HEADER IMMUNE SYSTEM 11-SEP-17 6AZL
TITLE STRUCTURE OF CETUXIMAB WITH AMINOHEPTANOIC ACID-LINKED N-
TITLE 2 CARBOXYETHYLARGININE MEDITOPE VARIANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CETUXIMAB FAB LIGHT CHAIN;
COMPND 3 CHAIN: A, C;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: CHIMERIC MURINE/HUMAN ANTIBODY; PURIFIED FROM ERBITUX;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: CETUXIMAB FAB HEAVY CHAIN;
COMPND 8 CHAIN: B, D;
COMPND 9 ENGINEERED: YES;
COMPND 10 OTHER_DETAILS: CHIMERIC MURINE/HUMAN ANTIBODY; PURIFIED FROM ERBITUX;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: MEDITOPE;
COMPND 13 CHAIN: E, F;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS, HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 10090, 9606;
SOURCE 4 EXPRESSION_SYSTEM: UNIDENTIFIED;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 32644;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS, HOMO SAPIENS;
SOURCE 8 ORGANISM_TAXID: 10090, 9606;
SOURCE 9 EXPRESSION_SYSTEM: UNIDENTIFIED;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 32644;
SOURCE 11 MOL_ID: 3;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 14 ORGANISM_TAXID: 32630
KEYWDS ANTIBODY, ANTI-EGFR, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR K.P.BZYMEK,J.C.WILLIAMS
REVDAT 3 15-NOV-23 6AZL 1 LINK
REVDAT 2 04-OCT-23 6AZL 1 REMARK
REVDAT 1 13-DEC-17 6AZL 0
JRNL AUTH K.P.BZYMEK,Y.MA,K.N.AVERY,D.A.HORNE,J.C.WILLIAMS
JRNL TITL MEDITOPE-FAB INTERACTION: THREADING THE HOLE.
JRNL REF ACTA CRYSTALLOGR F STRUCT V. 73 688 2017
JRNL REF 2 BIOL COMMUN
JRNL REFN ESSN 2053-230X
JRNL PMID 29199990
JRNL DOI 10.1107/S2053230X17016272
REMARK 2
REMARK 2 RESOLUTION. 2.48 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.12_2829
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) : 2.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.17
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 40961
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2048
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 33.1764 - 6.1080 1.00 2807 147 0.2102 0.2084
REMARK 3 2 6.1080 - 4.8530 1.00 2675 141 0.1577 0.1922
REMARK 3 3 4.8530 - 4.2409 1.00 2639 139 0.1297 0.1588
REMARK 3 4 4.2409 - 3.8538 1.00 2632 139 0.1416 0.1726
REMARK 3 5 3.8538 - 3.5780 1.00 2600 137 0.1580 0.1921
REMARK 3 6 3.5780 - 3.3672 1.00 2609 137 0.1576 0.2394
REMARK 3 7 3.3672 - 3.1987 1.00 2579 136 0.1770 0.2190
REMARK 3 8 3.1987 - 3.0596 1.00 2602 137 0.1930 0.2659
REMARK 3 9 3.0596 - 2.9419 1.00 2580 135 0.1899 0.2571
REMARK 3 10 2.9419 - 2.8404 1.00 2573 136 0.1888 0.2452
REMARK 3 11 2.8404 - 2.7516 1.00 2589 136 0.1787 0.2487
REMARK 3 12 2.7516 - 2.6730 1.00 2562 135 0.1802 0.2456
REMARK 3 13 2.6730 - 2.6027 1.00 2559 134 0.1736 0.2434
REMARK 3 14 2.6027 - 2.5392 1.00 2589 137 0.1829 0.2469
REMARK 3 15 2.5392 - 2.4815 0.91 2318 122 0.2077 0.3021
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.880
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.008 6940
REMARK 3 ANGLE : 1.168 9457
REMARK 3 CHIRALITY : 0.079 1064
REMARK 3 PLANARITY : 0.005 1210
REMARK 3 DIHEDRAL : 10.922 4135
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 23
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1:25 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.4756 23.6096 -19.4194
REMARK 3 T TENSOR
REMARK 3 T11: 0.2275 T22: 0.1984
REMARK 3 T33: 0.1100 T12: 0.0328
REMARK 3 T13: -0.0507 T23: 0.0114
REMARK 3 L TENSOR
REMARK 3 L11: 0.4009 L22: 0.1503
REMARK 3 L33: 0.2852 L12: -0.0238
REMARK 3 L13: -0.3503 L23: -0.0490
REMARK 3 S TENSOR
REMARK 3 S11: 0.0605 S12: -0.0795 S13: 0.0381
REMARK 3 S21: -0.0835 S22: 0.1348 S23: -0.2520
REMARK 3 S31: 0.2283 S32: 0.2433 S33: 0.0146
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 26:75 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.2327 26.3381 -13.4153
REMARK 3 T TENSOR
REMARK 3 T11: 0.1857 T22: 0.1664
