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casp_data / casp16 /experiment_structures /H1233s2.pdb
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HEADER VIRAL PROTEIN/IMMUNE SYSTEM 19-JUN-24 9CBN
TITLE HASTV1 SPIKE IN COMPLEX WITH NEUTRALIZING FABS 3H4 AND 3B4
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HASTV1 NEUTRALIZING FAB 3B4 KAPPA CHAIN;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES;
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 STRAIN: BALB/C;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: CHO-S;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 12 ORGANISM_COMMON: MOUSE;
SOURCE 13 ORGANISM_TAXID: 10090;
SOURCE 14 STRAIN: BALB/C;
SOURCE 15 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 16 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: CHO-S;
SOURCE 19 MOL_ID: 3;
SOURCE 20 ORGANISM_SCIENTIFIC: HUMAN ASTROVIRUS 1;
SOURCE 21 ORGANISM_TAXID: 12456;
SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 23 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 24 MOL_ID: 4;
SOURCE 25 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 26 ORGANISM_COMMON: MOUSE;
SOURCE 27 ORGANISM_TAXID: 10090;
SOURCE 28 STRAIN: BALB/C;
SOURCE 29 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 30 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 31 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 32 EXPRESSION_SYSTEM_CELL_LINE: CHO-S;
SOURCE 33 MOL_ID: 5;
SOURCE 34 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 35 ORGANISM_COMMON: MOUSE;
SOURCE 36 ORGANISM_TAXID: 10090;
SOURCE 37 STRAIN: BALB/C;
SOURCE 38 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 39 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 40 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 41 EXPRESSION_SYSTEM_CELL_LINE: CHO-S
KEYWDS ANTIBODY, VIRUS, SPIKE, HOMODIMER, VIRAL PROTEIN-IMMUNE SYSTEM
KEYWDS 2 COMPLEX
EXPDTA ELECTRON MICROSCOPY
AUTHOR S.LANNING,R.M.DUBOIS,V.H.BALASCO SERRAO
REVDAT 3 05-MAR-25 9CBN 1 JRNL
REVDAT 2 05-FEB-25 9CBN 1 JRNL
REVDAT 1 25-DEC-24 9CBN 0
JRNL AUTH S.LANNING,N.AGUILAR-HERNANDEZ,V.H.B.SERRAO,T.LOPEZ,
JRNL AUTH 2 S.M.O'ROURKE,A.LENTZ,L.RICEMEYER,R.ESPINOSA,S.LOPEZ,
JRNL AUTH 3 C.F.ARIAS,R.M.DUBOIS
JRNL TITL DISCOVERY OF THREE NOVEL NEUTRALIZING ANTIBODY EPITOPES ON
JRNL TITL 2 THE HUMAN ASTROVIRUS CAPSID SPIKE AND MECHANISTIC INSIGHTS
JRNL TITL 3 INTO VIRUS NEUTRALIZATION.
JRNL REF J.VIROL. V. 99 61924 2025
JRNL REFN ESSN 1098-5514
JRNL PMID 39846739
JRNL DOI 10.1128/JVI.01619-24
REMARK 2
REMARK 2 RESOLUTION. 3.33 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : PHENIX
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : 5EWO
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : RIGID BODY FIT
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : 112.000
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) : 3.330
REMARK 3 NUMBER OF PARTICLES : 163237
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 9CBN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUN-24.
REMARK 100 THE DEPOSITION ID IS D_1000284956.
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 : HUMAN ASTROVIRUS 1 SPIKE IN
REMARK 245 COMPLEX WITH FAB 3B4 AND FAB
REMARK 245 3H4; HASTV1 NEUTRALIZING FAB
REMARK 245 3B4; RECOMBINANT HUMAN
REMARK 245 ASTROVIRUS SEROTYPE 1 SPIKE
REMARK 245 PROTEIN; HASTV1 NEUTRALIZING
REMARK 245 FAB 3H4
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.86
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 8.00
REMARK 245 SAMPLE DETAILS : RECOMBINANT FAB EXPRESSED IN
REMARK 245 CHO-S CELLS
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 7235
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : TFS KRIOS
REMARK 245 DETECTOR TYPE : GATAN K3 BIOCONTINUUM (6K X
REMARK 245 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 500.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 3226.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : NULL
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: OCTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J
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 GLN A 1
REMARK 465 LEU A 11
REMARK 465 VAL A 12
REMARK 465 LYS A 13
REMARK 465 PRO A 41
REMARK 465 GLY A 42
REMARK 465 GLN A 43
REMARK 465 GLU A 89
REMARK 465 ASP A 90
REMARK 465 VAL A 114
REMARK 465 SER A 115
REMARK 465 SER A 116
REMARK 465 ALA A 117
REMARK 465 SER A 118
REMARK 465 THR A 119
REMARK 465 LYS A 120
REMARK 465 GLY A 121
REMARK 465 PRO A 122
REMARK 465 SER A 123
REMARK 465 VAL A 124
REMARK 465 PHE A 125
REMARK 465 PRO A 126
REMARK 465 LEU A 127
REMARK 465 ALA A 128
REMARK 465 PRO A 129
REMARK 465 SER A 130
REMARK 465 SER A 131
REMARK 465 LYS A 132
REMARK 465 SER A 133
REMARK 465 THR A 134
REMARK 465 SER A 135
REMARK 465 GLY A 136
REMARK 465 GLY A 137
REMARK 465 THR A 138
REMARK 465 ALA A 139
REMARK 465 ALA A 140
REMARK 465 LEU A 141
REMARK 465 GLY A 142
REMARK 465 CYS A 143
REMARK 465 LEU A 144
REMARK 465 VAL A 145
REMARK 465 LYS A 146
REMARK 465 ASP A 147
REMARK 465 TYR A 148
REMARK 465 PHE A 149
REMARK 465 PRO A 150
REMARK 465 GLU A 151
REMARK 465 PRO A 152
REMARK 465 VAL A 153
REMARK 465 THR A 154
REMARK 465 VAL A 155
REMARK 465 SER A 156
REMARK 465 TRP A 157
REMARK 465 ASN A 158
REMARK 465 SER A 159
REMARK 465 GLY A 160
REMARK 465 ALA A 161
REMARK 465 LEU A 162
REMARK 465 THR A 163
REMARK 465 SER A 164
REMARK 465 GLY A 165
REMARK 465 VAL A 166
REMARK 465 HIS A 167
REMARK 465 THR A 168
REMARK 465 PHE A 169
REMARK 465 PRO A 170
REMARK 465 ALA A 171
REMARK 465 VAL A 172
REMARK 465 LEU A 173
REMARK 465 GLN A 174
REMARK 465 SER A 175
REMARK 465 SER A 176
REMARK 465 GLY A 177
REMARK 465 LEU A 178
REMARK 465 TYR A 179
REMARK 465 SER A 180
REMARK 465 LEU A 181
REMARK 465 SER A 182
REMARK 465 SER A 183
REMARK 465 VAL A 184
REMARK 465 VAL A 185
REMARK 465 THR A 186
REMARK 465 VAL A 187
REMARK 465 PRO A 188
REMARK 465 SER A 189
REMARK 465 SER A 190
REMARK 465 SER A 191
REMARK 465 LEU A 192
REMARK 465 GLY A 193
REMARK 465 THR A 194
REMARK 465 GLN A 195
REMARK 465 THR A 196
REMARK 465 TYR A 197
REMARK 465 ILE A 198
REMARK 465 CYS A 199
REMARK 465 ASN A 200
REMARK 465 VAL A 201
REMARK 465 ASN A 202
REMARK 465 HIS A 203
REMARK 465 LYS A 204
REMARK 465 PRO A 205
REMARK 465 SER A 206
REMARK 465 ASN A 207
REMARK 465 THR A 208
REMARK 465 LYS A 209
REMARK 465 VAL A 210
REMARK 465 ASP A 211
REMARK 465 LYS A 212
REMARK 465 LYS A 213
REMARK 465 VAL A 214
REMARK 465 GLU A 215
REMARK 465 PRO A 216
REMARK 465 LYS A 217
REMARK 465 SER A 218
REMARK 465 CYS A 219
REMARK 465 ALA A 220
REMARK 465 SER A 221
REMARK 465 LEU A 222
REMARK 465 VAL A 223
REMARK 465 PRO A 224
REMARK 465 ARG A 225
REMARK 465 ASP B 1
REMARK 465 PRO B 8
REMARK 465 ALA B 9
REMARK 465 THR B 10
REMARK 465 LEU B 11
REMARK 465 SER B 12
REMARK 465 VAL B 13
REMARK 465 THR B 14
REMARK 465 PRO B 15
REMARK 465 GLY B 16
REMARK 465 ASP B 17
REMARK 465 SER B 18
REMARK 465 GLN B 38
REMARK 465 LYS B 39
REMARK 465 SER B 40
REMARK 465 HIS B 41
REMARK 465 SER B 77
REMARK 465 VAL B 78
REMARK 465 GLU B 79
REMARK 465 THR B 80
REMARK 465 GLU B 81
REMARK 465 ASP B 82
REMARK 465 PHE B 83
REMARK 465 GLY B 101
REMARK 465 THR B 102
REMARK 465 LYS B 103
REMARK 465 LEU B 104
REMARK 465 ASP B 105
REMARK 465 LEU B 106
REMARK 465 LYS B 107
REMARK 465 ARG B 108
REMARK 465 ARG B 109
REMARK 465 THR B 110
REMARK 465 VAL B 111
REMARK 465 ALA B 112
REMARK 465 ALA B 113
REMARK 465 PRO B 114
REMARK 465 SER B 115
REMARK 465 VAL B 116
REMARK 465 PHE B 117
REMARK 465 ILE B 118
REMARK 465 PHE B 119
REMARK 465 PRO B 120
REMARK 465 PRO B 121
REMARK 465 SER B 122
REMARK 465 ASP B 123
REMARK 465 GLU B 124
REMARK 465 GLN B 125
REMARK 465 LEU B 126
REMARK 465 LYS B 127
REMARK 465 SER B 128
REMARK 465 GLY B 129
REMARK 465 THR B 130
REMARK 465 ALA B 131
REMARK 465 SER B 132
REMARK 465 VAL B 133
REMARK 465 VAL B 134
REMARK 465 CYS B 135
REMARK 465 LEU B 136
REMARK 465 LEU B 137
REMARK 465 ASN B 138
REMARK 465 ASN B 139
REMARK 465 PHE B 140
REMARK 465 TYR B 141
REMARK 465 PRO B 142
REMARK 465 ARG B 143
REMARK 465 GLU B 144
REMARK 465 ALA B 145
REMARK 465 LYS B 146
REMARK 465 VAL B 147
REMARK 465 GLN B 148
REMARK 465 TRP B 149
REMARK 465 LYS B 150
REMARK 465 VAL B 151
REMARK 465 ASP B 152
REMARK 465 ASN B 153
REMARK 465 ALA B 154
REMARK 465 LEU B 155
REMARK 465 GLN B 156
REMARK 465 SER B 157
REMARK 465 GLY B 158
REMARK 465 ASN B 159
REMARK 465 SER B 160
REMARK 465 GLN B 161
REMARK 465 GLU B 162
REMARK 465 SER B 163
REMARK 465 VAL B 164
REMARK 465 THR B 165
REMARK 465 GLU B 166
REMARK 465 GLN B 167
REMARK 465 ASP B 168
REMARK 465 SER B 169
REMARK 465 LYS B 170
REMARK 465 ASP B 171
REMARK 465 SER B 172
REMARK 465 THR B 173
REMARK 465 TYR B 174
REMARK 465 SER B 175
REMARK 465 LEU B 176
REMARK 465 SER B 177
REMARK 465 SER B 178
REMARK 465 THR B 179
REMARK 465 LEU B 180
REMARK 465 THR B 181
REMARK 465 LEU B 182
REMARK 465 SER B 183
REMARK 465 LYS B 184
REMARK 465 ALA B 185
REMARK 465 ASP B 186
REMARK 465 TYR B 187
REMARK 465 GLU B 188
REMARK 465 LYS B 189
REMARK 465 HIS B 190
REMARK 465 LYS B 191
REMARK 465 VAL B 192
REMARK 465 TYR B 193
REMARK 465 ALA B 194
REMARK 465 CYS B 195
REMARK 465 GLU B 196
REMARK 465 VAL B 197
REMARK 465 THR B 198
REMARK 465 HIS B 199
REMARK 465 GLN B 200
REMARK 465 GLY B 201
REMARK 465 LEU B 202
REMARK 465 SER B 203
REMARK 465 SER B 204
REMARK 465 PRO B 205
REMARK 465 VAL B 206
REMARK 465 THR B 207
REMARK 465 LYS B 208
REMARK 465 SER B 209
REMARK 465 PHE B 210
REMARK 465 ASN B 211
REMARK 465 ARG B 212
REMARK 465 GLY B 213
REMARK 465 GLU B 214
REMARK 465 MET C 428
REMARK 465 GLY C 429
REMARK 465 GLU C 430
REMARK 465 ALA C 599
REMARK 465 GLY C 603
REMARK 465 PRO C 645
REMARK 465 ALA C 646
REMARK 465 ALA C 647
REMARK 465 ALA C 648
REMARK 465 GLU C 649
REMARK 465 LEU C 650
REMARK 465 ALA C 651
REMARK 465 LEU C 652
REMARK 465 VAL C 653
REMARK 465 PRO C 654
