HEADER CELL ADHESION/IMMUNE SYSTEM 10-OCT-07 2VDO
TITLE INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO FIBRINOGEN GAMMA
TITLE 2 CHAIN PEPTIDE, HHLGGAKQAGDV
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTEGRIN ALPHA-IIB;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HEADPIECE, RESIDUES 32-483;
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;
COMPND 11 FRAGMENT: HEADPIECE, RESIDUES 27-487;
COMPND 12 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA, GPIIIA, CD61 ANTIGEN;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: MONOCLONAL ANTIBODY 10E5 HEAVY CHAIN;
COMPND 16 CHAIN: H;
COMPND 17 MOL_ID: 4;
COMPND 18 MOLECULE: MONOCLONAL ANTIBODY 10E5 LIGHT CHAIN;
COMPND 19 CHAIN: L;
COMPND 20 MOL_ID: 5;
COMPND 21 MOLECULE: FIBRINOGEN, GAMMA POLYPEPTIDE;
COMPND 22 CHAIN: C;
COMPND 23 FRAGMENT: GAMMA CHAIN C-TERMINAL PEPTIDE, RESIDUES 426-437
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: LEC 3.2.8.1;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 15 EXPRESSION_SYSTEM_CELL_LINE: LEC 3.2.8.1;
SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 19 ORGANISM_COMMON: MOUSE;
SOURCE 20 ORGANISM_TAXID: 10090;
SOURCE 21 STRAIN: BALB/C;
SOURCE 22 CELL_LINE: 10E5 HYBRIDOMA;
SOURCE 23 MOL_ID: 4;
SOURCE 24 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 25 ORGANISM_COMMON: MOUSE;
SOURCE 26 ORGANISM_TAXID: 10090;
SOURCE 27 STRAIN: BALB/C;
SOURCE 28 CELL_LINE: 10E5 HYBRIDOMA;
SOURCE 29 MOL_ID: 5;
SOURCE 30 SYNTHETIC: YES;
SOURCE 31 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 32 ORGANISM_COMMON: HUMAN;
SOURCE 33 ORGANISM_TAXID: 9606
KEYWDS CELL ADHESION-IMMUNE SYSTEM COMPLEX, FIBRINOGEN BINDING, PLATELET
KEYWDS 2 INTEGRIN ALPHAIIBBETA3, GLYCOPROTEIN, CELL ADHESION, MEMBRANE,
KEYWDS 3 INTEGRIN, RECEPTOR, ANTAGONIST, HOST-VIRUS INTERACTION, PYRROLIDONE
KEYWDS 4 CARBOXYLIC ACID, TRANSMEMBRANE, PHOSPHORYLATION, DISEASE MUTATION,
KEYWDS 5 CLEAVAGE ON PAIR OF BASIC RESIDUES, CELL ADHESION/IMMUNE SYSTEM
KEYWDS 6 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.A.SPRINGER,J.ZHU,T.XIAO
REVDAT 3 13-JUL-11 2VDO 1 VERSN
REVDAT 2 24-FEB-09 2VDO 1 VERSN
REVDAT 1 02-SEP-08 2VDO 0
JRNL AUTH T.A.SPRINGER,J.ZHU,T.XIAO
JRNL TITL STRUCTURAL BASIS FOR DISTINCTIVE RECOGNITION OF FIBRINOGEN
JRNL TITL 2 GAMMAC PEPTIDE BY THE PLATELET INTEGRIN ALPHAIIBBETA3.
JRNL REF J.CELL BIOL. V. 182 791 2008
JRNL REFN ISSN 0021-9525
JRNL PMID 18710925
JRNL DOI 10.1083/JCB.200801146
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.XIAO,J.TAKAGI,B.S.COLLER,J.-H.WANG,T.A.SPRINGER
REMARK 1 TITL STRUCTURAL BASIS FOR ALLOSTERY IN INTEGRINS AND BINDING TO
REMARK 1 TITL 2 FIBRINOGEN-MIMETIC THERAPEUTICS
REMARK 1 REF NATURE V. 432 59 2004
REMARK 1 REFN ISSN 0028-0836
REMARK 1 PMID 15378069
REMARK 1 DOI 10.1038/NATURE02976
REMARK 2
REMARK 2 RESOLUTION. 2.51 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0037
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.51
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.13
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 71126
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.148
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3807
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.51
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4785
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2160
REMARK 3 BIN FREE R VALUE SET COUNT : 260
REMARK 3 BIN FREE R VALUE : 0.2890
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10538
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 205
REMARK 3 SOLVENT ATOMS : 1043
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.03000
REMARK 3 B22 (A**2) : -0.03000
REMARK 3 B33 (A**2) : 0.05000
REMARK 3 B12 (A**2) : -0.02000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.266
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.199
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.131
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.761
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11034 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 7394 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15073 ; 1.046 ; 1.979
REMARK 3 BOND ANGLES OTHERS (DEGREES): 18001 ; 0.789 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1397 ; 5.497 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 481 ;33.588 ;24.324
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1735 ;12.148 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 61 ;13.892 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1698 ; 0.065 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12310 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2178 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1982 ; 0.183 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 7585 ; 0.179 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5314 ; 0.172 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 5775 ; 0.081 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 868 ; 0.137 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 18 ; 0.103 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 67 ; 0.177 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 34 ; 0.148 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 7079 ; 1.852 ; 5.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11024 ; 2.876 ;10.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4606 ; 1.939 ; 5.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4028 ; 2.908 ;10.000
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 31
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 17
REMARK 3 ORIGIN FOR THE GROUP (A): 132.9320 12.1020 78.3570
REMARK 3 T TENSOR
REMARK 3 T11: -0.1882 T22: 0.0993
REMARK 3 T33: 0.0165 T12: 0.0713
REMARK 3 T13: -0.0553 T23: 0.4004
REMARK 3 L TENSOR
REMARK 3 L11: 4.3390 L22: 13.4216
REMARK 3 L33: 3.7125 L12: -2.4833
REMARK 3 L13: -0.6286 L23: 0.0099
REMARK 3 S TENSOR
REMARK 3 S11: -0.1973 S12: -0.0949 S13: -0.3419
REMARK 3 S21: 0.5329 S22: -0.1952 S23: -0.9466
REMARK 3 S31: 0.5544 S32: 0.8323 S33: 0.3925
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 18 A 62
REMARK 3 ORIGIN FOR THE GROUP (A): 129.0170 21.6150 68.9240
REMARK 3 T TENSOR
REMARK 3 T11: -0.2484 T22: -0.0629
REMARK 3 T33: -0.0864 T12: 0.0313
REMARK 3 T13: 0.0143 T23: 0.2485
REMARK 3 L TENSOR
REMARK 3 L11: 3.1771 L22: 6.1405
REMARK 3 L33: 3.3315 L12: 0.0302
REMARK 3 L13: -0.1408 L23: 1.7500
REMARK 3 S TENSOR
REMARK 3 S11: 0.0547 S12: -0.0095 S13: -0.1112
