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casp_data / casp16 /experiment_structures /H1233s1.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 MOL_ID: 1;
COMPND 2 MOLECULE: HASTV1 NEUTRALIZING FAB 3B4 HEAVY CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 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
ATOM 1 N VAL A 2 153.844 161.691 180.434 1.00 62.83 N
ATOM 2 CA VAL A 2 154.846 160.860 181.167 1.00 62.98 C
ATOM 3 C VAL A 2 154.485 160.852 182.660 1.00 63.38 C
ATOM 4 O VAL A 2 154.704 159.808 183.311 1.00 64.92 O
ATOM 5 CB VAL A 2 156.281 161.376 180.951 1.00 62.83 C
ATOM 6 N GLN A 3 153.965 161.969 183.177 1.00 52.84 N
ATOM 7 CA GLN A 3 153.649 162.061 184.626 1.00 52.25 C
ATOM 8 C GLN A 3 152.306 162.779 184.822 1.00 52.13 C
ATOM 9 O GLN A 3 152.102 163.827 184.177 1.00 52.97 O
ATOM 10 CB GLN A 3 154.765 162.807 185.358 1.00 30.00 C
ATOM 11 CG GLN A 3 154.926 164.262 184.930 1.00 30.00 C
ATOM 12 CD GLN A 3 156.035 164.982 185.665 1.00 30.00 C
ATOM 13 OE1 GLN A 3 156.941 164.364 186.234 1.00 30.00 O
ATOM 14 NE2 GLN A 3 155.973 166.306 185.658 1.00 30.00 N
ATOM 15 N LEU A 4 151.441 162.239 185.686 1.00 37.26 N
ATOM 16 CA LEU A 4 150.139 162.892 185.985 1.00 37.46 C
ATOM 17 C LEU A 4 150.315 163.778 187.226 1.00 40.22 C
ATOM 18 O LEU A 4 150.741 163.249 188.275 1.00 40.82 O
ATOM 19 CB LEU A 4 149.051 161.841 186.201 1.00 33.73 C
ATOM 20 CG LEU A 4 148.554 161.118 184.945 1.00 34.65 C
ATOM 21 CD1 LEU A 4 148.528 159.616 185.148 1.00 34.21 C
ATOM 22 CD2 LEU A 4 147.184 161.621 184.534 1.00 32.93 C
ATOM 23 N HIS A 5 150.016 165.073 187.102 1.00 67.55 N
ATOM 24 CA HIS A 5 150.141 166.009 188.252 1.00 67.57 C
ATOM 25 C HIS A 5 148.740 166.352 188.766 1.00 67.87 C
ATOM 26 O HIS A 5 147.773 166.237 187.987 1.00 68.58 O
ATOM 27 CB HIS A 5 150.928 167.258 187.841 1.00 70.34 C
ATOM 28 N GLN A 6 148.637 166.777 190.028 1.00 41.49 N
ATOM 29 CA GLN A 6 147.309 167.077 190.625 1.00 41.08 C
ATOM 30 C GLN A 6 147.167 168.587 190.843 1.00 40.91 C
ATOM 31 O GLN A 6 148.047 169.180 191.502 1.00 39.33 O
ATOM 32 CB GLN A 6 147.156 166.394 191.982 1.00 41.86 C
ATOM 33 N PRO A 7 146.097 169.230 190.331 1.00 70.86 N
ATOM 34 CA PRO A 7 145.880 170.650 190.564 1.00 72.95 C
ATOM 35 C PRO A 7 145.192 170.946 191.888 1.00 72.99 C
ATOM 36 O PRO A 7 144.009 171.341 191.875 1.00 72.97 O
ATOM 37 CB PRO A 7 145.001 171.025 189.354 1.00 73.00 C
ATOM 38 CG PRO A 7 145.125 169.836 188.425 1.00 72.87 C
ATOM 39 CD PRO A 7 145.161 168.669 189.391 1.00 70.54 C
ATOM 40 N GLY A 8 145.904 170.758 193.004 1.00 66.15 N
ATOM 41 CA GLY A 8 145.362 171.126 194.329 1.00 66.75 C
ATOM 42 C GLY A 8 144.643 169.987 195.024 1.00 66.31 C
ATOM 43 O GLY A 8 144.167 169.073 194.319 1.00 66.66 O
ATOM 44 N ALA A 9 144.567 170.036 196.359 1.00 53.85 N
ATOM 45 CA ALA A 9 143.812 169.019 197.132 1.00 56.25 C
ATOM 46 C ALA A 9 142.324 169.111 196.788 1.00 56.88 C
ATOM 47 O ALA A 9 141.663 168.058 196.684 1.00 55.61 O
ATOM 48 CB ALA A 9 144.053 169.211 198.613 1.00 54.81 C
ATOM 49 N GLU A 10 141.810 170.336 196.642 1.00 56.36 N
ATOM 50 CA GLU A 10 140.366 170.537 196.347 1.00 56.36 C
ATOM 51 C GLU A 10 139.535 169.610 197.250 1.00 56.36 C
ATOM 52 O GLU A 10 139.650 169.765 198.486 1.00 56.36 O
ATOM 53 CB GLU A 10 140.077 170.283 194.867 1.00 56.36 C
ATOM 54 CG GLU A 10 139.553 171.514 194.135 1.00 56.36 C
ATOM 55 CD GLU A 10 139.333 171.299 192.649 1.00 56.36 C
ATOM 56 OE1 GLU A 10 140.237 170.745 191.991 1.00 56.36 O
ATOM 57 OE2 GLU A 10 138.256 171.687 192.151 1.00 56.36 O
ATOM 58 N PRO A 14 129.383 171.277 201.182 1.00 75.64 N
ATOM 59 CA PRO A 14 128.689 170.171 200.535 1.00 75.28 C
ATOM 60 C PRO A 14 127.646 170.682 199.555 1.00 75.40 C
ATOM 61 O PRO A 14 127.151 171.813 199.731 1.00 76.42 O
ATOM 62 CB PRO A 14 128.058 169.400 201.704 1.00 75.50 C
ATOM 63 CG PRO A 14 128.991 169.677 202.854 1.00 74.93 C
ATOM 64 CD PRO A 14 129.380 171.128 202.632 1.00 74.86 C
ATOM 65 N GLY A 15 127.320 169.874 198.542 1.00 66.46 N
ATOM 66 CA GLY A 15 126.300 170.265 197.550 1.00 65.69 C
ATOM 67 C GLY A 15 126.901 171.147 196.475 1.00 65.07 C
ATOM 68 O GLY A 15 126.209 171.407 195.469 1.00 64.91 O
ATOM 69 N ALA A 16 128.146 171.586 196.673 1.00 63.37 N
ATOM 70 CA ALA A 16 128.830 172.437 195.672 1.00 63.85 C
ATOM 71 C ALA A 16 129.633 171.548 194.722 1.00 64.16 C
ATOM 72 O ALA A 16 130.562 170.850 195.182 1.00 65.60 O
ATOM 73 CB ALA A 16 129.715 173.447 196.368 1.00 63.08 C
ATOM 74 N SER A 17 129.282 171.571 193.434 1.00 67.02 N
ATOM 75 CA SER A 17 129.999 170.739 192.436 1.00 66.56 C
ATOM 76 C SER A 17 131.498 171.063 192.486 1.00 68.17 C
ATOM 77 O SER A 17 131.848 172.257 192.367 1.00 69.99 O
ATOM 78 CB SER A 17 129.437 170.946 191.057 1.00 67.03 C
ATOM 79 OG SER A 17 128.094 170.488 190.985 1.00 67.07 O
ATOM 80 N VAL A 18 132.331 170.064 192.772 1.00 55.31 N
ATOM 81 CA VAL A 18 133.798 170.310 192.888 1.00 55.79 C
ATOM 82 C VAL A 18 134.498 169.386 191.885 1.00 54.71 C
ATOM 83 O VAL A 18 134.519 168.161 192.128 1.00 53.36 O
ATOM 84 CB VAL A 18 134.335 170.086 194.316 1.00 55.86 C
ATOM 85 CG1 VAL A 18 135.857 170.144 194.364 1.00 56.26 C
ATOM 86 CG2 VAL A 18 133.738 171.075 195.308 1.00 54.79 C
ATOM 87 N ASN A 19 135.032 169.946 190.798 1.00 44.50 N
ATOM 88 CA ASN A 19 135.793 169.068 189.877 1.00 42.03 C
ATOM 89 C ASN A 19 137.013 168.538 190.623 1.00 42.34 C
ATOM 90 O ASN A 19 137.628 169.314 191.364 1.00 43.54 O
ATOM 91 CB ASN A 19 136.336 169.800 188.658 1.00 42.67 C
ATOM 92 CG ASN A 19 135.277 170.332 187.725 1.00 41.90 C
ATOM 93 OD1 ASN A 19 134.080 170.290 188.031 1.00 43.92 O
ATOM 94 ND2 ASN A 19 135.720 170.843 186.586 1.00 41.20 N
ATOM 95 N LEU A 20 137.351 167.264 190.447 1.00 34.91 N
ATOM 96 CA LEU A 20 138.616 166.750 191.026 1.00 36.40 C
ATOM 97 C LEU A 20 139.489 166.559 189.792 1.00 36.83 C
