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7ra3.pdb
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7ra3.pdb
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HEADER MEMBRANE PROTEIN 29-JUN-21 7RA3
TITLE CRYO-EM OF HUMAN GASTRIC INHIBITORY POLYPEPTIDE RECEPTOR GIPR BOUND TO
TITLE 2 GIP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) SUBUNIT ALPHA-3,
COMPND 3 ISOFORM GNAS-2 OF GUANINE NUCLEOTIDE-BINDING PROTEIN G(S) SUBUNIT
COMPND 4 ALPHA ISOFORMS SHORT;
COMPND 5 CHAIN: A;
COMPND 6 SYNONYM: G(I) ALPHA-3,ADENYLATE CYCLASE-STIMULATING G ALPHA PROTEIN;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT
COMPND 10 BETA-1;
COMPND 11 CHAIN: B;
COMPND 12 SYNONYM: TRANSDUCIN BETA CHAIN 1;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: SINGLE-CHAIN VARIABLE FRAGMENT 16;
COMPND 16 CHAIN: E;
COMPND 17 ENGINEERED: YES;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT
COMPND 20 GAMMA-2;
COMPND 21 CHAIN: G;
COMPND 22 SYNONYM: G GAMMA-I;
COMPND 23 ENGINEERED: YES;
COMPND 24 MOL_ID: 5;
COMPND 25 MOLECULE: NANOBODY 35;
COMPND 26 CHAIN: N;
COMPND 27 ENGINEERED: YES;
COMPND 28 MOL_ID: 6;
COMPND 29 MOLECULE: GASTRIC INHIBITORY POLYPEPTIDE;
COMPND 30 CHAIN: P;
COMPND 31 SYNONYM: GIP,GLUCOSE-DEPENDENT INSULINOTROPIC POLYPEPTIDE,INCRETIN
COMPND 32 HORMONE;
COMPND 33 ENGINEERED: YES;
COMPND 34 MOL_ID: 7;
COMPND 35 MOLECULE: GASTRIC INHIBITORY POLYPEPTIDE RECEPTOR;
COMPND 36 CHAIN: R;
COMPND 37 SYNONYM: GIP-R,GLUCOSE-DEPENDENT INSULINOTROPIC POLYPEPTIDE RECEPTOR;
COMPND 38 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: GNAI3, GNAS, GNAS1, GSP;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: GNB1;
SOURCE 13 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 17 ORGANISM_TAXID: 10090;
SOURCE 18 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 20 MOL_ID: 4;
SOURCE 21 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 22 ORGANISM_COMMON: HUMAN;
SOURCE 23 ORGANISM_TAXID: 9606;
SOURCE 24 GENE: GNG2;
SOURCE 25 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 26 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 27 MOL_ID: 5;
SOURCE 28 ORGANISM_SCIENTIFIC: LAMA GLAMA;
SOURCE 29 ORGANISM_TAXID: 9844;
SOURCE 30 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 31 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 32 MOL_ID: 6;
SOURCE 33 SYNTHETIC: YES;
SOURCE 34 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 35 ORGANISM_COMMON: HUMAN;
SOURCE 36 ORGANISM_TAXID: 9606;
SOURCE 37 MOL_ID: 7;
SOURCE 38 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 39 ORGANISM_COMMON: HUMAN;
SOURCE 40 ORGANISM_TAXID: 9606;
SOURCE 41 GENE: GIPR;
SOURCE 42 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 43 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS CLASS B GPCR, GLUCAGON-LIKE PEPTIDE-1 RECEPTOR, G PROTEIN NUCLEOTIDE
KEYWDS 2 EXCHANGE FACTOR., MEMBRANE PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR B.SUN,B.K.KOBILKA,K.W.SLOOP,D.FENG,T.S.KOBILKA
REVDAT 1 13-APR-22 7RA3 0
JRNL AUTH B.SUN,F.S.WILLARD,D.FENG,J.ALSINA-FERNANDEZ,Q.CHEN,M.VIETH,
JRNL AUTH 2 J.D.HO,A.D.SHOWALTER,C.STUTSMAN,L.DING,T.M.SUTER,J.D.DUNBAR,
JRNL AUTH 3 J.W.CARPENTER,F.A.MOHAMMED,E.AIHARA,R.A.BROWN,A.B.BUENO,
JRNL AUTH 4 P.J.EMMERSON,J.S.MOYERS,T.S.KOBILKA,M.P.COGHLAN,B.K.KOBILKA,
JRNL AUTH 5 K.W.SLOOP
JRNL TITL STRUCTURAL DETERMINANTS OF DUAL INCRETIN RECEPTOR AGONISM BY
JRNL TITL 2 TIRZEPATIDE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 119 06119 2022
JRNL REFN ESSN 1091-6490
JRNL PMID 35333651
JRNL DOI 10.1073/PNAS.2116506119
REMARK 2
REMARK 2 RESOLUTION. 3.24 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : RELION, PHENIX, PHENIX, RELION
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : 6VCB
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.240
REMARK 3 NUMBER OF PARTICLES : 145195
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 7RA3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUN-21.
REMARK 100 THE DEPOSITION ID IS D_1000257859.
