HEADER CELL ADHESION/BLOOD CLOTTING 15-JUN-10 3NIG
TITLE THE CLOSED HEADPIECE OF INTEGRIN IIB 3 AND ITS COMPLEX WITH AN IIB 3 -
TITLE 2 SPECIFIC ANTAGONIST THAT DOES NOT INDUCE OPENING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTEGRIN ALPHA-IIB;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: INTEGRIN ALPHA-IIB, RESIDUES 32-488;
COMPND 5 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIB, GPALPHA IIB, GPIIB,
COMPND 6 INTEGRIN ALPHA-IIB HEAVY CHAIN;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: INTEGRIN BETA-3;
COMPND 10 CHAIN: B, D;
COMPND 11 FRAGMENT: INTEGRIN BETA-3, RESIDUES 27-497;
COMPND 12 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA, GPIIIA, CD61;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: MMONOCLONAL ANTIBODY 10E5 HEAVY CHAIN;
COMPND 16 CHAIN: E, H;
COMPND 17 ENGINEERED: YES;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: MMONOCLONAL ANTIBODY 10E5 LIGHT CHAIN;
COMPND 20 CHAIN: F, L;
COMPND 21 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ITGA2B, GP2B, ITGAB;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: CHO LEC 3.2.8.1;
SOURCE 10 EXPRESSION_SYSTEM_CELL_LINE: LEC 3.2.8.1;
SOURCE 11 EXPRESSION_SYSTEM_CELL: CHO;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PCDNA 3.1, PEF1;
SOURCE 14 MOL_ID: 2;
SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 16 ORGANISM_COMMON: HUMAN;
SOURCE 17 ORGANISM_TAXID: 9606;
SOURCE 18 GENE: ITGB3, GP3A;
SOURCE 19 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 20 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 22 EXPRESSION_SYSTEM_CELL_LINE: LEC 3.2.8.1;
SOURCE 23 EXPRESSION_SYSTEM_CELL: CHO;
SOURCE 24 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 25 EXPRESSION_SYSTEM_PLASMID: PCDNA 3.1, PEF1;
SOURCE 26 MOL_ID: 3;
SOURCE 27 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 28 ORGANISM_COMMON: MOUSE;
SOURCE 29 ORGANISM_TAXID: 10090;
SOURCE 30 STRAIN: BALB/C;
SOURCE 31 CELL_LINE: 10E5 HYBRIDOMA;
SOURCE 32 MOL_ID: 4;
SOURCE 33 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 34 ORGANISM_COMMON: MOUSE;
SOURCE 35 ORGANISM_TAXID: 10090;
SOURCE 36 STRAIN: BALB/C;
SOURCE 37 CELL_LINE: 10E5 HYBRIDOMA
KEYWDS INTEGRIN, HEADPIECE, ALPHAIIB, BETA3, CELL ADHESION-IMMUNE SYSTEM
KEYWDS 2 COMPLEX, CELL ADHESION-BLOOD CLOTTING COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.H.ZHU,J.Q.ZHU,T.A.SPRINGER
REVDAT 1 22-DEC-10 3NIG 0
JRNL AUTH J.ZHU,J.ZHU,A.NEGRI,D.PROVASI,M.FILIZOLA,B.S.COLLER,
JRNL AUTH 2 T.A.SPRINGER
JRNL TITL CLOSED HEADPIECE OF INTEGRIN {ALPHA}IIB{BETA}3 AND ITS
JRNL TITL 2 COMPLEX WITH AN {ALPHA}IIB{BETA}3-SPECIFIC ANTAGONIST THAT
JRNL TITL 3 DOES NOT INDUCE OPENING.
JRNL REF BLOOD V. 116 5050 2010
JRNL REFN ISSN 0006-4971
JRNL PMID 20679525
JRNL DOI 10.1182/BLOOD-2010-04-281154
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6_289)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.49
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 187662
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) : 0.172
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.540
REMARK 3 FREE R VALUE TEST SET COUNT : 1009
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 48.5026 - 4.3033 1.00 27438 150 0.1569 0.1850
REMARK 3 2 4.3033 - 3.4159 1.00 26772 155 0.1503 0.1741
REMARK 3 3 3.4159 - 2.9842 1.00 26563 153 0.1603 0.2383
REMARK 3 4 2.9842 - 2.7114 1.00 26594 136 0.1629 0.2130
REMARK 3 5 2.7114 - 2.5170 1.00 26453 140 0.1703 0.2404
REMARK 3 6 2.5170 - 2.3686 1.00 26447 129 0.1901 0.2532
REMARK 3 7 2.3686 - 2.2500 1.00 26386 146 0.2138 0.2560
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.38
REMARK 3 B_SOL : 44.27
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
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) : -2.08430
REMARK 3 B22 (A**2) : 3.05830
REMARK 3 B33 (A**2) : -0.97400
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 : 0.009 21518
REMARK 3 ANGLE : 1.153 29249
REMARK 3 CHIRALITY : 0.071 3252
REMARK 3 PLANARITY : 0.005 3795
REMARK 3 DIHEDRAL : 16.385 7692
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 18
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESID 1:450
REMARK 3 ORIGIN FOR THE GROUP (A): 51.3613 90.9646 54.3938
REMARK 3 T TENSOR
REMARK 3 T11: 0.1608 T22: -0.0197
REMARK 3 T33: 0.1245 T12: 0.0063
REMARK 3 T13: 0.0538 T23: 0.0499
REMARK 3 L TENSOR
REMARK 3 L11: 0.5303 L22: 0.4988
REMARK 3 L33: 0.6514 L12: -0.0187
REMARK 3 L13: -0.1490 L23: 0.3933
REMARK 3 S TENSOR
REMARK 3 S11: -0.0126 S12: -0.0168 S13: -0.0299
REMARK 3 S21: 0.0636 S22: -0.0078 S23: 0.0230
REMARK 3 S31: 0.1431 S32: -0.0262 S33: 0.0200
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN C AND RESID 1:450
REMARK 3 ORIGIN FOR THE GROUP (A): 84.9773 86.9114 117.5757
REMARK 3 T TENSOR
REMARK 3 T11: 0.2033 T22: 0.2029
REMARK 3 T33: 0.1340 T12: 0.0570
REMARK 3 T13: 0.0716 T23: 0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 1.3473 L22: 0.4964
REMARK 3 L33: 1.2867 L12: 0.2875
REMARK 3 L13: -0.5320 L23: -0.3513
REMARK 3 S TENSOR
REMARK 3 S11: -0.0901 S12: -0.0744 S13: -0.0675
REMARK 3 S21: -0.1104 S22: -0.0256 S23: -0.0593
REMARK 3 S31: 0.2669 S32: 0.3099 S33: 0.1219
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN B AND RESID 1:57
REMARK 3 ORIGIN FOR THE GROUP (A): 123.9426 88.7267 35.2145
REMARK 3 T TENSOR
REMARK 3 T11: 0.4733 T22: 1.6711
REMARK 3 T33: 0.9053 T12: 0.4182
REMARK 3 T13: 0.0453 T23: -0.3924
REMARK 3 L TENSOR
REMARK 3 L11: 1.9538 L22: 1.3354
REMARK 3 L33: 1.0358 L12: -1.3818
REMARK 3 L13: 1.3288 L23: -0.7231
REMARK 3 S TENSOR
REMARK 3 S11: -0.3116 S12: 0.6837 S13: 0.5466
REMARK 3 S21: 0.2251 S22: 0.0657 S23: -0.5124
REMARK 3 S31: 0.1870 S32: 1.3116 S33: -0.0131
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN B AND (RESID 58:107 OR RESID 354:432)
REMARK 3 ORIGIN FOR THE GROUP (A): 101.6846 108.0573 52.6381
REMARK 3 T TENSOR
REMARK 3 T11: 0.2276 T22: 0.6070
REMARK 3 T33: 0.6054 T12: 0.0869
REMARK 3 T13: 0.0114 T23: -0.2477
REMARK 3 L TENSOR
REMARK 3 L11: 0.2747 L22: 0.3170
REMARK 3 L33: 1.3540 L12: -0.0672
REMARK 3 L13: -0.3881 L23: 0.3908
REMARK 3 S TENSOR
REMARK 3 S11: 0.0085 S12: -0.0984 S13: 0.3100
REMARK 3 S21: -0.0261 S22: 0.3525 S23: -0.1703
REMARK 3 S31: 0.1141 S32: 0.9141 S33: -0.3826
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN B AND RESID 109:352
REMARK 3 ORIGIN FOR THE GROUP (A): 68.2942 119.0274 63.3295
REMARK 3 T TENSOR
REMARK 3 T11: 0.2181 T22: 0.0506
REMARK 3 T33: 0.2047 T12: 0.0102
REMARK 3 T13: 0.0462 T23: 0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 0.6443 L22: 1.1537
REMARK 3 L33: 0.5236 L12: 0.2311
REMARK 3 L13: -0.0516 L23: 0.4564
REMARK 3 S TENSOR
REMARK 3 S11: 0.0316 S12: -0.0234 S13: 0.1191
REMARK 3 S21: -0.0081 S22: 0.0780 S23: -0.0826
REMARK 3 S31: -0.1161 S32: 0.0270 S33: -0.0509
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN B AND RESID 433:461
REMARK 3 ORIGIN FOR THE GROUP (A): 117.6261 90.2055 19.8589
REMARK 3 T TENSOR