ATOM 98 O LEU A 20 139.058 165.812 188.890 1.00 37.22 O
ATOM 99 CB LEU A 20 138.388 165.454 191.797 1.00 35.66 C
ATOM 100 CG LEU A 20 138.017 165.610 193.275 1.00 35.16 C
ATOM 101 CD1 LEU A 20 137.165 166.833 193.548 1.00 33.07 C
ATOM 102 CD2 LEU A 20 137.303 164.368 193.755 1.00 34.65 C
ATOM 103 N SER A 21 140.633 167.240 189.713 1.00 64.41 N
ATOM 104 CA SER A 21 141.338 167.142 188.407 1.00 67.40 C
ATOM 105 C SER A 21 142.715 166.477 188.520 1.00 67.92 C
ATOM 106 O SER A 21 143.191 166.296 189.662 1.00 67.23 O
ATOM 107 CB SER A 21 141.468 168.509 187.783 1.00 66.96 C
ATOM 108 OG SER A 21 142.163 169.392 188.652 1.00 68.05 O
ATOM 109 N CYS A 22 143.307 166.106 187.378 1.00 50.28 N
ATOM 110 CA CYS A 22 144.685 165.542 187.351 1.00 46.79 C
ATOM 111 C CYS A 22 145.237 165.768 185.931 1.00 47.56 C
ATOM 112 O CYS A 22 144.605 165.285 184.969 1.00 46.46 O
ATOM 113 CB CYS A 22 144.705 164.085 187.800 1.00 43.76 C
ATOM 114 SG CYS A 22 144.301 162.903 186.490 1.00 53.00 S
ATOM 115 N LYS A 23 146.340 166.511 185.799 1.00 41.50 N
ATOM 116 CA LYS A 23 146.866 166.849 184.449 1.00 40.33 C
ATOM 117 C LYS A 23 148.164 166.078 184.171 1.00 41.17 C
ATOM 118 O LYS A 23 149.129 166.252 184.942 1.00 41.52 O
ATOM 119 CB LYS A 23 147.125 168.355 184.337 1.00 39.35 C
ATOM 120 CG LYS A 23 147.757 168.787 183.022 1.00 39.08 C
ATOM 121 CD LYS A 23 147.997 170.289 182.934 1.00 39.87 C
ATOM 122 CE LYS A 23 148.573 170.692 181.615 1.00 39.40 C
ATOM 123 NZ LYS A 23 148.801 172.137 181.545 1.00 40.05 N
ATOM 124 N ALA A 24 148.186 165.278 183.100 1.00 55.55 N
ATOM 125 CA ALA A 24 149.402 164.518 182.728 1.00 56.96 C
ATOM 126 C ALA A 24 150.216 165.341 181.729 1.00 58.21 C
ATOM 127 O ALA A 24 149.611 165.930 180.806 1.00 56.23 O
ATOM 128 CB ALA A 24 149.017 163.171 182.159 1.00 54.29 C
ATOM 129 N SER A 25 151.540 165.385 181.907 1.00 66.58 N
ATOM 130 CA SER A 25 152.405 166.207 181.020 1.00 66.05 C
ATOM 131 C SER A 25 153.518 165.336 180.423 1.00 63.58 C
ATOM 132 O SER A 25 153.704 164.201 180.910 1.00 61.73 O
ATOM 133 CB SER A 25 152.975 167.387 181.763 1.00 67.00 C
ATOM 134 N GLY A 26 154.227 165.851 179.414 1.00 55.15 N
ATOM 135 CA GLY A 26 155.277 165.060 178.744 1.00 57.42 C
ATOM 136 C GLY A 26 154.685 163.796 178.154 1.00 58.21 C
ATOM 137 O GLY A 26 155.360 162.747 178.203 1.00 57.48 O
ATOM 138 N TYR A 27 153.470 163.890 177.607 1.00 63.43 N
ATOM 139 CA TYR A 27 152.777 162.686 177.078 1.00 61.88 C
ATOM 140 C TYR A 27 152.922 162.623 175.566 1.00 61.62 C
ATOM 141 O TYR A 27 152.746 163.656 174.887 1.00 62.70 O
ATOM 142 CB TYR A 27 151.304 162.743 177.491 1.00 62.58 C
ATOM 143 CG TYR A 27 150.536 163.959 176.991 1.00 61.74 C
ATOM 144 CD1 TYR A 27 149.875 163.937 175.770 1.00 61.65 C
ATOM 145 CD2 TYR A 27 150.467 165.123 177.746 1.00 62.93 C
ATOM 146 CE1 TYR A 27 149.176 165.040 175.310 1.00 63.74 C
ATOM 147 CE2 TYR A 27 149.769 166.231 177.298 1.00 62.80 C
ATOM 148 CZ TYR A 27 149.122 166.189 176.077 1.00 64.00 C
ATOM 149 OH TYR A 27 148.432 167.277 175.629 1.00 65.92 O
ATOM 150 N THR A 28 153.253 161.441 175.045 1.00 37.07 N
ATOM 151 CA THR A 28 153.333 161.260 173.604 1.00 35.35 C
ATOM 152 C THR A 28 152.110 160.589 172.999 1.00 36.52 C
ATOM 153 O THR A 28 151.769 160.898 171.854 1.00 37.91 O
ATOM 154 CB THR A 28 154.577 160.436 173.232 1.00 34.01 C
ATOM 155 OG1 THR A 28 154.620 160.245 171.813 1.00 32.64 O
ATOM 156 CG2 THR A 28 154.546 159.081 173.919 1.00 34.16 C
ATOM 157 N PHE A 29 151.445 159.694 173.725 1.00 34.53 N
ATOM 158 CA PHE A 29 150.249 159.010 173.251 1.00 29.94 C
ATOM 159 C PHE A 29 149.035 159.577 173.973 1.00 32.01 C
ATOM 160 O PHE A 29 148.991 159.586 175.206 1.00 36.45 O
ATOM 161 CB PHE A 29 150.351 157.504 173.492 1.00 28.69 C
ATOM 162 CG PHE A 29 151.352 156.816 172.611 1.00 31.65 C
ATOM 163 CD1 PHE A 29 151.384 157.063 171.251 1.00 32.35 C
ATOM 164 CD2 PHE A 29 152.267 155.926 173.144 1.00 35.13 C
ATOM 165 CE1 PHE A 29 152.307 156.432 170.440 1.00 36.12 C
ATOM 166 CE2 PHE A 29 153.191 155.294 172.339 1.00 33.84 C
ATOM 167 CZ PHE A 29 153.211 155.547 170.986 1.00 34.43 C
ATOM 168 N THR A 30 148.051 160.045 173.207 1.00 35.09 N
ATOM 169 CA THR A 30 146.899 160.707 173.810 1.00 33.38 C
ATOM 170 C THR A 30 145.853 159.705 174.288 1.00 33.63 C
ATOM 171 O THR A 30 145.558 159.622 175.484 1.00 34.13 O
ATOM 172 CB THR A 30 146.274 161.687 172.814 1.00 36.92 C
ATOM 173 OG1 THR A 30 145.612 160.956 171.775 1.00 32.77 O
ATOM 174 CG2 THR A 30 147.342 162.569 172.196 1.00 36.83 C
ATOM 175 N SER A 31 145.296 158.923 173.365 1.00 21.59 N
ATOM 176 CA SER A 31 144.097 158.126 173.627 1.00 21.46 C
ATOM 177 C SER A 31 144.475 156.849 174.364 1.00 21.42 C
ATOM 178 O SER A 31 144.829 155.844 173.745 1.00 23.63 O
ATOM 179 CB SER A 31 143.379 157.805 172.322 1.00 20.80 C
ATOM 180 OG SER A 31 144.285 157.289 171.366 1.00 22.42 O
ATOM 181 N TYR A 32 144.386 156.880 175.699 1.00 31.46 N
ATOM 182 CA TYR A 32 144.609 155.669 176.480 1.00 30.72 C
ATOM 183 C TYR A 32 143.655 155.538 177.665 1.00 34.78 C
ATOM 184 O TYR A 32 143.992 154.863 178.645 1.00 37.37 O
ATOM 185 CB TYR A 32 146.055 155.594 176.965 1.00 31.87 C
ATOM 186 CG TYR A 32 146.942 154.789 176.046 1.00 34.72 C
ATOM 187 CD1 TYR A 32 146.641 153.470 175.747 1.00 33.75 C
ATOM 188 CD2 TYR A 32 148.071 155.348 175.471 1.00 35.78 C
ATOM 189 CE1 TYR A 32 147.442 152.731 174.905 1.00 32.18 C
ATOM 190 CE2 TYR A 32 148.877 154.617 174.628 1.00 32.46 C
ATOM 191 CZ TYR A 32 148.558 153.309 174.349 1.00 30.19 C
ATOM 192 OH TYR A 32 149.359 152.576 173.509 1.00 33.93 O
ATOM 193 N TRP A 33 142.476 156.157 177.605 1.00 25.28 N
ATOM 194 CA TRP A 33 141.428 155.903 178.589 1.00 25.78 C
ATOM 195 C TRP A 33 141.856 156.200 180.020 1.00 23.55 C
ATOM 196 O TRP A 33 141.980 155.281 180.835 1.00 23.70 O