REMARK 3 T33: 0.0987 T12: -0.0117
REMARK 3 T13: -0.0448 T23: 0.0408
REMARK 3 L TENSOR
REMARK 3 L11: 0.2935 L22: 0.5217
REMARK 3 L33: 0.4435 L12: -0.1185
REMARK 3 L13: -0.3218 L23: 0.3902
REMARK 3 S TENSOR
REMARK 3 S11: 0.0082 S12: 0.1084 S13: -0.0768
REMARK 3 S21: 0.0915 S22: -0.0024 S23: 0.0588
REMARK 3 S31: 0.0858 S32: 0.0181 S33: -0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 76:90 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.2808 23.9942 -21.7019
REMARK 3 T TENSOR
REMARK 3 T11: 0.2091 T22: 0.1798
REMARK 3 T33: 0.1360 T12: -0.0167
REMARK 3 T13: -0.0228 T23: -0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 0.1249 L22: 0.1095
REMARK 3 L33: 0.0163 L12: -0.0770
REMARK 3 L13: -0.0179 L23: -0.0220
REMARK 3 S TENSOR
REMARK 3 S11: 0.0638 S12: 0.0771 S13: -0.1343
REMARK 3 S21: 0.0235 S22: -0.0761 S23: -0.1545
REMARK 3 S31: 0.0855 S32: -0.0463 S33: -0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 91:128 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.1739 31.4922 -37.0266
REMARK 3 T TENSOR
REMARK 3 T11: 0.1306 T22: 0.0672
REMARK 3 T33: 0.1069 T12: -0.0030
REMARK 3 T13: -0.0257 T23: 0.0454
REMARK 3 L TENSOR
REMARK 3 L11: 0.2845 L22: 0.1054
REMARK 3 L33: 0.4591 L12: -0.0920
REMARK 3 L13: -0.2683 L23: 0.3875
REMARK 3 S TENSOR
REMARK 3 S11: -0.0076 S12: -0.0619 S13: 0.0133
REMARK 3 S21: 0.0526 S22: 0.0288 S23: 0.0213
REMARK 3 S31: 0.0007 S32: -0.1011 S33: 0.0005
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 129:150 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.9040 27.2138 -50.9330
REMARK 3 T TENSOR
REMARK 3 T11: 0.0880 T22: 0.1406
REMARK 3 T33: 0.2037 T12: -0.0008
REMARK 3 T13: -0.0204 T23: 0.0500
REMARK 3 L TENSOR
REMARK 3 L11: 0.1024 L22: 0.1241
REMARK 3 L33: 0.2231 L12: -0.0082
REMARK 3 L13: 0.0142 L23: 0.0515
REMARK 3 S TENSOR
REMARK 3 S11: 0.0421 S12: 0.0037 S13: -0.1117
REMARK 3 S21: -0.0344 S22: 0.0213 S23: 0.0571
REMARK 3 S31: -0.0069 S32: 0.1212 S33: 0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 151:163 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.1006 33.6060 -55.7591
REMARK 3 T TENSOR
REMARK 3 T11: 0.0980 T22: 0.1827
REMARK 3 T33: 0.2022 T12: -0.0216
REMARK 3 T13: -0.0184 T23: -0.0269
REMARK 3 L TENSOR
REMARK 3 L11: 0.0265 L22: 0.0499
REMARK 3 L33: 0.0420 L12: -0.0339
REMARK 3 L13: 0.0123 L23: -0.0577
REMARK 3 S TENSOR
REMARK 3 S11: 0.0069 S12: 0.0901 S13: -0.1003
REMARK 3 S21: -0.0449 S22: -0.0398 S23: -0.0633
REMARK 3 S31: 0.0547 S32: -0.0588 S33: 0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 164:212 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.8082 28.2593 -54.8807
REMARK 3 T TENSOR
REMARK 3 T11: 0.1266 T22: 0.1413
REMARK 3 T33: 0.1637 T12: 0.0111
REMARK 3 T13: -0.0019 T23: 0.0479
REMARK 3 L TENSOR
REMARK 3 L11: 0.5653 L22: 0.5745
REMARK 3 L33: 0.2582 L12: -0.1088
REMARK 3 L13: 0.0157 L23: 0.1798
REMARK 3 S TENSOR
REMARK 3 S11: 0.0247 S12: 0.1158 S13: -0.0374
REMARK 3 S21: -0.1030 S22: -0.0045 S23: -0.0070
REMARK 3 S31: -0.0433 S32: 0.0779 S33: -0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1:33 )
REMARK 3 ORIGIN FOR THE GROUP (A): -38.7965 47.9235 -20.1624
REMARK 3 T TENSOR
REMARK 3 T11: 0.1597 T22: 0.2473
REMARK 3 T33: 0.1849 T12: -0.0281
REMARK 3 T13: -0.0106 T23: 0.0132
REMARK 3 L TENSOR
REMARK 3 L11: 0.0097 L22: 0.2119
REMARK 3 L33: 0.1883 L12: 0.0147
REMARK 3 L13: -0.0073 L23: 0.2064
REMARK 3 S TENSOR
REMARK 3 S11: -0.2003 S12: -0.2258 S13: 0.1978
REMARK 3 S21: -0.0425 S22: 0.1168 S23: 0.1665
REMARK 3 S31: -0.2881 S32: -0.1347 S33: -0.0010
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 34:130 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.8813 46.9308 -19.5898
REMARK 3 T TENSOR
REMARK 3 T11: 0.1756 T22: 0.1504
REMARK 3 T33: 0.1396 T12: -0.0231
REMARK 3 T13: 0.0126 T23: 0.0216
REMARK 3 L TENSOR
REMARK 3 L11: 0.1899 L22: 0.0150
REMARK 3 L33: 0.6969 L12: 0.1205
REMARK 3 L13: 0.4105 L23: 0.0263