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 : CRYO-EM OF HUMAN GASTRIC
REMARK 245 INHIBITORY POLYPEPTIDE RECEPTOR
REMARK 245 GIPR BOUND TO GIP, TRIMERIC G
REMARK 245 PROTEIN COMPLEX AND STABILIZING
REMARK 245 ANTIBODIES; GASTRIC INHIBITORY
REMARK 245 POLYPEPTIDE GIP BOUND TO GIP
REMARK 245 RECEPTOR GIPR; TRIMERIC
REMARK 245 STIMULATORY G PROTEIN
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 10.00
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.50
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : NULL
REMARK 245 MAXIMUM DEFOCUS (NM) : NULL
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 2.70
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5360.00
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: HEPTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, G, N, P, R
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 MET A 8
REMARK 465 GLY A 9
REMARK 465 CYS A 10
REMARK 465 THR A 11
REMARK 465 GLY A 49
REMARK 465 GLU A 50
REMARK 465 MET A 74
REMARK 465 ARG A 75
REMARK 465 ILE A 76
REMARK 465 LEU A 77
REMARK 465 HIS A 78
REMARK 465 VAL A 79
REMARK 465 ASN A 80
REMARK 465 GLY A 81
REMARK 465 PHE A 82
REMARK 465 ASN A 83
REMARK 465 GLY A 84
REMARK 465 ASP A 85
REMARK 465 SER A 86
REMARK 465 GLU A 87
REMARK 465 LYS A 88
REMARK 465 ALA A 89
REMARK 465 THR A 90
REMARK 465 LYS A 91
REMARK 465 VAL A 92
REMARK 465 GLN A 93
REMARK 465 ASP A 94
REMARK 465 ILE A 95
REMARK 465 LYS A 96
REMARK 465 ASN A 97
REMARK 465 ASN A 98
REMARK 465 LEU A 99
REMARK 465 LYS A 100
REMARK 465 GLU A 101
REMARK 465 ALA A 102
REMARK 465 ILE A 103
REMARK 465 GLU A 104
REMARK 465 THR A 105
REMARK 465 ILE A 106
REMARK 465 VAL A 107
REMARK 465 ALA A 108
REMARK 465 ALA A 109
REMARK 465 MET A 110
REMARK 465 SER A 111
REMARK 465 ASN A 112
REMARK 465 LEU A 113
REMARK 465 VAL A 114
REMARK 465 PRO A 115
REMARK 465 PRO A 116
REMARK 465 VAL A 117
REMARK 465 GLU A 118
REMARK 465 LEU A 119
REMARK 465 ALA A 120
REMARK 465 ASN A 121
REMARK 465 PRO A 122
REMARK 465 GLU A 123
REMARK 465 ASN A 124
REMARK 465 GLN A 125
REMARK 465 PHE A 126
REMARK 465 ARG A 127
REMARK 465 VAL A 128
REMARK 465 ASP A 129
REMARK 465 TYR A 130
REMARK 465 ILE A 131
REMARK 465 LEU A 132
REMARK 465 SER A 133
REMARK 465 VAL A 134
REMARK 465 MET A 135
REMARK 465 ASN A 136
REMARK 465 VAL A 137
REMARK 465 PRO A 138
REMARK 465 ASP A 139
REMARK 465 PHE A 140
REMARK 465 ASP A 141
REMARK 465 PHE A 142
REMARK 465 PRO A 143
REMARK 465 PRO A 144
REMARK 465 GLU A 145
REMARK 465 PHE A 146
REMARK 465 TYR A 147
REMARK 465 GLU A 148
REMARK 465 HIS A 149
REMARK 465 ALA A 150
REMARK 465 LYS A 151
REMARK 465 ALA A 152
REMARK 465 LEU A 153
REMARK 465 TRP A 154
REMARK 465 GLU A 155
REMARK 465 ASP A 156
REMARK 465 GLU A 157
REMARK 465 GLY A 158
REMARK 465 VAL A 159
REMARK 465 ARG A 160
REMARK 465 ALA A 161
REMARK 465 CYS A 162
REMARK 465 TYR A 163
REMARK 465 GLU A 164
REMARK 465 ARG A 165
REMARK 465 SER A 166
REMARK 465 ASN A 167
REMARK 465 GLU A 168
REMARK 465 TYR A 169
REMARK 465 GLN A 170
REMARK 465 LEU A 171
REMARK 465 ILE A 172
REMARK 465 ASP A 173
REMARK 465 CYS A 174
REMARK 465 ALA A 175
REMARK 465 GLN A 176
REMARK 465 TYR A 177
REMARK 465 PHE A 178
REMARK 465 LEU A 179
REMARK 465 ASP A 180
REMARK 465 LYS A 181
REMARK 465 ILE A 182
REMARK 465 ASP A 183
REMARK 465 VAL A 184
REMARK 465 ILE A 185
REMARK 465 LYS A 186
REMARK 465 GLN A 187
REMARK 465 ALA A 188
REMARK 465 ASP A 189
REMARK 465 TYR A 190
REMARK 465 VAL A 191
REMARK 465 PRO A 192
REMARK 465 SER A 193
REMARK 465 ASP A 194
REMARK 465 GLN A 195
REMARK 465 ASP A 196
REMARK 465 LEU A 197
REMARK 465 LEU A 198
REMARK 465 ARG A 199
REMARK 465 CYS A 200
REMARK 465 ARG A 201
REMARK 465 VAL A 202
REMARK 465 LEU A 203
REMARK 465 THR A 204
REMARK 465 SER A 205
REMARK 465 GLY A 206
REMARK 465 TYR A 253
REMARK 465 ASN A 254
REMARK 465 MET A 255
REMARK 465 VAL A 256
REMARK 465 ILE A 257
REMARK 465 ARG A 258
REMARK 465 GLU A 259
REMARK 465 ASP A 260
REMARK 465 ASN A 261
REMARK 465 GLN A 262
REMARK 465 LYS A 305
REMARK 465 SER A 306
REMARK 465 ALA A 366
REMARK 465 VAL A 367
REMARK 465 MET B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 SER B 0
REMARK 465 GLY B 1
REMARK 465 MET E -37
