HEADER VIRAL PROTEIN 18-SEP-09 3JWD
TITLE STRUCTURE OF HIV-1 GP120 WITH GP41-INTERACTIVE REGION: LAYERED
TITLE 2 ARCHITECTURE AND BASIS OF CONFORMATIONAL MOBILITY
CAVEAT 3JWD NAG A 734 HAS WRONG CHIRALITY AT ATOM C1 NAG A 948 HAS WRONG
CAVEAT 2 3JWD CHIRALITY AT ATOM C1 NAG B 588 HAS WRONG CHIRALITY AT ATOM
CAVEAT 3 3JWD C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIV-1 GP120 ENVELOPE GLYCOPROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: T-CELL SURFACE GLYCOPROTEIN CD4;
COMPND 7 CHAIN: C, D;
COMPND 8 SYNONYM: T-CELL SURFACE ANTIGEN T4/LEU-3;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: FAB 48D LIGHT CHAIN;
COMPND 12 CHAIN: L, O;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 4;
COMPND 15 MOLECULE: FAB 48D HEAVY CHAIN;
COMPND 16 CHAIN: H, P;
COMPND 17 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 STRAIN: HXBC2;
SOURCE 5 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMT;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: CD4;
SOURCE 15 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 16 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 18 MOL_ID: 3;
SOURCE 19 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 20 ORGANISM_COMMON: HUMAN;
SOURCE 21 ORGANISM_TAXID: 9606;
SOURCE 22 EXPRESSION_SYSTEM: UNIDENTIFIED HERPESVIRUS;
SOURCE 23 EXPRESSION_SYSTEM_TAXID: 39059;
SOURCE 24 EXPRESSION_SYSTEM_CELL: IMMORTALIZED B-CELL CLONE FUSED WITH A
SOURCE 25 MURINE B-CELL FUSION PARTNER;
SOURCE 26 MOL_ID: 4;
SOURCE 27 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 28 ORGANISM_COMMON: HUMAN;
SOURCE 29 ORGANISM_TAXID: 9606;
SOURCE 30 EXPRESSION_SYSTEM: UNIDENTIFIED HERPESVIRUS;
SOURCE 31 EXPRESSION_SYSTEM_TAXID: 39059;
SOURCE 32 EXPRESSION_SYSTEM_CELL: IMMORTALIZED B-CELL CLONE FUSED WITH A
SOURCE 33 MURINE B-CELL FUSION PARTNER
KEYWDS HIV-1 VIRAL SPIKE, MOLECULAR MOTION, PROTEIN ARCHITECTURE, RECEPTOR-
KEYWDS 2 TRIGGERED ENTRY, TYPE 1 FUSION PROTEIN, CELL MEMBRANE, DISULFIDE
KEYWDS 3 BOND, GLYCOPROTEIN, HOST-VIRUS INTERACTION, IMMUNE RESPONSE, VIRAL
KEYWDS 4 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.PANCERA,S.MAJEED,Y.A.BAN,L.CHEN,C.C.HUANG,L.KONG,Y.D.KWON,
AUTHOR 2 J.STUCKEY,T.ZHOU,J.E.ROBINSON,W.R.SCHIEF,J.SODROSKI,R.WYATT,
AUTHOR 3 P.D.KWONG
REVDAT 6 06-SEP-23 3JWD 1 HETSYN
REVDAT 5 29-JUL-20 3JWD 1 CAVEAT COMPND SEQADV HETNAM
REVDAT 5 2 1 LINK
REVDAT 4 13-JUL-11 3JWD 1 VERSN
REVDAT 3 16-FEB-10 3JWD 1 JRNL
REVDAT 2 02-FEB-10 3JWD 1 JRNL
REVDAT 1 29-DEC-09 3JWD 0
JRNL AUTH M.PANCERA,S.MAJEED,Y.E.BAN,L.CHEN,C.C.HUANG,L.KONG,Y.D.KWON,
JRNL AUTH 2 J.STUCKEY,T.ZHOU,J.E.ROBINSON,W.R.SCHIEF,J.SODROSKI,R.WYATT,
JRNL AUTH 3 P.D.KWONG
JRNL TITL STRUCTURE OF HIV-1 GP120 WITH GP41-INTERACTIVE REGION
JRNL TITL 2 REVEALS LAYERED ENVELOPE ARCHITECTURE AND BASIS OF
JRNL TITL 3 CONFORMATIONAL MOBILITY.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 107 1166 2010
JRNL REFN ISSN 0027-8424
JRNL PMID 20080564
JRNL DOI 10.1073/PNAS.0911004107
REMARK 2
REMARK 2 RESOLUTION. 2.61 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (CCI APPS 2007_04_06_1210)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.61
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.86
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 63.8
REMARK 3 NUMBER OF REFLECTIONS : 54419
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.130
REMARK 3 FREE R VALUE TEST SET COUNT : 5512
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 56.15
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 114.4
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 34.67000
REMARK 3 B22 (A**2) : -1.46000
REMARK 3 B33 (A**2) : -33.22000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.000 NULL
REMARK 3 ANGLE : 0.350 NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : 8.100 NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESID 31:501
REMARK 3 ORIGIN FOR THE GROUP (A): 18.3876 67.7836 108.3390
REMARK 3 T TENSOR
REMARK 3 T11: 0.1665 T22: 0.2536
REMARK 3 T33: 0.3529 T12: -0.0370
REMARK 3 T13: -0.0341 T23: 0.0264
REMARK 3 L TENSOR
REMARK 3 L11: 0.4055 L22: 1.0227
REMARK 3 L33: 3.6650 L12: 0.1046
REMARK 3 L13: -0.5439 L23: -0.1835
REMARK 3 S TENSOR
REMARK 3 S11: 0.0167 S12: -0.0214 S13: 0.0455
REMARK 3 S21: 0.0982 S22: -0.0539 S23: 0.0778
REMARK 3 S31: 0.3314 S32: -0.3162 S33: 0.0243
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN C AND RESID 1000:1098
REMARK 3 ORIGIN FOR THE GROUP (A): 23.4818 86.8980 86.9070
REMARK 3 T TENSOR
REMARK 3 T11: 0.4217 T22: 0.2824
REMARK 3 T33: 0.3383 T12: -0.0391
REMARK 3 T13: 0.1160 T23: 0.0314
REMARK 3 L TENSOR
REMARK 3 L11: 2.4204 L22: 1.4207
REMARK 3 L33: 1.6617 L12: 1.4338
REMARK 3 L13: -1.1081 L23: -0.6145
REMARK 3 S TENSOR
REMARK 3 S11: 0.1995 S12: -0.3008 S13: -0.0527
REMARK 3 S21: -0.0931 S22: -0.3524 S23: -0.0955
REMARK 3 S31: -0.3698 S32: 0.1064 S33: 0.0618
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN C AND RESID 1099:1183
REMARK 3 ORIGIN FOR THE GROUP (A): 22.9129 102.9885 57.1569
REMARK 3 T TENSOR
REMARK 3 T11: 0.5755 T22: 0.5153
REMARK 3 T33: 0.4514 T12: -0.1283
REMARK 3 T13: 0.0970 T23: 0.1547
REMARK 3 L TENSOR
REMARK 3 L11: -0.3515 L22: 0.6795
REMARK 3 L33: 8.0807 L12: 0.3888
REMARK 3 L13: -1.3429 L23: -0.3511
REMARK 3 S TENSOR
REMARK 3 S11: 0.3127 S12: 0.0084 S13: 0.1027
REMARK 3 S21: 0.0903 S22: -0.1603 S23: 0.0459
REMARK 3 S31: -1.5280 S32: 0.3615 S33: -0.1448