REMARK 3 T11: 0.3959 T22: 1.4701
REMARK 3 T33: 0.7437 T12: 0.2528
REMARK 3 T13: 0.1294 T23: -0.1611
REMARK 3 L TENSOR
REMARK 3 L11: 0.1686 L22: 0.3950
REMARK 3 L33: 0.1515 L12: 0.2471
REMARK 3 L13: -0.1128 L23: -0.0994
REMARK 3 S TENSOR
REMARK 3 S11: 0.1645 S12: -1.0057 S13: 0.2120
REMARK 3 S21: -0.1366 S22: -0.4804 S23: -0.0674
REMARK 3 S31: 0.1065 S32: 0.4237 S33: 0.2345
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN D AND RESID 1:57
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5861 70.9675 140.7228
REMARK 3 T TENSOR
REMARK 3 T11: 0.6119 T22: 1.0559
REMARK 3 T33: 0.4547 T12: -0.6411
REMARK 3 T13: 0.1777 T23: -0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 1.2787 L22: 1.2559
REMARK 3 L33: 1.2203 L12: 1.1320
REMARK 3 L13: 0.2698 L23: -0.1139
REMARK 3 S TENSOR
REMARK 3 S11: -0.3800 S12: -0.0222 S13: -0.1525
REMARK 3 S21: -0.3072 S22: -0.1114 S23: 0.2415
REMARK 3 S31: 0.6495 S32: -1.1262 S33: 0.2315
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN D AND (RESID 58:107 OR RESID 354:432)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.8466 87.8586 115.8306
REMARK 3 T TENSOR
REMARK 3 T11: 0.3468 T22: 0.6914
REMARK 3 T33: 0.2498 T12: -0.2496
REMARK 3 T13: 0.0243 T23: 0.1116
REMARK 3 L TENSOR
REMARK 3 L11: 0.9256 L22: 0.3203
REMARK 3 L33: 1.9122 L12: 0.1841
REMARK 3 L13: -0.9632 L23: -0.3743
REMARK 3 S TENSOR
REMARK 3 S11: -0.2992 S12: 0.5466 S13: -0.0012
REMARK 3 S21: -0.1172 S22: 0.2293 S23: -0.0010
REMARK 3 S31: 0.4490 S32: -1.0005 S33: -0.0037
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN D AND RESID 109:352
REMARK 3 ORIGIN FOR THE GROUP (A): 61.0605 102.7883 99.3917
REMARK 3 T TENSOR
REMARK 3 T11: 0.1984 T22: 0.2125
REMARK 3 T33: 0.1335 T12: -0.0742
REMARK 3 T13: 0.0253 T23: 0.0768
REMARK 3 L TENSOR
REMARK 3 L11: 0.9902 L22: 0.2283
REMARK 3 L33: 1.4439 L12: -0.1538
REMARK 3 L13: 0.0264 L23: -0.3510
REMARK 3 S TENSOR
REMARK 3 S11: -0.0241 S12: 0.2252 S13: 0.1069
REMARK 3 S21: -0.0411 S22: 0.0950 S23: -0.0037
REMARK 3 S31: 0.0680 S32: -0.2386 S33: -0.0533
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN D AND RESID 433:461
REMARK 3 ORIGIN FOR THE GROUP (A): 19.7323 80.8706 153.3467
REMARK 3 T TENSOR
REMARK 3 T11: 0.4355 T22: 0.6250
REMARK 3 T33: 0.3865 T12: -0.2578
REMARK 3 T13: 0.1166 T23: -0.0774
REMARK 3 L TENSOR
REMARK 3 L11: 1.2160 L22: 0.0976
REMARK 3 L33: 3.1732 L12: 0.1980
REMARK 3 L13: -0.9027 L23: -0.1378
REMARK 3 S TENSOR
REMARK 3 S11: -0.3481 S12: -0.0293 S13: 0.5558
REMARK 3 S21: -0.0563 S22: -0.0792 S23: 0.1447
REMARK 3 S31: 0.3789 S32: -0.2698 S33: 0.2981
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN H AND RESID 1:119
REMARK 3 ORIGIN FOR THE GROUP (A): 18.3644 97.2739 82.6918
REMARK 3 T TENSOR
REMARK 3 T11: 0.3541 T22: 0.4370
REMARK 3 T33: 0.2923 T12: -0.1063
REMARK 3 T13: 0.1644 T23: -0.0875
REMARK 3 L TENSOR
REMARK 3 L11: 1.4127 L22: 1.3024
REMARK 3 L33: 0.7510 L12: -0.1364
REMARK 3 L13: -0.7886 L23: 0.3800
REMARK 3 S TENSOR
REMARK 3 S11: 0.1498 S12: -0.1767 S13: 0.0400
REMARK 3 S21: 0.4858 S22: -0.2690 S23: 0.1446
REMARK 3 S31: 0.2394 S32: -0.2643 S33: 0.1207
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN H AND RESID 120:221
REMARK 3 ORIGIN FOR THE GROUP (A): -13.7797 81.8670 92.8544
REMARK 3 T TENSOR
REMARK 3 T11: 0.3605 T22: 0.3576
REMARK 3 T33: 1.5889 T12: 0.0697
REMARK 3 T13: 0.2388 T23: 0.0766
REMARK 3 L TENSOR
REMARK 3 L11: 2.9402 L22: 0.6150
REMARK 3 L33: 2.8180 L12: -1.3359
REMARK 3 L13: 0.7469 L23: -0.2959
REMARK 3 S TENSOR
REMARK 3 S11: -0.2799 S12: 0.0339 S13: -1.6790
REMARK 3 S21: 0.2556 S22: 0.1555 S23: 0.5058
REMARK 3 S31: 0.8016 S32: 0.4030 S33: 0.1490
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN L AND RESID 1:108
REMARK 3 ORIGIN FOR THE GROUP (A): 7.0514 96.5009 64.3021
REMARK 3 T TENSOR
REMARK 3 T11: 0.1307 T22: 0.6580
REMARK 3 T33: 0.6109 T12: -0.0263
REMARK 3 T13: 0.0530 T23: -0.2727
REMARK 3 L TENSOR
REMARK 3 L11: 0.2638 L22: 1.8022
REMARK 3 L33: 1.3626 L12: 0.2718
REMARK 3 L13: -0.2794 L23: 0.7240
REMARK 3 S TENSOR
REMARK 3 S11: 0.0273 S12: 0.1909 S13: 0.0486
REMARK 3 S21: -0.0640 S22: -0.5460 S23: 0.8597
REMARK 3 S31: 0.0136 S32: -0.8488 S33: 0.5063
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN L AND RESID 109:214
REMARK 3 ORIGIN FOR THE GROUP (A): -22.1780 93.8591 86.1368
REMARK 3 T TENSOR
REMARK 3 T11: 0.1540 T22: 0.4951
REMARK 3 T33: 0.9255 T12: 0.0314
REMARK 3 T13: 0.2369 T23: -0.0864
REMARK 3 L TENSOR
REMARK 3 L11: 1.3704 L22: 0.2682
REMARK 3 L33: 0.7912 L12: -0.1037
REMARK 3 L13: -0.4124 L23: 0.3909
REMARK 3 S TENSOR
REMARK 3 S11: -0.4249 S12: 0.3680 S13: -1.5104
REMARK 3 S21: 0.0572 S22: -0.1206 S23: 0.4163
REMARK 3 S31: 0.0297 S32: -0.4374 S33: 0.5319
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN E AND RESID 1:119
REMARK 3 ORIGIN FOR THE GROUP (A): 115.6334 90.1745 86.1974
REMARK 3 T TENSOR
REMARK 3 T11: 0.8467 T22: 0.7989
REMARK 3 T33: 0.3600 T12: 0.0102
REMARK 3 T13: 0.2746 T23: 0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 1.1170 L22: 1.0556
REMARK 3 L33: 0.6431 L12: -0.3152
REMARK 3 L13: 0.3789 L23: -0.7136
REMARK 3 S TENSOR
REMARK 3 S11: 0.0537 S12: 0.2873 S13: -0.0110
REMARK 3 S21: -0.8477 S22: -0.1376 S23: -0.1463
REMARK 3 S31: 1.0628 S32: 0.2565 S33: 0.1594
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN E AND RESID 120:221
REMARK 3 ORIGIN FOR THE GROUP (A): 151.0473 82.2590 79.7093
REMARK 3 T TENSOR
REMARK 3 T11: 1.2746 T22: 1.4912
REMARK 3 T33: 0.7839 T12: 0.8762
REMARK 3 T13: 0.0844 T23: 0.0528
REMARK 3 L TENSOR
REMARK 3 L11: 0.3856 L22: 0.0001
REMARK 3 L33: 0.0384 L12: -0.0277
REMARK 3 L13: -0.0451 L23: 0.0210
REMARK 3 S TENSOR
REMARK 3 S11: 0.3915 S12: 0.3139 S13: -0.0281
REMARK 3 S21: -0.1959 S22: -0.1246 S23: -0.1544
REMARK 3 S31: 0.5536 S32: 0.2121 S33: -0.1337
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN F AND RESID 1:108
REMARK 3 ORIGIN FOR THE GROUP (A): 126.0399 100.3007 102.2099
REMARK 3 T TENSOR
REMARK 3 T11: 0.1945 T22: 0.8715
REMARK 3 T33: 0.5967 T12: -0.0599
REMARK 3 T13: 0.1679 T23: 0.0522
REMARK 3 L TENSOR
REMARK 3 L11: 1.5807 L22: 1.6921
REMARK 3 L33: 1.3636 L12: -1.5404
REMARK 3 L13: 0.7883 L23: -0.4055
REMARK 3 S TENSOR
REMARK 3 S11: -0.1456 S12: -0.2552 S13: 0.8793
REMARK 3 S21: -0.0266 S22: -0.1530 S23: -0.7551
REMARK 3 S31: 0.0970 S32: 0.6065 S33: 0.2330
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN F AND RESID 109:214
REMARK 3 ORIGIN FOR THE GROUP (A): 155.1109 98.2611 80.3064
REMARK 3 T TENSOR
REMARK 3 T11: 0.3789 T22: 1.5323
REMARK 3 T33: 0.7915 T12: 0.2512
REMARK 3 T13: 0.4200 T23: 0.3127
REMARK 3 L TENSOR
REMARK 3 L11: 0.0085 L22: 0.2637
REMARK 3 L33: 1.2072 L12: -0.0551
REMARK 3 L13: 0.0256 L23: 0.1395
REMARK 3 S TENSOR
REMARK 3 S11: -0.0630 S12: -0.2128 S13: 0.0787
REMARK 3 S21: -0.2116 S22: -0.0568 S23: -0.5257
REMARK 3 S31: -0.0092 S32: 1.5632 S33: 0.0552
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 3NIG COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-DEC-10.
