HEADER MEMBRANE PROTEIN 14-DEC-17 6BWD
TITLE 3.7 ANGSTROM CRYOEM STRUCTURE OF TRUNCATED MOUSE TRPM7
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL SUBFAMILY M
COMPND 3 MEMBER 7;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 SYNONYM: CHANNEL-KINASE 1,LONG TRANSIENT RECEPTOR POTENTIAL CHANNEL
COMPND 6 7,LTRPC7,TRANSIENT RECEPTOR POTENTIAL-PHOSPHOLIPASE C-INTERACTING
COMPND 7 KINASE,TRP-PLIK;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS CRYOEM, TRUNCATED MOUSE TRPM7, MEMBRANE PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR J.ZHANG,Z.LI,J.DUAN,J.LI,R.E.HULSE,A.SANTA-CRUZ,S.A.ABIRIA,
AUTHOR 2 G.KRAPIVINSKY,D.E.CLAPHAM
REVDAT 4 18-DEC-19 6BWD 1 SCALE
REVDAT 3 05-SEP-18 6BWD 1 JRNL
REVDAT 2 29-AUG-18 6BWD 1 JRNL
REVDAT 1 15-AUG-18 6BWD 0
JRNL AUTH J.DUAN,Z.LI,J.LI,R.E.HULSE,A.SANTA-CRUZ,W.C.VALINSKY,
JRNL AUTH 2 S.A.ABIRIA,G.KRAPIVINSKY,J.ZHANG,D.E.CLAPHAM
JRNL TITL STRUCTURE OF THE MAMMALIAN TRPM7, A MAGNESIUM CHANNEL
JRNL TITL 2 REQUIRED DURING EMBRYONIC DEVELOPMENT.
JRNL REF PROC. NATL. ACAD. SCI. V. 115 E8201 2018
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 30108148
JRNL DOI 10.1073/PNAS.1810719115
REMARK 2
REMARK 2 RESOLUTION. 3.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : NULL
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.700
REMARK 3 NUMBER OF PARTICLES : 232930
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 6BWD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-17.
REMARK 100 THE DEPOSITION ID IS D_1000231689.
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 : TRUNCATED MOUSE TRPM7 WITH MG2+
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
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 POLARA 300
REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K 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 : NULL
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 56.00
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 ARG A 332
REMARK 465 ASP A 333
REMARK 465 VAL A 334
REMARK 465 LYS A 335
REMARK 465 GLN A 336
REMARK 465 GLY A 337
REMARK 465 ASN A 338
REMARK 465 LEU A 339
REMARK 465 PRO A 340
REMARK 465 PRO A 341
REMARK 465 GLY A 342
REMARK 465 GLU A 401
REMARK 465 THR A 402
REMARK 465 PHE A 403
REMARK 465 GLY A 404
REMARK 465 ASN A 405
REMARK 465 ARG A 406
REMARK 465 ALA A 407
REMARK 465 ASP A 408
REMARK 465 LYS A 409
REMARK 465 LYS A 410
REMARK 465 GLU A 411
REMARK 465 GLU A 444
REMARK 465 ILE A 445
REMARK 465 VAL A 446
REMARK 465 ASP A 447
REMARK 465 ILE A 448
REMARK 465 ASP A 449
REMARK 465 ASP A 450
REMARK 465 PRO A 451
REMARK 465 GLU A 452
REMARK 465 THR A 453
REMARK 465 LEU A 509
REMARK 465 VAL A 510
REMARK 465 ASP A 511
REMARK 465 ASP A 512
REMARK 465 ARG A 592
REMARK 465 LYS A 593
REMARK 465 ASN A 594
REMARK 465 SER A 595
REMARK 465 MET A 632
REMARK 465 THR A 633
REMARK 465 MET A 634
REMARK 465 GLU A 635
REMARK 465 ASP A 636
REMARK 465 SER A 637
REMARK 465 GLU A 638
REMARK 465 ASN A 639
REMARK 465 ASN A 640
REMARK 465 PHE A 641
REMARK 465 HIS A 642
REMARK 465 ASN A 643
REMARK 465 ILE A 644
REMARK 465 THR A 645
REMARK 465 GLU A 646
REMARK 465 GLU A 647
REMARK 465 ILE A 648
REMARK 465 PRO A 649
REMARK 465 MET A 650
REMARK 465 GLU A 651
REMARK 465 VAL A 652
REMARK 465 PHE A 653
REMARK 465 LYS A 654
REMARK 465 GLU A 655
REMARK 465 VAL A 656
REMARK 465 LYS A 657
REMARK 465 ILE A 658
REMARK 465 LEU A 659
REMARK 465 ASP A 660
REMARK 465 SER A 661
REMARK 465 SER A 662
REMARK 465 ASP A 663
REMARK 465 GLY A 664
REMARK 465 LYS A 665
REMARK 465 ASN A 666
REMARK 465 GLU A 667
REMARK 465 MET A 668
REMARK 465 GLU A 669
REMARK 465 ILE A 670
REMARK 465 HIS A 671
REMARK 465 ILE A 672
REMARK 465 LYS A 673
REMARK 465 SER A 674
REMARK 465 LYS A 675
REMARK 465 LYS A 676
REMARK 465 LEU A 677
REMARK 465 PRO A 678
REMARK 465 ILE A 679
REMARK 465 THR A 680
REMARK 465 SER A 745
REMARK 465 GLU A 746
REMARK 465 ALA A 747
REMARK 465 GLY A 748
REMARK 465 LYS A 749
REMARK 465 ILE A 750
REMARK 465 SER A 751
REMARK 465 VAL A 977
REMARK 465 SER A 978
REMARK 465 LEU A 979
REMARK 465 PHE A 980
REMARK 465 CYS A 981
REMARK 465 CYS A 982
REMARK 465 VAL A 983
REMARK 465 CYS A 984
REMARK 465 LYS A 985
REMARK 465 ARG A 986
REMARK 465 ARG A 987
REMARK 465 LYS A 988
REMARK 465 LYS A 989
REMARK 465 ASP A 990
REMARK 465 LYS A 991
REMARK 465 THR A 992
REMARK 465 SER A 993
REMARK 465 ASP A 994
REMARK 465 GLN A 1069
REMARK 465 ILE A 1070
REMARK 465 GLY A 1071
REMARK 465 HIS A 1072
REMARK 465 LEU A 1073
REMARK 465 GLN A 1074
REMARK 465 ASP A 1075
REMARK 465 LEU A 1076
REMARK 465 SER A 1077
REMARK 465 ALA A 1078
REMARK 465 LEU A 1079
REMARK 465 THR A 1080
REMARK 465 VAL A 1081
REMARK 465 ASP A 1082
REMARK 465 THR A 1083
REMARK 465 LEU A 1084
REMARK 465 LYS A 1085
REMARK 465 THR A 1086
REMARK 465 LEU A 1087
REMARK 465 THR A 1088
REMARK 465 ALA A 1089
REMARK 465 GLN A 1090
REMARK 465 LYS A 1091
REMARK 465 ALA A 1092
REMARK 465 SER A 1093
REMARK 465 GLU A 1094
REMARK 465 ALA A 1095
REMARK 465 SER A 1096
REMARK 465 LYS A 1097
REMARK 465 VAL A 1098
REMARK 465 HIS A 1099
REMARK 465 ASN A 1100
REMARK 465 GLU A 1101
REMARK 465 ILE A 1102
REMARK 465 THR A 1103
REMARK 465 ARG A 1104
REMARK 465 GLU A 1105
REMARK 465 LEU A 1106
REMARK 465 SER A 1107
REMARK 465 ILE A 1108
REMARK 465 SER A 1109
REMARK 465 LYS A 1110
REMARK 465 HIS A 1111
REMARK 465 LEU A 1112
REMARK 465 ALA A 1113
REMARK 465 GLN A 1114
REMARK 465 ASN A 1115
REMARK 465 LEU A 1116
REMARK 465 ILE A 1117
REMARK 465 ASP A 1118
REMARK 465 ASP A 1119
REMARK 465 VAL A 1120
REMARK 465 PRO A 1121
REMARK 465 VAL A 1122
REMARK 465 ARG A 1123
REMARK 465 PRO A 1124
REMARK 465 LEU A 1125
REMARK 465 TRP A 1126
REMARK 465 LYS A 1127
REMARK 465 LYS A 1128
REMARK 465 PRO A 1129
REMARK 465 SER A 1130
REMARK 465 ALA A 1131
REMARK 465 VAL A 1132
REMARK 465 ASN A 1133
REMARK 465 THR A 1134
REMARK 465 LEU A 1135
REMARK 465 SER A 1136
REMARK 465 SER A 1137
REMARK 465 SER A 1138
REMARK 465 ARG B 332
REMARK 465 ASP B 333
REMARK 465 VAL B 334
REMARK 465 LYS B 335
REMARK 465 GLN B 336
REMARK 465 GLY B 337
REMARK 465 ASN B 338
REMARK 465 LEU B 339
REMARK 465 PRO B 340
REMARK 465 PRO B 341
REMARK 465 GLY B 342
REMARK 465 GLU B 401
REMARK 465 THR B 402
REMARK 465 PHE B 403
REMARK 465 GLY B 404
REMARK 465 ASN B 405
REMARK 465 ARG B 406
REMARK 465 ALA B 407
REMARK 465 ASP B 408
REMARK 465 LYS B 409
REMARK 465 LYS B 410
REMARK 465 GLU B 411
REMARK 465 GLU B 444
REMARK 465 ILE B 445
REMARK 465 VAL B 446
REMARK 465 ASP B 447
REMARK 465 ILE B 448
REMARK 465 ASP B 449
REMARK 465 ASP B 450
REMARK 465 PRO B 451
REMARK 465 GLU B 452
REMARK 465 THR B 453
REMARK 465 LEU B 509
REMARK 465 VAL B 510
REMARK 465 ASP B 511
REMARK 465 ASP B 512
REMARK 465 ARG B 592
REMARK 465 LYS B 593
REMARK 465 ASN B 594
REMARK 465 SER B 595
REMARK 465 MET B 632
REMARK 465 THR B 633
REMARK 465 MET B 634
REMARK 465 GLU B 635
REMARK 465 ASP B 636
REMARK 465 SER B 637
REMARK 465 GLU B 638
REMARK 465 ASN B 639
REMARK 465 ASN B 640
REMARK 465 PHE B 641
REMARK 465 HIS B 642
REMARK 465 ASN B 643
REMARK 465 ILE B 644
REMARK 465 THR B 645
REMARK 465 GLU B 646
REMARK 465 GLU B 647
REMARK 465 ILE B 648
REMARK 465 PRO B 649
REMARK 465 MET B 650
REMARK 465 GLU B 651
REMARK 465 VAL B 652
REMARK 465 PHE B 653
REMARK 465 LYS B 654
REMARK 465 GLU B 655
REMARK 465 VAL B 656
REMARK 465 LYS B 657
REMARK 465 ILE B 658
REMARK 465 LEU B 659
REMARK 465 ASP B 660
REMARK 465 SER B 661
REMARK 465 SER B 662
REMARK 465 ASP B 663
REMARK 465 GLY B 664
REMARK 465 LYS B 665
REMARK 465 ASN B 666
REMARK 465 GLU B 667
REMARK 465 MET B 668
REMARK 465 GLU B 669
REMARK 465 ILE B 670
REMARK 465 HIS B 671
REMARK 465 ILE B 672
REMARK 465 LYS B 673
REMARK 465 SER B 674
REMARK 465 LYS B 675
REMARK 465 LYS B 676
REMARK 465 LEU B 677
REMARK 465 PRO B 678
REMARK 465 ILE B 679
REMARK 465 THR B 680
REMARK 465 SER B 745
REMARK 465 GLU B 746
REMARK 465 ALA B 747
REMARK 465 GLY B 748
REMARK 465 LYS B 749
REMARK 465 ILE B 750
REMARK 465 SER B 751
REMARK 465 VAL B 977
REMARK 465 SER B 978
REMARK 465 LEU B 979
REMARK 465 PHE B 980
REMARK 465 CYS B 981
REMARK 465 CYS B 982
REMARK 465 VAL B 983
REMARK 465 CYS B 984
REMARK 465 LYS B 985
REMARK 465 ARG B 986
REMARK 465 ARG B 987
REMARK 465 LYS B 988
REMARK 465 LYS B 989
REMARK 465 ASP B 990
REMARK 465 LYS B 991
REMARK 465 THR B 992
REMARK 465 SER B 993
REMARK 465 ASP B 994
REMARK 465 GLN B 1069
REMARK 465 ILE B 1070
REMARK 465 GLY B 1071
REMARK 465 HIS B 1072
REMARK 465 LEU B 1073
REMARK 465 GLN B 1074
REMARK 465 ASP B 1075
REMARK 465 LEU B 1076
REMARK 465 SER B 1077
REMARK 465 ALA B 1078
REMARK 465 LEU B 1079
REMARK 465 THR B 1080
REMARK 465 VAL B 1081
REMARK 465 ASP B 1082
REMARK 465 THR B 1083
REMARK 465 LEU B 1084
REMARK 465 LYS B 1085
REMARK 465 THR B 1086
REMARK 465 LEU B 1087
REMARK 465 THR B 1088
REMARK 465 ALA B 1089
REMARK 465 GLN B 1090
REMARK 465 LYS B 1091
REMARK 465 ALA B 1092
REMARK 465 SER B 1093
REMARK 465 GLU B 1094
REMARK 465 ALA B 1095
REMARK 465 SER B 1096
REMARK 465 LYS B 1097
REMARK 465 VAL B 1098
REMARK 465 HIS B 1099
REMARK 465 ASN B 1100
REMARK 465 GLU B 1101
REMARK 465 ILE B 1102
REMARK 465 THR B 1103
REMARK 465 ARG B 1104
REMARK 465 GLU B 1105
REMARK 465 LEU B 1106
REMARK 465 SER B 1107
REMARK 465 ILE B 1108
REMARK 465 SER B 1109
REMARK 465 LYS B 1110
REMARK 465 HIS B 1111
REMARK 465 LEU B 1112
REMARK 465 ALA B 1113
REMARK 465 GLN B 1114
REMARK 465 ASN B 1115
REMARK 465 LEU B 1116
REMARK 465 ILE B 1117
REMARK 465 ASP B 1118
REMARK 465 ASP B 1119
REMARK 465 VAL B 1120
REMARK 465 PRO B 1121
REMARK 465 VAL B 1122
REMARK 465 ARG B 1123
REMARK 465 PRO B 1124
REMARK 465 LEU B 1125
REMARK 465 TRP B 1126
REMARK 465 LYS B 1127
REMARK 465 LYS B 1128
REMARK 465 PRO B 1129
REMARK 465 SER B 1130
REMARK 465 ALA B 1131
REMARK 465 VAL B 1132
REMARK 465 ASN B 1133
REMARK 465 THR B 1134
REMARK 465 LEU B 1135
REMARK 465 SER B 1136
REMARK 465 SER B 1137
