HEADER CELL ADHESION 25-JUL-11 3T3P
TITLE A NOVEL HIGH AFFINITY INTEGRIN ALPHAIIBBETA3 RECEPTOR ANTAGONIST THAT
TITLE 2 UNEXPECTEDLY DISPLACES MG2+ FROM THE BETA3 MIDAS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTEGRIN ALPHA-IIB;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: UNP RESIDUES 32-488;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: INTEGRIN BETA-3;
COMPND 8 CHAIN: B, D;
COMPND 9 FRAGMENT: UNP RESIDUES 27-498;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: MONOCLONAL ANTIBODY 10E5 HEAVY CHAIN;
COMPND 13 CHAIN: E, H;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 4;
COMPND 16 MOLECULE: MONOCLONAL ANTIBODY 10E5 LIGHT CHAIN;
COMPND 17 CHAIN: F, L;
COMPND 18 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_TAXID: 10029;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: ITGB3, GP3A;
SOURCE 13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 17 ORGANISM_COMMON: MOUSE;
SOURCE 18 ORGANISM_TAXID: 10090;
SOURCE 19 MOL_ID: 4;
SOURCE 20 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 21 ORGANISM_COMMON: MOUSE;
SOURCE 22 ORGANISM_TAXID: 10090
KEYWDS INTEGRIN, CELL ADHESION, BLOOD CLOTTING, FIBRINOGEN, PLATELET
EXPDTA X-RAY DIFFRACTION
AUTHOR J.ZHU,J.ZHU,T.A.SPRINGER
REVDAT 1 28-MAR-12 3T3P 0
JRNL AUTH J.ZHU,W.S.CHOI,J.G.MCCOY,A.NEGRI,J.ZHU,S.NAINI,J.LI,M.SHEN,
JRNL AUTH 2 W.HUANG,D.BOUGIE,M.RASMUSSEN,R.ASTER,C.J.THOMAS,M.FILIZOLA,
JRNL AUTH 3 T.A.SPRINGER,B.S.COLLER
JRNL TITL STRUCTURE-GUIDED DESIGN OF A HIGH-AFFINITY PLATELET INTEGRIN
JRNL TITL 2 ALPHAIIBBETA3 RECEPTOR ANTAGONIST THAT DISRUPTS MG2+ BINDING
JRNL TITL 3 TO THE MIDAS
JRNL REF SCI TRANSL MED V. 4 5RA32 2012
JRNL REFN ISSN 1946-6234
JRNL PMID 22422993
JRNL DOI 10.1126/SCITRANSLMED.3003576
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.39
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 199280
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.500
REMARK 3 FREE R VALUE TEST SET COUNT : 991
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 48.3986 - 4.2077 0.99 29172 148 0.1694 0.1914
REMARK 3 2 4.2077 - 3.3400 0.99 28515 147 0.1698 0.2033
REMARK 3 3 3.3400 - 2.9179 0.99 28275 164 0.1853 0.2050
REMARK 3 4 2.9179 - 2.6511 1.00 28282 131 0.1958 0.2370
REMARK 3 5 2.6511 - 2.4611 1.00 28243 140 0.2180 0.2650
REMARK 3 6 2.4611 - 2.3160 1.00 28117 132 0.2389 0.2709
REMARK 3 7 2.3160 - 2.2000 0.98 27685 129 0.2701 0.3270
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 : 0.40
REMARK 3 B_SOL : 40.00
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.700
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.370
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) : 14.27750
REMARK 3 B22 (A**2) : 13.77460
REMARK 3 B33 (A**2) : 13.83080
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 21749
REMARK 3 ANGLE : 0.850 29744
REMARK 3 CHIRALITY : 0.052 3280
REMARK 3 PLANARITY : 0.004 3825
REMARK 3 DIHEDRAL : 14.543 7897
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): 51.1300 90.6727 54.3053
REMARK 3 T TENSOR
REMARK 3 T11: -0.1110 T22: -0.3990
REMARK 3 T33: -0.2010 T12: 0.0409
REMARK 3 T13: 0.1980 T23: 0.1452
REMARK 3 L TENSOR
REMARK 3 L11: 0.0345 L22: 0.0611
REMARK 3 L33: 0.0683 L12: 0.0008
REMARK 3 L13: -0.0329 L23: 0.0411
REMARK 3 S TENSOR
REMARK 3 S11: -0.0102 S12: -0.0825 S13: -0.0353
REMARK 3 S21: 0.0968 S22: -0.0235 S23: 0.0877
REMARK 3 S31: 0.1419 S32: -0.0909 S33: -0.1230
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain C and resid 1:450
REMARK 3 ORIGIN FOR THE GROUP (A): 84.8740 86.9672 117.9781
REMARK 3 T TENSOR
REMARK 3 T11: -0.1061 T22: 0.2293
REMARK 3 T33: -0.1678 T12: 0.1014
REMARK 3 T13: 0.2384 T23: -0.0333
REMARK 3 L TENSOR
REMARK 3 L11: 0.1216 L22: 0.1558
REMARK 3 L33: 0.3417 L12: 0.0174
REMARK 3 L13: -0.0737 L23: -0.0234
REMARK 3 S TENSOR
REMARK 3 S11: -0.0503 S12: 0.0913 S13: -0.0638
REMARK 3 S21: -0.1178 S22: 0.0091 S23: -0.1813
REMARK 3 S31: 0.1619 S32: 0.3108 S33: 0.0296
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain B and resid 1:57
REMARK 3 ORIGIN FOR THE GROUP (A): 123.7801 88.7332 35.1695
REMARK 3 T TENSOR
REMARK 3 T11: 0.4183 T22: 0.9474
REMARK 3 T33: 0.6438 T12: 0.3067
REMARK 3 T13: -0.0011 T23: -0.1408
REMARK 3 L TENSOR
REMARK 3 L11: 4.9657 L22: 4.9349
REMARK 3 L33: 1.4760 L12: -1.0271
REMARK 3 L13: -0.8755 L23: -0.6823
REMARK 3 S TENSOR
REMARK 3 S11: -0.2084 S12: 0.0060 S13: -0.6187
REMARK 3 S21: -0.1877 S22: -0.1222 S23: -1.0363
REMARK 3 S31: 0.2515 S32: 0.3339 S33: 0.3228
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): 101.5006 107.9434 52.8595
REMARK 3 T TENSOR
REMARK 3 T11: 0.1140 T22: 0.3902
REMARK 3 T33: 0.3141 T12: 0.0672
REMARK 3 T13: -0.0517 T23: -0.1163
REMARK 3 L TENSOR
REMARK 3 L11: 3.0601 L22: 1.0923
REMARK 3 L33: 1.1977 L12: -0.5379
REMARK 3 L13: -0.4986 L23: 0.3974
REMARK 3 S TENSOR
REMARK 3 S11: 0.0338 S12: -0.0052 S13: 0.1576
REMARK 3 S21: 0.0150 S22: 0.0423 S23: -0.0959
REMARK 3 S31: 0.0411 S32: 0.1446 S33: -0.0566
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain B and resid 109:352
REMARK 3 ORIGIN FOR THE GROUP (A): 68.1358 118.8061 63.8023
REMARK 3 T TENSOR
REMARK 3 T11: 0.0080 T22: -0.2051
REMARK 3 T33: 0.0171 T12: 0.0176
REMARK 3 T13: 0.0477 T23: -0.0326
REMARK 3 L TENSOR
REMARK 3 L11: 0.1640 L22: 0.1986
REMARK 3 L33: 0.1437 L12: -0.1055
REMARK 3 L13: -0.0652 L23: 0.0271
REMARK 3 S TENSOR
REMARK 3 S11: 0.0464 S12: -0.0354 S13: 0.1171
REMARK 3 S21: 0.0243 S22: 0.0361 S23: -0.0483
REMARK 3 S31: -0.1032 S32: 0.0344 S33: 0.0996
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: chain B and resid 433:461
REMARK 3 ORIGIN FOR THE GROUP (A): 117.5010 90.3532 19.8517
REMARK 3 T TENSOR
REMARK 3 T11: 0.2912 T22: 0.7528