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN L AND RESID 1:111
REMARK 3 ORIGIN FOR THE GROUP (A): 42.7899 39.9984 73.5690
REMARK 3 T TENSOR
REMARK 3 T11: 0.7460 T22: 0.3206
REMARK 3 T33: 0.3482 T12: 0.3033
REMARK 3 T13: 0.1413 T23: 0.0517
REMARK 3 L TENSOR
REMARK 3 L11: 2.2579 L22: 1.3020
REMARK 3 L33: 1.2335 L12: -0.8477
REMARK 3 L13: -0.6586 L23: 0.3419
REMARK 3 S TENSOR
REMARK 3 S11: -0.4689 S12: -0.3386 S13: -0.2939
REMARK 3 S21: 0.5256 S22: 0.1039 S23: 0.0032
REMARK 3 S31: 0.7985 S32: 0.0429 S33: 0.3381
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN L AND RESID 112:214
REMARK 3 ORIGIN FOR THE GROUP (A): 64.0336 47.7355 45.0083
REMARK 3 T TENSOR
REMARK 3 T11: 0.6547 T22: 0.6721
REMARK 3 T33: 0.7615 T12: 0.1647
REMARK 3 T13: 0.2950 T23: 0.4177
REMARK 3 L TENSOR
REMARK 3 L11: -0.0113 L22: 2.2082
REMARK 3 L33: 0.5129 L12: -0.0725
REMARK 3 L13: -0.2907 L23: -0.2459
REMARK 3 S TENSOR
REMARK 3 S11: 0.3429 S12: 0.3463 S13: 0.2802
REMARK 3 S21: 0.0598 S22: -0.4737 S23: -0.6025
REMARK 3 S31: -0.1616 S32: 0.0644 S33: 0.0828
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN H AND RESID 1:128
REMARK 3 ORIGIN FOR THE GROUP (A): 33.6589 59.6144 66.4946
REMARK 3 T TENSOR
REMARK 3 T11: 0.8602 T22: 0.5473
REMARK 3 T33: 0.4912 T12: 0.4348
REMARK 3 T13: 0.2531 T23: 0.2193
REMARK 3 L TENSOR
REMARK 3 L11: 1.0367 L22: 1.8074
REMARK 3 L33: 3.1554 L12: -0.2372
REMARK 3 L13: -1.9329 L23: 0.5396
REMARK 3 S TENSOR
REMARK 3 S11: 0.5296 S12: 0.5975 S13: 0.1993
REMARK 3 S21: -1.0437 S22: -0.3110 S23: -0.3895
REMARK 3 S31: -0.4041 S32: -0.8635 S33: -0.1790
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN H AND RESID 129:214
REMARK 3 ORIGIN FOR THE GROUP (A): 49.6677 47.9314 38.6141
REMARK 3 T TENSOR
REMARK 3 T11: 1.7291 T22: 1.3901
REMARK 3 T33: 0.6894 T12: 0.8780
REMARK 3 T13: 0.2398 T23: 0.2152
REMARK 3 L TENSOR
REMARK 3 L11: 2.4653 L22: 3.0204
REMARK 3 L33: 4.5012 L12: -1.5682
REMARK 3 L13: -3.6440 L23: -0.2919
REMARK 3 S TENSOR
REMARK 3 S11: 1.3367 S12: 1.4258 S13: 0.1532
REMARK 3 S21: -1.3553 S22: -0.8512 S23: -0.0403
REMARK 3 S31: -0.3325 S32: -2.0523 S33: -0.4593
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN B AND RESID 31:499
REMARK 3 ORIGIN FOR THE GROUP (A): 58.7149 68.3867 160.0519
REMARK 3 T TENSOR
REMARK 3 T11: 0.3927 T22: 0.8588
REMARK 3 T33: 0.5801 T12: 0.2286
REMARK 3 T13: -0.0521 T23: 0.0173
REMARK 3 L TENSOR
REMARK 3 L11: 0.8082 L22: 1.1419
REMARK 3 L33: 4.0865 L12: -1.0161
REMARK 3 L13: -0.4398 L23: 0.8992
REMARK 3 S TENSOR
REMARK 3 S11: -0.0253 S12: 0.1130 S13: -0.0849
REMARK 3 S21: -0.0882 S22: 0.1681 S23: -0.0275
REMARK 3 S31: 0.3869 S32: 1.3077 S33: -0.1417
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN D AND RESID 1001:1098
REMARK 3 ORIGIN FOR THE GROUP (A): 59.6809 88.6261 181.0668
REMARK 3 T TENSOR
REMARK 3 T11: 0.5764 T22: 1.1134
REMARK 3 T33: 0.4114 T12: -0.1902
REMARK 3 T13: 0.0645 T23: 0.0492
REMARK 3 L TENSOR
REMARK 3 L11: 4.7213 L22: 0.8607
REMARK 3 L33: 7.7555 L12: 0.0965
REMARK 3 L13: 0.3650 L23: 0.1171
REMARK 3 S TENSOR
REMARK 3 S11: 0.0321 S12: -0.2276 S13: -0.3911
REMARK 3 S21: -0.0298 S22: -0.0382 S23: -0.0349
REMARK 3 S31: -1.3402 S32: 2.2920 S33: -0.0134
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN D AND RESID 1099:1183
REMARK 3 ORIGIN FOR THE GROUP (A): 64.3276 103.7747 211.0396
REMARK 3 T TENSOR
REMARK 3 T11: 0.8321 T22: 1.1634
REMARK 3 T33: 0.5670 T12: -0.0301
REMARK 3 T13: -0.0198 T23: -0.1901
REMARK 3 L TENSOR
REMARK 3 L11: -0.9262 L22: -0.3994
REMARK 3 L33: 9.9148 L12: 1.0460
REMARK 3 L13: 0.0977 L23: 0.4639
REMARK 3 S TENSOR
REMARK 3 S11: 0.4737 S12: -0.1476 S13: 0.1168
REMARK 3 S21: 0.3475 S22: 0.3197 S23: 0.0419
REMARK 3 S31: -0.2961 S32: 0.2206 S33: -0.6577
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN O AND RESID 1:111
REMARK 3 ORIGIN FOR THE GROUP (A): 24.6592 51.4166 193.0082
REMARK 3 T TENSOR
REMARK 3 T11: 1.7329 T22: 0.5112
REMARK 3 T33: 1.1255 T12: -0.4982
REMARK 3 T13: 0.4290 T23: 0.0915
REMARK 3 L TENSOR
REMARK 3 L11: 1.1883 L22: -3.2421
REMARK 3 L33: 2.2339 L12: -1.0264
REMARK 3 L13: -1.4582 L23: 0.3626
REMARK 3 S TENSOR
REMARK 3 S11: -1.1746 S12: 0.3762 S13: -1.0183
REMARK 3 S21: -0.0514 S22: 0.0549 S23: -0.3945
REMARK 3 S31: 1.5448 S32: -0.3738 S33: 1.1519
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN O AND RESID 112:213
REMARK 3 ORIGIN FOR THE GROUP (A): 6.5487 66.3501 220.8797
REMARK 3 T TENSOR
REMARK 3 T11: 0.9539 T22: 0.8827
REMARK 3 T33: 1.7770 T12: -0.0450
REMARK 3 T13: 0.3122 T23: 0.2286
REMARK 3 L TENSOR
REMARK 3 L11: 0.8647 L22: 5.2244
REMARK 3 L33: 1.4442 L12: 2.4566
REMARK 3 L13: 0.0196 L23: -2.1816
REMARK 3 S TENSOR
REMARK 3 S11: -0.0678 S12: -0.1321 S13: -0.0049
REMARK 3 S21: -0.6047 S22: 0.4987 S23: 1.2185
REMARK 3 S31: 0.4442 S32: -0.3901 S33: -0.4222
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN P AND RESID 1:128
REMARK 3 ORIGIN FOR THE GROUP (A): 40.0467 66.4144 200.9097
REMARK 3 T TENSOR
REMARK 3 T11: 0.7062 T22: 0.4869
REMARK 3 T33: 0.6801 T12: 0.1614
REMARK 3 T13: 0.1703 T23: 0.1654
REMARK 3 L TENSOR
REMARK 3 L11: 0.3535 L22: 1.2564
REMARK 3 L33: 2.7622 L12: -0.6464
REMARK 3 L13: -0.0067 L23: -0.0225
REMARK 3 S TENSOR
REMARK 3 S11: -0.2561 S12: -0.0792 S13: -0.0311
REMARK 3 S21: 0.8939 S22: 0.1078 S23: 0.3363
REMARK 3 S31: 0.3723 S32: 0.6207 S33: 0.1160
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN P AND RESID 129:212
REMARK 3 ORIGIN FOR THE GROUP (A): 19.9069 61.4106 227.4791