ATOM 197 CB TRP A 33 140.950 154.451 178.492 1.00 29.43 C
ATOM 198 CG TRP A 33 140.105 154.189 177.292 1.00 26.48 C
ATOM 199 CD1 TRP A 33 140.534 153.857 176.043 1.00 21.22 C
ATOM 200 CD2 TRP A 33 138.680 154.266 177.221 1.00 26.25 C
ATOM 201 NE1 TRP A 33 139.462 153.709 175.199 1.00 18.95 N
ATOM 202 CE2 TRP A 33 138.311 153.956 175.899 1.00 24.40 C
ATOM 203 CE3 TRP A 33 137.677 154.562 178.149 1.00 22.74 C
ATOM 204 CZ2 TRP A 33 136.984 153.934 175.481 1.00 27.04 C
ATOM 205 CZ3 TRP A 33 136.362 154.540 177.733 1.00 27.05 C
ATOM 206 CH2 TRP A 33 136.026 154.228 176.411 1.00 27.09 C
ATOM 207 N MET A 34 142.089 157.470 180.336 1.00 31.92 N
ATOM 208 CA MET A 34 142.396 157.848 181.709 1.00 30.95 C
ATOM 209 C MET A 34 141.299 157.358 182.646 1.00 31.28 C
ATOM 210 O MET A 34 140.116 157.628 182.426 1.00 36.37 O
ATOM 211 CB MET A 34 142.551 159.363 181.813 1.00 30.74 C
ATOM 212 CG MET A 34 143.165 159.838 183.116 1.00 32.50 C
ATOM 213 SD MET A 34 143.611 161.581 183.048 1.00 37.56 S
ATOM 214 CE MET A 34 143.585 161.859 181.281 1.00 35.01 C
ATOM 215 N HIS A 35 141.697 156.636 183.688 1.00 19.88 N
ATOM 216 CA HIS A 35 140.760 156.081 184.656 1.00 21.08 C
ATOM 217 C HIS A 35 140.428 157.135 185.707 1.00 21.69 C
ATOM 218 O HIS A 35 140.717 158.323 185.548 1.00 30.41 O
ATOM 219 CB HIS A 35 141.339 154.820 185.290 1.00 20.92 C
ATOM 220 CG HIS A 35 141.461 153.668 184.344 1.00 22.11 C
ATOM 221 ND1 HIS A 35 140.661 152.550 184.425 1.00 21.53 N
ATOM 222 CD2 HIS A 35 142.288 153.463 183.291 1.00 21.45 C
ATOM 223 CE1 HIS A 35 140.990 151.704 183.466 1.00 21.47 C
ATOM 224 NE2 HIS A 35 141.974 152.234 182.763 1.00 22.14 N
ATOM 225 N TRP A 36 139.800 156.707 186.798 1.00 26.29 N
ATOM 226 CA TRP A 36 139.548 157.590 187.927 1.00 28.95 C
ATOM 227 C TRP A 36 139.155 156.756 189.138 1.00 28.36 C
ATOM 228 O TRP A 36 138.292 155.881 189.040 1.00 40.39 O
ATOM 229 CB TRP A 36 138.465 158.612 187.582 1.00 34.49 C
ATOM 230 CG TRP A 36 138.997 160.002 187.361 1.00 37.42 C
ATOM 231 CD1 TRP A 36 139.077 160.670 186.173 1.00 35.60 C
ATOM 232 CD2 TRP A 36 139.522 160.892 188.355 1.00 38.67 C
ATOM 233 NE1 TRP A 36 139.618 161.917 186.367 1.00 37.68 N
ATOM 234 CE2 TRP A 36 139.899 162.077 187.698 1.00 36.50 C
ATOM 235 CE3 TRP A 36 139.705 160.802 189.738 1.00 37.09 C
ATOM 236 CZ2 TRP A 36 140.451 163.159 188.373 1.00 34.83 C
ATOM 237 CZ3 TRP A 36 140.254 161.875 190.406 1.00 31.40 C
ATOM 238 CH2 TRP A 36 140.619 163.039 189.724 1.00 34.50 C
ATOM 239 N VAL A 37 139.782 157.014 190.279 1.00 27.28 N
ATOM 240 CA VAL A 37 139.650 156.165 191.454 1.00 30.42 C
ATOM 241 C VAL A 37 139.311 157.013 192.670 1.00 36.34 C
ATOM 242 O VAL A 37 139.685 158.185 192.758 1.00 45.67 O
ATOM 243 CB VAL A 37 140.942 155.360 191.700 1.00 31.72 C
ATOM 244 CG1 VAL A 37 141.045 154.952 193.152 1.00 34.29 C
ATOM 245 CG2 VAL A 37 140.984 154.142 190.797 1.00 34.55 C
ATOM 246 N LYS A 38 138.594 156.408 193.614 1.00 33.62 N
ATOM 247 CA LYS A 38 138.316 157.023 194.903 1.00 31.45 C
ATOM 248 C LYS A 38 138.640 156.023 196.002 1.00 32.98 C
ATOM 249 O LYS A 38 138.173 154.881 195.961 1.00 39.84 O
ATOM 250 CB LYS A 38 136.855 157.471 195.004 1.00 33.69 C
ATOM 251 CG LYS A 38 136.225 157.228 196.365 1.00 37.54 C
ATOM 252 CD LYS A 38 134.885 157.931 196.481 1.00 37.63 C
ATOM 253 CE LYS A 38 134.226 157.640 197.814 1.00 37.76 C
ATOM 254 NZ LYS A 38 133.546 156.319 197.804 1.00 40.41 N
ATOM 255 N GLN A 39 139.433 156.452 196.982 1.00 31.77 N
ATOM 256 CA GLN A 39 139.878 155.585 198.074 1.00 33.56 C
ATOM 257 C GLN A 39 139.617 156.285 199.405 1.00 39.09 C
ATOM 258 O GLN A 39 140.320 157.235 199.761 1.00 42.63 O
ATOM 259 CB GLN A 39 141.353 155.231 197.922 1.00 35.57 C
ATOM 260 CG GLN A 39 141.863 154.242 198.958 1.00 38.02 C
ATOM 261 CD GLN A 39 143.377 154.201 199.027 1.00 39.28 C
ATOM 262 OE1 GLN A 39 143.973 154.557 200.043 1.00 42.39 O
ATOM 263 NE2 GLN A 39 144.007 153.767 197.942 1.00 35.23 N
ATOM 264 N ARG A 40 138.616 155.811 200.140 1.00 79.60 N
ATOM 265 CA ARG A 40 138.355 156.345 201.465 1.00 80.76 C
ATOM 266 C ARG A 40 139.453 155.911 202.434 1.00 81.94 C
ATOM 267 O ARG A 40 140.066 154.855 202.260 1.00 81.84 O
ATOM 268 CB ARG A 40 136.998 155.876 201.980 1.00 81.93 C
ATOM 269 N GLY A 44 140.139 150.522 200.625 1.00 79.88 N
ATOM 270 CA GLY A 44 140.299 149.905 199.322 1.00 79.14 C
ATOM 271 C GLY A 44 139.928 150.826 198.177 1.00 77.29 C
ATOM 272 O GLY A 44 139.268 151.845 198.376 1.00 78.66 O
ATOM 273 N LEU A 45 140.355 150.467 196.971 1.00 21.88 N
ATOM 274 CA LEU A 45 140.065 151.273 195.798 1.00 23.65 C
ATOM 275 C LEU A 45 138.651 151.008 195.297 1.00 24.87 C
ATOM 276 O LEU A 45 138.103 149.915 195.465 1.00 26.31 O
ATOM 277 CB LEU A 45 141.071 150.986 194.685 1.00 22.29 C
ATOM 278 CG LEU A 45 141.037 151.950 193.498 1.00 21.38 C
ATOM 279 CD1 LEU A 45 142.424 152.131 192.906 1.00 18.51 C
ATOM 280 CD2 LEU A 45 140.057 151.482 192.439 1.00 18.42 C
ATOM 281 N GLU A 46 138.065 152.026 194.672 1.00 52.17 N
ATOM 282 CA GLU A 46 136.722 151.935 194.111 1.00 53.89 C
ATOM 283 C GLU A 46 136.702 152.685 192.790 1.00 52.83 C
ATOM 284 O GLU A 46 136.945 153.894 192.762 1.00 59.13 O
ATOM 285 CB GLU A 46 135.680 152.514 195.073 1.00 54.19 C
ATOM 286 N TRP A 47 136.408 151.978 191.704 1.00 31.95 N
ATOM 287 CA TRP A 47 136.400 152.614 190.396 1.00 31.44 C
ATOM 288 C TRP A 47 135.324 153.690 190.340 1.00 34.82 C
ATOM 289 O TRP A 47 134.319 153.633 191.052 1.00 37.62 O
ATOM 290 CB TRP A 47 136.165 151.577 189.302 1.00 33.08 C
ATOM 291 CG TRP A 47 136.729 151.974 187.987 1.00 30.35 C
ATOM 292 CD1 TRP A 47 138.018 152.308 187.723 1.00 36.76 C
ATOM 293 CD2 TRP A 47 136.022 152.085 186.749 1.00 30.29 C
ATOM 294 NE1 TRP A 47 138.165 152.619 186.395 1.00 36.86 N
ATOM 295 CE2 TRP A 47 136.951 152.490 185.775 1.00 32.42 C