REMARK 3 S21: -0.1423 S22: -0.2830 S23: -0.5369
REMARK 3 S31: 0.1076 S32: 0.3626 S33: 0.2283
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 63 A 115
REMARK 3 ORIGIN FOR THE GROUP (A): 118.5350 33.3710 64.2890
REMARK 3 T TENSOR
REMARK 3 T11: -0.2743 T22: -0.1151
REMARK 3 T33: -0.1125 T12: -0.0931
REMARK 3 T13: -0.0503 T23: 0.1361
REMARK 3 L TENSOR
REMARK 3 L11: 1.0076 L22: 1.6247
REMARK 3 L33: 2.1037 L12: -0.4411
REMARK 3 L13: -0.3526 L23: -0.6230
REMARK 3 S TENSOR
REMARK 3 S11: 0.0394 S12: -0.0131 S13: 0.0086
REMARK 3 S21: 0.2021 S22: -0.2131 S23: -0.2712
REMARK 3 S31: -0.0583 S32: 0.3853 S33: 0.1737
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 116 A 167
REMARK 3 ORIGIN FOR THE GROUP (A): 106.9730 35.9030 63.4940
REMARK 3 T TENSOR
REMARK 3 T11: -0.2434 T22: -0.1651
REMARK 3 T33: -0.1988 T12: -0.0866
REMARK 3 T13: -0.0376 T23: 0.0904
REMARK 3 L TENSOR
REMARK 3 L11: 2.8786 L22: 1.4552
REMARK 3 L33: 2.5665 L12: 0.4195
REMARK 3 L13: -1.9370 L23: -0.1162
REMARK 3 S TENSOR
REMARK 3 S11: -0.0199 S12: 0.0112 S13: -0.1160
REMARK 3 S21: 0.0517 S22: -0.1345 S23: 0.2048
REMARK 3 S31: 0.0121 S32: -0.0421 S33: 0.1545
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 168 A 243
REMARK 3 ORIGIN FOR THE GROUP (A): 105.9430 24.3110 63.8110
REMARK 3 T TENSOR
REMARK 3 T11: -0.1889 T22: -0.1844
REMARK 3 T33: -0.1462 T12: -0.0824
REMARK 3 T13: -0.0100 T23: 0.0621
REMARK 3 L TENSOR
REMARK 3 L11: 0.9301 L22: 0.9556
REMARK 3 L33: 1.9082 L12: -0.0965
REMARK 3 L13: -0.6960 L23: -0.4877
REMARK 3 S TENSOR
REMARK 3 S11: 0.0272 S12: 0.1340 S13: -0.1451
REMARK 3 S21: 0.0620 S22: -0.1453 S23: -0.0107
REMARK 3 S31: 0.2669 S32: -0.1252 S33: 0.1181
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 244 A 290
REMARK 3 ORIGIN FOR THE GROUP (A): 99.5560 12.9550 72.2190
REMARK 3 T TENSOR
REMARK 3 T11: -0.0511 T22: -0.2704
REMARK 3 T33: -0.0903 T12: -0.1386
REMARK 3 T13: 0.0535 T23: 0.0520
REMARK 3 L TENSOR
REMARK 3 L11: 2.4651 L22: 2.1919
REMARK 3 L33: 3.8818 L12: 0.0965
REMARK 3 L13: -0.3252 L23: 0.5447
REMARK 3 S TENSOR
REMARK 3 S11: -0.0558 S12: 0.1083 S13: -0.2652
REMARK 3 S21: -0.0325 S22: -0.1912 S23: 0.1392
REMARK 3 S31: 0.4367 S32: -0.2824 S33: 0.2470
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 291 A 326
REMARK 3 ORIGIN FOR THE GROUP (A): 107.6080 7.0420 84.2450
REMARK 3 T TENSOR
REMARK 3 T11: 0.0178 T22: -0.2870
REMARK 3 T33: -0.0417 T12: -0.0921
REMARK 3 T13: 0.1011 T23: 0.2083
REMARK 3 L TENSOR
REMARK 3 L11: 3.1282 L22: 5.3829
REMARK 3 L33: 4.2387 L12: -0.3323
REMARK 3 L13: -0.8189 L23: 2.9501
REMARK 3 S TENSOR
REMARK 3 S11: -0.1844 S12: -0.2593 S13: -0.4108
REMARK 3 S21: 0.5516 S22: -0.0453 S23: 0.1828
REMARK 3 S31: 0.9945 S32: 0.0143 S33: 0.2297
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 327 A 372
REMARK 3 ORIGIN FOR THE GROUP (A): 110.1110 2.6630 78.4070
REMARK 3 T TENSOR
REMARK 3 T11: 0.1302 T22: -0.2959
REMARK 3 T33: -0.0399 T12: -0.0369
REMARK 3 T13: 0.1245 T23: 0.1794
REMARK 3 L TENSOR
REMARK 3 L11: 3.1018 L22: 3.3161
REMARK 3 L33: 3.5102 L12: 0.4561
REMARK 3 L13: -0.0668 L23: 1.5637
REMARK 3 S TENSOR
REMARK 3 S11: -0.1560 S12: -0.0510 S13: -0.4472
REMARK 3 S21: -0.0115 S22: -0.3381 S23: -0.0598
REMARK 3 S31: 0.7308 S32: -0.0741 S33: 0.4941
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 373 A 452
REMARK 3 ORIGIN FOR THE GROUP (A): 124.1760 7.3280 79.9870
REMARK 3 T TENSOR
REMARK 3 T11: -0.0488 T22: -0.1037
REMARK 3 T33: 0.0185 T12: 0.1029
REMARK 3 T13: 0.0088 T23: 0.3095
REMARK 3 L TENSOR
REMARK 3 L11: 2.9989 L22: 3.1486
REMARK 3 L33: 3.0821 L12: 0.7461
REMARK 3 L13: -0.5003 L23: 0.0210
REMARK 3 S TENSOR
REMARK 3 S11: -0.1362 S12: -0.2629 S13: -0.4431
REMARK 3 S21: 0.2734 S22: -0.2923 S23: -0.3881
REMARK 3 S31: 0.5990 S32: 0.6262 S33: 0.4285
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 72
REMARK 3 ORIGIN FOR THE GROUP (A): 106.2680 21.3490 169.1560
REMARK 3 T TENSOR
REMARK 3 T11: 0.4446 T22: -0.3282
REMARK 3 T33: -0.3172 T12: 0.2057
REMARK 3 T13: -0.1188 T23: -0.0935
REMARK 3 L TENSOR
REMARK 3 L11: 6.1423 L22: 4.0518
REMARK 3 L33: 12.2091 L12: -1.8839
REMARK 3 L13: 5.5295 L23: -2.9334
REMARK 3 S TENSOR
REMARK 3 S11: -0.2719 S12: -0.7559 S13: -0.1586
REMARK 3 S21: 1.1934 S22: 0.3932 S23: -0.4537
REMARK 3 S31: -1.3284 S32: -1.1794 S33: -0.1213
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 79 B 98
REMARK 3 ORIGIN FOR THE GROUP (A): 103.3770 29.3140 150.3420
REMARK 3 T TENSOR
REMARK 3 T11: 0.6342 T22: -0.0747
REMARK 3 T33: -0.0889 T12: 0.2407
REMARK 3 T13: 0.0477 T23: -0.0627
REMARK 3 L TENSOR
REMARK 3 L11: 9.6249 L22: 10.9980
REMARK 3 L33: 39.4491 L12: -4.3203
REMARK 3 L13: 18.1102 L23: -15.1056
REMARK 3 S TENSOR
REMARK 3 S11: -0.8897 S12: -0.1758 S13: 0.7367
REMARK 3 S21: 1.1894 S22: 0.2821 S23: -0.3446
REMARK 3 S31: -3.5011 S32: -1.1316 S33: 0.6077
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 99 B 172
REMARK 3 ORIGIN FOR THE GROUP (A): 97.2700 38.1520 104.2390
REMARK 3 T TENSOR
REMARK 3 T11: 0.1489 T22: -0.0805
REMARK 3 T33: -0.1421 T12: -0.2200
REMARK 3 T13: 0.0447 T23: 0.0203
REMARK 3 L TENSOR
REMARK 3 L11: 0.2900 L22: 0.6087
REMARK 3 L33: 1.4657 L12: -0.3639
REMARK 3 L13: 0.1069 L23: -0.6001
REMARK 3 S TENSOR
REMARK 3 S11: -0.0295 S12: -0.1666 S13: 0.0278
REMARK 3 S21: 0.4045 S22: 0.0270 S23: -0.0117
REMARK 3 S31: -0.4364 S32: 0.0948 S33: 0.0025
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 173 B 338
REMARK 3 ORIGIN FOR THE GROUP (A): 102.7660 34.2180 95.9670
REMARK 3 T TENSOR
REMARK 3 T11: -0.0421 T22: -0.1583
REMARK 3 T33: -0.1993 T12: -0.1953
REMARK 3 T13: -0.0108 T23: 0.0529
REMARK 3 L TENSOR
REMARK 3 L11: 1.4144 L22: 1.5802
REMARK 3 L33: 2.1419 L12: -0.2922
REMARK 3 L13: -0.7488 L23: 0.1298
REMARK 3 S TENSOR
REMARK 3 S11: 0.0546 S12: -0.2660 S13: 0.0958
REMARK 3 S21: 0.4302 S22: -0.0990 S23: -0.1348
REMARK 3 S31: -0.0602 S32: 0.2247 S33: 0.0444
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 339 B 393
REMARK 3 ORIGIN FOR THE GROUP (A): 99.9420 22.6510 130.8710
REMARK 3 T TENSOR
REMARK 3 T11: 0.2490 T22: -0.1016
REMARK 3 T33: -0.1234 T12: -0.1048
REMARK 3 T13: 0.0497 T23: -0.0054
REMARK 3 L TENSOR
REMARK 3 L11: 3.7877 L22: 2.6048
REMARK 3 L33: 26.1509 L12: -2.7908
REMARK 3 L13: 9.7730 L23: -6.4844
REMARK 3 S TENSOR
REMARK 3 S11: 0.6859 S12: 0.6576 S13: -0.4734
REMARK 3 S21: -0.3428 S22: 0.1939 S23: 0.1621
REMARK 3 S31: 1.4197 S32: 0.8471 S33: -0.8798
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 394 B 437