REMARK 3 T TENSOR
REMARK 3 T11: 1.3651 T22: 0.7619
REMARK 3 T33: 1.3675 T12: 0.1454
REMARK 3 T13: 0.6747 T23: 0.4704
REMARK 3 L TENSOR
REMARK 3 L11: 0.8320 L22: 0.1884
REMARK 3 L33: 0.8534 L12: -0.3252
REMARK 3 L13: -1.1489 L23: 0.5071
REMARK 3 S TENSOR
REMARK 3 S11: -0.3012 S12: -0.1959 S13: 0.1219
REMARK 3 S21: 0.1592 S22: 0.2555 S23: 0.5359
REMARK 3 S31: 0.5461 S32: 0.0345 S33: 0.0402
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 4
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 36:74)
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 84:124)
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 198:299)
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 4
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 329:394)
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 5
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 411:494)
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN L
REMARK 3 SELECTION : CHAIN O AND (RESSEQ 2:121)
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN L
REMARK 3 SELECTION : CHAIN O AND (RESSEQ 129:210)
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 3
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN H
REMARK 3 SELECTION : CHAIN P AND (RESSEQ 1:122)
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN H
REMARK 3 SELECTION : CHAIN P AND (RESSEQ 134:213)
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 4
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN C
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 1000:1056)
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN C
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 1060:1179)
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: WHEN REFINING TLS, THE OUTPUT PDB FILE
REMARK 3 ALWAYS HAS THE ANISOU RECORDS FOR THE ATOMS INVOLVED IN TLS
REMARK 3 GROUPS. THE ANISOTROPIC B-FACTOR IN ANISOU RECORDS IS THE TOTAL
REMARK 3 B-FACTOR (B_TLS + B_INDIVIDUAL). THE ISOTROPIC EQUIVALENT B-
REMARK 3 FACTOR IN ATOM RECORDS IS THE MEAN OF THE TRACE OF THE ANISOU
REMARK 3 MATRIX DIVIDED BY 10000 AND MULTIPLIED BY 8*PI^2 AND REPRESENTS
REMARK 3 THE ISOTROPIC EQUIVALENT OF THE TOTAL B-FACTOR (B_TLS + B_
REMARK 3 INDIVIDUAL). TO OBTAIN THE INDIVIDUAL B-FACTORS, ONE NEEDS TO
REMARK 3 COMPUTE THE TLS COMPONENT (B_TLS) USING THE TLS RECORDS IN THE
REMARK 3 PDB FILE HEADER AND THEN SUBTRACT IT FROM THE TOTAL B-FACTORS
REMARK 3 (ON THE ANISOU RECORDS).
REMARK 4
REMARK 4 3JWD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-SEP-09.
REMARK 100 THE DEPOSITION ID IS D_1000055242.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-FEB-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 9.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : SILICON CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59657
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.610
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 69.7
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.10700
REMARK 200 R SYM (I) : 0.07700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.61
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 17.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.57900
REMARK 200 R SYM FOR SHELL (I) : 0.47500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.380
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRIES 1RZJ, 1RZ7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 4.5 % PEG 8000, 01M CHES, PH 9.50,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 41.55600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 96.57200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 86.47700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 96.57200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.55600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 86.47700
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 47140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, L, H
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 45700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, O, P
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 TRP A 400
REMARK 465 SER A 401
REMARK 465 THR A 402
REMARK 465 GLU A 403
REMARK 465 GLY A 404
REMARK 465 SER A 405
REMARK 465 ASN A 406
REMARK 465 ASN A 407
REMARK 465 THR A 408
REMARK 465 LYS A 502
REMARK 465 ARG A 503
REMARK 465 ARG A 504
REMARK 465 VAL A 505
REMARK 465 VAL A 506
REMARK 465 GLN A 507
REMARK 465 SER A 508
REMARK 465 GLU A 509
REMARK 465 LYS A 510
REMARK 465 SER A 511
REMARK 465 ASN B 397
REMARK 465 SER B 398
REMARK 465 THR B 399
REMARK 465 TRP B 400
REMARK 465 SER B 401
REMARK 465 THR B 402
REMARK 465 GLU B 403
REMARK 465 GLY B 404
REMARK 465 SER B 405
REMARK 465 ASN B 406
REMARK 465 ASN B 407
REMARK 465 THR B 408
REMARK 465 GLU B 409
REMARK 465 LYS B 500
REMARK 465 ALA B 501
REMARK 465 LYS B 502
REMARK 465 ARG B 503
REMARK 465 ARG B 504
REMARK 465 VAL B 505
REMARK 465 VAL B 506
REMARK 465 GLN B 507
REMARK 465 SER B 508
REMARK 465 GLU B 509
REMARK 465 LYS B 510
REMARK 465 SER B 511
REMARK 465 MET D 1000
REMARK 465 YCM O 214
REMARK 465 LYS P 214
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 LYS A 33 -99.44 -127.65
REMARK 500 LEU A 34 -77.51 -119.04
REMARK 500 ASP A 57 38.63 -92.36
REMARK 500 THR A 77 -159.68 -94.65
REMARK 500 ASP A 78 -72.43 -64.38
REMARK 500 ASN A 94 84.43 -163.14
REMARK 500 LYS A 97 48.56 -144.85
REMARK 500 ASP A 99 4.18 -68.35