REMARK 465 ARG C 655
REMARK 465 MET D 428
REMARK 465 GLY D 429
REMARK 465 GLU D 430
REMARK 465 PRO D 602
REMARK 465 GLY D 603
REMARK 465 PRO D 645
REMARK 465 ALA D 646
REMARK 465 ALA D 647
REMARK 465 ALA D 648
REMARK 465 GLU D 649
REMARK 465 LEU D 650
REMARK 465 ALA D 651
REMARK 465 LEU D 652
REMARK 465 VAL D 653
REMARK 465 PRO D 654
REMARK 465 ARG D 655
REMARK 465 GLY E 42
REMARK 465 LYS E 43
REMARK 465 SER E 118
REMARK 465 SER E 119
REMARK 465 ALA E 120
REMARK 465 SER E 121
REMARK 465 THR E 122
REMARK 465 LYS E 123
REMARK 465 GLY E 124
REMARK 465 PRO E 125
REMARK 465 SER E 126
REMARK 465 VAL E 127
REMARK 465 PHE E 128
REMARK 465 PRO E 129
REMARK 465 LEU E 130
REMARK 465 ALA E 131
REMARK 465 PRO E 132
REMARK 465 SER E 133
REMARK 465 SER E 134
REMARK 465 LYS E 135
REMARK 465 SER E 136
REMARK 465 THR E 137
REMARK 465 SER E 138
REMARK 465 GLY E 139
REMARK 465 GLY E 140
REMARK 465 THR E 141
REMARK 465 ALA E 142
REMARK 465 ALA E 143
REMARK 465 LEU E 144
REMARK 465 GLY E 145
REMARK 465 CYS E 146
REMARK 465 LEU E 147
REMARK 465 VAL E 148
REMARK 465 LYS E 149
REMARK 465 ASP E 150
REMARK 465 TYR E 151
REMARK 465 PHE E 152
REMARK 465 PRO E 153
REMARK 465 GLU E 154
REMARK 465 PRO E 155
REMARK 465 VAL E 156
REMARK 465 THR E 157
REMARK 465 VAL E 158
REMARK 465 SER E 159
REMARK 465 TRP E 160
REMARK 465 ASN E 161
REMARK 465 SER E 162
REMARK 465 GLY E 163
REMARK 465 ALA E 164
REMARK 465 LEU E 165
REMARK 465 THR E 166
REMARK 465 SER E 167
REMARK 465 GLY E 168
REMARK 465 VAL E 169
REMARK 465 HIS E 170
REMARK 465 THR E 171
REMARK 465 PHE E 172
REMARK 465 PRO E 173
REMARK 465 ALA E 174
REMARK 465 VAL E 175
REMARK 465 LEU E 176
REMARK 465 GLN E 177
REMARK 465 SER E 178
REMARK 465 SER E 179
REMARK 465 GLY E 180
REMARK 465 LEU E 181
REMARK 465 TYR E 182
REMARK 465 SER E 183
REMARK 465 LEU E 184
REMARK 465 SER E 185
REMARK 465 SER E 186
REMARK 465 VAL E 187
REMARK 465 VAL E 188
REMARK 465 THR E 189
REMARK 465 VAL E 190
REMARK 465 PRO E 191
REMARK 465 SER E 192
REMARK 465 SER E 193
REMARK 465 SER E 194
REMARK 465 LEU E 195
REMARK 465 GLY E 196
REMARK 465 THR E 197
REMARK 465 GLN E 198
REMARK 465 THR E 199
REMARK 465 TYR E 200
REMARK 465 ILE E 201
REMARK 465 CYS E 202
REMARK 465 ASN E 203
REMARK 465 VAL E 204
REMARK 465 ASN E 205
REMARK 465 HIS E 206
REMARK 465 LYS E 207
REMARK 465 PRO E 208
REMARK 465 SER E 209
REMARK 465 ASN E 210
REMARK 465 THR E 211
REMARK 465 LYS E 212
REMARK 465 VAL E 213
REMARK 465 ASP E 214
REMARK 465 LYS E 215
REMARK 465 LYS E 216
REMARK 465 VAL E 217
REMARK 465 GLU E 218
REMARK 465 PRO E 219
REMARK 465 LYS E 220
REMARK 465 SER E 221
REMARK 465 CYS E 222
REMARK 465 ALA E 223
REMARK 465 SER E 224
REMARK 465 LEU E 225
REMARK 465 VAL E 226
REMARK 465 PRO E 227
REMARK 465 ARG E 228
REMARK 465 PRO F 14
REMARK 465 GLY F 15
REMARK 465 GLU F 16
REMARK 465 ASP F 43
REMARK 465 ALA F 62
REMARK 465 GLY F 79
REMARK 465 ALA F 80
REMARK 465 GLN F 81
REMARK 465 THR F 107
REMARK 465 VAL F 108
REMARK 465 LEU F 109
REMARK 465 GLY F 110
REMARK 465 ARG F 111
REMARK 465 THR F 112
REMARK 465 VAL F 113
REMARK 465 ALA F 114
REMARK 465 ALA F 115
REMARK 465 PRO F 116
REMARK 465 SER F 117
REMARK 465 VAL F 118
REMARK 465 PHE F 119
REMARK 465 ILE F 120
REMARK 465 PHE F 121
REMARK 465 PRO F 122
REMARK 465 PRO F 123
REMARK 465 SER F 124
REMARK 465 ASP F 125
REMARK 465 GLU F 126
REMARK 465 GLN F 127
REMARK 465 LEU F 128
REMARK 465 LYS F 129
REMARK 465 SER F 130
REMARK 465 GLY F 131
REMARK 465 THR F 132
REMARK 465 ALA F 133
REMARK 465 SER F 134
REMARK 465 VAL F 135
REMARK 465 VAL F 136
REMARK 465 CYS F 137
REMARK 465 LEU F 138
REMARK 465 LEU F 139
REMARK 465 ASN F 140
REMARK 465 ASN F 141
REMARK 465 PHE F 142
REMARK 465 TYR F 143
REMARK 465 PRO F 144
REMARK 465 ARG F 145
REMARK 465 GLU F 146
REMARK 465 ALA F 147
REMARK 465 LYS F 148
REMARK 465 VAL F 149
REMARK 465 GLN F 150
REMARK 465 TRP F 151
REMARK 465 LYS F 152
REMARK 465 VAL F 153
REMARK 465 ASP F 154
REMARK 465 ASN F 155
REMARK 465 ALA F 156
REMARK 465 LEU F 157
REMARK 465 GLN F 158
REMARK 465 SER F 159
REMARK 465 GLY F 160
REMARK 465 ASN F 161
REMARK 465 SER F 162
REMARK 465 GLN F 163
REMARK 465 GLU F 164
REMARK 465 SER F 165
REMARK 465 VAL F 166
REMARK 465 THR F 167
REMARK 465 GLU F 168
REMARK 465 GLN F 169
REMARK 465 ASP F 170
REMARK 465 SER F 171
REMARK 465 LYS F 172
REMARK 465 ASP F 173
REMARK 465 SER F 174
REMARK 465 THR F 175
REMARK 465 TYR F 176
REMARK 465 SER F 177
REMARK 465 LEU F 178
REMARK 465 SER F 179
REMARK 465 SER F 180
REMARK 465 THR F 181
REMARK 465 LEU F 182
REMARK 465 THR F 183
REMARK 465 LEU F 184
REMARK 465 SER F 185
REMARK 465 LYS F 186
REMARK 465 ALA F 187
REMARK 465 ASP F 188
REMARK 465 TYR F 189
REMARK 465 GLU F 190
REMARK 465 LYS F 191
REMARK 465 HIS F 192
REMARK 465 LYS F 193
REMARK 465 VAL F 194
REMARK 465 TYR F 195
REMARK 465 ALA F 196
REMARK 465 CYS F 197
REMARK 465 GLU F 198
REMARK 465 VAL F 199
REMARK 465 THR F 200
REMARK 465 HIS F 201
REMARK 465 GLN F 202
REMARK 465 GLY F 203
REMARK 465 LEU F 204
REMARK 465 SER F 205
REMARK 465 SER F 206
REMARK 465 PRO F 207
REMARK 465 VAL F 208
REMARK 465 THR F 209
REMARK 465 LYS F 210
REMARK 465 SER F 211
REMARK 465 PHE F 212
REMARK 465 ASN F 213
REMARK 465 ARG F 214
REMARK 465 GLY F 215
REMARK 465 GLU F 216
REMARK 465 CYS F 217
REMARK 465 ALA G 120
REMARK 465 SER G 121
REMARK 465 THR G 122
REMARK 465 LYS G 123
REMARK 465 GLY G 124
REMARK 465 PRO G 125
REMARK 465 SER G 126
REMARK 465 VAL G 127
REMARK 465 PHE G 128
REMARK 465 PRO G 129
REMARK 465 LEU G 130
REMARK 465 ALA G 131
REMARK 465 PRO G 132
REMARK 465 SER G 133
REMARK 465 SER G 134
REMARK 465 LYS G 135
REMARK 465 SER G 136
REMARK 465 THR G 137
REMARK 465 SER G 138
REMARK 465 GLY G 139
REMARK 465 GLY G 140
REMARK 465 THR G 141
REMARK 465 ALA G 142
REMARK 465 ALA G 143
REMARK 465 LEU G 144
REMARK 465 GLY G 145
REMARK 465 CYS G 146
REMARK 465 LEU G 147
REMARK 465 VAL G 148
REMARK 465 LYS G 149
REMARK 465 ASP G 150
REMARK 465 TYR G 151
REMARK 465 PHE G 152
REMARK 465 PRO G 153
REMARK 465 GLU G 154
REMARK 465 PRO G 155
REMARK 465 VAL G 156
REMARK 465 THR G 157
REMARK 465 VAL G 158
REMARK 465 SER G 159
REMARK 465 TRP G 160
REMARK 465 ASN G 161
REMARK 465 SER G 162
REMARK 465 GLY G 163
REMARK 465 ALA G 164
REMARK 465 LEU G 165
REMARK 465 THR G 166
REMARK 465 SER G 167
REMARK 465 GLY G 168
REMARK 465 VAL G 169
REMARK 465 HIS G 170
REMARK 465 THR G 171
REMARK 465 PHE G 172
REMARK 465 PRO G 173
REMARK 465 ALA G 174
REMARK 465 VAL G 175
REMARK 465 LEU G 176
REMARK 465 GLN G 177
REMARK 465 SER G 178
REMARK 465 SER G 179
REMARK 465 GLY G 180
REMARK 465 LEU G 181
REMARK 465 TYR G 182
REMARK 465 SER G 183
REMARK 465 LEU G 184
REMARK 465 SER G 185
REMARK 465 SER G 186
REMARK 465 VAL G 187
REMARK 465 VAL G 188
REMARK 465 THR G 189
REMARK 465 VAL G 190
REMARK 465 PRO G 191
REMARK 465 SER G 192
REMARK 465 SER G 193
REMARK 465 SER G 194
REMARK 465 LEU G 195
REMARK 465 GLY G 196
REMARK 465 THR G 197
REMARK 465 GLN G 198
REMARK 465 THR G 199
REMARK 465 TYR G 200
REMARK 465 ILE G 201
REMARK 465 CYS G 202
REMARK 465 ASN G 203
REMARK 465 VAL G 204
REMARK 465 ASN G 205
REMARK 465 HIS G 206
REMARK 465 LYS G 207
REMARK 465 PRO G 208
REMARK 465 SER G 209
REMARK 465 ASN G 210
REMARK 465 THR G 211
REMARK 465 LYS G 212
REMARK 465 VAL G 213
REMARK 465 ASP G 214
REMARK 465 LYS G 215
REMARK 465 LYS G 216
REMARK 465 VAL G 217
REMARK 465 GLU G 218
REMARK 465 PRO G 219
REMARK 465 LYS G 220
REMARK 465 SER G 221
REMARK 465 CYS G 222
REMARK 465 ALA G 223
REMARK 465 SER G 224
REMARK 465 LEU G 225
REMARK 465 VAL G 226
REMARK 465 PRO G 227
REMARK 465 ARG G 228
REMARK 465 GLN H 1
REMARK 465 GLY H 15
REMARK 465 GLU H 16
REMARK 465 THR H 82
REMARK 465 ASP H 83
REMARK 465 LEU H 109
REMARK 465 GLY H 110
REMARK 465 ARG H 111
REMARK 465 THR H 112
REMARK 465 VAL H 113
REMARK 465 ALA H 114
REMARK 465 ALA H 115
REMARK 465 PRO H 116
REMARK 465 SER H 117
REMARK 465 VAL H 118
REMARK 465 PHE H 119
REMARK 465 ILE H 120
REMARK 465 PHE H 121
REMARK 465 PRO H 122
REMARK 465 PRO H 123
REMARK 465 SER H 124
REMARK 465 ASP H 125
REMARK 465 GLU H 126
REMARK 465 GLN H 127
REMARK 465 LEU H 128
REMARK 465 LYS H 129
REMARK 465 SER H 130
REMARK 465 GLY H 131
REMARK 465 THR H 132
REMARK 465 ALA H 133
REMARK 465 SER H 134
REMARK 465 VAL H 135
REMARK 465 VAL H 136
REMARK 465 CYS H 137
REMARK 465 LEU H 138
REMARK 465 LEU H 139
REMARK 465 ASN H 140
REMARK 465 ASN H 141
REMARK 465 PHE H 142
REMARK 465 TYR H 143
REMARK 465 PRO H 144
REMARK 465 ARG H 145
REMARK 465 GLU H 146
REMARK 465 ALA H 147
REMARK 465 LYS H 148
REMARK 465 VAL H 149
REMARK 465 GLN H 150
REMARK 465 TRP H 151
REMARK 465 LYS H 152
REMARK 465 VAL H 153
REMARK 465 ASP H 154
REMARK 465 ASN H 155
REMARK 465 ALA H 156
REMARK 465 LEU H 157
REMARK 465 GLN H 158
REMARK 465 SER H 159
REMARK 465 GLY H 160
REMARK 465 ASN H 161
REMARK 465 SER H 162
REMARK 465 GLN H 163
REMARK 465 GLU H 164
REMARK 465 SER H 165
REMARK 465 VAL H 166
REMARK 465 THR H 167
REMARK 465 GLU H 168
REMARK 465 GLN H 169
REMARK 465 ASP H 170
REMARK 465 SER H 171
REMARK 465 LYS H 172
REMARK 465 ASP H 173
REMARK 465 SER H 174
REMARK 465 THR H 175
REMARK 465 TYR H 176
REMARK 465 SER H 177
REMARK 465 LEU H 178
REMARK 465 SER H 179
REMARK 465 SER H 180
REMARK 465 THR H 181
REMARK 465 LEU H 182
REMARK 465 THR H 183
REMARK 465 LEU H 184
REMARK 465 SER H 185
REMARK 465 LYS H 186
REMARK 465 ALA H 187
REMARK 465 ASP H 188
REMARK 465 TYR H 189
REMARK 465 GLU H 190
REMARK 465 LYS H 191
REMARK 465 HIS H 192
REMARK 465 LYS H 193
REMARK 465 VAL H 194
REMARK 465 TYR H 195
REMARK 465 ALA H 196
REMARK 465 CYS H 197
REMARK 465 GLU H 198
REMARK 465 VAL H 199
REMARK 465 THR H 200
REMARK 465 HIS H 201
REMARK 465 GLN H 202
REMARK 465 GLY H 203
REMARK 465 LEU H 204
REMARK 465 SER H 205
REMARK 465 SER H 206
REMARK 465 PRO H 207
REMARK 465 VAL H 208
REMARK 465 THR H 209
REMARK 465 LYS H 210