REMARK 465 LEU E -36
REMARK 465 LEU E -35
REMARK 465 VAL E -34
REMARK 465 ASN E -33
REMARK 465 GLN E -32
REMARK 465 SER E -31
REMARK 465 HIS E -30
REMARK 465 GLN E -29
REMARK 465 GLY E -28
REMARK 465 PHE E -27
REMARK 465 ASN E -26
REMARK 465 LYS E -25
REMARK 465 GLU E -24
REMARK 465 HIS E -23
REMARK 465 THR E -22
REMARK 465 SER E -21
REMARK 465 LYS E -20
REMARK 465 MET E -19
REMARK 465 VAL E -18
REMARK 465 SER E -17
REMARK 465 ALA E -16
REMARK 465 ILE E -15
REMARK 465 VAL E -14
REMARK 465 LEU E -13
REMARK 465 TYR E -12
REMARK 465 VAL E -11
REMARK 465 LEU E -10
REMARK 465 LEU E -9
REMARK 465 ALA E -8
REMARK 465 ALA E -7
REMARK 465 ALA E -6
REMARK 465 ALA E -5
REMARK 465 HIS E -4
REMARK 465 SER E -3
REMARK 465 ALA E -2
REMARK 465 PHE E -1
REMARK 465 ALA E 0
REMARK 465 ASP E 1
REMARK 465 GLY E 121A
REMARK 465 GLY E 121B
REMARK 465 GLY E 121C
REMARK 465 GLY E 121D
REMARK 465 SER E 121E
REMARK 465 GLY E 121F
REMARK 465 GLY E 121G
REMARK 465 GLY E 121H
REMARK 465 GLY E 121I
REMARK 465 SER E 121J
REMARK 465 GLY E 121K
REMARK 465 GLY E 121L
REMARK 465 GLY E 121M
REMARK 465 GLY E 121N
REMARK 465 LYS E 236
REMARK 465 ALA E 237
REMARK 465 ALA E 238
REMARK 465 ALA E 239
REMARK 465 HIS E 240
REMARK 465 HIS E 241
REMARK 465 HIS E 242
REMARK 465 HIS E 243
REMARK 465 HIS E 244
REMARK 465 HIS E 245
REMARK 465 HIS E 246
REMARK 465 HIS E 247
REMARK 465 MET G 1
REMARK 465 ALA G 2
REMARK 465 SER G 3
REMARK 465 ASN G 4
REMARK 465 LYS G 64
REMARK 465 LYS G 65
REMARK 465 PHE G 66
REMARK 465 PHE G 67
REMARK 465 CYS G 68
REMARK 465 ALA G 69
REMARK 465 ILE G 70
REMARK 465 LEU G 71
REMARK 465 MET N -21
REMARK 465 LYS N -20
REMARK 465 TYR N -19
REMARK 465 LEU N -18
REMARK 465 LEU N -17
REMARK 465 PRO N -16
REMARK 465 THR N -15
REMARK 465 ALA N -14
REMARK 465 ALA N -13
REMARK 465 ALA N -12
REMARK 465 GLY N -11
REMARK 465 LEU N -10
REMARK 465 LEU N -9
REMARK 465 LEU N -8
REMARK 465 LEU N -7
REMARK 465 ALA N -6
REMARK 465 ALA N -5
REMARK 465 GLN N -4
REMARK 465 PRO N -3
REMARK 465 ALA N -2
REMARK 465 MET N -1
REMARK 465 ALA N 0
REMARK 465 HIS N 129
REMARK 465 HIS N 130
REMARK 465 HIS N 131
REMARK 465 HIS N 132
REMARK 465 HIS N 133
REMARK 465 HIS N 134
REMARK 465 GLU N 135
REMARK 465 PRO N 136
REMARK 465 GLU N 137
REMARK 465 ALA N 138
REMARK 465 LYS P 33
REMARK 465 ASN P 34
REMARK 465 ASP P 35
REMARK 465 TRP P 36
REMARK 465 LYS P 37
REMARK 465 HIS P 38
REMARK 465 ASN P 39
REMARK 465 ILE P 40
REMARK 465 THR P 41
REMARK 465 GLN P 42
REMARK 465 ASP R 4
REMARK 465 TYR R 5
REMARK 465 LYS R 6
REMARK 465 ASP R 7
REMARK 465 ASP R 8
REMARK 465 ASP R 9
REMARK 465 ASP R 10
REMARK 465 ALA R 11
REMARK 465 ALA R 12
REMARK 465 ALA R 13
REMARK 465 LEU R 14
REMARK 465 GLU R 15
REMARK 465 VAL R 16
REMARK 465 LEU R 17
REMARK 465 PHE R 18
REMARK 465 GLN R 19
REMARK 465 GLY R 20
REMARK 465 PRO R 21
REMARK 465 ARG R 22
REMARK 465 ALA R 23
REMARK 465 GLU R 24
REMARK 465 THR R 25
REMARK 465 GLY R 26
REMARK 465 SER R 27
REMARK 465 LYS R 28
REMARK 465 LYS R 123
REMARK 465 ASN R 124
REMARK 465 GLU R 125
REMARK 465 ALA R 126
REMARK 465 GLY R 249
REMARK 465 GLY R 250
REMARK 465 SER R 251
REMARK 465 GLN R 329
REMARK 465 MET R 330
REMARK 465 ARG R 331
REMARK 465 CYS R 332
REMARK 465 ARG R 333
REMARK 465 LEU R 412
REMARK 465 ARG R 413
REMARK 465 ARG R 414
REMARK 465 SER R 415
REMARK 465 LEU R 416
REMARK 465 GLY R 417
REMARK 465 GLU R 418
REMARK 465 GLU R 419
REMARK 465 GLN R 420
REMARK 465 ARG R 421
REMARK 465 GLN R 422
REMARK 465 LEU R 423
REMARK 465 PRO R 424
REMARK 465 GLU R 425
REMARK 465 ARG R 426
REMARK 465 ALA R 427
REMARK 465 PHE R 428
REMARK 465 ARG R 429
REMARK 465 ALA R 430
REMARK 465 LEU R 431
REMARK 465 PRO R 432
REMARK 465 SER R 433
REMARK 465 GLY R 434
REMARK 465 SER R 435
REMARK 465 GLY R 436
REMARK 465 PRO R 437
REMARK 465 GLY R 438
REMARK 465 GLU R 439
REMARK 465 VAL R 440
REMARK 465 PRO R 441
REMARK 465 THR R 442
REMARK 465 SER R 443
REMARK 465 ARG R 444
REMARK 465 GLY R 445
REMARK 465 LEU R 446
REMARK 465 SER R 447
REMARK 465 SER R 448
REMARK 465 GLY R 449
REMARK 465 THR R 450
REMARK 465 LEU R 451
REMARK 465 PRO R 452
REMARK 465 GLY R 453
REMARK 465 PRO R 454
REMARK 465 GLY R 455
REMARK 465 ASN R 456
REMARK 465 GLU R 457