REMARK 465 SER B 1138
REMARK 465 ARG C 149
REMARK 465 ASP C 150
REMARK 465 VAL C 151
REMARK 465 LYS C 152
REMARK 465 GLN C 153
REMARK 465 GLY C 154
REMARK 465 ASN C 155
REMARK 465 LEU C 156
REMARK 465 PRO C 157
REMARK 465 PRO C 158
REMARK 465 GLY C 159
REMARK 465 GLU C 218
REMARK 465 THR C 219
REMARK 465 PHE C 220
REMARK 465 GLY C 221
REMARK 465 ASN C 222
REMARK 465 ARG C 223
REMARK 465 ALA C 224
REMARK 465 ASP C 225
REMARK 465 LYS C 226
REMARK 465 LYS C 227
REMARK 465 GLU C 228
REMARK 465 GLU C 261
REMARK 465 ILE C 262
REMARK 465 VAL C 263
REMARK 465 ASP C 264
REMARK 465 ILE C 265
REMARK 465 ASP C 266
REMARK 465 ASP C 267
REMARK 465 PRO C 268
REMARK 465 GLU C 269
REMARK 465 THR C 270
REMARK 465 LEU C 326
REMARK 465 VAL C 327
REMARK 465 ASP C 328
REMARK 465 ASP C 329
REMARK 465 ARG C 409
REMARK 465 LYS C 410
REMARK 465 ASN C 411
REMARK 465 SER C 412
REMARK 465 MET C 449
REMARK 465 THR C 450
REMARK 465 MET C 451
REMARK 465 GLU C 452
REMARK 465 ASP C 453
REMARK 465 SER C 454
REMARK 465 GLU C 455
REMARK 465 ASN C 456
REMARK 465 ASN C 457
REMARK 465 PHE C 458
REMARK 465 HIS C 459
REMARK 465 ASN C 460
REMARK 465 ILE C 461
REMARK 465 THR C 462
REMARK 465 GLU C 463
REMARK 465 GLU C 464
REMARK 465 ILE C 465
REMARK 465 PRO C 466
REMARK 465 MET C 467
REMARK 465 GLU C 468
REMARK 465 VAL C 469
REMARK 465 PHE C 470
REMARK 465 LYS C 471
REMARK 465 GLU C 472
REMARK 465 VAL C 473
REMARK 465 LYS C 474
REMARK 465 ILE C 475
REMARK 465 LEU C 476
REMARK 465 ASP C 477
REMARK 465 SER C 478
REMARK 465 SER C 479
REMARK 465 ASP C 480
REMARK 465 GLY C 481
REMARK 465 LYS C 482
REMARK 465 ASN C 483
REMARK 465 GLU C 484
REMARK 465 MET C 485
REMARK 465 GLU C 486
REMARK 465 ILE C 487
REMARK 465 HIS C 488
REMARK 465 ILE C 489
REMARK 465 LYS C 490
REMARK 465 SER C 491
REMARK 465 LYS C 492
REMARK 465 LYS C 493
REMARK 465 LEU C 494
REMARK 465 PRO C 495
REMARK 465 ILE C 496
REMARK 465 THR C 497
REMARK 465 SER C 562
REMARK 465 GLU C 563
REMARK 465 ALA C 564
REMARK 465 GLY C 565
REMARK 465 LYS C 566
REMARK 465 ILE C 567
REMARK 465 SER C 568
REMARK 465 VAL C 794
REMARK 465 SER C 795
REMARK 465 LEU C 796
REMARK 465 PHE C 797
REMARK 465 CYS C 798
REMARK 465 CYS C 799
REMARK 465 VAL C 800
REMARK 465 CYS C 801
REMARK 465 LYS C 802
REMARK 465 ARG C 803
REMARK 465 ARG C 804
REMARK 465 LYS C 805
REMARK 465 LYS C 806
REMARK 465 ASP C 807
REMARK 465 LYS C 808
REMARK 465 THR C 809
REMARK 465 SER C 810
REMARK 465 ASP C 811
REMARK 465 GLN C 886
REMARK 465 ILE C 887
REMARK 465 GLY C 888
REMARK 465 HIS C 889
REMARK 465 LEU C 890
REMARK 465 GLN C 891
REMARK 465 ASP C 892
REMARK 465 LEU C 893
REMARK 465 SER C 894
REMARK 465 ALA C 895
REMARK 465 LEU C 896
REMARK 465 THR C 897
REMARK 465 VAL C 898
REMARK 465 ASP C 899
REMARK 465 THR C 900
REMARK 465 LEU C 901
REMARK 465 LYS C 902
REMARK 465 THR C 903
REMARK 465 LEU C 904
REMARK 465 THR C 905
REMARK 465 ALA C 906
REMARK 465 GLN C 907
REMARK 465 LYS C 908
REMARK 465 ALA C 909
REMARK 465 SER C 910
REMARK 465 GLU C 911
REMARK 465 ALA C 912
REMARK 465 SER C 913
REMARK 465 LYS C 914
REMARK 465 VAL C 915
REMARK 465 HIS C 916
REMARK 465 ASN C 917
REMARK 465 GLU C 918
REMARK 465 ILE C 919
REMARK 465 THR C 920
REMARK 465 ARG C 921
REMARK 465 GLU C 922
REMARK 465 LEU C 923
REMARK 465 SER C 924
REMARK 465 ILE C 925
REMARK 465 SER C 926
REMARK 465 LYS C 927
REMARK 465 HIS C 928
REMARK 465 LEU C 929
REMARK 465 ALA C 930
REMARK 465 GLN C 931
REMARK 465 ASN C 932
REMARK 465 LEU C 933
REMARK 465 ILE C 934
REMARK 465 ASP C 935
REMARK 465 ASP C 936
REMARK 465 VAL C 937
REMARK 465 PRO C 938
REMARK 465 VAL C 939
REMARK 465 ARG C 940
REMARK 465 PRO C 941
REMARK 465 LEU C 942
REMARK 465 TRP C 943
REMARK 465 LYS C 944
REMARK 465 LYS C 945
REMARK 465 PRO C 946
REMARK 465 SER C 947
REMARK 465 ALA C 948
REMARK 465 VAL C 949
REMARK 465 ASN C 950
REMARK 465 THR C 951
REMARK 465 LEU C 952
REMARK 465 SER C 953
REMARK 465 SER C 954
REMARK 465 SER C 955
REMARK 465 ARG D 332
REMARK 465 ASP D 333
REMARK 465 VAL D 334
REMARK 465 LYS D 335
REMARK 465 GLN D 336
REMARK 465 GLY D 337
REMARK 465 ASN D 338
REMARK 465 LEU D 339
REMARK 465 PRO D 340
REMARK 465 PRO D 341
REMARK 465 GLY D 342
REMARK 465 GLU D 401
REMARK 465 THR D 402
REMARK 465 PHE D 403
REMARK 465 GLY D 404
REMARK 465 ASN D 405
REMARK 465 ARG D 406
REMARK 465 ALA D 407
REMARK 465 ASP D 408
REMARK 465 LYS D 409
REMARK 465 LYS D 410
REMARK 465 GLU D 411
REMARK 465 GLU D 444
REMARK 465 ILE D 445
REMARK 465 VAL D 446
REMARK 465 ASP D 447
REMARK 465 ILE D 448
REMARK 465 ASP D 449
REMARK 465 ASP D 450
REMARK 465 PRO D 451
REMARK 465 GLU D 452
REMARK 465 THR D 453
REMARK 465 LEU D 509
REMARK 465 VAL D 510
REMARK 465 ASP D 511
REMARK 465 ASP D 512
REMARK 465 ARG D 592
REMARK 465 LYS D 593
REMARK 465 ASN D 594
REMARK 465 SER D 595
REMARK 465 MET D 632
REMARK 465 THR D 633
REMARK 465 MET D 634
REMARK 465 GLU D 635
REMARK 465 ASP D 636
REMARK 465 SER D 637
REMARK 465 GLU D 638
REMARK 465 ASN D 639
REMARK 465 ASN D 640
REMARK 465 PHE D 641
REMARK 465 HIS D 642
REMARK 465 ASN D 643
REMARK 465 ILE D 644
REMARK 465 THR D 645
REMARK 465 GLU D 646
REMARK 465 GLU D 647
REMARK 465 ILE D 648
REMARK 465 PRO D 649
REMARK 465 MET D 650
REMARK 465 GLU D 651
REMARK 465 VAL D 652
REMARK 465 PHE D 653
REMARK 465 LYS D 654
REMARK 465 GLU D 655
REMARK 465 VAL D 656
REMARK 465 LYS D 657
REMARK 465 ILE D 658
REMARK 465 LEU D 659
REMARK 465 ASP D 660
REMARK 465 SER D 661
REMARK 465 SER D 662
REMARK 465 ASP D 663
REMARK 465 GLY D 664
REMARK 465 LYS D 665
REMARK 465 ASN D 666
REMARK 465 GLU D 667
REMARK 465 MET D 668
REMARK 465 GLU D 669
REMARK 465 ILE D 670
REMARK 465 HIS D 671
REMARK 465 ILE D 672
REMARK 465 LYS D 673
REMARK 465 SER D 674
REMARK 465 LYS D 675
REMARK 465 LYS D 676
REMARK 465 LEU D 677
REMARK 465 PRO D 678
REMARK 465 ILE D 679
REMARK 465 THR D 680
REMARK 465 SER D 745
REMARK 465 GLU D 746
REMARK 465 ALA D 747
REMARK 465 GLY D 748
REMARK 465 LYS D 749
REMARK 465 ILE D 750
REMARK 465 SER D 751
REMARK 465 VAL D 977
REMARK 465 SER D 978
REMARK 465 LEU D 979
REMARK 465 PHE D 980
REMARK 465 CYS D 981
REMARK 465 CYS D 982
REMARK 465 VAL D 983
REMARK 465 CYS D 984
REMARK 465 LYS D 985
REMARK 465 ARG D 986
REMARK 465 ARG D 987
REMARK 465 LYS D 988
REMARK 465 LYS D 989
REMARK 465 ASP D 990
REMARK 465 LYS D 991
REMARK 465 THR D 992
REMARK 465 SER D 993
REMARK 465 ASP D 994
REMARK 465 GLN D 1069
REMARK 465 ILE D 1070
REMARK 465 GLY D 1071
REMARK 465 HIS D 1072
REMARK 465 LEU D 1073
REMARK 465 GLN D 1074
REMARK 465 ASP D 1075
REMARK 465 LEU D 1076
REMARK 465 SER D 1077
REMARK 465 ALA D 1078
REMARK 465 LEU D 1079
REMARK 465 THR D 1080
REMARK 465 VAL D 1081
REMARK 465 ASP D 1082
REMARK 465 THR D 1083
REMARK 465 LEU D 1084
REMARK 465 LYS D 1085
REMARK 465 THR D 1086
REMARK 465 LEU D 1087
REMARK 465 THR D 1088
REMARK 465 ALA D 1089
REMARK 465 GLN D 1090
REMARK 465 LYS D 1091
REMARK 465 ALA D 1092
REMARK 465 SER D 1093
REMARK 465 GLU D 1094
REMARK 465 ALA D 1095
REMARK 465 SER D 1096
REMARK 465 LYS D 1097
REMARK 465 VAL D 1098
REMARK 465 HIS D 1099
REMARK 465 ASN D 1100
REMARK 465 GLU D 1101
REMARK 465 ILE D 1102
REMARK 465 THR D 1103
REMARK 465 ARG D 1104
REMARK 465 GLU D 1105
REMARK 465 LEU D 1106
REMARK 465 SER D 1107
REMARK 465 ILE D 1108
REMARK 465 SER D 1109
REMARK 465 LYS D 1110
REMARK 465 HIS D 1111
REMARK 465 LEU D 1112
REMARK 465 ALA D 1113
REMARK 465 GLN D 1114
REMARK 465 ASN D 1115
REMARK 465 LEU D 1116
REMARK 465 ILE D 1117
REMARK 465 ASP D 1118
REMARK 465 ASP D 1119
REMARK 465 VAL D 1120
REMARK 465 PRO D 1121
REMARK 465 VAL D 1122
REMARK 465 ARG D 1123
REMARK 465 PRO D 1124
REMARK 465 LEU D 1125
REMARK 465 TRP D 1126
REMARK 465 LYS D 1127
REMARK 465 LYS D 1128
REMARK 465 PRO D 1129
REMARK 465 SER D 1130
REMARK 465 ALA D 1131
REMARK 465 VAL D 1132
REMARK 465 ASN D 1133
REMARK 465 THR D 1134
REMARK 465 LEU D 1135
REMARK 465 SER D 1136
REMARK 465 SER D 1137
REMARK 465 SER D 1138
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 305 CG CD CE NZ
REMARK 470 PHE A 306 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR A 308 OG1 CG2
REMARK 470 PRO A 310 CG CD
REMARK 470 ARG A 311 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 313 CG CD OE1 OE2
REMARK 470 LEU A 315 CG CD1 CD2
REMARK 470 LYS A 319 CG CD CE NZ
REMARK 470 GLN A 320 CG CD OE1 NE2
REMARK 470 PRO A 322 CG CD
REMARK 470 PRO A 325 CG CD
REMARK 470 MET A 326 CG SD CE
REMARK 470 LEU A 327 CG CD1 CD2
REMARK 470 PHE A 328 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 330 CG CD1 CD2
REMARK 470 ILE A 331 CG1 CG2 CD1
REMARK 470 ILE A 354 CG1 CG2 CD1
REMARK 470 GLU A 355 CG CD OE1 OE2
REMARK 470 MET A 358 CG SD CE
REMARK 470 THR A 361 OG1 CG2
REMARK 470 TYR A 362 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 CYS A 364 SG
REMARK 470 THR A 365 OG1 CG2
REMARK 470 THR A 367 OG1 CG2
REMARK 470 ARG A 368 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 369 CG CD CE NZ
REMARK 470 ARG A 370 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 372 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 382 CG OD1 ND2
REMARK 470 ARG A 383 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 384 CG CD NE CZ NH1 NH2
REMARK 470 SER A 385 OG
REMARK 470 ARG A 387 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 388 CG OD1 ND2
REMARK 470 THR A 389 OG1 CG2
REMARK 470 SER A 390 OG
REMARK 470 MET A 413 CG SD CE
REMARK 470 ARG A 414 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 416 CG OD1 ND2
REMARK 470 HIS A 417 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 420 CG CD CE NZ
REMARK 470 ASP A 430 CG OD1 OD2
REMARK 470 SER A 432 OG
REMARK 470 GLU A 434 CG CD OE1 OE2
REMARK 470 ARG A 440 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 484 CG CD OE1 OE2
REMARK 470 GLU A 503 CG CD OE1 OE2
REMARK 470 ASP A 523 CG OD1 OD2
REMARK 470 GLU A 530 CG CD OE1 OE2
REMARK 470 MET A 542 CG SD CE
REMARK 470 MET A 544 CG SD CE