REMARK 465 SER H 211
REMARK 465 PHE H 212
REMARK 465 ASN H 213
REMARK 465 ARG H 214
REMARK 465 GLY H 215
REMARK 465 GLU H 216
REMARK 465 CYS H 217
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 VAL A 2 CG1 CG2
REMARK 470 HIS A 5 CG ND1 CD2 CE1 NE2
REMARK 470 GLN A 6 CG CD OE1 NE2
REMARK 470 SER A 25 OG
REMARK 470 ARG A 40 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 46 CG CD OE1 OE2
REMARK 470 ASN A 52 CG OD1 ND2
REMARK 470 SER A 55 OG
REMARK 470 ARG A 57 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 66 CG OD1 ND2
REMARK 470 THR A 71 OG1 CG2
REMARK 470 LYS A 74 CG CD CE NZ
REMARK 470 SER A 75 OG
REMARK 470 SER A 85 OG
REMARK 470 LEU A 86 CG CD1 CD2
REMARK 470 THR A 87 OG1 CG2
REMARK 470 SER A 91 OG
REMARK 470 ASP A 104 CG OD1 OD2
REMARK 470 GLN A 108 CG CD OE1 NE2
REMARK 470 VAL B 3 CG1 CG2
REMARK 470 THR B 5 OG1 CG2
REMARK 470 SER B 7 OG
REMARK 470 VAL B 19 CG1 CG2
REMARK 470 SER B 20 OG
REMARK 470 SER B 22 OG
REMARK 470 ARG B 24 CG CD NE CZ NH1 NH2
REMARK 470 SER B 26 OG
REMARK 470 SER B 28 OG
REMARK 470 GLN B 37 CG CD OE1 NE2
REMARK 470 GLU B 42 CG CD OE1 OE2
REMARK 470 ARG B 45 CG CD NE CZ NH1 NH2
REMARK 470 SER B 52 OG
REMARK 470 SER B 54 OG
REMARK 470 ASP B 70 CG OD1 OD2
REMARK 470 SER B 74 OG
REMARK 470 GLN B 89 CG CD OE1 NE2
REMARK 470 THR B 97 OG1 CG2
REMARK 470 THR B 100 OG1 CG2
REMARK 470 SER C 440 OG
REMARK 470 ASP C 458 CG OD1 OD2
REMARK 470 SER C 461 OG
REMARK 470 HIS C 463 CG ND1 CD2 CE1 NE2
REMARK 470 ASN C 465 CG OD1 ND2
REMARK 470 ASP C 471 CG OD1 OD2
REMARK 470 VAL C 472 CG1 CG2
REMARK 470 ASP C 473 CG OD1 OD2
REMARK 470 GLN C 495 CG CD OE1 NE2
REMARK 470 GLU C 498 CG CD OE1 OE2
REMARK 470 ASP C 517 CG OD1 OD2
REMARK 470 ASN C 530 CG OD1 ND2
REMARK 470 ASN C 531 CG OD1 ND2
REMARK 470 GLN C 548 CG CD OE1 NE2
REMARK 470 ASP C 564 CG OD1 OD2
REMARK 470 ASP C 597 CG OD1 OD2
REMARK 470 GLU C 632 CG CD OE1 OE2
REMARK 470 SER D 443 OG
REMARK 470 SER D 461 OG
REMARK 470 ASP D 473 CG OD1 OD2
REMARK 470 SER D 486 OG
REMARK 470 GLN D 495 CG CD OE1 NE2
REMARK 470 ILE D 512 CG1 CG2 CD1
REMARK 470 ASN D 530 CG OD1 ND2
REMARK 470 ASN D 531 CG OD1 ND2
REMARK 470 ASP D 564 CG OD1 OD2
REMARK 470 ASP D 574 CG OD1 OD2
REMARK 470 SER D 581 OG
REMARK 470 GLN E 1 CG CD OE1 NE2
REMARK 470 GLN E 3 CG CD OE1 NE2
REMARK 470 SER E 7 OG
REMARK 470 LEU E 11 CG CD1 CD2
REMARK 470 SER E 15 OG
REMARK 470 SER E 25 OG
REMARK 470 SER E 61 OG
REMARK 470 ASP E 72 CG OD1 OD2
REMARK 470 ARG E 75 CG CD NE CZ NH1 NH2
REMARK 470 GLN E 86 CG CD OE1 NE2
REMARK 470 GLU F 7 CG CD OE1 OE2
REMARK 470 SER F 8 OG
REMARK 470 THR F 11 OG1 CG2
REMARK 470 ARG F 23 CG CD NE CZ NH1 NH2
REMARK 470 GLU F 40 CG CD OE1 OE2
REMARK 470 LEU F 45 CG CD1 CD2
REMARK 470 SER F 65 OG
REMARK 470 ASP F 71 CG OD1 OD2
REMARK 470 THR F 82 OG1 CG2
REMARK 470 ASP F 83 CG OD1 OD2
REMARK 470 ASP F 84 CG OD1 OD2
REMARK 470 GLU F 85 CG CD OE1 OE2
REMARK 470 LYS F 105 CG CD CE NZ
REMARK 470 GLN G 1 CG CD OE1 NE2
REMARK 470 GLN G 3 CG CD OE1 NE2
REMARK 470 LYS G 5 CG CD CE NZ
REMARK 470 LEU G 11 CG CD1 CD2
REMARK 470 SER G 15 OG
REMARK 470 GLN G 16 CG CD OE1 NE2
REMARK 470 SER G 17 OG
REMARK 470 SER G 28 OG
REMARK 470 GLU G 46 CG CD OE1 OE2
REMARK 470 THR G 62 OG1 CG2
REMARK 470 LYS G 64 CG CD CE NZ
REMARK 470 SER G 65 OG
REMARK 470 ASP G 72 CG OD1 OD2
REMARK 470 ARG G 75 CG CD NE CZ NH1 NH2
REMARK 470 ASN G 83 CG OD1 ND2
REMARK 470 SER G 84 OG
REMARK 470 GLN G 86 CG CD OE1 NE2
REMARK 470 GLN G 111 CG CD OE1 NE2
REMARK 470 GLN H 6 CG CD OE1 NE2
REMARK 470 GLU H 7 CG CD OE1 OE2
REMARK 470 THR H 21 OG1 CG2
REMARK 470 ARG H 23 CG CD NE CZ NH1 NH2
REMARK 470 ASP H 43 CG OD1 OD2
REMARK 470 ASN H 54 CG OD1 ND2
REMARK 470 ARG H 63 CG CD NE CZ NH1 NH2
REMARK 470 SER H 65 OG
REMARK 470 SER H 67 OG
REMARK 470 LEU H 68 CG CD1 CD2
REMARK 470 ILE H 69 CG1 CG2 CD1
REMARK 470 ASP H 71 CG OD1 OD2
REMARK 470 LYS H 72 CG CD CE NZ
REMARK 470 THR H 78 OG1 CG2
REMARK 470 GLN H 81 CG CD OE1 NE2
REMARK 470 ASP H 84 CG OD1 OD2
REMARK 470 GLU H 85 CG CD OE1 OE2
REMARK 470 SER H 95 OG
REMARK 470 THR H 104 OG1 CG2
REMARK 470 LYS H 105 CG CD CE NZ
REMARK 470 THR H 107 OG1 CG2
REMARK 470 VAL H 108 CG1 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 HD22 ASN D 445 HE1 PHE D 481 1.19
REMARK 500 HE1 TRP D 604 CD1 TRP D 606 1.28
REMARK 500 HE1 TRP D 604 NE1 TRP D 606 1.30
REMARK 500 HD22 ASN D 445 CE1 PHE D 481 1.50
REMARK 500 SG CYS B 23 SG CYS B 88 1.79
REMARK 500 OH TYR A 60 N LEU A 70 1.88
REMARK 500 NE1 TRP D 604 NE1 TRP D 606 1.99
REMARK 500 O SER F 65 OG1 THR F 76 2.04
REMARK 500 NE1 TRP D 604 CD1 TRP D 606 2.06
REMARK 500 CD PRO E 40 OE1 GLU E 46 2.07
REMARK 500 OG1 THR H 17 O ILE H 77 2.10
REMARK 500 O LEU G 29 NZ LYS G 71 2.11
REMARK 500 CA THR B 91 CD2 LEU B 96 2.13
REMARK 500 NE2 HIS G 35 OE2 GLU G 98 2.14
REMARK 500 O GLY F 51 ND2 ASN F 55 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLY E 10 C LEU E 11 N 0.239
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 TYR A 94 N - CA - CB ANGL. DEV. = -19.2 DEGREES
REMARK 500 TYR A 94 N - CA - C ANGL. DEV. = 49.9 DEGREES
REMARK 500 TYR A 95 CB - CA - C ANGL. DEV. = -14.0 DEGREES
REMARK 500 TYR A 95 N - CA - CB ANGL. DEV. = -19.1 DEGREES
REMARK 500 MET A 103 CB - CA - C ANGL. DEV. = -15.8 DEGREES
REMARK 500 MET A 103 N - CA - CB ANGL. DEV. = 13.5 DEGREES
REMARK 500 MET A 103 N - CA - C ANGL. DEV. = 27.3 DEGREES
REMARK 500 ASP A 104 CB - CA - C ANGL. DEV. = 15.1 DEGREES
REMARK 500 ASP A 104 N - CA - CB ANGL. DEV. = -12.5 DEGREES
REMARK 500 TYR A 105 N - CA - CB ANGL. DEV. = -22.9 DEGREES
REMARK 500 TYR A 105 N - CA - C ANGL. DEV. = 18.5 DEGREES
REMARK 500 VAL C 510 N - CA - C ANGL. DEV. = -17.9 DEGREES
REMARK 500 ALA E 54 CB - CA - C ANGL. DEV. = -15.4 DEGREES
REMARK 500 PHE F 94 CB - CA - C ANGL. DEV. = 33.7 DEGREES
REMARK 500 PHE F 94 N - CA - C ANGL. DEV. = -28.8 DEGREES
REMARK 500 SER F 95 CB - CA - C ANGL. DEV. = 24.8 DEGREES
REMARK 500 SER F 95 N - CA - CB ANGL. DEV. = -29.1 DEGREES
REMARK 500 ASN F 96 N - CA - CB ANGL. DEV. = -20.1 DEGREES
REMARK 500 TYR G 59 CB - CA - C ANGL. DEV. = 12.8 DEGREES
REMARK 500 ASN G 60 CB - CA - C ANGL. DEV. = -31.6 DEGREES
REMARK 500 ASN G 60 N - CA - C ANGL. DEV. = -26.1 DEGREES
REMARK 500 SER G 61 N - CA - CB ANGL. DEV. = -17.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 TYR A 32 25.10 -140.86
REMARK 500 SER A 55 -14.12 75.04
REMARK 500 ASN A 66 -5.28 73.84
REMARK 500 ALA A 102 155.38 177.30
REMARK 500 MET A 103 24.67 45.44
REMARK 500 SER B 30 -126.35 56.47
REMARK 500 ALA B 51 -5.81 74.85
REMARK 500 THR B 69 -15.90 -141.36
REMARK 500 MET B 85 -121.50 41.81
REMARK 500 ASN C 511 -145.51 57.46
REMARK 500 ALA C 559 -169.95 -78.48
REMARK 500 TRP C 606 35.11 -99.84
REMARK 500 ASN C 614 30.02 70.60
REMARK 500 MET C 628 135.30 -170.80
REMARK 500 SER C 633 9.83 80.05
REMARK 500 ASN D 448 31.50 -98.51
REMARK 500 TYR D 475 142.09 -170.41
REMARK 500 THR D 491 -177.54 -68.47
REMARK 500 ASN D 511 -123.04 62.68
REMARK 500 ALA E 91 -178.73 -178.04
REMARK 500 TYR E 100 24.07 47.16
REMARK 500 ALA F 2 -169.09 -118.93
REMARK 500 THR F 53 -10.63 82.54
REMARK 500 PRO G 40 173.02 -58.55
REMARK 500 PHE G 104 -1.87 73.80
REMARK 500 THR H 53 -8.58 75.90
REMARK 500 ASN H 54 -32.00 -131.80
REMARK 500 SER H 67 -175.25 -171.01
REMARK 500 SER H 95 -12.56 72.55
REMARK 500 LYS H 105 60.31 65.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NAG I 1
REMARK 610 NAG J 2
REMARK 610 BMA J 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-45427 RELATED DB: EMDB
REMARK 900 HASTV1 SPIKE IN COMPLEX WITH NEUTRALIZING FABS 3H4 AND 3B4
DBREF 9CBN A 1 225 PDB 9CBN 9CBN 1 225
DBREF 9CBN B 1 214 PDB 9CBN 9CBN 1 214
DBREF 9CBN C 429 645 UNP Q82452 Q82452_HASV1 429 645
DBREF 9CBN D 429 645 UNP Q82452 Q82452_HASV1 429 645
DBREF 9CBN E 1 228 PDB 9CBN 9CBN 1 228
DBREF 9CBN F 1 217 PDB 9CBN 9CBN 1 217
DBREF 9CBN G 1 228 PDB 9CBN 9CBN 1 228
DBREF 9CBN H 1 217 PDB 9CBN 9CBN 1 217
SEQADV 9CBN MET C 428 UNP Q82452 INITIATING METHIONINE
SEQADV 9CBN ALA C 646 UNP Q82452 EXPRESSION TAG
SEQADV 9CBN ALA C 647 UNP Q82452 EXPRESSION TAG
SEQADV 9CBN ALA C 648 UNP Q82452 EXPRESSION TAG
SEQADV 9CBN GLU C 649 UNP Q82452 EXPRESSION TAG
SEQADV 9CBN LEU C 650 UNP Q82452 EXPRESSION TAG
SEQADV 9CBN ALA C 651 UNP Q82452 EXPRESSION TAG
SEQADV 9CBN LEU C 652 UNP Q82452 EXPRESSION TAG
SEQADV 9CBN VAL C 653 UNP Q82452 EXPRESSION TAG
SEQADV 9CBN PRO C 654 UNP Q82452 EXPRESSION TAG
SEQADV 9CBN ARG C 655 UNP Q82452 EXPRESSION TAG
SEQADV 9CBN MET D 428 UNP Q82452 INITIATING METHIONINE
SEQADV 9CBN ALA D 646 UNP Q82452 EXPRESSION TAG
SEQADV 9CBN ALA D 647 UNP Q82452 EXPRESSION TAG
SEQADV 9CBN ALA D 648 UNP Q82452 EXPRESSION TAG
SEQADV 9CBN GLU D 649 UNP Q82452 EXPRESSION TAG
SEQADV 9CBN LEU D 650 UNP Q82452 EXPRESSION TAG
SEQADV 9CBN ALA D 651 UNP Q82452 EXPRESSION TAG
SEQADV 9CBN LEU D 652 UNP Q82452 EXPRESSION TAG
SEQADV 9CBN VAL D 653 UNP Q82452 EXPRESSION TAG
SEQADV 9CBN PRO D 654 UNP Q82452 EXPRESSION TAG
SEQADV 9CBN ARG D 655 UNP Q82452 EXPRESSION TAG
SEQRES 1 A 225 GLN VAL GLN LEU HIS GLN PRO GLY ALA GLU LEU VAL LYS
SEQRES 2 A 225 PRO GLY ALA SER VAL ASN LEU SER CYS LYS ALA SER GLY
SEQRES 3 A 225 TYR THR PHE THR SER TYR TRP MET HIS TRP VAL LYS GLN
SEQRES 4 A 225 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY GLU ILE ASN
SEQRES 5 A 225 PRO SER SER GLY ARG ALA ASN TYR ASN GLU LYS PHE LYS
SEQRES 6 A 225 ASN LYS ALA THR LEU THR VAL ASP LYS SER SER ILE THR
SEQRES 7 A 225 ALA TYR MET HIS LEU SER SER LEU THR SER GLU ASP SER
SEQRES 8 A 225 ALA VAL TYR TYR CYS HIS TRP ASP TYR TYR ALA MET ASP
SEQRES 9 A 225 TYR TRP GLY GLN GLY THR SER VAL THR VAL SER SER ALA
SEQRES 10 A 225 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER
SEQRES 11 A 225 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS
SEQRES 12 A 225 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER
SEQRES 13 A 225 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE
SEQRES 14 A 225 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER
SEQRES 15 A 225 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN
SEQRES 16 A 225 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR
SEQRES 17 A 225 LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ALA SER
SEQRES 18 A 225 LEU VAL PRO ARG
SEQRES 1 B 214 ASP ILE VAL LEU THR GLN SER PRO ALA THR LEU SER VAL
SEQRES 2 B 214 THR PRO GLY ASP SER VAL SER LEU SER CYS ARG ALA SER
SEQRES 3 B 214 GLN SER ILE SER ASN ASN LEU HIS TRP TYR GLN GLN LYS
SEQRES 4 B 214 SER HIS GLU SER PRO ARG LEU LEU PHE LYS SER ALA SER
SEQRES 5 B 214 GLN SER ILE SER GLY ILE PRO SER ARG PHE SER GLY SER
SEQRES 6 B 214 GLY SER GLY THR ASP PHE THR LEU SER ILE ASN SER VAL
SEQRES 7 B 214 GLU THR GLU ASP PHE GLY MET TYR PHE CYS GLN GLN THR
SEQRES 8 B 214 ASN SER TRP PRO LEU THR PHE GLY THR GLY THR LYS LEU
SEQRES 9 B 214 ASP LEU LYS ARG ARG THR VAL ALA ALA PRO SER VAL PHE
SEQRES 10 B 214 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR
SEQRES 11 B 214 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG
SEQRES 12 B 214 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN
SEQRES 13 B 214 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER
SEQRES 14 B 214 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU
SEQRES 15 B 214 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS
SEQRES 16 B 214 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS
SEQRES 17 B 214 SER PHE ASN ARG GLY GLU
SEQRES 1 C 228 MET GLY GLU GLU TYR LYS VAL VAL LEU THR PHE GLY SER
SEQRES 2 C 228 PRO MET SER PRO ASN ALA ASN ASN LYS GLN THR TRP VAL
SEQRES 3 C 228 ASN LYS PRO LEU ASP ALA PRO SER GLY HIS TYR ASN VAL
SEQRES 4 C 228 LYS ILE ALA LYS ASP VAL ASP HIS TYR LEU THR MET GLN
SEQRES 5 C 228 GLY PHE THR SER ILE ALA SER VAL ASP TRP TYR THR ILE
SEQRES 6 C 228 ASP PHE GLN PRO SER GLU ALA PRO ALA PRO ILE LYS GLY
SEQRES 7 C 228 LEU GLN VAL LEU VAL ASN ILE SER LYS LYS ALA ASP VAL
SEQRES 8 C 228 TYR ALA VAL LYS GLN PHE VAL THR ALA GLN THR ASN ASN
SEQRES 9 C 228 LYS HIS GLN VAL THR SER LEU PHE LEU VAL LYS VAL THR
SEQRES 10 C 228 THR GLY PHE GLN VAL ASN ASN TYR LEU SER TYR PHE TYR
SEQRES 11 C 228 ARG ALA SER ALA THR GLY ASP ALA THR THR ASN LEU LEU
SEQRES 12 C 228 VAL ARG GLY ASP THR TYR THR ALA GLY ILE SER PHE THR
SEQRES 13 C 228 GLN GLY GLY TRP TYR LEU LEU THR ASN THR SER ILE VAL
SEQRES 14 C 228 ASP GLY ALA MET PRO PRO GLY TRP VAL TRP ASN ASN VAL
SEQRES 15 C 228 GLU LEU LYS THR ASN THR ALA TYR HIS MET ASP LYS GLY
SEQRES 16 C 228 LEU VAL HIS LEU ILE MET PRO LEU PRO GLU SER THR GLN
SEQRES 17 C 228 MET CYS TYR GLU MET LEU THR SER ILE PRO ALA ALA ALA
SEQRES 18 C 228 GLU LEU ALA LEU VAL PRO ARG
SEQRES 1 D 228 MET GLY GLU GLU TYR LYS VAL VAL LEU THR PHE GLY SER
SEQRES 2 D 228 PRO MET SER PRO ASN ALA ASN ASN LYS GLN THR TRP VAL
SEQRES 3 D 228 ASN LYS PRO LEU ASP ALA PRO SER GLY HIS TYR ASN VAL
SEQRES 4 D 228 LYS ILE ALA LYS ASP VAL ASP HIS TYR LEU THR MET GLN
SEQRES 5 D 228 GLY PHE THR SER ILE ALA SER VAL ASP TRP TYR THR ILE
SEQRES 6 D 228 ASP PHE GLN PRO SER GLU ALA PRO ALA PRO ILE LYS GLY
SEQRES 7 D 228 LEU GLN VAL LEU VAL ASN ILE SER LYS LYS ALA ASP VAL
SEQRES 8 D 228 TYR ALA VAL LYS GLN PHE VAL THR ALA GLN THR ASN ASN
SEQRES 9 D 228 LYS HIS GLN VAL THR SER LEU PHE LEU VAL LYS VAL THR
SEQRES 10 D 228 THR GLY PHE GLN VAL ASN ASN TYR LEU SER TYR PHE TYR
SEQRES 11 D 228 ARG ALA SER ALA THR GLY ASP ALA THR THR ASN LEU LEU
SEQRES 12 D 228 VAL ARG GLY ASP THR TYR THR ALA GLY ILE SER PHE THR
SEQRES 13 D 228 GLN GLY GLY TRP TYR LEU LEU THR ASN THR SER ILE VAL
SEQRES 14 D 228 ASP GLY ALA MET PRO PRO GLY TRP VAL TRP ASN ASN VAL
SEQRES 15 D 228 GLU LEU LYS THR ASN THR ALA TYR HIS MET ASP LYS GLY
SEQRES 16 D 228 LEU VAL HIS LEU ILE MET PRO LEU PRO GLU SER THR GLN
SEQRES 17 D 228 MET CYS TYR GLU MET LEU THR SER ILE PRO ALA ALA ALA
SEQRES 18 D 228 GLU LEU ALA LEU VAL PRO ARG
SEQRES 1 E 228 GLN VAL GLN LEU LYS GLU SER GLY PRO GLY LEU VAL ALA
SEQRES 2 E 228 PRO SER GLN SER LEU SER ILE SER CYS THR VAL SER GLY
SEQRES 3 E 228 PHE SER LEU THR THR PHE GLY ILE HIS TRP ILE ARG GLN
SEQRES 4 E 228 PRO PRO GLY LYS GLY LEU GLU TRP LEU GLY VAL ILE TRP
SEQRES 5 E 228 ALA ALA GLY THR THR ASN TYR ASN SER THR LEU LYS SER
SEQRES 6 E 228 ARG LEU THR ILE THR LYS ASP ASN SER ARG SER GLN VAL
SEQRES 7 E 228 PHE LEU LYS MET ASN SER LEU GLN THR TYR ASP THR ALA
SEQRES 8 E 228 ILE TYR TYR CYS VAL ARG GLU ASP TYR ASP TYR PHE PHE
SEQRES 9 E 228 GLY LEU ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL
SEQRES 10 E 228 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU
SEQRES 11 E 228 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA
SEQRES 12 E 228 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL
SEQRES 13 E 228 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL
SEQRES 14 E 228 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR
SEQRES 15 E 228 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU
SEQRES 16 E 228 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO
SEQRES 17 E 228 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER
SEQRES 18 E 228 CYS ALA SER LEU VAL PRO ARG
SEQRES 1 F 217 GLN ALA VAL VAL THR GLN GLU SER ALA LEU THR THR SER
SEQRES 2 F 217 PRO GLY GLU THR VAL THR LEU THR CYS ARG SER SER THR
SEQRES 3 F 217 GLY ALA VAL THR THR SER ASN TYR ALA SER TRP VAL GLN
SEQRES 4 F 217 GLU LYS PRO ASP HIS LEU PHE ILE GLY LEU ILE GLY GLY
SEQRES 5 F 217 THR ASN ASN ARG ALA PRO GLY VAL PRO ALA ARG PHE SER
SEQRES 6 F 217 GLY SER LEU ILE GLY ASP LYS ALA ALA LEU THR ILE THR
SEQRES 7 F 217 GLY ALA GLN THR ASP ASP GLU ALA ILE TYR PHE CYS ALA
SEQRES 8 F 217 LEU TRP PHE SER ASN HIS TRP VAL PHE GLY GLY GLY THR
SEQRES 9 F 217 LYS LEU THR VAL LEU GLY ARG THR VAL ALA ALA PRO SER
SEQRES 10 F 217 VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER
SEQRES 11 F 217 GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR
SEQRES 12 F 217 PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA
SEQRES 13 F 217 LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN
SEQRES 14 F 217 ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU
SEQRES 15 F 217 THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR
SEQRES 16 F 217 ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL
SEQRES 17 F 217 THR LYS SER PHE ASN ARG GLY GLU CYS
SEQRES 1 G 228 GLN VAL GLN LEU LYS GLU SER GLY PRO GLY LEU VAL ALA
SEQRES 2 G 228 PRO SER GLN SER LEU SER ILE SER CYS THR VAL SER GLY
SEQRES 3 G 228 PHE SER LEU THR THR PHE GLY ILE HIS TRP ILE ARG GLN
SEQRES 4 G 228 PRO PRO GLY LYS GLY LEU GLU TRP LEU GLY VAL ILE TRP
SEQRES 5 G 228 ALA ALA GLY THR THR ASN TYR ASN SER THR LEU LYS SER
SEQRES 6 G 228 ARG LEU THR ILE THR LYS ASP ASN SER ARG SER GLN VAL
SEQRES 7 G 228 PHE LEU LYS MET ASN SER LEU GLN THR TYR ASP THR ALA
SEQRES 8 G 228 ILE TYR TYR CYS VAL ARG GLU ASP TYR ASP TYR PHE PHE
SEQRES 9 G 228 GLY LEU ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL
SEQRES 10 G 228 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU
SEQRES 11 G 228 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA
SEQRES 12 G 228 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL
SEQRES 13 G 228 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL
SEQRES 14 G 228 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR
SEQRES 15 G 228 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU
SEQRES 16 G 228 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO
SEQRES 17 G 228 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER
SEQRES 18 G 228 CYS ALA SER LEU VAL PRO ARG
SEQRES 1 H 217 GLN ALA VAL VAL THR GLN GLU SER ALA LEU THR THR SER
SEQRES 2 H 217 PRO GLY GLU THR VAL THR LEU THR CYS ARG SER SER THR
SEQRES 3 H 217 GLY ALA VAL THR THR SER ASN TYR ALA SER TRP VAL GLN
SEQRES 4 H 217 GLU LYS PRO ASP HIS LEU PHE ILE GLY LEU ILE GLY GLY
SEQRES 5 H 217 THR ASN ASN ARG ALA PRO GLY VAL PRO ALA ARG PHE SER
SEQRES 6 H 217 GLY SER LEU ILE GLY ASP LYS ALA ALA LEU THR ILE THR
SEQRES 7 H 217 GLY ALA GLN THR ASP ASP GLU ALA ILE TYR PHE CYS ALA
SEQRES 8 H 217 LEU TRP PHE SER ASN HIS TRP VAL PHE GLY GLY GLY THR
SEQRES 9 H 217 LYS LEU THR VAL LEU GLY ARG THR VAL ALA ALA PRO SER
SEQRES 10 H 217 VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER
SEQRES 11 H 217 GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR
SEQRES 12 H 217 PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA
SEQRES 13 H 217 LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN
SEQRES 14 H 217 ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU
SEQRES 15 H 217 THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR
SEQRES 16 H 217 ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL
SEQRES 17 H 217 THR LYS SER PHE ASN ARG GLY GLU CYS
HET NAG I 1 14
HET NAG I 2 14
HET BMA I 3 11
HET NAG J 1 14
HET NAG J 2 13
HET BMA J 3 6
HET NAG A 301 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 9 NAG 5(C8 H15 N O6)
FORMUL 9 BMA 2(C6 H12 O6)
HELIX 1 AA1 ASN A 61 LYS A 65 5 5
HELIX 2 AA2 LEU C 623 ILE C 627 5 5
HELIX 3 AA3 ASP D 620 VAL D 624 5 5
HELIX 4 AA4 SER E 61 LYS E 64 5 4
HELIX 5 AA5 THR F 30 TYR F 34 5 5
HELIX 6 AA6 GLN G 86 THR G 90 5 5
HELIX 7 AA7 THR H 30 TYR H 34 5 5
SHEET 1 AA1 3 GLN A 3 HIS A 5 0
SHEET 2 AA1 3 VAL A 18 SER A 25 -1 O LYS A 23 N HIS A 5
SHEET 3 AA1 3 ALA A 79 LEU A 83 -1 O ALA A 79 N CYS A 22
SHEET 1 AA2 2 VAL A 37 LYS A 38 0
SHEET 2 AA2 2 GLU A 46 TRP A 47 -1 O GLU A 46 N LYS A 38
SHEET 1 AA3 4 THR B 5 SER B 7 0
SHEET 2 AA3 4 SER B 20 ARG B 24 -1 O ARG B 24 N THR B 5
SHEET 3 AA3 4 ASP B 70 ILE B 75 -1 O LEU B 73 N LEU B 21
SHEET 4 AA3 4 PHE B 62 SER B 65 -1 N SER B 63 O SER B 74
SHEET 1 AA4 4 GLN B 53 SER B 54 0
SHEET 2 AA4 4 ARG B 45 LYS B 49 -1 N LYS B 49 O GLN B 53
SHEET 3 AA4 4 LEU B 33 GLN B 37 -1 N GLN B 37 O ARG B 45
SHEET 4 AA4 4 PHE B 87 GLN B 90 -1 O PHE B 87 N TYR B 36
SHEET 1 AA5 7 GLN C 507 LEU C 509 0