REMARK 465 ALA R 458
REMARK 465 SER R 459
REMARK 465 ARG R 460
REMARK 465 GLU R 461
REMARK 465 LEU R 462
REMARK 465 GLU R 463
REMARK 465 SER R 464
REMARK 465 TYR R 465
REMARK 465 CYS R 466
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 LYS A 58 CG CD CE NZ
REMARK 470 GLN A 59 CG CD OE1 NE2
REMARK 470 LYS A 216 CG CD CE NZ
REMARK 470 ASP A 240 CG OD1 OD2
REMARK 470 LYS A 300 CG CD CE NZ
REMARK 470 LYS A 307 CG CD CE NZ
REMARK 470 GLU A 322 CG CD OE1 OE2
REMARK 470 ASP A 354 CG OD1 OD2
REMARK 470 THR A 369 OG1 CG2
REMARK 470 ARG B 42 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 129 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 130 CG CD OE1 OE2
REMARK 470 GLU B 172 CG CD OE1 OE2
REMARK 470 PHE B 234 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER E 17 OG
REMARK 470 GLU E 42 CG CD OE1 OE2
REMARK 470 SER E 52 OG
REMARK 470 ASP E 73 CG OD1 OD2
REMARK 470 GLU E 89 CG CD OE1 OE2
REMARK 470 SER E 121 OG
REMARK 470 SER E 124 OG
REMARK 470 GLU E 141 CG CD OE1 OE2
REMARK 470 ASP E 189 CG OD1 OD2
REMARK 470 ARG E 206 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 210 CG CD OE1 OE2
REMARK 470 GLU E 234 CG CD OE1 OE2
REMARK 470 LYS N 43 CG CD CE NZ
REMARK 470 SER N 112 OG
REMARK 470 THR N 113 OG1 CG2
REMARK 470 GLU R 122 CG CD OE1 OE2
REMARK 470 ARG R 196 CG CD NE CZ NH1 NH2
REMARK 470 LEU R 201 CG CD1 CD2
REMARK 470 ASP R 203 CG OD1 OD2
REMARK 470 GLN R 204 CG CD OE1 NE2
REMARK 470 LEU R 206 CG CD1 CD2
REMARK 470 GLU R 363 CG CD OE1 OE2
REMARK 470 GLN R 364 CG CD OE1 NE2
REMARK 470 ARG R 366 CG CD NE CZ NH1 NH2
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 GLU A 15 16.82 -141.83
REMARK 500 PHE A 238 50.90 -91.79
REMARK 500 ASP A 354 36.53 -98.63
REMARK 500 GLU A 392 63.26 60.23
REMARK 500 LEU B 51 57.77 -96.08
REMARK 500 THR B 87 48.90 36.86
REMARK 500 LYS B 127 38.11 -98.25
REMARK 500 ASP B 163 46.88 -103.03
REMARK 500 LEU B 198 144.51 -173.15
REMARK 500 CYS B 204 36.33 -97.18
REMARK 500 ASP B 258 -5.35 77.11
REMARK 500 SER B 265 149.00 -171.62
REMARK 500 SER B 279 -168.34 -79.28
REMARK 500 PHE B 292 15.24 82.27
REMARK 500 ALA B 309 -167.31 -77.36
REMARK 500 ASN E 77 61.41 61.88
REMARK 500 SER E 99 111.13 -163.17
REMARK 500 LEU E 176 -62.18 -95.02
REMARK 500 MET E 180 -13.31 72.31
REMARK 500 SER E 181 -2.14 -140.37
REMARK 500 GLU E 234 -169.31 -123.03
REMARK 500 PRO G 49 9.98 -65.81
REMARK 500 VAL N 48 -64.11 -99.44
REMARK 500 THR N 113 -11.22 74.77
REMARK 500 THR N 114 53.80 -97.45
REMARK 500 TYR N 117 54.61 -92.36
REMARK 500 MET R 67 -2.47 74.94
REMARK 500 GLN R 204 51.88 -91.23
REMARK 500 THR R 284 -64.87 -94.27
REMARK 500 GLN R 285 -143.86 -163.74
REMARK 500 CYS R 286 0.69 -60.77
REMARK 500 TRP R 287 4.39 82.58
REMARK 500 ASN R 290 42.24 39.81
REMARK 500 TYR R 392 16.60 -140.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-24334 RELATED DB: EMDB
REMARK 900 CRYO-EM OF HUMAN GASTRIC INHIBITORY POLYPEPTIDE RECEPTOR GIPR BOUND
REMARK 900 TO GIP
DBREF 7RA3 A 8 25 UNP P08754 GNAI3_HUMAN 1 18
DBREF 7RA3 A 26 394 UNP P63092 GNAS2_HUMAN 26 380
DBREF 7RA3 B 2 340 UNP P62873 GBB1_HUMAN 2 340
DBREF 7RA3 E -37 247 PDB 7RA3 7RA3 -37 247
DBREF 7RA3 G 1 71 UNP P59768 GBG2_HUMAN 1 71
DBREF 7RA3 N -21 138 PDB 7RA3 7RA3 -21 138
DBREF 7RA3 P 1 42 UNP P09681 GIP_HUMAN 52 93
DBREF 7RA3 R 22 466 UNP P48546 GIPR_HUMAN 22 466
SEQADV 7RA3 MET B -9 UNP P62873 EXPRESSION TAG
SEQADV 7RA3 HIS B -8 UNP P62873 EXPRESSION TAG
SEQADV 7RA3 HIS B -7 UNP P62873 EXPRESSION TAG
SEQADV 7RA3 HIS B -6 UNP P62873 EXPRESSION TAG
SEQADV 7RA3 HIS B -5 UNP P62873 EXPRESSION TAG
SEQADV 7RA3 HIS B -4 UNP P62873 EXPRESSION TAG
SEQADV 7RA3 HIS B -3 UNP P62873 EXPRESSION TAG
SEQADV 7RA3 GLY B -2 UNP P62873 EXPRESSION TAG
SEQADV 7RA3 SER B -1 UNP P62873 EXPRESSION TAG
SEQADV 7RA3 SER B 0 UNP P62873 EXPRESSION TAG
SEQADV 7RA3 GLY B 1 UNP P62873 EXPRESSION TAG
SEQADV 7RA3 ASP R 4 UNP P48546 EXPRESSION TAG
SEQADV 7RA3 TYR R 5 UNP P48546 EXPRESSION TAG
SEQADV 7RA3 LYS R 6 UNP P48546 EXPRESSION TAG
SEQADV 7RA3 ASP R 7 UNP P48546 EXPRESSION TAG
SEQADV 7RA3 ASP R 8 UNP P48546 EXPRESSION TAG
SEQADV 7RA3 ASP R 9 UNP P48546 EXPRESSION TAG
SEQADV 7RA3 ASP R 10 UNP P48546 EXPRESSION TAG