REMARK 3 T33: 0.5023 T12: 0.1691
REMARK 3 T13: 0.0832 T23: -0.0899
REMARK 3 L TENSOR
REMARK 3 L11: 8.8150 L22: 3.6415
REMARK 3 L33: 4.9664 L12: 0.3334
REMARK 3 L13: -2.1042 L23: -2.1995
REMARK 3 S TENSOR
REMARK 3 S11: 0.0887 S12: -0.1741 S13: -0.1110
REMARK 3 S21: -0.3868 S22: 0.0494 S23: -0.9285
REMARK 3 S31: 0.1069 S32: 0.2016 S33: -0.1393
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: chain D and resid 1:57
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5145 70.6928 141.0641
REMARK 3 T TENSOR
REMARK 3 T11: 0.4418 T22: 0.6083
REMARK 3 T33: 0.4342 T12: -0.3195
REMARK 3 T13: 0.0626 T23: -0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 5.0415 L22: 4.7360
REMARK 3 L33: 1.8488 L12: 0.9524
REMARK 3 L13: -1.1770 L23: -1.0849
REMARK 3 S TENSOR
REMARK 3 S11: -0.1849 S12: -0.0253 S13: -0.7064
REMARK 3 S21: -0.0480 S22: 0.1148 S23: 0.6681
REMARK 3 S31: 0.2482 S32: -0.2452 S33: 0.0440
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): 31.6803 87.5761 116.0653
REMARK 3 T TENSOR
REMARK 3 T11: 0.1904 T22: 0.4901
REMARK 3 T33: 0.1529 T12: -0.1716
REMARK 3 T13: -0.0116 T23: 0.0655
REMARK 3 L TENSOR
REMARK 3 L11: 1.0094 L22: 0.3178
REMARK 3 L33: 3.0520 L12: 0.2168
REMARK 3 L13: -0.9019 L23: -0.6588
REMARK 3 S TENSOR
REMARK 3 S11: -0.0917 S12: 0.1660 S13: -0.0328
REMARK 3 S21: -0.0476 S22: 0.0318 S23: 0.0074
REMARK 3 S31: 0.1448 S32: -0.1752 S33: 0.0372
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: chain D and resid 109:352
REMARK 3 ORIGIN FOR THE GROUP (A): 60.9133 102.6524 99.5730
REMARK 3 T TENSOR
REMARK 3 T11: 0.0904 T22: 0.2466
REMARK 3 T33: -0.0435 T12: -0.0721
REMARK 3 T13: 0.0478 T23: 0.1068
REMARK 3 L TENSOR
REMARK 3 L11: 0.2123 L22: 0.1816
REMARK 3 L33: 0.5261 L12: -0.0402
REMARK 3 L13: 0.0294 L23: -0.0527
REMARK 3 S TENSOR
REMARK 3 S11: -0.0073 S12: 0.1353 S13: 0.0853
REMARK 3 S21: -0.0820 S22: 0.0316 S23: 0.0272
REMARK 3 S31: -0.0764 S32: -0.1410 S33: -0.0775
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: chain D and resid 433:461
REMARK 3 ORIGIN FOR THE GROUP (A): 19.5643 80.5564 153.7085
REMARK 3 T TENSOR
REMARK 3 T11: 0.1802 T22: 0.3382
REMARK 3 T33: 0.2739 T12: -0.1238
REMARK 3 T13: 0.0715 T23: -0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 6.5701 L22: 4.1000
REMARK 3 L33: 1.2041 L12: 1.2830
REMARK 3 L13: -0.5479 L23: 1.0230
REMARK 3 S TENSOR
REMARK 3 S11: -0.0058 S12: -0.0233 S13: 0.0026
REMARK 3 S21: 0.1105 S22: 0.2406 S23: 0.4118
REMARK 3 S31: 0.0803 S32: -0.2909 S33: -0.2494
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: chain H and resid 1:119
REMARK 3 ORIGIN FOR THE GROUP (A): 18.3847 96.9792 82.7917
REMARK 3 T TENSOR
REMARK 3 T11: 0.3252 T22: 0.4289
REMARK 3 T33: 0.2151 T12: 0.0141
REMARK 3 T13: 0.1490 T23: -0.0750
REMARK 3 L TENSOR
REMARK 3 L11: 0.6123 L22: 0.3045
REMARK 3 L33: 2.0494 L12: 0.3983
REMARK 3 L13: -0.3725 L23: -0.5264
REMARK 3 S TENSOR
REMARK 3 S11: -0.1413 S12: -0.4464 S13: -0.0065
REMARK 3 S21: 0.4342 S22: 0.0732 S23: 0.1920
REMARK 3 S31: 0.1015 S32: -0.0086 S33: 0.0505
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: chain H and resid 120:221
REMARK 3 ORIGIN FOR THE GROUP (A): -13.6762 81.5543 93.4142
REMARK 3 T TENSOR
REMARK 3 T11: 0.4041 T22: 0.4868
REMARK 3 T33: 1.1394 T12: 0.0823
REMARK 3 T13: 0.2039 T23: 0.1641
REMARK 3 L TENSOR
REMARK 3 L11: 5.4640 L22: 0.7850
REMARK 3 L33: 4.4357 L12: -0.0981
REMARK 3 L13: 0.9319 L23: 1.2248
REMARK 3 S TENSOR
REMARK 3 S11: 0.0187 S12: -0.3435 S13: -1.1221
REMARK 3 S21: 0.2138 S22: 0.0142 S23: 0.0746
REMARK 3 S31: 0.6843 S32: -0.1549 S33: -0.0427
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: chain L and resid 1:108
REMARK 3 ORIGIN FOR THE GROUP (A): 6.8917 96.1019 64.5145
REMARK 3 T TENSOR
REMARK 3 T11: 0.0848 T22: 0.4169
REMARK 3 T33: 0.3429 T12: -0.0084
REMARK 3 T13: 0.0811 T23: -0.1250
REMARK 3 L TENSOR
REMARK 3 L11: 1.5907 L22: 0.3026
REMARK 3 L33: 0.4104 L12: 0.1617
REMARK 3 L13: -0.0590 L23: -0.1645
REMARK 3 S TENSOR
REMARK 3 S11: -0.0608 S12: 0.1752 S13: -0.1713
REMARK 3 S21: 0.0129 S22: -0.0210 S23: 0.2982
REMARK 3 S31: 0.0966 S32: -0.3205 S33: 0.0071
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: chain L and resid 109:214
REMARK 3 ORIGIN FOR THE GROUP (A): -22.0736 93.5481 86.6806
REMARK 3 T TENSOR
REMARK 3 T11: 0.1460 T22: 0.4800
REMARK 3 T33: 0.5755 T12: 0.0110
REMARK 3 T13: 0.1723 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 2.3280 L22: 0.6033
REMARK 3 L33: 2.3618 L12: 0.0948
REMARK 3 L13: -0.6156 L23: 0.1840
REMARK 3 S TENSOR
REMARK 3 S11: -0.0926 S12: -0.0383 S13: -0.2490
REMARK 3 S21: 0.0555 S22: -0.0145 S23: 0.0824
REMARK 3 S31: 0.1464 S32: -0.0993 S33: 0.1071
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: chain E and resid 1:119
REMARK 3 ORIGIN FOR THE GROUP (A): 115.5604 90.3136 86.5574
REMARK 3 T TENSOR
REMARK 3 T11: 0.5941 T22: 0.6559
REMARK 3 T33: 0.3731 T12: -0.0871
REMARK 3 T13: 0.2694 T23: -0.0128
REMARK 3 L TENSOR
REMARK 3 L11: 1.6300 L22: 0.6002
REMARK 3 L33: 3.4031 L12: -0.8788
REMARK 3 L13: -0.9564 L23: 1.1138
REMARK 3 S TENSOR
REMARK 3 S11: -0.1919 S12: 0.4681 S13: -0.2678
REMARK 3 S21: -0.3509 S22: -0.0593 S23: -0.1181
REMARK 3 S31: 0.6525 S32: -0.0475 S33: 0.2973
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: chain E and resid 120:221
REMARK 3 ORIGIN FOR THE GROUP (A): 151.4353 82.9927 80.0385
REMARK 3 T TENSOR
REMARK 3 T11: 0.9147 T22: 1.1268
REMARK 3 T33: 1.1023 T12: 0.3202
REMARK 3 T13: 0.2816 T23: 0.1210
REMARK 3 L TENSOR
REMARK 3 L11: 6.1436 L22: 3.7941
REMARK 3 L33: 3.3905 L12: -0.1935
REMARK 3 L13: 0.7826 L23: 2.0382
REMARK 3 S TENSOR
REMARK 3 S11: 0.2198 S12: 1.1242 S13: -0.7982
REMARK 3 S21: -0.3155 S22: -0.1196 S23: -1.0255