REMARK 3 S TENSOR
REMARK 3 S11: -0.0029 S12: -0.0459 S13: 0.0158
REMARK 3 S21: 0.0318 S22: 0.0026 S23: 0.0329
REMARK 3 S31: -0.1486 S32: 0.0964 S33: 0.0000
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 131:151 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.4220 30.8791 -52.8069
REMARK 3 T TENSOR
REMARK 3 T11: 0.1232 T22: 0.1188
REMARK 3 T33: 0.2397 T12: -0.0112
REMARK 3 T13: -0.0090 T23: -0.0123
REMARK 3 L TENSOR
REMARK 3 L11: 0.2296 L22: 0.0027
REMARK 3 L33: 0.2841 L12: -0.0251
REMARK 3 L13: 0.0792 L23: 0.0171
REMARK 3 S TENSOR
REMARK 3 S11: 0.0065 S12: -0.0365 S13: -0.3244
REMARK 3 S21: -0.1794 S22: -0.0174 S23: -0.1714
REMARK 3 S31: -0.0490 S32: -0.0156 S33: 0.0000
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 152:194 )
REMARK 3 ORIGIN FOR THE GROUP (A): -36.4806 35.4529 -43.6504
REMARK 3 T TENSOR
REMARK 3 T11: 0.0687 T22: 0.1055
REMARK 3 T33: 0.1871 T12: -0.0162
REMARK 3 T13: -0.0144 T23: 0.0249
REMARK 3 L TENSOR
REMARK 3 L11: 0.0574 L22: 0.4110
REMARK 3 L33: 0.6154 L12: -0.1239
REMARK 3 L13: -0.0691 L23: -0.0637
REMARK 3 S TENSOR
REMARK 3 S11: 0.0224 S12: -0.0919 S13: 0.1260
REMARK 3 S21: 0.0728 S22: -0.0927 S23: 0.1286
REMARK 3 S31: 0.0413 S32: -0.0255 S33: 0.0000
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 195:220 )
REMARK 3 ORIGIN FOR THE GROUP (A): -45.2886 38.5661 -47.4459
REMARK 3 T TENSOR
REMARK 3 T11: 0.1150 T22: 0.1080
REMARK 3 T33: 0.1960 T12: -0.0046
REMARK 3 T13: -0.0085 T23: -0.0338
REMARK 3 L TENSOR
REMARK 3 L11: 0.3041 L22: 0.0408
REMARK 3 L33: 0.1700 L12: -0.0933
REMARK 3 L13: 0.0303 L23: -0.0693
REMARK 3 S TENSOR
REMARK 3 S11: -0.0425 S12: -0.1109 S13: 0.0263
REMARK 3 S21: -0.0443 S22: -0.0432 S23: 0.1883
REMARK 3 S31: -0.0245 S32: -0.1590 S33: 0.0000
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1:25 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.7135 16.9750 -18.2450
REMARK 3 T TENSOR
REMARK 3 T11: 0.1960 T22: 0.1881
REMARK 3 T33: 0.1929 T12: 0.0269
REMARK 3 T13: -0.0042 T23: 0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 0.1776 L22: 0.0715
REMARK 3 L33: 0.1924 L12: 0.0169
REMARK 3 L13: 0.1845 L23: 0.0869
REMARK 3 S TENSOR
REMARK 3 S11: -0.0252 S12: -0.1476 S13: 0.0818
REMARK 3 S21: -0.1473 S22: -0.0742 S23: 0.0023
REMARK 3 S31: -0.1348 S32: -0.1148 S33: -0.0000
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 26:75 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.1023 14.2376 -11.8558
REMARK 3 T TENSOR
REMARK 3 T11: 0.2145 T22: 0.1495
REMARK 3 T33: 0.0910 T12: 0.0148
REMARK 3 T13: 0.0111 T23: -0.0193
REMARK 3 L TENSOR
REMARK 3 L11: 0.4067 L22: 0.4239
REMARK 3 L33: 0.5017 L12: -0.0466
REMARK 3 L13: 0.4191 L23: -0.2233
REMARK 3 S TENSOR
REMARK 3 S11: 0.1303 S12: 0.0103 S13: 0.0797
REMARK 3 S21: -0.0744 S22: 0.0820 S23: 0.0270
REMARK 3 S31: -0.3206 S32: 0.0541 S33: 0.0007
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 76:128 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.8573 9.8133 -30.3155
REMARK 3 T TENSOR
REMARK 3 T11: 0.2095 T22: 0.0825
REMARK 3 T33: 0.1133 T12: -0.0091
REMARK 3 T13: 0.0217 T23: -0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.2082 L22: -0.0379
REMARK 3 L33: 0.4732 L12: -0.1416
REMARK 3 L13: 0.3485 L23: -0.2445
REMARK 3 S TENSOR
REMARK 3 S11: -0.0005 S12: -0.0031 S13: -0.0219
REMARK 3 S21: 0.0622 S22: 0.0383 S23: -0.0267
REMARK 3 S31: -0.1313 S32: -0.0794 S33: -0.0005
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 129:150 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.0816 10.1287 -48.9550
REMARK 3 T TENSOR
REMARK 3 T11: 0.0918 T22: 0.0998
REMARK 3 T33: 0.2070 T12: -0.0008
REMARK 3 T13: 0.0089 T23: -0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 0.0826 L22: 0.1208
REMARK 3 L33: 0.2424 L12: 0.1303
REMARK 3 L13: -0.0199 L23: 0.0683
REMARK 3 S TENSOR
REMARK 3 S11: 0.0268 S12: -0.0452 S13: 0.0533
REMARK 3 S21: -0.0702 S22: 0.1007 S23: 0.0277
REMARK 3 S31: 0.0619 S32: 0.0062 S33: -0.0000