SEQADV 7RA3 ALA R 11 UNP P48546 EXPRESSION TAG
SEQADV 7RA3 ALA R 12 UNP P48546 EXPRESSION TAG
SEQADV 7RA3 ALA R 13 UNP P48546 EXPRESSION TAG
SEQADV 7RA3 LEU R 14 UNP P48546 EXPRESSION TAG
SEQADV 7RA3 GLU R 15 UNP P48546 EXPRESSION TAG
SEQADV 7RA3 VAL R 16 UNP P48546 EXPRESSION TAG
SEQADV 7RA3 LEU R 17 UNP P48546 EXPRESSION TAG
SEQADV 7RA3 PHE R 18 UNP P48546 EXPRESSION TAG
SEQADV 7RA3 GLN R 19 UNP P48546 EXPRESSION TAG
SEQADV 7RA3 GLY R 20 UNP P48546 EXPRESSION TAG
SEQADV 7RA3 PRO R 21 UNP P48546 EXPRESSION TAG
SEQRES 1 A 373 MET GLY CYS THR LEU SER ALA GLU ASP LYS ALA ALA VAL
SEQRES 2 A 373 GLU ARG SER LYS MET ILE GLU LYS GLN LEU GLN LYS ASP
SEQRES 3 A 373 LYS GLN VAL TYR ARG ALA THR HIS ARG LEU LEU LEU LEU
SEQRES 4 A 373 GLY ALA GLY GLU SER GLY LYS SER THR ILE VAL LYS GLN
SEQRES 5 A 373 MET ARG ILE LEU HIS VAL ASN GLY PHE ASN GLY ASP SER
SEQRES 6 A 373 GLU LYS ALA THR LYS VAL GLN ASP ILE LYS ASN ASN LEU
SEQRES 7 A 373 LYS GLU ALA ILE GLU THR ILE VAL ALA ALA MET SER ASN
SEQRES 8 A 373 LEU VAL PRO PRO VAL GLU LEU ALA ASN PRO GLU ASN GLN
SEQRES 9 A 373 PHE ARG VAL ASP TYR ILE LEU SER VAL MET ASN VAL PRO
SEQRES 10 A 373 ASP PHE ASP PHE PRO PRO GLU PHE TYR GLU HIS ALA LYS
SEQRES 11 A 373 ALA LEU TRP GLU ASP GLU GLY VAL ARG ALA CYS TYR GLU
SEQRES 12 A 373 ARG SER ASN GLU TYR GLN LEU ILE ASP CYS ALA GLN TYR
SEQRES 13 A 373 PHE LEU ASP LYS ILE ASP VAL ILE LYS GLN ALA ASP TYR
SEQRES 14 A 373 VAL PRO SER ASP GLN ASP LEU LEU ARG CYS ARG VAL LEU
SEQRES 15 A 373 THR SER GLY ILE PHE GLU THR LYS PHE GLN VAL ASP LYS
SEQRES 16 A 373 VAL ASN PHE HIS MET PHE ASP VAL GLY GLY GLN ARG ASP
SEQRES 17 A 373 GLU ARG ARG LYS TRP ILE GLN CYS PHE ASN ASP VAL THR
SEQRES 18 A 373 ALA ILE ILE PHE VAL VAL ALA SER SER SER TYR ASN MET
SEQRES 19 A 373 VAL ILE ARG GLU ASP ASN GLN THR ASN ARG LEU GLN GLU
SEQRES 20 A 373 ALA LEU ASN LEU PHE LYS SER ILE TRP ASN ASN ARG TRP
SEQRES 21 A 373 LEU ARG THR ILE SER VAL ILE LEU PHE LEU ASN LYS GLN
SEQRES 22 A 373 ASP LEU LEU ALA GLU LYS VAL LEU ALA GLY LYS SER LYS
SEQRES 23 A 373 ILE GLU ASP TYR PHE PRO GLU PHE ALA ARG TYR THR THR
SEQRES 24 A 373 PRO GLU ASP ALA THR PRO GLU PRO GLY GLU ASP PRO ARG
SEQRES 25 A 373 VAL THR ARG ALA LYS TYR PHE ILE ARG ASP GLU PHE LEU
SEQRES 26 A 373 ARG ILE SER THR ALA SER GLY ASP GLY ARG HIS TYR CYS
SEQRES 27 A 373 TYR PRO HIS PHE THR CYS ALA VAL ASP THR GLU ASN ILE
SEQRES 28 A 373 ARG ARG VAL PHE ASN ASP CYS ARG ASP ILE ILE GLN ARG
SEQRES 29 A 373 MET HIS LEU ARG GLN TYR GLU LEU LEU
SEQRES 1 B 350 MET HIS HIS HIS HIS HIS HIS GLY SER SER GLY SER GLU
SEQRES 2 B 350 LEU ASP GLN LEU ARG GLN GLU ALA GLU GLN LEU LYS ASN
SEQRES 3 B 350 GLN ILE ARG ASP ALA ARG LYS ALA CYS ALA ASP ALA THR
SEQRES 4 B 350 LEU SER GLN ILE THR ASN ASN ILE ASP PRO VAL GLY ARG
SEQRES 5 B 350 ILE GLN MET ARG THR ARG ARG THR LEU ARG GLY HIS LEU
SEQRES 6 B 350 ALA LYS ILE TYR ALA MET HIS TRP GLY THR ASP SER ARG
SEQRES 7 B 350 LEU LEU VAL SER ALA SER GLN ASP GLY LYS LEU ILE ILE
SEQRES 8 B 350 TRP ASP SER TYR THR THR ASN LYS VAL HIS ALA ILE PRO
SEQRES 9 B 350 LEU ARG SER SER TRP VAL MET THR CYS ALA TYR ALA PRO
SEQRES 10 B 350 SER GLY ASN TYR VAL ALA CYS GLY GLY LEU ASP ASN ILE
SEQRES 11 B 350 CYS SER ILE TYR ASN LEU LYS THR ARG GLU GLY ASN VAL
SEQRES 12 B 350 ARG VAL SER ARG GLU LEU ALA GLY HIS THR GLY TYR LEU
SEQRES 13 B 350 SER CYS CYS ARG PHE LEU ASP ASP ASN GLN ILE VAL THR
SEQRES 14 B 350 SER SER GLY ASP THR THR CYS ALA LEU TRP ASP ILE GLU
SEQRES 15 B 350 THR GLY GLN GLN THR THR THR PHE THR GLY HIS THR GLY
SEQRES 16 B 350 ASP VAL MET SER LEU SER LEU ALA PRO ASP THR ARG LEU
SEQRES 17 B 350 PHE VAL SER GLY ALA CYS ASP ALA SER ALA LYS LEU TRP
SEQRES 18 B 350 ASP VAL ARG GLU GLY MET CYS ARG GLN THR PHE THR GLY
SEQRES 19 B 350 HIS GLU SER ASP ILE ASN ALA ILE CYS PHE PHE PRO ASN
SEQRES 20 B 350 GLY ASN ALA PHE ALA THR GLY SER ASP ASP ALA THR CYS
SEQRES 21 B 350 ARG LEU PHE ASP LEU ARG ALA ASP GLN GLU LEU MET THR
SEQRES 22 B 350 TYR SER HIS ASP ASN ILE ILE CYS GLY ILE THR SER VAL
SEQRES 23 B 350 SER PHE SER LYS SER GLY ARG LEU LEU LEU ALA GLY TYR
SEQRES 24 B 350 ASP ASP PHE ASN CYS ASN VAL TRP ASP ALA LEU LYS ALA
SEQRES 25 B 350 ASP ARG ALA GLY VAL LEU ALA GLY HIS ASP ASN ARG VAL