REMARK 100 THE RCSB ID CODE IS RCSB059869.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97948
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 187671
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.630
REMARK 200 R MERGE (I) : 0.09400
REMARK 200 R SYM (I) : 0.09400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.1100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.98
REMARK 200 R MERGE FOR SHELL (I) : 0.99400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3NID
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 11% PEG 8000, 0.2 M AMMONIUM SULFATE,
REMARK 280 0.1 M TRIS-HCL, PH 8.9, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 130.33500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 72.58500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 130.33500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 72.58500
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 APPLY THE FOLLOWING TO CHAINS: A, B, H, L
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 APPLY THE FOLLOWING TO CHAINS: C, D, E, 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 LEU B 467
REMARK 465 GLY B 468
REMARK 465 SER B 469
REMARK 465 GLN B 470
REMARK 465 CYS B 471
REMARK 465 VAL C 454
REMARK 465 LYS C 455
REMARK 465 ALA C 456
REMARK 465 SER C 457
REMARK 465 GLY E 135
REMARK 465 ASP E 136
REMARK 465 THR E 137
REMARK 465 THR E 138
REMARK 465 GLY E 139
REMARK 465 GLY E 220
REMARK 465 PRO E 221
REMARK 465 GLY H 135
REMARK 465 ASP H 136
REMARK 465 THR H 137
REMARK 465 GLY H 220
REMARK 465 PRO H 221
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 L 765 O HOH L 1141 2.00
REMARK 500 ND2 ASN B 371 C2 NAG B 3371 2.06
REMARK 500 O HOH B 514 O HOH B 1038 2.12
REMARK 500 O3 SO4 A 461 O HOH A 1036 2.13
REMARK 500 O HOH A 1053 O HOH A 1142 2.14
REMARK 500 O HOH C 1051 O HOH C 1146 2.14
REMARK 500 O HOH A 1173 O HOH B 1174 2.16
REMARK 500 O HOH C 1190 O HOH D 766 2.18
REMARK 500 O HOH A 1054 O HOH A 1142 2.18
REMARK 500 O HOH A 820 O HOH A 1118 2.19
REMARK 500 O HOH C 583 O HOH C 1191 2.19
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 ARG B 202 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 202 NE - CZ - NH2 ANGL. DEV. = -3.3 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 SER A 46 32.88 -83.34
REMARK 500 GLN A 47 28.31 48.09
REMARK 500 SER A 101 -129.85 54.20
REMARK 500 LYS A 118 -119.41 59.01
REMARK 500 GLU A 123 138.09 93.49
REMARK 500 LEU A 212 -43.86 73.29
REMARK 500 SER A 222 -167.00 -78.17
REMARK 500 ASP A 319 39.55 78.76
REMARK 500 PRO A 337 100.08 -50.14
REMARK 500 PHE A 417 121.18 -39.36
REMARK 500 PRO B 2 92.50 -49.01
REMARK 500 ASN B 3 -173.97 -65.61
REMARK 500 ALA B 30 54.47 -104.37
REMARK 500 PRO B 32 177.41 -52.64
REMARK 500 PHE B 56 85.25 -156.12
REMARK 500 ASP B 66 28.67 -143.11
REMARK 500 ARG B 67 133.34 -36.04
REMARK 500 ASP B 76 100.90 -50.26
REMARK 500 VAL B 157 -77.30 -125.38
REMARK 500 MET B 180 -163.04 -101.18
REMARK 500 SER B 213 -159.88 -121.66
REMARK 500 ASP B 241 72.32 -117.41
REMARK 500 LYS B 253 173.81 -57.42
REMARK 500 LEU B 258 -10.88 88.81
REMARK 500 CYS B 374 -92.52 -109.58
REMARK 500 PRO B 381 151.27 -48.19
REMARK 500 GLN B 440 47.64 -140.23
REMARK 500 ASN B 450 69.08 66.38
REMARK 500 SER C 101 -130.87 59.55
REMARK 500 LYS C 118 -111.11 58.05
REMARK 500 GLU C 123 137.10 98.59
REMARK 500 PHE C 191 13.33 81.39
REMARK 500 LEU C 212 -51.85 73.14
REMARK 500 ASP C 319 34.17 79.38
REMARK 500 ALA C 424 9.57 81.52
REMARK 500 ASN D 3 -174.15 -172.67
REMARK 500 ASP D 47 33.90 -99.58
REMARK 500 PHE D 56 76.92 -153.30
REMARK 500 ASP D 66 42.14 -143.25
REMARK 500 PRO D 85 170.96 -59.88
REMARK 500 VAL D 157 -80.70 -126.61
REMARK 500 LYS D 181 33.51 -88.36
REMARK 500 SER D 213 -159.21 -121.76
REMARK 500 ASP D 241 74.58 -111.11
REMARK 500 LYS D 253 173.22 -53.04
REMARK 500 LEU D 258 -13.97 88.15
REMARK 500 SER D 337 15.12 56.35
REMARK 500 CYS D 374 -87.48 -103.58
REMARK 500 ASN D 376 -157.68 54.26
REMARK 500 ASP E 73 92.89 -168.40
REMARK 500
REMARK 500 THIS ENTRY HAS 86 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 SER B 78 GLN B 79 138.50
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 B2001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B1037 O
REMARK 620 2 GLU B 220 OE2 108.8
REMARK 620 3 HOH B1039 O 97.2 89.6
REMARK 620 4 HOH B 514 O 167.3 76.1 94.6
REMARK 620 5 SER B 121 OG 71.3 88.4 167.0 97.4
REMARK 620 6 HOH B 897 O 113.1 131.3 108.2 58.1 82.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D2001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH D 475 O
REMARK 620 2 HOH D 505 O 105.2
REMARK 620 3 GLU D 220 OE2 104.9 95.9
REMARK 620 4 HOH D 864 O 86.7 94.6 161.7
REMARK 620 5 HOH D1092 O 160.9 93.8 74.4 89.9
REMARK 620 6 SER D 121 OG 71.5 170.9 77.1 93.7 90.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D2003 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 217 OD1
REMARK 620 2 GLU D 220 OE1 162.7
REMARK 620 3 PRO D 219 O 98.8 81.1
REMARK 620 4 ASN D 215 OD1 93.8 85.1 166.1
REMARK 620 5 ASP D 158 OD2 97.5 99.5 81.7 102.5
REMARK 620 6 ASP D 217 O 75.4 87.3 87.4 90.1 166.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C2004 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 250 O
REMARK 620 2 ASP C 245 OD2 155.5
REMARK 620 3 ASP C 247 O 90.4 95.4
REMARK 620 4 GLU C 243 OE1 78.4 125.4 89.7
REMARK 620 5 GLU C 243 OE2 128.5 75.2 91.8 50.2
REMARK 620 6 GLU C 252 OE2 88.7 71.7 140.1 129.0 119.2
REMARK 620 7 GLU C 252 OE1 101.3 76.3 167.0 87.1 76.4 47.1
REMARK 620 8 THR C 250 OG1 77.0 82.2 71.9 148.9 150.8 69.1 116.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B2003 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 217 OD1
REMARK 620 2 PRO B 219 O 101.1
REMARK 620 3 ASP B 158 OD2 94.7 84.9
REMARK 620 4 GLU B 220 OE1 168.1 82.1 97.0
REMARK 620 5 ASN B 215 OD1 89.4 168.8 98.2 86.9
REMARK 620 6 ASP B 217 O 76.1 88.6 167.6 92.6 90.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C2007 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR C 432 O
REMARK 620 2 HOH C 566 O 129.8
REMARK 620 3 ASP C 428 OD1 154.7 73.9
REMARK 620 4 ASP C 426 OD1 79.3 148.0 75.7
REMARK 620 5 ASP C 434 OD2 83.7 72.1 115.8 131.9
REMARK 620 6 ASN C 430 OD1 85.9 83.0 89.4 86.8 136.5
REMARK 620 7 ASP C 434 OD1 95.1 100.1 87.5 88.3 48.7 174.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C2005 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG C 303 O
REMARK 620 2 ASN C 299 OD1 155.3
REMARK 620 3 ASP C 297 OD1 73.5 81.8
REMARK 620 4 HOH C 810 O 116.1 87.3 157.9
REMARK 620 5 ASP C 305 OD2 93.6 85.3 88.7 109.5
REMARK 620 6 ASP C 305 OD1 89.1 108.3 134.2 67.5 49.6
REMARK 620 7 ASP C 301 OD1 86.7 87.6 75.6 84.8 163.6 146.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2004 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 245 OD2
REMARK 620 2 THR A 250 O 156.8
REMARK 620 3 GLU A 243 OE1 128.2 74.7
REMARK 620 4 GLU A 243 OE2 75.7 127.4 52.7
REMARK 620 5 THR A 250 OG1 80.7 77.0 142.5 147.8
REMARK 620 6 ASP A 247 O 93.6 87.2 78.8 84.2 75.7
REMARK 620 7 GLU A 252 OE2 76.7 90.0 131.9 122.4 71.6 147.0
REMARK 620 8 GLU A 252 OE1 83.8 102.0 88.9 78.1 121.0 162.2 49.4
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2005 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 299 OD1
REMARK 620 2 ARG A 303 O 155.6
REMARK 620 3 ASP A 297 OD1 81.0 74.7
REMARK 620 4 HOH A 559 O 92.3 109.0 155.8
REMARK 620 5 ASP A 305 OD1 114.0 83.4 127.4 76.6
REMARK 620 6 ASP A 305 OD2 85.6 93.5 82.7 120.2 51.2
REMARK 620 7 ASP A 301 OD1 84.9 86.8 75.1 81.1 151.1 157.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2006 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 371 O
REMARK 620 2 ASP A 367 OD1 160.7
REMARK 620 3 HOH A 491 O 101.0 96.9
REMARK 620 4 ASP A 365 OD2 76.7 84.0 154.5
REMARK 620 5 ASP A 373 OD2 77.7 114.6 74.6 128.2
REMARK 620 6 ASP A 369 OD1 91.8 84.6 77.9 76.8 147.9
REMARK 620 7 ASP A 373 OD1 89.1 88.4 120.1 85.3 50.0 161.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2007 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 432 O
REMARK 620 2 ASP A 428 OD1 157.3
REMARK 620 3 ASP A 426 OD1 82.8 74.5
REMARK 620 4 HOH A 478 O 123.5 77.9 149.6
REMARK 620 5 ASN A 430 OD1 88.8 88.1 87.0 79.4
REMARK 620 6 ASP A 434 OD1 94.1 87.5 88.9 102.6 174.7
REMARK 620 7 ASP A 434 OD2 77.7 119.4 132.7 73.0 134.6 50.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C2006 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 495 O