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 151:163 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.1218 3.6194 -53.0506
REMARK 3 T TENSOR
REMARK 3 T11: 0.0806 T22: 0.1952
REMARK 3 T33: 0.1787 T12: -0.0173
REMARK 3 T13: -0.0363 T23: 0.0179
REMARK 3 L TENSOR
REMARK 3 L11: 0.1375 L22: 0.7782
REMARK 3 L33: 0.1559 L12: -0.0262
REMARK 3 L13: -0.1458 L23: -0.0202
REMARK 3 S TENSOR
REMARK 3 S11: 0.0924 S12: 0.1497 S13: -0.0089
REMARK 3 S21: -0.0147 S22: 0.1391 S23: 0.1450
REMARK 3 S31: 0.0470 S32: 0.2789 S33: 0.0822
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 164:212 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.4234 8.7243 -52.9158
REMARK 3 T TENSOR
REMARK 3 T11: 0.1178 T22: 0.1492
REMARK 3 T33: 0.1251 T12: -0.0069
REMARK 3 T13: -0.0421 T23: -0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 0.7705 L22: 0.4122
REMARK 3 L33: 0.4932 L12: 0.1299
REMARK 3 L13: -0.0514 L23: 0.0258
REMARK 3 S TENSOR
REMARK 3 S11: -0.0956 S12: 0.1203 S13: 0.0134
REMARK 3 S21: -0.0545 S22: 0.1093 S23: -0.0057
REMARK 3 S31: -0.0453 S32: 0.1238 S33: -0.0000
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1:117 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.1350 -7.0409 -13.8715
REMARK 3 T TENSOR
REMARK 3 T11: 0.2019 T22: 0.1524
REMARK 3 T33: 0.1304 T12: 0.0201
REMARK 3 T13: -0.0115 T23: -0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 0.0369 L22: 0.3640
REMARK 3 L33: 0.8265 L12: 0.3453
REMARK 3 L13: 0.1601 L23: 0.0715
REMARK 3 S TENSOR
REMARK 3 S11: -0.0734 S12: -0.0157 S13: -0.0248
REMARK 3 S21: -0.0100 S22: 0.1221 S23: 0.0318
REMARK 3 S31: 0.1407 S32: 0.0671 S33: 0.0000
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 118:140 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.0711 -5.0418 -45.7558
REMARK 3 T TENSOR
REMARK 3 T11: 0.0427 T22: 0.0682
REMARK 3 T33: 0.1963 T12: 0.0117
REMARK 3 T13: 0.0423 T23: 0.0259
REMARK 3 L TENSOR
REMARK 3 L11: 0.3010 L22: 0.1936
REMARK 3 L33: 0.9660 L12: -0.1325
REMARK 3 L13: -0.1136 L23: 0.4148
REMARK 3 S TENSOR
REMARK 3 S11: -0.0893 S12: 0.0850 S13: 0.2024
REMARK 3 S21: 0.0438 S22: 0.0187 S23: -0.1185
REMARK 3 S31: 0.4337 S32: 0.1036 S33: -0.0478
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 141:220 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.2175 0.8090 -43.3921
REMARK 3 T TENSOR
REMARK 3 T11: 0.1027 T22: 0.1225
REMARK 3 T33: 0.1695 T12: -0.0076
REMARK 3 T13: -0.0179 T23: -0.0324
REMARK 3 L TENSOR
REMARK 3 L11: 0.0112 L22: 0.6692
REMARK 3 L33: 0.6838 L12: 0.1715
REMARK 3 L13: -0.1597 L23: -0.1753
REMARK 3 S TENSOR
REMARK 3 S11: 0.0083 S12: -0.0420 S13: -0.0480
REMARK 3 S21: 0.0019 S22: -0.0236 S23: -0.0402
REMARK 3 S31: 0.0547 S32: 0.1028 S33: 0.0000
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 2:11 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.2037 36.3287 -30.7885
REMARK 3 T TENSOR
REMARK 3 T11: 0.1470 T22: 0.2325
REMARK 3 T33: 0.2140 T12: 0.0081
REMARK 3 T13: -0.0032 T23: 0.0368
REMARK 3 L TENSOR
REMARK 3 L11: 0.0333 L22: 0.0392
REMARK 3 L33: 0.0585 L12: 0.0224
REMARK 3 L13: 0.0418 L23: 0.0197
REMARK 3 S TENSOR
REMARK 3 S11: 0.1424 S12: -0.1266 S13: 0.2008
REMARK 3 S21: -0.5014 S22: 0.0344 S23: 0.2344
REMARK 3 S31: -0.0312 S32: -0.0540 S33: 0.0012
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 2:11 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.4413 2.7400 -28.1088
REMARK 3 T TENSOR
REMARK 3 T11: 0.1588 T22: 0.2421
REMARK 3 T33: 0.1822 T12: 0.0017
REMARK 3 T13: -0.0573 T23: -0.0147
REMARK 3 L TENSOR
REMARK 3 L11: 0.0681 L22: 0.2809
REMARK 3 L33: 0.0416 L12: -0.1411
REMARK 3 L13: -0.0467 L23: 0.0993
REMARK 3 S TENSOR
REMARK 3 S11: 0.2368 S12: -0.1782 S13: 0.1573
REMARK 3 S21: -0.4876 S22: 0.0183 S23: 0.0344
REMARK 3 S31: 0.2597 S32: -0.1414 S33: 0.0167
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6AZL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-17.