ATOM 296 CE3 TRP A 47 134.696 151.878 186.368 1.00 38.32 C
ATOM 297 CZ2 TRP A 47 136.597 152.695 184.448 1.00 34.48 C
ATOM 298 CZ3 TRP A 47 134.346 152.082 185.049 1.00 39.97 C
ATOM 299 CH2 TRP A 47 135.292 152.486 184.105 1.00 37.52 C
ATOM 300 N ILE A 48 135.580 154.744 189.569 1.00 31.99 N
ATOM 301 CA ILE A 48 134.564 155.827 189.425 1.00 34.03 C
ATOM 302 C ILE A 48 134.125 155.834 187.960 1.00 34.38 C
ATOM 303 O ILE A 48 132.902 155.799 187.695 1.00 37.93 O
ATOM 304 CB ILE A 48 135.148 157.189 189.835 1.00 34.31 C
ATOM 305 CG1 ILE A 48 135.711 157.161 191.251 1.00 35.49 C
ATOM 306 CG2 ILE A 48 134.113 158.301 189.664 1.00 34.59 C
ATOM 307 CD1 ILE A 48 136.334 158.476 191.675 1.00 30.93 C
ATOM 308 N GLY A 49 135.104 155.861 187.058 1.00 30.06 N
ATOM 309 CA GLY A 49 134.799 155.880 185.620 1.00 29.15 C
ATOM 310 C GLY A 49 136.063 156.085 184.822 1.00 31.15 C
ATOM 311 O GLY A 49 137.133 156.270 185.439 1.00 40.02 O
ATOM 312 N GLU A 50 135.952 156.041 183.498 1.00 29.53 N
ATOM 313 CA GLU A 50 137.094 156.242 182.622 1.00 33.67 C
ATOM 314 C GLU A 50 136.695 157.091 181.426 1.00 33.97 C
ATOM 315 O GLU A 50 135.606 156.926 180.870 1.00 36.67 O
ATOM 316 CB GLU A 50 137.664 154.905 182.144 1.00 36.33 C
ATOM 317 CG GLU A 50 136.633 153.961 181.558 1.00 37.61 C
ATOM 318 CD GLU A 50 137.232 152.630 181.160 1.00 38.46 C
ATOM 319 OE1 GLU A 50 138.340 152.313 181.638 1.00 38.25 O
ATOM 320 OE2 GLU A 50 136.595 151.899 180.375 1.00 41.08 O
ATOM 321 N ILE A 51 137.583 157.999 181.037 1.00 24.52 N
ATOM 322 CA ILE A 51 137.376 158.866 179.887 1.00 24.43 C
ATOM 323 C ILE A 51 138.585 158.758 178.974 1.00 23.40 C
ATOM 324 O ILE A 51 139.730 158.846 179.431 1.00 31.60 O
ATOM 325 CB ILE A 51 137.148 160.333 180.304 1.00 22.86 C
ATOM 326 CG1 ILE A 51 137.296 161.251 179.092 1.00 21.77 C
ATOM 327 CG2 ILE A 51 138.119 160.735 181.399 1.00 16.92 C
ATOM 328 CD1 ILE A 51 136.793 162.650 179.327 1.00 27.20 C
ATOM 329 N ASN A 52 138.326 158.587 177.678 1.00 49.15 N
ATOM 330 CA ASN A 52 139.447 158.604 176.705 1.00 51.46 C
ATOM 331 C ASN A 52 139.902 160.058 176.602 1.00 53.65 C
ATOM 332 O ASN A 52 139.021 160.937 176.521 1.00 57.15 O
ATOM 333 CB ASN A 52 139.012 158.071 175.347 1.00 54.20 C
ATOM 334 N PRO A 53 141.214 160.366 176.591 1.00 30.06 N
ATOM 335 CA PRO A 53 141.658 161.738 176.419 1.00 26.34 C
ATOM 336 C PRO A 53 141.153 162.196 175.065 1.00 29.26 C
ATOM 337 O PRO A 53 140.752 163.367 174.933 1.00 33.03 O
ATOM 338 CB PRO A 53 143.173 161.621 176.494 1.00 25.08 C
ATOM 339 CG PRO A 53 143.440 160.237 175.953 1.00 25.78 C
ATOM 340 CD PRO A 53 142.284 159.416 176.500 1.00 27.79 C
ATOM 341 N SER A 54 141.170 161.301 174.076 1.00 24.06 N
ATOM 342 CA SER A 54 140.639 161.639 172.730 1.00 22.75 C
ATOM 343 C SER A 54 139.206 161.089 172.698 1.00 26.75 C
ATOM 344 O SER A 54 138.953 160.108 173.428 1.00 29.67 O
ATOM 345 CB SER A 54 141.587 161.213 171.646 1.00 27.27 C
ATOM 346 OG SER A 54 141.084 161.573 170.367 1.00 28.79 O
ATOM 347 N SER A 55 138.317 161.708 171.911 1.00 30.95 N
ATOM 348 CA SER A 55 136.891 161.286 171.770 1.00 30.53 C
ATOM 349 C SER A 55 135.963 161.628 172.944 1.00 30.56 C
ATOM 350 O SER A 55 134.731 161.542 172.751 1.00 29.23 O
ATOM 351 CB SER A 55 136.848 159.812 171.443 1.00 28.11 C
ATOM 352 N GLY A 56 136.510 162.002 174.102 1.00 41.02 N
ATOM 353 CA GLY A 56 135.663 162.469 175.219 1.00 42.18 C
ATOM 354 C GLY A 56 134.600 161.453 175.590 1.00 46.31 C
ATOM 355 O GLY A 56 133.468 161.884 175.890 1.00 46.35 O
ATOM 356 N ARG A 57 134.927 160.158 175.586 1.00 80.74 N
ATOM 357 CA ARG A 57 133.897 159.117 175.850 1.00 81.06 C
ATOM 358 C ARG A 57 134.134 158.535 177.249 1.00 81.34 C
ATOM 359 O ARG A 57 135.303 158.232 177.568 1.00 82.71 O
ATOM 360 CB ARG A 57 133.947 158.019 174.783 1.00 81.96 C
ATOM 361 N ALA A 58 133.076 158.388 178.050 1.00 47.26 N
ATOM 362 CA ALA A 58 133.284 157.914 179.409 1.00 44.96 C
ATOM 363 C ALA A 58 132.365 156.734 179.684 1.00 46.35 C
ATOM 364 O ALA A 58 131.297 156.606 179.080 1.00 50.05 O
ATOM 365 CB ALA A 58 133.035 159.022 180.439 1.00 42.80 C
ATOM 366 N ASN A 59 132.793 155.869 180.601 1.00 35.66 N
ATOM 367 CA ASN A 59 132.012 154.711 181.036 1.00 34.65 C
ATOM 368 C ASN A 59 132.036 154.682 182.560 1.00 35.46 C
ATOM 369 O ASN A 59 132.903 154.040 183.160 1.00 37.25 O
ATOM 370 CB ASN A 59 132.565 153.412 180.458 1.00 33.11 C
ATOM 371 CG ASN A 59 132.896 153.519 178.984 1.00 35.18 C
ATOM 372 OD1 ASN A 59 132.323 154.335 178.263 1.00 37.09 O
ATOM 373 ND2 ASN A 59 133.828 152.691 178.528 1.00 34.82 N
ATOM 374 N TYR A 60 131.076 155.357 183.184 1.00 41.90 N
ATOM 375 CA TYR A 60 131.047 155.499 184.633 1.00 42.56 C
ATOM 376 C TYR A 60 130.524 154.219 185.267 1.00 41.48 C
ATOM 377 O TYR A 60 129.550 153.633 184.784 1.00 41.37 O
ATOM 378 CB TYR A 60 130.168 156.678 185.060 1.00 41.46 C
ATOM 379 CG TYR A 60 130.662 158.042 184.632 1.00 41.53 C
ATOM 380 CD1 TYR A 60 131.562 158.755 185.412 1.00 45.00 C
ATOM 381 CD2 TYR A 60 130.242 158.609 183.439 1.00 41.78 C
ATOM 382 CE1 TYR A 60 132.018 159.996 185.025 1.00 44.48 C
ATOM 383 CE2 TYR A 60 130.694 159.851 183.042 1.00 43.07 C
ATOM 384 CZ TYR A 60 131.583 160.539 183.840 1.00 44.08 C
ATOM 385 OH TYR A 60 132.040 161.778 183.454 1.00 45.39 O
ATOM 386 N ASN A 61 131.174 153.785 186.341 1.00 35.74 N
ATOM 387 CA ASN A 61 130.588 152.752 187.182 1.00 36.06 C
ATOM 388 C ASN A 61 129.255 153.259 187.708 1.00 42.52 C
ATOM 389 O ASN A 61 129.189 154.328 188.322 1.00 47.81 O
ATOM 390 CB ASN A 61 131.533 152.404 188.330 1.00 34.87 C
ATOM 391 CG ASN A 61 130.899 151.481 189.349 1.00 37.89 C
ATOM 392 OD1 ASN A 61 129.830 150.921 189.117 1.00 42.97 O
ATOM 393 ND2 ASN A 61 131.563 151.312 190.484 1.00 37.24 N
ATOM 394 N GLU A 62 128.188 152.496 187.464 1.00 53.20 N
ATOM 395 CA GLU A 62 126.847 153.016 187.715 1.00 52.51 C