REMARK 470 TYR A 549 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TRP A 596 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 596 CZ3 CH2
REMARK 470 PRO A 606 CG CD
REMARK 470 ILE A 609 CG1 CG2 CD1
REMARK 470 LEU A 610 CG CD1 CD2
REMARK 470 MET A 611 CG SD CE
REMARK 470 LEU A 612 CG CD1 CD2
REMARK 470 GLU A 613 CG CD OE1 OE2
REMARK 470 TYR A 614 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 615 CG CD CE NZ
REMARK 470 THR A 616 OG1 CG2
REMARK 470 LYS A 617 CG CD CE NZ
REMARK 470 GLU A 619 CG CD OE1 OE2
REMARK 470 MET A 620 CG SD CE
REMARK 470 SER A 621 OG
REMARK 470 HIS A 622 CG ND1 CD2 CE1 NE2
REMARK 470 ILE A 623 CG1 CG2 CD1
REMARK 470 PRO A 624 CG CD
REMARK 470 GLN A 625 CG CD OE1 NE2
REMARK 470 SER A 626 OG
REMARK 470 GLN A 627 CG CD OE1 NE2
REMARK 470 ASP A 628 CG OD1 OD2
REMARK 470 HIS A 630 CG ND1 CD2 CE1 NE2
REMARK 470 GLN A 631 CG CD OE1 NE2
REMARK 470 TYR A 761 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 784 CG CD CE NZ
REMARK 470 TRP A 785 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 785 CZ3 CH2
REMARK 470 ASN A 786 CG OD1 ND2
REMARK 470 TYR A 787 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE A 788 CG1 CG2 CD1
REMARK 470 ASN A 789 CG OD1 ND2
REMARK 470 TYR A 791 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASN A 793 CG OD1 ND2
REMARK 470 HIS A 794 CG ND1 CD2 CE1 NE2
REMARK 470 VAL A 795 CG1 CG2
REMARK 470 PRO A 967 CG CD
REMARK 470 PRO A 968 CG CD
REMARK 470 PRO A 969 CG CD
REMARK 470 LEU A 970 CG CD1 CD2
REMARK 470 ILE A 971 CG1 CG2 CD1
REMARK 470 ILE A 972 CG1 CG2 CD1
REMARK 470 LEU A 973 CG CD1 CD2
REMARK 470 SER A 974 OG
REMARK 470 HIS A 975 CG ND1 CD2 CE1 NE2
REMARK 470 ILE A 976 CG1 CG2 CD1
REMARK 470 PRO A 996 CG CD
REMARK 470 LYS A 997 CG CD CE NZ
REMARK 470 LEU A 998 CG CD1 CD2
REMARK 470 LEU A1000 CG CD1 CD2
REMARK 470 THR A1001 OG1 CG2
REMARK 470 LEU A1063 CG CD1 CD2
REMARK 470 GLN A1064 CG CD OE1 NE2
REMARK 470 SER A1065 OG
REMARK 470 LEU A1066 CG CD1 CD2
REMARK 470 ASP A1067 CG OD1 OD2
REMARK 470 SER A1068 OG
REMARK 470 LYS B 305 CG CD CE NZ
REMARK 470 PHE B 306 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PRO B 310 CG CD
REMARK 470 ARG B 311 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 313 CG CD OE1 OE2
REMARK 470 LEU B 315 CG CD1 CD2
REMARK 470 LYS B 319 CG CD CE NZ
REMARK 470 GLN B 320 CG CD OE1 NE2
REMARK 470 PRO B 322 CG CD
REMARK 470 PRO B 325 CG CD
REMARK 470 MET B 326 CG SD CE
REMARK 470 LEU B 327 CG CD1 CD2
REMARK 470 PHE B 328 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU B 330 CG CD1 CD2
REMARK 470 ILE B 331 CG1 CG2 CD1
REMARK 470 LEU B 352 CG CD1 CD2
REMARK 470 MET B 358 CG SD CE
REMARK 470 THR B 361 OG1 CG2
REMARK 470 TYR B 362 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 CYS B 364 SG
REMARK 470 THR B 365 OG1 CG2
REMARK 470 THR B 367 OG1 CG2
REMARK 470 ARG B 368 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 369 CG CD CE NZ
REMARK 470 ARG B 370 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 372 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 382 CG OD1 ND2
REMARK 470 ARG B 383 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 384 CG CD NE CZ NH1 NH2
REMARK 470 SER B 385 OG
REMARK 470 ARG B 387 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 388 CG OD1 ND2
REMARK 470 THR B 389 OG1 CG2
REMARK 470 SER B 390 OG
REMARK 470 MET B 413 CG SD CE
REMARK 470 ARG B 414 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 416 CG OD1 ND2
REMARK 470 HIS B 417 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 420 CG CD CE NZ
REMARK 470 ASP B 430 CG OD1 OD2
REMARK 470 SER B 432 OG
REMARK 470 MET B 433 CG SD CE
REMARK 470 GLU B 434 CG CD OE1 OE2
REMARK 470 GLU B 484 CG CD OE1 OE2
REMARK 470 GLU B 503 CG CD OE1 OE2
REMARK 470 GLU B 530 CG CD OE1 OE2
REMARK 470 GLU B 540 CG CD OE1 OE2
REMARK 470 MET B 542 CG SD CE
REMARK 470 MET B 544 CG SD CE
REMARK 470 TYR B 549 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU B 551 CG CD1 CD2
REMARK 470 TRP B 596 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 596 CZ3 CH2
REMARK 470 PRO B 606 CG CD
REMARK 470 ILE B 609 CG1 CG2 CD1
REMARK 470 LEU B 610 CG CD1 CD2
REMARK 470 MET B 611 CG SD CE
REMARK 470 LEU B 612 CG CD1 CD2
REMARK 470 GLU B 613 CG CD OE1 OE2
REMARK 470 TYR B 614 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 615 CG CD CE NZ
REMARK 470 THR B 616 OG1 CG2
REMARK 470 LYS B 617 CG CD CE NZ
REMARK 470 GLU B 619 CG CD OE1 OE2
REMARK 470 MET B 620 CG SD CE
REMARK 470 SER B 621 OG
REMARK 470 HIS B 622 CG ND1 CD2 CE1 NE2
REMARK 470 ILE B 623 CG1 CG2 CD1
REMARK 470 PRO B 624 CG CD
REMARK 470 GLN B 625 CG CD OE1 NE2
REMARK 470 SER B 626 OG
REMARK 470 GLN B 627 CG CD OE1 NE2
REMARK 470 ASP B 628 CG OD1 OD2
REMARK 470 HIS B 630 CG ND1 CD2 CE1 NE2
REMARK 470 GLN B 631 CG CD OE1 NE2
REMARK 470 TYR B 761 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 784 CG CD CE NZ
REMARK 470 TRP B 785 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 785 CZ3 CH2
REMARK 470 ASN B 786 CG OD1 ND2
REMARK 470 TYR B 787 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE B 788 CG1 CG2 CD1
REMARK 470 ASN B 789 CG OD1 ND2
REMARK 470 TYR B 791 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASN B 793 CG OD1 ND2
REMARK 470 HIS B 794 CG ND1 CD2 CE1 NE2
REMARK 470 VAL B 795 CG1 CG2
REMARK 470 PRO B 967 CG CD
REMARK 470 PRO B 968 CG CD
REMARK 470 PRO B 969 CG CD
REMARK 470 LEU B 970 CG CD1 CD2
REMARK 470 ILE B 971 CG1 CG2 CD1
REMARK 470 ILE B 972 CG1 CG2 CD1
REMARK 470 LEU B 973 CG CD1 CD2
REMARK 470 SER B 974 OG
REMARK 470 HIS B 975 CG ND1 CD2 CE1 NE2
REMARK 470 ILE B 976 CG1 CG2 CD1
REMARK 470 PRO B 996 CG CD
REMARK 470 LYS B 997 CG CD CE NZ
REMARK 470 LEU B 998 CG CD1 CD2
REMARK 470 LEU B1000 CG CD1 CD2
REMARK 470 THR B1001 OG1 CG2
REMARK 470 LEU B1063 CG CD1 CD2
REMARK 470 GLN B1064 CG CD OE1 NE2
REMARK 470 SER B1065 OG
REMARK 470 LEU B1066 CG CD1 CD2
REMARK 470 ASP B1067 CG OD1 OD2
REMARK 470 SER B1068 OG
REMARK 470 LYS C 122 CG CD CE NZ
REMARK 470 PHE C 123 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PRO C 127 CG CD
REMARK 470 ARG C 128 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 130 CG CD OE1 OE2
REMARK 470 LEU C 132 CG CD1 CD2
REMARK 470 LYS C 136 CG CD CE NZ
REMARK 470 GLN C 137 CG CD OE1 NE2
REMARK 470 PRO C 139 CG CD
REMARK 470 PRO C 142 CG CD
REMARK 470 MET C 143 CG SD CE
REMARK 470 LEU C 144 CG CD1 CD2
REMARK 470 PHE C 145 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU C 147 CG CD1 CD2
REMARK 470 ILE C 148 CG1 CG2 CD1
REMARK 470 LEU C 169 CG CD1 CD2
REMARK 470 GLU C 172 CG CD OE1 OE2
REMARK 470 MET C 175 CG SD CE
REMARK 470 THR C 178 OG1 CG2
REMARK 470 TYR C 179 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 CYS C 181 SG
REMARK 470 THR C 182 OG1 CG2
REMARK 470 THR C 184 OG1 CG2
REMARK 470 ARG C 185 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 186 CG CD CE NZ
REMARK 470 ARG C 187 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 189 CG CD NE CZ NH1 NH2
REMARK 470 ASN C 199 CG OD1 ND2
REMARK 470 ARG C 200 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 201 CG CD NE CZ NH1 NH2
REMARK 470 SER C 202 OG
REMARK 470 ARG C 204 CG CD NE CZ NH1 NH2
REMARK 470 ASN C 205 CG OD1 ND2
REMARK 470 THR C 206 OG1 CG2
REMARK 470 SER C 207 OG
REMARK 470 MET C 230 CG SD CE
REMARK 470 ARG C 231 CG CD NE CZ NH1 NH2
REMARK 470 HIS C 234 CG ND1 CD2 CE1 NE2
REMARK 470 LYS C 237 CG CD CE NZ
REMARK 470 ASP C 247 CG OD1 OD2
REMARK 470 SER C 249 OG
REMARK 470 LYS C 271 CG CD CE NZ
REMARK 470 GLU C 320 CG CD OE1 OE2
REMARK 470 GLU C 347 CG CD OE1 OE2
REMARK 470 MET C 359 CG SD CE
REMARK 470 MET C 361 CG SD CE
REMARK 470 TYR C 366 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU C 368 CG CD1 CD2
REMARK 470 TRP C 413 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP C 413 CZ3 CH2
REMARK 470 PRO C 423 CG CD
REMARK 470 ILE C 426 CG1 CG2 CD1
REMARK 470 LEU C 427 CG CD1 CD2
REMARK 470 MET C 428 CG SD CE
REMARK 470 LEU C 429 CG CD1 CD2
REMARK 470 GLU C 430 CG CD OE1 OE2
REMARK 470 TYR C 431 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS C 432 CG CD CE NZ
REMARK 470 THR C 433 OG1 CG2
REMARK 470 LYS C 434 CG CD CE NZ
REMARK 470 GLU C 436 CG CD OE1 OE2
REMARK 470 MET C 437 CG SD CE
REMARK 470 SER C 438 OG
REMARK 470 HIS C 439 CG ND1 CD2 CE1 NE2
REMARK 470 ILE C 440 CG1 CG2 CD1
REMARK 470 PRO C 441 CG CD
REMARK 470 GLN C 442 CG CD OE1 NE2
REMARK 470 SER C 443 OG
REMARK 470 GLN C 444 CG CD OE1 NE2
REMARK 470 ASP C 445 CG OD1 OD2
REMARK 470 HIS C 447 CG ND1 CD2 CE1 NE2
REMARK 470 GLN C 448 CG CD OE1 NE2
REMARK 470 TYR C 578 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS C 601 CG CD CE NZ
REMARK 470 TRP C 602 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP C 602 CZ3 CH2
REMARK 470 ASN C 603 CG OD1 ND2
REMARK 470 TYR C 604 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE C 605 CG1 CG2 CD1
REMARK 470 ASN C 606 CG OD1 ND2
REMARK 470 TYR C 608 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASN C 610 CG OD1 ND2
REMARK 470 HIS C 611 CG ND1 CD2 CE1 NE2
REMARK 470 VAL C 612 CG1 CG2
REMARK 470 PRO C 784 CG CD
REMARK 470 PRO C 785 CG CD
REMARK 470 PRO C 786 CG CD
REMARK 470 LEU C 787 CG CD1 CD2
REMARK 470 ILE C 788 CG1 CG2 CD1
REMARK 470 ILE C 789 CG1 CG2 CD1
REMARK 470 LEU C 790 CG CD1 CD2
REMARK 470 SER C 791 OG
REMARK 470 HIS C 792 CG ND1 CD2 CE1 NE2
REMARK 470 ILE C 793 CG1 CG2 CD1
REMARK 470 PRO C 813 CG CD
REMARK 470 LYS C 814 CG CD CE NZ
REMARK 470 LEU C 815 CG CD1 CD2
REMARK 470 LEU C 817 CG CD1 CD2
REMARK 470 THR C 818 OG1 CG2
REMARK 470 LEU C 880 CG CD1 CD2
REMARK 470 GLN C 881 CG CD OE1 NE2
REMARK 470 SER C 882 OG
REMARK 470 LEU C 883 CG CD1 CD2
REMARK 470 ASP C 884 CG OD1 OD2
REMARK 470 SER C 885 OG
REMARK 470 LYS D 305 CG CD CE NZ
REMARK 470 PHE D 306 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PRO D 310 CG CD