REMARK 100 THE DEPOSITION ID IS D_1000230042.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40967
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.480
REMARK 200 RESOLUTION RANGE LOW (A) : 33.173
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.03200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 42.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.48
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.10300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 14.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 4GW1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M CITRATE PH 5.5, 1.8 M AMMONIUM
REMARK 280 SULFATE, 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 32.28500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 106.05500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.52500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 106.05500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.28500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.52500
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, F
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 ALA A 213
REMARK 465 SER B 221
REMARK 465 ALA C 213
REMARK 465 SER D 134
REMARK 465 LYS D 135
REMARK 465 SER D 136
REMARK 465 THR D 137
REMARK 465 SER D 138
REMARK 465 SER D 221
REMARK 465 011 E 12
REMARK 465 011 F 12
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 169 CG CD CE NZ
REMARK 470 GLN B 1 CG CD OE1 NE2
REMARK 470 ARG C 24 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 169 CG CD CE NZ
REMARK 470 GLN D 1 CG CD OE1 NE2
REMARK 470 LYS F 11 CG CD CE NZ
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 O HOH B 351 O HOH B 389 1.86
REMARK 500 O SER A 60 O HOH A 401 1.90
REMARK 500 O HOH D 331 O HOH D 386 2.00
REMARK 500 O HOH D 387 O HOH D 391 2.01
REMARK 500 OE2 GLU C 161 O HOH C 401 2.02
REMARK 500 O ALA A 144 O HOH A 402 2.02
REMARK 500 OE1 GLU B 105 O HOH B 301 2.05
REMARK 500 O HOH B 398 O HOH B 405 2.08
REMARK 500 O HOH B 364 O HOH B 373 2.08
REMARK 500 O HOH A 463 O HOH A 502 2.09
REMARK 500 OE2 GLU A 123 O HOH A 403 2.10
REMARK 500 O HOH D 337 O HOH D 362 2.13
REMARK 500 OE1 GLU A 123 O HOH A 404 2.13
REMARK 500 O GLY C 64 O HOH C 402 2.13
REMARK 500 OD1 ASN C 93 O HOH C 403 2.14
REMARK 500 O THR C 164 O HOH C 404 2.18
REMARK 500 O HOH A 440 O HOH A 451 2.18
REMARK 500 OG SER A 14 O HOH A 405 2.18
REMARK 500 O HOH C 433 O HOH C 509 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 406 O HOH D 368 3554 1.94
REMARK 500 O HOH B 380 O HOH C 464 3454 2.13
REMARK 500 O HOH A 489 O HOH C 433 4455 2.19
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 ALA A 51 -43.95 66.90
REMARK 500 SER A 52 -7.91 -141.75
REMARK 500 ASN A 138 70.50 48.87
REMARK 500 ASN A 152 -8.74 69.96
REMARK 500 SER A 171 16.11 59.27
REMARK 500 SER B 15 -9.15 70.86
REMARK 500 ASP B 150 61.94 66.12
REMARK 500 ALA C 51 -46.29 72.36
REMARK 500 ALA C 84 176.26 175.82
REMARK 500 ASN C 138 70.35 55.90
REMARK 500 SER D 15 -2.70 72.99
REMARK 500 SER D 84 58.97 38.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5ID0 RELATED DB: PDB
REMARK 900 RELATED ID: 6AU5 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SEQUENCE OF CETUXIMAB FAB LIGHT CHAIN IN THIS ENTRY MATCHES TO THE
REMARK 999 SEQUENCE OF CETUXIMAB FAB LIGHT CHAIN FROM THE FIRST DEPOSITED
REMARK 999 CETUXIMAB STRUCTURE IN PDB (1YY8)
DBREF 6AZL A 1 107 PDB 6AZL 6AZL 1 107
DBREF 6AZL A 108 213 UNP P01834 IGKC_HUMAN 1 106
DBREF 6AZL B 1 107 PDB 6AZL 6AZL 1 107
DBREF 6AZL B 108 221 UNP S6B291 S6B291_HUMAN 125 238
DBREF 6AZL C 1 107 PDB 6AZL 6AZL 1 107
DBREF 6AZL C 108 213 UNP P01834 IGKC_HUMAN 1 106
DBREF 6AZL D 1 107 PDB 6AZL 6AZL 1 107
DBREF 6AZL D 108 221 UNP S6B291 S6B291_HUMAN 125 238
DBREF 6AZL E 2 12 PDB 6AZL 6AZL 2 12
DBREF 6AZL F 2 12 PDB 6AZL 6AZL 2 12
SEQADV 6AZL ALA A 213 UNP P01834 GLU 106 CONFLICT
SEQADV 6AZL ALA B 119 UNP S6B291 SER 136 CONFLICT
SEQADV 6AZL ALA C 213 UNP P01834 GLU 106 CONFLICT
SEQADV 6AZL ALA D 119 UNP S6B291 SER 136 CONFLICT