ATOM 396 C GLU A 62 126.666 153.457 189.160 1.00 51.97 C
ATOM 397 O GLU A 62 125.868 154.359 189.435 1.00 51.64 O
ATOM 398 CB GLU A 62 125.798 151.973 187.335 1.00 54.25 C
ATOM 399 CG GLU A 62 125.300 152.125 185.911 1.00 55.22 C
ATOM 400 CD GLU A 62 125.388 153.559 185.425 1.00 54.80 C
ATOM 401 OE1 GLU A 62 124.872 154.456 186.122 1.00 55.34 O
ATOM 402 OE2 GLU A 62 125.974 153.790 184.347 1.00 53.76 O
ATOM 403 N LYS A 63 127.396 152.847 190.095 1.00 52.17 N
ATOM 404 CA LYS A 63 127.336 153.312 191.475 1.00 52.84 C
ATOM 405 C LYS A 63 127.774 154.765 191.587 1.00 55.10 C
ATOM 406 O LYS A 63 127.362 155.470 192.515 1.00 56.47 O
ATOM 407 CB LYS A 63 128.199 152.421 192.369 1.00 52.73 C
ATOM 408 CG LYS A 63 128.708 153.109 193.623 1.00 54.07 C
ATOM 409 CD LYS A 63 129.396 152.124 194.550 1.00 54.61 C
ATOM 410 CE LYS A 63 128.452 151.007 194.961 1.00 54.72 C
ATOM 411 NZ LYS A 63 128.994 150.210 196.095 1.00 55.37 N
ATOM 412 N PHE A 64 128.598 155.232 190.649 1.00 55.15 N
ATOM 413 CA PHE A 64 129.111 156.595 190.644 1.00 53.81 C
ATOM 414 C PHE A 64 128.617 157.389 189.439 1.00 53.34 C
ATOM 415 O PHE A 64 129.354 158.209 188.888 1.00 55.00 O
ATOM 416 CB PHE A 64 130.637 156.595 190.681 1.00 52.96 C
ATOM 417 CG PHE A 64 131.207 156.330 192.039 1.00 54.32 C
ATOM 418 CD1 PHE A 64 131.356 157.356 192.952 1.00 54.45 C
ATOM 419 CD2 PHE A 64 131.592 155.052 192.406 1.00 54.94 C
ATOM 420 CE1 PHE A 64 131.881 157.115 194.205 1.00 54.15 C
ATOM 421 CE2 PHE A 64 132.116 154.804 193.657 1.00 54.90 C
ATOM 422 CZ PHE A 64 132.261 155.836 194.558 1.00 54.93 C
ATOM 423 N LYS A 65 127.385 157.146 189.007 1.00 48.77 N
ATOM 424 CA LYS A 65 126.773 157.938 187.952 1.00 50.40 C
ATOM 425 C LYS A 65 125.709 158.852 188.546 1.00 53.30 C
ATOM 426 O LYS A 65 125.088 158.533 189.563 1.00 53.33 O
ATOM 427 CB LYS A 65 126.161 157.048 186.870 1.00 52.01 C
ATOM 428 CG LYS A 65 125.842 157.794 185.586 1.00 51.81 C
ATOM 429 CD LYS A 65 125.505 156.840 184.455 1.00 50.45 C
ATOM 430 CE LYS A 65 125.286 157.592 183.154 1.00 50.32 C
ATOM 431 NZ LYS A 65 124.991 156.669 182.025 1.00 51.29 N
ATOM 432 N ASN A 66 125.509 160.000 187.901 1.00 74.09 N
ATOM 433 CA ASN A 66 124.700 161.106 188.399 1.00 75.12 C
ATOM 434 C ASN A 66 125.407 161.854 189.520 1.00 74.18 C
ATOM 435 O ASN A 66 124.895 162.879 189.986 1.00 74.27 O
ATOM 436 CB ASN A 66 123.318 160.654 188.893 1.00 75.55 C
ATOM 437 N LYS A 67 126.564 161.375 189.969 1.00 54.63 N
ATOM 438 CA LYS A 67 127.366 162.033 190.988 1.00 53.58 C
ATOM 439 C LYS A 67 128.733 162.469 190.491 1.00 53.06 C
ATOM 440 O LYS A 67 129.308 163.400 191.057 1.00 54.63 O
ATOM 441 CB LYS A 67 127.552 161.107 192.199 1.00 54.60 C
ATOM 442 CG LYS A 67 128.443 161.673 193.287 1.00 55.40 C
ATOM 443 CD LYS A 67 129.187 160.565 194.013 1.00 56.33 C
ATOM 444 CE LYS A 67 128.991 160.664 195.516 1.00 55.94 C
ATOM 445 NZ LYS A 67 130.036 159.911 196.261 1.00 55.11 N
ATOM 446 N ALA A 68 129.266 161.826 189.456 1.00 24.38 N
ATOM 447 CA ALA A 68 130.556 162.177 188.885 1.00 19.33 C
ATOM 448 C ALA A 68 130.410 162.370 187.384 1.00 20.67 C
ATOM 449 O ALA A 68 129.743 161.580 186.710 1.00 28.74 O
ATOM 450 CB ALA A 68 131.605 161.099 189.175 1.00 15.46 C
ATOM 451 N THR A 69 131.036 163.421 186.864 1.00 53.77 N
ATOM 452 CA THR A 69 131.004 163.719 185.435 1.00 56.57 C
ATOM 453 C THR A 69 132.418 164.070 184.998 1.00 60.12 C
ATOM 454 O THR A 69 132.946 165.119 185.379 1.00 60.00 O
ATOM 455 CB THR A 69 130.037 164.859 185.125 1.00 59.06 C
ATOM 456 OG1 THR A 69 128.771 164.589 185.738 1.00 61.86 O
ATOM 457 CG2 THR A 69 129.846 164.997 183.622 1.00 58.46 C
ATOM 458 N LEU A 70 133.023 163.200 184.195 1.00 47.19 N
ATOM 459 CA LEU A 70 134.414 163.336 183.789 1.00 43.15 C
ATOM 460 C LEU A 70 134.496 163.954 182.400 1.00 42.87 C
ATOM 461 O LEU A 70 133.814 163.505 181.473 1.00 43.52 O
ATOM 462 CB LEU A 70 135.107 161.975 183.805 1.00 41.64 C
ATOM 463 CG LEU A 70 134.604 161.041 184.903 1.00 41.35 C
ATOM 464 CD1 LEU A 70 135.247 159.680 184.783 1.00 44.63 C
ATOM 465 CD2 LEU A 70 134.879 161.640 186.268 1.00 39.69 C
ATOM 466 N THR A 71 135.331 164.982 182.263 1.00 32.53 N
ATOM 467 CA THR A 71 135.533 165.646 180.978 1.00 33.22 C
ATOM 468 C THR A 71 136.978 166.118 180.918 1.00 33.01 C
ATOM 469 O THR A 71 137.372 167.001 181.684 1.00 31.21 O
ATOM 470 CB THR A 71 134.571 166.818 180.801 1.00 36.77 C
ATOM 471 N VAL A 72 137.758 165.535 180.018 1.00 44.22 N
ATOM 472 CA VAL A 72 139.159 165.899 179.846 1.00 44.27 C
ATOM 473 C VAL A 72 139.266 166.985 178.788 1.00 48.57 C
ATOM 474 O VAL A 72 138.505 167.017 177.816 1.00 50.15 O
ATOM 475 CB VAL A 72 140.011 164.671 179.472 1.00 42.85 C
ATOM 476 CG1 VAL A 72 139.618 163.478 180.321 1.00 44.95 C
ATOM 477 CG2 VAL A 72 139.856 164.357 177.996 1.00 42.64 C
ATOM 478 N ASP A 73 140.228 167.884 178.977 1.00 65.67 N
ATOM 479 CA ASP A 73 140.429 168.972 178.035 1.00 65.90 C
ATOM 480 C ASP A 73 140.994 168.442 176.720 1.00 66.11 C
ATOM 481 O ASP A 73 141.612 167.376 176.659 1.00 65.32 O
ATOM 482 CB ASP A 73 141.363 170.027 178.625 1.00 66.15 C
ATOM 483 CG ASP A 73 141.042 171.424 178.140 1.00 67.62 C
ATOM 484 OD1 ASP A 73 141.105 171.659 176.915 1.00 67.61 O
ATOM 485 OD2 ASP A 73 140.724 172.288 178.983 1.00 67.63 O
ATOM 486 N LYS A 74 140.816 169.213 175.644 1.00 66.07 N
ATOM 487 CA LYS A 74 141.249 168.721 174.308 1.00 66.94 C
ATOM 488 C LYS A 74 142.676 169.185 173.971 1.00 67.15 C
ATOM 489 O LYS A 74 143.505 168.311 173.635 1.00 67.45 O
ATOM 490 CB LYS A 74 140.264 169.203 173.236 1.00 65.88 C
ATOM 491 N SER A 75 142.963 170.488 174.064 1.00 42.67 N
ATOM 492 CA SER A 75 144.292 170.999 173.628 1.00 40.08 C
ATOM 493 C SER A 75 145.415 170.381 174.470 1.00 40.58 C
ATOM 494 O SER A 75 146.449 170.001 173.881 1.00 41.27 O