REMARK 3 S31: 0.5760 S32: 1.2000 S33: -0.1019
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: chain F and resid 1:108
REMARK 3 ORIGIN FOR THE GROUP (A): 125.8902 100.5827 102.5532
REMARK 3 T TENSOR
REMARK 3 T11: 0.1840 T22: 0.6480
REMARK 3 T33: 0.5571 T12: -0.0546
REMARK 3 T13: 0.1482 T23: 0.0179
REMARK 3 L TENSOR
REMARK 3 L11: 1.2792 L22: 0.2825
REMARK 3 L33: 0.2763 L12: 0.2564
REMARK 3 L13: 0.4093 L23: 0.1034
REMARK 3 S TENSOR
REMARK 3 S11: -0.0312 S12: -0.0724 S13: 0.0886
REMARK 3 S21: -0.0779 S22: -0.0050 S23: -0.4562
REMARK 3 S31: 0.0187 S32: 0.3655 S33: -0.0055
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: chain F and resid 109:214
REMARK 3 ORIGIN FOR THE GROUP (A): 154.8666 98.9069 80.6566
REMARK 3 T TENSOR
REMARK 3 T11: 0.7721 T22: 1.2149
REMARK 3 T33: 1.1278 T12: 0.1657
REMARK 3 T13: 0.3641 T23: 0.3062
REMARK 3 L TENSOR
REMARK 3 L11: 4.0184 L22: 2.2580
REMARK 3 L33: 5.6044 L12: 1.3399
REMARK 3 L13: -1.9952 L23: 1.7295
REMARK 3 S TENSOR
REMARK 3 S11: 0.0004 S12: 0.3091 S13: 0.0944
REMARK 3 S21: -0.8932 S22: 0.2842 S23: -0.9231
REMARK 3 S31: -0.2536 S32: 1.2454 S33: -0.2919
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 3T3P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-SEP-11.
REMARK 100 THE RCSB ID CODE IS RCSB066997.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-OCT-10
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) : 1.0332
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 : 199292
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.32
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 129.76650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 72.62850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 129.76650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 72.62850
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, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, 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 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 LYS A 455
REMARK 465 ALA A 456
REMARK 465 SER A 457
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 GLU B 472
REMARK 465 VAL C 454
REMARK 465 LYS C 455
REMARK 465 ALA C 456
REMARK 465 SER C 457
REMARK 465 GLU D 472
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 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU B 174 CG CD OE1 OE2
REMARK 480 LYS D 350 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 A 1282 O HOH A 1284 1.70
REMARK 500 O HOH A 475 O HOH A 1141 1.75
REMARK 500 O HOH A 484 O HOH A 1234 1.77
REMARK 500 O HOH C 1237 O HOH C 1287 1.78
REMARK 500 O HOH A 1127 O HOH A 1234 1.84
REMARK 500 O HOH A 593 O HOH A 1154 1.88
REMARK 500 O HOH L 216 O HOH L 1197 1.89
REMARK 500 O HOH A 1280 O HOH A 1282 1.91
REMARK 500 O HOH C 1247 O HOH D 1117 1.96
REMARK 500 O HOH A 1282 O HOH A 1288 1.96
REMARK 500 O HOH D 513 O HOH D 1126 2.01
REMARK 500 O HOH B 563 O HOH B 1213 2.02
REMARK 500 O HOH C 926 O HOH D 1171 2.02
REMARK 500 O HOH C 510 O HOH C 1135 2.02
REMARK 500 O HOH A 1128 O HOH A 1188 2.05
REMARK 500 O HOH A 518 O HOH A 593 2.05
REMARK 500 O HOH B 935 O HOH B 1136 2.05
REMARK 500 O HOH A 1280 O HOH A 1281 2.06
REMARK 500 O HOH A 517 O HOH B 673 2.07
REMARK 500 ND2 ASN D 371 C2 NAG D 3371 2.08
REMARK 500 O HOH B 555 O HOH B 1166 2.08
REMARK 500 O HOH C 970 O HOH C 1291 2.10
REMARK 500 O HOH D 1158 O HOH D 1160 2.10
REMARK 500 O HOH A 669 O HOH A 1162 2.12
REMARK 500 O HOH A 1128 O HOH A 1190 2.14
REMARK 500 O HOH C 929 O HOH C 1131 2.14
REMARK 500 O HOH A 604 O HOH D 1238 2.14
REMARK 500 O4 SO4 A 460 O HOH A 691 2.14
REMARK 500 O HOH A 517 O HOH A 1111 2.15
REMARK 500 O HOH A 1151 O HOH B 1113 2.15
REMARK 500 O HOH A 566 O HOH A 1279 2.15
REMARK 500 O HOH C 586 O HOH C 1179 2.16
REMARK 500 O HOH L 1132 O HOH L 1175 2.18
REMARK 500 O HOH A 928 O HOH A 1122 2.18
REMARK 500 O HOH A 928 O HOH A 1110 2.18
REMARK 500 O HOH B 541 O HOH B 925 2.18
REMARK 500 O HOH A 859 O HOH A 977 2.18
REMARK 500 O HOH C 1148 O HOH C 1236 2.19
REMARK 500 O HOH B 526 O HOH B 1264 2.19
REMARK 500 OG SER F 201 O SER F 203 2.19
REMARK 500 O HOH A 592 O HOH B 974 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 SER A 46 28.58 -79.39
REMARK 500 SER A 101 -128.70 52.47
REMARK 500 LYS A 118 -115.43 57.33
REMARK 500 GLU A 123 135.70 98.03
REMARK 500 LEU A 212 -44.64 74.49
REMARK 500 SER A 222 -167.50 -77.49
REMARK 500 ASP A 319 39.38 75.51
REMARK 500 PRO A 337 104.85 -58.32
REMARK 500 PHE A 417 117.03 -38.54
REMARK 500 PHE B 56 79.56 -161.89
REMARK 500 ASP B 66 43.67 -144.56
REMARK 500 ASP B 76 165.88 65.47
REMARK 500 SER B 77 62.13 -100.33
REMARK 500 VAL B 157 -80.77 -127.38
REMARK 500 MET B 180 -164.45 -100.84
REMARK 500 SER B 213 -160.85 -122.71
REMARK 500 ASP B 241 77.03 -109.67
REMARK 500 LEU B 258 -9.60 87.02
REMARK 500 LEU B 375 -94.39 48.51
REMARK 500 ASN B 377 18.70 45.59
REMARK 500 SER C 101 -128.70 54.28
REMARK 500 LYS C 118 -115.88 60.86
REMARK 500 GLU C 123 135.51 98.33
REMARK 500 LEU C 212 -52.04 76.68
REMARK 500 SER C 222 -174.58 -69.06
REMARK 500 ALA D 30 40.72 -95.77
REMARK 500 ASP D 47 35.66 -87.00
REMARK 500 ASN D 48 16.78 55.50
REMARK 500 PHE D 56 81.94 -161.01
REMARK 500 ASP D 66 40.19 -144.62
REMARK 500 VAL D 157 -77.09 -130.68
REMARK 500 PRO D 169 -175.83 -69.35
REMARK 500 SER D 213 -163.21 -120.96
REMARK 500 ASP D 241 74.75 -108.23
REMARK 500 LEU D 258 -13.97 94.18
REMARK 500 CYS D 374 -123.06 -97.69
REMARK 500 ASN D 376 -136.84 58.95
REMARK 500 ASN E 55 -18.93 -162.84
REMARK 500 PHE E 152 141.10 -171.93
REMARK 500 SER E 167 94.77 -66.20
REMARK 500 SER F 43 -158.98 -85.63
REMARK 500 SER F 77 75.31 57.51
REMARK 500 SER F 127 33.53 -91.59
REMARK 500 LEU F 136 78.06 -117.11