SHEET 2 AA5 7 LYS C 514 THR C 529 -1 O ALA C 516 N VAL C 508
SHEET 3 AA5 7 LYS C 532 VAL C 543 -1 O GLN C 534 N THR C 526
SHEET 4 AA5 7 TRP C 587 ASP C 597 -1 O SER C 594 N VAL C 535
SHEET 5 AA5 7 SER C 483 TYR C 490 -1 N ILE C 484 O TRP C 587
SHEET 6 AA5 7 TYR C 432 PHE C 438 -1 N VAL C 435 O ASP C 488
SHEET 7 AA5 7 GLN C 635 MET C 640 -1 O TYR C 638 N VAL C 434
SHEET 1 AA6 3 VAL C 453 ASN C 454 0
SHEET 2 AA6 3 PHE C 547 SER C 554 -1 O SER C 554 N VAL C 453
SHEET 3 AA6 3 TYR C 576 PHE C 582 -1 O ILE C 580 N VAL C 549
SHEET 1 AA7 2 LYS C 467 ASP C 471 0
SHEET 2 AA7 2 HIS C 474 THR C 477 -1 O HIS C 474 N LYS C 470
SHEET 1 AA8 2 PHE C 556 TYR C 557 0
SHEET 2 AA8 2 LEU C 570 VAL C 571 -1 O LEU C 570 N TYR C 557
SHEET 1 AA9 6 TYR D 475 THR D 477 0
SHEET 2 AA9 6 VAL D 466 ALA D 469 -1 N ILE D 468 O LEU D 476
SHEET 3 AA9 6 GLN D 507 VAL D 510 -1 O LEU D 509 N LYS D 467
SHEET 4 AA9 6 SER D 513 ALA D 527 -1 O SER D 513 N VAL D 510
SHEET 5 AA9 6 LYS D 532 VAL D 543 -1 O GLN D 534 N THR D 526
SHEET 6 AA9 6 ASN D 592 ASP D 597 -1 O ASN D 592 N SER D 537
SHEET 1 AB1 9 TYR D 475 THR D 477 0
SHEET 2 AB1 9 VAL D 466 ALA D 469 -1 N ILE D 468 O LEU D 476
SHEET 3 AB1 9 GLN D 507 VAL D 510 -1 O LEU D 509 N LYS D 467
SHEET 4 AB1 9 SER D 513 ALA D 527 -1 O SER D 513 N VAL D 510
SHEET 5 AB1 9 LYS D 532 VAL D 543 -1 O GLN D 534 N THR D 526
SHEET 6 AB1 9 TRP D 587 LEU D 589 -1 O TYR D 588 N VAL D 541
SHEET 7 AB1 9 THR D 482 TYR D 490 -1 N ILE D 484 O TRP D 587
SHEET 8 AB1 9 LYS D 433 PHE D 438 -1 N THR D 437 O ALA D 485
SHEET 9 AB1 9 THR D 634 CYS D 637 -1 O THR D 634 N PHE D 438
SHEET 1 AB2 3 VAL D 453 ASN D 454 0
SHEET 2 AB2 3 GLN D 548 SER D 554 -1 O SER D 554 N VAL D 453
SHEET 3 AB2 3 TYR D 576 SER D 581 -1 O ILE D 580 N VAL D 549
SHEET 1 AB3 2 PHE D 556 TYR D 557 0
SHEET 2 AB3 2 LEU D 570 VAL D 571 -1 O LEU D 570 N TYR D 557
SHEET 1 AB4 4 GLN E 3 SER E 7 0
SHEET 2 AB4 4 LEU E 18 SER E 25 -1 O THR E 23 N LYS E 5
SHEET 3 AB4 4 GLN E 77 MET E 82 -1 O VAL E 78 N CYS E 22
SHEET 4 AB4 4 LEU E 67 ASP E 72 -1 N THR E 70 O PHE E 79
SHEET 1 AB5 5 THR E 57 TYR E 59 0
SHEET 2 AB5 5 GLU E 46 ILE E 51 -1 N VAL E 50 O ASN E 58
SHEET 3 AB5 5 GLY E 33 GLN E 39 -1 N TRP E 36 O GLY E 49
SHEET 4 AB5 5 ALA E 91 GLU E 98 -1 O TYR E 94 N ILE E 37
SHEET 5 AB5 5 LEU E 106 TRP E 109 -1 O TYR E 108 N ARG E 97
SHEET 1 AB6 5 THR E 57 TYR E 59 0
SHEET 2 AB6 5 GLU E 46 ILE E 51 -1 N VAL E 50 O ASN E 58
SHEET 3 AB6 5 GLY E 33 GLN E 39 -1 N TRP E 36 O GLY E 49
SHEET 4 AB6 5 ALA E 91 GLU E 98 -1 O TYR E 94 N ILE E 37
SHEET 5 AB6 5 THR E 113 VAL E 115 -1 O VAL E 115 N ALA E 91
SHEET 1 AB7 4 VAL F 4 GLN F 6 0
SHEET 2 AB7 4 VAL F 18 SER F 24 -1 O ARG F 23 N THR F 5
SHEET 3 AB7 4 LYS F 72 ILE F 77 -1 O ALA F 73 N CYS F 22
SHEET 4 AB7 4 SER F 67 ILE F 69 -1 N SER F 67 O ALA F 74
SHEET 1 AB8 2 GLN F 39 LYS F 41 0
SHEET 2 AB8 2 LEU F 45 ILE F 47 -1 O ILE F 47 N GLN F 39
SHEET 1 AB9 2 ILE F 87 TYR F 88 0
SHEET 2 AB9 2 THR F 104 LYS F 105 -1 O THR F 104 N TYR F 88
SHEET 1 AC1 3 LEU G 18 CYS G 22 0
SHEET 2 AC1 3 GLN G 77 MET G 82 -1 O MET G 82 N LEU G 18
SHEET 3 AC1 3 THR G 68 ASP G 72 -1 N THR G 70 O PHE G 79
SHEET 1 AC2 5 THR G 57 TYR G 59 0
SHEET 2 AC2 5 GLU G 46 ILE G 51 -1 N VAL G 50 O ASN G 58
SHEET 3 AC2 5 GLY G 33 GLN G 39 -1 N TRP G 36 O LEU G 48
SHEET 4 AC2 5 ALA G 91 GLU G 98 -1 O VAL G 96 N HIS G 35
SHEET 5 AC2 5 LEU G 106 TRP G 109 -1 O TYR G 108 N ARG G 97
SHEET 1 AC3 5 THR G 57 TYR G 59 0
SHEET 2 AC3 5 GLU G 46 ILE G 51 -1 N VAL G 50 O ASN G 58
SHEET 3 AC3 5 GLY G 33 GLN G 39 -1 N TRP G 36 O LEU G 48
SHEET 4 AC3 5 ALA G 91 GLU G 98 -1 O VAL G 96 N HIS G 35
SHEET 5 AC3 5 THR G 113 VAL G 115 -1 O THR G 113 N TYR G 93
SHEET 1 AC4 4 VAL H 4 GLN H 6 0
SHEET 2 AC4 4 VAL H 18 SER H 24 -1 O ARG H 23 N THR H 5
SHEET 3 AC4 4 LYS H 72 ILE H 77 -1 O ALA H 73 N CYS H 22
SHEET 4 AC4 4 PHE H 64 ILE H 69 -1 N SER H 65 O THR H 76
SHEET 1 AC5 4 LEU H 45 GLY H 51 0
SHEET 2 AC5 4 SER H 36 LYS H 41 -1 N TRP H 37 O LEU H 49
SHEET 3 AC5 4 ILE H 87 TRP H 93 -1 O ILE H 87 N GLU H 40
SHEET 4 AC5 4 TRP H 98 PHE H 100 -1 O VAL H 99 N LEU H 92
SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.05
SSBOND 2 CYS C 637 CYS D 637 1555 1555 2.30
SSBOND 3 CYS E 22 CYS E 95 1555 1555 2.03
SSBOND 4 CYS F 22 CYS F 90 1555 1555 2.04
SSBOND 5 CYS G 22 CYS G 95 1555 1555 2.03
SSBOND 6 CYS H 22 CYS H 90 1555 1555 2.03
LINK ND2 ASN A 19 C1 NAG A 301 1555 1555 1.44
LINK ND2 ASN G 60 C1 NAG J 1 1555 1555 1.45
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44
LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.39
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.39
LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.39
CISPEP 1 TRP B 94 PRO B 95 0 -12.96
CISPEP 2 SER C 443 PRO C 444 0 1.73
CISPEP 3 SER D 443 PRO D 444 0 -22.31
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 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
TER 774 THR A 113
ATOM 775 N ILE B 2 131.594 141.370 189.258 1.00 47.84 N
ATOM 776 CA ILE B 2 132.617 140.352 189.455 1.00 45.77 C
ATOM 777 C ILE B 2 133.247 140.529 190.827 1.00 48.27 C
ATOM 778 O ILE B 2 133.644 141.636 191.209 1.00 50.74 O
ATOM 779 CB ILE B 2 133.666 140.432 188.338 1.00 43.43 C
ATOM 780 CG1 ILE B 2 133.012 140.184 186.978 1.00 45.40 C
ATOM 781 CG2 ILE B 2 134.783 139.438 188.589 1.00 42.66 C
ATOM 782 CD1 ILE B 2 133.992 140.101 185.834 1.00 45.11 C
ATOM 783 N VAL B 3 133.344 139.435 191.576 1.00 58.35 N
ATOM 784 CA VAL B 3 133.886 139.450 192.931 1.00 59.77 C
ATOM 785 C VAL B 3 135.169 138.634 192.938 1.00 58.22 C
ATOM 786 O VAL B 3 135.155 137.440 192.613 1.00 59.17 O
ATOM 787 CB VAL B 3 132.881 138.899 193.955 1.00 60.08 C
ATOM 788 N LEU B 4 136.272 139.271 193.319 1.00 27.57 N
ATOM 789 CA LEU B 4 137.584 138.641 193.352 1.00 22.88 C
ATOM 790 C LEU B 4 138.046 138.527 194.796 1.00 27.64 C
ATOM 791 O LEU B 4 138.060 139.523 195.527 1.00 33.01 O
ATOM 792 CB LEU B 4 138.595 139.444 192.531 1.00 19.50 C
ATOM 793 CG LEU B 4 138.314 139.588 191.034 1.00 21.42 C
ATOM 794 CD1 LEU B 4 137.118 140.488 190.781 1.00 21.01 C
ATOM 795 CD2 LEU B 4 139.539 140.120 190.313 1.00 22.06 C
ATOM 796 N THR B 5 138.428 137.321 195.203 1.00 69.16 N
ATOM 797 CA THR B 5 138.834 137.049 196.575 1.00 72.72 C
ATOM 798 C THR B 5 140.343 136.867 196.635 1.00 72.97 C
ATOM 799 O THR B 5 140.911 136.091 195.860 1.00 73.37 O
ATOM 800 CB THR B 5 138.133 135.802 197.121 1.00 73.29 C
ATOM 801 N GLN B 6 140.985 137.579 197.556 1.00 82.51 N
ATOM 802 CA GLN B 6 142.423 137.490 197.767 1.00 81.83 C
ATOM 803 C GLN B 6 142.694 136.912 199.148 1.00 83.94 C
ATOM 804 O GLN B 6 142.137 137.386 200.144 1.00 85.12 O
ATOM 805 CB GLN B 6 143.086 138.862 197.632 1.00 80.76 C
ATOM 806 CG GLN B 6 144.605 138.820 197.669 1.00 81.64 C
ATOM 807 CD GLN B 6 145.230 140.202 197.636 1.00 83.32 C
ATOM 808 OE1 GLN B 6 145.744 140.687 198.643 1.00 82.34 O
ATOM 809 NE2 GLN B 6 145.188 140.843 196.474 1.00 82.24 N
ATOM 810 N SER B 7 143.541 135.891 199.202 1.00 71.59 N
ATOM 811 CA SER B 7 143.934 135.265 200.453 1.00 71.60 C
ATOM 812 C SER B 7 145.434 135.019 200.437 1.00 71.74 C
ATOM 813 O SER B 7 146.029 134.859 199.365 1.00 71.43 O
ATOM 814 CB SER B 7 143.195 133.937 200.682 1.00 69.71 C
ATOM 815 N VAL B 19 156.619 133.689 199.125 1.00 55.59 N
ATOM 816 CA VAL B 19 155.212 133.585 199.484 1.00 55.08 C
ATOM 817 C VAL B 19 154.377 133.562 198.212 1.00 54.94 C
ATOM 818 O VAL B 19 154.838 133.924 197.128 1.00 54.89 O
ATOM 819 CB VAL B 19 154.759 134.740 200.401 1.00 54.28 C
ATOM 820 N SER B 20 153.127 133.127 198.361 1.00 54.76 N
ATOM 821 CA SER B 20 152.191 133.019 197.246 1.00 54.93 C
ATOM 822 C SER B 20 150.888 133.704 197.633 1.00 55.16 C
ATOM 823 O SER B 20 150.166 133.224 198.513 1.00 56.09 O
ATOM 824 CB SER B 20 151.948 131.556 196.873 1.00 56.86 C
ATOM 825 N LEU B 21 150.588 134.821 196.976 1.00 65.73 N
ATOM 826 CA LEU B 21 149.345 135.552 197.183 1.00 68.15 C
ATOM 827 C LEU B 21 148.381 135.221 196.052 1.00 65.88 C
ATOM 828 O LEU B 21 148.753 135.282 194.876 1.00 65.36 O
ATOM 829 CB LEU B 21 149.600 137.059 197.242 1.00 68.21 C
ATOM 830 CG LEU B 21 150.046 137.647 198.583 1.00 65.74 C
ATOM 831 CD1 LEU B 21 151.393 137.084 199.000 1.00 66.02 C
ATOM 832 CD2 LEU B 21 150.098 139.164 198.507 1.00 64.31 C
ATOM 833 N SER B 22 147.146 134.878 196.409 1.00 51.23 N
ATOM 834 CA SER B 22 146.153 134.411 195.453 1.00 52.69 C
ATOM 835 C SER B 22 145.001 135.401 195.359 1.00 53.49 C
ATOM 836 O SER B 22 144.604 136.007 196.359 1.00 54.43 O
ATOM 837 CB SER B 22 145.619 133.028 195.845 1.00 55.37 C
ATOM 838 N CYS B 23 144.472 135.561 194.147 1.00 63.34 N
ATOM 839 CA CYS B 23 143.291 136.383 193.888 1.00 64.60 C
ATOM 840 C CYS B 23 142.402 135.618 192.912 1.00 63.05 C
ATOM 841 O CYS B 23 142.606 135.683 191.697 1.00 61.08 O
ATOM 842 CB CYS B 23 143.673 137.751 193.334 1.00 64.43 C
ATOM 843 SG CYS B 23 142.359 138.989 193.450 1.00 66.86 S
ATOM 844 N ARG B 24 141.414 134.903 193.447 1.00 80.09 N
ATOM 845 CA ARG B 24 140.520 134.081 192.643 1.00 80.25 C
ATOM 846 C ARG B 24 139.311 134.898 192.207 1.00 79.20 C
ATOM 847 O ARG B 24 138.740 135.648 193.005 1.00 79.37 O
ATOM 848 CB ARG B 24 140.070 132.852 193.433 1.00 80.59 C
ATOM 849 N ALA B 25 138.927 134.750 190.943 1.00 38.90 N
ATOM 850 CA ALA B 25 137.814 135.508 190.396 1.00 39.54 C
ATOM 851 C ALA B 25 136.489 134.794 190.649 1.00 41.07 C
ATOM 852 O ALA B 25 136.440 133.592 190.926 1.00 41.93 O
ATOM 853 CB ALA B 25 138.006 135.740 188.898 1.00 36.40 C
ATOM 854 N SER B 26 135.402 135.560 190.556 1.00 57.75 N
ATOM 855 CA SER B 26 134.059 135.008 190.676 1.00 58.34 C
ATOM 856 C SER B 26 133.549 134.414 189.373 1.00 58.95 C
ATOM 857 O SER B 26 132.681 133.534 189.406 1.00 60.29 O
ATOM 858 CB SER B 26 133.081 136.084 191.156 1.00 57.63 C
ATOM 859 N GLN B 27 134.059 134.875 188.234 1.00 65.70 N