ATOM 495 CB SER A 75 144.332 172.502 173.696 1.00 40.13 C
ATOM 496 N SER A 76 145.219 170.273 175.783 1.00 53.03 N
ATOM 497 CA SER A 76 146.217 169.607 176.659 1.00 54.96 C
ATOM 498 C SER A 76 145.458 168.595 177.519 1.00 56.83 C
ATOM 499 O SER A 76 144.381 168.958 178.036 1.00 56.81 O
ATOM 500 CB SER A 76 146.968 170.594 177.506 1.00 54.03 C
ATOM 501 OG SER A 76 147.708 169.924 178.516 1.00 53.66 O
ATOM 502 N ILE A 77 145.980 167.379 177.669 1.00 62.89 N
ATOM 503 CA ILE A 77 145.158 166.367 178.396 1.00 62.23 C
ATOM 504 C ILE A 77 145.118 166.733 179.887 1.00 61.47 C
ATOM 505 O ILE A 77 146.192 167.052 180.443 1.00 62.36 O
ATOM 506 CB ILE A 77 145.726 164.955 178.164 1.00 61.12 C
ATOM 507 CG1 ILE A 77 145.864 164.641 176.674 1.00 60.63 C
ATOM 508 CG2 ILE A 77 144.888 163.901 178.885 1.00 60.58 C
ATOM 509 CD1 ILE A 77 144.628 164.964 175.853 1.00 58.92 C
ATOM 510 N THR A 78 143.932 166.669 180.502 1.00 47.92 N
ATOM 511 CA THR A 78 143.772 166.951 181.948 1.00 45.95 C
ATOM 512 C THR A 78 142.393 166.481 182.351 1.00 46.02 C
ATOM 513 O THR A 78 141.418 166.906 181.700 1.00 48.79 O
ATOM 514 CB THR A 78 143.990 168.430 182.265 1.00 48.05 C
ATOM 515 OG1 THR A 78 143.012 169.108 181.484 1.00 49.28 O
ATOM 516 CG2 THR A 78 145.377 168.924 181.900 1.00 48.22 C
ATOM 517 N ALA A 79 142.298 165.637 183.379 1.00 53.51 N
ATOM 518 CA ALA A 79 141.021 165.057 183.763 1.00 56.09 C
ATOM 519 C ALA A 79 140.247 166.011 184.663 1.00 56.50 C
ATOM 520 O ALA A 79 140.809 166.645 185.559 1.00 59.79 O
ATOM 521 CB ALA A 79 141.223 163.719 184.475 1.00 55.51 C
ATOM 522 N TYR A 80 138.943 166.109 184.411 1.00 30.51 N
ATOM 523 CA TYR A 80 138.057 166.980 185.184 1.00 29.64 C
ATOM 524 C TYR A 80 136.868 166.143 185.644 1.00 30.64 C
ATOM 525 O TYR A 80 135.898 165.972 184.900 1.00 29.33 O
ATOM 526 CB TYR A 80 137.606 168.181 184.363 1.00 31.04 C
ATOM 527 CG TYR A 80 138.702 169.183 184.083 1.00 31.80 C
ATOM 528 CD1 TYR A 80 139.813 169.275 184.909 1.00 29.58 C
ATOM 529 CD2 TYR A 80 138.627 170.036 182.990 1.00 31.19 C
ATOM 530 CE1 TYR A 80 140.816 170.187 184.656 1.00 29.22 C
ATOM 531 CE2 TYR A 80 139.626 170.951 182.729 1.00 31.61 C
ATOM 532 CZ TYR A 80 140.718 171.022 183.566 1.00 31.28 C
ATOM 533 OH TYR A 80 141.716 171.933 183.311 1.00 30.35 O
ATOM 534 N MET A 81 136.946 165.624 186.867 1.00 33.55 N
ATOM 535 CA MET A 81 135.872 164.813 187.439 1.00 34.40 C
ATOM 536 C MET A 81 134.899 165.756 188.134 1.00 38.03 C
ATOM 537 O MET A 81 135.051 166.088 189.309 1.00 38.68 O
ATOM 538 CB MET A 81 136.432 163.769 188.396 1.00 33.55 C
ATOM 539 CG MET A 81 135.374 163.006 189.166 1.00 34.26 C
ATOM 540 SD MET A 81 136.063 161.687 190.177 1.00 30.92 S
ATOM 541 CE MET A 81 135.319 162.060 191.759 1.00 31.23 C
ATOM 542 N HIS A 82 133.875 166.185 187.397 1.00 58.16 N
ATOM 543 CA HIS A 82 132.927 167.165 187.910 1.00 56.90 C
ATOM 544 C HIS A 82 131.999 166.540 188.944 1.00 53.85 C
ATOM 545 O HIS A 82 130.829 166.272 188.658 1.00 55.41 O
ATOM 546 CB HIS A 82 132.116 167.774 186.764 1.00 57.39 C
ATOM 547 CG HIS A 82 131.101 168.780 187.210 1.00 60.29 C
ATOM 548 ND1 HIS A 82 131.430 169.885 187.966 1.00 60.02 N
ATOM 549 CD2 HIS A 82 129.765 168.851 187.004 1.00 60.07 C
ATOM 550 CE1 HIS A 82 130.341 170.591 188.208 1.00 59.47 C
ATOM 551 NE2 HIS A 82 129.316 169.986 187.635 1.00 61.08 N
ATOM 552 N LEU A 83 132.514 166.307 190.147 1.00 36.05 N
ATOM 553 CA LEU A 83 131.685 165.774 191.217 1.00 41.19 C
ATOM 554 C LEU A 83 130.555 166.744 191.543 1.00 46.75 C
ATOM 555 O LEU A 83 130.711 167.966 191.461 1.00 49.44 O
ATOM 556 CB LEU A 83 132.533 165.506 192.461 1.00 40.99 C
ATOM 557 CG LEU A 83 132.798 164.041 192.810 1.00 39.07 C
ATOM 558 CD1 LEU A 83 133.736 163.930 193.996 1.00 38.51 C
ATOM 559 CD2 LEU A 83 131.494 163.328 193.101 1.00 42.62 C
ATOM 560 N SER A 84 129.400 166.188 191.900 1.00 60.65 N
ATOM 561 CA SER A 84 128.226 166.985 192.222 1.00 59.93 C
ATOM 562 C SER A 84 127.571 166.443 193.483 1.00 59.28 C
ATOM 563 O SER A 84 127.642 165.246 193.774 1.00 59.72 O
ATOM 564 CB SER A 84 127.215 166.990 191.069 1.00 60.69 C
ATOM 565 OG SER A 84 127.837 167.351 189.849 1.00 60.12 O
ATOM 566 N SER A 85 126.926 167.340 194.227 1.00 65.34 N
ATOM 567 CA SER A 85 126.189 166.979 195.436 1.00 66.38 C
ATOM 568 C SER A 85 127.051 166.143 196.379 1.00 67.12 C
ATOM 569 O SER A 85 126.677 165.048 196.802 1.00 67.96 O
ATOM 570 CB SER A 85 124.893 166.249 195.083 1.00 66.54 C
ATOM 571 N LEU A 86 128.225 166.675 196.708 1.00 58.15 N
ATOM 572 CA LEU A 86 129.140 165.967 197.592 1.00 57.44 C
ATOM 573 C LEU A 86 128.480 165.699 198.938 1.00 56.67 C
ATOM 574 O LEU A 86 127.743 166.534 199.466 1.00 56.73 O
ATOM 575 CB LEU A 86 130.426 166.771 197.788 1.00 56.59 C
ATOM 576 N THR A 87 128.746 164.521 199.489 1.00 67.13 N
ATOM 577 CA THR A 87 128.170 164.090 200.754 1.00 67.48 C
ATOM 578 C THR A 87 129.287 163.860 201.772 1.00 67.22 C
ATOM 579 O THR A 87 130.459 164.146 201.518 1.00 68.06 O
ATOM 580 CB THR A 87 127.323 162.832 200.556 1.00 69.36 C
ATOM 581 N SER A 88 128.909 163.340 202.934 1.00 64.74 N
ATOM 582 CA SER A 88 129.866 163.074 204.001 1.00 65.07 C
ATOM 583 C SER A 88 130.932 162.083 203.552 1.00 65.42 C
ATOM 584 O SER A 88 131.820 161.722 204.323 1.00 65.88 O
ATOM 585 CB SER A 88 129.149 162.544 205.244 1.00 64.65 C
ATOM 586 OG SER A 88 128.852 161.165 205.110 1.00 65.40 O
ATOM 587 N SER A 91 134.286 159.666 201.872 1.00 55.05 N
ATOM 588 CA SER A 91 135.305 160.640 202.347 1.00 54.14 C
ATOM 589 C SER A 91 136.105 161.190 201.158 1.00 54.86 C
ATOM 590 O SER A 91 135.470 161.624 200.172 1.00 57.39 O
ATOM 591 CB SER A 91 136.216 160.018 203.376 1.00 54.67 C
ATOM 592 N ALA A 92 137.437 161.186 201.255 1.00 48.63 N
ATOM 593 CA ALA A 92 138.298 161.751 200.185 1.00 49.12 C
ATOM 594 C ALA A 92 138.210 160.949 198.885 1.00 50.99 C
