120.76
REMARK 500 PRO B 335 -179.75 -63.99
REMARK 500 ASN B 357 51.15 -92.05
REMARK 500 SER B 362 -31.05 -131.62
REMARK 500 SER B 380 -163.23 -79.09
REMARK 500 ASP B 463 50.50 -93.62
REMARK 500 PRO B 470 52.66 -93.57
REMARK 500 ASN B 530 98.31 -69.64
REMARK 500 ILE B 652 -61.84 -106.65
REMARK 500 LEU B 681 36.31 -99.99
REMARK 500 ASP B 727 62.21 62.75
REMARK 500 CYS B1014 -31.73 -132.67
REMARK 500 ASP B1023 -8.26 72.55
REMARK 500 LEU B1031 -60.09 -100.18
REMARK 500 MET C 37 30.29 -141.47
REMARK 500 ASN C 73 -23.18 68.20
REMARK 500 HIS C 74 -22.70 -143.34
REMARK 500 ASN C 78 83.45 -156.95
REMARK 500 LYS C 84 -25.25 69.49
REMARK 500 ASP C 85 -29.93 -141.60
REMARK 500 ARG C 207 109.22 -161.22
REMARK 500 PRO C 317 -169.25 -71.85
REMARK 500 PRO C 335 -169.07 -74.35
REMARK 500 PHE C 379 -159.10 -150.96
REMARK 500 SER C 380 -161.78 -76.04
REMARK 500 ASN C 381 109.91 -57.84
REMARK 500 HIS C 445 99.46 -69.12
REMARK 500 ASN C 457 51.70 -92.89
REMARK 500 PRO C 547 4.04 -67.06
REMARK 500 PHE C 551 -169.25 -161.41
REMARK 500 CYS C 576 -71.76 -63.39
REMARK 500 ALA C 577 157.06 179.19
REMARK 500 ASN C 627 79.91 -103.42
REMARK 500 ASP C 643 33.81 -98.03
REMARK 500 ILE C 652 -59.46 -123.94
REMARK 500 HIS C 661 -166.27 -116.12
REMARK 500 LEU C1031 -61.85 -91.01
REMARK 500 GLN C1053 70.70 60.10
REMARK 500 THR C1098 -168.40 -125.37
REMARK 500 VAL C1110 -61.55 -121.18
REMARK 500 SER A 35 40.57 -103.97
REMARK 500 MET A 37 21.76 -140.85
REMARK 500
REMARK 500 THIS ENTRY HAS 73 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 CYS B 576 ALA B 577 146.23
REMARK 500 ASP C 85 GLY C 86 -141.37
REMARK 500 SER A 35 SER A 36 -141.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-7579 RELATED DB: EMDB
REMARK 900 SARS SPIKE GLYCOPROTEIN, TRYPSIN-CLEAVED, STABILIZED VARIANT, TWO
REMARK 900 S1 CTDS IN AN UPWARDS CONFORMATION
DBREF 6CS1 B 14 1190 UNP P59594 SPIKE_CVHSA 14 1190
DBREF 6CS1 B 1192 1219 UNP D9IEJ2 D9IEJ2_BPT4 457 484
DBREF 6CS1 C 14 1190 UNP P59594 SPIKE_CVHSA 14 1190
DBREF 6CS1 C 1192 1219 UNP D9IEJ2 D9IEJ2_BPT4 457 484
DBREF 6CS1 A 14 1190 UNP P59594 SPIKE_CVHSA 14 1190
DBREF 6CS1 A 1192 1219 UNP D9IEJ2 D9IEJ2_BPT4 457 484
SEQADV 6CS1 ALA B 577 UNP P59594 SER 577 CONFLICT
SEQADV 6CS1 PRO B 968 UNP P59594 LYS 968 ENGINEERED MUTATION
SEQADV 6CS1 PRO B 969 UNP P59594 VAL 969 ENGINEERED MUTATION
SEQADV 6CS1 GLY B 1191 UNP P59594 LINKER
SEQADV 6CS1 SER B 1192 UNP D9IEJ2 ALA 457 LINKER
SEQADV 6CS1 GLY B 1220 UNP D9IEJ2 EXPRESSION TAG
SEQADV 6CS1 ARG B 1221 UNP D9IEJ2 EXPRESSION TAG
SEQADV 6CS1 SER B 1222 UNP D9IEJ2 EXPRESSION TAG
SEQADV 6CS1 LEU B 1223 UNP D9IEJ2 EXPRESSION TAG
SEQADV 6CS1 GLU B 1224 UNP D9IEJ2 EXPRESSION TAG
SEQADV 6CS1 VAL B 1225 UNP D9IEJ2 EXPRESSION TAG
SEQADV 6CS1 LEU B 1226 UNP D9IEJ2 EXPRESSION TAG
SEQADV 6CS1 PHE B 1227 UNP D9IEJ2 EXPRESSION TAG
SEQADV 6CS1 GLN B 1228 UNP D9IEJ2 EXPRESSION TAG
SEQADV 6CS1 ALA C 577 UNP P59594 SER 577 CONFLICT
SEQADV 6CS1 PRO C 968 UNP P59594 LYS 968 ENGINEERED MUTATION
SEQADV 6CS1 PRO C 969 UNP P59594 VAL 969 ENGINEERED MUTATION
SEQADV 6CS1 GLY C 1191 UNP P59594 LINKER
SEQADV 6CS1 SER C 1192 UNP D9IEJ2 ALA 457 LINKER
SEQADV 6CS1 GLY C 1220 UNP D9IEJ2 EXPRESSION TAG
SEQADV 6CS1 ARG C 1221 UNP D9IEJ2 EXPRESSION TAG
SEQADV 6CS1 SER C 1222 UNP D9IEJ2 EXPRESSION TAG
SEQADV 6CS1 LEU C 1223 UNP D9IEJ2 EXPRESSION TAG
SEQADV 6CS1 GLU C 1224 UNP D9IEJ2 EXPRESSION TAG
SEQADV 6CS1 VAL C 1225 UNP D9IEJ2 EXPRESSION TAG
SEQADV 6CS1 LEU C 1226 UNP D9IEJ2 EXPRESSION TAG
SEQADV 6CS1 PHE C 1227 UNP D9IEJ2 EXPRESSION TAG
SEQADV 6CS1 GLN C 1228 UNP D9IEJ2 EXPRESSION TAG
SEQADV 6CS1 ALA A 577 UNP P59594 SER 577 CONFLICT
SEQADV 6CS1 PRO A 968 UNP P59594 LYS 968 ENGINEERED MUTATION
SEQADV 6CS1 PRO A 969 UNP P59594 VAL 969 ENGINEERED MUTATION
SEQADV 6CS1 GLY A 1191 UNP P59594 LINKER
SEQADV 6CS1 SER A 1192 UNP D9IEJ2 ALA 457 LINKER
SEQADV 6CS1 GLY A 1220 UNP D9IEJ2 EXPRESSION TAG
SEQADV 6CS1 ARG A 1221 UNP D9IEJ2 EXPRESSION TAG
SEQADV 6CS1 SER A 1222 UNP D9IEJ2 EXPRESSION TAG
SEQADV 6CS1 LEU A 1223 UNP D9IEJ2 EXPRESSION TAG
SEQADV 6CS1 GLU A 1224 UNP D9IEJ2 EXPRESSION TAG
SEQADV 6CS1 VAL A 1225 UNP D9IEJ2 EXPRESSION TAG
SEQADV 6CS1 LEU A 1226 UNP D9IEJ2 EXPRESSION TAG
SEQADV 6CS1 PHE A 1227 UNP D9IEJ2 EXPRESSION TAG
SEQADV 6CS1 GLN A 1228 UNP D9IEJ2 EXPRESSION TAG
SEQRES 1 B 1215 SER ASP LEU ASP ARG CYS THR THR PHE ASP ASP VAL GLN
SEQRES 2 B 1215 ALA PRO ASN TYR THR GLN HIS THR SER SER MET ARG GLY
SEQRES 3 B 1215 VAL TYR TYR PRO ASP GLU ILE PHE ARG SER ASP THR LEU
SEQRES 4 B 1215 TYR LEU THR GLN ASP LEU PHE LEU PRO PHE TYR SER ASN
SEQRES 5 B 1215 VAL THR GLY PHE HIS THR ILE ASN HIS THR PHE GLY ASN
SEQRES 6 B 1215 PRO VAL ILE PRO PHE LYS ASP GLY ILE TYR PHE ALA ALA
SEQRES 7 B 1215 THR GLU LYS SER ASN VAL VAL ARG GLY TRP VAL PHE GLY
SEQRES 8 B 1215 SER THR MET ASN ASN LYS SER GLN SER VAL ILE ILE ILE
SEQRES 9 B 1215 ASN ASN SER THR ASN VAL VAL ILE ARG ALA CYS ASN PHE
SEQRES 10 B 1215 GLU LEU CYS ASP ASN PRO PHE PHE ALA VAL SER LYS PRO
SEQRES 11 B 1215 MET GLY THR GLN THR HIS THR MET ILE PHE ASP ASN ALA
SEQRES 12 B 1215 PHE ASN CYS THR PHE GLU TYR ILE SER ASP ALA PHE SER
SEQRES 13 B 1215 LEU ASP VAL SER GLU LYS SER GLY ASN PHE LYS HIS LEU
SEQRES 14 B 1215 ARG GLU PHE VAL PHE LYS ASN LYS ASP GLY PHE LEU TYR
SEQRES 15 B 1215 VAL TYR LYS GLY TYR GLN PRO ILE ASP VAL VAL ARG ASP
SEQRES 16 B 1215 LEU PRO SER GLY PHE ASN THR LEU LYS PRO ILE PHE LYS
SEQRES 17 B 1215 LEU PRO LEU GLY ILE ASN ILE THR ASN PHE ARG ALA ILE
SEQRES 18 B 1215 LEU THR ALA PHE SER PRO ALA GLN ASP ILE TRP GLY THR