REMARK 500 ASN F 138 82.70 57.99
REMARK 500 PRO F 141 -168.62 -72.71
REMARK 500 LEU F 181 -169.26 -167.71
REMARK 500 GLU F 187 36.75 -77.32
REMARK 500 ASN F 190 -52.24 -125.65
REMARK 500 ALA F 196 124.79 -171.47
REMARK 500
REMARK 500 THIS ENTRY HAS 64 RAMACHANDRAN OUTLIERS.
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 CA A2004 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 245 OD2
REMARK 620 2 THR A 250 O 166.0
REMARK 620 3 GLU A 243 OE1 119.4 74.5
REMARK 620 4 THR A 250 OG1 87.2 79.1 146.4
REMARK 620 5 GLU A 243 OE2 64.5 129.4 54.9 146.0
REMARK 620 6 GLU A 252 OE2 89.2 83.1 126.4 69.3 125.1
REMARK 620 7 ASP A 247 O 89.8 90.1 82.5 77.1 84.1 146.4
REMARK 620 8 GLU A 252 OE1 80.6 103.3 87.1 119.3 76.1 51.5 160.2
REMARK 620 N 1 2 3 4 5 6 7
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 GLU B 220 OE2
REMARK 620 2 SER B 121 OG 91.8
REMARK 620 3 HOH B 477 O 106.0 70.2
REMARK 620 4 HOH B1120 O 78.2 101.6 170.6
REMARK 620 5 HOH B1121 O 94.9 166.4 96.5 91.4
REMARK 620 6 HOH B 920 O 168.5 86.8 84.3 90.9 89.0
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 PRO D 219 O 102.3
REMARK 620 3 GLU D 220 OE1 163.9 78.2
REMARK 620 4 ASN D 215 OD1 91.0 163.3 86.2
REMARK 620 5 ASP D 158 OD2 96.2 87.2 99.9 101.5
REMARK 620 6 ASP D 217 O 73.8 85.7 90.2 88.4 166.2
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 GLU D 220 OE2
REMARK 620 2 SER D 121 OG 92.7
REMARK 620 3 HOH D1118 O 113.4 72.4
REMARK 620 4 HOH D 476 O 89.4 172.9 100.6
REMARK 620 5 HOH D1126 O 79.9 99.0 164.0 88.0
REMARK 620 6 HOH D1115 O 167.0 92.5 79.6 87.0 87.5
REMARK 620 N 1 2 3 4 5
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 154.8
REMARK 620 3 ASP C 297 OD1 77.7 77.6
REMARK 620 4 ASP C 305 OD2 92.4 90.2 84.4
REMARK 620 5 ASP C 305 OD1 92.6 108.5 135.1 51.9
REMARK 620 6 ASP C 301 OD1 88.1 81.1 76.0 159.8 148.2
REMARK 620 7 HOH C1134 O 113.9 87.5 156.0 114.7 67.5 83.2
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 158.7
REMARK 620 3 ASP A 365 OD2 74.2 84.6
REMARK 620 4 ASP A 369 OD1 90.1 86.2 77.0
REMARK 620 5 ASP A 373 OD2 82.6 111.4 130.9 146.6
REMARK 620 6 ASP A 373 OD1 91.7 85.9 87.2 162.9 50.4
REMARK 620 7 HOH A 486 O 103.2 96.5 154.9 78.0 72.1 118.0
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 90.9
REMARK 620 3 ASP D 126 OD1 78.1 126.0
REMARK 620 4 SER D 123 O 91.9 161.9 72.1
REMARK 620 5 ASP D 126 OD2 91.0 76.5 51.4 121.3
REMARK 620 6 HOH D 509 O 177.6 90.7 99.5 87.1 87.5
REMARK 620 7 HOH D 488 O 98.0 78.4 154.9 83.4 153.5 84.1
REMARK 620 N 1 2 3 4 5 6
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 ASP C 428 OD1 151.2
REMARK 620 3 ASN C 430 OD1 88.2 86.8
REMARK 620 4 ASP C 434 OD2 86.3 116.5 135.5
REMARK 620 5 ASP C 426 OD1 77.3 74.1 85.9 135.2
REMARK 620 6 ASP C 434 OD1 98.7 83.3 169.5 53.4 87.9
REMARK 620 7 HOH C 478 O 127.4 78.6 75.9 72.9 147.9 105.5
REMARK 620 N 1 2 3 4 5 6
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 165.4
REMARK 620 3 GLU C 243 OE1 76.7 114.8
REMARK 620 4 ASP C 247 O 88.6 84.0 83.3
REMARK 620 5 GLU C 243 OE2 131.7 60.3 55.1 85.3
REMARK 620 6 THR C 250 OG1 84.6 81.0 147.9 70.3 136.3
REMARK 620 7 GLU C 252 OE2 91.5 86.4 134.4 141.1 121.6 71.0
REMARK 620 8 GLU C 252 OE1 115.8 73.9 94.0 154.2 72.4 117.7 51.8
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 160.5
REMARK 620 3 ASP A 297 OD1 84.9 75.6
REMARK 620 4 ASP A 305 OD2 88.2 90.4 83.6
REMARK 620 5 ASP A 305 OD1 112.9 80.8 128.4 51.1
REMARK 620 6 ASP A 301 OD1 88.5 86.8 78.4 161.9 145.2
REMARK 620 7 HOH A 478 O 90.4 107.3 157.4 118.4 73.6 79.4
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 TYR C 371 O
REMARK 620 2 ASP C 365 OD2 75.7
REMARK 620 3 ASP C 367 OD1 152.4 77.9
REMARK 620 4 ASP C 369 OD1 91.4 78.9 75.8
REMARK 620 5 ASP C 373 OD2 85.5 134.9 119.3 143.1
REMARK 620 6 ASP C 373 OD1 93.8 87.9 92.9 164.1 52.4
REMARK 620 7 HOH C 494 O 97.8 150.2 101.2 72.1 71.9 121.8
REMARK 620 N 1 2 3 4 5 6
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 103.6
REMARK 620 3 ASN B 215 OD1 86.9 168.2
REMARK 620 4 ASP B 217 O 76.3 89.8 87.4
REMARK 620 5 ASP B 158 OD2 94.2 84.3 100.6 167.4
REMARK 620 6 GLU B 220 OE1 170.1 80.1 88.7 94.6 95.3
REMARK 620 N 1 2 3 4 5
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 156.8
REMARK 620 3 ASP A 426 OD1 79.2 78.0
REMARK 620 4 ASP A 434 OD1 95.1 90.7 93.7
REMARK 620 5 ASN A 430 OD1 86.2 86.6 82.8 175.9
REMARK 620 6 ASP A 434 OD2 79.5 121.2 138.1 53.0 131.0
REMARK 620 7 HOH A 467 O 127.3 72.6 145.9 103.4 78.7 73.8
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 ASP B 127 OD1
REMARK 620 2 MET B 335 O 87.9
REMARK 620 3 ASP B 126 OD1 85.3 124.8
REMARK 620 4 SER B 123 O 94.7 160.2 75.0
REMARK 620 5 ASP B 126 OD2 93.6 74.2 51.7 125.0
REMARK 620 6 HOH B 525 O 175.8 94.4 90.5 84.3 83.7
REMARK 620 7 HOH B 502 O 93.8 77.0 158.0 83.2 150.0 90.2
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 SO4 A 458
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 459
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 460
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 461
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 473
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3099
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3320
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3321
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 3322
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 3323
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 3324
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3371
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3372
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 458
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 459