ATOM 860 CA GLN B 27 133.712 134.301 186.944 1.00 65.47 C
ATOM 861 C GLN B 27 134.915 134.425 186.023 1.00 66.77 C
ATOM 862 O GLN B 27 135.808 135.247 186.245 1.00 67.02 O
ATOM 863 CB GLN B 27 132.490 134.985 186.325 1.00 65.36 C
ATOM 864 CG GLN B 27 132.820 136.245 185.551 1.00 65.36 C
ATOM 865 CD GLN B 27 131.632 136.778 184.781 1.00 67.62 C
ATOM 866 OE1 GLN B 27 130.611 137.141 185.364 1.00 67.65 O
ATOM 867 NE2 GLN B 27 131.760 136.830 183.460 1.00 67.44 N
ATOM 868 N SER B 28 134.931 133.594 184.983 1.00 69.12 N
ATOM 869 CA SER B 28 136.046 133.599 184.046 1.00 67.74 C
ATOM 870 C SER B 28 136.221 134.984 183.436 1.00 69.37 C
ATOM 871 O SER B 28 135.266 135.580 182.930 1.00 68.31 O
ATOM 872 CB SER B 28 135.817 132.563 182.947 1.00 67.18 C
ATOM 873 N ILE B 29 137.453 135.490 183.483 1.00 49.50 N
ATOM 874 CA ILE B 29 137.775 136.830 183.003 1.00 44.11 C
ATOM 875 C ILE B 29 138.966 136.751 182.059 1.00 43.57 C
ATOM 876 O ILE B 29 139.628 137.760 181.792 1.00 40.92 O
ATOM 877 CB ILE B 29 138.069 137.780 184.177 1.00 37.72 C
ATOM 878 CG1 ILE B 29 138.903 137.060 185.237 1.00 38.40 C
ATOM 879 CG2 ILE B 29 136.779 138.285 184.788 1.00 41.27 C
ATOM 880 CD1 ILE B 29 139.104 137.854 186.499 1.00 39.51 C
ATOM 881 N SER B 30 139.238 135.553 181.541 1.00 51.25 N
ATOM 882 CA SER B 30 140.446 135.296 180.767 1.00 48.11 C
ATOM 883 C SER B 30 141.683 135.652 181.581 1.00 50.38 C
ATOM 884 O SER B 30 141.839 135.190 182.715 1.00 52.82 O
ATOM 885 CB SER B 30 140.429 136.077 179.453 1.00 45.76 C
ATOM 886 OG SER B 30 139.267 135.784 178.699 1.00 44.56 O
ATOM 887 N ASN B 31 142.554 136.491 181.024 1.00 35.16 N
ATOM 888 CA ASN B 31 143.806 136.859 181.673 1.00 30.47 C
ATOM 889 C ASN B 31 143.848 138.349 181.979 1.00 32.98 C
ATOM 890 O ASN B 31 144.925 138.947 182.036 1.00 35.25 O
ATOM 891 CB ASN B 31 145.002 136.460 180.811 1.00 27.91 C
ATOM 892 CG ASN B 31 145.213 137.399 179.639 1.00 28.05 C
ATOM 893 OD1 ASN B 31 144.275 138.039 179.165 1.00 28.20 O
ATOM 894 ND2 ASN B 31 146.449 137.487 179.167 1.00 30.93 N
ATOM 895 N ASN B 32 142.682 138.965 182.175 1.00 32.60 N
ATOM 896 CA ASN B 32 142.591 140.411 182.367 1.00 30.31 C
ATOM 897 C ASN B 32 142.575 140.709 183.860 1.00 32.41 C
ATOM 898 O ASN B 32 141.529 140.897 184.482 1.00 39.02 O
ATOM 899 CB ASN B 32 141.355 140.958 181.671 1.00 34.64 C
ATOM 900 CG ASN B 32 141.533 141.046 180.182 1.00 33.28 C
ATOM 901 OD1 ASN B 32 142.644 141.223 179.700 1.00 32.74 O
ATOM 902 ND2 ASN B 32 140.441 140.921 179.441 1.00 34.08 N
ATOM 903 N LEU B 33 143.770 140.751 184.447 1.00 30.79 N
ATOM 904 CA LEU B 33 143.878 141.013 185.879 1.00 31.65 C
ATOM 905 C LEU B 33 145.251 141.626 186.150 1.00 34.52 C
ATOM 906 O LEU B 33 146.235 140.895 186.290 1.00 35.80 O
ATOM 907 CB LEU B 33 143.665 139.736 186.674 1.00 33.14 C
ATOM 908 CG LEU B 33 143.740 139.817 188.197 1.00 32.50 C
ATOM 909 CD1 LEU B 33 142.799 138.804 188.835 1.00 33.38 C
ATOM 910 CD2 LEU B 33 145.161 139.587 188.657 1.00 33.55 C
ATOM 911 N HIS B 34 145.301 142.954 186.233 1.00 32.47 N
ATOM 912 CA HIS B 34 146.526 143.638 186.619 1.00 29.62 C
ATOM 913 C HIS B 34 146.657 143.655 188.133 1.00 32.79 C
ATOM 914 O HIS B 34 145.671 143.825 188.854 1.00 34.83 O
ATOM 915 CB HIS B 34 146.554 145.072 186.091 1.00 26.31 C
ATOM 916 CG HIS B 34 145.920 145.244 184.748 1.00 28.31 C
ATOM 917 ND1 HIS B 34 145.921 144.255 183.790 1.00 33.69 N
ATOM 918 CD2 HIS B 34 145.281 146.301 184.196 1.00 28.96 C
ATOM 919 CE1 HIS B 34 145.300 144.691 182.709 1.00 32.24 C
ATOM 920 NE2 HIS B 34 144.902 145.931 182.930 1.00 32.20 N
ATOM 921 N TRP B 35 147.883 143.481 188.613 1.00 50.85 N
ATOM 922 CA TRP B 35 148.177 143.513 190.038 1.00 52.06 C
ATOM 923 C TRP B 35 148.684 144.896 190.419 1.00 51.65 C
ATOM 924 O TRP B 35 149.602 145.422 189.782 1.00 52.69 O
ATOM 925 CB TRP B 35 149.209 142.447 190.407 1.00 53.11 C
ATOM 926 CG TRP B 35 148.630 141.074 190.510 1.00 54.82 C
ATOM 927 CD1 TRP B 35 148.223 140.277 189.483 1.00 53.32 C
ATOM 928 CD2 TRP B 35 148.394 140.333 191.711 1.00 55.04 C
ATOM 929 NE1 TRP B 35 147.748 139.085 189.969 1.00 54.06 N
ATOM 930 CE2 TRP B 35 147.842 139.095 191.335 1.00 54.49 C
ATOM 931 CE3 TRP B 35 148.598 140.596 193.067 1.00 55.52 C
ATOM 932 CZ2 TRP B 35 147.492 138.123 192.266 1.00 54.94 C
ATOM 933 CZ3 TRP B 35 148.248 139.630 193.989 1.00 53.86 C
ATOM 934 CH2 TRP B 35 147.700 138.410 193.586 1.00 54.11 C
ATOM 935 N TYR B 36 148.085 145.479 191.453 1.00 26.49 N
ATOM 936 CA TYR B 36 148.443 146.808 191.925 1.00 26.30 C
ATOM 937 C TYR B 36 148.981 146.707 193.343 1.00 27.08 C
ATOM 938 O TYR B 36 148.395 146.019 194.185 1.00 29.35 O
ATOM 939 CB TYR B 36 147.242 147.753 191.873 1.00 21.29 C
ATOM 940 CG TYR B 36 146.945 148.279 190.489 1.00 18.92 C
ATOM 941 CD1 TYR B 36 147.946 148.839 189.711 1.00 22.49 C
ATOM 942 CD2 TYR B 36 145.665 148.221 189.963 1.00 18.08 C
ATOM 943 CE1 TYR B 36 147.681 149.322 188.448 1.00 23.31 C
ATOM 944 CE2 TYR B 36 145.392 148.703 188.700 1.00 19.93 C
ATOM 945 CZ TYR B 36 146.403 149.252 187.947 1.00 21.48 C
ATOM 946 OH TYR B 36 146.136 149.732 186.687 1.00 18.53 O
ATOM 947 N GLN B 37 150.097 147.385 193.599 1.00 43.06 N
ATOM 948 CA GLN B 37 150.757 147.370 194.896 1.00 45.70 C
ATOM 949 C GLN B 37 150.760 148.771 195.487 1.00 45.07 C
ATOM 950 O GLN B 37 150.934 149.758 194.767 1.00 45.75 O
ATOM 951 CB GLN B 37 152.196 146.849 194.782 1.00 46.97 C
ATOM 952 N GLU B 42 151.571 156.387 200.007 1.00 75.75 N
ATOM 953 CA GLU B 42 152.113 156.411 198.658 1.00 73.90 C
ATOM 954 C GLU B 42 151.035 155.982 197.674 1.00 74.30 C
ATOM 955 O GLU B 42 150.078 155.292 198.031 1.00 75.44 O
ATOM 956 CB GLU B 42 153.340 155.500 198.525 1.00 72.99 C
ATOM 957 N SER B 43 151.201 156.406 196.428 1.00 60.59 N
ATOM 958 CA SER B 43 150.287 156.011 195.364 1.00 59.13 C
ATOM 959 C SER B 43 150.535 154.556 194.989 1.00 58.67 C
ATOM 960 O SER B 43 151.690 154.172 194.774 1.00 59.17 O
ATOM 961 CB SER B 43 150.469 156.905 194.147 1.00 57.65 C
ATOM 962 OG SER B 43 150.468 158.270 194.519 1.00 60.06 O
ATOM 963 N PRO B 44 149.501 153.719 194.904 1.00 30.57 N
ATOM 964 CA PRO B 44 149.726 152.316 194.539 1.00 30.56 C
ATOM 965 C PRO B 44 150.451 152.204 193.207 1.00 34.87 C
ATOM 966 O PRO B 44 150.222 152.988 192.284 1.00 37.34 O
ATOM 967 CB PRO B 44 148.309 151.742 194.457 1.00 27.88 C
ATOM 968 CG PRO B 44 147.507 152.593 195.369 1.00 27.81 C
ATOM 969 CD PRO B 44 148.116 153.968 195.340 1.00 28.96 C
ATOM 970 N ARG B 45 151.387 151.261 193.114 1.00 73.42 N
ATOM 971 CA ARG B 45 152.161 151.055 191.865 1.00 73.81 C
ATOM 972 C ARG B 45 151.807 149.678 191.281 1.00 71.40 C
ATOM 973 O ARG B 45 151.689 148.703 192.046 1.00 69.61 O
ATOM 974 CB ARG B 45 153.665 151.203 192.128 1.00 76.02 C
ATOM 975 N LEU B 46 151.635 149.628 189.963 1.00 49.90 N
ATOM 976 CA LEU B 46 151.293 148.407 189.251 1.00 49.23 C
ATOM 977 C LEU B 46 152.471 147.440 189.239 1.00 50.44 C
ATOM 978 O LEU B 46 153.633 147.835 189.357 1.00 55.03 O
ATOM 979 CB LEU B 46 150.862 148.730 187.823 1.00 48.44 C
ATOM 980 CG LEU B 46 150.464 147.569 186.912 1.00 47.10 C
ATOM 981 CD1 LEU B 46 149.479 148.027 185.855 1.00 50.58 C
ATOM 982 CD2 LEU B 46 151.694 146.978 186.254 1.00 46.82 C
ATOM 983 N LEU B 47 152.155 146.155 189.101 1.00 40.72 N
ATOM 984 CA LEU B 47 153.167 145.111 189.027 1.00 41.60 C
ATOM 985 C LEU B 47 153.100 144.322 187.731 1.00 43.23 C
ATOM 986 O LEU B 47 154.130 144.129 187.076 1.00 43.22 O
ATOM 987 CB LEU B 47 153.030 144.161 190.227 1.00 42.09 C
ATOM 988 CG LEU B 47 152.970 144.821 191.604 1.00 43.92 C
ATOM 989 CD1 LEU B 47 153.214 143.798 192.703 1.00 42.93 C
ATOM 990 CD2 LEU B 47 153.971 145.959 191.694 1.00 43.09 C
ATOM 991 N PHE B 48 151.915 143.861 187.334 1.00 54.67 N
ATOM 992 CA PHE B 48 151.756 143.016 186.159 1.00 51.14 C
ATOM 993 C PHE B 48 150.619 143.525 185.287 1.00 47.98 C
ATOM 994 O PHE B 48 149.612 144.030 185.792 1.00 53.54 O
ATOM 995 CB PHE B 48 151.477 141.562 186.549 1.00 50.51 C
ATOM 996 CG PHE B 48 152.535 140.952 187.414 1.00 50.87 C
ATOM 997 CD1 PHE B 48 153.786 140.663 186.898 1.00 52.40 C
ATOM 998 CD2 PHE B 48 152.279 140.659 188.740 1.00 50.62 C
ATOM 999 CE1 PHE B 48 154.763 140.098 187.691 1.00 53.42 C
ATOM 1000 CE2 PHE B 48 153.250 140.094 189.538 1.00 51.90 C
ATOM 1001 CZ PHE B 48 154.495 139.813 189.012 1.00 53.71 C
ATOM 1002 N LYS B 49 150.785 143.377 183.978 1.00 16.54 N
ATOM 1003 CA LYS B 49 149.742 143.659 183.002 1.00 17.69 C
ATOM 1004 C LYS B 49 149.339 142.345 182.350 1.00 23.54 C
ATOM 1005 O LYS B 49 150.196 141.619 181.836 1.00 34.33 O
ATOM 1006 CB LYS B 49 150.229 144.657 181.954 1.00 19.43 C
ATOM 1007 CG LYS B 49 149.230 144.932 180.847 1.00 20.42 C
ATOM 1008 CD LYS B 49 149.749 145.994 179.895 1.00 22.33 C
ATOM 1009 CE LYS B 49 148.776 146.237 178.755 1.00 24.64 C
ATOM 1010 NZ LYS B 49 149.230 147.334 177.857 1.00 23.83 N
ATOM 1011 N SER B 50 148.042 142.039 182.373 1.00 14.00 N
ATOM 1012 CA SER B 50 147.490 140.789 181.862 1.00 17.06 C
ATOM 1013 C SER B 50 147.759 139.612 182.788 1.00 16.34 C
ATOM 1014 O SER B 50 147.611 138.458 182.381 1.00 14.17 O
ATOM 1015 CB SER B 50 148.015 140.467 180.460 1.00 13.41 C
ATOM 1016 OG SER B 50 147.481 141.362 179.502 1.00 17.71 O
ATOM 1017 N ALA B 51 148.163 139.874 184.028 1.00 31.11 N
ATOM 1018 CA ALA B 51 148.314 138.888 185.091 1.00 33.87 C
ATOM 1019 C ALA B 51 149.545 138.008 184.934 1.00 40.29 C
ATOM 1020 O ALA B 51 149.831 137.210 185.833 1.00 46.29 O
ATOM 1021 CB ALA B 51 147.082 137.984 185.219 1.00 37.55 C
ATOM 1022 N SER B 52 150.285 138.117 183.832 1.00 41.82 N
ATOM 1023 CA SER B 52 151.489 137.323 183.640 1.00 41.07 C
ATOM 1024 C SER B 52 152.671 138.116 183.107 1.00 41.11 C
ATOM 1025 O SER B 52 153.798 137.613 183.163 1.00 45.61 O
ATOM 1026 CB SER B 52 151.214 136.153 182.683 1.00 43.91 C
ATOM 1027 N GLN B 53 152.456 139.326 182.603 1.00 16.73 N
ATOM 1028 CA GLN B 53 153.502 140.126 181.983 1.00 12.20 C