REMARK 500 SER A 115 -84.52 -99.25
REMARK 500 THR A 240 42.47 -104.39
REMARK 500 ASN A 241 52.53 -170.81
REMARK 500 THR A 248 -173.66 -68.22
REMARK 500 GLN A 258 -61.20 63.74
REMARK 500 GLU A 268 -93.58 -122.09
REMARK 500 ASN A 276 96.15 -166.74
REMARK 500 ASN A 356 -9.47 -169.92
REMARK 500 CYS A 378 82.65 -155.66
REMARK 500 PHE A 391 59.72 -109.42
REMARK 500 SER A 398 93.85 -68.71
REMARK 500 ILE A 439 -93.91 -84.56
REMARK 500 ASP A 457 -63.92 -90.34
REMARK 500 ASN A 460 42.72 -75.96
REMARK 500 SER A 461 -42.72 -146.02
REMARK 500 ASN A 462 89.09 -63.70
REMARK 500 LEU A 483 36.54 -86.26
REMARK 500 LYS A 487 114.58 179.72
REMARK 500 PRO A 493 146.61 -39.65
REMARK 500 GLN C1025 108.07 -53.39
REMARK 500 ASN C1030 -145.76 -100.07
REMARK 500 PRO C1048 20.79 -77.52
REMARK 500 ASP C1056 99.47 179.66
REMARK 500 GLU C1087 70.32 41.72
REMARK 500 GLN C1110 -67.04 -141.60
REMARK 500 GLN C1165 -23.11 78.70
REMARK 500 ARG L 24 115.79 -161.87
REMARK 500 SER L 30 -139.79 61.09
REMARK 500 ALA L 51 -32.53 71.32
REMARK 500 ASN L 76 -98.91 -67.55
REMARK 500 ALA L 84 -159.97 -159.25
REMARK 500 SER L 93 -71.10 -165.93
REMARK 500 SER L 121 -163.73 -78.10
REMARK 500 ASN L 138 91.22 34.92
REMARK 500 LYS L 169 -61.01 -95.85
REMARK 500 LEU L 181 -110.05 -129.25
REMARK 500 SER L 182 -150.27 -156.59
REMARK 500 LYS L 190 -11.30 -147.76
REMARK 500 ASN L 210 -133.94 -133.90
REMARK 500 ALA H 16 -171.89 -69.75
REMARK 500 CYS H 22 74.40 -167.43
REMARK 500 PRO H 41 109.45 -53.45
REMARK 500
REMARK 500 THIS ENTRY HAS 123 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3JWO RELATED DB: PDB
DBREF 3JWD C 1001 1183 UNP P01730 CD4_HUMAN 26 208
DBREF 3JWD D 1001 1183 UNP P01730 CD4_HUMAN 26 208
DBREF 3JWD A 31 511 PDB 3JWD 3JWD 31 511
DBREF 3JWD B 31 511 PDB 3JWD 3JWD 31 511
DBREF 3JWD L 1 214 PDB 3JWD 3JWD 1 214
DBREF 3JWD O 1 214 PDB 3JWD 3JWD 1 214
DBREF 3JWD H 1 214 PDB 3JWD 3JWD 1 214
DBREF 3JWD P 1 214 PDB 3JWD 3JWD 1 214
SEQADV 3JWD MET C 1000 UNP P01730 INITIATING METHIONINE
SEQADV 3JWD MET D 1000 UNP P01730 INITIATING METHIONINE
SEQRES 1 A 379 THR GLU LYS LEU TRP VAL THR VAL TYR TYR GLY VAL PRO
SEQRES 2 A 379 VAL TRP LYS GLU ALA THR THR THR LEU PHE CYS ALA SER
SEQRES 3 A 379 ASP ALA LYS ALA TYR ASP THR GLU VAL HIS ASN VAL TRP
SEQRES 4 A 379 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN
SEQRES 5 A 379 GLU VAL VAL LEU VAL ASN VAL THR GLU ASN PHE ASN MET
SEQRES 6 A 379 TRP LYS ASN ASP MET VAL GLU GLN MET HIS GLU ASP ILE
SEQRES 7 A 379 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS
SEQRES 8 A 379 LEU THR GLY GLY SER VAL ILE THR GLN ALA CYS PRO LYS
SEQRES 9 A 379 VAL SER PHE GLU PRO ILE PRO ILE HIS TYR CYS ALA PRO
SEQRES 10 A 379 ALA GLY PHE ALA ILE LEU LYS CYS ASN ASN LYS THR PHE
SEQRES 11 A 379 ASN GLY THR GLY PRO CYS THR ASN VAL SER THR VAL GLN
SEQRES 12 A 379 CYS THR HIS GLY ILE ARG PRO VAL VAL SER SER GLN LEU
SEQRES 13 A 379 LEU LEU ASN GLY SER LEU ALA GLU GLU GLU VAL VAL ILE
SEQRES 14 A 379 ARG SER VAL ASN PHE THR ASP ASN ALA LYS THR ILE ILE
SEQRES 15 A 379 VAL GLN LEU ASN THR SER VAL GLU ILE ASN CYS THR GLY
SEQRES 16 A 379 ALA GLY HIS CYS ASN ILE ALA ARG ALA LYS TRP ASN ASN
SEQRES 17 A 379 THR LEU LYS GLN ILE ALA SER LYS LEU ARG GLU GLN PHE
SEQRES 18 A 379 GLY ASN ASN LYS THR ILE ILE PHE LYS GLN SER SER GLY
SEQRES 19 A 379 GLY ASP PRO GLU ILE VAL THR HIS TRP PHE ASN CYS GLY
SEQRES 20 A 379 GLY GLU PHE PHE TYR CYS ASN SER THR GLN LEU PHE ASN
SEQRES 21 A 379 SER THR TRP PHE ASN SER THR TRP SER THR GLU GLY SER
SEQRES 22 A 379 ASN ASN THR GLU GLY SER ASP THR ILE THR LEU PRO CYS
SEQRES 23 A 379 ARG ILE LYS GLN ILE ILE ASN MET TRP GLN LYS VAL GLY
SEQRES 24 A 379 LYS ALA MET TYR ALA PRO PRO ILE SER GLY GLN ILE ARG
SEQRES 25 A 379 CYS SER SER ASN ILE THR GLY LEU LEU LEU THR ARG ASP
SEQRES 26 A 379 GLY GLY ASN SER ASN ASN GLU SER GLU ILE PHE ARG PRO
SEQRES 27 A 379 GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SER GLU LEU
SEQRES 28 A 379 TYR LYS TYR LYS VAL VAL LYS ILE GLU PRO LEU GLY VAL
SEQRES 29 A 379 ALA PRO THR LYS ALA LYS ARG ARG VAL VAL GLN SER GLU
SEQRES 30 A 379 LYS SER
SEQRES 1 C 184 MET LYS LYS VAL VAL LEU GLY LYS LYS GLY ASP THR VAL
SEQRES 2 C 184 GLU LEU THR CYS THR ALA SER GLN LYS LYS SER ILE GLN
SEQRES 3 C 184 PHE HIS TRP LYS ASN SER ASN GLN ILE LYS ILE LEU GLY
SEQRES 4 C 184 ASN GLN GLY SER PHE LEU THR LYS GLY PRO SER LYS LEU
SEQRES 5 C 184 ASN ASP ARG ALA ASP SER ARG ARG SER LEU TRP ASP GLN
SEQRES 6 C 184 GLY ASN PHE PRO LEU ILE ILE LYS ASN LEU LYS ILE GLU
SEQRES 7 C 184 ASP SER ASP THR TYR ILE CYS GLU VAL GLU ASP GLN LYS
SEQRES 8 C 184 GLU GLU VAL GLN LEU LEU VAL PHE GLY LEU THR ALA ASN
SEQRES 9 C 184 SER ASP THR HIS LEU LEU GLN GLY GLN SER LEU THR LEU
SEQRES 10 C 184 THR LEU GLU SER PRO PRO GLY SER SER PRO SER VAL GLN
SEQRES 11 C 184 CYS ARG SER PRO ARG GLY LYS ASN ILE GLN GLY GLY LYS
SEQRES 12 C 184 THR LEU SER VAL SER GLN LEU GLU LEU GLN ASP SER GLY
SEQRES 13 C 184 THR TRP THR CYS THR VAL LEU GLN ASN GLN LYS LYS VAL
SEQRES 14 C 184 GLU PHE LYS ILE ASP ILE VAL VAL LEU ALA PHE GLN LYS
SEQRES 15 C 184 ALA SER
SEQRES 1 L 213 ASP ILE GLN MET THR GLN SER PRO SER SER VAL SER ALA
SEQRES 2 L 213 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER
SEQRES 3 L 213 GLN ASP ILE SER THR TRP LEU ALA TRP TYR GLN GLN LYS
SEQRES 4 L 213 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER
SEQRES 5 L 213 THR LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 L 213 GLY SER GLY THR ASP PHE SER LEU THR ILE ASN SER LEU