REMARK 620 2 TYR C 371 O 103.9
REMARK 620 3 ASP C 367 OD1 102.1 148.3
REMARK 620 4 ASP C 373 OD2 76.8 86.5 117.1
REMARK 620 5 ASP C 365 OD2 149.8 75.3 73.1 132.5
REMARK 620 6 ASP C 369 OD1 75.1 85.3 84.2 147.7 74.8
REMARK 620 7 ASP C 373 OD1 123.4 92.4 88.2 50.2 86.6 161.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D2002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 127 OD1
REMARK 620 2 MET D 335 O 89.6
REMARK 620 3 HOH D 515 O 173.4 92.7
REMARK 620 4 SER D 123 O 88.7 162.2 90.9
REMARK 620 5 HOH D 503 O 91.9 80.2 94.5 82.2
REMARK 620 6 ASP D 126 OD1 79.4 121.5 94.2 75.6 156.2
REMARK 620 7 ASP D 126 OD2 90.5 75.8 84.1 121.9 155.8 47.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B2002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET B 335 O
REMARK 620 2 HOH B 537 O 98.8
REMARK 620 3 ASP B 127 OD1 91.2 170.0
REMARK 620 4 HOH B 750 O 73.5 90.2 93.4
REMARK 620 5 SER B 123 O 156.6 80.1 91.1 83.2
REMARK 620 6 ASP B 126 OD1 123.1 88.2 85.7 163.4 80.2
REMARK 620 7 ASP B 126 OD2 75.4 91.7 90.0 148.8 127.8 47.9
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 458
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 459
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 460
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 461
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3099
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3320
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3321
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 3322
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3371
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3372
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2005
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2006
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2007
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 458
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 459
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 460
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3099
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3320
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3321
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D 3322
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3371
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3372
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 472
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 215
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VDR RELATED DB: PDB
REMARK 900 RELATED ID: 3NID RELATED DB: PDB
REMARK 900 RELATED ID: 3NIF RELATED DB: PDB
DBREF 3NIG A 1 457 UNP P08514 ITA2B_HUMAN 32 488
DBREF 3NIG B 1 471 UNP P05106 ITB3_HUMAN 27 497
DBREF 3NIG C 1 457 UNP P08514 ITA2B_HUMAN 32 488
DBREF 3NIG D 1 471 UNP P05106 ITB3_HUMAN 27 497
DBREF 3NIG E 1 221 PDB 3NIG 3NIG 1 221
DBREF 3NIG H 1 221 PDB 3NIG 3NIG 1 221
DBREF 3NIG F 1 214 PDB 3NIG 3NIG 1 214
DBREF 3NIG L 1 214 PDB 3NIG 3NIG 1 214
SEQRES 1 A 457 LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY
SEQRES 2 A 457 PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS
SEQRES 3 A 457 LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA
SEQRES 4 A 457 PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY
SEQRES 5 A 457 VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS
SEQRES 6 A 457 PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN
SEQRES 7 A 457 VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN
SEQRES 8 A 457 GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE
SEQRES 9 A 457 VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU
SEQRES 10 A 457 LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS
SEQRES 11 A 457 PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR
SEQRES 12 A 457 SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL
SEQRES 13 A 457 GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA
SEQRES 14 A 457 GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL
SEQRES 15 A 457 LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU
SEQRES 16 A 457 ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG
SEQRES 17 A 457 PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU
SEQRES 18 A 457 SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR
SEQRES 19 A 457 TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP
SEQRES 20 A 457 LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP
SEQRES 21 A 457 SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR
SEQRES 22 A 457 TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA
SEQRES 23 A 457 SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN
SEQRES 24 A 457 GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU
SEQRES 25 A 457 TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL
SEQRES 26 A 457 GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS
SEQRES 27 A 457 ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN
SEQRES 28 A 457 LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY
SEQRES 29 A 457 ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA
SEQRES 30 A 457 ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU
SEQRES 31 A 457 VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO
SEQRES 32 A 457 SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA
SEQRES 33 A 457 PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP
SEQRES 34 A 457 ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA
SEQRES 35 A 457 ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL LYS
SEQRES 36 A 457 ALA SER
SEQRES 1 B 471 GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS
SEQRES 2 B 471 GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS
SEQRES 3 B 471 SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP
SEQRES 4 B 471 LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU
SEQRES 5 B 471 SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU
SEQRES 6 B 471 ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER
SEQRES 7 B 471 GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG
SEQRES 8 B 471 LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL
SEQRES 9 B 471 ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU
SEQRES 10 B 471 MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER
SEQRES 11 B 471 ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG
SEQRES 12 B 471 LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE
SEQRES 13 B 471 VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO
SEQRES 14 B 471 PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR
SEQRES 15 B 471 THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR
SEQRES 16 B 471 LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS
SEQRES 17 B 471 LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY
SEQRES 18 B 471 GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU
SEQRES 19 B 471 LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL
SEQRES 20 B 471 PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY
SEQRES 21 B 471 ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS
SEQRES 22 B 471 HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR
SEQRES 23 B 471 MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU
SEQRES 24 B 471 SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU
SEQRES 25 B 471 ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE
SEQRES 26 B 471 PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER
SEQRES 27 B 471 ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE
SEQRES 28 B 471 ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU
SEQRES 29 B 471 GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN
SEQRES 30 B 471 GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS
SEQRES 31 B 471 ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL
SEQRES 32 B 471 ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE
SEQRES 33 B 471 LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL
SEQRES 34 B 471 THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU
SEQRES 35 B 471 PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE
SEQRES 36 B 471 GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY
SEQRES 37 B 471 SER GLN CYS
SEQRES 1 C 457 LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY
SEQRES 2 C 457 PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS
SEQRES 3 C 457 LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA
SEQRES 4 C 457 PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY
SEQRES 5 C 457 VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS
SEQRES 6 C 457 PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN
SEQRES 7 C 457 VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN
SEQRES 8 C 457 GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE
SEQRES 9 C 457 VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU
SEQRES 10 C 457 LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS
SEQRES 11 C 457 PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR
SEQRES 12 C 457 SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL
SEQRES 13 C 457 GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA
SEQRES 14 C 457 GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL
SEQRES 15 C 457 LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU
SEQRES 16 C 457 ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG
SEQRES 17 C 457 PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU
SEQRES 18 C 457 SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR
SEQRES 19 C 457 TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP
SEQRES 20 C 457 LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP
SEQRES 21 C 457 SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR
SEQRES 22 C 457 TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA
SEQRES 23 C 457 SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN
SEQRES 24 C 457 GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU
SEQRES 25 C 457 TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL
SEQRES 26 C 457 GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS
SEQRES 27 C 457 ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN
SEQRES 28 C 457 LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY
SEQRES 29 C 457 ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA
SEQRES 30 C 457 ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU
SEQRES 31 C 457 VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO
SEQRES 32 C 457 SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA
SEQRES 33 C 457 PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP
SEQRES 34 C 457 ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA
SEQRES 35 C 457 ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL LYS
SEQRES 36 C 457 ALA SER
SEQRES 1 D 471 GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS
SEQRES 2 D 471 GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS
SEQRES 3 D 471 SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP
SEQRES 4 D 471 LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU
SEQRES 5 D 471 SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU
SEQRES 6 D 471 ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER
SEQRES 7 D 471 GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG
SEQRES 8 D 471 LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL
SEQRES 9 D 471 ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU
SEQRES 10 D 471 MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER
SEQRES 11 D 471 ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG
SEQRES 12 D 471 LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE
SEQRES 13 D 471 VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO
SEQRES 14 D 471 PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR
SEQRES 15 D 471 THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR
SEQRES 16 D 471 LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS
SEQRES 17 D 471 LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY
SEQRES 18 D 471 GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU
SEQRES 19 D 471 LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL
SEQRES 20 D 471 PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY
SEQRES 21 D 471 ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS
SEQRES 22 D 471 HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR
SEQRES 23 D 471 MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU
SEQRES 24 D 471 SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU
SEQRES 25 D 471 ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE
SEQRES 26 D 471 PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER
SEQRES 27 D 471 ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE
SEQRES 28 D 471 ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU
SEQRES 29 D 471 GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN
SEQRES 30 D 471 GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS
SEQRES 31 D 471 ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL
SEQRES 32 D 471 ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE
SEQRES 33 D 471 LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL
SEQRES 34 D 471 THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU
SEQRES 35 D 471 PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE
SEQRES 36 D 471 GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY
SEQRES 37 D 471 SER GLN CYS
SEQRES 1 E 221 GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS
SEQRES 2 E 221 PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY
SEQRES 3 E 221 PHE ASN ILE LYS ASP THR TYR VAL HIS TRP VAL LYS GLN
SEQRES 4 E 221 ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP
SEQRES 5 E 221 PRO ALA ASN GLY TYR THR LYS TYR ASP PRO LYS PHE GLN
SEQRES 6 E 221 GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR
SEQRES 7 E 221 ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR
SEQRES 8 E 221 ALA VAL TYR TYR CYS VAL ARG PRO LEU TYR ASP TYR TYR
SEQRES 9 E 221 ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL
SEQRES 10 E 221 SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU
SEQRES 11 E 221 ALA PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR
SEQRES 12 E 221 LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL
SEQRES 13 E 221 THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL
SEQRES 14 E 221 HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR
SEQRES 15 E 221 LEU SER SER SER VAL THR VAL THR SER SER THR TRP PRO
SEQRES 16 E 221 SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER
SEQRES 17 E 221 SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY PRO
SEQRES 1 F 214 ASP ILE LEU MET THR GLN SER PRO SER SER MET SER VAL
SEQRES 2 F 214 SER LEU GLY ASP THR VAL SER ILE THR CYS HIS ALA SER
SEQRES 3 F 214 GLN GLY ILE SER SER ASN ILE GLY TRP LEU GLN GLN LYS
SEQRES 4 F 214 PRO GLY LYS SER PHE MET GLY LEU ILE TYR TYR GLY THR
SEQRES 5 F 214 ASN LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 F 214 GLY SER GLY ALA ASP TYR SER LEU THR ILE SER SER LEU
SEQRES 7 F 214 ASP SER GLU ASP PHE ALA ASP TYR TYR CYS VAL GLN TYR
SEQRES 8 F 214 ALA GLN LEU PRO TYR THR PHE GLY GLY GLY THR LYS LEU
SEQRES 9 F 214 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE
SEQRES 10 F 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA
SEQRES 11 F 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP
SEQRES 12 F 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN
SEQRES 13 F 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS
SEQRES 14 F 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR
SEQRES 15 F 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU
SEQRES 16 F 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER
SEQRES 17 F 214 PHE ASN ARG ASN GLU CYS
SEQRES 1 H 221 GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS
SEQRES 2 H 221 PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY
SEQRES 3 H 221 PHE ASN ILE LYS ASP THR TYR VAL HIS TRP VAL LYS GLN
SEQRES 4 H 221 ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP
SEQRES 5 H 221 PRO ALA ASN GLY TYR THR LYS TYR ASP PRO LYS PHE GLN
SEQRES 6 H 221 GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR
SEQRES 7 H 221 ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR
SEQRES 8 H 221 ALA VAL TYR TYR CYS VAL ARG PRO LEU TYR ASP TYR TYR
SEQRES 9 H 221 ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL
SEQRES 10 H 221 SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU
SEQRES 11 H 221 ALA PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR
SEQRES 12 H 221 LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL
SEQRES 13 H 221 THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL
SEQRES 14 H 221 HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR
SEQRES 15 H 221 LEU SER SER SER VAL THR VAL THR SER SER THR TRP PRO
SEQRES 16 H 221 SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER
SEQRES 17 H 221 SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY PRO