REMARK 470 ARG D 311 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 313 CG CD OE1 OE2
REMARK 470 LEU D 315 CG CD1 CD2
REMARK 470 LYS D 319 CG CD CE NZ
REMARK 470 GLN D 320 CG CD OE1 NE2
REMARK 470 PRO D 322 CG CD
REMARK 470 PRO D 325 CG CD
REMARK 470 MET D 326 CG SD CE
REMARK 470 LEU D 327 CG CD1 CD2
REMARK 470 PHE D 328 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU D 330 CG CD1 CD2
REMARK 470 ILE D 331 CG1 CG2 CD1
REMARK 470 LEU D 347 CG CD1 CD2
REMARK 470 ILE D 348 CG1 CG2 CD1
REMARK 470 LEU D 352 CG CD1 CD2
REMARK 470 GLU D 355 CG CD OE1 OE2
REMARK 470 MET D 358 CG SD CE
REMARK 470 THR D 361 OG1 CG2
REMARK 470 TYR D 362 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG D 363 CG CD NE CZ NH1 NH2
REMARK 470 CYS D 364 SG
REMARK 470 THR D 365 OG1 CG2
REMARK 470 THR D 367 OG1 CG2
REMARK 470 ARG D 368 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 369 CG CD CE NZ
REMARK 470 ARG D 370 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 372 CG CD NE CZ NH1 NH2
REMARK 470 ASN D 382 CG OD1 ND2
REMARK 470 ARG D 383 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 384 CG CD NE CZ NH1 NH2
REMARK 470 SER D 385 OG
REMARK 470 ARG D 387 CG CD NE CZ NH1 NH2
REMARK 470 ASN D 388 CG OD1 ND2
REMARK 470 THR D 389 OG1 CG2
REMARK 470 SER D 390 OG
REMARK 470 MET D 413 CG SD CE
REMARK 470 ARG D 414 CG CD NE CZ NH1 NH2
REMARK 470 ASN D 416 CG OD1 ND2
REMARK 470 HIS D 417 CG ND1 CD2 CE1 NE2
REMARK 470 LYS D 420 CG CD CE NZ
REMARK 470 ASP D 430 CG OD1 OD2
REMARK 470 SER D 432 OG
REMARK 470 MET D 433 CG SD CE
REMARK 470 GLU D 484 CG CD OE1 OE2
REMARK 470 GLU D 485 CG CD OE1 OE2
REMARK 470 GLU D 503 CG CD OE1 OE2
REMARK 470 GLU D 515 CG CD OE1 OE2
REMARK 470 GLU D 516 CG CD OE1 OE2
REMARK 470 ASP D 523 CG OD1 OD2
REMARK 470 GLU D 530 CG CD OE1 OE2
REMARK 470 ASP D 539 CG OD1 OD2
REMARK 470 GLU D 540 CG CD OE1 OE2
REMARK 470 MET D 542 CG SD CE
REMARK 470 MET D 544 CG SD CE
REMARK 470 TYR D 549 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TRP D 596 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP D 596 CZ3 CH2
REMARK 470 ILE D 609 CG1 CG2 CD1
REMARK 470 LEU D 610 CG CD1 CD2
REMARK 470 MET D 611 CG SD CE
REMARK 470 LEU D 612 CG CD1 CD2
REMARK 470 GLU D 613 CG CD OE1 OE2
REMARK 470 TYR D 614 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS D 615 CG CD CE NZ
REMARK 470 THR D 616 OG1 CG2
REMARK 470 LYS D 617 CG CD CE NZ
REMARK 470 GLU D 619 CG CD OE1 OE2
REMARK 470 MET D 620 CG SD CE
REMARK 470 SER D 621 OG
REMARK 470 HIS D 622 CG ND1 CD2 CE1 NE2
REMARK 470 ILE D 623 CG1 CG2 CD1
REMARK 470 PRO D 624 CG CD
REMARK 470 GLN D 625 CG CD OE1 NE2
REMARK 470 SER D 626 OG
REMARK 470 GLN D 627 CG CD OE1 NE2
REMARK 470 ASP D 628 CG OD1 OD2
REMARK 470 HIS D 630 CG ND1 CD2 CE1 NE2
REMARK 470 GLN D 631 CG CD OE1 NE2
REMARK 470 TYR D 761 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS D 784 CG CD CE NZ
REMARK 470 TRP D 785 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP D 785 CZ3 CH2
REMARK 470 ASN D 786 CG OD1 ND2
REMARK 470 TYR D 787 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE D 788 CG1 CG2 CD1
REMARK 470 ASN D 789 CG OD1 ND2
REMARK 470 TYR D 791 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASN D 793 CG OD1 ND2
REMARK 470 HIS D 794 CG ND1 CD2 CE1 NE2
REMARK 470 VAL D 795 CG1 CG2
REMARK 470 PRO D 967 CG CD
REMARK 470 PRO D 968 CG CD
REMARK 470 PRO D 969 CG CD
REMARK 470 LEU D 970 CG CD1 CD2
REMARK 470 ILE D 971 CG1 CG2 CD1
REMARK 470 ILE D 972 CG1 CG2 CD1
REMARK 470 LEU D 973 CG CD1 CD2
REMARK 470 SER D 974 OG
REMARK 470 HIS D 975 CG ND1 CD2 CE1 NE2
REMARK 470 ILE D 976 CG1 CG2 CD1
REMARK 470 PRO D 996 CG CD
REMARK 470 LYS D 997 CG CD CE NZ
REMARK 470 LEU D 998 CG CD1 CD2
REMARK 470 LEU D1000 CG CD1 CD2
REMARK 470 THR D1001 OG1 CG2
REMARK 470 LEU D1063 CG CD1 CD2
REMARK 470 GLN D1064 CG CD OE1 NE2
REMARK 470 SER D1065 OG
REMARK 470 LEU D1066 CG CD1 CD2
REMARK 470 ASP D1067 CG OD1 OD2
REMARK 470 SER D1068 OG
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 MG MG D 1201 O HOH D 1307 1.25
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 PRO A 310 N - CA - CB ANGL. DEV. = 7.2 DEGREES
REMARK 500 LEU A 562 CA - CB - CG ANGL. DEV. = 14.6 DEGREES
REMARK 500 LEU A 568 CA - CB - CG ANGL. DEV. = 18.0 DEGREES
REMARK 500 LEU A 818 CA - CB - CG ANGL. DEV. = 13.8 DEGREES
REMARK 500 HIS A 961 N - CA - C ANGL. DEV. = 17.7 DEGREES
REMARK 500 PRO A 996 N - CA - CB ANGL. DEV. = 8.2 DEGREES
REMARK 500 LEU B 562 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500 LEU B 568 CA - CB - CG ANGL. DEV. = 18.0 DEGREES
REMARK 500 LEU B 818 CA - CB - CG ANGL. DEV. = 13.8 DEGREES
REMARK 500 HIS B 961 N - CA - C ANGL. DEV. = 17.7 DEGREES
REMARK 500 PRO B 996 N - CA - CB ANGL. DEV. = 8.2 DEGREES
REMARK 500 PRO C 127 N - CA - CB ANGL. DEV. = 7.3 DEGREES
REMARK 500 GLY C 168 C - N - CA ANGL. DEV. = 18.5 DEGREES
REMARK 500 GLY C 168 N - CA - C ANGL. DEV. = 17.8 DEGREES
REMARK 500 LEU C 379 CA - CB - CG ANGL. DEV. = 14.6 DEGREES
REMARK 500 LEU C 385 CA - CB - CG ANGL. DEV. = 18.0 DEGREES
REMARK 500 LEU C 635 CA - CB - CG ANGL. DEV. = 13.8 DEGREES
REMARK 500 HIS C 778 N - CA - C ANGL. DEV. = 17.7 DEGREES
REMARK 500 PRO C 813 N - CA - CB ANGL. DEV. = 8.2 DEGREES
REMARK 500 PRO D 310 N - CA - CB ANGL. DEV. = 7.3 DEGREES
REMARK 500 LEU D 562 CA - CB - CG ANGL. DEV. = 14.6 DEGREES
REMARK 500 LEU D 568 CA - CB - CG ANGL. DEV. = 18.0 DEGREES
REMARK 500 LEU D 818 CA - CB - CG ANGL. DEV. = 13.8 DEGREES
REMARK 500 HIS D 961 N - CA - C ANGL. DEV. = 17.6 DEGREES
REMARK 500 PRO D 996 N - CA - CB ANGL. DEV. = 8.2 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 UNK A 232 30.65 -95.22
REMARK 500 UNK A 267 68.32 61.33
REMARK 500 UNK A 272 78.04 50.20
REMARK 500 UNK A 300 119.84 132.76
REMARK 500 UNK A 301 148.42 -174.16
REMARK 500 MET A 326 53.07 -94.11
REMARK 500 PHE A 328 -12.25 74.40
REMARK 500 LEU A 352 61.62 39.18
REMARK 500 ILE A 354 -11.94 52.44
REMARK 500 GLU A 355 -12.00 -143.82
REMARK 500 THR A 361 75.34 53.31
REMARK 500 THR A 367 70.61 59.65
REMARK 500 HIS A 415 30.41 -88.23
REMARK 500 MET A 433 120.95 72.31
REMARK 500 GLN A 481 60.54 38.31
REMARK 500 HIS A 482 114.67 -160.73
REMARK 500 LEU A 562 77.00 66.77
REMARK 500 LEU A 568 -84.96 -67.93
REMARK 500 ARG A 569 -57.08 -122.31
REMARK 500 CYS A 576 -75.48 -53.22
REMARK 500 PRO A 607 14.31 -54.47
REMARK 500 LYS A 715 74.07 47.57
REMARK 500 VAL A 722 -60.46 -132.00
REMARK 500 ASN A 789 79.78 -101.26
REMARK 500 TYR A 791 70.11 59.25
REMARK 500 VAL A 795 -169.55 -100.56
REMARK 500 PHE A 796 -25.17 71.44
REMARK 500 ALA A 819 37.65 -99.08
REMARK 500 ARG A 856 -60.83 -90.48
REMARK 500 ASN A 896 30.84 -94.82
REMARK 500 ASN A 928 -33.22 -134.87
REMARK 500 ASN A 935 -38.30 -134.15
REMARK 500 GLU A 962 14.13 -143.08
REMARK 500 LEU A 998 148.51 -172.75
REMARK 500 PHE A 999 -165.20 -160.34
REMARK 500 LEU A1000 -59.28 -123.29
REMARK 500 UNK B 232 30.62 -95.23
REMARK 500 UNK B 267 68.36 61.33
REMARK 500 UNK B 272 78.07 50.21
REMARK 500 UNK B 300 119.82 132.71
REMARK 500 UNK B 301 148.44 -174.15
REMARK 500 MET B 326 53.05 -95.64
REMARK 500 PHE B 328 -12.27 74.37
REMARK 500 THR B 361 75.27 53.33
REMARK 500 THR B 367 70.62 59.68
REMARK 500 HIS B 415 30.46 -88.21
REMARK 500 SER B 432 34.86 72.53
REMARK 500 MET B 433 106.09 61.82
REMARK 500 GLN B 481 60.56 38.20
REMARK 500 HIS B 482 114.65 -160.71
REMARK 500
REMARK 500 THIS ENTRY HAS 139 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 UNK A 270 UNK A 271 -84.29
REMARK 500 UNK A 272 UNK A 273 -43.17
REMARK 500 ILE A 350 GLY A 351 -38.47
REMARK 500 VAL A 353 ILE A 354 126.35
REMARK 500 THR A 361 TYR A 362 37.00
REMARK 500 ARG A 372 LEU A 373 -30.28
REMARK 500 PHE A 418 ILE A 419 143.10
REMARK 500 TRP A 480 GLN A 481 45.40
REMARK 500 LEU A 517 LYS A 518 149.04
REMARK 500 GLN A 519 TYR A 520 148.25
REMARK 500 TRP A 554 SER A 555 -147.79
REMARK 500 LYS A 561 LEU A 562 -137.26
REMARK 500 SER A 566 ARG A 567 -144.52
REMARK 500 ARG A 567 LEU A 568 -139.94
REMARK 500 LEU A 568 ARG A 569 84.41
REMARK 500 PRO A 570 PHE A 571 39.22
REMARK 500 VAL A 714 LYS A 715 148.93
REMARK 500 LEU A 719 PRO A 720 -142.71
REMARK 500 GLY A 778 LEU A 779 147.78
REMARK 500 LEU A 779 ARG A 780 40.35
REMARK 500 ASP A 792 ASN A 793 -33.08
REMARK 500 MET A 881 ILE A 882 143.14
REMARK 500 ILE A 882 PHE A 883 43.29
REMARK 500 ILE A 925 MET A 926 147.67
REMARK 500 TYR A 960 HIS A 961 -35.38
REMARK 500 ASN A 1028 SER A 1029 -99.12
REMARK 500 UNK B 270 UNK B 271 -84.30
REMARK 500 UNK B 272 UNK B 273 -43.13
REMARK 500 ILE B 350 GLY B 351 -40.75
REMARK 500 THR B 361 TYR B 362 37.06
REMARK 500 ARG B 372 LEU B 373 -30.18
REMARK 500 LYS B 412 MET B 413 -83.09
REMARK 500 PHE B 418 ILE B 419 143.08
REMARK 500 TRP B 480 GLN B 481 45.51
REMARK 500 LEU B 517 LYS B 518 149.03
REMARK 500 GLN B 519 TYR B 520 148.27
REMARK 500 TRP B 554 SER B 555 -147.79
REMARK 500 LYS B 561 LEU B 562 -137.20
REMARK 500 SER B 566 ARG B 567 -144.53
REMARK 500 ARG B 567 LEU B 568 -139.97
REMARK 500 LEU B 568 ARG B 569 84.36
REMARK 500 PRO B 570 PHE B 571 39.23
REMARK 500 VAL B 714 LYS B 715 149.00
REMARK 500 LEU B 719 PRO B 720 -142.73
REMARK 500 GLY B 778 LEU B 779 147.72
REMARK 500 LEU B 779 ARG B 780 40.45
REMARK 500 ASP B 792 ASN B 793 -33.08
REMARK 500 MET B 881 ILE B 882 143.19
REMARK 500 ILE B 882 PHE B 883 43.21
REMARK 500 ILE B 925 MET B 926 147.63
REMARK 500
REMARK 500 THIS ENTRY HAS 104 NON CIS, NON-TRANS OMEGA OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ILE C 167 11.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1304 O
REMARK 620 2 HOH B1301 O 131.3
REMARK 620 3 HOH C1404 O 150.6 68.4
REMARK 620 4 HOH D1303 O 83.3 119.0 67.4
REMARK 620 5 HOH D1305 O 91.0 65.4 78.0 66.1
REMARK 620 6 HOH D1308 O 86.3 127.3 96.6 97.6 163.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1302 O
REMARK 620 2 HOH B1304 O 83.8
REMARK 620 3 HOH C1405 O 173.3 89.5