SEQRES 7 L 213 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN ALA
SEQRES 8 L 213 ASN SER PHE PHE THR PHE GLY GLY GLY THR LYS VAL GLU
SEQRES 9 L 213 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE
SEQRES 10 L 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER
SEQRES 11 L 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA
SEQRES 12 L 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY
SEQRES 13 L 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP
SEQRES 14 L 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS
SEQRES 15 L 213 ALA ASP TYR GLU LYS HIS LYS LEU TYR ALA CYS GLU VAL
SEQRES 16 L 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE
SEQRES 17 L 213 ASN ARG GLY GLU YCM
SEQRES 1 H 220 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS
SEQRES 2 H 220 PRO GLY ALA THR VAL LYS ILE SER CYS LYS ALA SER GLY
SEQRES 3 H 220 TYR THR PHE SER ASP PHE TYR MET TYR TRP VAL ARG GLN
SEQRES 4 H 220 ALA PRO GLY LYS GLY LEU GLU TRP MET GLY LEU ILE ASP
SEQRES 5 H 220 PRO GLU ASP ALA ASP THR MET TYR ALA GLU LYS PHE ARG
SEQRES 6 H 220 GLY ARG VAL THR ILE THR ALA ASP THR SER THR ASP THR
SEQRES 7 H 220 GLY TYR LEU GLU LEU SER SER LEU ARG SER GLU ASP THR
SEQRES 8 H 220 ALA VAL TYR TYR CYS ALA ALA ASP PRO TRP GLU LEU ASN
SEQRES 9 H 220 ALA PHE ASN VAL TRP GLY GLN GLY THR LEU VAL SER VAL
SEQRES 10 H 220 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU
SEQRES 11 H 220 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA
SEQRES 12 H 220 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL
SEQRES 13 H 220 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL
SEQRES 14 H 220 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR
SEQRES 15 H 220 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU
SEQRES 16 H 220 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO
SEQRES 17 H 220 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS
SEQRES 1 B 379 THR GLU LYS LEU TRP VAL THR VAL TYR TYR GLY VAL PRO
SEQRES 2 B 379 VAL TRP LYS GLU ALA THR THR THR LEU PHE CYS ALA SER
SEQRES 3 B 379 ASP ALA LYS ALA TYR ASP THR GLU VAL HIS ASN VAL TRP
SEQRES 4 B 379 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN
SEQRES 5 B 379 GLU VAL VAL LEU VAL ASN VAL THR GLU ASN PHE ASN MET
SEQRES 6 B 379 TRP LYS ASN ASP MET VAL GLU GLN MET HIS GLU ASP ILE
SEQRES 7 B 379 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS
SEQRES 8 B 379 LEU THR GLY GLY SER VAL ILE THR GLN ALA CYS PRO LYS
SEQRES 9 B 379 VAL SER PHE GLU PRO ILE PRO ILE HIS TYR CYS ALA PRO
SEQRES 10 B 379 ALA GLY PHE ALA ILE LEU LYS CYS ASN ASN LYS THR PHE
SEQRES 11 B 379 ASN GLY THR GLY PRO CYS THR ASN VAL SER THR VAL GLN
SEQRES 12 B 379 CYS THR HIS GLY ILE ARG PRO VAL VAL SER SER GLN LEU
SEQRES 13 B 379 LEU LEU ASN GLY SER LEU ALA GLU GLU GLU VAL VAL ILE
SEQRES 14 B 379 ARG SER VAL ASN PHE THR ASP ASN ALA LYS THR ILE ILE
SEQRES 15 B 379 VAL GLN LEU ASN THR SER VAL GLU ILE ASN CYS THR GLY
SEQRES 16 B 379 ALA GLY HIS CYS ASN ILE ALA ARG ALA LYS TRP ASN ASN
SEQRES 17 B 379 THR LEU LYS GLN ILE ALA SER LYS LEU ARG GLU GLN PHE
SEQRES 18 B 379 GLY ASN ASN LYS THR ILE ILE PHE LYS GLN SER SER GLY
SEQRES 19 B 379 GLY ASP PRO GLU ILE VAL THR HIS TRP PHE ASN CYS GLY
SEQRES 20 B 379 GLY GLU PHE PHE TYR CYS ASN SER THR GLN LEU PHE ASN
SEQRES 21 B 379 SER THR TRP PHE ASN SER THR TRP SER THR GLU GLY SER
SEQRES 22 B 379 ASN ASN THR GLU GLY SER ASP THR ILE THR LEU PRO CYS
SEQRES 23 B 379 ARG ILE LYS GLN ILE ILE ASN MET TRP GLN LYS VAL GLY
SEQRES 24 B 379 LYS ALA MET TYR ALA PRO PRO ILE SER GLY GLN ILE ARG
SEQRES 25 B 379 CYS SER SER ASN ILE THR GLY LEU LEU LEU THR ARG ASP
SEQRES 26 B 379 GLY GLY ASN SER ASN ASN GLU SER GLU ILE PHE ARG PRO
SEQRES 27 B 379 GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SER GLU LEU
SEQRES 28 B 379 TYR LYS TYR LYS VAL VAL LYS ILE GLU PRO LEU GLY VAL
SEQRES 29 B 379 ALA PRO THR LYS ALA LYS ARG ARG VAL VAL GLN SER GLU
SEQRES 30 B 379 LYS SER
SEQRES 1 D 184 MET LYS LYS VAL VAL LEU GLY LYS LYS GLY ASP THR VAL
SEQRES 2 D 184 GLU LEU THR CYS THR ALA SER GLN LYS LYS SER ILE GLN
SEQRES 3 D 184 PHE HIS TRP LYS ASN SER ASN GLN ILE LYS ILE LEU GLY
SEQRES 4 D 184 ASN GLN GLY SER PHE LEU THR LYS GLY PRO SER LYS LEU
SEQRES 5 D 184 ASN ASP ARG ALA ASP SER ARG ARG SER LEU TRP ASP GLN
SEQRES 6 D 184 GLY ASN PHE PRO LEU ILE ILE LYS ASN LEU LYS ILE GLU
SEQRES 7 D 184 ASP SER ASP THR TYR ILE CYS GLU VAL GLU ASP GLN LYS
SEQRES 8 D 184 GLU GLU VAL GLN LEU LEU VAL PHE GLY LEU THR ALA ASN
SEQRES 9 D 184 SER ASP THR HIS LEU LEU GLN GLY GLN SER LEU THR LEU
SEQRES 10 D 184 THR LEU GLU SER PRO PRO GLY SER SER PRO SER VAL GLN
SEQRES 11 D 184 CYS ARG SER PRO ARG GLY LYS ASN ILE GLN GLY GLY LYS
SEQRES 12 D 184 THR LEU SER VAL SER GLN LEU GLU LEU GLN ASP SER GLY
SEQRES 13 D 184 THR TRP THR CYS THR VAL LEU GLN ASN GLN LYS LYS VAL
SEQRES 14 D 184 GLU PHE LYS ILE ASP ILE VAL VAL LEU ALA PHE GLN LYS
SEQRES 15 D 184 ALA SER
SEQRES 1 O 213 ASP ILE GLN MET THR GLN SER PRO SER SER VAL SER ALA
SEQRES 2 O 213 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER
SEQRES 3 O 213 GLN ASP ILE SER THR TRP LEU ALA TRP TYR GLN GLN LYS
SEQRES 4 O 213 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER
SEQRES 5 O 213 THR LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 O 213 GLY SER GLY THR ASP PHE SER LEU THR ILE ASN SER LEU
SEQRES 7 O 213 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN ALA