REMARK 3 ORIGIN FOR THE GROUP (A): 109.1530 28.2510 149.0690
REMARK 3 T TENSOR
REMARK 3 T11: 0.4274 T22: -0.3109
REMARK 3 T33: -0.1764 T12: -0.1030
REMARK 3 T13: -0.0343 T23: -0.0266
REMARK 3 L TENSOR
REMARK 3 L11: 6.1854 L22: 2.3089
REMARK 3 L33: 23.1613 L12: -1.4769
REMARK 3 L13: 8.9390 L23: -1.7802
REMARK 3 S TENSOR
REMARK 3 S11: -0.4599 S12: 0.6106 S13: 0.1900
REMARK 3 S21: 0.6233 S22: 0.4505 S23: -0.6388
REMARK 3 S31: -2.2981 S32: 1.6894 S33: 0.0094
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 438 B 461
REMARK 3 ORIGIN FOR THE GROUP (A): 119.0870 31.3350 183.1630
REMARK 3 T TENSOR
REMARK 3 T11: 1.9511 T22: 0.8137
REMARK 3 T33: 0.6802 T12: -0.1471
REMARK 3 T13: -0.8658 T23: -0.1889
REMARK 3 L TENSOR
REMARK 3 L11: 3.7646 L22: 5.4692
REMARK 3 L33: 18.1237 L12: 4.5045
REMARK 3 L13: -6.9758 L23: -8.9896
REMARK 3 S TENSOR
REMARK 3 S11: -0.2075 S12: -0.8478 S13: 1.0823
REMARK 3 S21: 2.1226 S22: -0.1486 S23: -1.9113
REMARK 3 S31: -4.3227 S32: 3.7870 S33: 0.3561
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 13
REMARK 3 ORIGIN FOR THE GROUP (A): 89.7690 36.5350 33.1670
REMARK 3 T TENSOR
REMARK 3 T11: -0.2245 T22: -0.0696
REMARK 3 T33: -0.0902 T12: -0.1700
REMARK 3 T13: -0.0138 T23: 0.0502
REMARK 3 L TENSOR
REMARK 3 L11: 12.0138 L22: 17.6137
REMARK 3 L33: 11.8823 L12: -12.1686
REMARK 3 L13: 8.8313 L23: -9.6293
REMARK 3 S TENSOR
REMARK 3 S11: 0.3507 S12: 0.3005 S13: -1.1269
REMARK 3 S21: -0.7807 S22: 0.1389 S23: 0.8024
REMARK 3 S31: 0.9651 S32: -0.1217 S33: -0.4896
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 14 H 54
REMARK 3 ORIGIN FOR THE GROUP (A): 93.9400 41.8470 41.1790
REMARK 3 T TENSOR
REMARK 3 T11: -0.2765 T22: -0.1044
REMARK 3 T33: -0.1415 T12: -0.0490
REMARK 3 T13: -0.0106 T23: 0.0860
REMARK 3 L TENSOR
REMARK 3 L11: 2.8415 L22: 1.8079
REMARK 3 L33: 2.1204 L12: 0.2694
REMARK 3 L13: 0.3730 L23: -0.0486
REMARK 3 S TENSOR
REMARK 3 S11: 0.0117 S12: 0.0100 S13: 0.0240
REMARK 3 S21: 0.0131 S22: 0.0321 S23: 0.1562
REMARK 3 S31: 0.2438 S32: -0.2276 S33: -0.0438
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 55 H 110
REMARK 3 ORIGIN FOR THE GROUP (A): 93.7550 42.7160 43.4000
REMARK 3 T TENSOR
REMARK 3 T11: -0.2598 T22: -0.1033
REMARK 3 T33: -0.1137 T12: -0.0739
REMARK 3 T13: -0.0109 T23: 0.0807
REMARK 3 L TENSOR
REMARK 3 L11: 3.2994 L22: 0.4697
REMARK 3 L33: 2.9323 L12: -0.6681
REMARK 3 L13: 1.2150 L23: -0.8749
REMARK 3 S TENSOR
REMARK 3 S11: -0.0618 S12: 0.0211 S13: 0.0989
REMARK 3 S21: -0.0239 S22: 0.0014 S23: 0.0234
REMARK 3 S31: 0.1811 S32: -0.3198 S33: 0.0604
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 111 H 134
REMARK 3 ORIGIN FOR THE GROUP (A): 86.1990 47.5650 12.7000
REMARK 3 T TENSOR
REMARK 3 T11: -0.3169 T22: 0.1195
REMARK 3 T33: -0.0732 T12: -0.0740
REMARK 3 T13: -0.0794 T23: 0.0470
REMARK 3 L TENSOR
REMARK 3 L11: 1.2362 L22: 1.0957
REMARK 3 L33: 3.7495 L12: -1.1328
REMARK 3 L13: 0.2121 L23: 0.2679
REMARK 3 S TENSOR
REMARK 3 S11: 0.2808 S12: -0.0405 S13: -0.2693
REMARK 3 S21: -0.0160 S22: -0.1528 S23: 0.0973
REMARK 3 S31: -0.0467 S32: -0.6355 S33: -0.1279
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 137 H 164
REMARK 3 ORIGIN FOR THE GROUP (A): 92.2760 44.6200 4.6690
REMARK 3 T TENSOR
REMARK 3 T11: -0.2932 T22: -0.1692
REMARK 3 T33: -0.2078 T12: 0.0717
REMARK 3 T13: -0.1150 T23: -0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 7.9266 L22: 1.0004
REMARK 3 L33: 14.2986 L12: -2.4433
REMARK 3 L13: -4.7739 L23: 1.6041
REMARK 3 S TENSOR
REMARK 3 S11: 0.4514 S12: 0.2063 S13: -0.7114
REMARK 3 S21: -0.2674 S22: -0.3841 S23: 0.1243
REMARK 3 S31: 0.7970 S32: 0.2007 S33: -0.0672
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 165 H 189
REMARK 3 ORIGIN FOR THE GROUP (A): 94.3010 47.3970 9.1790
REMARK 3 T TENSOR
REMARK 3 T11: -0.3257 T22: -0.1987
REMARK 3 T33: -0.2788 T12: 0.1107
REMARK 3 T13: -0.0909 T23: 0.0562
REMARK 3 L TENSOR
REMARK 3 L11: 10.6160 L22: 1.9983
REMARK 3 L33: 13.2310 L12: -0.4580
REMARK 3 L13: -3.7996 L23: -0.2035
REMARK 3 S TENSOR
REMARK 3 S11: 0.4320 S12: -0.4239 S13: 0.0020
REMARK 3 S21: -0.3732 S22: -0.1038 S23: -0.0466
REMARK 3 S31: 0.6002 S32: 0.6535 S33: -0.3282
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 190 H 206
REMARK 3 ORIGIN FOR THE GROUP (A): 93.7780 40.4300 -3.6580
REMARK 3 T TENSOR
REMARK 3 T11: 0.1870 T22: -0.0426
REMARK 3 T33: -0.1476 T12: 0.2758
REMARK 3 T13: -0.0960 T23: -0.1315
REMARK 3 L TENSOR
REMARK 3 L11: 7.7757 L22: 3.9136
REMARK 3 L33: 6.2447 L12: 0.4237
REMARK 3 L13: -2.4523 L23: -0.9758
REMARK 3 S TENSOR
REMARK 3 S11: 0.6118 S12: 0.4813 S13: -1.2766
REMARK 3 S21: -0.8540 S22: -0.7092 S23: -0.0382
REMARK 3 S31: 0.5831 S32: 0.3961 S33: 0.0974
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 207 H 221
REMARK 3 ORIGIN FOR THE GROUP (A): 85.8370 43.5500 -1.9310
REMARK 3 T TENSOR
REMARK 3 T11: -0.1855 T22: 0.0345
REMARK 3 T33: -0.0956 T12: 0.0578
REMARK 3 T13: -0.2759 T23: -0.0964
REMARK 3 L TENSOR
REMARK 3 L11: 6.9762 L22: 4.6661
REMARK 3 L33: 15.7770 L12: 2.5961
REMARK 3 L13: -8.4835 L23: -0.0704
REMARK 3 S TENSOR
REMARK 3 S11: -0.3870 S12: 0.5271 S13: -0.6436
REMARK 3 S21: -1.3335 S22: 0.1229 S23: 0.8409
REMARK 3 S31: 1.9895 S32: -0.8019 S33: 0.2641
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 1 L 38
REMARK 3 ORIGIN FOR THE GROUP (A): 114.1070 49.9490 35.1290
REMARK 3 T TENSOR
REMARK 3 T11: -0.2726 T22: -0.0949
REMARK 3 T33: -0.0562 T12: 0.0350
REMARK 3 T13: 0.0170 T23: 0.1437
REMARK 3 L TENSOR
REMARK 3 L11: 2.0134 L22: 0.7562
REMARK 3 L33: 2.1007 L12: 0.7360
REMARK 3 L13: -0.5759 L23: 0.4119
REMARK 3 S TENSOR
REMARK 3 S11: 0.1040 S12: 0.2783 S13: 0.2746
REMARK 3 S21: -0.0646 S22: -0.0411 S23: 0.0119
REMARK 3 S31: -0.0664 S32: 0.0992 S33: -0.0630
REMARK 3
REMARK 3 TLS GROUP : 26
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 39 L 69
REMARK 3 ORIGIN FOR THE GROUP (A): 113.4010 39.0080 36.1690
REMARK 3 T TENSOR
REMARK 3 T11: -0.2137 T22: -0.1133
REMARK 3 T33: -0.1353 T12: 0.0267
REMARK 3 T13: -0.0125 T23: 0.0945
REMARK 3 L TENSOR
REMARK 3 L11: 4.5345 L22: 1.8099
REMARK 3 L33: 2.2669 L12: 0.3649
REMARK 3 L13: -0.0669 L23: -0.8368
REMARK 3 S TENSOR
REMARK 3 S11: -0.0157 S12: 0.3718 S13: -0.2639
REMARK 3 S21: -0.1599 S22: 0.1330 S23: -0.0711
REMARK 3 S31: 0.5319 S32: 0.1353 S33: -0.1174
REMARK 3
REMARK 3 TLS GROUP : 27
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 70 L 97
REMARK 3 ORIGIN FOR THE GROUP (A): 112.1810 45.5600 35.6380
REMARK 3 T TENSOR
REMARK 3 T11: -0.2667 T22: -0.1490
REMARK 3 T33: -0.1319 T12: -0.0084