SEQRES 1 A 213 ASP ILE LEU LEU THR GLN SER PRO VAL ILE LEU SER VAL
SEQRES 2 A 213 SER PRO GLY GLU ARG VAL SER PHE SER CYS ARG ALA SER
SEQRES 3 A 213 GLN SER ILE GLY THR ASN ILE HIS TRP TYR GLN GLN ARG
SEQRES 4 A 213 THR ASN GLY SER PRO ARG LEU LEU ILE LYS TYR ALA SER
SEQRES 5 A 213 GLU SER ILE SER GLY ILE PRO SER ARG PHE SER GLY SER
SEQRES 6 A 213 GLY SER GLY THR ASP PHE THR LEU SER ILE ASN SER VAL
SEQRES 7 A 213 GLU SER GLU ASP ILE ALA ASP TYR TYR CYS GLN GLN ASN
SEQRES 8 A 213 ASN ASN TRP PRO THR THR PHE GLY ALA GLY THR LYS LEU
SEQRES 9 A 213 GLU LEU LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE
SEQRES 10 A 213 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA
SEQRES 11 A 213 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU
SEQRES 12 A 213 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER
SEQRES 13 A 213 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS
SEQRES 14 A 213 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER
SEQRES 15 A 213 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU
SEQRES 16 A 213 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER
SEQRES 17 A 213 PHE ASN ARG GLY ALA
SEQRES 1 B 221 GLN VAL GLN LEU LYS GLN SER GLY PRO GLY LEU VAL GLN
SEQRES 2 B 221 PRO SER GLN SER LEU SER ILE THR CYS THR VAL SER GLY
SEQRES 3 B 221 PHE SER LEU THR ASN TYR GLY VAL HIS TRP VAL ARG GLN
SEQRES 4 B 221 SER PRO GLY LYS GLY LEU GLU TRP LEU GLY VAL ILE TRP
SEQRES 5 B 221 SER GLY GLY ASN THR ASP TYR ASN THR PRO PHE THR SER
SEQRES 6 B 221 ARG LEU SER ILE ASN LYS ASP ASN SER LYS SER GLN VAL
SEQRES 7 B 221 PHE PHE LYS MET ASN SER LEU GLN SER ASN ASP THR ALA
SEQRES 8 B 221 ILE TYR TYR CYS ALA ARG ALA LEU THR TYR TYR ASP TYR
SEQRES 9 B 221 GLU PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR VAL
SEQRES 10 B 221 SER ALA ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU
SEQRES 11 B 221 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA
SEQRES 12 B 221 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL
SEQRES 13 B 221 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL
SEQRES 14 B 221 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR
SEQRES 15 B 221 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU
SEQRES 16 B 221 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO
SEQRES 17 B 221 SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER
SEQRES 1 C 213 ASP ILE LEU LEU THR GLN SER PRO VAL ILE LEU SER VAL
SEQRES 2 C 213 SER PRO GLY GLU ARG VAL SER PHE SER CYS ARG ALA SER
SEQRES 3 C 213 GLN SER ILE GLY THR ASN ILE HIS TRP TYR GLN GLN ARG
SEQRES 4 C 213 THR ASN GLY SER PRO ARG LEU LEU ILE LYS TYR ALA SER
SEQRES 5 C 213 GLU SER ILE SER GLY ILE PRO SER ARG PHE SER GLY SER
SEQRES 6 C 213 GLY SER GLY THR ASP PHE THR LEU SER ILE ASN SER VAL
SEQRES 7 C 213 GLU SER GLU ASP ILE ALA ASP TYR TYR CYS GLN GLN ASN
SEQRES 8 C 213 ASN ASN TRP PRO THR THR PHE GLY ALA GLY THR LYS LEU
SEQRES 9 C 213 GLU LEU LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE
SEQRES 10 C 213 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA
SEQRES 11 C 213 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU
SEQRES 12 C 213 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER
SEQRES 13 C 213 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS
SEQRES 14 C 213 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER
SEQRES 15 C 213 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU
SEQRES 16 C 213 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER
SEQRES 17 C 213 PHE ASN ARG GLY ALA
SEQRES 1 D 221 GLN VAL GLN LEU LYS GLN SER GLY PRO GLY LEU VAL GLN
SEQRES 2 D 221 PRO SER GLN SER LEU SER ILE THR CYS THR VAL SER GLY
SEQRES 3 D 221 PHE SER LEU THR ASN TYR GLY VAL HIS TRP VAL ARG GLN
SEQRES 4 D 221 SER PRO GLY LYS GLY LEU GLU TRP LEU GLY VAL ILE TRP
SEQRES 5 D 221 SER GLY GLY ASN THR ASP TYR ASN THR PRO PHE THR SER
SEQRES 6 D 221 ARG LEU SER ILE ASN LYS ASP ASN SER LYS SER GLN VAL
SEQRES 7 D 221 PHE PHE LYS MET ASN SER LEU GLN SER ASN ASP THR ALA
SEQRES 8 D 221 ILE TYR TYR CYS ALA ARG ALA LEU THR TYR TYR ASP TYR