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 460
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 461
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 462
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2005
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2006
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2007
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 473
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3099
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3320
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3321
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA D 3322
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D 3323
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3371
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3372
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
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: 3NID RELATED DB: PDB
REMARK 900 RELATED ID: 3NIF RELATED DB: PDB
REMARK 900 RELATED ID: 3NIG RELATED DB: PDB
REMARK 900 RELATED ID: 2VDR RELATED DB: PDB
REMARK 900 RELATED ID: 3T3M RELATED DB: PDB
DBREF 3T3P A 1 457 UNP P08514 ITA2B_HUMAN 32 488
DBREF 3T3P B 1 472 UNP P05106 ITB3_HUMAN 27 498
DBREF 3T3P C 1 457 UNP P08514 ITA2B_HUMAN 32 488
DBREF 3T3P D 1 472 UNP P05106 ITB3_HUMAN 27 498
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 472 GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS
SEQRES 2 B 472 GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS
SEQRES 3 B 472 SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP
SEQRES 4 B 472 LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU
SEQRES 5 B 472 SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU
SEQRES 6 B 472 ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER
SEQRES 7 B 472 GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG
SEQRES 8 B 472 LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL
SEQRES 9 B 472 ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU
SEQRES 10 B 472 MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER
SEQRES 11 B 472 ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG
SEQRES 12 B 472 LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE
SEQRES 13 B 472 VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO
SEQRES 14 B 472 PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR
SEQRES 15 B 472 THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR
SEQRES 16 B 472 LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS
SEQRES 17 B 472 LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY
SEQRES 18 B 472 GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU
SEQRES 19 B 472 LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL
SEQRES 20 B 472 PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY
SEQRES 21 B 472 ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS
SEQRES 22 B 472 HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR
SEQRES 23 B 472 MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU
SEQRES 24 B 472 SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU
SEQRES 25 B 472 ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE
SEQRES 26 B 472 PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER
SEQRES 27 B 472 ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE
SEQRES 28 B 472 ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU
SEQRES 29 B 472 GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN
SEQRES 30 B 472 GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS
SEQRES 31 B 472 ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL
SEQRES 32 B 472 ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE
SEQRES 33 B 472 LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL
SEQRES 34 B 472 THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU
SEQRES 35 B 472 PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE
SEQRES 36 B 472 GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY
SEQRES 37 B 472 SER GLN CYS GLU
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 472 GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS
SEQRES 2 D 472 GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS
SEQRES 3 D 472 SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP
SEQRES 4 D 472 LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU
SEQRES 5 D 472 SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU
SEQRES 6 D 472 ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER
SEQRES 7 D 472 GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG
SEQRES 8 D 472 LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL
SEQRES 9 D 472 ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU
SEQRES 10 D 472 MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER
SEQRES 11 D 472 ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG
SEQRES 12 D 472 LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE
SEQRES 13 D 472 VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO
SEQRES 14 D 472 PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR
SEQRES 15 D 472 THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR
SEQRES 16 D 472 LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS
SEQRES 17 D 472 LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY
SEQRES 18 D 472 GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU
SEQRES 19 D 472 LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL
SEQRES 20 D 472 PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY
SEQRES 21 D 472 ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS
SEQRES 22 D 472 HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR
SEQRES 23 D 472 MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU
SEQRES 24 D 472 SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU
SEQRES 25 D 472 ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE
SEQRES 26 D 472 PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER
SEQRES 27 D 472 ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE
SEQRES 28 D 472 ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU
SEQRES 29 D 472 GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN
SEQRES 30 D 472 GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS
SEQRES 31 D 472 ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL
SEQRES 32 D 472 ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE
SEQRES 33 D 472 LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL
SEQRES 34 D 472 THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU
SEQRES 35 D 472 PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE
SEQRES 36 D 472 GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY
SEQRES 37 D 472 SER GLN CYS GLU
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 3T3P ASN D 99 ASN GLYCOSYLATION SITE
MODRES 3T3P ASN D 371 ASN GLYCOSYLATION SITE
MODRES 3T3P ASN B 99 ASN GLYCOSYLATION SITE
MODRES 3T3P ASN D 320 ASN GLYCOSYLATION SITE
MODRES 3T3P ASN B 371 ASN GLYCOSYLATION SITE
MODRES 3T3P ASN B 320 ASN GLYCOSYLATION SITE
HET SO4 A 458 5
HET SO4 A 459 5
HET SO4 A 460 5
HET GOL A 461 6
HET CA A2004 1
HET CA A2005 1
HET CA A2006 1
HET CA A2007 1
HET CL B 473 1
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 BMA B3322 11
HET MAN B3323 11
HET MAN B3324 11
HET NAG B3371 14
HET NAG B3372 14
HET SO4 C 458 5
HET SO4 C 459 5
HET SO4 C 460 5
HET CL C 461 1
HET CL C 462 1
HET CA C2004 1
HET CA C2005 1
HET CA C2006 1
HET CA C2007 1
HET CL D 473 1
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 BMA D3322 11
HET MAN D3323 11
HET NAG D3371 14
HET NAG D3372 14
HET SO4 L 215 5
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
HETNAM MG MAGNESIUM ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM BMA BETA-D-MANNOSE
HETNAM MAN ALPHA-D-MANNOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 9 SO4 7(O4 S 2-)
FORMUL 12 GOL C3 H8 O3
FORMUL 13 CA 12(CA 2+)
FORMUL 17 CL 4(CL 1-)
FORMUL 18 MG 2(MG 2+)
FORMUL 21 NAG 10(C8 H15 N O6)
FORMUL 22 BMA 2(C6 H12 O6)
FORMUL 22 MAN 3(C6 H12 O6)
FORMUL 41 HOH *1291(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 ARG B 8 1 6
HELIX 8 8 SER B 12 SER B 20 1 9
HELIX 9 9 LEU B 40 ASP B 47 1 8
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 GLN B 210 1 12
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 LEU B 324 1 11
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 ALA D 18 1 7
HELIX 31 31 LEU D 40 ASP D 47 1 8
HELIX 32 32 ALA D 50 GLU D 52 5 3
HELIX 33 33 ASP D 76 VAL D 80 5 5
HELIX 34 34 SER D 121 SER D 123 5 3
HELIX 35 35 MET D 124 GLN D 132 1 9
HELIX 36 36 ASN D 133 ARG D 143 1 11
HELIX 37 37 PRO D 169 ASN D 175 1 7
HELIX 38 38 GLN D 199 GLN D 210 1 12
HELIX 39 39 GLY D 221 CYS D 232 1 12
HELIX 40 40 CYS D 232 GLY D 237 1 6
HELIX 41 41 LEU D 258 GLY D 264 5 7
HELIX 42 42 SER D 291 LYS D 302 1 12
HELIX 43 43 VAL D 314 GLU D 323 1 10
HELIX 44 44 ASN D 339 ARG D 352 1 14
HELIX 45 45 CYS D 435 ALA D 441 5 7
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 HIS E 205 SER E 209 5 5
HELIX 49 49 ASP F 79 PHE F 83 5 5
HELIX 50 50 SER F 121 SER F 127 1 7
HELIX 51 51 LYS F 183 GLU F 187 1 5
HELIX 52 52 ASN H 28 THR H 32 5 5
HELIX 53 53 PRO H 62 GLN H 65 5 4
HELIX 54 54 THR H 74 SER H 76 5 3
HELIX 55 55 THR H 87 THR H 91 5 5
HELIX 56 56 PRO H 206 SER H 209 5 4
HELIX 57 57 ASP L 79 PHE L 83 5 5
HELIX 58 58 SER L 121 SER L 127 1 7
HELIX 59 59 LYS L 183 ARG L 188 1 6
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 447 N THR A 9
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 4 LEU A 23 LYS A 27 0
SHEET 2 B 4 VAL A 33 ALA A 39 -1 O ALA A 34 N HIS A 26
SHEET 3 B 4 GLY A 52 PRO A 57 -1 O CYS A 56 N ILE A 35
SHEET 4 B 4 SER A 67 LEU A 68 -1 O LEU A 68 N VAL A 53
SHEET 1 C 4 THR A 76 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 ALA A 266 N ALA A 257
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 PHE A 331 N LEU A 306
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 CYS B 374 -1 N ASN B 371 O SER B 398
SHEET 5 M 5 GLU B 378 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 ALA B 155 O LYS B 191
SHEET 3 N 6 VAL B 112 ASP B 119 1 N MET B 118 O GLY B 154
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 ALA B 309 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 ALA C 39 -1 O ALA C 34 N HIS C 26
SHEET 3 Q 3 GLY C 52 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 VAL C 182 N VAL C 174
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 277 N ILE C 269
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 GLY C 364
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 ASP D 39 0
SHEET 2 Z 3 ALA D 24 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 GLU D 358 O LYS D 417
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 ILE D 399 N PHE D 100
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 ILE D 114 O ARG D 150
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 ALA D 309 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 LEU E 83 N VAL E 18
SHEET 4 AE 4 ALA E 68 ASP E 73 -1 N THR E 69 O GLN E 82
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 TYR E 94 O THR E 113
SHEET 4 AF 6 VAL E 34 ARG E 40 -1 N GLN E 39 O VAL E 93
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 TYR E 94 O THR E 113
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 LYS E 149 -1 O LEU E 147 N TYR E 128
SHEET 3 AH 4 LEU E 180 THR E 190 -1 O VAL E 189 N VAL E 142
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 LYS E 149 -1 O LEU E 147 N TYR E 128