REMARK 3 T13: -0.0302 T23: 0.0966
REMARK 3 L TENSOR
REMARK 3 L11: 3.9213 L22: 0.9542
REMARK 3 L33: 5.4599 L12: -0.7525
REMARK 3 L13: -1.7655 L23: 0.0516
REMARK 3 S TENSOR
REMARK 3 S11: -0.0217 S12: 0.3695 S13: -0.0510
REMARK 3 S21: -0.0058 S22: -0.0539 S23: 0.1147
REMARK 3 S31: 0.3861 S32: -0.1419 S33: 0.0755
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 98 L 135
REMARK 3 ORIGIN FOR THE GROUP (A): 100.3050 52.9530 8.0760
REMARK 3 T TENSOR
REMARK 3 T11: -0.2881 T22: 0.0465
REMARK 3 T33: -0.1507 T12: 0.0622
REMARK 3 T13: 0.0160 T23: 0.0590
REMARK 3 L TENSOR
REMARK 3 L11: 2.2854 L22: 1.9437
REMARK 3 L33: 5.8958 L12: -1.9374
REMARK 3 L13: 3.5235 L23: -2.6131
REMARK 3 S TENSOR
REMARK 3 S11: 0.4621 S12: 0.3527 S13: -0.2704
REMARK 3 S21: -0.2924 S22: -0.3435 S23: 0.1354
REMARK 3 S31: 0.4835 S32: 0.3681 S33: -0.1186
REMARK 3
REMARK 3 TLS GROUP : 29
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 136 L 167
REMARK 3 ORIGIN FOR THE GROUP (A): 101.4590 59.6270 8.7240
REMARK 3 T TENSOR
REMARK 3 T11: -0.3834 T22: 0.1493
REMARK 3 T33: -0.2440 T12: 0.0510
REMARK 3 T13: -0.0031 T23: 0.0308
REMARK 3 L TENSOR
REMARK 3 L11: 6.6961 L22: 5.2547
REMARK 3 L33: 2.8572 L12: -4.4602
REMARK 3 L13: 2.9753 L23: -2.3522
REMARK 3 S TENSOR
REMARK 3 S11: -0.1208 S12: -0.1972 S13: 0.5044
REMARK 3 S21: 0.1206 S22: -0.1868 S23: -0.4294
REMARK 3 S31: -0.0663 S32: 0.3298 S33: 0.3076
REMARK 3
REMARK 3 TLS GROUP : 30
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 168 L 197
REMARK 3 ORIGIN FOR THE GROUP (A): 95.1880 59.8360 2.9730
REMARK 3 T TENSOR
REMARK 3 T11: -0.3512 T22: -0.0006
REMARK 3 T33: -0.2585 T12: 0.0468
REMARK 3 T13: -0.0067 T23: 0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 9.7968 L22: 4.3387
REMARK 3 L33: 4.7133 L12: -5.0596
REMARK 3 L13: 4.5306 L23: -2.6858
REMARK 3 S TENSOR
REMARK 3 S11: 0.0511 S12: 0.2758 S13: 0.0881
REMARK 3 S21: -0.2341 S22: -0.1424 S23: -0.0250
REMARK 3 S31: 0.0375 S32: 0.2784 S33: 0.0913
REMARK 3
REMARK 3 TLS GROUP : 31
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 198 L 214
REMARK 3 ORIGIN FOR THE GROUP (A): 102.6600 62.2790 -2.3980
REMARK 3 T TENSOR
REMARK 3 T11: -0.3440 T22: 0.1709
REMARK 3 T33: -0.1917 T12: 0.1622
REMARK 3 T13: 0.0901 T23: 0.1440
REMARK 3 L TENSOR
REMARK 3 L11: 14.1961 L22: 5.2787
REMARK 3 L33: 12.6441 L12: -4.6242
REMARK 3 L13: 9.7312 L23: -5.3059
REMARK 3 S TENSOR
REMARK 3 S11: 0.5371 S12: 1.5211 S13: 0.3215
REMARK 3 S21: -0.5150 S22: -0.7958 S23: -0.3958
REMARK 3 S31: 0.2665 S32: 1.2939 S33: 0.2587
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2VDO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-OCT-07.
REMARK 100 THE PDBE ID CODE IS EBI-34088.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.07223
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : CUSTOM (SBC2 3K)
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 557015
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.80
REMARK 200 RESOLUTION RANGE LOW (A) : 50.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.2
REMARK 200 R MERGE (I) : 0.11
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.20
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.62
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.80
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.2
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.8
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 11% PEG 3350, 0.7 M MAGNESIUM
REMARK 280 ACETATE, 0.1 M SODIUM CACODYLATE, PH 6.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 117.71133
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 58.85567
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 58.85567
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 117.71133
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 11960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 72750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, 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 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 GLY B 73
REMARK 465 SER B 74
REMARK 465 GLY B 75
REMARK 465 ASP B 76
REMARK 465 SER B 77
REMARK 465 SER B 78
REMARK 465 GLY H 135
REMARK 465 ASP H 136
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 4100 O HOH A 4252 2.04
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 101 -122.75 50.05
REMARK 500 LYS A 118 -122.03 51.68
REMARK 500 GLU A 123 134.43 99.29
REMARK 500 LEU A 212 -46.37 71.52
REMARK 500 SER A 222 -176.60 -68.49
REMARK 500 SER A 261 70.41 53.50
REMARK 500 PRO A 337 20.70 -78.97
REMARK 500 VAL B 10 72.70 41.75
REMARK 500 PHE B 56 79.46 -151.14
REMARK 500 ASP B 71 -158.49 -114.49
REMARK 500 VAL B 80 103.48 66.94
REMARK 500 ASP B 95 15.65 59.99
REMARK 500 VAL B 157 -87.56 -125.17
REMARK 500 SER B 213 -156.57 -114.46
REMARK 500 ASP B 241 51.69 -111.55
REMARK 500 LEU B 258 -12.59 83.66
REMARK 500 VAL B 275 -84.29 -91.16
REMARK 500 CYS B 374 -158.98 -95.87
REMARK 500 LYS B 410 -23.04 75.11
REMARK 500 GLU B 442 82.06 55.65
REMARK 500 HIS B 446 -63.52 67.44
REMARK 500 ASN B 452 -60.71 -106.21
REMARK 500 THR B 454 147.91 69.28
REMARK 500 HIS C 401 -56.05 -145.80
REMARK 500 LEU C 402 -11.91 -160.62
REMARK 500 GLN C 407 70.24 -114.72
REMARK 500 ASP H 179 -16.30 77.13
REMARK 500 SER L 30 58.49 31.85
REMARK 500 SER L 77 75.63 58.09
REMARK 500 ASN L 212 70.10 51.30
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 GLU A 243 OE1
REMARK 620 2 GLU A 243 OE2 52.0
REMARK 620 3 ASP A 245 OD2 122.3 70.3
REMARK 620 4 ASP A 247 O 78.0 77.3 90.7
REMARK 620 5 THR A 250 O 76.3 126.9 158.1 81.7
REMARK 620 6 THR A 250 OG1 145.2 139.5 80.4 75.7 77.8
REMARK 620 7 GLU A 252 OE1 88.8 81.6 82.5 158.9 111.4 122.3
REMARK 620 8 GLU A 252 OE2 132.1 126.1 80.3 148.5 95.6 73.1 49.8
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 HOH A4304 O
REMARK 620 2 ASN A 299 OD1 96.2
REMARK 620 3 ASP A 301 OD1 82.8 81.5
REMARK 620 4 ASP A 297 OD1 162.9 79.1 80.2
REMARK 620 5 ARG A 303 O 98.6 161.9 90.1 83.7
REMARK 620 6 ASP A 305 OD1 69.0 112.9 149.1 128.0 82.3
REMARK 620 7 ASP A 305 OD2 113.0 85.7 160.7 83.2 97.9 50.0
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 ASP A 365 OD2
REMARK 620 2 ASP A 369 OD1 75.7
REMARK 620 3 TYR A 371 O 75.6 87.2
REMARK 620 4 ASP A 367 OD1 87.3 93.6 162.2
REMARK 620 5 HOH A4342 O 151.4 76.2 97.8 99.6
REMARK 620 6 ASP A 373 OD1 93.6 164.0 101.7 73.8 115.1
REMARK 620 7 ASP A 373 OD2 129.0 147.5 80.7 106.9 75.7 48.3
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 ASN A 430 OD1 86.3