SEQRES 19 B 1215 SER ALA ALA ALA TYR PHE VAL GLY TYR LEU LYS PRO THR
SEQRES 20 B 1215 THR PHE MET LEU LYS TYR ASP GLU ASN GLY THR ILE THR
SEQRES 21 B 1215 ASP ALA VAL ASP CYS SER GLN ASN PRO LEU ALA GLU LEU
SEQRES 22 B 1215 LYS CYS SER VAL LYS SER PHE GLU ILE ASP LYS GLY ILE
SEQRES 23 B 1215 TYR GLN THR SER ASN PHE ARG VAL VAL PRO SER GLY ASP
SEQRES 24 B 1215 VAL VAL ARG PHE PRO ASN ILE THR ASN LEU CYS PRO PHE
SEQRES 25 B 1215 GLY GLU VAL PHE ASN ALA THR LYS PHE PRO SER VAL TYR
SEQRES 26 B 1215 ALA TRP GLU ARG LYS LYS ILE SER ASN CYS VAL ALA ASP
SEQRES 27 B 1215 TYR SER VAL LEU TYR ASN SER THR PHE PHE SER THR PHE
SEQRES 28 B 1215 LYS CYS TYR GLY VAL SER ALA THR LYS LEU ASN ASP LEU
SEQRES 29 B 1215 CYS PHE SER ASN VAL TYR ALA ASP SER PHE VAL VAL LYS
SEQRES 30 B 1215 GLY ASP ASP VAL ARG GLN ILE ALA PRO GLY GLN THR GLY
SEQRES 31 B 1215 VAL ILE ALA ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE
SEQRES 32 B 1215 MET GLY CYS VAL LEU ALA TRP ASN THR ARG ASN ILE ASP
SEQRES 33 B 1215 ALA THR SER THR GLY ASN TYR ASN TYR LYS TYR ARG TYR
SEQRES 34 B 1215 LEU ARG HIS GLY LYS LEU ARG PRO PHE GLU ARG ASP ILE
SEQRES 35 B 1215 SER ASN VAL PRO PHE SER PRO ASP GLY LYS PRO CYS THR
SEQRES 36 B 1215 PRO PRO ALA LEU ASN CYS TYR TRP PRO LEU ASN ASP TYR
SEQRES 37 B 1215 GLY PHE TYR THR THR THR GLY ILE GLY TYR GLN PRO TYR
SEQRES 38 B 1215 ARG VAL VAL VAL LEU SER PHE GLU LEU LEU ASN ALA PRO
SEQRES 39 B 1215 ALA THR VAL CYS GLY PRO LYS LEU SER THR ASP LEU ILE
SEQRES 40 B 1215 LYS ASN GLN CYS VAL ASN PHE ASN PHE ASN GLY LEU THR
SEQRES 41 B 1215 GLY THR GLY VAL LEU THR PRO SER SER LYS ARG PHE GLN
SEQRES 42 B 1215 PRO PHE GLN GLN PHE GLY ARG ASP VAL SER ASP PHE THR
SEQRES 43 B 1215 ASP SER VAL ARG ASP PRO LYS THR SER GLU ILE LEU ASP
SEQRES 44 B 1215 ILE SER PRO CYS ALA PHE GLY GLY VAL SER VAL ILE THR
SEQRES 45 B 1215 PRO GLY THR ASN ALA SER SER GLU VAL ALA VAL LEU TYR
SEQRES 46 B 1215 GLN ASP VAL ASN CYS THR ASP VAL SER THR ALA ILE HIS
SEQRES 47 B 1215 ALA ASP GLN LEU THR PRO ALA TRP ARG ILE TYR SER THR
SEQRES 48 B 1215 GLY ASN ASN VAL PHE GLN THR GLN ALA GLY CYS LEU ILE
SEQRES 49 B 1215 GLY ALA GLU HIS VAL ASP THR SER TYR GLU CYS ASP ILE
SEQRES 50 B 1215 PRO ILE GLY ALA GLY ILE CYS ALA SER TYR HIS THR VAL
SEQRES 51 B 1215 SER LEU LEU ARG SER THR SER GLN LYS SER ILE VAL ALA
SEQRES 52 B 1215 TYR THR MET SER LEU GLY ALA ASP SER SER ILE ALA TYR
SEQRES 53 B 1215 SER ASN ASN THR ILE ALA ILE PRO THR ASN PHE SER ILE
SEQRES 54 B 1215 SER ILE THR THR GLU VAL MET PRO VAL SER MET ALA LYS
SEQRES 55 B 1215 THR SER VAL ASP CYS ASN MET TYR ILE CYS GLY ASP SER
SEQRES 56 B 1215 THR GLU CYS ALA ASN LEU LEU LEU GLN TYR GLY SER PHE
SEQRES 57 B 1215 CYS THR GLN LEU ASN ARG ALA LEU SER GLY ILE ALA ALA
SEQRES 58 B 1215 GLU GLN ASP ARG ASN THR ARG GLU VAL PHE ALA GLN VAL
SEQRES 59 B 1215 LYS GLN MET TYR LYS THR PRO THR LEU LYS TYR PHE GLY
SEQRES 60 B 1215 GLY PHE ASN PHE SER GLN ILE LEU PRO ASP PRO LEU LYS
SEQRES 61 B 1215 PRO THR LYS ARG SER PHE ILE GLU ASP LEU LEU PHE ASN
SEQRES 62 B 1215 LYS VAL THR LEU ALA ASP ALA GLY PHE MET LYS GLN TYR
SEQRES 63 B 1215 GLY GLU CYS LEU GLY ASP ILE ASN ALA ARG ASP LEU ILE
SEQRES 64 B 1215 CYS ALA GLN LYS PHE ASN GLY LEU THR VAL LEU PRO PRO
SEQRES 65 B 1215 LEU LEU THR ASP ASP MET ILE ALA ALA TYR THR ALA ALA
SEQRES 66 B 1215 LEU VAL SER GLY THR ALA THR ALA GLY TRP THR PHE GLY
SEQRES 67 B 1215 ALA GLY ALA ALA LEU GLN ILE PRO PHE ALA MET GLN MET
SEQRES 68 B 1215 ALA TYR ARG PHE ASN GLY ILE GLY VAL THR GLN ASN VAL
SEQRES 69 B 1215 LEU TYR GLU ASN GLN LYS GLN ILE ALA ASN GLN PHE ASN
SEQRES 70 B 1215 LYS ALA ILE SER GLN ILE GLN GLU SER LEU THR THR THR
SEQRES 71 B 1215 SER THR ALA LEU GLY LYS LEU GLN ASP VAL VAL ASN GLN
SEQRES 72 B 1215 ASN ALA GLN ALA LEU ASN THR LEU VAL LYS GLN LEU SER
SEQRES 73 B 1215 SER ASN PHE GLY ALA ILE SER SER VAL LEU ASN ASP ILE
SEQRES 74 B 1215 LEU SER ARG LEU ASP PRO PRO GLU ALA GLU VAL GLN ILE
SEQRES 75 B 1215 ASP ARG LEU ILE THR GLY ARG LEU GLN SER LEU GLN THR
SEQRES 76 B 1215 TYR VAL THR GLN GLN LEU ILE ARG ALA ALA GLU ILE ARG
SEQRES 77 B 1215 ALA SER ALA ASN LEU ALA ALA THR LYS MET SER GLU CYS
SEQRES 78 B 1215 VAL LEU GLY GLN SER LYS ARG VAL ASP PHE CYS GLY LYS
SEQRES 79 B 1215 GLY TYR HIS LEU MET SER PHE PRO GLN ALA ALA PRO HIS
SEQRES 80 B 1215 GLY VAL VAL PHE LEU HIS VAL THR TYR VAL PRO SER GLN
SEQRES 81 B 1215 GLU ARG ASN PHE THR THR ALA PRO ALA ILE CYS HIS GLU
SEQRES 82 B 1215 GLY LYS ALA TYR PHE PRO ARG GLU GLY VAL PHE VAL PHE
SEQRES 83 B 1215 ASN GLY THR SER TRP PHE ILE THR GLN ARG ASN PHE PHE
SEQRES 84 B 1215 SER PRO GLN ILE ILE THR THR ASP ASN THR PHE VAL SER
SEQRES 85 B 1215 GLY ASN CYS ASP VAL VAL ILE GLY ILE ILE ASN ASN THR
SEQRES 86 B 1215 VAL TYR ASP PRO LEU GLN PRO GLU LEU ASP SER PHE LYS
SEQRES 87 B 1215 GLU GLU LEU ASP LYS TYR PHE LYS ASN HIS THR SER PRO
SEQRES 88 B 1215 ASP VAL ASP LEU GLY ASP ILE SER GLY ILE ASN ALA SER
SEQRES 89 B 1215 VAL VAL ASN ILE GLN LYS GLU ILE ASP ARG LEU ASN GLU
SEQRES 90 B 1215 VAL ALA LYS ASN LEU ASN GLU SER LEU ILE ASP LEU GLN
SEQRES 91 B 1215 GLU LEU GLY LYS TYR GLU GLN GLY SER GLY TYR ILE PRO
SEQRES 92 B 1215 GLU ALA PRO ARG ASP GLY GLN ALA TYR VAL ARG LYS ASP
SEQRES 93 B 1215 GLY GLU TRP VAL LEU LEU SER THR PHE LEU GLY ARG SER
SEQRES 94 B 1215 LEU GLU VAL LEU PHE GLN
SEQRES 1 C 1215 SER ASP LEU ASP ARG CYS THR THR PHE ASP ASP VAL GLN
SEQRES 2 C 1215 ALA PRO ASN TYR THR GLN HIS THR SER SER MET ARG GLY
SEQRES 3 C 1215 VAL TYR TYR PRO ASP GLU ILE PHE ARG SER ASP THR LEU