SHEET 3 AI 4 LEU E 180 THR E 190 -1 O VAL E 189 N VAL E 142
SHEET 4 AI 4 VAL E 175 GLN E 177 -1 N GLN E 177 O LEU E 180
SHEET 1 AJ 3 THR E 157 TRP E 160 0
SHEET 2 AJ 3 THR E 200 ALA E 204 -1 O ALA E 204 N THR E 157
SHEET 3 AJ 3 ASP E 213 LYS E 215 -1 O LYS E 214 N CYS E 201
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 LEU F 73 N ILE F 21
SHEET 4 AK 4 PHE F 62 SER F 67 -1 N SER F 65 O SER F 72
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 GLY F 34 O VAL F 89
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 GLY F 129 PHE F 139 -1 O VAL F 133 N PHE F 118
SHEET 3 AN 4 TYR F 173 THR F 182 -1 O MET F 175 N LEU F 136
SHEET 4 AN 4 VAL F 159 TRP F 163 -1 N LEU F 160 O THR F 178
SHEET 1 AO 3 SER F 153 ARG F 155 0
SHEET 2 AO 3 ASN F 145 ILE F 150 -1 N ILE F 150 O SER F 153
SHEET 3 AO 3 TYR F 192 THR F 197 -1 O THR F 197 N ASN F 145
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 83 N VAL H 18
SHEET 4 AP 4 ALA H 68 ASP H 73 -1 N THR H 69 O GLN H 82
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 TYR H 94 O THR H 113
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 TYR H 94 O THR H 113
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 LEU H 147 N TYR H 128
SHEET 3 AS 4 LEU H 180 THR H 190 -1 O LEU H 183 N VAL H 148
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 LEU H 147 N TYR H 128
SHEET 3 AT 4 LEU H 180 THR H 190 -1 O LEU H 183 N VAL H 148
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 2.06
SSBOND 2 CYS A 107 CYS A 130 1555 1555 2.06
SSBOND 3 CYS A 146 CYS A 167 1555 1555 2.06
SSBOND 4 CYS B 5 CYS B 23 1555 1555 2.04
SSBOND 5 CYS B 13 CYS B 435 1555 1555 2.04
SSBOND 6 CYS B 16 CYS B 38 1555 1555 2.03
SSBOND 7 CYS B 26 CYS B 49 1555 1555 2.04
SSBOND 8 CYS B 177 CYS B 184 1555 1555 2.07
SSBOND 9 CYS B 232 CYS B 273 1555 1555 2.08
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 2.05
SSBOND 15 CYS C 107 CYS C 130 1555 1555 2.06
SSBOND 16 CYS C 146 CYS C 167 1555 1555 2.04
SSBOND 17 CYS D 5 CYS D 23 1555 1555 2.04
SSBOND 18 CYS D 13 CYS D 435 1555 1555 2.02
SSBOND 19 CYS D 16 CYS D 38 1555 1555 2.03
SSBOND 20 CYS D 26 CYS D 49 1555 1555 2.04
SSBOND 21 CYS D 177 CYS D 184 1555 1555 2.05
SSBOND 22 CYS D 232 CYS D 273 1555 1555 2.05
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 2.04
SSBOND 26 CYS D 448 CYS D 460 1555 1555 2.05
SSBOND 27 CYS D 462 CYS D 471 1555 1555 2.03
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 2.03
SSBOND 31 CYS F 23 CYS F 88 1555 1555 2.04
SSBOND 32 CYS F 134 CYS F 194 1555 1555 2.03
SSBOND 33 CYS H 22 CYS H 96 1555 1555 2.04
SSBOND 34 CYS H 134 CYS L 214 1555 1555 2.04
SSBOND 35 CYS H 146 CYS H 201 1555 1555 2.03
SSBOND 36 CYS L 23 CYS L 88 1555 1555 2.05
SSBOND 37 CYS L 134 CYS L 194 1555 1555 2.04
LINK ND2 ASN D 99 C1 NAG D3099 1555 1555 1.44
LINK ND2 ASN D 371 C1 NAG D3371 1555 1555 1.44
LINK O4 NAG D3320 C1 NAG D3321 1555 1555 1.44
LINK O4 NAG D3371 C1 NAG D3372 1555 1555 1.44
LINK ND2 ASN B 99 C1 NAG B3099 1555 1555 1.44
LINK O4 NAG B3371 C1 NAG B3372 1555 1555 1.44
LINK ND2 ASN D 320 C1 NAG D3320 1555 1555 1.44
LINK ND2 ASN B 371 C1 NAG B3371 1555 1555 1.44
LINK O4 NAG B3320 C1 NAG B3321 1555 1555 1.44
LINK ND2 ASN B 320 C1 NAG B3320 1555 1555 1.45
LINK OD2 ASP A 245 CA CA A2004 1555 1555 2.14
LINK OE2 GLU B 220 MG MG B2001 1555 1555 2.16
LINK OD1 ASP D 217 CA CA D2003 1555 1555 2.17
LINK OE2 GLU D 220 MG MG D2001 1555 1555 2.19
LINK O THR A 250 CA CA A2004 1555 1555 2.22
LINK O ARG C 303 CA CA C2005 1555 1555 2.23
LINK O TYR A 371 CA CA A2006 1555 1555 2.24
LINK OD1 ASP D 127 CA CA D2002 1555 1555 2.24
LINK O TYR C 432 CA CA C2007 1555 1555 2.25
LINK O THR C 250 CA CA C2004 1555 1555 2.25
LINK OD2 ASP C 245 CA CA C2004 1555 1555 2.26
LINK O MET D 335 CA CA D2002 1555 1555 2.27
LINK OD1 ASN A 299 CA CA A2005 1555 1555 2.27
LINK O TYR C 371 CA CA C2006 1555 1555 2.27
LINK O PRO D 219 CA CA D2003 1555 1555 2.28
LINK OD1 ASP B 217 CA CA B2003 1555 1555 2.28
LINK O TYR A 432 CA CA A2007 1555 1555 2.29
LINK OD1 ASP A 428 CA CA A2007 1555 1555 2.29
LINK OG SER D 121 MG MG D2001 1555 1555 2.30
LINK OD1 ASP B 127 CA CA B2002 1555 1555 2.30
LINK O ARG A 303 CA CA A2005 1555 1555 2.30
LINK OD1 ASN C 299 CA CA C2005 1555 1555 2.31
LINK OD1 ASP A 297 CA CA A2005 1555 1555 2.31
LINK OD1 ASP C 428 CA CA C2007 1555 1555 2.31
LINK OE1 GLU A 243 CA CA A2004 1555 1555 2.32
LINK OD1 ASP C 297 CA CA C2005 1555 1555 2.33
LINK O PRO B 219 CA CA B2003 1555 1555 2.34
LINK OD1 ASP A 426 CA CA A2007 1555 1555 2.34
LINK OE1 GLU D 220 CA CA D2003 1555 1555 2.34
LINK OE1 GLU C 243 CA CA C2004 1555 1555 2.35
LINK O ASP C 247 CA CA C2004 1555 1555 2.36
LINK OD1 ASP A 367 CA CA A2006 1555 1555 2.36
LINK OG SER B 121 MG MG B2001 1555 1555 2.37
LINK O MET B 335 CA CA B2002 1555 1555 2.37
LINK OD1 ASN B 215 CA CA B2003 1555 1555 2.37
LINK O ASP B 217 CA CA B2003 1555 1555 2.38
LINK OD1 ASN D 215 CA CA D2003 1555 1555 2.38
LINK OD2 ASP C 365 CA CA C2006 1555 1555 2.38
LINK OE2 GLU C 243 CA CA C2004 1555 1555 2.39
LINK OD2 ASP D 158 CA CA D2003 1555 1555 2.39
LINK OD1 ASN C 430 CA CA C2007 1555 1555 2.39
LINK OG1 THR C 250 CA CA C2004 1555 1555 2.39
LINK OD2 ASP A 365 CA CA A2006 1555 1555 2.40
LINK OD2 ASP B 158 CA CA B2003 1555 1555 2.40
LINK OE1 GLU B 220 CA CA B2003 1555 1555 2.40
LINK OG1 THR A 250 CA CA A2004 1555 1555 2.40
LINK OD1 ASP C 367 CA CA C2006 1555 1555 2.41
LINK O ASP D 217 CA CA D2003 1555 1555 2.41
LINK OD1 ASP D 126 CA CA D2002 1555 1555 2.41
LINK OD1 ASP A 434 CA CA A2007 1555 1555 2.43
LINK OD2 ASP C 434 CA CA C2007 1555 1555 2.43
LINK OD1 ASP B 126 CA CA B2002 1555 1555 2.43
LINK OD1 ASN A 430 CA CA A2007 1555 1555 2.44