REMARK 620 3 HOH A4381 O 134.6 88.6
REMARK 620 4 ASP A 426 OD1 78.2 83.8 145.8
REMARK 620 5 ASP A 428 OD1 157.6 93.8 67.8 79.5
REMARK 620 6 ASP A 434 OD1 100.4 170.8 91.2 91.2 77.6
REMARK 620 7 ASP A 434 OD2 82.1 138.2 72.2 131.9 111.4 50.0
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 GOL B1462 C2
REMARK 620 2 GOL B1462 O2 27.8
REMARK 620 3 HOH C4014 O 95.7 81.6
REMARK 620 4 ASP B 127 OD1 82.0 92.4 170.6
REMARK 620 5 ASP B 251 OD2 99.2 126.0 104.6 84.7
REMARK 620 6 GOL B1462 O1 46.8 62.8 70.2 113.5 69.3
REMARK 620 7 SER B 123 O 177.1 155.0 86.0 96.8 78.0 132.1
REMARK 620 8 ASP B 126 OD1 105.1 80.8 88.6 83.3 151.0 139.6 77.3
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 O
REMARK 620 2 ASP B 158 OD2 164.1
REMARK 620 3 ASN B 215 OD1 96.3 95.5
REMARK 620 4 ASP B 217 OD1 76.8 91.5 94.8
REMARK 620 5 PRO B 219 O 89.1 81.8 166.7 98.3
REMARK 620 6 GLU B 220 OE2 92.4 100.0 81.4 168.1 86.2
REMARK 620 N 1 2 3 4 5
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 ASP C 410 OD1
REMARK 620 2 HOH B4088 O 92.1
REMARK 620 3 SER B 121 OG 90.3 176.5
REMARK 620 4 SER B 123 OG 79.3 89.3 88.7
REMARK 620 5 GLU B 220 OE1 93.6 90.9 91.5 172.9
REMARK 620 6 HOH B4022 O 154.7 98.7 78.1 78.1 108.9
REMARK 620 N 1 2 3 4 5
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A3015
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A3249
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3099
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3320
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3321
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3322
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3323
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3324
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3371
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3372
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3373
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3374
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3375
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3376
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3377
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1453
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1462
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MK7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF AN INTEGRIN BETA3-TALIN
REMARK 900 CHIMERA
REMARK 900 RELATED ID: 2VDQ RELATED DB: PDB
REMARK 900 INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO A
REMARK 900 CHIMERIC FIBRINOGEN GAMMA CHAIN PEPTIDE,
REMARK 900 HHLGGAKQRGDV
REMARK 900 RELATED ID: 1M8O RELATED DB: PDB
REMARK 900 PLATELET INTEGRIN ALFAIIB-BETA3 CYTOPLASMIC
REMARK 900 DOMAIN
REMARK 900 RELATED ID: 1S4X RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE INTEGRIN B3 CYTOPLASMIC
REMARK 900 DOMAIN IN DPCMICELLES
REMARK 900 RELATED ID: 2VDN RELATED DB: PDB
REMARK 900 RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3
REMARK 900 HEADPIECE BOUND TO ANTAGONIST EPTIFIBATIDE
REMARK 900 RELATED ID: 1UV9 RELATED DB: PDB
REMARK 900 HOMOLOGY MODELING OF GPIIB
REMARK 900 RELATED ID: 1TYE RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR ALLOSTERY IN INTEGRINS
REMARK 900 AND BINDING OFLIGAND-MIMETIC THERAPEUTICS TO
REMARK 900 THE PLATELET RECEPTOR FORFIBRINOGEN
REMARK 900 RELATED ID: 1S4W RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE CYTOPLASMIC DOMAIN OF
REMARK 900 INTEGRIN AIIB INDPC MICELLES
REMARK 900 RELATED ID: 1MK9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF AN INTEGRIN BETA3-TALIN
REMARK 900 CHIMERA
REMARK 900 RELATED ID: 1M1X RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT
REMARK 900 OF INTEGRINALPHA VBETA3 BOUND TO MN2+
REMARK 900 RELATED ID: 1RN0 RELATED DB: PDB
REMARK 900 A REFINED THREE-DIMENSIONAL MODEL OF
REMARK 900 INTEGRIN AIIBB3
REMARK 900 RELATED ID: 1L5G RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT
REMARK 900 OF INTEGRINAVB3 IN COMPLEX WITH AN ARG-
REMARK 900 GLY-ASP LIGAND
REMARK 900 RELATED ID: 2VDM RELATED DB: PDB
REMARK 900 RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3
REMARK 900 HEADPIECE BOUND TO ANTAGONIST TIROFIBAN
REMARK 900 RELATED ID: 1DPQ RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE CONSTITUTIVELY
REMARK 900 ACTIVE MUTANT OF THE INTEGRIN ALPHA IIB
REMARK 900 CYTOPLASMIC DOMAIN.
REMARK 900 RELATED ID: 2VDO RELATED DB: PDB
REMARK 900 INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO
REMARK 900 FIBRINOGEN GAMMA CHAIN PEPTIDE, HHLGGAKQAGDV
REMARK 900 RELATED ID: 2VDP RELATED DB: PDB
REMARK 900 INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO
REMARK 900 FIBRINOGEN GAMMA CHAIN PEPTIDE,LGGAKQAGDV
REMARK 900 RELATED ID: 1JV2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT
REMARK 900 OF INTEGRINALPHAVBETA3
REMARK 900 RELATED ID: 1DPK RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE CYTOPLASMIC DOMAIN
REMARK 900 OF THE INTEGRIN ALPHA-IIB SUBUNIT
REMARK 900 RELATED ID: 2VDR RELATED DB: PDB
REMARK 900 INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO
REMARK 900 FIBRINOGEN GAMMA CHAIN CHIMERA PEPTIDE,
REMARK 900 LGGAKQRGDV
REMARK 900 RELATED ID: 2VDK RELATED DB: PDB
REMARK 900 RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3
REMARK 900 HEADPIECE
REMARK 900 RELATED ID: 1KUP RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE MEMBRANE PROXIMAL
REMARK 900 REGIONS OFALPHA-IIB AND BETA-3 INTEGRINS
REMARK 900 RELATED ID: 1KUZ RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE MEMBRANE PROXIMAL
REMARK 900 REGIONS OFALPHA-IIB AND BETA-3 INTEGRINS
REMARK 900 RELATED ID: 2VDL RELATED DB: PDB
REMARK 900 RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3
REMARK 900 HEADPIECE
REMARK 900 RELATED ID: 1MIZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF AN INTEGRIN BETA3-TALIN
REMARK 900 CHIMERA
REMARK 900 RELATED ID: 1U8C RELATED DB: PDB
REMARK 900 A NOVEL ADAPTATION OF THE INTEGRIN PSI
REMARK 900 DOMAIN REVEALED FROMITS CRYSTAL STRUCTURE
REMARK 900 RELATED ID: 1JX5 RELATED DB: PDB
REMARK 900 THEORETICAL MODEL OF THE BETA-PROPELLER
REMARK 900 DOMAIN OF INTEGRINALPHAIIB
REMARK 900 RELATED ID: 2VC2 RELATED DB: PDB
REMARK 900 RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3
REMARK 900 HEADPIECE BOUND TO ANTAGONIST L-739758
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 ACCORDING TO THE AUTHORS THE CORRECT CHAIN A SEQUENCE IS
REMARK 999 ANNOTATED IN NCBI ENTRY GI 88758615 WHICH SHOULD BE USED
REMARK 999 IN PLACE OF P08514.