SEQRES 4 C 1215 TYR LEU THR GLN ASP LEU PHE LEU PRO PHE TYR SER ASN
SEQRES 5 C 1215 VAL THR GLY PHE HIS THR ILE ASN HIS THR PHE GLY ASN
SEQRES 6 C 1215 PRO VAL ILE PRO PHE LYS ASP GLY ILE TYR PHE ALA ALA
SEQRES 7 C 1215 THR GLU LYS SER ASN VAL VAL ARG GLY TRP VAL PHE GLY
SEQRES 8 C 1215 SER THR MET ASN ASN LYS SER GLN SER VAL ILE ILE ILE
SEQRES 9 C 1215 ASN ASN SER THR ASN VAL VAL ILE ARG ALA CYS ASN PHE
SEQRES 10 C 1215 GLU LEU CYS ASP ASN PRO PHE PHE ALA VAL SER LYS PRO
SEQRES 11 C 1215 MET GLY THR GLN THR HIS THR MET ILE PHE ASP ASN ALA
SEQRES 12 C 1215 PHE ASN CYS THR PHE GLU TYR ILE SER ASP ALA PHE SER
SEQRES 13 C 1215 LEU ASP VAL SER GLU LYS SER GLY ASN PHE LYS HIS LEU
SEQRES 14 C 1215 ARG GLU PHE VAL PHE LYS ASN LYS ASP GLY PHE LEU TYR
SEQRES 15 C 1215 VAL TYR LYS GLY TYR GLN PRO ILE ASP VAL VAL ARG ASP
SEQRES 16 C 1215 LEU PRO SER GLY PHE ASN THR LEU LYS PRO ILE PHE LYS
SEQRES 17 C 1215 LEU PRO LEU GLY ILE ASN ILE THR ASN PHE ARG ALA ILE
SEQRES 18 C 1215 LEU THR ALA PHE SER PRO ALA GLN ASP ILE TRP GLY THR
SEQRES 19 C 1215 SER ALA ALA ALA TYR PHE VAL GLY TYR LEU LYS PRO THR
SEQRES 20 C 1215 THR PHE MET LEU LYS TYR ASP GLU ASN GLY THR ILE THR
SEQRES 21 C 1215 ASP ALA VAL ASP CYS SER GLN ASN PRO LEU ALA GLU LEU
SEQRES 22 C 1215 LYS CYS SER VAL LYS SER PHE GLU ILE ASP LYS GLY ILE
SEQRES 23 C 1215 TYR GLN THR SER ASN PHE ARG VAL VAL PRO SER GLY ASP
SEQRES 24 C 1215 VAL VAL ARG PHE PRO ASN ILE THR ASN LEU CYS PRO PHE
SEQRES 25 C 1215 GLY GLU VAL PHE ASN ALA THR LYS PHE PRO SER VAL TYR
SEQRES 26 C 1215 ALA TRP GLU ARG LYS LYS ILE SER ASN CYS VAL ALA ASP
SEQRES 27 C 1215 TYR SER VAL LEU TYR ASN SER THR PHE PHE SER THR PHE
SEQRES 28 C 1215 LYS CYS TYR GLY VAL SER ALA THR LYS LEU ASN ASP LEU
SEQRES 29 C 1215 CYS PHE SER ASN VAL TYR ALA ASP SER PHE VAL VAL LYS
SEQRES 30 C 1215 GLY ASP ASP VAL ARG GLN ILE ALA PRO GLY GLN THR GLY
SEQRES 31 C 1215 VAL ILE ALA ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE
SEQRES 32 C 1215 MET GLY CYS VAL LEU ALA TRP ASN THR ARG ASN ILE ASP
SEQRES 33 C 1215 ALA THR SER THR GLY ASN TYR ASN TYR LYS TYR ARG TYR
SEQRES 34 C 1215 LEU ARG HIS GLY LYS LEU ARG PRO PHE GLU ARG ASP ILE
SEQRES 35 C 1215 SER ASN VAL PRO PHE SER PRO ASP GLY LYS PRO CYS THR
SEQRES 36 C 1215 PRO PRO ALA LEU ASN CYS TYR TRP PRO LEU ASN ASP TYR
SEQRES 37 C 1215 GLY PHE TYR THR THR THR GLY ILE GLY TYR GLN PRO TYR
SEQRES 38 C 1215 ARG VAL VAL VAL LEU SER PHE GLU LEU LEU ASN ALA PRO
SEQRES 39 C 1215 ALA THR VAL CYS GLY PRO LYS LEU SER THR ASP LEU ILE
SEQRES 40 C 1215 LYS ASN GLN CYS VAL ASN PHE ASN PHE ASN GLY LEU THR
SEQRES 41 C 1215 GLY THR GLY VAL LEU THR PRO SER SER LYS ARG PHE GLN
SEQRES 42 C 1215 PRO PHE GLN GLN PHE GLY ARG ASP VAL SER ASP PHE THR
SEQRES 43 C 1215 ASP SER VAL ARG ASP PRO LYS THR SER GLU ILE LEU ASP
SEQRES 44 C 1215 ILE SER PRO CYS ALA PHE GLY GLY VAL SER VAL ILE THR
SEQRES 45 C 1215 PRO GLY THR ASN ALA SER SER GLU VAL ALA VAL LEU TYR
SEQRES 46 C 1215 GLN ASP VAL ASN CYS THR ASP VAL SER THR ALA ILE HIS
SEQRES 47 C 1215 ALA ASP GLN LEU THR PRO ALA TRP ARG ILE TYR SER THR
SEQRES 48 C 1215 GLY ASN ASN VAL PHE GLN THR GLN ALA GLY CYS LEU ILE
SEQRES 49 C 1215 GLY ALA GLU HIS VAL ASP THR SER TYR GLU CYS ASP ILE
SEQRES 50 C 1215 PRO ILE GLY ALA GLY ILE CYS ALA SER TYR HIS THR VAL
SEQRES 51 C 1215 SER LEU LEU ARG SER THR SER GLN LYS SER ILE VAL ALA
SEQRES 52 C 1215 TYR THR MET SER LEU GLY ALA ASP SER SER ILE ALA TYR
SEQRES 53 C 1215 SER ASN ASN THR ILE ALA ILE PRO THR ASN PHE SER ILE
SEQRES 54 C 1215 SER ILE THR THR GLU VAL MET PRO VAL SER MET ALA LYS
SEQRES 55 C 1215 THR SER VAL ASP CYS ASN MET TYR ILE CYS GLY ASP SER
SEQRES 56 C 1215 THR GLU CYS ALA ASN LEU LEU LEU GLN TYR GLY SER PHE
SEQRES 57 C 1215 CYS THR GLN LEU ASN ARG ALA LEU SER GLY ILE ALA ALA
SEQRES 58 C 1215 GLU GLN ASP ARG ASN THR ARG GLU VAL PHE ALA GLN VAL
SEQRES 59 C 1215 LYS GLN MET TYR LYS THR PRO THR LEU LYS TYR PHE GLY
SEQRES 60 C 1215 GLY PHE ASN PHE SER GLN ILE LEU PRO ASP PRO LEU LYS
SEQRES 61 C 1215 PRO THR LYS ARG SER PHE ILE GLU ASP LEU LEU PHE ASN
SEQRES 62 C 1215 LYS VAL THR LEU ALA ASP ALA GLY PHE MET LYS GLN TYR
SEQRES 63 C 1215 GLY GLU CYS LEU GLY ASP ILE ASN ALA ARG ASP LEU ILE
SEQRES 64 C 1215 CYS ALA GLN LYS PHE ASN GLY LEU THR VAL LEU PRO PRO
SEQRES 65 C 1215 LEU LEU THR ASP ASP MET ILE ALA ALA TYR THR ALA ALA
SEQRES 66 C 1215 LEU VAL SER GLY THR ALA THR ALA GLY TRP THR PHE GLY
SEQRES 67 C 1215 ALA GLY ALA ALA LEU GLN ILE PRO PHE ALA MET GLN MET
SEQRES 68 C 1215 ALA TYR ARG PHE ASN GLY ILE GLY VAL THR GLN ASN VAL
SEQRES 69 C 1215 LEU TYR GLU ASN GLN LYS GLN ILE ALA ASN GLN PHE ASN
SEQRES 70 C 1215 LYS ALA ILE SER GLN ILE GLN GLU SER LEU THR THR THR
SEQRES 71 C 1215 SER THR ALA LEU GLY LYS LEU GLN ASP VAL VAL ASN GLN
SEQRES 72 C 1215 ASN ALA GLN ALA LEU ASN THR LEU VAL LYS GLN LEU SER
SEQRES 73 C 1215 SER ASN PHE GLY ALA ILE SER SER VAL LEU ASN ASP ILE
SEQRES 74 C 1215 LEU SER ARG LEU ASP PRO PRO GLU ALA GLU VAL GLN ILE
SEQRES 75 C 1215 ASP ARG LEU ILE THR GLY ARG LEU GLN SER LEU GLN THR
SEQRES 76 C 1215 TYR VAL THR GLN GLN LEU ILE ARG ALA ALA GLU ILE ARG
SEQRES 77 C 1215 ALA SER ALA ASN LEU ALA ALA THR LYS MET SER GLU CYS
SEQRES 78 C 1215 VAL LEU GLY GLN SER LYS ARG VAL ASP PHE CYS GLY LYS
SEQRES 79 C 1215 GLY TYR HIS LEU MET SER PHE PRO GLN ALA ALA PRO HIS
SEQRES 80 C 1215 GLY VAL VAL PHE LEU HIS VAL THR TYR VAL PRO SER GLN
SEQRES 81 C 1215 GLU ARG ASN PHE THR THR ALA PRO ALA ILE CYS HIS GLU
SEQRES 82 C 1215 GLY LYS ALA TYR PHE PRO ARG GLU GLY VAL PHE VAL PHE