ATOM 595 O ALA A 92 138.142 159.703 198.953 1.00 53.56 O
ATOM 596 CB ALA A 92 139.727 161.823 200.678 1.00 47.77 C
ATOM 597 N VAL A 93 138.232 161.636 197.737 1.00 34.15 N
ATOM 598 CA VAL A 93 138.277 160.932 196.423 1.00 29.17 C
ATOM 599 C VAL A 93 139.500 161.218 195.547 1.00 26.20 C
ATOM 600 O VAL A 93 139.426 162.183 194.759 1.00 33.35 O
ATOM 601 CB VAL A 93 137.120 161.425 195.542 1.00 26.37 C
ATOM 602 CG1 VAL A 93 137.206 160.849 194.137 1.00 27.07 C
ATOM 603 CG2 VAL A 93 135.757 161.175 196.172 1.00 28.85 C
ATOM 604 N TYR A 94 140.536 160.375 195.584 1.00 29.07 N
ATOM 605 CA TYR A 94 141.710 160.760 194.758 1.00 29.38 C
ATOM 606 C TYR A 94 142.781 160.735 193.661 1.00 34.15 C
ATOM 607 O TYR A 94 143.208 161.835 193.256 1.00 37.89 O
ATOM 608 CB TYR A 94 142.510 161.145 196.007 1.00 32.26 C
ATOM 609 CG TYR A 94 142.672 160.128 197.127 1.00 35.21 C
ATOM 610 CD1 TYR A 94 142.201 160.399 198.405 1.00 33.38 C
ATOM 611 CD2 TYR A 94 143.336 158.926 196.924 1.00 38.43 C
ATOM 612 CE1 TYR A 94 142.361 159.495 199.440 1.00 33.95 C
ATOM 613 CE2 TYR A 94 143.500 158.011 197.949 1.00 38.38 C
ATOM 614 CZ TYR A 94 143.013 158.297 199.211 1.00 37.79 C
ATOM 615 OH TYR A 94 143.168 157.397 200.226 1.00 40.62 O
ATOM 616 N TYR A 95 143.173 159.539 193.194 1.00 35.98 N
ATOM 617 CA TYR A 95 144.155 159.309 192.085 1.00 33.66 C
ATOM 618 C TYR A 95 143.548 158.953 190.727 1.00 32.81 C
ATOM 619 O TYR A 95 142.401 158.468 190.684 1.00 38.44 O
ATOM 620 CB TYR A 95 144.401 157.866 192.546 1.00 24.45 C
ATOM 621 CG TYR A 95 145.229 157.701 193.812 1.00 28.16 C
ATOM 622 CD1 TYR A 95 146.249 158.589 194.126 1.00 32.95 C
ATOM 623 CD2 TYR A 95 144.990 156.651 194.689 1.00 30.89 C
ATOM 624 CE1 TYR A 95 147.005 158.441 195.276 1.00 34.33 C
ATOM 625 CE2 TYR A 95 145.740 156.491 195.842 1.00 33.49 C
ATOM 626 CZ TYR A 95 146.750 157.388 196.136 1.00 36.55 C
ATOM 627 OH TYR A 95 147.492 157.236 197.271 1.00 38.45 O
ATOM 628 N CYS A 96 144.303 159.182 189.649 1.00 24.14 N
ATOM 629 CA CYS A 96 143.876 158.787 188.280 1.00 23.09 C
ATOM 630 C CYS A 96 144.907 158.090 187.374 1.00 31.67 C
ATOM 631 O CYS A 96 146.039 158.608 187.298 1.00 46.51 O
ATOM 632 CB CYS A 96 143.582 160.111 187.577 1.00 28.83 C
ATOM 633 SG CYS A 96 145.035 161.137 187.226 1.00 46.71 S
ATOM 634 N HIS A 97 144.561 156.973 186.726 1.00 24.77 N
ATOM 635 CA HIS A 97 145.561 156.228 185.908 1.00 24.24 C
ATOM 636 C HIS A 97 145.463 156.307 184.380 1.00 25.39 C
ATOM 637 O HIS A 97 144.563 155.669 183.800 1.00 30.82 O
ATOM 638 CB HIS A 97 145.330 154.779 186.350 1.00 19.58 C
ATOM 639 CG HIS A 97 144.928 154.605 187.772 1.00 19.78 C
ATOM 640 ND1 HIS A 97 145.567 155.226 188.822 1.00 25.24 N
ATOM 641 CD2 HIS A 97 143.955 153.866 188.313 1.00 19.46 C
ATOM 642 CE1 HIS A 97 144.976 154.879 189.955 1.00 27.01 C
ATOM 643 NE2 HIS A 97 144.003 154.045 189.670 1.00 26.23 N
ATOM 644 N TRP A 98 146.369 157.053 183.745 1.00 30.60 N
ATOM 645 CA TRP A 98 146.293 157.217 182.268 1.00 32.19 C
ATOM 646 C TRP A 98 147.304 156.281 181.626 1.00 39.14 C
ATOM 647 O TRP A 98 148.439 156.741 181.389 1.00 41.40 O
ATOM 648 CB TRP A 98 146.591 158.667 181.892 1.00 35.37 C
ATOM 649 CG TRP A 98 146.490 158.961 180.421 1.00 36.44 C
ATOM 650 CD1 TRP A 98 145.696 158.360 179.488 1.00 34.99 C
ATOM 651 CD2 TRP A 98 147.230 159.980 179.722 1.00 36.51 C
ATOM 652 NE1 TRP A 98 145.897 158.930 178.259 1.00 32.68 N
ATOM 653 CE2 TRP A 98 146.830 159.928 178.373 1.00 34.56 C
ATOM 654 CE3 TRP A 98 148.187 160.922 180.108 1.00 35.59 C
ATOM 655 CZ2 TRP A 98 147.356 160.790 177.418 1.00 35.96 C
ATOM 656 CZ3 TRP A 98 148.702 161.774 179.159 1.00 35.96 C
ATOM 657 CH2 TRP A 98 148.287 161.710 177.833 1.00 37.97 C
ATOM 658 N ASP A 99 146.896 155.067 181.258 1.00 70.54 N
ATOM 659 CA ASP A 99 147.847 154.008 180.802 1.00 70.35 C
ATOM 660 C ASP A 99 148.767 154.333 179.617 1.00 69.69 C
ATOM 661 O ASP A 99 148.483 155.291 178.876 1.00 71.61 O
ATOM 662 CB ASP A 99 147.095 152.706 180.565 1.00 71.17 C
ATOM 663 CG ASP A 99 146.362 152.175 181.788 1.00 73.35 C
ATOM 664 OD1 ASP A 99 146.609 152.705 182.892 1.00 71.62 O
ATOM 665 OD2 ASP A 99 145.550 151.242 181.626 1.00 75.06 O
ATOM 666 N TYR A 100 149.827 153.539 179.451 1.00 49.91 N
ATOM 667 CA TYR A 100 150.822 153.632 178.395 1.00 52.56 C
ATOM 668 C TYR A 100 151.356 152.229 178.156 1.00 54.71 C
ATOM 669 O TYR A 100 150.796 151.237 178.635 1.00 54.50 O
ATOM 670 CB TYR A 100 151.923 154.635 178.762 1.00 52.61 C
ATOM 671 CG TYR A 100 151.589 156.058 178.404 1.00 49.03 C
ATOM 672 CD1 TYR A 100 151.720 156.504 177.100 1.00 47.91 C
ATOM 673 CD2 TYR A 100 151.155 156.955 179.363 1.00 50.90 C
ATOM 674 CE1 TYR A 100 151.425 157.795 176.756 1.00 47.49 C
ATOM 675 CE2 TYR A 100 150.857 158.255 179.030 1.00 51.88 C
ATOM 676 CZ TYR A 100 150.994 158.668 177.723 1.00 51.93 C
ATOM 677 OH TYR A 100 150.700 159.964 177.379 1.00 56.67 O
ATOM 678 N TYR A 101 152.274 152.123 177.191 1.00 56.65 N
ATOM 679 CA TYR A 101 152.792 150.774 176.844 1.00 55.18 C
ATOM 680 C TYR A 101 153.166 150.127 178.163 1.00 59.24 C
ATOM 681 O TYR A 101 153.034 148.890 178.286 1.00 56.40 O
ATOM 682 CB TYR A 101 153.957 150.892 175.858 1.00 57.52 C
ATOM 683 CG TYR A 101 153.575 151.248 174.426 1.00 56.16 C
ATOM 684 CD1 TYR A 101 154.541 151.622 173.500 1.00 58.20 C
ATOM 685 CD2 TYR A 101 152.255 151.205 174.000 1.00 53.46 C
ATOM 686 CE1 TYR A 101 154.207 151.945 172.195 1.00 57.72 C
ATOM 687 CE2 TYR A 101 151.910 151.526 172.698 1.00 55.31 C
ATOM 688 CZ TYR A 101 152.885 151.901 171.794 1.00 57.49 C
ATOM 689 OH TYR A 101 152.541 152.214 170.511 1.00 55.70 O
ATOM 690 N ALA A 102 153.588 150.949 179.131 1.00 73.50 N
ATOM 691 CA ALA A 102 153.936 150.452 180.484 1.00 72.35 C
ATOM 692 C ALA A 102 154.444 151.619 181.334 1.00 70.13 C