SEQRES 26 B 350 SER CYS LEU GLY VAL THR ASP ASP GLY MET ALA VAL ALA
SEQRES 27 B 350 THR GLY SER TRP ASP SER PHE LEU LYS ILE TRP ASN
SEQRES 1 E 297 MET LEU LEU VAL ASN GLN SER HIS GLN GLY PHE ASN LYS
SEQRES 2 E 297 GLU HIS THR SER LYS MET VAL SER ALA ILE VAL LEU TYR
SEQRES 3 E 297 VAL LEU LEU ALA ALA ALA ALA HIS SER ALA PHE ALA ASP
SEQRES 4 E 297 VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO
SEQRES 5 E 297 GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY PHE
SEQRES 6 E 297 ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN ALA
SEQRES 7 E 297 PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SER
SEQRES 8 E 297 GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS GLY
SEQRES 9 E 297 ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR LEU
SEQRES 10 E 297 PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR ALA
SEQRES 11 E 297 MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SER
SEQRES 12 E 297 SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU THR
SEQRES 13 E 297 VAL SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER
SEQRES 14 E 297 GLY GLY GLY GLY SER ASP ILE VAL MET THR GLN ALA THR
SEQRES 15 E 297 SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SER ILE
SEQRES 16 E 297 SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN GLY
SEQRES 17 E 297 ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY GLN
SEQRES 18 E 297 SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU ALA
SEQRES 19 E 297 SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER GLY
SEQRES 20 E 297 THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA GLU
SEQRES 21 E 297 ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU TYR
SEQRES 22 E 297 PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU LYS
SEQRES 23 E 297 ALA ALA ALA HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 G 71 MET ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG
SEQRES 2 G 71 LYS LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP
SEQRES 3 G 71 ARG ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA
SEQRES 4 G 71 TYR CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR
SEQRES 5 G 71 PRO VAL PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS
SEQRES 6 G 71 PHE PHE CYS ALA ILE LEU
SEQRES 1 N 160 MET LYS TYR LEU LEU PRO THR ALA ALA ALA GLY LEU LEU
SEQRES 2 N 160 LEU LEU ALA ALA GLN PRO ALA MET ALA GLN VAL GLN LEU
SEQRES 3 N 160 GLN GLU SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SER
SEQRES 4 N 160 LEU ARG LEU SER CYS ALA ALA SER GLY PHE THR PHE SER
SEQRES 5 N 160 ASN TYR LYS MET ASN TRP VAL ARG GLN ALA PRO GLY LYS
SEQRES 6 N 160 GLY LEU GLU TRP VAL SER ASP ILE SER GLN SER GLY ALA
SEQRES 7 N 160 SER ILE SER TYR THR GLY SER VAL LYS GLY ARG PHE THR
SEQRES 8 N 160 ILE SER ARG ASP ASN ALA LYS ASN THR LEU TYR LEU GLN
SEQRES 9 N 160 MET ASN SER LEU LYS PRO GLU ASP THR ALA VAL TYR TYR
SEQRES 10 N 160 CYS ALA ARG CYS PRO ALA PRO PHE THR ARG ASP CYS PHE
SEQRES 11 N 160 ASP VAL THR SER THR THR TYR ALA TYR ARG GLY GLN GLY
SEQRES 12 N 160 THR GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS
SEQRES 13 N 160 GLU PRO GLU ALA
SEQRES 1 P 42 TYR ALA GLU GLY THR PHE ILE SER ASP TYR SER ILE ALA
SEQRES 2 P 42 MET ASP LYS ILE HIS GLN GLN ASP PHE VAL ASN TRP LEU
SEQRES 3 P 42 LEU ALA GLN LYS GLY LYS LYS ASN ASP TRP LYS HIS ASN
SEQRES 4 P 42 ILE THR GLN
SEQRES 1 R 463 ASP TYR LYS ASP ASP ASP ASP ALA ALA ALA LEU GLU VAL
SEQRES 2 R 463 LEU PHE GLN GLY PRO ARG ALA GLU THR GLY SER LYS GLY
SEQRES 3 R 463 GLN THR ALA GLY GLU LEU TYR GLN ARG TRP GLU ARG TYR
SEQRES 4 R 463 ARG ARG GLU CYS GLN GLU THR LEU ALA ALA ALA GLU PRO
SEQRES 5 R 463 PRO SER GLY LEU ALA CYS ASN GLY SER PHE ASP MET TYR
SEQRES 6 R 463 VAL CYS TRP ASP TYR ALA ALA PRO ASN ALA THR ALA ARG
SEQRES 7 R 463 ALA SER CYS PRO TRP TYR LEU PRO TRP HIS HIS HIS VAL
SEQRES 8 R 463 ALA ALA GLY PHE VAL LEU ARG GLN CYS GLY SER ASP GLY
SEQRES 9 R 463 GLN TRP GLY LEU TRP ARG ASP HIS THR GLN CYS GLU ASN
SEQRES 10 R 463 PRO GLU LYS ASN GLU ALA PHE LEU ASP GLN ARG LEU ILE
SEQRES 11 R 463 LEU GLU ARG LEU GLN VAL MET TYR THR VAL GLY TYR SER
SEQRES 12 R 463 LEU SER LEU ALA THR LEU LEU LEU ALA LEU LEU ILE LEU