REMARK 620 4 HOH D1304 O 93.7 175.8 92.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1303 O
REMARK 620 2 HOH B1303 O 75.7
REMARK 620 3 HOH B1306 O 161.4 97.9
REMARK 620 4 HOH C1403 O 114.6 84.4 81.6
REMARK 620 5 HOH D1302 O 72.1 128.3 123.5 74.0
REMARK 620 6 HOH D1309 O 79.9 120.4 88.7 154.5 92.4
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 A 1203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 A 1204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 A 1205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 A 1206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 A 1207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 A 1208
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 B 1203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 B 1204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 B 1205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 B 1206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 C 1301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 C 1302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 C 1303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 C 1304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 C 1305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 C 1306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 C 1307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 C 1308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 D 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 D 1203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-7297 RELATED DB: EMDB
REMARK 900 3.7 ANGSTROM CRYOEM STRUCTURE OF TRUNCATED MOUSE TRPM7
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE FULL SAMPLE SEQUENCE IS
REMARK 999 MSQKSWIESTLTKRECVYIIPSSKDPHRCLPGCQICQQLVRCFCGRLVKQHACFTASLAMKYSDV
REMARK 999 KLGEHFNQAIEEWSVEKHTEQSPTDAYGVINFQGGSHSYRAKYVRLSYDTKPEIILQLLLKEWQM
REMARK 999 ELPKLVISVHGGMQKFELHPRIKQLLGKGLIKAAVTTGAWILTGGVNTGVAKHVGDALKEHASRS
REMARK 999 SRKICTIGIAPWGVIENRNDLVGRDVVAPYQTLLNPLSKLNVLNNLHSHFILVDDGTVGKYGAEV
REMARK 999 RLRRELEKTINQQRIHARIGQGVPVVALIFEGGPNVILTVLEYLQESPPVPVVVCEGTGRAADLL
REMARK 999 AYIHKQTEEGGNLPDAAEPDIISTIKKTFNFGQSEAVHLFQTMMECMKKKELITVFHIGSEDHQD
REMARK 999 IDVAILTALLKGTNASAFDQLILTLAWDRVDIAKNHVFVYGQQWLVGSLEQAMLDALVMDRVSFV
REMARK 999 KLLIENGVSMHKFLTIPRLEELYNTKQGPTNPMLFHLIRDVKQGNLPPGYKITLIDIGLVIEYLM
REMARK 999 GGTYRCTYTRKRFRLIYNSLGGNNRRSGRNTSSSTPQLRKSHETFGNRADKKEKMRHNHFIKTAQ
REMARK 999 PYRPKMDASMEEGKKKRTKDEIVDIDDPETKRFPYPLNELLIWACLMKRQVMARFLWQHGEESMA
REMARK 999 KALVACKIYRSMAYEAKQSDLVDDTSEELKQYSNDFGQLAVELLEQSFRQDETMAMKLLTYELKN
REMARK 999 WSNSTCLKLAVSSRLRPFVAHTCTQMLLSDMWMGRLNMRKNSWYKVILSILVPPAILMLEYKTKA
REMARK 999 EMSHIPQSQDAHQMTMEDSENNFHNITEEIPMEVFKEVKILDSSDGKNEMEIHIKSKKLPITRKF
REMARK 999 YAFYHAPIVKFWFNTLAYLGFLMLYTFVVLVKMEQLPSVQEWIVIAYIFTYAIEKVREVFMSEAG
REMARK 999 KISQKIKVWFSDYFNVSDTIAIISFFVGFGLRFGAKWNYINAYDNHVFVAGRLIYCLNIIFWYVR
REMARK 999 LLDFLAVNQQAGPYVMMIGKMVANMFYIVVIMALVLLSFGVPRKAILYPHEEPSWSLAKDIVFHP
REMARK 999 YWMIFGEVYAYEIDVCANDSTLPTICGPGTWLTPFLQAVYLFVQYIIMVNLLIAFFNNVYLQVKA
REMARK 999 ISNIVWKYQRYHFIMAYHEKPVLPPPLIILSHIVSLFCCVCKRRKKDKTSDGPKLFLTEEDQKKL
REMARK 999 HDFEEQCVEMYFDEKDDKFNSGSEERIRVTFERVEQMSIQIKEVGDRVNYIKRSLQSLDSQIGHL
REMARK 999 QDLSALTVDTLKTLTAQKASEASKVHNEITRELSISKHLAQNLIDDVPVRPLWKKPSAVNTLSSS
DBREF 6BWD A 1 1138 PDB 6BWD 6BWD 1 1138
DBREF 6BWD B 1 1138 PDB 6BWD 6BWD 1 1138
DBREF 6BWD C 1 955 PDB 6BWD 6BWD 1 955
DBREF 6BWD D 1 1138 PDB 6BWD 6BWD 1 1138
SEQRES 1 A 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 2 A 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 3 A 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 4 A 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 5 A 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 6 A 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 7 A 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 8 A 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 9 A 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 10 A 955 UNK UNK UNK UNK LYS PHE LEU THR ILE PRO ARG LEU GLU
SEQRES 11 A 955 GLU LEU TYR ASN THR LYS GLN GLY PRO THR ASN PRO MET
SEQRES 12 A 955 LEU PHE HIS LEU ILE ARG ASP VAL LYS GLN GLY ASN LEU
SEQRES 13 A 955 PRO PRO GLY TYR LYS ILE THR LEU ILE ASP ILE GLY LEU
SEQRES 14 A 955 VAL ILE GLU TYR LEU MET GLY GLY THR TYR ARG CYS THR
SEQRES 15 A 955 TYR THR ARG LYS ARG PHE ARG LEU ILE TYR ASN SER LEU
SEQRES 16 A 955 GLY GLY ASN ASN ARG ARG SER GLY ARG ASN THR SER SER
SEQRES 17 A 955 SER THR PRO GLN LEU ARG LYS SER HIS GLU THR PHE GLY
SEQRES 18 A 955 ASN ARG ALA ASP LYS LYS GLU LYS MET ARG HIS ASN HIS
SEQRES 19 A 955 PHE ILE LYS THR ALA GLN PRO TYR ARG PRO LYS MET ASP
SEQRES 20 A 955 ALA SER MET GLU GLU GLY LYS LYS LYS ARG THR LYS ASP
SEQRES 21 A 955 GLU ILE VAL ASP ILE ASP ASP PRO GLU THR LYS ARG PHE
SEQRES 22 A 955 PRO TYR PRO LEU ASN GLU LEU LEU ILE TRP ALA CYS LEU
SEQRES 23 A 955 MET LYS ARG GLN VAL MET ALA ARG PHE LEU TRP GLN HIS
SEQRES 24 A 955 GLY GLU GLU SER MET ALA LYS ALA LEU VAL ALA CYS LYS
SEQRES 25 A 955 ILE TYR ARG SER MET ALA TYR GLU ALA LYS GLN SER ASP
SEQRES 26 A 955 LEU VAL ASP ASP THR SER GLU GLU LEU LYS GLN TYR SER
SEQRES 27 A 955 ASN ASP PHE GLY GLN LEU ALA VAL GLU LEU LEU GLU GLN
SEQRES 28 A 955 SER PHE ARG GLN ASP GLU THR MET ALA MET LYS LEU LEU
SEQRES 29 A 955 THR TYR GLU LEU LYS ASN TRP SER ASN SER THR CYS LEU
SEQRES 30 A 955 LYS LEU ALA VAL SER SER ARG LEU ARG PRO PHE VAL ALA
SEQRES 31 A 955 HIS THR CYS THR GLN MET LEU LEU SER ASP MET TRP MET
SEQRES 32 A 955 GLY ARG LEU ASN MET ARG LYS ASN SER TRP TYR LYS VAL
SEQRES 33 A 955 ILE LEU SER ILE LEU VAL PRO PRO ALA ILE LEU MET LEU
SEQRES 34 A 955 GLU TYR LYS THR LYS ALA GLU MET SER HIS ILE PRO GLN
SEQRES 35 A 955 SER GLN ASP ALA HIS GLN MET THR MET GLU ASP SER GLU
SEQRES 36 A 955 ASN ASN PHE HIS ASN ILE THR GLU GLU ILE PRO MET GLU
SEQRES 37 A 955 VAL PHE LYS GLU VAL LYS ILE LEU ASP SER SER ASP GLY
SEQRES 38 A 955 LYS ASN GLU MET GLU ILE HIS ILE LYS SER LYS LYS LEU
SEQRES 39 A 955 PRO ILE THR ARG LYS PHE TYR ALA PHE TYR HIS ALA PRO
SEQRES 40 A 955 ILE VAL LYS PHE TRP PHE ASN THR LEU ALA TYR LEU GLY
SEQRES 41 A 955 PHE LEU MET LEU TYR THR PHE VAL VAL LEU VAL LYS MET
SEQRES 42 A 955 GLU GLN LEU PRO SER VAL GLN GLU TRP ILE VAL ILE ALA
SEQRES 43 A 955 TYR ILE PHE THR TYR ALA ILE GLU LYS VAL ARG GLU VAL
SEQRES 44 A 955 PHE MET SER GLU ALA GLY LYS ILE SER GLN LYS ILE LYS
SEQRES 45 A 955 VAL TRP PHE SER ASP TYR PHE ASN VAL SER ASP THR ILE
SEQRES 46 A 955 ALA ILE ILE SER PHE PHE VAL GLY PHE GLY LEU ARG PHE
SEQRES 47 A 955 GLY ALA LYS TRP ASN TYR ILE ASN ALA TYR ASP ASN HIS
SEQRES 48 A 955 VAL PHE VAL ALA GLY ARG LEU ILE TYR CYS LEU ASN ILE
SEQRES 49 A 955 ILE PHE TRP TYR VAL ARG LEU LEU ASP PHE LEU ALA VAL
SEQRES 50 A 955 ASN GLN GLN ALA GLY PRO TYR VAL MET MET ILE GLY LYS
SEQRES 51 A 955 MET VAL ALA ASN MET PHE TYR ILE VAL VAL ILE MET ALA
SEQRES 52 A 955 LEU VAL LEU LEU SER PHE GLY VAL PRO ARG LYS ALA ILE
SEQRES 53 A 955 LEU TYR PRO HIS GLU GLU PRO SER TRP SER LEU ALA LYS
SEQRES 54 A 955 ASP ILE VAL PHE HIS PRO TYR TRP MET ILE PHE GLY GLU
SEQRES 55 A 955 VAL TYR ALA TYR GLU ILE ASP VAL CYS ALA ASN ASP SER
SEQRES 56 A 955 THR LEU PRO THR ILE CYS GLY PRO GLY THR TRP LEU THR
SEQRES 57 A 955 PRO PHE LEU GLN ALA VAL TYR LEU PHE VAL GLN TYR ILE
SEQRES 58 A 955 ILE MET VAL ASN LEU LEU ILE ALA PHE PHE ASN ASN VAL
SEQRES 59 A 955 TYR LEU GLN VAL LYS ALA ILE SER ASN ILE VAL TRP LYS
SEQRES 60 A 955 TYR GLN ARG TYR HIS PHE ILE MET ALA TYR HIS GLU LYS
SEQRES 61 A 955 PRO VAL LEU PRO PRO PRO LEU ILE ILE LEU SER HIS ILE
SEQRES 62 A 955 VAL SER LEU PHE CYS CYS VAL CYS LYS ARG ARG LYS LYS
SEQRES 63 A 955 ASP LYS THR SER ASP GLY PRO LYS LEU PHE LEU THR GLU
SEQRES 64 A 955 GLU ASP GLN LYS LYS LEU HIS ASP PHE GLU GLU GLN CYS
SEQRES 65 A 955 VAL GLU MET TYR PHE ASP GLU LYS ASP ASP LYS PHE ASN
SEQRES 66 A 955 SER GLY SER GLU GLU ARG ILE ARG VAL THR PHE GLU ARG
SEQRES 67 A 955 VAL GLU GLN MET SER ILE GLN ILE LYS GLU VAL GLY ASP
SEQRES 68 A 955 ARG VAL ASN TYR ILE LYS ARG SER LEU GLN SER LEU ASP
SEQRES 69 A 955 SER GLN ILE GLY HIS LEU GLN ASP LEU SER ALA LEU THR
SEQRES 70 A 955 VAL ASP THR LEU LYS THR LEU THR ALA GLN LYS ALA SER
SEQRES 71 A 955 GLU ALA SER LYS VAL HIS ASN GLU ILE THR ARG GLU LEU
SEQRES 72 A 955 SER ILE SER LYS HIS LEU ALA GLN ASN LEU ILE ASP ASP
SEQRES 73 A 955 VAL PRO VAL ARG PRO LEU TRP LYS LYS PRO SER ALA VAL
SEQRES 74 A 955 ASN THR LEU SER SER SER
SEQRES 1 B 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 2 B 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 3 B 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 4 B 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 5 B 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 6 B 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 7 B 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 8 B 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 9 B 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 10 B 955 UNK UNK UNK UNK LYS PHE LEU THR ILE PRO ARG LEU GLU
SEQRES 11 B 955 GLU LEU TYR ASN THR LYS GLN GLY PRO THR ASN PRO MET
SEQRES 12 B 955 LEU PHE HIS LEU ILE ARG ASP VAL LYS GLN GLY ASN LEU
SEQRES 13 B 955 PRO PRO GLY TYR LYS ILE THR LEU ILE ASP ILE GLY LEU
SEQRES 14 B 955 VAL ILE GLU TYR LEU MET GLY GLY THR TYR ARG CYS THR
SEQRES 15 B 955 TYR THR ARG LYS ARG PHE ARG LEU ILE TYR ASN SER LEU
SEQRES 16 B 955 GLY GLY ASN ASN ARG ARG SER GLY ARG ASN THR SER SER
SEQRES 17 B 955 SER THR PRO GLN LEU ARG LYS SER HIS GLU THR PHE GLY
SEQRES 18 B 955 ASN ARG ALA ASP LYS LYS GLU LYS MET ARG HIS ASN HIS
SEQRES 19 B 955 PHE ILE LYS THR ALA GLN PRO TYR ARG PRO LYS MET ASP
SEQRES 20 B 955 ALA SER MET GLU GLU GLY LYS LYS LYS ARG THR LYS ASP
SEQRES 21 B 955 GLU ILE VAL ASP ILE ASP ASP PRO GLU THR LYS ARG PHE
SEQRES 22 B 955 PRO TYR PRO LEU ASN GLU LEU LEU ILE TRP ALA CYS LEU
SEQRES 23 B 955 MET LYS ARG GLN VAL MET ALA ARG PHE LEU TRP GLN HIS