REMARK 999 ACCORDING TO THE AUTHORS THE CORRECT CHAIN C SEQUENCE IS
REMARK 999 ANNOTATED IN NCBI ENTRY GI 70906437 WHICH CORRESPONDS TO
REMARK 999 THE UNIPROT ENTRY Q53Y18
DBREF 2VDO A 1 452 UNP P08514 ITA2B_HUMAN 32 483
DBREF 2VDO B 1 461 UNP P05106 ITB3_HUMAN 27 487
DBREF 2VDO C 400 411 UNP Q53Y18 Q53Y18_HUMAN 426 437
DBREF 2VDO H 1 221 PDB 2VDO 2VDO 1 221
DBREF 2VDO L 1 214 PDB 2VDO 2VDO 1 214
SEQADV 2VDO GLY A 282 UNP P08514 ALA 313 CONFLICT SEE REMARK 999
SEQRES 1 A 452 LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY
SEQRES 2 A 452 PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS
SEQRES 3 A 452 LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA
SEQRES 4 A 452 PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY
SEQRES 5 A 452 VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS
SEQRES 6 A 452 PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN
SEQRES 7 A 452 VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN
SEQRES 8 A 452 GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE
SEQRES 9 A 452 VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU
SEQRES 10 A 452 LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS
SEQRES 11 A 452 PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR
SEQRES 12 A 452 SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL
SEQRES 13 A 452 GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA
SEQRES 14 A 452 GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL
SEQRES 15 A 452 LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU
SEQRES 16 A 452 ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG
SEQRES 17 A 452 PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU
SEQRES 18 A 452 SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR
SEQRES 19 A 452 TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP
SEQRES 20 A 452 LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP
SEQRES 21 A 452 SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR
SEQRES 22 A 452 TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA
SEQRES 23 A 452 SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN
SEQRES 24 A 452 GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU
SEQRES 25 A 452 TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL
SEQRES 26 A 452 GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS
SEQRES 27 A 452 ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN
SEQRES 28 A 452 LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY
SEQRES 29 A 452 ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA
SEQRES 30 A 452 ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU
SEQRES 31 A 452 VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO
SEQRES 32 A 452 SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA
SEQRES 33 A 452 PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP
SEQRES 34 A 452 ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA
SEQRES 35 A 452 ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO
SEQRES 1 B 461 GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS
SEQRES 2 B 461 GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS
SEQRES 3 B 461 SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP
SEQRES 4 B 461 LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU
SEQRES 5 B 461 SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU
SEQRES 6 B 461 ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER
SEQRES 7 B 461 GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG
SEQRES 8 B 461 LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL
SEQRES 9 B 461 ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU
SEQRES 10 B 461 MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER
SEQRES 11 B 461 ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG
SEQRES 12 B 461 LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE
SEQRES 13 B 461 VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO
SEQRES 14 B 461 PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR
SEQRES 15 B 461 THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR
SEQRES 16 B 461 LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS
SEQRES 17 B 461 LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY
SEQRES 18 B 461 GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU
SEQRES 19 B 461 LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL
SEQRES 20 B 461 PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY
SEQRES 21 B 461 ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS
SEQRES 22 B 461 HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR
SEQRES 23 B 461 MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU
SEQRES 24 B 461 SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU
SEQRES 25 B 461 ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE
SEQRES 26 B 461 PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER
SEQRES 27 B 461 ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE
SEQRES 28 B 461 ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU
SEQRES 29 B 461 GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN
SEQRES 30 B 461 GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS
SEQRES 31 B 461 ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL
SEQRES 32 B 461 ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE
SEQRES 33 B 461 LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL
SEQRES 34 B 461 THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU
SEQRES 35 B 461 PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE
SEQRES 36 B 461 GLU CYS GLY VAL CYS ARG
SEQRES 1 C 12 HIS HIS LEU GLY GLY ALA LYS GLN ALA GLY ASP VAL
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
HET CA A2004 1
HET CA A2005 1
HET CA A2006 1
HET CA A2007 1
HET NAG A3015 14
HET NAG A3249 14
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 MAN B3323 11
HET MAN B3324 11
HET NAG B3371 14
HET NAG B3372 14
HET MAN B3373 11
HET MAN B3374 11
HET MAN B3375 11
HET MAN B3376 11
HET MAN B3377 11
HET GOL A1453 6
HET GOL B1462 6
HETNAM GOL GLYCEROL
HETNAM CA CALCIUM ION
HETNAM MAN ALPHA-D-MANNOSE
HETNAM MG MAGNESIUM ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 6 GOL 2(C3 H8 O3)