SEQRES 8 O 213 ASN SER PHE PHE THR PHE GLY GLY GLY THR LYS VAL GLU
SEQRES 9 O 213 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE
SEQRES 10 O 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER
SEQRES 11 O 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA
SEQRES 12 O 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY
SEQRES 13 O 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP
SEQRES 14 O 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS
SEQRES 15 O 213 ALA ASP TYR GLU LYS HIS LYS LEU TYR ALA CYS GLU VAL
SEQRES 16 O 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE
SEQRES 17 O 213 ASN ARG GLY GLU YCM
SEQRES 1 P 220 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS
SEQRES 2 P 220 PRO GLY ALA THR VAL LYS ILE SER CYS LYS ALA SER GLY
SEQRES 3 P 220 TYR THR PHE SER ASP PHE TYR MET TYR TRP VAL ARG GLN
SEQRES 4 P 220 ALA PRO GLY LYS GLY LEU GLU TRP MET GLY LEU ILE ASP
SEQRES 5 P 220 PRO GLU ASP ALA ASP THR MET TYR ALA GLU LYS PHE ARG
SEQRES 6 P 220 GLY ARG VAL THR ILE THR ALA ASP THR SER THR ASP THR
SEQRES 7 P 220 GLY TYR LEU GLU LEU SER SER LEU ARG SER GLU ASP THR
SEQRES 8 P 220 ALA VAL TYR TYR CYS ALA ALA ASP PRO TRP GLU LEU ASN
SEQRES 9 P 220 ALA PHE ASN VAL TRP GLY GLN GLY THR LEU VAL SER VAL
SEQRES 10 P 220 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU
SEQRES 11 P 220 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA
SEQRES 12 P 220 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL
SEQRES 13 P 220 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL
SEQRES 14 P 220 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR
SEQRES 15 P 220 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU
SEQRES 16 P 220 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO
SEQRES 17 P 220 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS
MODRES 3JWD ASN A 88 ASN GLYCOSYLATION SITE
MODRES 3JWD ASN A 234 ASN GLYCOSYLATION SITE
MODRES 3JWD ASN A 241 ASN GLYCOSYLATION SITE
MODRES 3JWD ASN A 262 ASN GLYCOSYLATION SITE
MODRES 3JWD ASN A 276 ASN GLYCOSYLATION SITE
MODRES 3JWD ASN A 289 ASN GLYCOSYLATION SITE
MODRES 3JWD ASN A 386 ASN GLYCOSYLATION SITE
MODRES 3JWD ASN A 392 ASN GLYCOSYLATION SITE
MODRES 3JWD ASN A 397 ASN GLYCOSYLATION SITE
MODRES 3JWD ASN A 448 ASN GLYCOSYLATION SITE
MODRES 3JWD ASN B 88 ASN GLYCOSYLATION SITE
MODRES 3JWD ASN B 234 ASN GLYCOSYLATION SITE
MODRES 3JWD ASN B 262 ASN GLYCOSYLATION SITE
MODRES 3JWD ASN B 276 ASN GLYCOSYLATION SITE
MODRES 3JWD ASN B 289 ASN GLYCOSYLATION SITE
MODRES 3JWD ASN B 295 ASN GLYCOSYLATION SITE
MODRES 3JWD ASN B 386 ASN GLYCOSYLATION SITE
MODRES 3JWD ASN B 392 ASN GLYCOSYLATION SITE
MODRES 3JWD ASN B 448 ASN GLYCOSYLATION SITE
MODRES 3JWD YCM L 214 CYS S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE
HET YCM L 214 11
HET NAG A 588 14
HET NAG A 734 14
HET NAG A 741 14
HET NAG A 762 14
HET NAG A 776 14
HET NAG A 789 14
HET NAG A 886 14
HET NAG A 892 14
HET NAG A 897 14
HET NAG A 948 14
HET NAG B 588 14
HET NAG B 734 14
HET NAG B 762 14
HET NAG B 776 14
HET NAG B 789 14
HET NAG B 795 14
HET NAG B 886 14
HET GOL B 1 6
HET NAG B 892 14
HET NAG B 948 14
HET GOL P 215 6
HETNAM YCM S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM GOL GLYCEROL
HETSYN YCM CYSTEINE-S-ACETAMIDE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 YCM C5 H10 N2 O3 S
FORMUL 9 NAG 19(C8 H15 N O6)
FORMUL 26 GOL 2(C3 H8 O3)
FORMUL 30 HOH *450(H2 O)
HELIX 1 1 GLU A 64 CYS A 74 1 11
HELIX 2 2 ASN A 98 SER A 115 1 18
HELIX 3 3 ARG A 335 PHE A 353 1 19
HELIX 4 4 ASP A 368 THR A 373 1 6
HELIX 5 5 SER A 387 PHE A 391 5 5
HELIX 6 6 ASP A 474 TYR A 484 1 11
HELIX 7 7 ARG C 1058 GLY C 1065 5 8
HELIX 8 8 LYS C 1075 SER C 1079 5 5
HELIX 9 9 GLU C 1150 SER C 1154 5 5
HELIX 10 10 GLN L 79 PHE L 83 5 5
HELIX 11 11 SER L 121 LEU L 125 5 5
HELIX 12 12 SER L 182 GLU L 187 1 6
HELIX 13 13 THR H 28 PHE H 32 5 5
HELIX 14 14 ARG H 83 THR H 87 5 5
HELIX 15 15 SER H 127 LYS H 129 5 3
HELIX 16 16 SER H 156 ALA H 158 5 3
HELIX 17 17 SER H 187 LEU H 189 5 3
HELIX 18 18 LYS H 201 ASN H 204 5 4
HELIX 19 19 GLU B 64 CYS B 74 1 11
HELIX 20 20 ASN B 98 LEU B 116 1 19
HELIX 21 21 ARG B 335 ARG B 350 1 16
HELIX 22 22 ASP B 368 THR B 373 1 6
HELIX 23 23 SER B 387 PHE B 391 5 5
HELIX 24 24 ASP B 474 TYR B 486 1 13
HELIX 25 25 ARG D 1058 GLY D 1065 5 8
HELIX 26 26 LYS D 1075 SER D 1079 5 5
HELIX 27 27 GLU D 1150 SER D 1154 5 5
HELIX 28 28 GLN O 79 PHE O 83 5 5
HELIX 29 29 SER O 121 LEU O 125 5 5
HELIX 30 30 SER O 182 GLU O 187 1 6
HELIX 31 31 THR P 28 PHE P 32 5 5
HELIX 32 32 ARG P 83 THR P 87 5 5
HELIX 33 33 SER P 127 LYS P 129 5 3
HELIX 34 34 TRP P 154 ALA P 158 5 5
HELIX 35 35 SER P 187 LEU P 189 5 3
HELIX 36 36 LYS P 201 ASN P 204 5 4
SHEET 1 A 2 TYR A 40 VAL A 42 0
SHEET 2 A 2 GLY A 495 ALA A 497 -1 O ALA A 497 N TYR A 40
SHEET 1 B 5 VAL A 44 GLU A 47 0
SHEET 2 B 5 LYS A 485 GLU A 492 -1 O LYS A 490 N LYS A 46
SHEET 3 B 5 GLY A 222 ASN A 229 -1 N ALA A 224 O VAL A 489
SHEET 4 B 5 ASN A 241 VAL A 245 -1 O SER A 243 N LYS A 227
SHEET 5 B 5 VAL A 84 LEU A 86 -1 N VAL A 84 O THR A 244
SHEET 1 C 4 VAL A 75 THR A 77 0
SHEET 2 C 4 PHE A 53 SER A 56 1
SHEET 3 C 4 ILE A 215 ALA A 219 -1
SHEET 4 C 4 GLN A 246 ILE A 251 -1
SHEET 1 D 2 GLU A 91 MET A 95 0
SHEET 2 D 2 GLY A 235 CYS A 239 -1 O CYS A 239 N GLU A 91
SHEET 1 E 4 SER A 199 GLN A 203 0
SHEET 2 E 4 CYS A 119 THR A 123 -1 N THR A 123 O SER A 199
SHEET 3 E 4 GLY A 431 TYR A 435 -1 O LYS A 432 N LEU A 122