SEQRES 1 L 214 ASP ILE LEU MET THR GLN SER PRO SER SER MET SER VAL
SEQRES 2 L 214 SER LEU GLY ASP THR VAL SER ILE THR CYS HIS ALA SER
SEQRES 3 L 214 GLN GLY ILE SER SER ASN ILE GLY TRP LEU GLN GLN LYS
SEQRES 4 L 214 PRO GLY LYS SER PHE MET GLY LEU ILE TYR TYR GLY THR
SEQRES 5 L 214 ASN LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 L 214 GLY SER GLY ALA ASP TYR SER LEU THR ILE SER SER LEU
SEQRES 7 L 214 ASP SER GLU ASP PHE ALA ASP TYR TYR CYS VAL GLN TYR
SEQRES 8 L 214 ALA GLN LEU PRO TYR THR PHE GLY GLY GLY THR LYS LEU
SEQRES 9 L 214 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE
SEQRES 10 L 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA
SEQRES 11 L 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP
SEQRES 12 L 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN
SEQRES 13 L 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS
SEQRES 14 L 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR
SEQRES 15 L 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU
SEQRES 16 L 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER
SEQRES 17 L 214 PHE ASN ARG ASN GLU CYS
MODRES 3NIG ASN D 99 ASN GLYCOSYLATION SITE
MODRES 3NIG ASN B 99 ASN GLYCOSYLATION SITE
MODRES 3NIG ASN D 371 ASN GLYCOSYLATION SITE
MODRES 3NIG ASN B 371 ASN GLYCOSYLATION SITE
MODRES 3NIG ASN B 320 ASN GLYCOSYLATION SITE
MODRES 3NIG ASN D 320 ASN GLYCOSYLATION SITE
HET CA A2004 1
HET CA A2005 1
HET CA A2006 1
HET CA A2007 1
HET GOL A 458 6
HET GOL A 459 6
HET SO4 A 460 5
HET SO4 A 461 5
HET MG B2001 1
HET CA B2002 1
HET CA B2003 1
HET NAG B3099 14
HET NAG B3320 14
HET NAG B3321 14
HET MAN B3322 11
HET NAG B3371 14
HET NAG B3372 14
HET CA C2004 1
HET CA C2005 1
HET CA C2006 1
HET CA C2007 1
HET GOL C 458 6
HET SO4 C 459 5
HET SO4 C 460 5
HET MG D2001 1
HET CA D2002 1
HET CA D2003 1
HET NAG D3099 14
HET NAG D3320 14
HET NAG D3321 14
HET MAN D3322 11
HET NAG D3371 14
HET NAG D3372 14
HET SO4 D 472 5
HET SO4 L 215 5
HETNAM CA CALCIUM ION
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETNAM MG MAGNESIUM ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MAN ALPHA-D-MANNOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 9 CA 12(CA 2+)
FORMUL 13 GOL 3(C3 H8 O3)
FORMUL 15 SO4 6(O4 S 2-)
FORMUL 17 MG 2(MG 2+)
FORMUL 20 NAG 10(C8 H15 N O6)
FORMUL 21 MAN 2(C6 H12 O6)
FORMUL 38 HOH *1227(H2 O)
HELIX 1 1 LEU A 151 ASN A 158 1 8
HELIX 2 2 GLY A 187 LEU A 192 1 6
HELIX 3 3 VAL A 200 TYR A 207 1 8
HELIX 4 4 ASN A 227 PHE A 231 5 5
HELIX 5 5 THR A 259 LEU A 264 1 6
HELIX 6 6 TYR A 440 ALA A 442 5 3
HELIX 7 7 ASN B 3 GLY B 9 1 7
HELIX 8 8 SER B 12 SER B 20 1 9
HELIX 9 9 LEU B 40 LYS B 46 1 7
HELIX 10 10 ALA B 50 GLU B 52 5 3
HELIX 11 11 SER B 121 SER B 123 5 3
HELIX 12 12 MET B 124 ILE B 131 1 8
HELIX 13 13 ASN B 133 ARG B 143 1 11
HELIX 14 14 PRO B 169 ASN B 175 1 7
HELIX 15 15 GLN B 199 LYS B 209 1 11
HELIX 16 16 GLY B 221 CYS B 232 1 12
HELIX 17 17 CYS B 232 GLY B 237 1 6
HELIX 18 18 LEU B 258 GLY B 264 5 7
HELIX 19 19 SER B 291 LYS B 302 1 12
HELIX 20 20 VAL B 314 ILE B 325 1 12
HELIX 21 21 ASN B 339 ARG B 352 1 14
HELIX 22 22 CYS B 435 ALA B 441 5 7
HELIX 23 23 LEU C 151 ASN C 158 1 8
HELIX 24 24 GLY C 187 LEU C 192 1 6
HELIX 25 25 VAL C 200 TYR C 207 1 8
HELIX 26 26 ASN C 227 PHE C 231 5 5
HELIX 27 27 THR C 259 LEU C 264 1 6
HELIX 28 28 TYR C 440 ALA C 442 5 3
HELIX 29 29 ASN D 3 ARG D 8 1 6
HELIX 30 30 SER D 12 SER D 20 1 9
HELIX 31 31 LYS D 41 ASP D 47 1 7
HELIX 32 32 ALA D 50 GLU D 52 5 3
HELIX 33 33 SER D 121 SER D 123 5 3
HELIX 34 34 MET D 124 ILE D 131 1 8
HELIX 35 35 ASN D 133 ARG D 143 1 11
HELIX 36 36 PRO D 169 ASN D 175 1 7
HELIX 37 37 GLN D 199 GLN D 210 1 12
HELIX 38 38 GLY D 221 CYS D 232 1 12
HELIX 39 39 CYS D 232 GLY D 237 1 6
HELIX 40 40 LEU D 258 GLY D 264 5 7
HELIX 41 41 SER D 291 LYS D 302 1 12
HELIX 42 42 VAL D 314 ILE D 325 1 12
HELIX 43 43 ASN D 339 ARG D 352 1 14
HELIX 44 44 CYS D 435 ALA D 441 5 7
HELIX 45 45 ASN E 28 THR E 32 5 5
HELIX 46 46 PRO E 62 GLN E 65 5 4
HELIX 47 47 THR E 87 THR E 91 5 5
HELIX 48 48 ASP F 79 PHE F 83 5 5
HELIX 49 49 SER F 121 THR F 126 1 6
HELIX 50 50 THR F 182 GLU F 187 1 6
HELIX 51 51 ASN H 28 THR H 32 5 5
HELIX 52 52 PRO H 62 GLN H 65 5 4
HELIX 53 53 THR H 74 SER H 76 5 3
HELIX 54 54 THR H 87 THR H 91 5 5
HELIX 55 55 PRO H 206 SER H 209 5 4
HELIX 56 56 ASP L 79 PHE L 83 5 5
HELIX 57 57 SER L 121 SER L 127 1 7
HELIX 58 58 LYS L 183 GLU L 187 1 5
SHEET 1 A 4 THR A 9 ALA A 12 0
SHEET 2 A 4 GLN A 444 TYR A 448 -1 O VAL A 445 N TYR A 11
SHEET 3 A 4 ASP A 434 ALA A 439 -1 N LEU A 435 O TYR A 448
SHEET 4 A 4 SER A 420 VAL A 425 -1 N ARG A 422 O ILE A 436
SHEET 1 B 3 LEU A 23 LYS A 27 0
SHEET 2 B 3 VAL A 33 ALA A 39 -1 O ALA A 34 N HIS A 26
SHEET 3 B 3 GLY A 52 PRO A 57 -1 O CYS A 56 N ILE A 35
SHEET 1 C 4 GLU A 75 VAL A 79 0
SHEET 2 C 4 GLN A 82 PHE A 87 -1 O LEU A 84 N ARG A 77
SHEET 3 C 4 HIS A 112 GLU A 117 -1 O LEU A 116 N THR A 83
SHEET 4 C 4 GLU A 120 GLU A 121 -1 O GLU A 120 N GLU A 117
SHEET 1 D 4 VAL A 97 TRP A 100 0
SHEET 2 D 4 VAL A 103 ALA A 108 -1 O VAL A 105 N VAL A 98
SHEET 3 D 4 SER A 129 ALA A 133 -1 O SER A 129 N ALA A 108
SHEET 4 D 4 ARG A 140 TYR A 143 -1 O ALA A 141 N LEU A 132
SHEET 1 E 4 SER A 172 VAL A 175 0
SHEET 2 E 4 GLU A 180 ALA A 185 -1 O VAL A 182 N VAL A 174
SHEET 3 E 4 LEU A 194 PRO A 199 -1 O ALA A 196 N LEU A 183
SHEET 4 E 4 SER A 220 LEU A 221 -1 O SER A 220 N GLN A 197
SHEET 1 F 4 VAL A 239 GLY A 242 0
SHEET 2 F 4 GLU A 252 ALA A 257 -1 O VAL A 254 N ALA A 240
SHEET 3 F 4 ALA A 266 LEU A 270 -1 O LEU A 270 N TYR A 253
SHEET 4 F 4 ARG A 276 ARG A 281 -1 O LEU A 280 N VAL A 267
SHEET 1 G 4 VAL A 293 THR A 296 0
SHEET 2 G 4 ASP A 305 ALA A 310 -1 O LEU A 307 N ALA A 294
SHEET 3 G 4 ARG A 327 PHE A 331 -1 O ARG A 327 N ALA A 310
SHEET 4 G 4 LEU A 345 THR A 348 -1 O LEU A 347 N VAL A 328
SHEET 1 H 2 MET A 314 ARG A 317 0
SHEET 2 H 2 LYS A 321 GLU A 324 -1 O LYS A 321 N ARG A 317
SHEET 1 I 4 ILE A 360 GLY A 364 0
SHEET 2 I 4 ASP A 373 ALA A 378 -1 O ASP A 373 N LEU A 363
SHEET 3 I 4 GLN A 388 PHE A 392 -1 O LEU A 390 N VAL A 376
SHEET 4 I 4 GLN A 405 ASP A 408 -1 O LEU A 407 N VAL A 389
SHEET 1 J 2 GLY A 394 GLN A 395 0
SHEET 2 J 2 GLY A 398 LEU A 399 -1 O GLY A 398 N GLN A 395
SHEET 1 K 3 CYS B 38 ASP B 39 0
SHEET 2 K 3 ALA B 24 CYS B 26 -1 N ALA B 24 O ASP B 39
SHEET 3 K 3 ILE B 54 GLU B 55 -1 O GLU B 55 N TRP B 25
SHEET 1 L 6 GLU B 60 GLU B 65 0
SHEET 2 L 6 ARG B 87 LEU B 92 -1 O ALA B 89 N ARG B 62
SHEET 3 L 6 LEU B 425 PHE B 431 1 O GLN B 428 N LEU B 90
SHEET 4 L 6 GLU B 411 PRO B 418 -1 N LYS B 412 O VAL B 429
SHEET 5 L 6 VAL B 355 ARG B 360 -1 N GLU B 358 O LYS B 417
SHEET 6 L 6 SER B 385 CYS B 386 -1 O CYS B 386 N VAL B 355
SHEET 1 M 5 VAL B 83 SER B 84 0
SHEET 2 M 5 SER B 97 ARG B 105 -1 O GLN B 103 N SER B 84
SHEET 3 M 5 THR B 394 VAL B 403 -1 O ILE B 399 N PHE B 100
SHEET 4 M 5 LEU B 366 THR B 373 -1 N ASN B 371 O SER B 398
SHEET 5 M 5 VAL B 379 PRO B 381 -1 O ILE B 380 N ALA B 372
SHEET 1 N 6 TYR B 190 THR B 197 0
SHEET 2 N 6 LEU B 149 PHE B 156 -1 N PHE B 153 O LEU B 194
SHEET 3 N 6 VAL B 112 ASP B 119 1 N TYR B 116 O GLY B 152
SHEET 4 N 6 SER B 243 THR B 250 1 O VAL B 247 N LEU B 117
SHEET 5 N 6 ASN B 305 VAL B 310 1 O ILE B 307 N PHE B 248
SHEET 6 N 6 THR B 329 VAL B 332 1 O THR B 329 N PHE B 308
SHEET 1 O 2 GLY B 453 GLU B 456 0
SHEET 2 O 2 VAL B 459 CYS B 462 -1 O ARG B 461 N THR B 454
SHEET 1 P 4 THR C 9 ALA C 12 0
SHEET 2 P 4 GLN C 444 TYR C 448 -1 O VAL C 445 N TYR C 11
SHEET 3 P 4 ASP C 434 ALA C 439 -1 N LEU C 435 O TYR C 448
SHEET 4 P 4 SER C 420 VAL C 425 -1 N ARG C 422 O ILE C 436
SHEET 1 Q 3 LEU C 23 LYS C 27 0
SHEET 2 Q 3 VAL C 33 GLY C 38 -1 O ALA C 34 N HIS C 26
SHEET 3 Q 3 VAL C 53 PRO C 57 -1 O CYS C 56 N ILE C 35
SHEET 1 R 4 THR C 76 VAL C 79 0
SHEET 2 R 4 GLN C 82 PHE C 87 -1 O LEU C 84 N ARG C 77
SHEET 3 R 4 HIS C 112 GLU C 117 -1 O LEU C 116 N THR C 83
SHEET 4 R 4 GLU C 120 GLU C 121 -1 O GLU C 120 N GLU C 117
SHEET 1 S 4 VAL C 97 TRP C 100 0
SHEET 2 S 4 VAL C 103 ALA C 108 -1 O VAL C 105 N VAL C 98
SHEET 3 S 4 SER C 129 ALA C 133 -1 O SER C 129 N ALA C 108
SHEET 4 S 4 ARG C 140 TYR C 143 -1 O ALA C 141 N LEU C 132
SHEET 1 T 4 SER C 172 VAL C 175 0
SHEET 2 T 4 GLU C 180 ALA C 185 -1 O GLY C 184 N SER C 172
SHEET 3 T 4 LEU C 194 PRO C 199 -1 O ALA C 196 N LEU C 183
SHEET 4 T 4 SER C 220 LEU C 221 -1 O SER C 220 N GLN C 197
SHEET 1 U 4 VAL C 239 GLY C 242 0