SEQRES 83 C 1215 ASN GLY THR SER TRP PHE ILE THR GLN ARG ASN PHE PHE
SEQRES 84 C 1215 SER PRO GLN ILE ILE THR THR ASP ASN THR PHE VAL SER
SEQRES 85 C 1215 GLY ASN CYS ASP VAL VAL ILE GLY ILE ILE ASN ASN THR
SEQRES 86 C 1215 VAL TYR ASP PRO LEU GLN PRO GLU LEU ASP SER PHE LYS
SEQRES 87 C 1215 GLU GLU LEU ASP LYS TYR PHE LYS ASN HIS THR SER PRO
SEQRES 88 C 1215 ASP VAL ASP LEU GLY ASP ILE SER GLY ILE ASN ALA SER
SEQRES 89 C 1215 VAL VAL ASN ILE GLN LYS GLU ILE ASP ARG LEU ASN GLU
SEQRES 90 C 1215 VAL ALA LYS ASN LEU ASN GLU SER LEU ILE ASP LEU GLN
SEQRES 91 C 1215 GLU LEU GLY LYS TYR GLU GLN GLY SER GLY TYR ILE PRO
SEQRES 92 C 1215 GLU ALA PRO ARG ASP GLY GLN ALA TYR VAL ARG LYS ASP
SEQRES 93 C 1215 GLY GLU TRP VAL LEU LEU SER THR PHE LEU GLY ARG SER
SEQRES 94 C 1215 LEU GLU VAL LEU PHE GLN
SEQRES 1 A 1215 SER ASP LEU ASP ARG CYS THR THR PHE ASP ASP VAL GLN
SEQRES 2 A 1215 ALA PRO ASN TYR THR GLN HIS THR SER SER MET ARG GLY
SEQRES 3 A 1215 VAL TYR TYR PRO ASP GLU ILE PHE ARG SER ASP THR LEU
SEQRES 4 A 1215 TYR LEU THR GLN ASP LEU PHE LEU PRO PHE TYR SER ASN
SEQRES 5 A 1215 VAL THR GLY PHE HIS THR ILE ASN HIS THR PHE GLY ASN
SEQRES 6 A 1215 PRO VAL ILE PRO PHE LYS ASP GLY ILE TYR PHE ALA ALA
SEQRES 7 A 1215 THR GLU LYS SER ASN VAL VAL ARG GLY TRP VAL PHE GLY
SEQRES 8 A 1215 SER THR MET ASN ASN LYS SER GLN SER VAL ILE ILE ILE
SEQRES 9 A 1215 ASN ASN SER THR ASN VAL VAL ILE ARG ALA CYS ASN PHE
SEQRES 10 A 1215 GLU LEU CYS ASP ASN PRO PHE PHE ALA VAL SER LYS PRO
SEQRES 11 A 1215 MET GLY THR GLN THR HIS THR MET ILE PHE ASP ASN ALA
SEQRES 12 A 1215 PHE ASN CYS THR PHE GLU TYR ILE SER ASP ALA PHE SER
SEQRES 13 A 1215 LEU ASP VAL SER GLU LYS SER GLY ASN PHE LYS HIS LEU
SEQRES 14 A 1215 ARG GLU PHE VAL PHE LYS ASN LYS ASP GLY PHE LEU TYR
SEQRES 15 A 1215 VAL TYR LYS GLY TYR GLN PRO ILE ASP VAL VAL ARG ASP
SEQRES 16 A 1215 LEU PRO SER GLY PHE ASN THR LEU LYS PRO ILE PHE LYS
SEQRES 17 A 1215 LEU PRO LEU GLY ILE ASN ILE THR ASN PHE ARG ALA ILE
SEQRES 18 A 1215 LEU THR ALA PHE SER PRO ALA GLN ASP ILE TRP GLY THR
SEQRES 19 A 1215 SER ALA ALA ALA TYR PHE VAL GLY TYR LEU LYS PRO THR
SEQRES 20 A 1215 THR PHE MET LEU LYS TYR ASP GLU ASN GLY THR ILE THR
SEQRES 21 A 1215 ASP ALA VAL ASP CYS SER GLN ASN PRO LEU ALA GLU LEU
SEQRES 22 A 1215 LYS CYS SER VAL LYS SER PHE GLU ILE ASP LYS GLY ILE
SEQRES 23 A 1215 TYR GLN THR SER ASN PHE ARG VAL VAL PRO SER GLY ASP
SEQRES 24 A 1215 VAL VAL ARG PHE PRO ASN ILE THR ASN LEU CYS PRO PHE
SEQRES 25 A 1215 GLY GLU VAL PHE ASN ALA THR LYS PHE PRO SER VAL TYR
SEQRES 26 A 1215 ALA TRP GLU ARG LYS LYS ILE SER ASN CYS VAL ALA ASP
SEQRES 27 A 1215 TYR SER VAL LEU TYR ASN SER THR PHE PHE SER THR PHE
SEQRES 28 A 1215 LYS CYS TYR GLY VAL SER ALA THR LYS LEU ASN ASP LEU
SEQRES 29 A 1215 CYS PHE SER ASN VAL TYR ALA ASP SER PHE VAL VAL LYS
SEQRES 30 A 1215 GLY ASP ASP VAL ARG GLN ILE ALA PRO GLY GLN THR GLY
SEQRES 31 A 1215 VAL ILE ALA ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE
SEQRES 32 A 1215 MET GLY CYS VAL LEU ALA TRP ASN THR ARG ASN ILE ASP
SEQRES 33 A 1215 ALA THR SER THR GLY ASN TYR ASN TYR LYS TYR ARG TYR
SEQRES 34 A 1215 LEU ARG HIS GLY LYS LEU ARG PRO PHE GLU ARG ASP ILE
SEQRES 35 A 1215 SER ASN VAL PRO PHE SER PRO ASP GLY LYS PRO CYS THR
SEQRES 36 A 1215 PRO PRO ALA LEU ASN CYS TYR TRP PRO LEU ASN ASP TYR
SEQRES 37 A 1215 GLY PHE TYR THR THR THR GLY ILE GLY TYR GLN PRO TYR
SEQRES 38 A 1215 ARG VAL VAL VAL LEU SER PHE GLU LEU LEU ASN ALA PRO
SEQRES 39 A 1215 ALA THR VAL CYS GLY PRO LYS LEU SER THR ASP LEU ILE
SEQRES 40 A 1215 LYS ASN GLN CYS VAL ASN PHE ASN PHE ASN GLY LEU THR
SEQRES 41 A 1215 GLY THR GLY VAL LEU THR PRO SER SER LYS ARG PHE GLN
SEQRES 42 A 1215 PRO PHE GLN GLN PHE GLY ARG ASP VAL SER ASP PHE THR
SEQRES 43 A 1215 ASP SER VAL ARG ASP PRO LYS THR SER GLU ILE LEU ASP
SEQRES 44 A 1215 ILE SER PRO CYS ALA PHE GLY GLY VAL SER VAL ILE THR
SEQRES 45 A 1215 PRO GLY THR ASN ALA SER SER GLU VAL ALA VAL LEU TYR
SEQRES 46 A 1215 GLN ASP VAL ASN CYS THR ASP VAL SER THR ALA ILE HIS
SEQRES 47 A 1215 ALA ASP GLN LEU THR PRO ALA TRP ARG ILE TYR SER THR
SEQRES 48 A 1215 GLY ASN ASN VAL PHE GLN THR GLN ALA GLY CYS LEU ILE
SEQRES 49 A 1215 GLY ALA GLU HIS VAL ASP THR SER TYR GLU CYS ASP ILE
SEQRES 50 A 1215 PRO ILE GLY ALA GLY ILE CYS ALA SER TYR HIS THR VAL
SEQRES 51 A 1215 SER LEU LEU ARG SER THR SER GLN LYS SER ILE VAL ALA
SEQRES 52 A 1215 TYR THR MET SER LEU GLY ALA ASP SER SER ILE ALA TYR
SEQRES 53 A 1215 SER ASN ASN THR ILE ALA ILE PRO THR ASN PHE SER ILE
SEQRES 54 A 1215 SER ILE THR THR GLU VAL MET PRO VAL SER MET ALA LYS
SEQRES 55 A 1215 THR SER VAL ASP CYS ASN MET TYR ILE CYS GLY ASP SER
SEQRES 56 A 1215 THR GLU CYS ALA ASN LEU LEU LEU GLN TYR GLY SER PHE
SEQRES 57 A 1215 CYS THR GLN LEU ASN ARG ALA LEU SER GLY ILE ALA ALA
SEQRES 58 A 1215 GLU GLN ASP ARG ASN THR ARG GLU VAL PHE ALA GLN VAL
SEQRES 59 A 1215 LYS GLN MET TYR LYS THR PRO THR LEU LYS TYR PHE GLY
SEQRES 60 A 1215 GLY PHE ASN PHE SER GLN ILE LEU PRO ASP PRO LEU LYS
SEQRES 61 A 1215 PRO THR LYS ARG SER PHE ILE GLU ASP LEU LEU PHE ASN
SEQRES 62 A 1215 LYS VAL THR LEU ALA ASP ALA GLY PHE MET LYS GLN TYR
SEQRES 63 A 1215 GLY GLU CYS LEU GLY ASP ILE ASN ALA ARG ASP LEU ILE
SEQRES 64 A 1215 CYS ALA GLN LYS PHE ASN GLY LEU THR VAL LEU PRO PRO
SEQRES 65 A 1215 LEU LEU THR ASP ASP MET ILE ALA ALA TYR THR ALA ALA
SEQRES 66 A 1215 LEU VAL SER GLY THR ALA THR ALA GLY TRP THR PHE GLY
SEQRES 67 A 1215 ALA GLY ALA ALA LEU GLN ILE PRO PHE ALA MET GLN MET