SHEET 4 E 4 GLN A 422 MET A 426 -1 N ILE A 424 O ALA A 433
SHEET 1 F 4 GLN A 258 ASN A 262 0
SHEET 2 F 4 THR A 450 LEU A 453 -1
SHEET 3 F 4 ILE A 285 LEU A 288 -1
SHEET 4 F 4 VAL A 271 ARG A 273 -1
SHEET 1 G 6 ILE A 443 ILE A 449 0
SHEET 2 G 6 VAL A 292 GLY A 298 -1
SHEET 3 G 6 GLY A 329 ALA A 334 -1
SHEET 4 G 6 ASP A 412 ILE A 420 -1
SHEET 5 G 6 GLU A 381 ASN A 386 -1
SHEET 6 G 6 HIS A 374 CYS A 378 -1
SHEET 1 H 4 LEU A 453 ASP A 457 0
SHEET 2 H 4 GLU A 464 GLY A 471 -1
SHEET 3 H 4 THR A 358 LYS A 362 -1
SHEET 4 H 4 SER A 393 TRP A 395 -1
SHEET 1 I 6 LYS C1002 LYS C1007 0
SHEET 2 I 6 GLN C1089 ASN C1103 1 O GLN C1094 N VAL C1004
SHEET 3 I 6 ASP C1080 VAL C1086 -1 N TYR C1082 O VAL C1093
SHEET 4 I 6 PHE C1026 LYS C1029 -1 N HIS C1027 O GLU C1085
SHEET 5 I 6 LYS C1035 ASN C1039 -1 O LEU C1037 N TRP C1028
SHEET 6 I 6 LEU C1044 LYS C1046 -1 O THR C1045 N GLY C1038
SHEET 1 J 4 LYS C1002 LYS C1007 0
SHEET 2 J 4 GLN C1089 ASN C1103 1 O GLN C1094 N VAL C1004
SHEET 3 J 4 LEU C1114 GLU C1119 -1 O GLU C1119 N GLY C1099
SHEET 4 J 4 THR C1143 VAL C1146 -1 O LEU C1144 N LEU C1116
SHEET 1 K 3 VAL C1012 LEU C1014 0
SHEET 2 K 3 LEU C1069 ILE C1071 -1 O LEU C1069 N LEU C1014
SHEET 3 K 3 ALA C1055 ASP C1056 -1 N ASP C1056 O ILE C1070
SHEET 1 L 2 THR C1106 HIS C1107 0
SHEET 2 L 2 GLY C1111 GLN C1112 -1 O GLY C1111 N HIS C1107
SHEET 1 M 4 ASN C1137 GLY C1140 0
SHEET 2 M 4 SER C1127 ARG C1131 -1 N CYS C1130 O ILE C1138
SHEET 3 M 4 GLY C1155 GLN C1163 -1 O THR C1160 N GLN C1129
SHEET 4 M 4 LYS C1166 ILE C1174 -1 O VAL C1168 N VAL C1161
SHEET 1 N 4 GLN L 3 SER L 7 0
SHEET 2 N 4 VAL L 19 ARG L 24 -1 O ARG L 24 N THR L 5
SHEET 3 N 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21
SHEET 4 N 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74
SHEET 1 O 6 SER L 10 ALA L 13 0
SHEET 2 O 6 THR L 102 ILE L 106 1 O LYS L 103 N VAL L 11
SHEET 3 O 6 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102
SHEET 4 O 6 LEU L 33 GLN L 38 -1 N TYR L 36 O TYR L 87
SHEET 5 O 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37
SHEET 6 O 6 THR L 53 LEU L 54 -1 O THR L 53 N TYR L 49
SHEET 1 P 4 SER L 114 PHE L 118 0
SHEET 2 P 4 ALA L 130 PHE L 139 -1 O VAL L 133 N PHE L 118
SHEET 3 P 4 TYR L 173 THR L 180 -1 O LEU L 175 N LEU L 136
SHEET 4 P 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178
SHEET 1 Q 4 ALA L 153 GLN L 155 0
SHEET 2 Q 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153
SHEET 3 Q 4 TYR L 192 THR L 197 -1 O THR L 197 N LYS L 145
SHEET 4 Q 4 VAL L 205 PHE L 209 -1 O VAL L 205 N VAL L 196
SHEET 1 R 4 GLN H 3 GLN H 6 0
SHEET 2 R 4 VAL H 18 SER H 25 -1 O LYS H 23 N VAL H 5
SHEET 3 R 4 THR H 77 LEU H 82 -1 O LEU H 82 N VAL H 18
SHEET 4 R 4 VAL H 67 ASP H 72 -1 N THR H 68 O GLU H 81
SHEET 1 S 6 GLU H 10 LYS H 12 0
SHEET 2 S 6 THR H 107 VAL H 111 1 O SER H 110 N LYS H 12
SHEET 3 S 6 ALA H 88 ALA H 94 -1 N ALA H 88 O VAL H 109
SHEET 4 S 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 91
SHEET 5 S 6 LEU H 45 ASP H 52 -1 O GLU H 46 N ARG H 38
SHEET 6 S 6 ASP H 56 TYR H 59 -1 O ASP H 56 N ASP H 52
SHEET 1 T 4 GLU H 10 LYS H 12 0
SHEET 2 T 4 THR H 107 VAL H 111 1 O SER H 110 N LYS H 12
SHEET 3 T 4 ALA H 88 ALA H 94 -1 N ALA H 88 O VAL H 109
SHEET 4 T 4 VAL H 102 TRP H 103 -1 O VAL H 102 N ALA H 94
SHEET 1 U 4 SER H 120 VAL H 121 0
SHEET 2 U 4 THR H 135 TYR H 145 -1 O LYS H 143 N SER H 120
SHEET 3 U 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA H 136
SHEET 4 U 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181
SHEET 1 V 4 THR H 131 SER H 132 0
SHEET 2 V 4 THR H 135 TYR H 145 -1 O THR H 135 N SER H 132
SHEET 3 V 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145
SHEET 4 V 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177
SHEET 1 W 3 THR H 151 TRP H 154 0
SHEET 2 W 3 TYR H 194 HIS H 200 -1 O ASN H 197 N SER H 153
SHEET 3 W 3 THR H 205 VAL H 211 -1 O VAL H 207 N VAL H 198
SHEET 1 X 2 TYR B 40 VAL B 42 0
SHEET 2 X 2 GLY B 495 ALA B 497 -1
SHEET 1 Y 5 VAL B 44 GLU B 47 0
SHEET 2 Y 5 LYS B 485 GLU B 492 -1
SHEET 3 Y 5 GLY B 222 CYS B 228 -1
SHEET 4 Y 5 ASN B 241 VAL B 245 -1
SHEET 5 Y 5 VAL B 84 LEU B 86 -1
SHEET 1 Z 4 VAL B 75 THR B 77 0
SHEET 2 Z 4 PHE B 53 SER B 56 1
SHEET 3 Z 4 ILE B 215 ALA B 219 -1
SHEET 4 Z 4 GLN B 246 ILE B 251 -1
SHEET 1 AA 2 GLU B 91 MET B 95 0
SHEET 2 AA 2 GLY B 235 CYS B 239 -1
SHEET 1 AB 4 SER B 199 THR B 202 0
SHEET 2 AB 4 CYS B 119 THR B 123 -1
SHEET 3 AB 4 LYS B 432 TYR B 435 -1
SHEET 4 AB 4 GLN B 422 MET B 426 -1
SHEET 1 AC 4 GLN B 258 ASN B 262 0
SHEET 2 AC 4 THR B 450 LEU B 453 -1
SHEET 3 AC 4 ILE B 285 LEU B 288 -1
SHEET 4 AC 4 VAL B 271 ARG B 273 -1
SHEET 1 AD 6 ILE B 443 ILE B 449 0
SHEET 2 AD 6 VAL B 292 GLY B 298 -1
SHEET 3 AD 6 GLY B 329 ALA B 334 -1
SHEET 4 AD 6 ASP B 412 LYS B 421 -1
SHEET 5 AD 6 GLU B 381 ASN B 386 -1
SHEET 6 AD 6 HIS B 374 CYS B 378 -1
SHEET 1 AE 4 LEU B 453 ASP B 457 0
SHEET 2 AE 4 GLU B 464 GLY B 471 -1
SHEET 3 AE 4 THR B 358 LYS B 362 -1
SHEET 4 AE 4 SER B 393 TRP B 395 -1
SHEET 1 AF 6 LYS D1002 LYS D1007 0
SHEET 2 AF 6 LYS D1090 ASN D1103 1 O LEU D1096 N GLY D1006
SHEET 3 AF 6 THR D1081 GLU D1085 -1 N TYR D1082 O VAL D1093
SHEET 4 AF 6 HIS D1027 LYS D1029 -1 N LYS D1029 O ILE D1083
SHEET 5 AF 6 LYS D1035 ASN D1039 -1 O ILE D1036 N TRP D1028
SHEET 6 AF 6 LEU D1044 LYS D1046 -1 O THR D1045 N GLY D1038
SHEET 1 AG 4 LYS D1002 LYS D1007 0
SHEET 2 AG 4 LYS D1090 ASN D1103 1 O LEU D1096 N GLY D1006