FORMUL 7 CA 6(CA 2+)
FORMUL 8 MAN 8(C6 H12 O6)
FORMUL 9 MG MG 2+
FORMUL 10 NAG 7(C8 H15 N O6)
FORMUL 11 HOH *1043(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 SER B 12 SER B 20 1 9
HELIX 8 8 LYS B 41 ASP B 47 1 7
HELIX 9 9 SER B 121 ASP B 126 5 6
HELIX 10 10 ASP B 127 THR B 146 1 20
HELIX 11 11 PRO B 169 LEU B 173 5 5
HELIX 12 12 CYS B 177 LYS B 181 5 5
HELIX 13 13 GLN B 199 GLN B 210 1 12
HELIX 14 14 GLY B 221 CYS B 232 1 12
HELIX 15 15 CYS B 232 GLY B 237 1 6
HELIX 16 16 LEU B 258 GLY B 264 5 7
HELIX 17 17 SER B 291 LYS B 302 1 12
HELIX 18 18 VAL B 314 GLU B 323 1 10
HELIX 19 19 SER B 337 LYS B 350 1 14
HELIX 20 20 CYS B 435 ALA B 439 5 5
HELIX 21 21 ASN H 28 THR H 32 5 5
HELIX 22 22 PRO H 62 PHE H 64 5 3
HELIX 23 23 THR H 74 SER H 76 5 3
HELIX 24 24 THR H 87 THR H 91 5 5
HELIX 25 25 SER H 162 SER H 164 5 3
HELIX 26 26 PRO H 206 SER H 209 5 4
HELIX 27 27 ASP L 79 PHE L 83 5 5
HELIX 28 28 SER L 121 SER L 127 1 7
HELIX 29 29 LYS L 183 GLU L 187 1 5
SHEET 1 AA 4 THR A 9 ALA A 12 0
SHEET 2 AA 4 GLN A 444 TYR A 448 -1 O VAL A 445 N TYR A 11
SHEET 3 AA 4 ASP A 434 ALA A 439 -1 O LEU A 435 N TYR A 448
SHEET 4 AA 4 SER A 420 VAL A 425 -1 O SER A 420 N GLY A 438
SHEET 1 AB 3 LEU A 23 LYS A 27 0
SHEET 2 AB 3 VAL A 33 ALA A 39 -1 O ALA A 34 N HIS A 26
SHEET 3 AB 3 GLY A 52 PRO A 57 -1 O GLY A 52 N ALA A 39
SHEET 1 AC 4 THR A 76 VAL A 79 0
SHEET 2 AC 4 GLN A 82 PHE A 87 -1 O GLN A 82 N VAL A 79
SHEET 3 AC 4 HIS A 112 GLU A 117 -1 O HIS A 112 N PHE A 87
SHEET 4 AC 4 THR A 125 PRO A 126 -1 O THR A 125 N TRP A 113
SHEET 1 AD 4 THR A 76 VAL A 79 0
SHEET 2 AD 4 GLN A 82 PHE A 87 -1 O GLN A 82 N VAL A 79
SHEET 3 AD 4 HIS A 112 GLU A 117 -1 O HIS A 112 N PHE A 87
SHEET 4 AD 4 GLU A 120 GLU A 121 -1 O GLU A 120 N GLU A 117
SHEET 1 AE 4 VAL A 97 TRP A 100 0
SHEET 2 AE 4 VAL A 103 ALA A 108 -1 O VAL A 103 N TRP A 100
SHEET 3 AE 4 SER A 129 ALA A 133 -1 O SER A 129 N ALA A 108
SHEET 4 AE 4 ARG A 140 TYR A 143 -1 O ALA A 141 N LEU A 132
SHEET 1 AF 4 SER A 172 VAL A 175 0
SHEET 2 AF 4 GLU A 180 ALA A 185 -1 O VAL A 182 N VAL A 174
SHEET 3 AF 4 LEU A 194 PRO A 199 -1 O LEU A 194 N ALA A 185
SHEET 4 AF 4 SER A 220 LEU A 221 -1 O SER A 220 N GLN A 197
SHEET 1 AG 4 VAL A 239 GLY A 242 0
SHEET 2 AG 4 GLU A 252 ALA A 257 -1 O GLU A 252 N GLY A 242
SHEET 3 AG 4 ALA A 266 LEU A 270 -1 O ALA A 266 N ALA A 257
SHEET 4 AG 4 ARG A 276 ARG A 281 -1 N LEU A 277 O ILE A 269
SHEET 1 AH 4 VAL A 293 THR A 296 0
SHEET 2 AH 4 ASP A 305 ALA A 310 -1 O ASP A 305 N THR A 296
SHEET 3 AH 4 ARG A 327 PHE A 331 -1 O ARG A 327 N ALA A 310
SHEET 4 AH 4 LEU A 345 THR A 348 -1 O LEU A 345 N LEU A 330
SHEET 1 AI 2 MET A 314 ARG A 317 0
SHEET 2 AI 2 LYS A 321 GLU A 324 -1 O LYS A 321 N ARG A 317
SHEET 1 AJ 4 ILE A 360 GLY A 364 0
SHEET 2 AJ 4 ASP A 373 ALA A 378 -1 O ASP A 373 N LEU A 363
SHEET 3 AJ 4 GLN A 388 PHE A 392 -1 O GLN A 388 N ALA A 378
SHEET 4 AJ 4 GLN A 405 ASP A 408 -1 O GLN A 405 N VAL A 391
SHEET 1 AK 2 GLY A 394 GLN A 395 0
SHEET 2 AK 2 GLY A 398 LEU A 399 -1 O GLY A 398 N GLN A 395
SHEET 1 BA 3 CYS B 38 LEU B 40 0
SHEET 2 BA 3 CYS B 23 CYS B 26 -1 O ALA B 24 N ASP B 39
SHEET 3 BA 3 ILE B 54 GLU B 55 -1 O GLU B 55 N TRP B 25
SHEET 1 BB 6 GLU B 60 GLU B 65 0
SHEET 2 BB 6 ARG B 87 LEU B 92 -1 O ARG B 87 N LEU B 64
SHEET 3 BB 6 LEU B 425 PHE B 431 1 O ILE B 426 N ILE B 88
SHEET 4 BB 6 GLU B 411 PRO B 418 -1 O LYS B 412 N VAL B 429
SHEET 5 BB 6 SER B 353 ARG B 360 -1 O GLU B 358 N LYS B 417
SHEET 6 BB 6 SER B 385 LEU B 389 -1 O CYS B 386 N VAL B 355
SHEET 1 BC 5 VAL B 83 SER B 84 0
SHEET 2 BC 5 SER B 97 ARG B 105 -1 O GLN B 103 N SER B 84
SHEET 3 BC 5 THR B 394 VAL B 403 -1 O VAL B 395 N VAL B 104
SHEET 4 BC 5 LEU B 366 THR B 373 -1 O SER B 367 N LYS B 402
SHEET 5 BC 5 VAL B 379 PRO B 381 -1 O ILE B 380 N ALA B 372
SHEET 1 BD 6 TYR B 190 THR B 197 0
SHEET 2 BD 6 LEU B 149 PHE B 156 -1 O ILE B 151 N THR B 197
SHEET 3 BD 6 VAL B 112 ASP B 119 1 O VAL B 112 N ARG B 150
SHEET 4 BD 6 SER B 243 THR B 250 1 O SER B 243 N ASP B 113
SHEET 5 BD 6 ASN B 305 VAL B 310 1 O ASN B 305 N LEU B 246
SHEET 6 BD 6 THR B 329 VAL B 332 1 O THR B 329 N PHE B 308
SHEET 1 HA 4 GLN H 3 GLN H 6 0
SHEET 2 HA 4 VAL H 18 SER H 25 -1 O THR H 23 N GLN H 5
SHEET 3 HA 4 THR H 78 LEU H 83 -1 O ALA H 79 N CYS H 22
SHEET 4 HA 4 ALA H 68 ASP H 73 -1 O THR H 69 N GLN H 82
SHEET 1 HB 6 GLU H 10 VAL H 12 0
SHEET 2 HB 6 THR H 113 VAL H 117 1 O SER H 114 N GLU H 10
SHEET 3 HB 6 ALA H 92 ARG H 98 -1 O ALA H 92 N VAL H 115
SHEET 4 HB 6 VAL H 34 ARG H 40 -1 O HIS H 35 N VAL H 97
SHEET 5 HB 6 GLY H 44 ILE H 51 -1 O GLY H 44 N ARG H 40
SHEET 6 HB 6 THR H 58 TYR H 60 -1 O LYS H 59 N ARG H 50
SHEET 1 HC 4 GLU H 10 VAL H 12 0
SHEET 2 HC 4 THR H 113 VAL H 117 1 O SER H 114 N GLU H 10
SHEET 3 HC 4 ALA H 92 ARG H 98 -1 O ALA H 92 N VAL H 115
SHEET 4 HC 4 TYR H 108 TRP H 109 -1 O TYR H 108 N ARG H 98
SHEET 1 HD 4 SER H 126 LEU H 130 0
SHEET 2 HD 4 SER H 141 TYR H 151 -1 O GLY H 145 N LEU H 130
SHEET 3 HD 4 LEU H 180 THR H 190 -1 O TYR H 181 N TYR H 151
SHEET 4 HD 4 VAL H 169 THR H 171 -1 O HIS H 170 N SER H 186
SHEET 1 HE 4 SER H 126 LEU H 130 0
SHEET 2 HE 4 SER H 141 TYR H 151 -1 O GLY H 145 N LEU H 130
SHEET 3 HE 4 LEU H 180 THR H 190 -1 O TYR H 181 N TYR H 151
SHEET 4 HE 4 VAL H 175 GLN H 177 -1 O VAL H 175 N THR H 182
SHEET 1 HF 3 THR H 157 TRP H 160 0
SHEET 2 HF 3 THR H 200 HIS H 205 -1 O ASN H 202 N THR H 159
SHEET 3 HF 3 THR H 210 LYS H 215 -1 O THR H 210 N HIS H 205
SHEET 1 LA 4 MET L 4 SER L 7 0
SHEET 2 LA 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7
SHEET 3 LA 4 ASP L 70 ILE L 75 -1 O TYR L 71 N CYS L 23
SHEET 4 LA 4 PHE L 62 SER L 67 -1 O SER L 63 N THR L 74
SHEET 1 LB 9 SER L 10 VAL L 13 0
SHEET 2 LB 9 THR L 102 ILE L 106 1 O LYS L 103 N MET L 11
SHEET 3 LB 9 ASP L 85 GLN L 90 -1 O TYR L 86 N THR L 102
SHEET 4 LB 9 ASN L 53 LEU L 54
SHEET 5 LB 9 PHE L 44 TYR L 49 -1 O TYR L 49 N ASN L 53
SHEET 6 LB 9 ILE L 33 GLN L 38 -1 O TRP L 35 N LEU L 47
SHEET 7 LB 9 ASP L 85 GLN L 90 -1 O ASP L 85 N GLN L 38
SHEET 8 LB 9 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90
SHEET 9 LB 9 ASP L 85 GLN L 90 -1 O GLN L 90 N THR L 97