SHEET 2 U 4 GLU C 252 ALA C 257 -1 O VAL C 254 N ALA C 240
SHEET 3 U 4 ALA C 266 LEU C 270 -1 O LEU C 270 N TYR C 253
SHEET 4 U 4 ARG C 276 ARG C 281 -1 O LEU C 280 N VAL C 267
SHEET 1 V 4 VAL C 293 THR C 296 0
SHEET 2 V 4 ASP C 305 ALA C 310 -1 O LEU C 307 N ALA C 294
SHEET 3 V 4 ARG C 327 PHE C 331 -1 O PHE C 331 N LEU C 306
SHEET 4 V 4 LEU C 345 THR C 348 -1 O LEU C 347 N VAL C 328
SHEET 1 W 2 MET C 314 ARG C 317 0
SHEET 2 W 2 LYS C 321 GLU C 324 -1 O LYS C 321 N ARG C 317
SHEET 1 X 4 ILE C 360 GLY C 364 0
SHEET 2 X 4 ASP C 373 ALA C 378 -1 O ASP C 373 N LEU C 363
SHEET 3 X 4 GLN C 388 PHE C 392 -1 O LEU C 390 N VAL C 376
SHEET 4 X 4 GLN C 405 ASP C 408 -1 O LEU C 407 N VAL C 389
SHEET 1 Y 2 GLY C 394 GLN C 395 0
SHEET 2 Y 2 GLY C 398 LEU C 399 -1 O GLY C 398 N GLN C 395
SHEET 1 Z 3 CYS D 38 LEU D 40 0
SHEET 2 Z 3 CYS D 23 CYS D 26 -1 N ALA D 24 O ASP D 39
SHEET 3 Z 3 ILE D 54 GLU D 55 -1 O GLU D 55 N TRP D 25
SHEET 1 AA 6 GLU D 60 GLU D 65 0
SHEET 2 AA 6 ARG D 87 LEU D 92 -1 O ALA D 89 N ARG D 62
SHEET 3 AA 6 LEU D 425 PHE D 431 1 O GLN D 428 N LEU D 90
SHEET 4 AA 6 GLU D 411 PRO D 418 -1 N PHE D 414 O VAL D 427
SHEET 5 AA 6 VAL D 355 ARG D 360 -1 N ARG D 360 O THR D 415
SHEET 6 AA 6 SER D 385 CYS D 386 -1 O CYS D 386 N VAL D 355
SHEET 1 AB 5 VAL D 83 SER D 84 0
SHEET 2 AB 5 SER D 97 ARG D 105 -1 O GLN D 103 N SER D 84
SHEET 3 AB 5 THR D 394 VAL D 403 -1 O VAL D 395 N VAL D 104
SHEET 4 AB 5 LEU D 366 THR D 373 -1 N ASN D 371 O SER D 398
SHEET 5 AB 5 VAL D 379 PRO D 381 -1 O ILE D 380 N ALA D 372
SHEET 1 AC 6 TYR D 190 THR D 197 0
SHEET 2 AC 6 LEU D 149 PHE D 156 -1 N ILE D 151 O THR D 197
SHEET 3 AC 6 VAL D 112 ASP D 119 1 N TYR D 116 O GLY D 152
SHEET 4 AC 6 SER D 243 THR D 250 1 O SER D 243 N ASP D 113
SHEET 5 AC 6 ASN D 305 THR D 311 1 O ILE D 307 N PHE D 248
SHEET 6 AC 6 THR D 329 LEU D 333 1 O THR D 329 N PHE D 308
SHEET 1 AD 2 GLY D 453 GLU D 456 0
SHEET 2 AD 2 VAL D 459 CYS D 462 -1 O ARG D 461 N THR D 454
SHEET 1 AE 4 GLN E 3 GLN E 6 0
SHEET 2 AE 4 VAL E 18 SER E 25 -1 O THR E 23 N GLN E 5
SHEET 3 AE 4 THR E 78 LEU E 83 -1 O ALA E 79 N CYS E 22
SHEET 4 AE 4 ALA E 68 ASP E 73 -1 N THR E 71 O TYR E 80
SHEET 1 AF 6 GLU E 10 VAL E 12 0
SHEET 2 AF 6 THR E 113 VAL E 117 1 O SER E 114 N GLU E 10
SHEET 3 AF 6 ALA E 92 ARG E 98 -1 N ALA E 92 O VAL E 115
SHEET 4 AF 6 VAL E 34 ARG E 40 -1 N VAL E 37 O TYR E 95
SHEET 5 AF 6 GLY E 44 ILE E 51 -1 O GLU E 46 N LYS E 38
SHEET 6 AF 6 THR E 58 TYR E 60 -1 O LYS E 59 N ARG E 50
SHEET 1 AG 4 GLU E 10 VAL E 12 0
SHEET 2 AG 4 THR E 113 VAL E 117 1 O SER E 114 N GLU E 10
SHEET 3 AG 4 ALA E 92 ARG E 98 -1 N ALA E 92 O VAL E 115
SHEET 4 AG 4 TYR E 108 TRP E 109 -1 O TYR E 108 N ARG E 98
SHEET 1 AH 4 SER E 126 LEU E 130 0
SHEET 2 AH 4 SER E 141 TYR E 151 -1 O LEU E 147 N TYR E 128
SHEET 3 AH 4 LEU E 180 THR E 190 -1 O TYR E 181 N TYR E 151
SHEET 4 AH 4 VAL E 169 THR E 171 -1 N HIS E 170 O SER E 186
SHEET 1 AI 4 SER E 126 LEU E 130 0
SHEET 2 AI 4 SER E 141 TYR E 151 -1 O LEU E 147 N TYR E 128
SHEET 3 AI 4 LEU E 180 THR E 190 -1 O TYR E 181 N TYR E 151
SHEET 4 AI 4 VAL E 175 GLN E 177 -1 N GLN E 177 O LEU E 180
SHEET 1 AJ 2 THR E 159 TRP E 160 0
SHEET 2 AJ 2 CYS E 201 ASN E 202 -1 O ASN E 202 N THR E 159
SHEET 1 AK 4 MET F 4 SER F 7 0
SHEET 2 AK 4 VAL F 19 ALA F 25 -1 O HIS F 24 N THR F 5
SHEET 3 AK 4 ASP F 70 ILE F 75 -1 O ILE F 75 N VAL F 19
SHEET 4 AK 4 PHE F 62 SER F 67 -1 N SER F 63 O THR F 74
SHEET 1 AL 6 SER F 10 VAL F 13 0
SHEET 2 AL 6 THR F 102 ILE F 106 1 O GLU F 105 N VAL F 13
SHEET 3 AL 6 ASP F 85 GLN F 90 -1 N TYR F 86 O THR F 102
SHEET 4 AL 6 ILE F 33 GLN F 38 -1 N GLN F 38 O ASP F 85
SHEET 5 AL 6 PHE F 44 TYR F 49 -1 O LEU F 47 N TRP F 35
SHEET 6 AL 6 ASN F 53 LEU F 54 -1 O ASN F 53 N TYR F 49
SHEET 1 AM 4 SER F 10 VAL F 13 0
SHEET 2 AM 4 THR F 102 ILE F 106 1 O GLU F 105 N VAL F 13
SHEET 3 AM 4 ASP F 85 GLN F 90 -1 N TYR F 86 O THR F 102
SHEET 4 AM 4 THR F 97 PHE F 98 -1 O THR F 97 N GLN F 90
SHEET 1 AN 4 THR F 114 PHE F 118 0
SHEET 2 AN 4 ALA F 130 PHE F 139 -1 O VAL F 133 N PHE F 118
SHEET 3 AN 4 TYR F 173 LEU F 181 -1 O MET F 175 N LEU F 136
SHEET 4 AN 4 VAL F 159 TRP F 163 -1 N SER F 162 O SER F 176
SHEET 1 AO 4 SER F 153 ARG F 155 0
SHEET 2 AO 4 ASN F 145 ILE F 150 -1 N ILE F 150 O SER F 153
SHEET 3 AO 4 TYR F 192 HIS F 198 -1 O GLU F 195 N LYS F 147
SHEET 4 AO 4 SER F 201 ILE F 205 -1 O ILE F 205 N ALA F 196
SHEET 1 AP 4 GLN H 3 GLN H 6 0
SHEET 2 AP 4 VAL H 18 SER H 25 -1 O THR H 23 N GLN H 5
SHEET 3 AP 4 THR H 78 LEU H 83 -1 O LEU H 81 N LEU H 20
SHEET 4 AP 4 ALA H 68 ASP H 73 -1 N THR H 71 O TYR H 80
SHEET 1 AQ 6 GLU H 10 VAL H 12 0
SHEET 2 AQ 6 THR H 113 VAL H 117 1 O SER H 114 N GLU H 10
SHEET 3 AQ 6 ALA H 92 ARG H 98 -1 N ALA H 92 O VAL H 115
SHEET 4 AQ 6 VAL H 34 ARG H 40 -1 N HIS H 35 O VAL H 97
SHEET 5 AQ 6 GLY H 44 ILE H 51 -1 O GLU H 46 N LYS H 38
SHEET 6 AQ 6 THR H 58 TYR H 60 -1 O LYS H 59 N ARG H 50
SHEET 1 AR 4 GLU H 10 VAL H 12 0
SHEET 2 AR 4 THR H 113 VAL H 117 1 O SER H 114 N GLU H 10
SHEET 3 AR 4 ALA H 92 ARG H 98 -1 N ALA H 92 O VAL H 115
SHEET 4 AR 4 TYR H 108 TRP H 109 -1 O TYR H 108 N ARG H 98
SHEET 1 AS 4 SER H 126 LEU H 130 0
SHEET 2 AS 4 SER H 141 TYR H 151 -1 O LYS H 149 N SER H 126
SHEET 3 AS 4 LEU H 180 THR H 190 -1 O TYR H 181 N TYR H 151
SHEET 4 AS 4 VAL H 169 THR H 171 -1 N HIS H 170 O SER H 186
SHEET 1 AT 4 SER H 126 LEU H 130 0
SHEET 2 AT 4 SER H 141 TYR H 151 -1 O LYS H 149 N SER H 126
SHEET 3 AT 4 LEU H 180 THR H 190 -1 O TYR H 181 N TYR H 151
SHEET 4 AT 4 VAL H 175 GLN H 177 -1 N GLN H 177 O LEU H 180
SHEET 1 AU 3 THR H 157 TRP H 160 0
SHEET 2 AU 3 THR H 200 HIS H 205 -1 O ASN H 202 N THR H 159
SHEET 3 AU 3 THR H 210 LYS H 215 -1 O THR H 210 N HIS H 205
SHEET 1 AV 4 MET L 4 SER L 7 0
SHEET 2 AV 4 VAL L 19 ALA L 25 -1 O HIS L 24 N THR L 5
SHEET 3 AV 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21
SHEET 4 AV 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74
SHEET 1 AW 6 SER L 10 VAL L 13 0
SHEET 2 AW 6 THR L 102 ILE L 106 1 O GLU L 105 N MET L 11
SHEET 3 AW 6 ASP L 85 GLN L 90 -1 N TYR L 86 O THR L 102
SHEET 4 AW 6 ILE L 33 GLN L 38 -1 N GLY L 34 O VAL L 89
SHEET 5 AW 6 PHE L 44 TYR L 49 -1 O LEU L 47 N TRP L 35
SHEET 6 AW 6 ASN L 53 LEU L 54 -1 O ASN L 53 N TYR L 49
SHEET 1 AX 4 SER L 10 VAL L 13 0
SHEET 2 AX 4 THR L 102 ILE L 106 1 O GLU L 105 N MET L 11
SHEET 3 AX 4 ASP L 85 GLN L 90 -1 N TYR L 86 O THR L 102
SHEET 4 AX 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90
SHEET 1 AY 4 THR L 114 PHE L 118 0
SHEET 2 AY 4 GLY L 129 PHE L 139 -1 O VAL L 133 N PHE L 118
SHEET 3 AY 4 TYR L 173 THR L 182 -1 O LEU L 181 N ALA L 130
SHEET 4 AY 4 VAL L 159 TRP L 163 -1 N SER L 162 O SER L 176
SHEET 1 AZ 4 SER L 153 ARG L 155 0
SHEET 2 AZ 4 ASN L 145 ILE L 150 -1 N TRP L 148 O ARG L 155
SHEET 3 AZ 4 SER L 191 THR L 197 -1 O THR L 197 N ASN L 145
SHEET 4 AZ 4 ILE L 205 ASN L 210 -1 O ILE L 205 N ALA L 196
SSBOND 1 CYS A 56 CYS A 65 1555 1555 2.09
SSBOND 2 CYS A 107 CYS A 130 1555 1555 2.08
SSBOND 3 CYS A 146 CYS A 167 1555 1555 2.12
SSBOND 4 CYS B 5 CYS B 23 1555 1555 2.04
SSBOND 5 CYS B 13 CYS B 435 1555 1555 2.03
SSBOND 6 CYS B 16 CYS B 38 1555 1555 2.03
SSBOND 7 CYS B 26 CYS B 49 1555 1555 2.03
SSBOND 8 CYS B 177 CYS B 184 1555 1555 2.13
SSBOND 9 CYS B 232 CYS B 273 1555 1555 2.13
SSBOND 10 CYS B 374 CYS B 386 1555 1555 2.04
SSBOND 11 CYS B 406 CYS B 433 1555 1555 2.03
SSBOND 12 CYS B 437 CYS B 457 1555 1555 2.04
SSBOND 13 CYS B 448 CYS B 460 1555 1555 2.04
SSBOND 14 CYS C 56 CYS C 65 1555 1555 2.06
SSBOND 15 CYS C 107 CYS C 130 1555 1555 2.07
SSBOND 16 CYS C 146 CYS C 167 1555 1555 2.07
SSBOND 17 CYS D 5 CYS D 23 1555 1555 2.04
SSBOND 18 CYS D 13 CYS D 435 1555 1555 2.03
SSBOND 19 CYS D 16 CYS D 38 1555 1555 2.04
SSBOND 20 CYS D 26 CYS D 49 1555 1555 2.04
SSBOND 21 CYS D 177 CYS D 184 1555 1555 2.11
SSBOND 22 CYS D 232 CYS D 273 1555 1555 2.09
SSBOND 23 CYS D 374 CYS D 386 1555 1555 2.04
SSBOND 24 CYS D 406 CYS D 433 1555 1555 2.03
SSBOND 25 CYS D 437 CYS D 457 1555 1555 2.05
SSBOND 26 CYS D 448 CYS D 460 1555 1555 2.06
SSBOND 27 CYS D 462 CYS D 471 1555 1555 2.04
SSBOND 28 CYS E 22 CYS E 96 1555 1555 2.04
SSBOND 29 CYS E 134 CYS F 214 1555 1555 2.03
SSBOND 30 CYS E 146 CYS E 201 1555 1555 2.04
SSBOND 31 CYS F 23 CYS F 88 1555 1555 2.05
SSBOND 32 CYS F 134 CYS F 194 1555 1555 2.03
SSBOND 33 CYS H 22 CYS H 96 1555 1555 2.05
SSBOND 34 CYS H 134 CYS L 214 1555 1555 2.03
SSBOND 35 CYS H 146 CYS H 201 1555 1555 2.04
SSBOND 36 CYS L 23 CYS L 88 1555 1555 2.05