ATOM 1029 C GLN B 53 154.136 141.033 183.029 1.00 13.64 C
ATOM 1030 O GLN B 53 153.454 141.880 183.616 1.00 20.15 O
ATOM 1031 CB GLN B 53 152.933 140.956 180.835 1.00 10.12 C
ATOM 1032 CG GLN B 53 153.851 142.063 180.372 1.00 12.72 C
ATOM 1033 CD GLN B 53 153.286 142.825 179.197 1.00 17.92 C
ATOM 1034 OE1 GLN B 53 152.280 142.428 178.612 1.00 15.49 O
ATOM 1035 NE2 GLN B 53 153.937 143.924 178.838 1.00 17.11 N
ATOM 1036 N SER B 54 155.433 140.856 183.260 1.00 36.44 N
ATOM 1037 CA SER B 54 156.157 141.746 184.153 1.00 39.97 C
ATOM 1038 C SER B 54 156.236 143.144 183.551 1.00 40.14 C
ATOM 1039 O SER B 54 156.276 143.318 182.331 1.00 40.29 O
ATOM 1040 CB SER B 54 157.562 141.210 184.425 1.00 40.68 C
ATOM 1041 N ILE B 55 156.262 144.147 184.421 1.00 48.89 N
ATOM 1042 CA ILE B 55 156.222 145.540 183.996 1.00 50.47 C
ATOM 1043 C ILE B 55 157.603 146.156 184.153 1.00 50.32 C
ATOM 1044 O ILE B 55 158.376 145.790 185.045 1.00 50.10 O
ATOM 1045 CB ILE B 55 155.166 146.344 184.783 1.00 51.33 C
ATOM 1046 CG1 ILE B 55 153.809 146.264 184.085 1.00 51.34 C
ATOM 1047 CG2 ILE B 55 155.596 147.787 184.936 1.00 49.83 C
ATOM 1048 CD1 ILE B 55 153.723 147.103 182.831 1.00 50.47 C
ATOM 1049 N SER B 56 157.903 147.111 183.274 1.00 31.92 N
ATOM 1050 CA SER B 56 159.215 147.742 183.253 1.00 29.40 C
ATOM 1051 C SER B 56 159.524 148.397 184.593 1.00 30.32 C
ATOM 1052 O SER B 56 158.688 149.106 185.161 1.00 33.71 O
ATOM 1053 CB SER B 56 159.276 148.780 182.132 1.00 28.80 C
ATOM 1054 OG SER B 56 158.684 148.286 180.943 1.00 29.45 O
ATOM 1055 N GLY B 57 160.733 148.154 185.097 1.00 54.40 N
ATOM 1056 CA GLY B 57 161.206 148.759 186.320 1.00 55.46 C
ATOM 1057 C GLY B 57 160.976 147.946 187.576 1.00 56.19 C
ATOM 1058 O GLY B 57 161.645 148.191 188.586 1.00 55.06 O
ATOM 1059 N ILE B 58 160.053 146.990 187.547 1.00 70.23 N
ATOM 1060 CA ILE B 58 159.783 146.145 188.708 1.00 71.37 C
ATOM 1061 C ILE B 58 160.912 145.137 188.866 1.00 71.12 C
ATOM 1062 O ILE B 58 161.460 144.660 187.862 1.00 70.40 O
ATOM 1063 CB ILE B 58 158.427 145.433 188.582 1.00 71.83 C
ATOM 1064 CG1 ILE B 58 157.459 146.271 187.749 1.00 70.80 C
ATOM 1065 CG2 ILE B 58 157.847 145.137 189.955 1.00 72.10 C
ATOM 1066 CD1 ILE B 58 157.182 147.631 188.342 1.00 71.76 C
ATOM 1067 N PRO B 59 161.296 144.788 190.091 1.00 53.50 N
ATOM 1068 CA PRO B 59 162.275 143.712 190.268 1.00 52.03 C
ATOM 1069 C PRO B 59 161.733 142.405 189.713 1.00 53.10 C
ATOM 1070 O PRO B 59 160.533 142.131 189.782 1.00 56.03 O
ATOM 1071 CB PRO B 59 162.467 143.646 191.788 1.00 51.00 C
ATOM 1072 CG PRO B 59 161.954 144.950 192.305 1.00 52.01 C
ATOM 1073 CD PRO B 59 160.858 145.356 191.375 1.00 52.37 C
ATOM 1074 N SER B 60 162.633 141.591 189.163 1.00 47.62 N
ATOM 1075 CA SER B 60 162.220 140.321 188.582 1.00 48.07 C
ATOM 1076 C SER B 60 161.748 139.326 189.631 1.00 48.06 C
ATOM 1077 O SER B 60 161.212 138.274 189.266 1.00 48.60 O
ATOM 1078 CB SER B 60 163.366 139.718 187.771 1.00 49.63 C
ATOM 1079 OG SER B 60 163.437 140.305 186.483 1.00 50.52 O
ATOM 1080 N ARG B 61 161.936 139.628 190.917 1.00 48.19 N
ATOM 1081 CA ARG B 61 161.499 138.714 191.966 1.00 48.37 C
ATOM 1082 C ARG B 61 159.999 138.448 191.884 1.00 50.24 C
ATOM 1083 O ARG B 61 159.543 137.335 192.170 1.00 50.95 O
ATOM 1084 CB ARG B 61 161.878 139.278 193.335 1.00 48.48 C
ATOM 1085 CG ARG B 61 160.929 140.336 193.864 1.00 47.37 C
ATOM 1086 CD ARG B 61 161.103 140.531 195.361 1.00 47.43 C
ATOM 1087 NE ARG B 61 162.265 141.352 195.677 1.00 48.31 N
ATOM 1088 CZ ARG B 61 162.310 142.670 195.538 1.00 48.08 C
ATOM 1089 NH1 ARG B 61 161.274 143.352 195.078 1.00 48.76 N
ATOM 1090 NH2 ARG B 61 163.422 143.320 195.869 1.00 46.66 N
ATOM 1091 N PHE B 62 159.218 139.454 191.496 1.00 53.38 N
ATOM 1092 CA PHE B 62 157.775 139.285 191.386 1.00 52.61 C
ATOM 1093 C PHE B 62 157.425 138.359 190.227 1.00 51.72 C
ATOM 1094 O PHE B 62 158.067 138.385 189.174 1.00 49.84 O
ATOM 1095 CB PHE B 62 157.092 140.638 191.192 1.00 50.35 C
ATOM 1096 CG PHE B 62 157.313 141.599 192.322 1.00 48.18 C
ATOM 1097 CD1 PHE B 62 156.452 141.626 193.403 1.00 48.38 C
ATOM 1098 CD2 PHE B 62 158.378 142.481 192.300 1.00 50.57 C
ATOM 1099 CE1 PHE B 62 156.651 142.512 194.442 1.00 50.84 C
ATOM 1100 CE2 PHE B 62 158.583 143.369 193.337 1.00 51.94 C
ATOM 1101 CZ PHE B 62 157.718 143.385 194.409 1.00 52.07 C
ATOM 1102 N SER B 63 156.395 137.537 190.427 1.00 52.09 N
ATOM 1103 CA SER B 63 155.909 136.621 189.402 1.00 52.48 C
ATOM 1104 C SER B 63 154.393 136.529 189.481 1.00 52.20 C
ATOM 1105 O SER B 63 153.829 136.462 190.578 1.00 51.82 O
ATOM 1106 CB SER B 63 156.531 135.231 189.562 1.00 51.51 C
ATOM 1107 OG SER B 63 155.666 134.228 189.060 1.00 54.05 O
ATOM 1108 N GLY B 64 153.740 136.522 188.321 1.00 37.63 N
ATOM 1109 CA GLY B 64 152.295 136.404 188.256 1.00 37.86 C
ATOM 1110 C GLY B 64 151.833 135.386 187.233 1.00 38.12 C
ATOM 1111 O GLY B 64 152.270 135.421 186.078 1.00 35.90 O
ATOM 1112 N SER B 65 150.945 134.479 187.638 1.00 55.02 N
ATOM 1113 CA SER B 65 150.501 133.377 186.795 1.00 57.05 C
ATOM 1114 C SER B 65 148.981 133.263 186.858 1.00 57.20 C
ATOM 1115 O SER B 65 148.290 134.132 187.399 1.00 55.85 O
ATOM 1116 CB SER B 65 151.164 132.059 187.215 1.00 57.60 C
ATOM 1117 OG SER B 65 150.705 131.639 188.487 1.00 56.69 O
ATOM 1118 N GLY B 66 148.463 132.176 186.293 1.00 61.04 N
ATOM 1119 CA GLY B 66 147.038 131.947 186.184 1.00 61.66 C
ATOM 1120 C GLY B 66 146.475 132.505 184.888 1.00 62.85 C
ATOM 1121 O GLY B 66 146.865 133.570 184.404 1.00 63.85 O
ATOM 1122 N SER B 67 145.540 131.754 184.305 1.00 63.80 N
ATOM 1123 CA SER B 67 145.025 132.161 183.003 1.00 63.15 C
ATOM 1124 C SER B 67 143.505 132.203 182.902 1.00 62.31 C
ATOM 1125 O SER B 67 142.964 133.062 182.200 1.00 64.02 O
ATOM 1126 CB SER B 67 145.574 131.235 181.915 1.00 63.38 C
ATOM 1127 OG SER B 67 146.809 131.718 181.413 1.00 66.18 O
ATOM 1128 N GLY B 68 142.796 131.288 183.559 1.00 46.41 N
ATOM 1129 CA GLY B 68 141.361 131.268 183.340 1.00 48.51 C
ATOM 1130 C GLY B 68 140.500 132.014 184.339 1.00 47.97 C
ATOM 1131 O GLY B 68 139.788 132.953 183.970 1.00 43.68 O
ATOM 1132 N THR B 69 140.548 131.605 185.606 1.00 57.64 N
ATOM 1133 CA THR B 69 139.829 132.294 186.671 1.00 57.05 C
ATOM 1134 C THR B 69 140.591 132.381 187.982 1.00 57.46 C
ATOM 1135 O THR B 69 140.206 133.185 188.839 1.00 57.18 O
ATOM 1136 CB THR B 69 138.476 131.618 186.943 1.00 57.39 C
ATOM 1137 OG1 THR B 69 138.652 130.553 187.886 1.00 58.14 O
ATOM 1138 CG2 THR B 69 137.877 131.065 185.659 1.00 55.72 C
ATOM 1139 N ASP B 70 141.643 131.593 188.173 1.00 66.12 N
ATOM 1140 CA ASP B 70 142.373 131.533 189.431 1.00 66.98 C
ATOM 1141 C ASP B 70 143.769 132.095 189.207 1.00 66.52 C
ATOM 1142 O ASP B 70 144.615 131.438 188.591 1.00 67.50 O
ATOM 1143 CB ASP B 70 142.437 130.097 189.952 1.00 68.63 C
ATOM 1144 N PHE B 71 144.007 133.299 189.716 1.00 40.58 N
ATOM 1145 CA PHE B 71 145.267 134.000 189.530 1.00 38.04 C
ATOM 1146 C PHE B 71 146.034 134.020 190.842 1.00 38.84 C
ATOM 1147 O PHE B 71 145.466 134.309 191.900 1.00 40.58 O
ATOM 1148 CB PHE B 71 145.036 135.430 189.041 1.00 38.49 C
ATOM 1149 CG PHE B 71 144.499 135.514 187.643 1.00 36.23 C
ATOM 1150 CD1 PHE B 71 145.355 135.540 186.559 1.00 33.14 C
ATOM 1151 CD2 PHE B 71 143.138 135.578 187.414 1.00 37.01 C
ATOM 1152 CE1 PHE B 71 144.862 135.622 185.275 1.00 32.42 C
ATOM 1153 CE2 PHE B 71 142.642 135.660 186.131 1.00 35.33 C
ATOM 1154 CZ PHE B 71 143.505 135.683 185.061 1.00 33.12 C
ATOM 1155 N THR B 72 147.328 133.719 190.768 1.00 57.40 N
ATOM 1156 CA THR B 72 148.177 133.639 191.945 1.00 59.09 C
ATOM 1157 C THR B 72 149.379 134.556 191.779 1.00 59.35 C
ATOM 1158 O THR B 72 149.859 134.785 190.666 1.00 59.59 O
ATOM 1159 CB THR B 72 148.656 132.204 192.200 1.00 58.51 C
ATOM 1160 OG1 THR B 72 149.861 131.963 191.463 1.00 59.18 O
ATOM 1161 CG2 THR B 72 147.596 131.205 191.768 1.00 56.69 C
ATOM 1162 N LEU B 73 149.854 135.082 192.903 1.00 48.97 N
ATOM 1163 CA LEU B 73 151.035 135.930 192.952 1.00 49.04 C
ATOM 1164 C LEU B 73 152.066 135.297 193.872 1.00 48.83 C
ATOM 1165 O LEU B 73 151.726 134.798 194.949 1.00 48.41 O
ATOM 1166 CB LEU B 73 150.686 137.339 193.443 1.00 49.21 C
ATOM 1167 CG LEU B 73 151.847 138.286 193.747 1.00 48.06 C
ATOM 1168 CD1 LEU B 73 152.340 138.957 192.478 1.00 47.81 C
ATOM 1169 CD2 LEU B 73 151.432 139.323 194.775 1.00 47.50 C
ATOM 1170 N SER B 74 153.315 135.279 193.403 1.00 64.49 N
ATOM 1171 CA SER B 74 154.417 134.696 194.207 1.00 65.75 C
ATOM 1172 C SER B 74 155.612 135.655 194.176 1.00 65.50 C
ATOM 1173 O SER B 74 156.071 135.999 193.065 1.00 65.76 O
ATOM 1174 CB SER B 74 154.798 133.334 193.698 1.00 67.45 C
ATOM 1175 N ILE B 75 156.081 136.074 195.352 1.00 48.23 N
ATOM 1176 CA ILE B 75 157.235 137.015 195.430 1.00 48.51 C
ATOM 1177 C ILE B 75 158.415 136.262 196.061 1.00 48.69 C
ATOM 1178 O ILE B 75 158.224 135.683 197.153 1.00 48.40 O
ATOM 1179 CB ILE B 75 156.852 138.269 196.236 1.00 49.45 C
ATOM 1180 CG1 ILE B 75 155.459 138.775 195.862 1.00 47.31 C
ATOM 1181 CG2 ILE B 75 157.908 139.363 196.085 1.00 48.61 C
ATOM 1182 CD1 ILE B 75 154.556 139.038 197.052 1.00 46.74 C
ATOM 1183 N ASN B 76 159.577 136.277 195.400 1.00 65.11 N
ATOM 1184 CA ASN B 76 160.775 135.559 195.917 1.00 66.76 C
ATOM 1185 C ASN B 76 162.010 136.013 195.133 1.00 67.42 C
ATOM 1186 O ASN B 76 161.997 135.828 193.896 1.00 67.91 O
ATOM 1187 CB ASN B 76 160.594 134.046 195.850 1.00 67.10 C
ATOM 1188 CG ASN B 76 160.566 133.415 197.222 1.00 66.67 C
ATOM 1189 OD1 ASN B 76 160.573 134.124 198.234 1.00 66.06 O
ATOM 1190 ND2 ASN B 76 160.534 132.092 197.278 1.00 66.59 N
ATOM 1191 N GLY B 84 146.491 147.860 201.663 1.00 65.65 N
ATOM 1192 CA GLY B 84 147.347 148.085 200.482 1.00 65.56 C
ATOM 1193 C GLY B 84 147.855 146.772 199.927 1.00 67.73 C
ATOM 1194 O GLY B 84 147.366 146.362 198.854 1.00 67.04 O