SEQRES 68 A 1215 ALA TYR ARG PHE ASN GLY ILE GLY VAL THR GLN ASN VAL
SEQRES 69 A 1215 LEU TYR GLU ASN GLN LYS GLN ILE ALA ASN GLN PHE ASN
SEQRES 70 A 1215 LYS ALA ILE SER GLN ILE GLN GLU SER LEU THR THR THR
SEQRES 71 A 1215 SER THR ALA LEU GLY LYS LEU GLN ASP VAL VAL ASN GLN
SEQRES 72 A 1215 ASN ALA GLN ALA LEU ASN THR LEU VAL LYS GLN LEU SER
SEQRES 73 A 1215 SER ASN PHE GLY ALA ILE SER SER VAL LEU ASN ASP ILE
SEQRES 74 A 1215 LEU SER ARG LEU ASP PRO PRO GLU ALA GLU VAL GLN ILE
SEQRES 75 A 1215 ASP ARG LEU ILE THR GLY ARG LEU GLN SER LEU GLN THR
SEQRES 76 A 1215 TYR VAL THR GLN GLN LEU ILE ARG ALA ALA GLU ILE ARG
SEQRES 77 A 1215 ALA SER ALA ASN LEU ALA ALA THR LYS MET SER GLU CYS
SEQRES 78 A 1215 VAL LEU GLY GLN SER LYS ARG VAL ASP PHE CYS GLY LYS
SEQRES 79 A 1215 GLY TYR HIS LEU MET SER PHE PRO GLN ALA ALA PRO HIS
SEQRES 80 A 1215 GLY VAL VAL PHE LEU HIS VAL THR TYR VAL PRO SER GLN
SEQRES 81 A 1215 GLU ARG ASN PHE THR THR ALA PRO ALA ILE CYS HIS GLU
SEQRES 82 A 1215 GLY LYS ALA TYR PHE PRO ARG GLU GLY VAL PHE VAL PHE
SEQRES 83 A 1215 ASN GLY THR SER TRP PHE ILE THR GLN ARG ASN PHE PHE
SEQRES 84 A 1215 SER PRO GLN ILE ILE THR THR ASP ASN THR PHE VAL SER
SEQRES 85 A 1215 GLY ASN CYS ASP VAL VAL ILE GLY ILE ILE ASN ASN THR
SEQRES 86 A 1215 VAL TYR ASP PRO LEU GLN PRO GLU LEU ASP SER PHE LYS
SEQRES 87 A 1215 GLU GLU LEU ASP LYS TYR PHE LYS ASN HIS THR SER PRO
SEQRES 88 A 1215 ASP VAL ASP LEU GLY ASP ILE SER GLY ILE ASN ALA SER
SEQRES 89 A 1215 VAL VAL ASN ILE GLN LYS GLU ILE ASP ARG LEU ASN GLU
SEQRES 90 A 1215 VAL ALA LYS ASN LEU ASN GLU SER LEU ILE ASP LEU GLN
SEQRES 91 A 1215 GLU LEU GLY LYS TYR GLU GLN GLY SER GLY TYR ILE PRO
SEQRES 92 A 1215 GLU ALA PRO ARG ASP GLY GLN ALA TYR VAL ARG LYS ASP
SEQRES 93 A 1215 GLY GLU TRP VAL LEU LEU SER THR PHE LEU GLY ARG SER
SEQRES 94 A 1215 LEU GLU VAL LEU PHE GLN
HET NAG D 1 14
HET NAG D 2 14
HET NAG E 1 14
HET NAG E 2 14
HET BMA E 3 11
HET NAG F 1 14
HET NAG F 2 14
HET NAG G 1 14
HET NAG G 2 14
HET BMA G 3 11
HET MAN G 4 11
HET MAN G 5 11
HET NAG H 1 14
HET NAG H 2 14
HET BMA H 3 11
HET MAN H 4 11
HET MAN H 5 11
HET NAG I 1 14
HET NAG I 2 14
HET NAG J 1 14
HET NAG J 2 14
HET NAG K 1 14
HET NAG K 2 14
HET NAG L 1 14
HET NAG L 2 14
HET BMA L 3 11
HET NAG M 1 14
HET NAG M 2 14
HET NAG N 1 14
HET NAG N 2 14
HET BMA N 3 11
HET MAN N 4 11
HET NAG O 1 14
HET NAG O 2 14
HET BMA O 3 11
HET MAN O 4 11
HET NAG P 1 14
HET NAG P 2 14
HET BMA P 3 11
HET MAN P 4 11
HET NAG Q 1 14
HET NAG Q 2 14
HET BMA Q 3 11
HET NAG R 1 14
HET NAG R 2 14
HET NAG S 1 14
HET NAG S 2 14
HET BMA S 3 11
HET MAN S 4 11
HET MAN S 5 11
HET NAG T 1 14
HET NAG T 2 14
HET NAG U 1 14
HET NAG U 2 14
HET BMA U 3 11
HET NAG V 1 14
HET NAG V 2 14
HET BMA V 3 11
HET NAG W 1 14
HET NAG W 2 14
HET NAG X 1 14
HET NAG X 2 14
HET BMA X 3 11
HET NAG B1301 14
HET NAG B1302 14
HET NAG B1322 14
HET NAG B1323 14
HET NAG C1308 14
HET NAG C1321 14
HET NAG C1327 14
HET NAG A1301 14
HET NAG A1307 14
HET NAG A1316 14
HET NAG A1317 14
HET NAG A1323 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
FORMUL 4 NAG 54(C8 H15 N O6)
FORMUL 5 BMA 12(C6 H12 O6)
FORMUL 7 MAN 9(C6 H12 O6)
HELIX 1 AA1 ASN B 281 LYS B 291 1 11
HELIX 2 AA2 TYR B 352 ASN B 357 1 6
HELIX 3 AA3 THR B 372 LEU B 377 1 6
HELIX 4 AA4 ASP B 392 VAL B 394 5 3
HELIX 5 AA5 VAL B 404 ASN B 409 1 6
HELIX 6 AA6 CYS B 603 ALA B 612 1 10
HELIX 7 AA7 ASP B 719 ILE B 724 1 6
HELIX 8 AA8 SER B 728 LEU B 736 1 9
HELIX 9 AA9 GLN B 737 GLY B 739 5 3
HELIX 10 AB1 THR B 743 ALA B 765 1 23
HELIX 11 AB2 SER B 798 LYS B 807 1 10
HELIX 12 AB3 THR B 848 ALA B 864 1 17
HELIX 13 AB4 ALA B 866 PHE B 870 5 5
HELIX 14 AB5 PRO B 879 ILE B 891 1 13
HELIX 15 AB6 GLN B 895 GLU B 900 1 6
HELIX 16 AB7 ASN B 901 THR B 923 1 23
HELIX 17 AB8 LEU B 927 LYS B 946 1 20
HELIX 18 AB9 VAL B 958 LEU B 966 1 9
HELIX 19 AC1 GLU B 970 LEU B 1016 1 47
HELIX 20 AC2 ASN C 281 LYS C 291 1 11
HELIX 21 AC3 PHE C 325 ASN C 330 1 6
HELIX 22 AC4 TYR C 352 ASN C 357 1 6
HELIX 23 AC5 LYS C 390 ARG C 395 1 6
HELIX 24 AC6 THR C 425 ALA C 430 1 6
HELIX 25 AC7 GLY C 488 GLN C 492 5 5
HELIX 26 AC8 ASN C 602 ALA C 612 1 11
HELIX 27 AC9 ASP C 719 CYS C 725 1 7
HELIX 28 AD1 SER C 728 LEU C 734 1 7
HELIX 29 AD2 LEU C 735 GLY C 739 5 5
HELIX 30 AD3 SER C 740 ALA C 765 1 26
HELIX 31 AD4 SER C 798 LYS C 807 1 10
HELIX 32 AD5 THR C 848 ALA C 864 1 17
HELIX 33 AD6 TRP C 868 GLY C 873 1 6
HELIX 34 AD7 PRO C 879 GLY C 892 1 14
HELIX 35 AD8 GLN C 895 ASN C 901 1 7
HELIX 36 AD9 LYS C 903 THR C 922 1 20
HELIX 37 AE1 LEU C 927 GLN C 947 1 21
HELIX 38 AE2 LEU C 959 SER C 964 1 6
HELIX 39 AE3 ASP C 967 VAL C 1015 1 49
HELIX 40 AE4 ASN A 281 LYS A 291 1 11
HELIX 41 AE5 ALA A 371 ASN A 375 5 5
HELIX 42 AE6 GLY A 403 ASN A 409 1 7
HELIX 43 AE7 GLY A 488 GLN A 492 5 5
HELIX 44 AE8 CYS A 603 ASP A 613 1 11
HELIX 45 AE9 ASP A 719 CYS A 725 1 7
HELIX 46 AF1 SER A 728 LEU A 736 1 9
HELIX 47 AF2 SER A 740 PHE A 764 1 25
HELIX 48 AF3 SER A 798 LYS A 807 1 10
HELIX 49 AF4 THR A 848 GLY A 867 1 20
HELIX 50 AF5 TRP A 868 GLY A 871 5 4
HELIX 51 AF6 PRO A 879 GLY A 892 1 14
HELIX 52 AF7 GLN A 895 ASN A 901 1 7
HELIX 53 AF8 ASN A 901 THR A 922 1 22
HELIX 54 AF9 LEU A 927 GLN A 947 1 21
HELIX 55 AG1 LEU A 948 SER A 950 5 3
HELIX 56 AG2 VAL A 958 LEU A 963 1 6
HELIX 57 AG3 ASP A 967 GLU A 1013 1 47
SHEET 1 AA1 7 THR B 31 THR B 34 0
SHEET 2 AA1 7 ASN B 65 THR B 71 -1 O GLY B 68 N THR B 31
SHEET 3 AA1 7 ALA B 250 TYR B 256 -1 O ALA B 250 N THR B 71
SHEET 4 AA1 7 GLY B 86 GLU B 93 -1 N ALA B 90 O PHE B 253
SHEET 5 AA1 7 PHE B 179 LYS B 190 -1 O HIS B 181 N GLU B 93