SSBOND 37 CYS L 134 CYS L 194 1555 1555 2.03
LINK ND2 ASN D 99 C1 NAG D3099 1555 1555 1.43
LINK ND2 ASN B 99 C1 NAG B3099 1555 1555 1.43
LINK O4 NAG B3371 C1 NAG B3372 1555 1555 1.44
LINK ND2 ASN D 371 C1 NAG D3371 1555 1555 1.44
LINK O4 NAG D3371 C1 NAG D3372 1555 1555 1.44
LINK ND2 ASN B 371 C1 NAG B3371 1555 1555 1.44
LINK ND2 ASN B 320 C1 NAG B3320 1555 1555 1.44
LINK O4 NAG D3320 C1 NAG D3321 1555 1555 1.45
LINK ND2 ASN D 320 C1 NAG D3320 1555 1555 1.45
LINK O4 NAG B3320 C1 NAG B3321 1555 1555 1.45
LINK O4 NAG B3321 C1 MAN B3322 1555 1555 1.45
LINK O4 NAG D3321 C1 MAN D3322 1555 1555 1.46
LINK MG MG B2001 O HOH B1037 1555 1555 2.05
LINK MG MG D2001 O HOH D 475 1555 1555 2.19
LINK OD1 ASP D 217 CA CA D2003 1555 1555 2.20
LINK OE2 GLU B 220 MG MG B2001 1555 1555 2.25
LINK MG MG D2001 O HOH D 505 1555 1555 2.26
LINK O THR C 250 CA CA C2004 1555 1555 2.26
LINK OD1 ASP B 217 CA CA B2003 1555 1555 2.28
LINK MG MG B2001 O HOH B1039 1555 1555 2.28
LINK O TYR C 432 CA CA C2007 1555 1555 2.29
LINK OE2 GLU D 220 MG MG D2001 1555 1555 2.31
LINK O ARG C 303 CA CA C2005 1555 1555 2.32
LINK OD2 ASP A 245 CA CA A2004 1555 1555 2.32
LINK OD1 ASN A 299 CA CA A2005 1555 1555 2.33
LINK O TYR A 371 CA CA A2006 1555 1555 2.33
LINK O TYR A 432 CA CA A2007 1555 1555 2.34
LINK OD1 ASP A 367 CA CA A2006 1555 1555 2.35
LINK O PRO B 219 CA CA B2003 1555 1555 2.35
LINK OD1 ASP A 428 CA CA A2007 1555 1555 2.35
LINK CA CA C2006 O HOH C 495 1555 1555 2.35
LINK OE1 GLU D 220 CA CA D2003 1555 1555 2.36
LINK O PRO D 219 CA CA D2003 1555 1555 2.36
LINK O THR A 250 CA CA A2004 1555 1555 2.37
LINK OD2 ASP B 158 CA CA B2003 1555 1555 2.37
LINK O ARG A 303 CA CA A2005 1555 1555 2.37
LINK CA CA A2006 O HOH A 491 1555 1555 2.37
LINK OE1 GLU B 220 CA CA B2003 1555 1555 2.38
LINK OD1 ASN C 299 CA CA C2005 1555 1555 2.39
LINK OD1 ASP A 297 CA CA A2005 1555 1555 2.39
LINK O TYR C 371 CA CA C2006 1555 1555 2.39
LINK OD1 ASP D 127 CA CA D2002 1555 1555 2.40
LINK OD1 ASN B 215 CA CA B2003 1555 1555 2.40
LINK OD1 ASP A 426 CA CA A2007 1555 1555 2.41
LINK MG MG D2001 O HOH D 864 1555 1555 2.41
LINK OD2 ASP C 245 CA CA C2004 1555 1555 2.42
LINK O MET B 335 CA CA B2002 1555 1555 2.42
LINK CA CA A2005 O HOH A 559 1555 1555 2.42
LINK CA CA B2002 O HOH B 537 1555 1555 2.43
LINK O MET D 335 CA CA D2002 1555 1555 2.43
LINK OD1 ASP B 127 CA CA B2002 1555 1555 2.43
LINK OD1 ASP C 297 CA CA C2005 1555 1555 2.43
LINK OD2 ASP A 365 CA CA A2006 1555 1555 2.44
LINK O ASP B 217 CA CA B2003 1555 1555 2.45
LINK CA CA D2002 O HOH D 515 1555 1555 2.45
LINK OD1 ASP C 367 CA CA C2006 1555 1555 2.45
LINK MG MG D2001 O HOH D1092 1555 1555 2.45
LINK OE1 GLU A 243 CA CA A2004 1555 1555 2.47
LINK MG MG B2001 O HOH B 514 1555 1555 2.48
LINK O SER D 123 CA CA D2002 1555 1555 2.49
LINK CA CA A2007 O HOH A 478 1555 1555 2.49
LINK OD1 ASN D 215 CA CA D2003 1555 1555 2.49
LINK CA CA C2007 O HOH C 566 1555 1555 2.50
LINK OD2 ASP D 158 CA CA D2003 1555 1555 2.51
LINK CA CA D2002 O HOH D 503 1555 1555 2.52
LINK CA CA B2002 O HOH B 750 1555 1555 2.52
LINK OD1 ASP A 305 CA CA A2005 1555 1555 2.52
LINK OD1 ASP C 428 CA CA C2007 1555 1555 2.52
LINK O ASP C 247 CA CA C2004 1555 1555 2.52
LINK OD2 ASP A 373 CA CA A2006 1555 1555 2.52
LINK OE2 GLU A 243 CA CA A2004 1555 1555 2.53
LINK OD1 ASN A 430 CA CA A2007 1555 1555 2.53
LINK OD1 ASP D 126 CA CA D2002 1555 1555 2.53
LINK CA CA C2005 O HOH C 810 1555 1555 2.53
LINK OD1 ASP C 426 CA CA C2007 1555 1555 2.54
LINK OG1 THR A 250 CA CA A2004 1555 1555 2.55
LINK OG SER B 121 MG MG B2001 1555 1555 2.55
LINK O ASP D 217 CA CA D2003 1555 1555 2.56
LINK OD2 ASP C 373 CA CA C2006 1555 1555 2.56
LINK OE1 GLU C 243 CA CA C2004 1555 1555 2.56
LINK OD1 ASP A 434 CA CA A2007 1555 1555 2.56
LINK O SER B 123 CA CA B2002 1555 1555 2.57
LINK OD2 ASP A 305 CA CA A2005 1555 1555 2.57
LINK OD2 ASP C 365 CA CA C2006 1555 1555 2.58
LINK OD1 ASP A 369 CA CA A2006 1555 1555 2.58
LINK OD2 ASP A 434 CA CA A2007 1555 1555 2.58
LINK OD2 ASP C 305 CA CA C2005 1555 1555 2.60
LINK OD1 ASP B 126 CA CA B2002 1555 1555 2.62
LINK O ASP A 247 CA CA A2004 1555 1555 2.62
LINK OD1 ASP C 369 CA CA C2006 1555 1555 2.62
LINK OG SER D 121 MG MG D2001 1555 1555 2.63
LINK OE2 GLU C 243 CA CA C2004 1555 1555 2.64
LINK OD2 ASP C 434 CA CA C2007 1555 1555 2.65
LINK OD1 ASN C 430 CA CA C2007 1555 1555 2.65
LINK OD1 ASP A 373 CA CA A2006 1555 1555 2.66
LINK OE2 GLU A 252 CA CA A2004 1555 1555 2.66
LINK OD1 ASP C 373 CA CA C2006 1555 1555 2.67
LINK OE1 GLU A 252 CA CA A2004 1555 1555 2.67
LINK OE2 GLU C 252 CA CA C2004 1555 1555 2.68
LINK OD1 ASP C 434 CA CA C2007 1555 1555 2.69
LINK OD1 ASP C 305 CA CA C2005 1555 1555 2.71
LINK OD1 ASP C 301 CA CA C2005 1555 1555 2.73
LINK MG MG B2001 O HOH B 897 1555 1555 2.75
LINK OD2 ASP B 126 CA CA B2002 1555 1555 2.76
LINK OD1 ASP A 301 CA CA A2005 1555 1555 2.77
LINK OE1 GLU C 252 CA CA C2004 1555 1555 2.79
LINK OG1 THR C 250 CA CA C2004 1555 1555 2.79
LINK OD2 ASP D 126 CA CA D2002 1555 1555 2.86
CISPEP 1 SER B 77 SER B 78 0 5.71
CISPEP 2 SER B 84 PRO B 85 0 -4.85
CISPEP 3 SER B 162 PRO B 163 0 8.79
CISPEP 4 SER B 168 PRO B 169 0 -10.73
CISPEP 5 PRO B 464 GLY B 465 0 -6.92
CISPEP 6 SER D 77 SER D 78 0 -3.68
CISPEP 7 SER D 84 PRO D 85 0 -6.50
CISPEP 8 SER D 162 PRO D 163 0 8.88
CISPEP 9 SER D 168 PRO D 169 0 -6.15
CISPEP 10 PHE E 152 PRO E 153 0 -5.58
CISPEP 11 GLU E 154 PRO E 155 0 -3.45
CISPEP 12 TRP E 194 PRO E 195 0 -4.68
CISPEP 13 SER F 7 PRO F 8 0 -10.96
CISPEP 14 LEU F 94 PRO F 95 0 -0.01
CISPEP 15 TYR F 140 PRO F 141 0 5.63
CISPEP 16 PHE H 152 PRO H 153 0 -2.58
CISPEP 17 GLU H 154 PRO H 155 0 -4.44
CISPEP 18 TRP H 194 PRO H 195 0 4.69
CISPEP 19 SER L 7 PRO L 8 0 -9.93
CISPEP 20 LEU L 94 PRO L 95 0 0.15
CISPEP 21 TYR L 140 PRO L 141 0 9.44
SITE 1 AC1 5 GLU A 243 ASP A 245 ASP A 247 THR A 250
SITE 2 AC1 5 GLU A 252
SITE 1 AC2 6 ASP A 297 ASN A 299 ASP A 301 ARG A 303
SITE 2 AC2 6 ASP A 305 HOH A 559
SITE 1 AC3 6 ASP A 365 ASP A 367 ASP A 369 TYR A 371
SITE 2 AC3 6 ASP A 373 HOH A 491
SITE 1 AC4 6 ASP A 426 ASP A 428 ASN A 430 TYR A 432
SITE 2 AC4 6 ASP A 434 HOH A 478
SITE 1 AC5 3 ARG A 90 LYS A 124 HOH A 581
SITE 1 AC6 4 GLN A 395 ARG A 400 SER A 401 ARG A 402
SITE 1 AC7 4 PHE A 10 PHE A 411 GLN A 444 HOH A 474
SITE 1 AC8 7 ARG A 386 PRO A 412 HOH A 894 HOH A1036
SITE 2 AC8 7 ARG C 386 PRO C 412 THR C 413
SITE 1 AC9 6 SER B 121 GLU B 220 HOH B 514 HOH B 897
SITE 2 AC9 6 HOH B1037 HOH B1039
SITE 1 BC1 6 SER B 123 ASP B 126 ASP B 127 MET B 335
SITE 2 BC1 6 HOH B 537 HOH B 750
SITE 1 BC2 5 ASP B 158 ASN B 215 ASP B 217 PRO B 219
SITE 2 BC2 5 GLU B 220
SITE 1 BC3 1 ASN B 99
SITE 1 BC4 7 MET A 285 ASN B 320 HOH B 482 HOH B 534
SITE 2 BC4 7 HOH B 536 HOH B 552 NAG B3321
SITE 1 BC5 2 NAG B3320 MAN B3322
SITE 1 BC6 2 HOH B 725 NAG B3321
SITE 1 BC7 7 SER B 369 ASN B 371 PRO B 381 SER B 398
SITE 2 BC7 7 ILE B 399 GLU B 400 NAG B3372
SITE 1 BC8 1 NAG B3371
SITE 1 BC9 5 GLU C 243 ASP C 245 ASP C 247 THR C 250
SITE 2 BC9 5 GLU C 252
SITE 1 CC1 6 ASP C 297 ASN C 299 ASP C 301 ARG C 303
SITE 2 CC1 6 ASP C 305 HOH C 810
SITE 1 CC2 6 ASP C 365 ASP C 367 ASP C 369 TYR C 371
SITE 2 CC2 6 ASP C 373 HOH C 495
SITE 1 CC3 6 ASP C 426 ASP C 428 ASN C 430 TYR C 432
SITE 2 CC3 6 ASP C 434 HOH C 566
SITE 1 CC4 3 ALA C 89 HIS C 112 HOH C 504
SITE 1 CC5 5 PRO A 383 PHE C 10 PRO C 410 GLN C 444
SITE 2 CC5 5 HOH C 985
SITE 1 CC6 3 ASN C 227 TYR C 230 ARG C 276
SITE 1 CC7 6 SER D 121 GLU D 220 HOH D 475 HOH D 505
SITE 2 CC7 6 HOH D 864 HOH D1092
SITE 1 CC8 6 SER D 123 ASP D 126 ASP D 127 MET D 335
SITE 2 CC8 6 HOH D 503 HOH D 515
SITE 1 CC9 5 ASP D 158 ASN D 215 ASP D 217 PRO D 219
SITE 2 CC9 5 GLU D 220
SITE 1 DC1 4 ASN D 99 PHE D 100 SER D 101 NAG D3372
SITE 1 DC2 8 MET C 285 ASN D 320 HOH D 541 HOH D 581
SITE 2 DC2 8 HOH D 583 HOH D 818 HOH D 893 NAG D3321
SITE 1 DC3 4 ARG C 281 HOH D 581 NAG D3320 MAN D3322
SITE 1 DC4 1 NAG D3321
SITE 1 DC5 3 ASN D 371 SER D 398 NAG D3372
SITE 1 DC6 2 NAG D3099 NAG D3371
SITE 1 DC7 7 GLN D 106 TYR D 110 SER D 243 ARG D 352
SITE 2 DC7 7 GLY D 420 HOH D1019 HOH D1065
SITE 1 DC8 5 ARG C 73 GLU L 154 ARG L 155 GLN L 156
SITE 2 DC8 5 ASN L 157
CRYST1 260.670 145.170 104.440 90.00 90.00 90.00 P 21 21 2 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 0.003836 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006888 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009575 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