SEQRES 24 B 955 GLY GLU GLU SER MET ALA LYS ALA LEU VAL ALA CYS LYS
SEQRES 25 B 955 ILE TYR ARG SER MET ALA TYR GLU ALA LYS GLN SER ASP
SEQRES 26 B 955 LEU VAL ASP ASP THR SER GLU GLU LEU LYS GLN TYR SER
SEQRES 27 B 955 ASN ASP PHE GLY GLN LEU ALA VAL GLU LEU LEU GLU GLN
SEQRES 28 B 955 SER PHE ARG GLN ASP GLU THR MET ALA MET LYS LEU LEU
SEQRES 29 B 955 THR TYR GLU LEU LYS ASN TRP SER ASN SER THR CYS LEU
SEQRES 30 B 955 LYS LEU ALA VAL SER SER ARG LEU ARG PRO PHE VAL ALA
SEQRES 31 B 955 HIS THR CYS THR GLN MET LEU LEU SER ASP MET TRP MET
SEQRES 32 B 955 GLY ARG LEU ASN MET ARG LYS ASN SER TRP TYR LYS VAL
SEQRES 33 B 955 ILE LEU SER ILE LEU VAL PRO PRO ALA ILE LEU MET LEU
SEQRES 34 B 955 GLU TYR LYS THR LYS ALA GLU MET SER HIS ILE PRO GLN
SEQRES 35 B 955 SER GLN ASP ALA HIS GLN MET THR MET GLU ASP SER GLU
SEQRES 36 B 955 ASN ASN PHE HIS ASN ILE THR GLU GLU ILE PRO MET GLU
SEQRES 37 B 955 VAL PHE LYS GLU VAL LYS ILE LEU ASP SER SER ASP GLY
SEQRES 38 B 955 LYS ASN GLU MET GLU ILE HIS ILE LYS SER LYS LYS LEU
SEQRES 39 B 955 PRO ILE THR ARG LYS PHE TYR ALA PHE TYR HIS ALA PRO
SEQRES 40 B 955 ILE VAL LYS PHE TRP PHE ASN THR LEU ALA TYR LEU GLY
SEQRES 41 B 955 PHE LEU MET LEU TYR THR PHE VAL VAL LEU VAL LYS MET
SEQRES 42 B 955 GLU GLN LEU PRO SER VAL GLN GLU TRP ILE VAL ILE ALA
SEQRES 43 B 955 TYR ILE PHE THR TYR ALA ILE GLU LYS VAL ARG GLU VAL
SEQRES 44 B 955 PHE MET SER GLU ALA GLY LYS ILE SER GLN LYS ILE LYS
SEQRES 45 B 955 VAL TRP PHE SER ASP TYR PHE ASN VAL SER ASP THR ILE
SEQRES 46 B 955 ALA ILE ILE SER PHE PHE VAL GLY PHE GLY LEU ARG PHE
SEQRES 47 B 955 GLY ALA LYS TRP ASN TYR ILE ASN ALA TYR ASP ASN HIS
SEQRES 48 B 955 VAL PHE VAL ALA GLY ARG LEU ILE TYR CYS LEU ASN ILE
SEQRES 49 B 955 ILE PHE TRP TYR VAL ARG LEU LEU ASP PHE LEU ALA VAL
SEQRES 50 B 955 ASN GLN GLN ALA GLY PRO TYR VAL MET MET ILE GLY LYS
SEQRES 51 B 955 MET VAL ALA ASN MET PHE TYR ILE VAL VAL ILE MET ALA
SEQRES 52 B 955 LEU VAL LEU LEU SER PHE GLY VAL PRO ARG LYS ALA ILE
SEQRES 53 B 955 LEU TYR PRO HIS GLU GLU PRO SER TRP SER LEU ALA LYS
SEQRES 54 B 955 ASP ILE VAL PHE HIS PRO TYR TRP MET ILE PHE GLY GLU
SEQRES 55 B 955 VAL TYR ALA TYR GLU ILE ASP VAL CYS ALA ASN ASP SER
SEQRES 56 B 955 THR LEU PRO THR ILE CYS GLY PRO GLY THR TRP LEU THR
SEQRES 57 B 955 PRO PHE LEU GLN ALA VAL TYR LEU PHE VAL GLN TYR ILE
SEQRES 58 B 955 ILE MET VAL ASN LEU LEU ILE ALA PHE PHE ASN ASN VAL
SEQRES 59 B 955 TYR LEU GLN VAL LYS ALA ILE SER ASN ILE VAL TRP LYS
SEQRES 60 B 955 TYR GLN ARG TYR HIS PHE ILE MET ALA TYR HIS GLU LYS
SEQRES 61 B 955 PRO VAL LEU PRO PRO PRO LEU ILE ILE LEU SER HIS ILE
SEQRES 62 B 955 VAL SER LEU PHE CYS CYS VAL CYS LYS ARG ARG LYS LYS
SEQRES 63 B 955 ASP LYS THR SER ASP GLY PRO LYS LEU PHE LEU THR GLU
SEQRES 64 B 955 GLU ASP GLN LYS LYS LEU HIS ASP PHE GLU GLU GLN CYS
SEQRES 65 B 955 VAL GLU MET TYR PHE ASP GLU LYS ASP ASP LYS PHE ASN
SEQRES 66 B 955 SER GLY SER GLU GLU ARG ILE ARG VAL THR PHE GLU ARG
SEQRES 67 B 955 VAL GLU GLN MET SER ILE GLN ILE LYS GLU VAL GLY ASP
SEQRES 68 B 955 ARG VAL ASN TYR ILE LYS ARG SER LEU GLN SER LEU ASP
SEQRES 69 B 955 SER GLN ILE GLY HIS LEU GLN ASP LEU SER ALA LEU THR
SEQRES 70 B 955 VAL ASP THR LEU LYS THR LEU THR ALA GLN LYS ALA SER
SEQRES 71 B 955 GLU ALA SER LYS VAL HIS ASN GLU ILE THR ARG GLU LEU
SEQRES 72 B 955 SER ILE SER LYS HIS LEU ALA GLN ASN LEU ILE ASP ASP
SEQRES 73 B 955 VAL PRO VAL ARG PRO LEU TRP LYS LYS PRO SER ALA VAL
SEQRES 74 B 955 ASN THR LEU SER SER SER
SEQRES 1 C 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 2 C 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 3 C 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 4 C 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 5 C 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 6 C 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 7 C 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 8 C 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 9 C 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 10 C 955 UNK UNK UNK UNK LYS PHE LEU THR ILE PRO ARG LEU GLU
SEQRES 11 C 955 GLU LEU TYR ASN THR LYS GLN GLY PRO THR ASN PRO MET
SEQRES 12 C 955 LEU PHE HIS LEU ILE ARG ASP VAL LYS GLN GLY ASN LEU
SEQRES 13 C 955 PRO PRO GLY TYR LYS ILE THR LEU ILE ASP ILE GLY LEU
SEQRES 14 C 955 VAL ILE GLU TYR LEU MET GLY GLY THR TYR ARG CYS THR
SEQRES 15 C 955 TYR THR ARG LYS ARG PHE ARG LEU ILE TYR ASN SER LEU
SEQRES 16 C 955 GLY GLY ASN ASN ARG ARG SER GLY ARG ASN THR SER SER
SEQRES 17 C 955 SER THR PRO GLN LEU ARG LYS SER HIS GLU THR PHE GLY
SEQRES 18 C 955 ASN ARG ALA ASP LYS LYS GLU LYS MET ARG HIS ASN HIS
SEQRES 19 C 955 PHE ILE LYS THR ALA GLN PRO TYR ARG PRO LYS MET ASP
SEQRES 20 C 955 ALA SER MET GLU GLU GLY LYS LYS LYS ARG THR LYS ASP
SEQRES 21 C 955 GLU ILE VAL ASP ILE ASP ASP PRO GLU THR LYS ARG PHE
SEQRES 22 C 955 PRO TYR PRO LEU ASN GLU LEU LEU ILE TRP ALA CYS LEU
SEQRES 23 C 955 MET LYS ARG GLN VAL MET ALA ARG PHE LEU TRP GLN HIS
SEQRES 24 C 955 GLY GLU GLU SER MET ALA LYS ALA LEU VAL ALA CYS LYS
SEQRES 25 C 955 ILE TYR ARG SER MET ALA TYR GLU ALA LYS GLN SER ASP
SEQRES 26 C 955 LEU VAL ASP ASP THR SER GLU GLU LEU LYS GLN TYR SER
SEQRES 27 C 955 ASN ASP PHE GLY GLN LEU ALA VAL GLU LEU LEU GLU GLN
SEQRES 28 C 955 SER PHE ARG GLN ASP GLU THR MET ALA MET LYS LEU LEU
SEQRES 29 C 955 THR TYR GLU LEU LYS ASN TRP SER ASN SER THR CYS LEU
SEQRES 30 C 955 LYS LEU ALA VAL SER SER ARG LEU ARG PRO PHE VAL ALA
SEQRES 31 C 955 HIS THR CYS THR GLN MET LEU LEU SER ASP MET TRP MET
SEQRES 32 C 955 GLY ARG LEU ASN MET ARG LYS ASN SER TRP TYR LYS VAL
SEQRES 33 C 955 ILE LEU SER ILE LEU VAL PRO PRO ALA ILE LEU MET LEU
SEQRES 34 C 955 GLU TYR LYS THR LYS ALA GLU MET SER HIS ILE PRO GLN
SEQRES 35 C 955 SER GLN ASP ALA HIS GLN MET THR MET GLU ASP SER GLU
SEQRES 36 C 955 ASN ASN PHE HIS ASN ILE THR GLU GLU ILE PRO MET GLU
SEQRES 37 C 955 VAL PHE LYS GLU VAL LYS ILE LEU ASP SER SER ASP GLY
SEQRES 38 C 955 LYS ASN GLU MET GLU ILE HIS ILE LYS SER LYS LYS LEU
SEQRES 39 C 955 PRO ILE THR ARG LYS PHE TYR ALA PHE TYR HIS ALA PRO
SEQRES 40 C 955 ILE VAL LYS PHE TRP PHE ASN THR LEU ALA TYR LEU GLY
SEQRES 41 C 955 PHE LEU MET LEU TYR THR PHE VAL VAL LEU VAL LYS MET
SEQRES 42 C 955 GLU GLN LEU PRO SER VAL GLN GLU TRP ILE VAL ILE ALA
SEQRES 43 C 955 TYR ILE PHE THR TYR ALA ILE GLU LYS VAL ARG GLU VAL
SEQRES 44 C 955 PHE MET SER GLU ALA GLY LYS ILE SER GLN LYS ILE LYS
SEQRES 45 C 955 VAL TRP PHE SER ASP TYR PHE ASN VAL SER ASP THR ILE
SEQRES 46 C 955 ALA ILE ILE SER PHE PHE VAL GLY PHE GLY LEU ARG PHE
SEQRES 47 C 955 GLY ALA LYS TRP ASN TYR ILE ASN ALA TYR ASP ASN HIS
SEQRES 48 C 955 VAL PHE VAL ALA GLY ARG LEU ILE TYR CYS LEU ASN ILE
SEQRES 49 C 955 ILE PHE TRP TYR VAL ARG LEU LEU ASP PHE LEU ALA VAL
SEQRES 50 C 955 ASN GLN GLN ALA GLY PRO TYR VAL MET MET ILE GLY LYS
SEQRES 51 C 955 MET VAL ALA ASN MET PHE TYR ILE VAL VAL ILE MET ALA
SEQRES 52 C 955 LEU VAL LEU LEU SER PHE GLY VAL PRO ARG LYS ALA ILE
SEQRES 53 C 955 LEU TYR PRO HIS GLU GLU PRO SER TRP SER LEU ALA LYS
SEQRES 54 C 955 ASP ILE VAL PHE HIS PRO TYR TRP MET ILE PHE GLY GLU
SEQRES 55 C 955 VAL TYR ALA TYR GLU ILE ASP VAL CYS ALA ASN ASP SER
SEQRES 56 C 955 THR LEU PRO THR ILE CYS GLY PRO GLY THR TRP LEU THR
SEQRES 57 C 955 PRO PHE LEU GLN ALA VAL TYR LEU PHE VAL GLN TYR ILE
SEQRES 58 C 955 ILE MET VAL ASN LEU LEU ILE ALA PHE PHE ASN ASN VAL
SEQRES 59 C 955 TYR LEU GLN VAL LYS ALA ILE SER ASN ILE VAL TRP LYS
SEQRES 60 C 955 TYR GLN ARG TYR HIS PHE ILE MET ALA TYR HIS GLU LYS
SEQRES 61 C 955 PRO VAL LEU PRO PRO PRO LEU ILE ILE LEU SER HIS ILE
SEQRES 62 C 955 VAL SER LEU PHE CYS CYS VAL CYS LYS ARG ARG LYS LYS
SEQRES 63 C 955 ASP LYS THR SER ASP GLY PRO LYS LEU PHE LEU THR GLU
SEQRES 64 C 955 GLU ASP GLN LYS LYS LEU HIS ASP PHE GLU GLU GLN CYS
SEQRES 65 C 955 VAL GLU MET TYR PHE ASP GLU LYS ASP ASP LYS PHE ASN
SEQRES 66 C 955 SER GLY SER GLU GLU ARG ILE ARG VAL THR PHE GLU ARG
SEQRES 67 C 955 VAL GLU GLN MET SER ILE GLN ILE LYS GLU VAL GLY ASP
SEQRES 68 C 955 ARG VAL ASN TYR ILE LYS ARG SER LEU GLN SER LEU ASP
SEQRES 69 C 955 SER GLN ILE GLY HIS LEU GLN ASP LEU SER ALA LEU THR
SEQRES 70 C 955 VAL ASP THR LEU LYS THR LEU THR ALA GLN LYS ALA SER
SEQRES 71 C 955 GLU ALA SER LYS VAL HIS ASN GLU ILE THR ARG GLU LEU
SEQRES 72 C 955 SER ILE SER LYS HIS LEU ALA GLN ASN LEU ILE ASP ASP
SEQRES 73 C 955 VAL PRO VAL ARG PRO LEU TRP LYS LYS PRO SER ALA VAL
SEQRES 74 C 955 ASN THR LEU SER SER SER
SEQRES 1 D 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 2 D 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 3 D 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 4 D 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 5 D 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 6 D 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 7 D 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 8 D 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 9 D 955 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 10 D 955 UNK UNK UNK UNK LYS PHE LEU THR ILE PRO ARG LEU GLU
SEQRES 11 D 955 GLU LEU TYR ASN THR LYS GLN GLY PRO THR ASN PRO MET
SEQRES 12 D 955 LEU PHE HIS LEU ILE ARG ASP VAL LYS GLN GLY ASN LEU
SEQRES 13 D 955 PRO PRO GLY TYR LYS ILE THR LEU ILE ASP ILE GLY LEU
SEQRES 14 D 955 VAL ILE GLU TYR LEU MET GLY GLY THR TYR ARG CYS THR
SEQRES 15 D 955 TYR THR ARG LYS ARG PHE ARG LEU ILE TYR ASN SER LEU
SEQRES 16 D 955 GLY GLY ASN ASN ARG ARG SER GLY ARG ASN THR SER SER
SEQRES 17 D 955 SER THR PRO GLN LEU ARG LYS SER HIS GLU THR PHE GLY
SEQRES 18 D 955 ASN ARG ALA ASP LYS LYS GLU LYS MET ARG HIS ASN HIS
SEQRES 19 D 955 PHE ILE LYS THR ALA GLN PRO TYR ARG PRO LYS MET ASP
SEQRES 20 D 955 ALA SER MET GLU GLU GLY LYS LYS LYS ARG THR LYS ASP
SEQRES 21 D 955 GLU ILE VAL ASP ILE ASP ASP PRO GLU THR LYS ARG PHE
SEQRES 22 D 955 PRO TYR PRO LEU ASN GLU LEU LEU ILE TRP ALA CYS LEU