SHEET 6 AA1 7 PHE B 193 VAL B 205 -1 O GLY B 199 N GLU B 184
SHEET 7 AA1 7 LYS B 217 PRO B 218 -1 O LYS B 217 N LYS B 198
SHEET 1 AA2 7 THR B 31 THR B 34 0
SHEET 2 AA2 7 ASN B 65 THR B 71 -1 O GLY B 68 N THR B 31
SHEET 3 AA2 7 ALA B 250 TYR B 256 -1 O ALA B 250 N THR B 71
SHEET 4 AA2 7 GLY B 86 GLU B 93 -1 N ALA B 90 O PHE B 253
SHEET 5 AA2 7 PHE B 179 LYS B 190 -1 O HIS B 181 N GLU B 93
SHEET 6 AA2 7 PHE B 193 VAL B 205 -1 O GLY B 199 N GLU B 184
SHEET 7 AA2 7 LEU B 222 PRO B 223 -1 O LEU B 222 N LEU B 194
SHEET 1 AA3 3 ILE B 46 PHE B 47 0
SHEET 2 AA3 3 PHE A 551 ARG A 553 1 O ARG A 553 N PHE B 47
SHEET 3 AA3 3 THR A 559 VAL A 562 -1 O SER A 561 N GLY A 552
SHEET 1 AA4 3 THR B 51 GLN B 56 0
SHEET 2 AA4 3 THR B 261 TYR B 266 -1 O LEU B 264 N TYR B 53
SHEET 3 AA4 3 ILE B 272 ASP B 277 -1 O ASP B 274 N LYS B 265
SHEET 1 AA5 6 VAL B 80 PRO B 82 0
SHEET 2 AA5 6 ASN B 230 PHE B 238 -1 O PHE B 231 N ILE B 81
SHEET 3 AA5 6 VAL B 98 GLY B 104 -1 N GLY B 100 O ILE B 234
SHEET 4 AA5 6 SER B 113 ASN B 118 -1 O VAL B 114 N PHE B 103
SHEET 5 AA5 6 ASN B 122 SER B 141 -1 O ARG B 126 N ILE B 115
SHEET 6 AA5 6 THR B 146 ALA B 167 -1 O TYR B 163 N ILE B 125
SHEET 1 AA6 4 VAL B 80 PRO B 82 0
SHEET 2 AA6 4 ASN B 230 PHE B 238 -1 O PHE B 231 N ILE B 81
SHEET 3 AA6 4 ASN B 122 SER B 141 1 N VAL B 140 O ALA B 237
SHEET 4 AA6 4 THR B 146 ALA B 167 -1 O TYR B 163 N ILE B 125
SHEET 1 AA7 6 LEU B 615 THR B 616 0
SHEET 2 AA7 6 GLY B 298 VAL B 307 -1 N ARG B 306 O THR B 616
SHEET 3 AA7 6 PHE B 578 THR B 585 -1 O GLY B 579 N PHE B 305
SHEET 4 AA7 6 ALA B 595 GLN B 599 -1 O ALA B 595 N ILE B 584
SHEET 5 AA7 6 GLY B 634 ILE B 637 -1 O ILE B 637 N VAL B 596
SHEET 6 AA7 6 VAL B 628 GLN B 630 -1 N PHE B 629 O LEU B 636
SHEET 1 AA8 6 ASP B 312 ARG B 315 0
SHEET 2 AA8 6 VAL B 525 PHE B 529 1 O ASN B 528 N VAL B 313
SHEET 3 AA8 6 THR B 533 PRO B 540 -1 O GLY B 536 N VAL B 525
SHEET 4 AA8 6 ILE B 570 SER B 574 -1 O ASP B 572 N THR B 539
SHEET 5 AA8 6 THR B 559 ARG B 563 -1 N VAL B 562 O LEU B 571
SHEET 6 AA8 6 PHE B 551 ARG B 553 -1 N GLY B 552 O SER B 561
SHEET 1 AA9 3 LYS B 344 ILE B 345 0
SHEET 2 AA9 3 SER B 380 TYR B 383 -1 O VAL B 382 N ILE B 345
SHEET 3 AA9 3 PHE B 501 GLU B 502 -1 O GLU B 502 N ASN B 381
SHEET 1 AB1 2 CYS B 348 VAL B 349 0
SHEET 2 AB1 2 VAL B 510 CYS B 511 1 O CYS B 511 N CYS B 348
SHEET 1 AB2 4 LYS B 365 CYS B 366 0
SHEET 2 AB2 4 CYS B 419 ASN B 424 -1 O VAL B 420 N LYS B 365
SHEET 3 AB2 4 PRO B 493 LEU B 499 -1 O LEU B 499 N CYS B 419
SHEET 4 AB2 4 ASP B 385 LYS B 390 -1 N PHE B 387 O VAL B 496
SHEET 1 AB3 2 LYS B 439 ARG B 441 0
SHEET 2 AB3 2 LEU B 478 ASP B 480 -1 O ASN B 479 N TYR B 440
SHEET 1 AB4 4 GLU B 640 TYR B 646 0
SHEET 2 AB4 4 SER B 673 MET B 679 1 O ALA B 676 N GLU B 640
SHEET 3 AB4 4 ILE B 656 HIS B 661 -1 N SER B 659 O VAL B 675
SHEET 4 AB4 4 ILE B 650 GLY B 653 -1 N ILE B 650 O ALA B 658
SHEET 1 AB5 2 ASP B 684 SER B 685 0
SHEET 2 AB5 2 MET C 770 TYR C 771 1 O MET C 770 N SER B 685
SHEET 1 AB6 3 THR B 693 MET B 709 0
SHEET 2 AB6 3 GLY B1041 ALA B1060 -1 O PHE B1044 N GLU B 707
SHEET 3 AB6 3 TYR B1029 ALA B1038 -1 N LEU B1031 O VAL B1047
SHEET 1 AB7 4 THR B 693 MET B 709 0
SHEET 2 AB7 4 GLY B1041 ALA B1060 -1 O PHE B1044 N GLU B 707
SHEET 3 AB7 4 VAL B1076 PHE B1079 -1 O PHE B1079 N THR B1058
SHEET 4 AB7 4 TRP B1084 THR B1087 -1 O PHE B1085 N VAL B1078
SHEET 1 AB8 2 THR B 716 VAL B 718 0
SHEET 2 AB8 2 LEU B 840 VAL B 842 -1 O THR B 841 N SER B 717
SHEET 1 AB9 2 GLN B 769 TYR B 771 0
SHEET 2 AB9 2 ALA A 683 SER A 685 1 O ALA A 683 N MET B 770
SHEET 1 AC1 2 TYR B 778 PHE B 779 0
SHEET 2 AC1 2 PHE B 782 ASN B 783 -1 O PHE B 782 N PHE B 779
SHEET 1 AC2 4 THR B1102 ASN B1107 0
SHEET 2 AC2 4 LYS B1068 PRO B1072 -1 N PHE B1071 O PHE B1103
SHEET 3 AC2 4 ILE B1063 HIS B1065 -1 N HIS B1065 O LYS B1068
SHEET 4 AC2 4 ILE B1115 ASN B1116 1 O ILE B1115 N CYS B1064
SHEET 1 AC3 8 THR C 31 HIS C 33 0
SHEET 2 AC3 8 VAL C 66 THR C 71 -1 O VAL C 66 N HIS C 33
SHEET 3 AC3 8 ALA C 250 TYR C 256 -1 O ALA C 250 N THR C 71
SHEET 4 AC3 8 ILE C 87 GLU C 93 -1 N TYR C 88 O GLY C 255
SHEET 5 AC3 8 PHE C 179 LYS C 190 -1 O PHE C 185 N PHE C 89
SHEET 6 AC3 8 PHE C 193 VAL C 205 -1 O TYR C 195 N LYS C 188
SHEET 7 AC3 8 THR C 215 PRO C 223 -1 O ILE C 219 N VAL C 196
SHEET 8 AC3 8 VAL C 40 TYR C 41 1 N VAL C 40 O LEU C 216
SHEET 1 AC4 3 LEU C 52 PHE C 59 0
SHEET 2 AC4 3 LYS C 258 TYR C 266 -1 O LYS C 258 N PHE C 59
SHEET 3 AC4 3 ILE C 272 ASP C 277 -1 O THR C 273 N LYS C 265
SHEET 1 AC5 4 ILE C 81 PRO C 82 0
SHEET 2 AC5 4 ASN C 230 SER C 239 -1 O PHE C 231 N ILE C 81
SHEET 3 AC5 4 PHE C 137 SER C 141 1 N PHE C 138 O LEU C 235
SHEET 4 AC5 4 GLN C 147 HIS C 149 -1 O HIS C 149 N ALA C 139
SHEET 1 AC6 6 ILE C 81 PRO C 82 0
SHEET 2 AC6 6 ASN C 230 SER C 239 -1 O PHE C 231 N ILE C 81
SHEET 3 AC6 6 VAL C 98 GLY C 104 -1 N GLY C 104 O ASN C 230
SHEET 4 AC6 6 SER C 113 ASN C 118 -1 O VAL C 114 N PHE C 103
SHEET 5 AC6 6 VAL C 123 ASN C 129 -1 O CYS C 128 N SER C 113
SHEET 6 AC6 6 PHE C 157 ILE C 164 -1 O TYR C 163 N ILE C 125
SHEET 1 AC7 6 LEU C 615 THR C 616 0
SHEET 2 AC7 6 GLY C 298 VAL C 307 -1 N ARG C 306 O THR C 616
SHEET 3 AC7 6 PHE C 578 THR C 585 -1 O VAL C 583 N TYR C 300
SHEET 4 AC7 6 ALA C 595 GLN C 599 -1 O LEU C 597 N SER C 582
SHEET 5 AC7 6 GLY C 634 ILE C 637 -1 O CYS C 635 N TYR C 598
SHEET 6 AC7 6 VAL C 628 THR C 631 -1 N THR C 631 O GLY C 634
SHEET 1 AC8 7 ASP C 312 VAL C 314 0
SHEET 2 AC8 7 CYS C 524 ASN C 528 1 O ASN C 528 N VAL C 313