SHEET 1 LC 4 THR L 114 PHE L 118 0
SHEET 2 LC 4 GLY L 129 PHE L 139 -1 O VAL L 133 N PHE L 118
SHEET 3 LC 4 TYR L 173 THR L 182 -1 O TYR L 173 N PHE L 139
SHEET 4 LC 4 VAL L 159 TRP L 163 -1 O LEU L 160 N THR L 178
SHEET 1 LD 4 SER L 153 ARG L 155 0
SHEET 2 LD 4 ASN L 145 ILE L 150 -1 O TRP L 148 N ARG L 155
SHEET 3 LD 4 SER L 191 THR L 197 -1 O THR L 193 N LYS L 149
SHEET 4 LD 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 2.03
SSBOND 2 CYS A 107 CYS A 130 1555 1555 2.08
SSBOND 3 CYS A 146 CYS A 167 1555 1555 2.05
SSBOND 4 CYS B 5 CYS B 23 1555 1555 2.05
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 2.04
SSBOND 8 CYS B 177 CYS B 184 1555 1555 2.09
SSBOND 9 CYS B 232 CYS B 273 1555 1555 2.07
SSBOND 10 CYS B 374 CYS B 386 1555 1555 2.05
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 H 22 CYS H 96 1555 1555 2.05
SSBOND 15 CYS H 134 CYS L 214 1555 1555 2.03
SSBOND 16 CYS H 146 CYS H 201 1555 1555 2.05
SSBOND 17 CYS L 23 CYS L 88 1555 1555 2.11
SSBOND 18 CYS L 134 CYS L 194 1555 1555 2.04
LINK ND2 ASN A 15 C1 ANAG A3015 1555 1555 1.45
LINK ND2 ASN A 249 C1 ANAG A3249 1555 1555 1.44
LINK CA CA A2004 OD2 ASP A 245 1555 1555 2.30
LINK CA CA A2004 O ASP A 247 1555 1555 2.37
LINK CA CA A2004 O THR A 250 1555 1555 2.51
LINK CA CA A2004 OG1 THR A 250 1555 1555 2.45
LINK CA CA A2004 OE1 GLU A 252 1555 1555 2.47
LINK CA CA A2004 OE2 GLU A 252 1555 1555 2.71
LINK CA CA A2004 OE1 GLU A 243 1555 1555 2.26
LINK CA CA A2004 OE2 GLU A 243 1555 1555 2.66
LINK CA CA A2005 OD1 ASP A 301 1555 1555 2.46
LINK CA CA A2005 OD1 ASP A 297 1555 1555 2.32
LINK CA CA A2005 O ARG A 303 1555 1555 2.39
LINK CA CA A2005 OD1 ASP A 305 1555 1555 2.57
LINK CA CA A2005 OD2 ASP A 305 1555 1555 2.62
LINK CA CA A2005 OD1 ASN A 299 1555 1555 2.26
LINK CA CA A2005 O HOH A4304 1555 1555 2.18
LINK CA CA A2006 O TYR A 371 1555 1555 2.30
LINK CA CA A2006 OD1 ASP A 367 1555 1555 2.27
LINK CA CA A2006 O HOH A4342 1555 1555 2.34
LINK CA CA A2006 OD1 ASP A 373 1555 1555 2.67
LINK CA CA A2006 OD2 ASP A 373 1555 1555 2.69
LINK CA CA A2006 OD2 ASP A 365 1555 1555 2.49
LINK CA CA A2006 OD1 ASP A 369 1555 1555 2.57
LINK CA CA A2007 O HOH A4381 1555 1555 2.26
LINK CA CA A2007 OD1 ASP A 426 1555 1555 2.35
LINK CA CA A2007 OD1 ASP A 428 1555 1555 2.41
LINK CA CA A2007 OD1 ASP A 434 1555 1555 2.65
LINK CA CA A2007 OD2 ASP A 434 1555 1555 2.52
LINK CA CA A2007 O TYR A 432 1555 1555 2.31
LINK CA CA A2007 OD1 ASN A 430 1555 1555 2.21
LINK ND2 ASN B 99 C1 NAG B3099 1555 1555 1.45
LINK ND2 ASN B 320 C1 NAG B3320 1555 1555 1.44
LINK ND2 ASN B 371 C1 NAG B3371 1555 1555 1.44
LINK MG MG B2001 OG SER B 123 1555 1555 2.20
LINK MG MG B2001 OD1 ASP C 410 1555 1555 2.21
LINK MG MG B2001 O HOH B4022 1555 1555 2.21
LINK MG MG B2001 O HOH B4088 1555 1555 2.19
LINK MG MG B2001 OE1 GLU B 220 1555 1555 1.95
LINK MG MG B2001 OG SER B 121 1555 1555 2.27
LINK CA CA B2002 OD1 ASP B 126 1555 1555 2.34
LINK CA CA B2002 O SER B 123 1555 1555 2.37
LINK CA CA B2002 O1 GOL B1462 1555 1555 2.98
LINK CA CA B2002 OD2 ASP B 251 1555 1555 2.24
LINK CA CA B2002 OD1 ASP B 127 1555 1555 2.24
LINK CA CA B2002 O HOH C4014 1555 1555 2.39
LINK CA CA B2002 O2 GOL B1462 1555 1555 2.47
LINK CA CA B2002 C2 GOL B1462 1555 1555 2.99
LINK CA CA B2003 OE2 GLU B 220 1555 1555 2.35
LINK CA CA B2003 O PRO B 219 1555 1555 2.29
LINK CA CA B2003 OD1 ASP B 217 1555 1555 2.23
LINK CA CA B2003 OD1 ASN B 215 1555 1555 2.32
LINK CA CA B2003 OD2 ASP B 158 1555 1555 2.36
LINK CA CA B2003 O ASP B 217 1555 1555 2.33
LINK O4 NAG B3320 C1 NAG B3321 1555 1555 1.44
LINK O4 NAG B3321 C1 MAN B3322 1555 1555 1.45
LINK O6 MAN B3322 C1 MAN B3324 1555 1555 1.45
LINK O3 MAN B3322 C1 MAN B3323 1555 1555 1.44
LINK O4 NAG B3371 C1 NAG B3372 1555 1555 1.44
LINK O4 NAG B3372 C1 MAN B3373 1555 1555 1.44
LINK O6 MAN B3373 C1 MAN B3375 1555 1555 1.44
LINK O3 MAN B3373 C1 AMAN B3374 1555 1555 1.44
LINK O6 MAN B3375 C1 MAN B3377 1555 1555 1.44
LINK O3 MAN B3375 C1 MAN B3376 1555 1555 1.43
CISPEP 1 SER B 84 PRO B 85 0 -0.41
CISPEP 2 SER B 162 PRO B 163 0 5.17
CISPEP 3 SER B 168 PRO B 169 0 -10.76
CISPEP 4 PHE H 152 PRO H 153 0 -2.06
CISPEP 5 GLU H 154 PRO H 155 0 1.44
CISPEP 6 TRP H 194 PRO H 195 0 3.25
CISPEP 7 SER L 7 PRO L 8 0 -10.16
CISPEP 8 LEU L 94 PRO L 95 0 -2.78
CISPEP 9 TYR L 140 PRO L 141 0 -0.99
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 A4304
SITE 1 AC3 6 ASP A 365 ASP A 367 ASP A 369 TYR A 371
SITE 2 AC3 6 ASP A 373 HOH A4342
SITE 1 AC4 6 ASP A 426 ASP A 428 ASN A 430 TYR A 432
SITE 2 AC4 6 ASP A 434 HOH A4381
SITE 1 AC5 1 ASN A 15
SITE 1 AC6 1 ASN A 249
SITE 1 AC7 6 SER B 121 SER B 123 GLU B 220 HOH B4022
SITE 2 AC7 6 HOH B4088 ASP C 410
SITE 1 AC8 6 SER B 123 ASP B 126 ASP B 127 ASP B 251
SITE 2 AC8 6 GOL B1462 HOH C4014
SITE 1 AC9 5 ASP B 158 ASN B 215 ASP B 217 PRO B 219
SITE 2 AC9 5 GLU B 220
SITE 1 BC1 4 ASN B 99 SER B 398 NAG B3371 HOH B4197
SITE 1 BC2 10 MET A 285 LEU B 317 ASN B 320 NAG B3321
SITE 2 BC2 10 HOH B4198 HOH B4199 HOH B4200 HOH B4201
SITE 3 BC2 10 HOH B4202 HOH B4203
SITE 1 BC3 6 ARG A 281 NAG B3320 MAN B3322 MAN B3324
SITE 2 BC3 6 HOH B4201 HOH B4204
SITE 1 BC4 3 NAG B3321 MAN B3323 MAN B3324
SITE 1 BC5 2 ARG A 281 MAN B3322
SITE 1 BC6 2 NAG B3321 MAN B3322
SITE 1 BC7 6 SER B 369 ASN B 371 SER B 398 GLU B 400
SITE 2 BC7 6 NAG B3099 NAG B3372
SITE 1 BC8 4 NAG B3371 MAN B3373 MAN B3375 MAN B3376
SITE 1 BC9 6 LEU A 332 SER A 344 NAG B3372 MAN B3374
SITE 2 BC9 6 MAN B3375 HOH B4205
SITE 1 CC1 5 ASN A 299 LEU A 332 SER A 396 GLU A 397
SITE 2 CC1 5 MAN B3373
SITE 1 CC2 6 ALA A 342 PRO A 343 NAG B3372 MAN B3373
SITE 2 CC2 6 MAN B3376 MAN B3377
SITE 1 CC3 6 SER A 344 LEU A 346 NAG B3372 MAN B3375
SITE 2 CC3 6 HOH B4206 HOH B4208
SITE 1 CC4 1 MAN B3375
SITE 1 CC5 3 ARG A 90 HOH A4391 HOH A4393
SITE 1 CC6 7 ASP B 126 ASP B 127 ASP B 251 ASN B 313
SITE 2 CC6 7 CA B2002 HOH B4196 HOH H4021
CRYST1 148.331 148.331 176.567 90.00 90.00 120.00 P 32 2 1 6
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 0.006742 0.003892 0.000000 0.00000
SCALE2 0.000000 0.007785 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005664 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