SEQRES 23 D 955 MET LYS ARG GLN VAL MET ALA ARG PHE LEU TRP GLN HIS
SEQRES 24 D 955 GLY GLU GLU SER MET ALA LYS ALA LEU VAL ALA CYS LYS
SEQRES 25 D 955 ILE TYR ARG SER MET ALA TYR GLU ALA LYS GLN SER ASP
SEQRES 26 D 955 LEU VAL ASP ASP THR SER GLU GLU LEU LYS GLN TYR SER
SEQRES 27 D 955 ASN ASP PHE GLY GLN LEU ALA VAL GLU LEU LEU GLU GLN
SEQRES 28 D 955 SER PHE ARG GLN ASP GLU THR MET ALA MET LYS LEU LEU
SEQRES 29 D 955 THR TYR GLU LEU LYS ASN TRP SER ASN SER THR CYS LEU
SEQRES 30 D 955 LYS LEU ALA VAL SER SER ARG LEU ARG PRO PHE VAL ALA
SEQRES 31 D 955 HIS THR CYS THR GLN MET LEU LEU SER ASP MET TRP MET
SEQRES 32 D 955 GLY ARG LEU ASN MET ARG LYS ASN SER TRP TYR LYS VAL
SEQRES 33 D 955 ILE LEU SER ILE LEU VAL PRO PRO ALA ILE LEU MET LEU
SEQRES 34 D 955 GLU TYR LYS THR LYS ALA GLU MET SER HIS ILE PRO GLN
SEQRES 35 D 955 SER GLN ASP ALA HIS GLN MET THR MET GLU ASP SER GLU
SEQRES 36 D 955 ASN ASN PHE HIS ASN ILE THR GLU GLU ILE PRO MET GLU
SEQRES 37 D 955 VAL PHE LYS GLU VAL LYS ILE LEU ASP SER SER ASP GLY
SEQRES 38 D 955 LYS ASN GLU MET GLU ILE HIS ILE LYS SER LYS LYS LEU
SEQRES 39 D 955 PRO ILE THR ARG LYS PHE TYR ALA PHE TYR HIS ALA PRO
SEQRES 40 D 955 ILE VAL LYS PHE TRP PHE ASN THR LEU ALA TYR LEU GLY
SEQRES 41 D 955 PHE LEU MET LEU TYR THR PHE VAL VAL LEU VAL LYS MET
SEQRES 42 D 955 GLU GLN LEU PRO SER VAL GLN GLU TRP ILE VAL ILE ALA
SEQRES 43 D 955 TYR ILE PHE THR TYR ALA ILE GLU LYS VAL ARG GLU VAL
SEQRES 44 D 955 PHE MET SER GLU ALA GLY LYS ILE SER GLN LYS ILE LYS
SEQRES 45 D 955 VAL TRP PHE SER ASP TYR PHE ASN VAL SER ASP THR ILE
SEQRES 46 D 955 ALA ILE ILE SER PHE PHE VAL GLY PHE GLY LEU ARG PHE
SEQRES 47 D 955 GLY ALA LYS TRP ASN TYR ILE ASN ALA TYR ASP ASN HIS
SEQRES 48 D 955 VAL PHE VAL ALA GLY ARG LEU ILE TYR CYS LEU ASN ILE
SEQRES 49 D 955 ILE PHE TRP TYR VAL ARG LEU LEU ASP PHE LEU ALA VAL
SEQRES 50 D 955 ASN GLN GLN ALA GLY PRO TYR VAL MET MET ILE GLY LYS
SEQRES 51 D 955 MET VAL ALA ASN MET PHE TYR ILE VAL VAL ILE MET ALA
SEQRES 52 D 955 LEU VAL LEU LEU SER PHE GLY VAL PRO ARG LYS ALA ILE
SEQRES 53 D 955 LEU TYR PRO HIS GLU GLU PRO SER TRP SER LEU ALA LYS
SEQRES 54 D 955 ASP ILE VAL PHE HIS PRO TYR TRP MET ILE PHE GLY GLU
SEQRES 55 D 955 VAL TYR ALA TYR GLU ILE ASP VAL CYS ALA ASN ASP SER
SEQRES 56 D 955 THR LEU PRO THR ILE CYS GLY PRO GLY THR TRP LEU THR
SEQRES 57 D 955 PRO PHE LEU GLN ALA VAL TYR LEU PHE VAL GLN TYR ILE
SEQRES 58 D 955 ILE MET VAL ASN LEU LEU ILE ALA PHE PHE ASN ASN VAL
SEQRES 59 D 955 TYR LEU GLN VAL LYS ALA ILE SER ASN ILE VAL TRP LYS
SEQRES 60 D 955 TYR GLN ARG TYR HIS PHE ILE MET ALA TYR HIS GLU LYS
SEQRES 61 D 955 PRO VAL LEU PRO PRO PRO LEU ILE ILE LEU SER HIS ILE
SEQRES 62 D 955 VAL SER LEU PHE CYS CYS VAL CYS LYS ARG ARG LYS LYS
SEQRES 63 D 955 ASP LYS THR SER ASP GLY PRO LYS LEU PHE LEU THR GLU
SEQRES 64 D 955 GLU ASP GLN LYS LYS LEU HIS ASP PHE GLU GLU GLN CYS
SEQRES 65 D 955 VAL GLU MET TYR PHE ASP GLU LYS ASP ASP LYS PHE ASN
SEQRES 66 D 955 SER GLY SER GLU GLU ARG ILE ARG VAL THR PHE GLU ARG
SEQRES 67 D 955 VAL GLU GLN MET SER ILE GLN ILE LYS GLU VAL GLY ASP
SEQRES 68 D 955 ARG VAL ASN TYR ILE LYS ARG SER LEU GLN SER LEU ASP
SEQRES 69 D 955 SER GLN ILE GLY HIS LEU GLN ASP LEU SER ALA LEU THR
SEQRES 70 D 955 VAL ASP THR LEU LYS THR LEU THR ALA GLN LYS ALA SER
SEQRES 71 D 955 GLU ALA SER LYS VAL HIS ASN GLU ILE THR ARG GLU LEU
SEQRES 72 D 955 SER ILE SER LYS HIS LEU ALA GLN ASN LEU ILE ASP ASP
SEQRES 73 D 955 VAL PRO VAL ARG PRO LEU TRP LYS LYS PRO SER ALA VAL
SEQRES 74 D 955 ASN THR LEU SER SER SER
HET MG A1201 1
HET MG A1202 1
HET Y01 A1203 35
HET Y01 A1204 35
HET Y01 A1205 35
HET Y01 A1206 35
HET Y01 A1207 35
HET Y01 A1208 35
HET MG B1201 1
HET MG B1202 1
HET Y01 B1203 35
HET Y01 B1204 35
HET Y01 B1205 35
HET Y01 B1206 35
HET Y01 C1301 35
HET Y01 C1302 35
HET Y01 C1303 35
HET Y01 C1304 35
HET Y01 C1305 35
HET Y01 C1306 35
HET Y01 C1307 35
HET Y01 C1308 35
HET MG D1201 1
HET Y01 D1202 35
HET Y01 D1203 35
HETNAM MG MAGNESIUM ION
HETNAM Y01 CHOLESTEROL HEMISUCCINATE
FORMUL 5 MG 5(MG 2+)
FORMUL 7 Y01 20(C31 H50 O4)
FORMUL 30 HOH *30(H2 O)
HELIX 1 AA1 UNK A 2 UNK A 9 1 8
HELIX 2 AA2 UNK A 10 UNK A 16 1 7
HELIX 3 AA3 UNK A 27 UNK A 34 1 8
HELIX 4 AA4 UNK A 226 UNK A 231 1 6
HELIX 5 AA5 UNK A 236 UNK A 246 1 11
HELIX 6 AA6 UNK A 273 UNK A 285 1 13
HELIX 7 AA7 UNK A 287 UNK A 291 1 5
HELIX 8 AA8 THR A 308 ASN A 317 1 10
HELIX 9 AA9 LYS A 319 ASN A 324 1 6
HELIX 10 AB1 LYS A 344 ASP A 349 1 6
HELIX 11 AB2 TYR A 356 GLY A 360 5 5
HELIX 12 AB3 ARG A 414 PHE A 418 5 5
HELIX 13 AB4 GLU A 435 LYS A 442 1 8
HELIX 14 AB5 PRO A 459 MET A 470 1 12
HELIX 15 AB6 ARG A 472 ARG A 477 1 6
HELIX 16 AB7 GLU A 485 GLU A 503 1 19
HELIX 17 AB8 THR A 513 LEU A 517 5 5
HELIX 18 AB9 TYR A 520 GLY A 525 1 6
HELIX 19 AC1 LEU A 527 GLN A 538 1 12
HELIX 20 AC2 GLU A 540 LYS A 545 1 6
HELIX 21 AC3 LEU A 546 THR A 548 5 3
HELIX 22 AC4 HIS A 574 GLY A 587 1 14
HELIX 23 AC5 TYR A 597 LEU A 604 1 8
HELIX 24 AC6 ILE A 609 GLU A 613 5 5
HELIX 25 AC7 GLU A 619 ILE A 623 5 5
HELIX 26 AC8 LYS A 682 TYR A 687 1 6
HELIX 27 AC9 ALA A 689 VAL A 714 1 26
HELIX 28 AD1 GLN A 723 PHE A 743 1 21
HELIX 29 AD2 LYS A 753 PHE A 758 1 6
HELIX 30 AD3 TYR A 761 LEU A 779 1 19
HELIX 31 AD4 PHE A 796 LEU A 805 1 10
HELIX 32 AD5 ILE A 808 ALA A 819 1 12
HELIX 33 AD6 GLN A 823 GLY A 832 1 10
HELIX 34 AD7 MET A 834 TYR A 861 1 28
HELIX 35 AD8 SER A 869 TRP A 880 1 12
HELIX 36 AD9 LEU A 910 GLN A 922 1 13
HELIX 37 AE1 ASN A 928 PHE A 933 1 6
HELIX 38 AE2 TYR A 938 ARG A 953 1 16
HELIX 39 AE3 ARG A 953 MET A 958 1 6
HELIX 40 AE4 LEU A 970 SER A 974 5 5
HELIX 41 AE5 THR A 1001 LYS A 1023 1 23
HELIX 42 AE6 ASP A 1024 LYS A 1026 5 3
HELIX 43 AE7 SER A 1031 SER A 1068 1 38
HELIX 44 AE8 UNK B 2 UNK B 9 1 8
HELIX 45 AE9 UNK B 10 UNK B 16 1 7
HELIX 46 AF1 UNK B 27 UNK B 34 1 8
HELIX 47 AF2 UNK B 226 UNK B 231 1 6
HELIX 48 AF3 UNK B 236 UNK B 246 1 11
HELIX 49 AF4 UNK B 273 UNK B 285 1 13
HELIX 50 AF5 UNK B 287 UNK B 291 1 5
HELIX 51 AF6 THR B 308 ASN B 317 1 10
HELIX 52 AF7 LYS B 319 ASN B 324 1 6
HELIX 53 AF8 LYS B 344 ASP B 349 1 6
HELIX 54 AF9 VAL B 353 GLY B 360 5 8
HELIX 55 AG1 ARG B 414 PHE B 418 5 5
HELIX 56 AG2 GLU B 435 LYS B 442 1 8
HELIX 57 AG3 PRO B 459 MET B 470 1 12
HELIX 58 AG4 ARG B 472 ARG B 477 1 6
HELIX 59 AG5 GLU B 485 GLU B 503 1 19
HELIX 60 AG6 THR B 513 LEU B 517 5 5
HELIX 61 AG7 TYR B 520 GLY B 525 1 6
HELIX 62 AG8 LEU B 527 GLN B 538 1 12
HELIX 63 AG9 GLU B 540 LYS B 545 1 6
HELIX 64 AH1 LEU B 546 THR B 548 5 3
HELIX 65 AH2 HIS B 574 GLY B 587 1 14
HELIX 66 AH3 TYR B 597 LEU B 604 1 8
HELIX 67 AH4 PRO B 606 GLU B 613 5 8
HELIX 68 AH5 GLU B 619 ILE B 623 5 5
HELIX 69 AH6 LYS B 682 TYR B 687 1 6
HELIX 70 AH7 ALA B 689 VAL B 714 1 26
HELIX 71 AH8 GLN B 723 PHE B 743 1 21
HELIX 72 AH9 LYS B 753 PHE B 758 1 6
HELIX 73 AI1 TYR B 761 LEU B 779 1 19
HELIX 74 AI2 PHE B 796 LEU B 805 1 10
HELIX 75 AI3 ILE B 808 ALA B 819 1 12
HELIX 76 AI4 GLN B 823 GLY B 832 1 10
HELIX 77 AI5 MET B 834 TYR B 861 1 28
HELIX 78 AI6 SER B 869 TRP B 880 1 12
HELIX 79 AI7 LEU B 910 GLN B 922 1 13
HELIX 80 AI8 ASN B 928 PHE B 933 1 6
HELIX 81 AI9 TYR B 938 ARG B 953 1 16
HELIX 82 AJ1 ARG B 953 MET B 958 1 6
HELIX 83 AJ2 LEU B 970 SER B 974 5 5
HELIX 84 AJ3 THR B 1001 LYS B 1023 1 23
HELIX 85 AJ4 ASP B 1024 LYS B 1026 5 3
HELIX 86 AJ5 SER B 1031 SER B 1068 1 38
HELIX 87 AJ6 UNK C 2 UNK C 9 1 8
HELIX 88 AJ7 UNK C 10 UNK C 16 1 7
HELIX 89 AJ8 UNK C 27 UNK C 34 1 8
HELIX 90 AJ9 UNK C 44 UNK C 49 1 6
HELIX 91 AK1 UNK C 54 UNK C 64 1 11
HELIX 92 AK2 UNK C 91 UNK C 103 1 13
HELIX 93 AK3 UNK C 105 UNK C 109 1 5
HELIX 94 AK4 THR C 125 ASN C 134 1 10
HELIX 95 AK5 LYS C 136 ASN C 141 1 6
HELIX 96 AK6 LYS C 161 ASP C 166 1 6
HELIX 97 AK7 VAL C 170 GLY C 177 5 8
HELIX 98 AK8 ARG C 231 PHE C 235 5 5
HELIX 99 AK9 GLU C 252 LYS C 259 1 8
HELIX 100 AL1 PRO C 276 MET C 287 1 12
HELIX 101 AL2 ARG C 289 ARG C 294 1 6
HELIX 102 AL3 GLU C 302 GLU C 320 1 19
HELIX 103 AL4 THR C 330 LEU C 334 5 5
HELIX 104 AL5 TYR C 337 GLY C 342 1 6
HELIX 105 AL6 LEU C 344 GLN C 355 1 12
HELIX 106 AL7 GLU C 357 LYS C 362 1 6
HELIX 107 AL8 LEU C 363 THR C 365 5 3
HELIX 108 AL9 HIS C 391 GLY C 404 1 14
HELIX 109 AM1 TYR C 414 LEU C 421 1 8
HELIX 110 AM2 PRO C 423 GLU C 430 5 8
HELIX 111 AM3 GLU C 436 ILE C 440 5 5
HELIX 112 AM4 LYS C 499 TYR C 504 1 6
HELIX 113 AM5 ALA C 506 VAL C 531 1 26
HELIX 114 AM6 GLN C 540 PHE C 560 1 21
HELIX 115 AM7 LYS C 570 PHE C 575 1 6
HELIX 116 AM8 TYR C 578 LEU C 596 1 19
HELIX 117 AM9 PHE C 613 LEU C 622 1 10
HELIX 118 AN1 ILE C 625 ALA C 636 1 12
HELIX 119 AN2 GLN C 640 GLY C 649 1 10
HELIX 120 AN3 MET C 651 TYR C 678 1 28
HELIX 121 AN4 SER C 686 TRP C 697 1 12
HELIX 122 AN5 LEU C 727 GLN C 739 1 13
HELIX 123 AN6 ASN C 745 PHE C 750 1 6
HELIX 124 AN7 TYR C 755 ARG C 770 1 16
HELIX 125 AN8 ARG C 770 MET C 775 1 6
HELIX 126 AN9 LEU C 787 SER C 791 5 5
HELIX 127 AO1 THR C 818 LYS C 840 1 23
HELIX 128 AO2 ASP C 841 LYS C 843 5 3
HELIX 129 AO3 SER C 848 SER C 885 1 38
HELIX 130 AO4 UNK D 2 UNK D 9 1 8
HELIX 131 AO5 UNK D 10 UNK D 16 1 7
HELIX 132 AO6 UNK D 27 UNK D 34 1 8
HELIX 133 AO7 UNK D 226 UNK D 231 1 6
HELIX 134 AO8 UNK D 236 UNK D 246 1 11
HELIX 135 AO9 UNK D 273 UNK D 285 1 13
HELIX 136 AP1 UNK D 287 UNK D 291 1 5
HELIX 137 AP2 THR D 308 ASN D 317 1 10
HELIX 138 AP3 LYS D 319 ASN D 324 1 6
HELIX 139 AP4 LYS D 344 ASP D 349 1 6
HELIX 140 AP5 VAL D 353 GLY D 360 5 8
HELIX 141 AP6 ARG D 414 PHE D 418 5 5
HELIX 142 AP7 GLU D 435 LYS D 442 1 8
HELIX 143 AP8 PRO D 459 MET D 470 1 12
HELIX 144 AP9 ARG D 472 ARG D 477 1 6
HELIX 145 AQ1 GLU D 485 GLU D 503 1 19
HELIX 146 AQ2 THR D 513 LEU D 517 5 5
HELIX 147 AQ3 TYR D 520 GLY D 525 1 6
HELIX 148 AQ4 LEU D 527 GLN D 538 1 12
HELIX 149 AQ5 GLU D 540 LYS D 545 1 6
HELIX 150 AQ6 LEU D 546 THR D 548 5 3
HELIX 151 AQ7 HIS D 574 GLY D 587 1 14
HELIX 152 AQ8 TYR D 597 LEU D 604 1 8
HELIX 153 AQ9 PRO D 606 GLU D 613 5 8