ATOM 693 O ALA A 102 154.927 152.617 180.755 1.00 70.68 O
ATOM 694 CB ALA A 102 154.977 149.358 180.393 1.00 72.55 C
ATOM 695 N MET A 103 154.330 151.509 182.659 1.00 65.73 N
ATOM 696 CA MET A 103 154.855 152.556 183.579 1.00 67.76 C
ATOM 697 C MET A 103 154.846 154.089 183.697 1.00 71.00 C
ATOM 698 O MET A 103 155.757 154.605 184.379 1.00 70.99 O
ATOM 699 CB MET A 103 156.082 152.372 184.477 1.00 66.92 C
ATOM 700 CG MET A 103 156.101 151.050 185.214 1.00 66.84 C
ATOM 701 SD MET A 103 154.661 150.868 186.285 1.00 66.56 S
ATOM 702 CE MET A 103 154.993 152.148 187.502 1.00 68.10 C
ATOM 703 N ASP A 104 153.846 154.762 183.102 1.00 69.10 N
ATOM 704 CA ASP A 104 153.694 156.248 183.135 1.00 65.58 C
ATOM 705 C ASP A 104 152.432 156.797 183.798 1.00 64.62 C
ATOM 706 O ASP A 104 152.418 158.003 184.119 1.00 66.02 O
ATOM 707 CB ASP A 104 154.144 156.542 181.714 1.00 65.61 C
ATOM 708 N TYR A 105 151.422 155.950 184.024 1.00 51.19 N
ATOM 709 CA TYR A 105 150.149 156.468 184.515 1.00 52.26 C
ATOM 710 C TYR A 105 149.634 156.586 185.954 1.00 51.52 C
ATOM 711 O TYR A 105 148.633 155.984 186.328 1.00 52.25 O
ATOM 712 CB TYR A 105 149.467 155.314 183.784 1.00 55.89 C
ATOM 713 CG TYR A 105 149.896 153.948 184.260 1.00 51.73 C
ATOM 714 CD1 TYR A 105 149.181 153.278 185.240 1.00 51.50 C
ATOM 715 CD2 TYR A 105 151.038 153.345 183.757 1.00 49.80 C
ATOM 716 CE1 TYR A 105 149.574 152.032 185.683 1.00 50.63 C
ATOM 717 CE2 TYR A 105 151.440 152.111 184.196 1.00 51.01 C
ATOM 718 CZ TYR A 105 150.706 151.457 185.157 1.00 51.43 C
ATOM 719 OH TYR A 105 151.117 150.222 185.587 1.00 52.29 O
ATOM 720 N TRP A 106 150.278 157.402 186.789 1.00 51.35 N
ATOM 721 CA TRP A 106 149.710 157.594 188.153 1.00 49.59 C
ATOM 722 C TRP A 106 149.844 159.054 188.588 1.00 50.87 C
ATOM 723 O TRP A 106 150.828 159.708 188.184 1.00 56.92 O
ATOM 724 CB TRP A 106 150.373 156.655 189.171 1.00 53.02 C
ATOM 725 CG TRP A 106 149.730 155.297 189.263 1.00 52.05 C
ATOM 726 CD1 TRP A 106 149.919 154.240 188.423 1.00 53.55 C
ATOM 727 CD2 TRP A 106 148.798 154.846 190.268 1.00 51.25 C
ATOM 728 NE1 TRP A 106 149.162 153.171 188.822 1.00 53.68 N
ATOM 729 CE2 TRP A 106 148.467 153.510 189.952 1.00 51.89 C
ATOM 730 CE3 TRP A 106 148.218 155.436 191.395 1.00 53.02 C
ATOM 731 CZ2 TRP A 106 147.586 152.758 190.724 1.00 49.76 C
ATOM 732 CZ3 TRP A 106 147.350 154.689 192.159 1.00 52.62 C
ATOM 733 CH2 TRP A 106 147.041 153.370 191.828 1.00 46.75 C
ATOM 734 N GLY A 107 148.896 159.540 189.393 1.00 26.45 N
ATOM 735 CA GLY A 107 148.928 160.940 189.858 1.00 29.64 C
ATOM 736 C GLY A 107 148.525 161.047 191.314 1.00 33.13 C
ATOM 737 O GLY A 107 147.802 160.150 191.792 1.00 36.02 O
ATOM 738 N GLN A 108 148.973 162.102 192.000 1.00 62.49 N
ATOM 739 CA GLN A 108 148.668 162.257 193.416 1.00 65.29 C
ATOM 740 C GLN A 108 147.204 162.631 193.594 1.00 62.65 C
ATOM 741 O GLN A 108 146.728 163.607 193.012 1.00 63.57 O
ATOM 742 CB GLN A 108 149.556 163.323 194.061 1.00 64.68 C
ATOM 743 N GLY A 109 146.497 161.856 194.410 1.00 38.99 N
ATOM 744 CA GLY A 109 145.075 162.055 194.596 1.00 40.56 C
ATOM 745 C GLY A 109 144.736 163.397 195.220 1.00 40.66 C
ATOM 746 O GLY A 109 145.403 163.865 196.139 1.00 41.00 O
ATOM 747 N THR A 110 143.674 164.016 194.699 1.00 23.65 N
ATOM 748 CA THR A 110 143.179 165.291 195.218 1.00 18.55 C
ATOM 749 C THR A 110 142.277 165.025 196.423 1.00 18.94 C
ATOM 750 O THR A 110 141.054 165.162 196.374 1.00 20.40 O
ATOM 751 CB THR A 110 142.435 166.065 194.140 1.00 17.16 C
ATOM 752 OG1 THR A 110 141.086 165.590 194.059 1.00 17.21 O
ATOM 753 CG2 THR A 110 143.101 165.887 192.794 1.00 20.31 C
ATOM 754 N SER A 111 142.914 164.633 197.524 1.00 37.89 N
ATOM 755 CA SER A 111 142.190 164.306 198.746 1.00 40.23 C
ATOM 756 C SER A 111 141.190 165.400 199.092 1.00 42.80 C
ATOM 757 O SER A 111 141.568 166.538 199.379 1.00 45.44 O
ATOM 758 CB SER A 111 143.174 164.110 199.900 1.00 43.13 C
ATOM 759 OG SER A 111 142.495 163.730 201.084 1.00 44.78 O
ATOM 760 N VAL A 112 139.902 165.050 199.026 1.00 54.32 N
ATOM 761 CA VAL A 112 138.826 166.046 199.308 1.00 57.50 C
ATOM 762 C VAL A 112 138.304 165.816 200.732 1.00 56.57 C
ATOM 763 O VAL A 112 138.195 164.638 201.130 1.00 57.39 O
ATOM 764 CB VAL A 112 137.679 165.933 198.286 1.00 56.14 C
ATOM 765 CG1 VAL A 112 136.499 166.827 198.646 1.00 55.50 C
ATOM 766 CG2 VAL A 112 138.146 166.217 196.866 1.00 53.60 C
ATOM 767 N THR A 113 138.035 166.893 201.473 1.00 51.55 N
ATOM 768 CA THR A 113 137.430 166.756 202.815 1.00 52.05 C
ATOM 769 C THR A 113 136.104 167.480 202.777 1.00 54.03 C
ATOM 770 O THR A 113 136.079 168.676 203.139 1.00 54.33 O
ATOM 771 CB THR A 113 138.368 167.321 203.879 1.00 52.46 C
ATOM 772 OG1 THR A 113 139.658 166.818 203.549 1.00 53.58 O
ATOM 773 CG2 THR A 113 137.986 166.881 205.281 1.00 51.84 C
TER 774 THR A 113
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
HETATM10962 C1 NAG A 301 134.952 171.424 185.520 1.00 30.00 C
HETATM10963 C2 NAG A 301 135.940 171.942 184.475 1.00 30.00 C
HETATM10964 C3 NAG A 301 135.178 172.603 183.332 1.00 30.00 C
HETATM10965 C4 NAG A 301 134.162 171.627 182.757 1.00 30.00 C
HETATM10966 C5 NAG A 301 133.242 171.127 183.866 1.00 30.00 C
HETATM10967 C6 NAG A 301 132.275 170.072 183.381 1.00 30.00 C
HETATM10968 C7 NAG A 301 137.253 174.047 184.775 1.00 30.00 C
HETATM10969 C8 NAG A 301 138.695 174.253 184.427 1.00 30.00 C
HETATM10970 N2 NAG A 301 136.911 172.804 185.122 1.00 30.00 N
HETATM10971 O3 NAG A 301 136.080 173.033 182.322 1.00 30.00 O
HETATM10972 O4 NAG A 301 133.380 172.293 181.770 1.00 30.00 O
HETATM10973 O5 NAG A 301 134.012 170.536 184.934 1.00 30.00 O
HETATM10974 O6 NAG A 301 131.266 169.808 184.349 1.00 30.00 O
HETATM10975 O7 NAG A 301 136.443 174.969 184.760 1.00 30.00 O
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