ATOM 1195 N MET B 85 148.809 146.141 200.617 1.00 73.03 N
ATOM 1196 CA MET B 85 149.311 144.809 200.190 1.00 70.68 C
ATOM 1197 C MET B 85 149.471 144.812 198.664 1.00 68.56 C
ATOM 1198 O MET B 85 150.230 145.662 198.148 1.00 67.13 O
ATOM 1199 CB MET B 85 148.342 143.699 200.613 1.00 70.81 C
ATOM 1200 CG MET B 85 148.981 142.331 200.749 1.00 71.27 C
ATOM 1201 SD MET B 85 147.805 141.080 201.302 1.00 73.49 S
ATOM 1202 CE MET B 85 147.232 141.830 202.832 1.00 70.64 C
ATOM 1203 N TYR B 86 148.780 143.898 197.978 1.00 47.81 N
ATOM 1204 CA TYR B 86 148.861 143.828 196.495 1.00 49.10 C
ATOM 1205 C TYR B 86 147.460 143.615 195.927 1.00 49.29 C
ATOM 1206 O TYR B 86 147.025 142.453 195.800 1.00 46.64 O
ATOM 1207 CB TYR B 86 149.832 142.725 196.067 1.00 48.50 C
ATOM 1208 CG TYR B 86 151.237 142.844 196.640 1.00 47.08 C
ATOM 1209 CD1 TYR B 86 152.228 143.545 195.967 1.00 43.88 C
ATOM 1210 CD2 TYR B 86 151.572 142.253 197.852 1.00 48.02 C
ATOM 1211 CE1 TYR B 86 153.508 143.655 196.481 1.00 44.79 C
ATOM 1212 CE2 TYR B 86 152.849 142.358 198.379 1.00 46.37 C
ATOM 1213 CZ TYR B 86 153.820 143.062 197.691 1.00 46.56 C
ATOM 1214 OH TYR B 86 155.080 143.169 198.202 1.00 49.43 O
ATOM 1215 N PHE B 87 146.766 144.707 195.601 1.00 44.62 N
ATOM 1216 CA PHE B 87 145.424 144.607 194.968 1.00 42.10 C
ATOM 1217 C PHE B 87 145.550 143.859 193.655 1.00 38.19 C
ATOM 1218 O PHE B 87 146.643 143.819 193.054 1.00 37.60 O
ATOM 1219 CB PHE B 87 144.822 145.977 194.651 1.00 40.54 C
ATOM 1220 CG PHE B 87 144.965 147.012 195.756 1.00 39.79 C
ATOM 1221 CD1 PHE B 87 144.044 147.073 196.794 1.00 40.20 C
ATOM 1222 CD2 PHE B 87 146.007 147.931 195.740 1.00 39.41 C
ATOM 1223 CE1 PHE B 87 144.173 148.018 197.797 1.00 43.71 C
ATOM 1224 CE2 PHE B 87 146.130 148.875 196.745 1.00 41.62 C
ATOM 1225 CZ PHE B 87 145.213 148.916 197.768 1.00 44.42 C
ATOM 1226 N CYS B 88 144.427 143.287 193.207 1.00 25.74 N
ATOM 1227 CA CYS B 88 144.391 142.542 191.924 1.00 26.41 C
ATOM 1228 C CYS B 88 143.237 143.097 191.082 1.00 22.08 C
ATOM 1229 O CYS B 88 142.114 142.565 191.204 1.00 24.81 O
ATOM 1230 CB CYS B 88 144.159 141.060 192.179 1.00 30.26 C
ATOM 1231 SG CYS B 88 142.674 140.723 193.162 1.00 35.06 S
ATOM 1232 N GLN B 89 143.499 144.117 190.265 1.00 9.28 N
ATOM 1233 CA GLN B 89 142.405 144.776 189.508 1.00 10.10 C
ATOM 1234 C GLN B 89 142.076 144.001 188.233 1.00 14.88 C
ATOM 1235 O GLN B 89 142.927 143.992 187.322 1.00 28.56 O
ATOM 1236 CB GLN B 89 142.823 146.188 189.108 1.00 17.05 C
ATOM 1237 N GLN B 90 140.888 143.393 188.165 1.00 34.33 N
ATOM 1238 CA GLN B 90 140.475 142.733 186.936 1.00 36.65 C
ATOM 1239 C GLN B 90 139.771 143.749 186.050 1.00 34.92 C
ATOM 1240 O GLN B 90 139.026 144.601 186.541 1.00 44.35 O
ATOM 1241 CB GLN B 90 139.555 141.544 187.225 1.00 34.99 C
ATOM 1242 CG GLN B 90 138.259 141.902 187.925 1.00 35.16 C
ATOM 1243 CD GLN B 90 137.205 142.415 186.969 1.00 36.81 C
ATOM 1244 OE1 GLN B 90 137.334 142.271 185.753 1.00 35.19 O
ATOM 1245 NE2 GLN B 90 136.161 143.029 187.511 1.00 39.63 N
ATOM 1246 N THR B 91 140.004 143.658 184.746 1.00 27.95 N
ATOM 1247 CA THR B 91 139.479 144.631 183.796 1.00 31.81 C
ATOM 1248 C THR B 91 138.657 143.935 182.727 1.00 33.61 C
ATOM 1249 O THR B 91 138.802 144.184 181.528 1.00 32.73 O
ATOM 1250 CB THR B 91 140.602 145.438 183.160 1.00 30.95 C
ATOM 1251 OG1 THR B 91 141.151 144.702 182.063 1.00 33.99 O
ATOM 1252 CG2 THR B 91 141.694 145.704 184.178 1.00 32.44 C
ATOM 1253 N ASN B 92 137.788 143.022 183.161 1.00 39.20 N
ATOM 1254 CA ASN B 92 136.984 142.234 182.186 1.00 41.68 C
ATOM 1255 C ASN B 92 135.620 142.898 181.987 1.00 40.22 C
ATOM 1256 O ASN B 92 135.043 142.744 180.890 1.00 41.71 O
ATOM 1257 CB ASN B 92 136.835 140.780 182.621 1.00 43.43 C
ATOM 1258 CG ASN B 92 136.848 139.829 181.450 1.00 44.16 C
ATOM 1259 OD1 ASN B 92 135.985 138.949 181.352 1.00 48.35 O
ATOM 1260 ND2 ASN B 92 137.812 139.983 180.555 1.00 43.37 N
ATOM 1261 N SER B 93 135.122 143.599 183.008 1.00 40.65 N
ATOM 1262 CA SER B 93 133.774 144.216 182.907 1.00 43.74 C
ATOM 1263 C SER B 93 133.715 145.497 183.746 1.00 44.40 C
ATOM 1264 O SER B 93 134.203 145.469 184.894 1.00 47.41 O
ATOM 1265 CB SER B 93 132.707 143.245 183.332 1.00 45.58 C
ATOM 1266 OG SER B 93 132.952 142.767 184.647 1.00 45.14 O
ATOM 1267 N TRP B 94 133.043 146.532 183.233 1.00 47.79 N
ATOM 1268 CA TRP B 94 132.819 147.751 184.048 1.00 48.98 C
ATOM 1269 C TRP B 94 131.978 147.353 185.261 1.00 51.00 C
ATOM 1270 O TRP B 94 131.056 146.528 185.098 1.00 51.61 O
ATOM 1271 CB TRP B 94 132.082 148.811 183.222 1.00 48.33 C
ATOM 1272 CG TRP B 94 132.838 149.311 182.021 1.00 47.19 C
ATOM 1273 CD1 TRP B 94 133.850 150.223 182.010 1.00 46.72 C
ATOM 1274 CD2 TRP B 94 132.620 148.935 180.645 1.00 49.22 C
ATOM 1275 NE1 TRP B 94 134.282 150.437 180.729 1.00 49.07 N
ATOM 1276 CE2 TRP B 94 133.548 149.662 179.870 1.00 48.37 C
ATOM 1277 CE3 TRP B 94 131.741 148.061 179.997 1.00 49.66 C
ATOM 1278 CZ2 TRP B 94 133.620 149.539 178.485 1.00 47.57 C
ATOM 1279 CZ3 TRP B 94 131.813 147.941 178.627 1.00 48.70 C
ATOM 1280 CH2 TRP B 94 132.739 148.671 177.884 1.00 47.74 C
ATOM 1281 N PRO B 95 132.239 147.890 186.472 1.00 48.97 N
ATOM 1282 CA PRO B 95 133.465 148.627 186.731 1.00 47.34 C
ATOM 1283 C PRO B 95 134.615 147.704 187.094 1.00 48.55 C
ATOM 1284 O PRO B 95 134.443 146.838 187.974 1.00 48.40 O
ATOM 1285 CB PRO B 95 133.026 149.492 187.913 1.00 47.06 C
ATOM 1286 CG PRO B 95 132.103 148.586 188.694 1.00 49.01 C
ATOM 1287 CD PRO B 95 131.359 147.802 187.627 1.00 48.79 C
ATOM 1288 N LEU B 96 135.760 147.872 186.429 1.00 37.96 N
ATOM 1289 CA LEU B 96 136.955 147.062 186.772 1.00 32.11 C
ATOM 1290 C LEU B 96 137.048 146.986 188.301 1.00 33.35 C
ATOM 1291 O LEU B 96 137.275 148.040 188.927 1.00 36.61 O
ATOM 1292 CB LEU B 96 138.178 147.719 186.138 1.00 33.31 C
ATOM 1293 CG LEU B 96 138.206 147.739 184.605 1.00 33.38 C
ATOM 1294 CD1 LEU B 96 139.383 148.538 184.071 1.00 31.92 C
ATOM 1295 CD2 LEU B 96 138.215 146.334 184.033 1.00 36.20 C
ATOM 1296 N THR B 97 136.883 145.795 188.881 1.00 28.50 N
ATOM 1297 CA THR B 97 136.836 145.682 190.358 1.00 31.36 C
ATOM 1298 C THR B 97 138.216 145.550 190.961 1.00 28.20 C
ATOM 1299 O THR B 97 139.192 145.434 190.190 1.00 28.82 O
ATOM 1300 CB THR B 97 135.957 144.490 190.730 1.00 32.00 C
ATOM 1301 N PHE B 98 138.296 145.570 192.297 1.00 15.34 N
ATOM 1302 CA PHE B 98 139.563 145.418 192.993 1.00 12.35 C
ATOM 1303 C PHE B 98 139.406 144.383 194.095 1.00 11.60 C
ATOM 1304 O PHE B 98 138.302 144.119 194.576 1.00 15.06 O
ATOM 1305 CB PHE B 98 140.045 146.742 193.602 1.00 14.50 C
ATOM 1306 CG PHE B 98 140.764 147.638 192.635 1.00 16.42 C
ATOM 1307 CD1 PHE B 98 140.134 148.101 191.494 1.00 17.09 C
ATOM 1308 CD2 PHE B 98 142.069 148.027 192.877 1.00 12.23 C
ATOM 1309 CE1 PHE B 98 140.795 148.927 190.609 1.00 11.76 C
ATOM 1310 CE2 PHE B 98 142.733 148.853 191.997 1.00 12.26 C
ATOM 1311 CZ PHE B 98 142.094 149.305 190.863 1.00 10.20 C
ATOM 1312 N GLY B 99 140.525 143.796 194.494 1.00 21.74 N
ATOM 1313 CA GLY B 99 140.511 142.840 195.578 1.00 27.05 C
ATOM 1314 C GLY B 99 140.591 143.502 196.939 1.00 30.41 C
ATOM 1315 O GLY B 99 140.781 144.710 197.070 1.00 32.29 O
ATOM 1316 N THR B 100 140.441 142.677 197.978 1.00 60.97 N
ATOM 1317 CA THR B 100 140.549 143.188 199.340 1.00 63.30 C
ATOM 1318 C THR B 100 141.975 143.608 199.670 1.00 61.06 C
ATOM 1319 O THR B 100 142.179 144.542 200.452 1.00 60.66 O
ATOM 1320 CB THR B 100 140.063 142.141 200.343 1.00 62.82 C
TER 1321 THR B 100
TER 4509 ILE C 644
TER 7726 ILE D 644
TER 8617 VAL E 117
TER 9312 LEU F 106
TER 10193 SER G 119
TER 10889 VAL H 108
CONECT 9410962
CONECT 114 633
CONECT 633 114
CONECT 4386 7608
CONECT 7608 4386
CONECT 7867 8430
CONECT 8430 7867
CONECT 8744 9185
CONECT 9185 8744
CONECT 9445 9998
CONECT 973710929
CONECT 9998 9445
CONECT1031510755
CONECT1075510315
CONECT108901089110901
CONECT10891108901089210898
CONECT10892108911089310899
CONECT10893108921089410900
CONECT10894108931089510901
CONECT108951089410902
CONECT10896108971089810903
CONECT1089710896
CONECT108981089110896
CONECT1089910892
CONECT109001089310904
CONECT109011089010894
CONECT1090210895
CONECT1090310896
CONECT10904109001090510915
CONECT10905109041090610912
CONECT10906109051090710913
CONECT10907109061090810914
CONECT10908109071090910915
CONECT109091090810916
CONECT10910109111091210917
CONECT1091110910
CONECT109121090510910
CONECT1091310906
CONECT109141090710918
CONECT109151090410908
CONECT1091610909
CONECT1091710910
CONECT10918109141091910927
CONECT10919109181092010924
CONECT10920109191092110925
CONECT10921109201092210926
CONECT10922109211092310927
CONECT109231092210928
CONECT1092410919
CONECT1092510920
CONECT1092610921
CONECT109271091810922
CONECT1092810923
CONECT10929 97371093010940
CONECT10930109291093110937
CONECT10931109301093210938
CONECT10932109311093310939
CONECT10933109321093410940
CONECT109341093310941
CONECT10935109361093710942
CONECT1093610935
CONECT109371093010935
CONECT1093810931
CONECT109391093210943
CONECT109401092910933
CONECT1094110934
CONECT1094210935
CONECT10943109391094410953
CONECT10944109431094510951
CONECT109451094410946
CONECT10946109451094710952
CONECT10947109461094810953
CONECT109481094710954
CONECT10949109501095110955
CONECT1095010949
CONECT109511094410949
CONECT109521094610956
CONECT109531094310947
CONECT1095410948
CONECT1095510949
CONECT10956109521095710961
CONECT109571095610958
CONECT109581095710959
CONECT109591095810960
CONECT109601095910961
CONECT109611095610960
CONECT10962 941096310973
CONECT10963109621096410970
CONECT10964109631096510971
CONECT10965109641096610972
CONECT10966109651096710973
CONECT109671096610974
CONECT10968109691097010975
CONECT1096910968
CONECT109701096310968
CONECT1097110964
CONECT1097210965
CONECT109731096210966
CONECT1097410967
CONECT1097510968
MASTER 1131 0 7 7 90 0 0 6 7813 8 100 141
END