SEQRES 9 D 221 GLU PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR VAL
SEQRES 10 D 221 SER ALA ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU
SEQRES 11 D 221 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA
SEQRES 12 D 221 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL
SEQRES 13 D 221 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL
SEQRES 14 D 221 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR
SEQRES 15 D 221 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU
SEQRES 16 D 221 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO
SEQRES 17 D 221 SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER
SEQRES 1 E 11 GLN PHE ASP LEU SER THR C67 ARG LEU LYS 011
SEQRES 1 F 11 GLN PHE ASP LEU SER THR C67 ARG LEU LYS 011
HET C67 E 8 25
HET C67 F 8 25
HET SO4 A 301 5
HET SO4 C 301 5
HET SO4 C 302 5
HETNAM C67 N~5~-[N-(2-CARBOXYETHYL)CARBAMIMIDOYL]-L-ORNITHINE
HETNAM SO4 SULFATE ION
FORMUL 5 C67 2(C9 H18 N4 O4)
FORMUL 7 SO4 3(O4 S 2-)
FORMUL 10 HOH *431(H2 O)
HELIX 1 AA1 GLU A 79 ILE A 83 5 5
HELIX 2 AA2 SER A 121 SER A 127 1 7
HELIX 3 AA3 LYS A 183 LYS A 188 1 6
HELIX 4 AA4 THR B 61 THR B 64 5 4
HELIX 5 AA5 GLN B 86 THR B 90 5 5
HELIX 6 AA6 SER B 133 LYS B 135 5 3
HELIX 7 AA7 SER B 162 ALA B 164 5 3
HELIX 8 AA8 SER B 193 LEU B 195 5 3
HELIX 9 AA9 LYS B 207 ASN B 210 5 4
HELIX 10 AB1 GLU C 79 ILE C 83 5 5
HELIX 11 AB2 SER C 121 LYS C 126 1 6
HELIX 12 AB3 LYS C 183 HIS C 189 1 7
HELIX 13 AB4 THR D 61 THR D 64 5 4
HELIX 14 AB5 GLN D 86 THR D 90 5 5
HELIX 15 AB6 SER D 162 ALA D 164 5 3
HELIX 16 AB7 SER D 193 LEU D 195 5 3
HELIX 17 AB8 LYS D 207 ASN D 210 5 4
SHEET 1 AA1 4 LEU A 4 SER A 7 0
SHEET 2 AA1 4 VAL A 19 ALA A 25 -1 O ARG A 24 N THR A 5
SHEET 3 AA1 4 ASP A 70 ILE A 75 -1 O LEU A 73 N PHE A 21
SHEET 4 AA1 4 PHE A 62 SER A 67 -1 N SER A 63 O SER A 74
SHEET 1 AA2 6 ILE A 10 VAL A 13 0
SHEET 2 AA2 6 THR A 102 LEU A 106 1 O GLU A 105 N LEU A 11
SHEET 3 AA2 6 ALA A 84 GLN A 90 -1 N TYR A 86 O THR A 102
SHEET 4 AA2 6 ILE A 33 GLN A 38 -1 N HIS A 34 O GLN A 89
SHEET 5 AA2 6 ARG A 45 LYS A 49 -1 O LEU A 47 N TRP A 35
SHEET 6 AA2 6 GLU A 53 SER A 54 -1 O GLU A 53 N LYS A 49
SHEET 1 AA3 4 ILE A 10 VAL A 13 0
SHEET 2 AA3 4 THR A 102 LEU A 106 1 O GLU A 105 N LEU A 11
SHEET 3 AA3 4 ALA A 84 GLN A 90 -1 N TYR A 86 O THR A 102
SHEET 4 AA3 4 THR A 97 PHE A 98 -1 O THR A 97 N GLN A 90
SHEET 1 AA4 4 SER A 114 PHE A 118 0
SHEET 2 AA4 4 THR A 129 PHE A 139 -1 O LEU A 135 N PHE A 116
SHEET 3 AA4 4 TYR A 173 SER A 182 -1 O LEU A 179 N VAL A 132
SHEET 4 AA4 4 SER A 159 VAL A 163 -1 N SER A 162 O SER A 176
SHEET 1 AA5 4 ALA A 153 LEU A 154 0
SHEET 2 AA5 4 LYS A 145 VAL A 150 -1 N VAL A 150 O ALA A 153
SHEET 3 AA5 4 VAL A 191 THR A 197 -1 O ALA A 193 N LYS A 149
SHEET 4 AA5 4 VAL A 205 ASN A 210 -1 O VAL A 205 N VAL A 196
SHEET 1 AA6 4 GLN B 3 GLN B 6 0
SHEET 2 AA6 4 LEU B 18 SER B 25 -1 O THR B 23 N LYS B 5
SHEET 3 AA6 4 GLN B 77 MET B 82 -1 O VAL B 78 N CYS B 22
SHEET 4 AA6 4 LEU B 67 ASP B 72 -1 N ASN B 70 O PHE B 79
SHEET 1 AA7 6 GLY B 10 VAL B 12 0
SHEET 2 AA7 6 THR B 113 VAL B 117 1 O THR B 116 N VAL B 12
SHEET 3 AA7 6 ALA B 91 ALA B 98 -1 N ALA B 91 O VAL B 115
SHEET 4 AA7 6 VAL B 34 SER B 40 -1 N VAL B 37 O TYR B 94
SHEET 5 AA7 6 GLY B 44 ILE B 51 -1 O LEU B 48 N TRP B 36
SHEET 6 AA7 6 THR B 57 TYR B 59 -1 O ASP B 58 N VAL B 50
SHEET 1 AA8 4 GLY B 10 VAL B 12 0
SHEET 2 AA8 4 THR B 113 VAL B 117 1 O THR B 116 N VAL B 12
SHEET 3 AA8 4 ALA B 91 ALA B 98 -1 N ALA B 91 O VAL B 115
SHEET 4 AA8 4 PHE B 106 TRP B 109 -1 O TYR B 108 N ARG B 97
SHEET 1 AA9 4 SER B 126 LEU B 130 0
SHEET 2 AA9 4 THR B 141 TYR B 151 -1 O GLY B 145 N LEU B 130
SHEET 3 AA9 4 TYR B 182 PRO B 191 -1 O LEU B 184 N VAL B 148
SHEET 4 AA9 4 VAL B 169 THR B 171 -1 N HIS B 170 O VAL B 187
SHEET 1 AB1 4 THR B 137 SER B 138 0
SHEET 2 AB1 4 THR B 141 TYR B 151 -1 O THR B 141 N SER B 138
SHEET 3 AB1 4 TYR B 182 PRO B 191 -1 O LEU B 184 N VAL B 148
SHEET 4 AB1 4 VAL B 175 LEU B 176 -1 N VAL B 175 O SER B 183
SHEET 1 AB2 3 THR B 157 TRP B 160 0
SHEET 2 AB2 3 ILE B 201 HIS B 206 -1 O ASN B 203 N SER B 159