SEQRES 13 R 463 SER LEU PHE ARG ARG LEU HIS CYS THR ARG ASN TYR ILE
SEQRES 14 R 463 HIS ILE ASN LEU PHE THR SER PHE MET LEU ARG ALA ALA
SEQRES 15 R 463 ALA ILE LEU SER ARG ASP ARG LEU LEU PRO ARG PRO GLY
SEQRES 16 R 463 PRO TYR LEU GLY ASP GLN ALA LEU ALA LEU TRP ASN GLN
SEQRES 17 R 463 ALA LEU ALA ALA CYS ARG THR ALA GLN ILE VAL THR GLN
SEQRES 18 R 463 TYR CYS VAL GLY ALA ASN TYR THR TRP LEU LEU VAL GLU
SEQRES 19 R 463 GLY VAL TYR LEU HIS SER LEU LEU VAL LEU VAL GLY GLY
SEQRES 20 R 463 SER GLU GLU GLY HIS PHE ARG TYR TYR LEU LEU LEU GLY
SEQRES 21 R 463 TRP GLY ALA PRO ALA LEU PHE VAL ILE PRO TRP VAL ILE
SEQRES 22 R 463 VAL ARG TYR LEU TYR GLU ASN THR GLN CYS TRP GLU ARG
SEQRES 23 R 463 ASN GLU VAL LYS ALA ILE TRP TRP ILE ILE ARG THR PRO
SEQRES 24 R 463 ILE LEU MET THR ILE LEU ILE ASN PHE LEU ILE PHE ILE
SEQRES 25 R 463 ARG ILE LEU GLY ILE LEU LEU SER LYS LEU ARG THR ARG
SEQRES 26 R 463 GLN MET ARG CYS ARG ASP TYR ARG LEU ARG LEU ALA ARG
SEQRES 27 R 463 SER THR LEU THR LEU VAL PRO LEU LEU GLY VAL HIS GLU
SEQRES 28 R 463 VAL VAL PHE ALA PRO VAL THR GLU GLU GLN ALA ARG GLY
SEQRES 29 R 463 ALA LEU ARG PHE ALA LYS LEU GLY PHE GLU ILE PHE LEU
SEQRES 30 R 463 SER SER PHE GLN GLY PHE LEU VAL SER VAL LEU TYR CYS
SEQRES 31 R 463 PHE ILE ASN LYS GLU VAL GLN SER GLU ILE ARG ARG GLY
SEQRES 32 R 463 TRP HIS HIS CYS ARG LEU ARG ARG SER LEU GLY GLU GLU
SEQRES 33 R 463 GLN ARG GLN LEU PRO GLU ARG ALA PHE ARG ALA LEU PRO
SEQRES 34 R 463 SER GLY SER GLY PRO GLY GLU VAL PRO THR SER ARG GLY
SEQRES 35 R 463 LEU SER SER GLY THR LEU PRO GLY PRO GLY ASN GLU ALA
SEQRES 36 R 463 SER ARG GLU LEU GLU SER TYR CYS
HELIX 1 AA1 ASP A 16 ARG A 38 1 23
HELIX 2 AA2 SER A 54 GLN A 59 1 6
HELIX 3 AA3 LYS A 233 ASP A 240 5 8
HELIX 4 AA4 ASN A 264 ASN A 278 1 15
HELIX 5 AA5 LYS A 293 GLY A 304 1 12
HELIX 6 AA6 PHE A 312 ARG A 317 5 6
HELIX 7 AA7 ASP A 331 SER A 352 1 22
HELIX 8 AA8 ASN A 371 TYR A 391 1 21
HELIX 9 AA9 LEU B 4 CYS B 25 1 22
HELIX 10 AB1 LEU B 30 ASN B 35 1 6
HELIX 11 AB2 ALA E 28 PHE E 32 5 5
HELIX 12 AB3 SER E 53 GLY E 56 5 4
HELIX 13 AB4 ASP E 62 LYS E 65 5 4
HELIX 14 AB5 ARG E 87 THR E 91 5 5
HELIX 15 AB6 ALA G 7 ASN G 24 1 18
HELIX 16 AB7 LYS G 29 ALA G 45 1 17
HELIX 17 AB8 LYS G 46 ASP G 48 5 3
HELIX 18 AB9 THR N 28 TYR N 32 5 5
HELIX 19 AC1 GLY N 62 LYS N 65 5 4
HELIX 20 AC2 LYS N 87 THR N 91 5 5
HELIX 21 AC3 ALA P 2 GLN P 29 1 28
HELIX 22 AC4 LYS P 30 LYS P 32 5 3
HELIX 23 AC5 THR R 31 ALA R 53 1 23
HELIX 24 AC6 LEU R 88 HIS R 93 5 6
HELIX 25 AC7 LEU R 128 PHE R 162 1 35
HELIX 26 AC8 CYS R 167 LEU R 194 1 28
HELIX 27 AC9 LEU R 208 VAL R 246 1 39
HELIX 28 AD1 GLU R 253 TYR R 281 1 29
HELIX 29 AD2 VAL R 292 ARG R 328 1 37
HELIX 30 AD3 ARG R 336 GLY R 351 1 16
HELIX 31 AD4 VAL R 352 VAL R 356 5 5
HELIX 32 AD5 GLU R 362 GLY R 367 1 6
HELIX 33 AD6 ARG R 370 CYS R 393 1 24
HELIX 34 AD7 ASN R 396 CYS R 410 1 15
SHEET 1 AA1 6 THR A 210 GLN A 213 0
SHEET 2 AA1 6 ASN A 218 PHE A 222 -1 O PHE A 219 N PHE A 212
SHEET 3 AA1 6 THR A 40 LEU A 46 1 N HIS A 41 O ASN A 218
SHEET 4 AA1 6 ALA A 243 VAL A 248 1 O ILE A 245 N LEU A 44
SHEET 5 AA1 6 VAL A 287 LEU A 291 1 O PHE A 290 N PHE A 246
SHEET 6 AA1 6 CYS A 359 HIS A 362 1 O HIS A 362 N LEU A 291
SHEET 1 AA2 4 THR B 47 LEU B 51 0
SHEET 2 AA2 4 LEU B 336 TRP B 339 -1 O ILE B 338 N ARG B 48
SHEET 3 AA2 4 VAL B 327 SER B 331 -1 N THR B 329 O LYS B 337
SHEET 4 AA2 4 VAL B 315 VAL B 320 -1 N SER B 316 O GLY B 330
SHEET 1 AA3 4 ILE B 58 TRP B 63 0
SHEET 2 AA3 4 LEU B 69 SER B 74 -1 O VAL B 71 N HIS B 62
SHEET 3 AA3 4 LYS B 78 ASP B 83 -1 O LYS B 78 N SER B 74
SHEET 4 AA3 4 ASN B 88 PRO B 94 -1 O VAL B 90 N ILE B 81
SHEET 1 AA4 4 THR B 102 TYR B 105 0
SHEET 2 AA4 4 TYR B 111 GLY B 115 -1 O ALA B 113 N ALA B 104
SHEET 3 AA4 4 CYS B 121 ASN B 125 -1 O TYR B 124 N VAL B 112
SHEET 4 AA4 4 ARG B 134 LEU B 139 -1 O ARG B 137 N ILE B 123
SHEET 1 AA5 4 LEU B 146 CYS B 149 0
SHEET 2 AA5 4 GLN B 156 SER B 161 -1 O SER B 160 N CYS B 148
SHEET 3 AA5 4 THR B 165 ASP B 170 -1 O TRP B 169 N ILE B 157
SHEET 4 AA5 4 GLN B 175 THR B 181 -1 O THR B 178 N LEU B 168
SHEET 1 AA6 4 VAL B 187 LEU B 192 0
SHEET 2 AA6 4 PHE B 199 ALA B 203 -1 O GLY B 202 N SER B 189
SHEET 3 AA6 4 ALA B 208 TRP B 211 -1 O LYS B 209 N SER B 201