HELIX 154 AR1 GLU D 619 ILE D 623 5 5
HELIX 155 AR2 LYS D 682 TYR D 687 1 6
HELIX 156 AR3 ALA D 689 VAL D 714 1 26
HELIX 157 AR4 GLN D 723 PHE D 743 1 21
HELIX 158 AR5 LYS D 753 PHE D 758 1 6
HELIX 159 AR6 TYR D 761 LEU D 779 1 19
HELIX 160 AR7 PHE D 796 LEU D 805 1 10
HELIX 161 AR8 ILE D 808 ALA D 819 1 12
HELIX 162 AR9 GLN D 823 GLY D 832 1 10
HELIX 163 AS1 MET D 834 TYR D 861 1 28
HELIX 164 AS2 SER D 869 TRP D 880 1 12
HELIX 165 AS3 LEU D 910 GLN D 922 1 13
HELIX 166 AS4 ASN D 928 PHE D 933 1 6
HELIX 167 AS5 TYR D 938 ARG D 953 1 16
HELIX 168 AS6 ARG D 953 MET D 958 1 6
HELIX 169 AS7 LEU D 970 SER D 974 5 5
HELIX 170 AS8 THR D 1001 LYS D 1023 1 23
HELIX 171 AS9 ASP D 1024 LYS D 1026 5 3
HELIX 172 AT1 SER D 1031 SER D 1068 1 38
SSBOND 1 CYS A 894 CYS A 904 1555 1555 2.02
SSBOND 2 CYS B 894 CYS B 904 1555 1555 2.02
SSBOND 3 CYS C 711 CYS C 721 1555 1555 2.02
SSBOND 4 CYS D 894 CYS D 904 1555 1555 2.02
LINK MG MG A1201 O HOH A1304 1555 1555 2.05
LINK MG MG A1201 O HOH B1301 1555 1555 2.04
LINK MG MG A1201 O HOH C1404 1555 1555 2.07
LINK MG MG A1201 O HOH D1303 1555 1555 2.08
LINK MG MG A1201 O HOH D1305 1555 1555 2.13
LINK MG MG A1201 O HOH D1308 1555 1555 2.11
LINK MG MG A1202 O HOH A1302 1555 1555 2.12
LINK MG MG A1202 O HOH B1304 1555 1555 2.10
LINK MG MG A1202 O HOH C1405 1555 1555 2.12
LINK MG MG A1202 O HOH D1304 1555 1555 2.11
LINK MG MG B1201 O HOH D1308 1555 1555 2.46
LINK MG MG B1202 O HOH A1303 1555 1555 2.13
LINK MG MG B1202 O HOH B1303 1555 1555 2.12
LINK MG MG B1202 O HOH B1306 1555 1555 2.10
LINK MG MG B1202 O HOH C1403 1555 1555 2.13
LINK MG MG B1202 O HOH D1302 1555 1555 2.11
LINK MG MG B1202 O HOH D1309 1555 1555 2.09
LINK MG MG D1201 O HOH C1402 1555 1555 2.44
CISPEP 1 UNK A 24 UNK A 25 0 -14.99
CISPEP 2 UNK A 249 UNK A 250 0 -18.68
CISPEP 3 UNK A 256 UNK A 257 0 -1.10
CISPEP 4 UNK A 291 UNK A 292 0 19.70
CISPEP 5 UNK A 301 UNK A 302 0 -2.50
CISPEP 6 TYR A 316 ASN A 317 0 2.69
CISPEP 7 HIS A 329 LEU A 330 0 -8.10
CISPEP 8 THR A 365 TYR A 366 0 2.79
CISPEP 9 THR A 367 ARG A 368 0 22.84
CISPEP 10 LEU A 373 ILE A 374 0 28.75
CISPEP 11 GLY A 379 GLY A 380 0 2.52
CISPEP 12 SER A 385 GLY A 386 0 -3.35
CISPEP 13 SER A 399 HIS A 400 0 13.05
CISPEP 14 LYS A 412 MET A 413 0 -0.74
CISPEP 15 MET A 429 ASP A 430 0 -6.28
CISPEP 16 ASP A 430 ALA A 431 0 -1.59
CISPEP 17 ALA A 431 SER A 432 0 6.76
CISPEP 18 MET A 433 GLU A 434 0 -14.51
CISPEP 19 GLN A 481 HIS A 482 0 27.75
CISPEP 20 SER A 507 ASP A 508 0 3.28
CISPEP 21 ASP A 539 GLU A 540 0 5.77
CISPEP 22 THR A 548 TYR A 549 0 16.72
CISPEP 23 LEU A 551 LYS A 552 0 20.32
CISPEP 24 SER A 555 ASN A 556 0 -15.32
CISPEP 25 LEU A 562 ALA A 563 0 29.25
CISPEP 26 ASN A 590 MET A 591 0 -0.41
CISPEP 27 GLN A 627 ASP A 628 0 -0.34
CISPEP 28 GLU A 717 GLN A 718 0 -21.56
CISPEP 29 GLN A 718 LEU A 719 0 -27.82
CISPEP 30 PRO A 720 SER A 721 0 -5.90
CISPEP 31 TRP A 785 ASN A 786 0 5.45
CISPEP 32 ASN A 786 TYR A 787 0 -12.18
CISPEP 33 SER A 867 TRP A 868 0 11.51
CISPEP 34 VAL A 893 CYS A 894 0 19.17
CISPEP 35 MET A 926 VAL A 927 0 -17.53
CISPEP 36 PRO A 964 VAL A 965 0 18.39
CISPEP 37 HIS A 975 ILE A 976 0 -0.20
CISPEP 38 LEU A 998 PHE A 999 0 9.74
CISPEP 39 PHE A 999 LEU A 1000 0 -11.26
CISPEP 40 UNK B 24 UNK B 25 0 -15.05
CISPEP 41 UNK B 249 UNK B 250 0 -18.70
CISPEP 42 UNK B 256 UNK B 257 0 -1.13
CISPEP 43 UNK B 291 UNK B 292 0 19.67
CISPEP 44 UNK B 301 UNK B 302 0 -2.58
CISPEP 45 TYR B 316 ASN B 317 0 2.77
CISPEP 46 HIS B 329 LEU B 330 0 -8.06
CISPEP 47 THR B 365 TYR B 366 0 2.71
CISPEP 48 THR B 367 ARG B 368 0 22.83
CISPEP 49 LEU B 373 ILE B 374 0 28.78
CISPEP 50 GLY B 379 GLY B 380 0 2.35
CISPEP 51 SER B 385 GLY B 386 0 -3.30
CISPEP 52 SER B 399 HIS B 400 0 13.05
CISPEP 53 MET B 429 ASP B 430 0 -9.73
CISPEP 54 ASP B 430 ALA B 431 0 -0.64
CISPEP 55 ALA B 431 SER B 432 0 8.54
CISPEP 56 MET B 433 GLU B 434 0 2.58
CISPEP 57 GLN B 481 HIS B 482 0 27.81
CISPEP 58 SER B 507 ASP B 508 0 3.17
CISPEP 59 ASP B 539 GLU B 540 0 5.70
CISPEP 60 THR B 548 TYR B 549 0 16.83
CISPEP 61 LEU B 551 LYS B 552 0 20.25
CISPEP 62 SER B 555 ASN B 556 0 -15.30
CISPEP 63 LEU B 562 ALA B 563 0 29.23
CISPEP 64 ASN B 590 MET B 591 0 0.13
CISPEP 65 GLN B 627 ASP B 628 0 -0.32
CISPEP 66 GLU B 717 GLN B 718 0 -21.57
CISPEP 67 GLN B 718 LEU B 719 0 -27.84
CISPEP 68 PRO B 720 SER B 721 0 -5.87
CISPEP 69 TRP B 785 ASN B 786 0 5.50
CISPEP 70 ASN B 786 TYR B 787 0 -12.18
CISPEP 71 SER B 867 TRP B 868 0 11.49
CISPEP 72 VAL B 893 CYS B 894 0 19.19
CISPEP 73 MET B 926 VAL B 927 0 -17.49
CISPEP 74 PRO B 964 VAL B 965 0 18.48
CISPEP 75 HIS B 975 ILE B 976 0 -0.12
CISPEP 76 LEU B 998 PHE B 999 0 9.73
CISPEP 77 PHE B 999 LEU B 1000 0 -11.23
CISPEP 78 UNK C 24 UNK C 25 0 -15.00
CISPEP 79 UNK C 67 UNK C 68 0 -18.61
CISPEP 80 UNK C 74 UNK C 75 0 -1.15
CISPEP 81 UNK C 109 UNK C 110 0 19.72
CISPEP 82 UNK C 119 UNK C 120 0 -2.54
CISPEP 83 TYR C 133 ASN C 134 0 2.67
CISPEP 84 HIS C 146 LEU C 147 0 -8.07
CISPEP 85 THR C 182 TYR C 183 0 2.71
CISPEP 86 THR C 184 ARG C 185 0 22.79
CISPEP 87 LEU C 190 ILE C 191 0 28.69
CISPEP 88 GLY C 196 GLY C 197 0 2.65
CISPEP 89 SER C 202 GLY C 203 0 -3.31
CISPEP 90 SER C 216 HIS C 217 0 13.16
CISPEP 91 MET C 246 ASP C 247 0 -5.77
CISPEP 92 ASP C 247 ALA C 248 0 1.09
CISPEP 93 MET C 250 GLU C 251 0 -14.58
CISPEP 94 GLN C 298 HIS C 299 0 27.81
CISPEP 95 SER C 324 ASP C 325 0 3.20
CISPEP 96 ASP C 356 GLU C 357 0 5.73
CISPEP 97 THR C 365 TYR C 366 0 16.95
CISPEP 98 LEU C 368 LYS C 369 0 20.32
CISPEP 99 SER C 372 ASN C 373 0 -15.28
CISPEP 100 LEU C 379 ALA C 380 0 29.30
CISPEP 101 ASN C 407 MET C 408 0 0.38
CISPEP 102 GLN C 444 ASP C 445 0 -0.50
CISPEP 103 GLU C 534 GLN C 535 0 -21.57
CISPEP 104 GLN C 535 LEU C 536 0 -27.90
CISPEP 105 PRO C 537 SER C 538 0 -5.92
CISPEP 106 TRP C 602 ASN C 603 0 5.41
CISPEP 107 ASN C 603 TYR C 604 0 -12.17
CISPEP 108 SER C 684 TRP C 685 0 11.44
CISPEP 109 VAL C 710 CYS C 711 0 19.25
CISPEP 110 MET C 743 VAL C 744 0 -17.58
CISPEP 111 PRO C 781 VAL C 782 0 18.52
CISPEP 112 HIS C 792 ILE C 793 0 -0.21
CISPEP 113 LEU C 815 PHE C 816 0 9.66
CISPEP 114 PHE C 816 LEU C 817 0 -11.25
CISPEP 115 UNK D 24 UNK D 25 0 -14.96
CISPEP 116 UNK D 249 UNK D 250 0 -18.72
CISPEP 117 UNK D 256 UNK D 257 0 -1.14
CISPEP 118 UNK D 291 UNK D 292 0 19.75
CISPEP 119 UNK D 301 UNK D 302 0 -2.46
CISPEP 120 TYR D 316 ASN D 317 0 2.77
CISPEP 121 HIS D 329 LEU D 330 0 -8.09
CISPEP 122 THR D 365 TYR D 366 0 2.65
CISPEP 123 THR D 367 ARG D 368 0 22.88
CISPEP 124 LEU D 373 ILE D 374 0 28.66
CISPEP 125 GLY D 379 GLY D 380 0 3.78
CISPEP 126 SER D 385 GLY D 386 0 -3.30
CISPEP 127 SER D 399 HIS D 400 0 13.20
CISPEP 128 MET D 429 ASP D 430 0 -3.43
CISPEP 129 ASP D 430 ALA D 431 0 -5.52
CISPEP 130 MET D 433 GLU D 434 0 1.11
CISPEP 131 GLN D 481 HIS D 482 0 27.79
CISPEP 132 SER D 507 ASP D 508 0 3.11
CISPEP 133 ASP D 539 GLU D 540 0 5.64
CISPEP 134 THR D 548 TYR D 549 0 17.60
CISPEP 135 LEU D 551 LYS D 552 0 20.32
CISPEP 136 SER D 555 ASN D 556 0 -15.30
CISPEP 137 LEU D 562 ALA D 563 0 29.34
CISPEP 138 ASN D 590 MET D 591 0 11.38
CISPEP 139 GLN D 627 ASP D 628 0 -0.37
CISPEP 140 GLU D 717 GLN D 718 0 -21.54
CISPEP 141 GLN D 718 LEU D 719 0 -27.77
CISPEP 142 PRO D 720 SER D 721 0 -5.90
CISPEP 143 TRP D 785 ASN D 786 0 5.54
CISPEP 144 ASN D 786 TYR D 787 0 -12.12
CISPEP 145 SER D 867 TRP D 868 0 11.59
CISPEP 146 VAL D 893 CYS D 894 0 19.30
CISPEP 147 MET D 926 VAL D 927 0 -17.57
CISPEP 148 PRO D 964 VAL D 965 0 18.47
CISPEP 149 HIS D 975 ILE D 976 0 -0.10
CISPEP 150 LEU D 998 PHE D 999 0 9.75
CISPEP 151 PHE D 999 LEU D 1000 0 -11.26
SITE 1 AC1 8 GLU A 885 HOH A1304 GLU B 885 HOH B1301
SITE 2 AC1 8 HOH C1404 HOH D1303 HOH D1305 HOH D1308
SITE 1 AC2 7 HOH A1302 HOH B1304 TYR C 740 HOH C1402
SITE 2 AC2 7 HOH C1405 TYR D 923 HOH D1304
SITE 1 AC3 7 TYR A 597 PHE A 694 TRP A 695 PHE A 817
SITE 2 AC3 7 LEU A 818 ASN A 821 Y01 A1208
SITE 1 AC4 4 MET A 706 PHE A 710 GLN A 723 Y01 A1208
SITE 1 AC5 10 LEU A 850 PRO A 866 TRP A 868 ALA A 871
SITE 2 AC5 10 LEU B 702 MET B 706 THR B 709 PHE B 710
SITE 3 AC5 10 TYR B 811 Y01 B1204
SITE 1 AC6 9 PHE A 762 LEU A 815 VAL A 828 MET A 829
SITE 2 AC6 9 GLY A 832 Y01 A1207 SER D 851 PHE D 852
SITE 3 AC6 9 VAL D 917
SITE 1 AC7 4 TYR A 761 SER A 765 PHE A 809 Y01 A1206
SITE 1 AC8 7 MET A 706 TYR A 811 Y01 A1203 Y01 A1204
SITE 2 AC8 7 PRO D 866 TRP D 868 LEU D 870
SITE 1 AC9 3 HOH B1302 HOH D1301 HOH D1308
SITE 1 AD1 6 HOH A1303 HOH B1303 HOH B1306 HOH C1403
SITE 2 AD1 6 HOH D1302 HOH D1309
SITE 1 AD2 5 PRO A 866 MET B 706 LEU B 707 PHE B 710
SITE 2 AD2 5 GLN B 723
SITE 1 AD3 9 LEU A 850 Y01 A1205 TYR B 597 PHE B 694
SITE 2 AD3 9 TRP B 695 LEU B 702 PHE B 817 LEU B 818
SITE 3 AD3 9 ASN B 821
SITE 1 AD4 10 SER A 851 LEU A 914 VAL A 917 TYR B 761
SITE 2 AD4 10 PHE B 762 VAL B 812 VAL B 828 MET B 829
SITE 3 AD4 10 GLN B 952 Y01 B1206
SITE 1 AD5 4 TYR B 761 SER B 765 PHE B 809 Y01 B1205
SITE 1 AD6 6 GLY C 520 MET C 523 LEU C 524 PHE C 527
SITE 2 AD6 6 GLN C 540 Y01 C1302
SITE 1 AD7 5 PRO B 866 ILE B 874 LEU C 522 TYR C 628
SITE 2 AD7 5 Y01 C1301
SITE 1 AD8 8 LEU B 850 TYR C 414 PHE C 511 TRP C 512
SITE 2 AD8 8 PHE C 634 LEU C 635 VAL C 637 ASN C 638
SITE 1 AD9 7 PRO C 683 TRP C 685 Y01 C1305 MET D 706
SITE 2 AD9 7 THR D 709 PHE D 710 Y01 D1202
SITE 1 AE1 6 LEU C 667 Y01 C1304 PHE D 694 TRP D 695
SITE 2 AE1 6 PHE D 817 VAL D 820
SITE 1 AE2 10 SER B 851 PHE B 852 TYR C 578 PHE C 579
SITE 2 AE2 10 LEU C 632 VAL C 645 MET C 646 GLY C 649
SITE 3 AE2 10 GLN C 769 Y01 C1307
SITE 1 AE3 4 TYR C 578 ILE C 625 PHE C 626 Y01 C1306
SITE 1 AE4 10 SER C 668 PHE C 669 LEU C 731 PHE D 762
SITE 2 AE4 10 ILE D 808 VAL D 812 LEU D 815 VAL D 828
SITE 3 AE4 10 GLN D 952 Y01 D1203
SITE 1 AE5 3 PHE B 883 HOH C1402 HOH D1307
SITE 1 AE6 4 Y01 C1304 GLY D 703 PHE D 710 GLN D 723
SITE 1 AE7 6 LEU C 731 Y01 C1308 TYR D 761 ILE D 808
SITE 2 AE7 6 PHE D 809 VAL D 812
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