SHEET 3 AG 4 LEU D1114 GLU D1119 -1 O GLU D1119 N GLY D1099
SHEET 4 AG 4 THR D1143 VAL D1146 -1 O VAL D1146 N LEU D1114
SHEET 1 AH 3 THR D1011 LEU D1014 0
SHEET 2 AH 3 LEU D1069 LYS D1072 -1 O LEU D1069 N LEU D1014
SHEET 3 AH 3 ALA D1055 ASP D1056 -1 N ASP D1056 O ILE D1070
SHEET 1 AI 2 THR D1106 HIS D1107 0
SHEET 2 AI 2 GLY D1111 GLN D1112 -1
SHEET 1 AJ 4 ASN D1137 GLY D1140 0
SHEET 2 AJ 4 VAL D1128 ARG D1131 -1 N CYS D1130 O ILE D1138
SHEET 3 AJ 4 THR D1156 GLN D1163 -1 O THR D1160 N GLN D1129
SHEET 4 AJ 4 LYS D1166 ASP D1173 -1 O VAL D1168 N VAL D1161
SHEET 1 AK 4 MET O 4 SER O 7 0
SHEET 2 AK 4 VAL O 19 ALA O 25 -1 O ARG O 24 N THR O 5
SHEET 3 AK 4 ASP O 70 ILE O 75 -1 O LEU O 73 N ILE O 21
SHEET 4 AK 4 SER O 63 GLY O 66 -1 N SER O 63 O THR O 74
SHEET 1 AL 6 SER O 10 ALA O 13 0
SHEET 2 AL 6 THR O 102 ILE O 106 1 O GLU O 105 N VAL O 11
SHEET 3 AL 6 THR O 85 GLN O 90 -1 N TYR O 86 O THR O 102
SHEET 4 AL 6 LEU O 33 GLN O 38 -1 N TYR O 36 O TYR O 87
SHEET 5 AL 6 LYS O 45 TYR O 49 -1 O LEU O 47 N TRP O 35
SHEET 6 AL 6 THR O 53 LEU O 54 -1 O THR O 53 N TYR O 49
SHEET 1 AM 4 SER O 114 PHE O 118 0
SHEET 2 AM 4 SER O 131 PHE O 139 -1 O LEU O 135 N PHE O 116
SHEET 3 AM 4 TYR O 173 THR O 180 -1 O LEU O 179 N VAL O 132
SHEET 4 AM 4 SER O 159 THR O 164 -1 N GLN O 160 O THR O 178
SHEET 1 AN 2 ALA O 144 VAL O 146 0
SHEET 2 AN 2 VAL O 196 HIS O 198 -1 O THR O 197 N LYS O 145
SHEET 1 AO 4 LEU O 154 GLN O 155 0
SHEET 2 AO 4 TRP O 148 VAL O 150 -1 N TRP O 148 O GLN O 155
SHEET 3 AO 4 LEU O 191 ALA O 193 -1 O ALA O 193 N LYS O 149
SHEET 4 AO 4 PHE O 209 ASN O 210 -1 O PHE O 209 N TYR O 192
SHEET 1 AP 4 GLN P 3 GLN P 6 0
SHEET 2 AP 4 VAL P 18 SER P 25 -1 O LYS P 23 N VAL P 5
SHEET 3 AP 4 THR P 77 LEU P 82 -1 O LEU P 82 N VAL P 18
SHEET 4 AP 4 VAL P 67 ASP P 72 -1 N ASP P 72 O THR P 77
SHEET 1 AQ 6 GLU P 10 LYS P 12 0
SHEET 2 AQ 6 THR P 107 VAL P 111 1 O LEU P 108 N GLU P 10
SHEET 3 AQ 6 ALA P 88 TYR P 91 -1 N TYR P 90 O THR P 107
SHEET 4 AQ 6 MET P 34 GLN P 39 -1 N GLN P 39 O VAL P 89
SHEET 5 AQ 6 LEU P 45 ASP P 52 -1 O MET P 48 N TRP P 36
SHEET 6 AQ 6 ASP P 56 TYR P 59 -1 O MET P 58 N LEU P 50
SHEET 1 AR 4 GLU P 10 LYS P 12 0
SHEET 2 AR 4 THR P 107 VAL P 111 1
SHEET 3 AR 4 ALA P 88 ALA P 94 -1
SHEET 4 AR 4 VAL P 102 TRP P 103 -1
SHEET 1 AS 4 SER P 120 VAL P 121 0
SHEET 2 AS 4 THR P 135 TYR P 145 -1
SHEET 3 AS 4 TYR P 176 PRO P 185 -1
SHEET 4 AS 4 VAL P 163 THR P 165 -1
SHEET 1 AT 4 THR P 131 SER P 132 0
SHEET 2 AT 4 THR P 135 TYR P 145 -1
SHEET 3 AT 4 TYR P 176 PRO P 185 -1
SHEET 4 AT 4 VAL P 169 LEU P 170 -1
SHEET 1 AU 3 THR P 151 TRP P 154 0
SHEET 2 AU 3 TYR P 194 HIS P 200 -1
SHEET 3 AU 3 THR P 205 VAL P 211 -1
SSBOND 1 CYS A 54 CYS A 74 1555 1555 2.03
SSBOND 2 CYS A 119 CYS A 205 1555 1555 2.03
SSBOND 3 CYS A 218 CYS A 247 1555 1555 2.03
SSBOND 4 CYS A 228 CYS A 239 1555 1555 2.03
SSBOND 5 CYS A 296 CYS A 331 1555 1555 2.03
SSBOND 6 CYS A 378 CYS A 445 1555 1555 2.03
SSBOND 7 CYS A 385 CYS A 418 1555 1555 2.03
SSBOND 8 CYS C 1016 CYS C 1084 1555 1555 2.04
SSBOND 9 CYS C 1130 CYS C 1159 1555 1555 2.03
SSBOND 10 CYS L 23 CYS L 88 1555 1555 2.03
SSBOND 11 CYS L 134 CYS L 194 1555 1555 2.04
SSBOND 12 CYS H 22 CYS H 92 1555 1555 2.03
SSBOND 13 CYS H 140 CYS H 196 1555 1555 2.03
SSBOND 14 CYS B 54 CYS B 74 1555 1555 2.03
SSBOND 15 CYS B 119 CYS B 205 1555 1555 2.03
SSBOND 16 CYS B 218 CYS B 247 1555 1555 2.03
SSBOND 17 CYS B 228 CYS B 239 1555 1555 2.03
SSBOND 18 CYS B 296 CYS B 331 1555 1555 2.03
SSBOND 19 CYS B 378 CYS B 445 1555 1555 2.03
SSBOND 20 CYS B 385 CYS B 418 1555 1555 2.03
SSBOND 21 CYS D 1016 CYS D 1084 1555 1555 2.03
SSBOND 22 CYS D 1130 CYS D 1159 1555 1555 2.03
SSBOND 23 CYS O 23 CYS O 88 1555 1555 2.04
SSBOND 24 CYS O 134 CYS O 194 1555 1555 2.03
SSBOND 25 CYS P 22 CYS P 92 1555 1555 2.03
SSBOND 26 CYS P 140 CYS P 196 1555 1555 2.03
LINK ND2 ASN A 88 C1 NAG A 588 1555 1555 1.44
LINK ND2 ASN A 234 C1 NAG A 734 1555 1555 1.44
LINK ND2 ASN A 241 C1 NAG A 741 1555 1555 1.44
LINK ND2 ASN A 262 C1 NAG A 762 1555 1555 1.44
LINK ND2 ASN A 276 C1 NAG A 776 1555 1555 1.44
LINK ND2 ASN A 289 C1 NAG A 789 1555 1555 1.44
LINK ND2 ASN A 386 C1 NAG A 886 1555 1555 1.45
LINK ND2 ASN A 392 C1 NAG A 892 1555 1555 1.44
LINK ND2 ASN A 397 C1 NAG A 897 1555 1555 1.44
LINK ND2 ASN A 448 C1 NAG A 948 1555 1555 1.44
LINK C GLU L 213 N YCM L 214 1555 1555 1.33
LINK ND2 ASN B 88 C1 NAG B 588 1555 1555 1.44
LINK ND2 ASN B 234 C1 NAG B 734 1555 1555 1.44
LINK ND2 ASN B 262 C1 NAG B 762 1555 1555 1.44
LINK ND2 ASN B 276 C1 NAG B 776 1555 1555 1.44
LINK ND2 ASN B 289 C1 NAG B 789 1555 1555 1.44
LINK ND2 ASN B 295 C1 NAG B 795 1555 1555 1.44
LINK ND2 ASN B 386 C1 NAG B 886 1555 1555 1.44
LINK ND2 ASN B 392 C1 NAG B 892 1555 1555 1.44
LINK ND2 ASN B 448 C1 NAG B 948 1555 1555 1.44
CISPEP 1 ASP A 78 PRO A 79 0 -9.03
CISPEP 2 SER L 7 PRO L 8 0 -1.71
CISPEP 3 TYR L 140 PRO L 141 0 2.14
CISPEP 4 PHE H 146 PRO H 147 0 -7.19
CISPEP 5 GLU H 148 PRO H 149 0 1.28
CISPEP 6 ASP B 78 PRO B 79 0 -6.87
CISPEP 7 SER O 7 PRO O 8 0 -1.94
CISPEP 8 TYR O 140 PRO O 141 0 2.11
CISPEP 9 PHE P 146 PRO P 147 0 -5.69
CISPEP 10 GLU P 148 PRO P 149 0 -4.83
CRYST1 83.112 172.954 193.144 90.00 90.00 90.00 P 21 21 21 8
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 0.012032 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005782 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005177 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