SHEET 4 AA6 4 CYS B 218 PHE B 222 -1 O PHE B 222 N ALA B 208
SHEET 1 AA7 4 ILE B 229 PHE B 234 0
SHEET 2 AA7 4 ALA B 240 SER B 245 -1 O GLY B 244 N ALA B 231
SHEET 3 AA7 4 CYS B 250 ASP B 254 -1 O PHE B 253 N PHE B 241
SHEET 4 AA7 4 GLU B 260 TYR B 264 -1 O LEU B 261 N LEU B 252
SHEET 1 AA8 4 SER B 275 PHE B 278 0
SHEET 2 AA8 4 LEU B 284 GLY B 288 -1 O LEU B 286 N SER B 277
SHEET 3 AA8 4 CYS B 294 ASP B 298 -1 O ASN B 295 N ALA B 287
SHEET 4 AA8 4 ARG B 304 LEU B 308 -1 O LEU B 308 N CYS B 294
SHEET 1 AA9 4 GLN E 3 SER E 7 0
SHEET 2 AA9 4 SER E 17 SER E 25 -1 O SER E 25 N GLN E 3
SHEET 3 AA9 4 THR E 78 THR E 84 -1 O LEU E 79 N CYS E 22
SHEET 4 AA9 4 PHE E 68 ASP E 73 -1 N SER E 71 O PHE E 80
SHEET 1 AB1 6 GLY E 10 VAL E 12 0
SHEET 2 AB1 6 THR E 115 VAL E 119 1 O THR E 118 N GLY E 10
SHEET 3 AB1 6 ALA E 92 SER E 99 -1 N TYR E 94 O THR E 115
SHEET 4 AB1 6 GLY E 33 GLN E 39 -1 N HIS E 35 O VAL E 97
SHEET 5 AB1 6 LEU E 45 ILE E 51 -1 O ILE E 51 N MET E 34
SHEET 6 AB1 6 ILE E 58 TYR E 60 -1 O TYR E 59 N TYR E 50
SHEET 1 AB2 4 MET E 128 THR E 129 0
SHEET 2 AB2 4 SER E 142 SER E 149 -1 N ARG E 148 O THR E 129
SHEET 3 AB2 4 ALA E 199 SER E 205 -1 O ILE E 204 N VAL E 143
SHEET 4 AB2 4 PHE E 191 SER E 196 -1 N SER E 194 O THR E 201
SHEET 1 AB3 2 SER E 134 VAL E 135 0
SHEET 2 AB3 2 LYS E 232 LEU E 233 1 O LYS E 232 N VAL E 135
SHEET 1 AB4 5 ASN E 182 LEU E 183 0
SHEET 2 AB4 5 GLN E 174 TYR E 178 -1 N TYR E 178 O ASN E 182
SHEET 3 AB4 5 LEU E 162 GLN E 167 -1 N TRP E 164 O LEU E 176
SHEET 4 AB4 5 VAL E 214 GLN E 219 -1 O VAL E 214 N GLN E 167
SHEET 5 AB4 5 THR E 226 PHE E 227 -1 O THR E 226 N GLN E 219
SHEET 1 AB5 4 GLN N 3 SER N 7 0
SHEET 2 AB5 4 SER N 17 SER N 25 -1 O SER N 21 N SER N 7
SHEET 3 AB5 4 THR N 78 ASN N 84 -1 O LEU N 81 N LEU N 20
SHEET 4 AB5 4 PHE N 68 ASP N 73 -1 N SER N 71 O TYR N 80
SHEET 1 AB6 5 SER N 59 TYR N 60 0
SHEET 2 AB6 5 LEU N 45 ILE N 51 -1 N ASP N 50 O SER N 59
SHEET 3 AB6 5 MET N 34 GLN N 39 -1 N ARG N 38 O GLU N 46
SHEET 4 AB6 5 ALA N 92 TYR N 95 -1 O VAL N 93 N GLN N 39
SHEET 5 AB6 5 THR N 122 VAL N 124 -1 O VAL N 124 N ALA N 92
SHEET 1 AB7 2 ALA R 78 ALA R 80 0
SHEET 2 AB7 2 ARG R 101 CYS R 103 -1 O CYS R 103 N ALA R 78
SSBOND 1 CYS E 22 CYS E 96 1555 1555 2.04
SSBOND 2 CYS E 147 CYS E 217 1555 1555 2.04
SSBOND 3 CYS N 22 CYS N 96 1555 1555 2.03
SSBOND 4 CYS N 99 CYS N 107 1555 1555 2.03
SSBOND 5 CYS R 46 CYS R 70 1555 1555 2.02
SSBOND 6 CYS R 61 CYS R 103 1555 1555 2.03
SSBOND 7 CYS R 84 CYS R 118 1555 1555 2.03
SSBOND 8 CYS R 216 CYS R 286 1555 1555 2.03
CISPEP 1 TYR E 223 PRO E 224 0 5.90
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 LEU A 12 132.913 111.163 161.071 1.00 76.04 N0
ATOM 2 CA LEU A 12 132.888 111.766 159.746 1.00 76.04 C0
ATOM 3 C LEU A 12 132.901 110.701 158.655 1.00 76.04 C0
ATOM 4 O LEU A 12 133.967 110.251 158.234 1.00 76.04 O0
ATOM 5 CB LEU A 12 134.080 112.708 159.565 1.00 76.04 C0
ATOM 6 CG LEU A 12 134.016 113.641 158.353 1.00 76.04 C0
ATOM 7 CD1 LEU A 12 133.263 114.916 158.702 1.00 76.04 C0
ATOM 8 CD2 LEU A 12 135.411 113.952 157.835 1.00 76.04 C0
ATOM 9 N SER A 13 131.713 110.314 158.187 1.00 72.12 N0
ATOM 10 CA SER A 13 131.563 109.356 157.093 1.00 72.12 C0
ATOM 11 C SER A 13 132.226 108.020 157.447 1.00 72.12 C0
ATOM 12 O SER A 13 133.236 107.614 156.871 1.00 72.12 O0
ATOM 13 CB SER A 13 132.136 109.928 155.791 1.00 72.12 C0
ATOM 14 OG SER A 13 131.477 111.128 155.430 1.00 72.12 O0
ATOM 15 N ALA A 14 131.634 107.360 158.442 1.00 69.06 N0
ATOM 16 CA ALA A 14 132.189 106.120 158.965 1.00 69.06 C0
ATOM 17 C ALA A 14 132.260 105.045 157.891 1.00 69.06 C0
ATOM 18 O ALA A 14 133.352 104.653 157.471 1.00 69.06 O0
ATOM 19 CB ALA A 14 131.352 105.627 160.144 1.00 69.06 C0
ATOM 20 N GLU A 15 131.104 104.561 157.438 1.00 68.31 N0
ATOM 21 CA GLU A 15 131.066 103.686 156.273 1.00 68.31 C0
ATOM 22 C GLU A 15 129.857 103.972 155.391 1.00 68.31 C0
ATOM 23 O GLU A 15 129.509 103.149 154.536 1.00 68.31 O0
ATOM 24 CB GLU A 15 131.098 102.216 156.706 1.00 68.31 C0
ATOM 25 CG GLU A 15 132.472 101.719 157.138 1.00 68.31 C0
ATOM 26 CD GLU A 15 133.523 101.890 156.068 1.00 68.31 C0
ATOM 27 OE1 GLU A 15 133.147 101.915 154.879 1.00 68.31 O0