SHEET 3 AC8 7 THR C 533 PRO C 540 -1 O GLY C 536 N VAL C 525
SHEET 4 AC8 7 ILE C 570 SER C 574 -1 O ASP C 572 N THR C 539
SHEET 5 AC8 7 THR C 559 ARG C 563 -1 N VAL C 562 O LEU C 571
SHEET 6 AC8 7 PHE C 551 ARG C 553 -1 N GLY C 552 O SER C 561
SHEET 7 AC8 7 ILE A 46 PHE A 47 1 O PHE A 47 N ARG C 553
SHEET 1 AC9 2 LYS C 344 ILE C 345 0
SHEET 2 AC9 2 VAL C 382 TYR C 383 -1 O VAL C 382 N ILE C 345
SHEET 1 AD1 4 LYS C 365 CYS C 366 0
SHEET 2 AD1 4 CYS C 419 ASN C 424 -1 O VAL C 420 N LYS C 365
SHEET 3 AD1 4 TYR C 494 VAL C 498 -1 O VAL C 497 N LEU C 421
SHEET 4 AD1 4 ASP C 385 VAL C 389 -1 N ASP C 385 O VAL C 498
SHEET 1 AD2 2 LYS C 439 ARG C 441 0
SHEET 2 AD2 2 LEU C 478 ASP C 480 -1 O ASN C 479 N TYR C 440
SHEET 1 AD3 4 GLU C 640 TYR C 646 0
SHEET 2 AD3 4 SER C 673 MET C 679 1 O ALA C 676 N VAL C 642
SHEET 3 AD3 4 ILE C 656 HIS C 661 -1 N HIS C 661 O SER C 673
SHEET 4 AD3 4 ILE C 650 GLY C 653 -1 N ILE C 650 O ALA C 658
SHEET 1 AD4 2 ALA C 683 SER C 685 0
SHEET 2 AD4 2 GLN A 769 TYR A 771 1 O MET A 770 N SER C 685
SHEET 1 AD5 3 THR C 693 MET C 709 0
SHEET 2 AD5 3 GLY C1041 ALA C1060 -1 O PHE C1044 N GLU C 707
SHEET 3 AD5 3 GLN C1036 ALA C1038 -1 N GLN C1036 O VAL C1043
SHEET 1 AD6 4 HIS C1030 SER C1033 0
SHEET 2 AD6 4 GLY C1041 ALA C1060 -1 O VAL C1047 N LEU C1031
SHEET 3 AD6 4 VAL C1076 PHE C1079 -1 O PHE C1079 N THR C1058
SHEET 4 AD6 4 TRP C1084 THR C1087 -1 O PHE C1085 N VAL C1078
SHEET 1 AD7 2 THR C 716 VAL C 718 0
SHEET 2 AD7 2 LEU C 840 VAL C 842 -1 O THR C 841 N SER C 717
SHEET 1 AD8 2 GLU C 821 LEU C 823 0
SHEET 2 AD8 2 ILE C 832 ALA C 834 -1 O ALA C 834 N GLU C 821
SHEET 1 AD9 3 ILE C1063 HIS C1065 0
SHEET 2 AD9 3 LYS C1068 PRO C1072 -1 O LYS C1068 N HIS C1065
SHEET 3 AD9 3 THR C1102 VAL C1104 -1 O PHE C1103 N PHE C1071
SHEET 1 AE1 8 THR A 31 HIS A 33 0
SHEET 2 AE1 8 VAL A 66 THR A 71 -1 O GLY A 68 N THR A 31
SHEET 3 AE1 8 ALA A 250 PHE A 253 -1 O ALA A 250 N THR A 71
SHEET 4 AE1 8 ILE A 87 GLU A 93 -1 N THR A 92 O ALA A 251
SHEET 5 AE1 8 HIS A 181 LYS A 190 -1 O PHE A 185 N PHE A 89
SHEET 6 AE1 8 PHE A 193 PRO A 202 -1 O GLY A 199 N GLU A 184
SHEET 7 AE1 8 THR A 215 PRO A 223 -1 O LYS A 217 N LYS A 198
SHEET 8 AE1 8 VAL A 40 TYR A 41 1 N VAL A 40 O LEU A 216
SHEET 1 AE2 3 LEU A 52 PHE A 59 0
SHEET 2 AE2 3 LYS A 258 TYR A 266 -1 O LYS A 258 N PHE A 59
SHEET 3 AE2 3 ILE A 272 ASP A 277 -1 O THR A 273 N LYS A 265
SHEET 1 AE3 4 ILE A 81 PRO A 82 0
SHEET 2 AE3 4 ASN A 230 SER A 239 -1 O PHE A 231 N ILE A 81
SHEET 3 AE3 4 LEU A 132 SER A 141 1 N PHE A 138 O ALA A 237
SHEET 4 AE3 4 GLN A 147 PHE A 153 -1 O THR A 148 N ALA A 139
SHEET 1 AE4 6 ILE A 81 PRO A 82 0
SHEET 2 AE4 6 ASN A 230 SER A 239 -1 O PHE A 231 N ILE A 81
SHEET 3 AE4 6 GLY A 100 GLY A 104 -1 N GLY A 104 O ASN A 230
SHEET 4 AE4 6 SER A 113 ASN A 118 -1 O VAL A 114 N PHE A 103
SHEET 5 AE4 6 VAL A 123 CYS A 128 -1 O ARG A 126 N ILE A 115
SHEET 6 AE4 6 PHE A 161 ILE A 164 -1 O TYR A 163 N ILE A 125
SHEET 1 AE5 5 TYR A 300 GLN A 301 0
SHEET 2 AE5 5 VAL A 581 ILE A 584 -1 O VAL A 583 N TYR A 300
SHEET 3 AE5 5 ALA A 595 GLN A 599 -1 O LEU A 597 N SER A 582
SHEET 4 AE5 5 GLY A 634 ILE A 637 -1 O CYS A 635 N TYR A 598
SHEET 5 AE5 5 VAL A 628 GLN A 630 -1 N PHE A 629 O LEU A 636
SHEET 1 AE6 3 PHE A 578 GLY A 579 0
SHEET 2 AE6 3 PHE A 305 VAL A 307 -1 N PHE A 305 O GLY A 579
SHEET 3 AE6 3 LEU A 615 THR A 616 -1 O THR A 616 N ARG A 306
SHEET 1 AE7 4 ASP A 312 VAL A 314 0
SHEET 2 AE7 4 VAL A 525 ASN A 528 1 O ASN A 528 N VAL A 313
SHEET 3 AE7 4 THR A 533 PRO A 540 -1 O GLY A 534 N PHE A 527
SHEET 4 AE7 4 LEU A 571 SER A 574 -1 O ASP A 572 N THR A 539
SHEET 1 AE8 5 GLU A 341 LYS A 344 0
SHEET 2 AE8 5 TYR A 383 VAL A 389 -1 O ALA A 384 N LYS A 343
SHEET 3 AE8 5 TYR A 494 SER A 500 -1 O VAL A 496 N PHE A 387
SHEET 4 AE8 5 MET A 417 ASN A 424 -1 N TRP A 423 O ARG A 495
SHEET 5 AE8 5 LYS A 365 CYS A 366 -1 N LYS A 365 O VAL A 420
SHEET 1 AE9 2 CYS A 348 VAL A 349 0
SHEET 2 AE9 2 VAL A 510 CYS A 511 1 O CYS A 511 N CYS A 348
SHEET 1 AF1 2 LYS A 439 ARG A 441 0
SHEET 2 AF1 2 LEU A 478 ASP A 480 -1 O ASN A 479 N TYR A 440
SHEET 1 AF2 4 GLU A 640 HIS A 641 0
SHEET 2 AF2 4 SER A 673 THR A 678 1 O ALA A 676 N GLU A 640
SHEET 3 AF2 4 ILE A 656 HIS A 661 -1 N SER A 659 O VAL A 675
SHEET 4 AF2 4 ILE A 650 GLY A 653 -1 N ILE A 650 O ALA A 658
SHEET 1 AF3 3 THR A 693 PRO A 710 0
SHEET 2 AF3 3 GLY A1041 ALA A1060 -1 O HIS A1046 N THR A 705
SHEET 3 AF3 3 GLN A1036 ALA A1038 -1 N GLN A1036 O VAL A1043
SHEET 1 AF4 5 TYR A1029 SER A1033 0
SHEET 2 AF4 5 GLY A1041 ALA A1060 -1 O TYR A1049 N TYR A1029
SHEET 3 AF4 5 VAL A1076 PHE A1079 -1 O PHE A1079 N THR A1058
SHEET 4 AF4 5 TRP A1084 THR A1087 -1 O PHE A1085 N VAL A1078
SHEET 5 AF4 5 GLN A1095 ILE A1096 -1 O GLN A1095 N ILE A1086
SHEET 1 AF5 2 THR A 716 VAL A 718 0
SHEET 2 AF5 2 LEU A 840 VAL A 842 -1 O THR A 841 N SER A 717
SHEET 1 AF6 2 TYR A 778 PHE A 779 0
SHEET 2 AF6 2 PHE A 782 ASN A 783 -1 O PHE A 782 N PHE A 779
SHEET 1 AF7 4 PHE A1103 VAL A1104 0
SHEET 2 AF7 4 ALA A1069 PHE A1071 -1 N PHE A1071 O PHE A1103
SHEET 3 AF7 4 ALA A1062 CYS A1064 -1 N ILE A1063 O TYR A1070
SHEET 4 AF7 4 ILE A1114 ASN A1116 1 O ILE A1115 N ALA A1062
SSBOND 1 CYS B 19 CYS B 133 1555 1555 2.04
SSBOND 2 CYS B 128 CYS B 159 1555 1555 2.03
SSBOND 3 CYS B 278 CYS B 288 1555 1555 2.03
SSBOND 4 CYS B 323 CYS B 348 1555 1555 2.03
SSBOND 5 CYS B 366 CYS B 419 1555 1555 2.03
SSBOND 6 CYS B 378 CYS B 511 1555 1555 2.03
SSBOND 7 CYS B 467 CYS B 474 1555 1555 2.03
SSBOND 8 CYS B 524 CYS B 576 1555 1555 2.02