LINK O SER D 123 CA CA D2002 1555 1555 2.44
LINK OE2 GLU A 243 CA CA A2004 1555 1555 2.45
LINK O SER B 123 CA CA B2002 1555 1555 2.45
LINK OD1 ASP C 369 CA CA C2006 1555 1555 2.45
LINK OD1 ASP C 426 CA CA C2007 1555 1555 2.46
LINK OD1 ASP C 434 CA CA C2007 1555 1555 2.47
LINK OD2 ASP C 373 CA CA C2006 1555 1555 2.48
LINK OE2 GLU A 252 CA CA A2004 1555 1555 2.48
LINK OD1 ASP C 373 CA CA C2006 1555 1555 2.49
LINK OD2 ASP C 305 CA CA C2005 1555 1555 2.49
LINK OE2 GLU C 252 CA CA C2004 1555 1555 2.49
LINK OD2 ASP A 305 CA CA A2005 1555 1555 2.50
LINK O ASP A 247 CA CA A2004 1555 1555 2.50
LINK OD2 ASP A 434 CA CA A2007 1555 1555 2.51
LINK OD1 ASP A 305 CA CA A2005 1555 1555 2.51
LINK OD1 ASP A 369 CA CA A2006 1555 1555 2.53
LINK OD2 ASP A 373 CA CA A2006 1555 1555 2.53
LINK OE1 GLU C 252 CA CA C2004 1555 1555 2.54
LINK OD1 ASP C 305 CA CA C2005 1555 1555 2.54
LINK OE1 GLU A 252 CA CA A2004 1555 1555 2.56
LINK OD2 ASP B 126 CA CA B2002 1555 1555 2.57
LINK OD1 ASP C 301 CA CA C2005 1555 1555 2.59
LINK OD1 ASP A 373 CA CA A2006 1555 1555 2.59
LINK OD2 ASP D 126 CA CA D2002 1555 1555 2.61
LINK OD1 ASP A 301 CA CA A2005 1555 1555 2.63
LINK MG MG D2001 O HOH D1118 1555 1555 2.00
LINK MG MG B2001 O HOH B 477 1555 1555 2.02
LINK MG MG B2001 O HOH B1120 1555 1555 2.06
LINK MG MG D2001 O HOH D 476 1555 1555 2.08
LINK MG MG D2001 O HOH D1126 1555 1555 2.09
LINK MG MG B2001 O HOH B1121 1555 1555 2.10
LINK MG MG B2001 O HOH B 920 1555 1555 2.11
LINK MG MG D2001 O HOH D1115 1555 1555 2.11
LINK CA CA C2006 O HOH C 494 1555 1555 2.26
LINK CA CA B2002 O HOH B 525 1555 1555 2.34
LINK CA CA A2007 O HOH A 467 1555 1555 2.36
LINK CA CA A2005 O HOH A 478 1555 1555 2.36
LINK CA CA A2006 O HOH A 486 1555 1555 2.39
LINK CA CA D2002 O HOH D 509 1555 1555 2.41
LINK CA CA C2005 O HOH C1134 1555 1555 2.42
LINK CA CA B2002 O HOH B 502 1555 1555 2.44
LINK CA CA D2002 O HOH D 488 1555 1555 2.44
LINK CA CA C2007 O HOH C 478 1555 1555 2.48
LINK O4 NAG D3321 C1 BMA D3322 1555 1555 1.44
LINK O4 NAG B3321 C1 BMA B3322 1555 1555 1.44
LINK O3 BMA D3322 C1 MAN D3323 1555 1555 1.44
LINK O3 BMA B3322 C1 MAN B3323 1555 1555 1.44
LINK O6 BMA B3322 C1 MAN B3324 1555 1555 1.44
CISPEP 1 SER B 84 PRO B 85 0 -4.72
CISPEP 2 SER B 162 PRO B 163 0 5.27
CISPEP 3 SER B 168 PRO B 169 0 -6.34
CISPEP 4 SER D 84 PRO D 85 0 -3.20
CISPEP 5 SER D 162 PRO D 163 0 8.46
CISPEP 6 SER D 168 PRO D 169 0 -5.87
CISPEP 7 PHE E 152 PRO E 153 0 -5.54
CISPEP 8 GLU E 154 PRO E 155 0 -2.32
CISPEP 9 TRP E 194 PRO E 195 0 0.72
CISPEP 10 SER F 7 PRO F 8 0 -5.93
CISPEP 11 LEU F 94 PRO F 95 0 -3.65
CISPEP 12 TYR F 140 PRO F 141 0 2.72
CISPEP 13 PHE H 152 PRO H 153 0 -3.41
CISPEP 14 GLU H 154 PRO H 155 0 -5.41
CISPEP 15 TRP H 194 PRO H 195 0 -1.76
CISPEP 16 SER L 7 PRO L 8 0 -4.85
CISPEP 17 LEU L 94 PRO L 95 0 1.14
CISPEP 18 TYR L 140 PRO L 141 0 0.12
SITE 1 AC1 2 TYR A 155 SER A 161
SITE 1 AC2 3 PHE A 10 GLN A 444 PRO C 383
SITE 1 AC3 5 ARG A 400 SER A 401 ARG A 402 HOH A 691
SITE 2 AC3 5 HOH A 696
SITE 1 AC4 4 ASN A 227 ARG A 276 ARG A 279 HOH A1172
SITE 1 AC5 5 GLU A 243 ASP A 245 ASP A 247 THR A 250
SITE 2 AC5 5 GLU A 252
SITE 1 AC6 6 ASP A 297 ASN A 299 ASP A 301 ARG A 303
SITE 2 AC6 6 ASP A 305 HOH A 478
SITE 1 AC7 6 ASP A 365 ASP A 367 ASP A 369 TYR A 371
SITE 2 AC7 6 ASP A 373 HOH A 486
SITE 1 AC8 6 ASP A 426 ASP A 428 ASN A 430 TYR A 432
SITE 2 AC8 6 ASP A 434 HOH A 467
SITE 1 AC9 6 SER B 121 TYR B 122 ARG B 214 ASN B 215
SITE 2 AC9 6 HOH B1120 HOH B1123
SITE 1 BC1 6 SER B 121 GLU B 220 HOH B 477 HOH B 920
SITE 2 BC1 6 HOH B1120 HOH B1121
SITE 1 BC2 6 SER B 123 ASP B 126 ASP B 127 MET B 335
SITE 2 BC2 6 HOH B 502 HOH B 525
SITE 1 BC3 5 ASP B 158 ASN B 215 ASP B 217 PRO B 219
SITE 2 BC3 5 GLU B 220
SITE 1 BC4 2 ASN B 99 PHE B 100
SITE 1 BC5 7 MET A 285 ASN B 320 HOH B 486 HOH B 534
SITE 2 BC5 7 HOH B 538 HOH B 547 NAG B3321
SITE 1 BC6 5 ARG A 281 HOH A1178 NAG B3320 BMA B3322
SITE 2 BC6 5 MAN B3324
SITE 1 BC7 4 HOH B 826 NAG B3321 MAN B3323 MAN B3324
SITE 1 BC8 3 ARG A 281 HOH B 826 BMA B3322
SITE 1 BC9 2 NAG B3321 BMA B3322
SITE 1 CC1 4 ASN B 371 SER B 398 GLU B 400 NAG B3372
SITE 1 CC2 1 NAG B3371
SITE 1 CC3 3 ALA C 89 HIS C 112 HOH C 576
SITE 1 CC4 4 ARG C 400 SER C 401 ARG C 402 HOH C1250
SITE 1 CC5 5 ASN C 227 TYR C 230 ARG C 276 ARG C 279
SITE 2 CC5 5 HOH C1239
SITE 1 CC6 1 GLN C 444
SITE 1 CC7 1 TRP C 58
SITE 1 CC8 5 GLU C 243 ASP C 245 ASP C 247 THR C 250
SITE 2 CC8 5 GLU C 252
SITE 1 CC9 6 ASP C 297 ASN C 299 ASP C 301 ARG C 303
SITE 2 CC9 6 ASP C 305 HOH C1134
SITE 1 DC1 6 ASP C 365 ASP C 367 ASP C 369 TYR C 371
SITE 2 DC1 6 ASP C 373 HOH C 494
SITE 1 DC2 6 ASP C 426 ASP C 428 ASN C 430 TYR C 432
SITE 2 DC2 6 ASP C 434 HOH C 478
SITE 1 DC3 5 SER D 121 TYR D 122 ARG D 214 ASN D 215
SITE 2 DC3 5 HOH D1126
SITE 1 DC4 6 SER D 121 GLU D 220 HOH D 476 HOH D1115
SITE 2 DC4 6 HOH D1118 HOH D1126
SITE 1 DC5 6 SER D 123 ASP D 126 ASP D 127 MET D 335
SITE 2 DC5 6 HOH D 488 HOH D 509
SITE 1 DC6 5 ASP D 158 ASN D 215 ASP D 217 PRO D 219
SITE 2 DC6 5 GLU D 220
SITE 1 DC7 2 ASN D 99 NAG D3372
SITE 1 DC8 7 MET C 285 ASN D 320 HOH D 529 HOH D 533
SITE 2 DC8 7 HOH D 551 HOH D 978 NAG D3321
SITE 1 DC9 4 ARG C 281 HOH C1016 NAG D3320 BMA D3322
SITE 1 EC1 2 NAG D3321 MAN D3323
SITE 1 EC2 2 ARG C 281 BMA D3322
SITE 1 EC3 5 ASN D 371 SER D 398 ILE D 399 GLU D 400
SITE 2 EC3 5 NAG D3372
SITE 1 EC4 2 NAG D3099 NAG D3371
SITE 1 EC5 4 SER L 30 SER L 67 GLY L 68 HOH L 961
CRYST1 259.533 145.257 104.798 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 0.003853 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006884 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009542 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