SHEET 3 AB2 3 THR B 211 ARG B 216 -1 O VAL B 213 N VAL B 204
SHEET 1 AB3 4 LEU C 4 SER C 7 0
SHEET 2 AB3 4 VAL C 19 ALA C 25 -1 O ARG C 24 N THR C 5
SHEET 3 AB3 4 ASP C 70 ILE C 75 -1 O ILE C 75 N VAL C 19
SHEET 4 AB3 4 PHE C 62 SER C 67 -1 N SER C 63 O SER C 74
SHEET 1 AB4 6 ILE C 10 VAL C 13 0
SHEET 2 AB4 6 THR C 102 LEU C 106 1 O LYS C 103 N LEU C 11
SHEET 3 AB4 6 ALA C 84 GLN C 90 -1 N TYR C 86 O THR C 102
SHEET 4 AB4 6 ILE C 33 GLN C 38 -1 N HIS C 34 O GLN C 89
SHEET 5 AB4 6 ARG C 45 LYS C 49 -1 O ILE C 48 N TRP C 35
SHEET 6 AB4 6 GLU C 53 SER C 54 -1 O GLU C 53 N LYS C 49
SHEET 1 AB5 4 ILE C 10 VAL C 13 0
SHEET 2 AB5 4 THR C 102 LEU C 106 1 O LYS C 103 N LEU C 11
SHEET 3 AB5 4 ALA C 84 GLN C 90 -1 N TYR C 86 O THR C 102
SHEET 4 AB5 4 THR C 97 PHE C 98 -1 O THR C 97 N GLN C 90
SHEET 1 AB6 4 SER C 114 PHE C 118 0
SHEET 2 AB6 4 THR C 129 PHE C 139 -1 O ASN C 137 N SER C 114
SHEET 3 AB6 4 TYR C 173 SER C 182 -1 O LEU C 179 N VAL C 132
SHEET 4 AB6 4 SER C 159 VAL C 163 -1 N GLN C 160 O THR C 178
SHEET 1 AB7 4 ALA C 153 LEU C 154 0
SHEET 2 AB7 4 LYS C 145 VAL C 150 -1 N VAL C 150 O ALA C 153
SHEET 3 AB7 4 VAL C 191 THR C 197 -1 O GLU C 195 N GLN C 147
SHEET 4 AB7 4 VAL C 205 ASN C 210 -1 O VAL C 205 N VAL C 196
SHEET 1 AB8 4 GLN D 3 GLN D 6 0
SHEET 2 AB8 4 LEU D 18 SER D 25 -1 O THR D 23 N LYS D 5
SHEET 3 AB8 4 GLN D 77 MET D 82 -1 O VAL D 78 N CYS D 22
SHEET 4 AB8 4 LEU D 67 ASP D 72 -1 N ASN D 70 O PHE D 79
SHEET 1 AB9 6 GLY D 10 VAL D 12 0
SHEET 2 AB9 6 THR D 113 VAL D 117 1 O THR D 116 N VAL D 12
SHEET 3 AB9 6 ALA D 91 ALA D 98 -1 N ALA D 91 O VAL D 115
SHEET 4 AB9 6 VAL D 34 SER D 40 -1 N VAL D 37 O TYR D 94
SHEET 5 AB9 6 GLY D 44 ILE D 51 -1 O LEU D 48 N TRP D 36
SHEET 6 AB9 6 THR D 57 TYR D 59 -1 O ASP D 58 N VAL D 50
SHEET 1 AC1 4 GLY D 10 VAL D 12 0
SHEET 2 AC1 4 THR D 113 VAL D 117 1 O THR D 116 N VAL D 12
SHEET 3 AC1 4 ALA D 91 ALA D 98 -1 N ALA D 91 O VAL D 115
SHEET 4 AC1 4 PHE D 106 TRP D 109 -1 O TYR D 108 N ARG D 97
SHEET 1 AC2 4 SER D 126 LEU D 130 0
SHEET 2 AC2 4 THR D 141 TYR D 151 -1 O GLY D 145 N LEU D 130
SHEET 3 AC2 4 TYR D 182 PRO D 191 -1 O LEU D 184 N VAL D 148
SHEET 4 AC2 4 VAL D 169 THR D 171 -1 N HIS D 170 O VAL D 187
SHEET 1 AC3 4 SER D 126 LEU D 130 0
SHEET 2 AC3 4 THR D 141 TYR D 151 -1 O GLY D 145 N LEU D 130
SHEET 3 AC3 4 TYR D 182 PRO D 191 -1 O LEU D 184 N VAL D 148
SHEET 4 AC3 4 VAL D 175 LEU D 176 -1 N VAL D 175 O SER D 183
SHEET 1 AC4 3 THR D 157 TRP D 160 0
SHEET 2 AC4 3 ILE D 201 HIS D 206 -1 O ASN D 203 N SER D 159
SHEET 3 AC4 3 THR D 211 ARG D 216 -1 O VAL D 213 N VAL D 204
SHEET 1 AC5 2 PHE E 3 ASP E 4 0
SHEET 2 AC5 2 ARG E 9 LEU E 10 -1 O ARG E 9 N ASP E 4
SHEET 1 AC6 2 PHE F 3 ASP F 4 0
SHEET 2 AC6 2 ARG F 9 LEU F 10 -1 O ARG F 9 N ASP F 4
SSBOND 1 CYS A 23 CYS A 88 1555 1555 2.07
SSBOND 2 CYS A 134 CYS A 194 1555 1555 2.03
SSBOND 3 CYS B 22 CYS B 95 1555 1555 2.05
SSBOND 4 CYS B 146 CYS B 202 1555 1555 2.01
SSBOND 5 CYS C 23 CYS C 88 1555 1555 2.07
SSBOND 6 CYS C 134 CYS C 194 1555 1555 2.02
SSBOND 7 CYS D 22 CYS D 95 1555 1555 2.05
SSBOND 8 CYS D 146 CYS D 202 1555 1555 2.04
LINK C THR E 7 N C67 E 8 1555 1555 1.33
LINK C C67 E 8 N ARG E 9 1555 1555 1.33
LINK C THR F 7 N C67 F 8 1555 1555 1.33
LINK C C67 F 8 N ARG F 9 1555 1555 1.33
CISPEP 1 SER A 7 PRO A 8 0 -12.96
CISPEP 2 TRP A 94 PRO A 95 0 -0.79
CISPEP 3 TYR A 140 PRO A 141 0 2.45
CISPEP 4 PHE B 152 PRO B 153 0 -4.81
CISPEP 5 GLU B 154 PRO B 155 0 -1.84
CISPEP 6 SER C 7 PRO C 8 0 -8.02
CISPEP 7 TRP C 94 PRO C 95 0 -2.85
CISPEP 8 TYR C 140 PRO C 141 0 3.09
CISPEP 9 PHE D 152 PRO D 153 0 -7.66
CISPEP 10 GLU D 154 PRO D 155 0 -2.60
SITE 1 AC1 3 PRO A 59 GLU A 81 HOH A 424
SITE 1 AC2 1 PRO C 59
SITE 1 AC3 5 SER C 156 GLY C 157 HOH C 407 HOH C 452
SITE 2 AC3 5 HOH C 477
CRYST1 64.570 83.050 212.110 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 0.015487 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012041 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004715 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