SSBOND 9 CYS B 603 CYS B 635 1555 1555 2.03
SSBOND 10 CYS B 648 CYS B 657 1555 1555 2.03
SSBOND 11 CYS B 720 CYS B 742 1555 1555 2.03
SSBOND 12 CYS B 725 CYS B 731 1555 1555 2.02
SSBOND 13 CYS B 822 CYS B 833 1555 1555 2.03
SSBOND 14 CYS B 1014 CYS B 1025 1555 1555 2.03
SSBOND 15 CYS B 1064 CYS B 1108 1555 1555 2.03
SSBOND 16 CYS C 19 CYS C 133 1555 1555 2.03
SSBOND 17 CYS C 128 CYS C 159 1555 1555 2.03
SSBOND 18 CYS C 278 CYS C 288 1555 1555 2.03
SSBOND 19 CYS C 323 CYS C 348 1555 1555 2.03
SSBOND 20 CYS C 366 CYS C 419 1555 1555 2.03
SSBOND 21 CYS C 378 CYS C 511 1555 1555 2.03
SSBOND 22 CYS C 467 CYS C 474 1555 1555 2.03
SSBOND 23 CYS C 524 CYS C 576 1555 1555 2.03
SSBOND 24 CYS C 603 CYS C 635 1555 1555 2.03
SSBOND 25 CYS C 648 CYS C 657 1555 1555 2.03
SSBOND 26 CYS C 720 CYS C 742 1555 1555 2.03
SSBOND 27 CYS C 725 CYS C 731 1555 1555 2.03
SSBOND 28 CYS C 822 CYS C 833 1555 1555 2.03
SSBOND 29 CYS C 1014 CYS C 1025 1555 1555 2.02
SSBOND 30 CYS C 1064 CYS C 1108 1555 1555 2.03
SSBOND 31 CYS A 19 CYS A 133 1555 1555 2.04
SSBOND 32 CYS A 128 CYS A 159 1555 1555 2.03
SSBOND 33 CYS A 278 CYS A 288 1555 1555 2.03
SSBOND 34 CYS A 323 CYS A 348 1555 1555 2.03
SSBOND 35 CYS A 366 CYS A 419 1555 1555 2.03
SSBOND 36 CYS A 378 CYS A 511 1555 1555 2.04
SSBOND 37 CYS A 467 CYS A 474 1555 1555 2.03
SSBOND 38 CYS A 524 CYS A 576 1555 1555 2.02
SSBOND 39 CYS A 603 CYS A 635 1555 1555 2.03
SSBOND 40 CYS A 648 CYS A 657 1555 1555 2.03
SSBOND 41 CYS A 720 CYS A 742 1555 1555 2.03
SSBOND 42 CYS A 725 CYS A 731 1555 1555 2.03
SSBOND 43 CYS A 822 CYS A 833 1555 1555 2.03
SSBOND 44 CYS A 1014 CYS A 1025 1555 1555 2.03
SSBOND 45 CYS A 1064 CYS A 1108 1555 1555 2.03
LINK ND2 ASN B 65 C1 NAG B1302 1555 1555 1.44
LINK ND2 ASN B 269 C1 NAG D 1 1555 1555 1.43
LINK ND2 ASN B 318 C1 NAG E 1 1555 1555 1.43
LINK ND2 ASN B 589 C1 NAG F 1 1555 1555 1.44
LINK ND2 ASN B 602 C1 NAG J 1 1555 1555 1.44
LINK ND2 ASN B 691 C1 NAG B1323 1555 1555 1.43
LINK ND2 ASN B 699 C1 NAG G 1 1555 1555 1.43
LINK ND2 ASN B 783 C1 NAG H 1 1555 1555 1.43
LINK ND2 ASN B1056 C1 NAG B1301 1555 1555 1.43
LINK ND2 ASN B1080 C1 NAG I 1 1555 1555 1.43
LINK ND2 ASN B1116 C1 NAG B1322 1555 1555 1.43
LINK ND2 ASN C 65 C1 NAG K 1 1555 1555 1.44
LINK ND2 ASN C 269 C1 NAG L 1 1555 1555 1.43
LINK ND2 ASN C 318 C1 NAG M 1 1555 1555 1.44
LINK ND2 ASN C 589 C1 NAG C1308 1555 1555 1.44
LINK ND2 ASN C 602 C1 NAG N 1 1555 1555 1.45
LINK ND2 ASN C 691 C1 NAG C1327 1555 1555 1.44
LINK ND2 ASN C 699 C1 NAG O 1 1555 1555 1.43
LINK ND2 ASN C 783 C1 NAG P 1 1555 1555 1.44
LINK ND2 ASN C1056 C1 NAG C1321 1555 1555 1.44
LINK ND2 ASN C1080 C1 NAG Q 1 1555 1555 1.43
LINK ND2 ASN C1116 C1 NAG R 1 1555 1555 1.44
LINK ND2 ASN A 65 C1 NAG A1301 1555 1555 1.44
LINK ND2 ASN A 269 C1 NAG S 1 1555 1555 1.43
LINK ND2 ASN A 318 C1 NAG X 1 1555 1555 1.44
LINK ND2 ASN A 589 C1 NAG A1307 1555 1555 1.44
LINK ND2 ASN A 602 C1 NAG T 1 1555 1555 1.44
LINK ND2 ASN A 691 C1 NAG A1323 1555 1555 1.43
LINK ND2 ASN A 699 C1 NAG U 1 1555 1555 1.44
LINK ND2 ASN A 783 C1 NAG V 1 1555 1555 1.44
LINK ND2 ASN A1056 C1 NAG A1316 1555 1555 1.43
LINK ND2 ASN A1080 C1 NAG W 1 1555 1555 1.43
LINK ND2 ASN A1116 C1 NAG A1317 1555 1555 1.44
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44
LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.45
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.45
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.43
LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.45
LINK O3 BMA G 3 C1 MAN G 4 1555 1555 1.44
LINK O6 BMA G 3 C1 MAN G 5 1555 1555 1.44
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.44
LINK O4 NAG H 2 C1 BMA H 3 1555 1555 1.45
LINK O3 BMA H 3 C1 MAN H 4 1555 1555 1.44
LINK O6 BMA H 3 C1 MAN H 5 1555 1555 1.44
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.45
LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44
LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.45
LINK O4 NAG L 2 C1 BMA L 3 1555 1555 1.45
LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.45
LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44
LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.45
LINK O3 BMA N 3 C1 MAN N 4 1555 1555 1.45
LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.44
LINK O4 NAG O 2 C1 BMA O 3 1555 1555 1.44
LINK O3 BMA O 3 C1 MAN O 4 1555 1555 1.44
LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.44
LINK O4 NAG P 2 C1 BMA P 3 1555 1555 1.44
LINK O3 BMA P 3 C1 MAN P 4 1555 1555 1.46
LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.44
LINK O4 NAG Q 2 C1 BMA Q 3 1555 1555 1.45
LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.43
LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.44
LINK O4 NAG S 2 C1 BMA S 3 1555 1555 1.45
LINK O3 BMA S 3 C1 MAN S 4 1555 1555 1.45
LINK O6 BMA S 3 C1 MAN S 5 1555 1555 1.44
LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.47
LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.45
LINK O4 NAG U 2 C1 BMA U 3 1555 1555 1.45
LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.46
LINK O4 NAG V 2 C1 BMA V 3 1555 1555 1.44
LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.45
LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.45
LINK O4 NAG X 2 C1 BMA X 3 1555 1555 1.44
CISPEP 1 PRO B 469 PRO B 470 0 7.97
CISPEP 2 THR B 616 PRO B 617 0 3.91
CISPEP 3 PRO C 469 PRO C 470 0 -0.16
CISPEP 4 THR C 616 PRO C 617 0 6.45
CISPEP 5 PRO A 469 PRO A 470 0 -0.71
CISPEP 6 THR A 616 PRO A 617 0 0.34
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
