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. 2.80 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) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.23 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3 REMARK 3 NUMBER OF REFLECTIONS : 51563 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) : 0.158 REMARK 3 R VALUE (WORKING SET) : 0.156 REMARK 3 FREE R VALUE : 0.204 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 2747 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) : 2.80 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.88 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3556 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2760 REMARK 3 BIN FREE R VALUE SET COUNT : 190 REMARK 3 BIN FREE R VALUE : 0.3470 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 10446 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 205 REMARK 3 SOLVENT ATOMS : 557 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) : 48.02 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.32000 REMARK 3 B22 (A**2) : 1.32000 REMARK 3 B33 (A**2) : -1.99000 REMARK 3 B12 (A**2) : 0.66000 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): 0.579 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.274 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.196 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.036 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10930 ; 0.006 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 7321 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14918 ; 0.988 ; 1.979 REMARK 3 BOND ANGLES OTHERS (DEGREES): 17798 ; 0.770 ; 3.004 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1375 ; 5.468 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 474 ;33.450 ;24.367 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1709 ;12.317 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 59 ;13.921 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1680 ; 0.061 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12178 ; 0.002 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 2152 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2025 ; 0.181 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 7483 ; 0.174 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5356 ; 0.171 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 5726 ; 0.080 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 521 ; 0.127 ; 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): 16 ; 0.104 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 53 ; 0.165 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 19 ; 0.112 ; 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): 7014 ; 1.677 ; 5.000 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10928 ; 2.702 ;10.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4553 ; 1.567 ; 5.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3977 ; 2.486 ;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): 133.0690 12.1600 78.4970 REMARK 3 T TENSOR REMARK 3 T11: -0.1785 T22: 0.0504 REMARK 3 T33: 0.0360 T12: 0.1509 REMARK 3 T13: -0.0454 T23: 0.3930 REMARK 3 L TENSOR REMARK 3 L11: 5.3750 L22: 8.6483 REMARK 3 L33: 2.8785 L12: -2.3624 REMARK 3 L13: 0.0495 L23: 2.2085 REMARK 3 S TENSOR REMARK 3 S11: 0.1002 S12: 0.0363 S13: -0.6719 REMARK 3 S21: 0.9044 S22: -0.4605 S23: -1.2706 REMARK 3 S31: 0.5267 S32: 0.8482 S33: 0.3604 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): 129.1270 21.5830 69.0850 REMARK 3 T TENSOR REMARK 3 T11: -0.1859 T22: 0.0273 REMARK 3 T33: -0.1243 T12: 0.0441 REMARK 3 T13: 0.0150 T23: 0.2365 REMARK 3 L TENSOR REMARK 3 L11: 3.8674 L22: 3.5417 REMARK 3 L33: 3.3466 L12: 0.5323 REMARK 3 L13: -0.4977 L23: 0.4667 REMARK 3 S TENSOR REMARK 3 S11: -0.0923 S12: -0.0516 S13: -0.1278 REMARK 3 S21: -0.0728 S22: -0.1415 S23: -0.4017 REMARK 3 S31: 0.1215 S32: 0.3962 S33: 0.2338 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): 118.6240 33.4510 64.5290 REMARK 3 T TENSOR REMARK 3 T11: -0.1027 T22: -0.0203 REMARK 3 T33: -0.0304 T12: -0.0561 REMARK 3 T13: -0.0160 T23: 0.1459 REMARK 3 L TENSOR REMARK 3 L11: 1.4535 L22: 1.3791 REMARK 3 L33: 1.7087 L12: -0.6441 REMARK 3 L13: -0.1526 L23: -1.0647 REMARK 3 S TENSOR REMARK 3 S11: -0.0081 S12: -0.0792 S13: 0.0914 REMARK 3 S21: 0.0890 S22: -0.1625 S23: -0.3784 REMARK 3 S31: 0.0419 S32: 0.3297 S33: 0.1706 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): 107.0350 35.9960 63.7770 REMARK 3 T TENSOR REMARK 3 T11: -0.0843 T22: -0.0087 REMARK 3 T33: -0.1198 T12: -0.1092 REMARK 3 T13: -0.0308 T23: 0.0871 REMARK 3 L TENSOR REMARK 3 L11: 4.4836 L22: 1.4638 REMARK 3 L33: 2.6104 L12: -0.1897 REMARK 3 L13: -2.0972 L23: -0.2311 REMARK 3 S TENSOR REMARK 3 S11: 0.0740 S12: -0.0332 S13: -0.1254 REMARK 3 S21: 0.0758 S22: -0.2023 S23: 0.2321 REMARK 3 S31: -0.0665 S32: -0.0686 S33: 0.1284 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): 106.0020 24.3650 64.1220 REMARK 3 T TENSOR REMARK 3 T11: -0.0762 T22: -0.0475 REMARK 3 T33: -0.0419 T12: -0.0889 REMARK 3 T13: 0.0044 T23: 0.0586 REMARK 3 L TENSOR REMARK 3 L11: 0.6330 L22: 1.5137 REMARK 3 L33: 2.9932 L12: -0.2184 REMARK 3 L13: -0.6197 L23: -1.0092 REMARK 3 S TENSOR REMARK 3 S11: 0.0352 S12: 0.2279 S13: -0.1223 REMARK 3 S21: 0.0101 S22: -0.1510 S23: 0.0540 REMARK 3 S31: 0.2412 S32: -0.2279 S33: 0.1158 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): 99.6470 13.0030 72.5440 REMARK 3 T TENSOR REMARK 3 T11: -0.0044 T22: -0.1718 REMARK 3 T33: -0.0534 T12: -0.1685 REMARK 3 T13: 0.0695 T23: 0.0688 REMARK 3 L TENSOR REMARK 3 L11: 2.4465 L22: 3.7954 REMARK 3 L33: 5.1675 L12: -0.9347 REMARK 3 L13: -0.3058 L23: 0.9602 REMARK 3 S TENSOR REMARK 3 S11: -0.0557 S12: 0.1869 S13: -0.3731 REMARK 3 S21: -0.0922 S22: -0.1533 S23: 0.0995 REMARK 3 S31: 0.1491 S32: -0.2706 S33: 0.2090 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): 107.7370 7.0990 84.5640 REMARK 3 T TENSOR REMARK 3 T11: 0.0223 T22: -0.2859 REMARK 3 T33: -0.0845 T12: -0.1026 REMARK 3 T13: 0.0496 T23: 0.1900 REMARK 3 L TENSOR REMARK 3 L11: 3.9057 L22: 5.2681 REMARK 3 L33: 4.9168 L12: -1.2266 REMARK 3 L13: -2.0852 L23: 2.4653 REMARK 3 S TENSOR REMARK 3 S11: -0.1696 S12: -0.2839 S13: -0.4264 REMARK 3 S21: 0.5635 S22: -0.0600 S23: 0.1427 REMARK 3 S31: 0.8740 S32: 0.0499 S33: 0.2296 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): 110.4340 2.8120 78.8920 REMARK 3 T TENSOR REMARK 3 T11: 0.1553 T22: -0.2789 REMARK 3 T33: -0.0902 T12: -0.0379 REMARK 3 T13: 0.0800 T23: 0.1978 REMARK 3 L TENSOR REMARK 3 L11: 3.1275 L22: 2.5921 REMARK 3 L33: 3.4108 L12: 0.4209 REMARK 3 L13: 0.1007 L23: 0.3809 REMARK 3 S TENSOR REMARK 3 S11: -0.1837 S12: 0.0120 S13: -0.3648 REMARK 3 S21: 0.0170 S22: -0.2326 S23: 0.0377 REMARK 3 S31: 0.9074 S32: -0.0394 S33: 0.4163 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): 124.3120 7.3840 80.2290 REMARK 3 T TENSOR REMARK 3 T11: 0.0044 T22: -0.1094 REMARK 3 T33: -0.0525 T12: 0.0789 REMARK 3 T13: 0.0232 T23: 0.2756 REMARK 3 L TENSOR REMARK 3 L11: 3.1197 L22: 2.3491 REMARK 3 L33: 2.8387 L12: 0.1586 REMARK 3 L13: -0.1203 L23: -0.5055 REMARK 3 S TENSOR REMARK 3 S11: -0.0731 S12: -0.2664 S13: -0.4662 REMARK 3 S21: 0.2293 S22: -0.2609 S23: -0.4038 REMARK 3 S31: 0.5759 S32: 0.5983 S33: 0.3339 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): 106.4150 21.3850 169.6260 REMARK 3 T TENSOR REMARK 3 T11: 0.3264 T22: -0.3717 REMARK 3 T33: -0.3740 T12: 0.1316 REMARK 3 T13: -0.1370 T23: -0.1472 REMARK 3 L TENSOR REMARK 3 L11: 4.1347 L22: 3.1839 REMARK 3 L33: 6.3418 L12: -1.6565 REMARK 3 L13: 2.1691 L23: -1.5740 REMARK 3 S TENSOR REMARK 3 S11: -0.1645 S12: -0.9077 S13: -0.0482 REMARK 3 S21: 1.0447 S22: 0.4577 S23: -0.2323 REMARK 3 S31: -0.6025 S32: -0.7964 S33: -0.2932 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): 102.8490 30.3390 149.4660 REMARK 3 T TENSOR REMARK 3 T11: 0.5938 T22: -0.1017 REMARK 3 T33: -0.2527 T12: 0.3005 REMARK 3 T13: 0.0271 T23: -0.0100 REMARK 3 L TENSOR REMARK 3 L11: 8.4990 L22: 10.5134 REMARK 3 L33: 38.3639 L12: -5.0049 REMARK 3 L13: 16.4455 L23: -16.7198 REMARK 3 S TENSOR REMARK 3 S11: -0.7776 S12: -0.7572 S13: 0.3265 REMARK 3 S21: 1.1927 S22: 0.6227 S23: -0.6324 REMARK 3 S31: -2.8502 S32: -1.5784 S33: 0.1549 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): 97.4680 38.1930 104.5680 REMARK 3 T TENSOR REMARK 3 T11: 0.2698 T22: -0.0311 REMARK 3 T33: -0.1119 T12: -0.1916 REMARK 3 T13: 0.0765 T23: 0.0206 REMARK 3 L TENSOR REMARK 3 L11: 0.2858 L22: 0.3609 REMARK 3 L33: 1.9942 L12: -0.2502 REMARK 3 L13: 0.2527 L23: -0.7224 REMARK 3 S TENSOR REMARK 3 S11: -0.0194 S12: -0.1443 S13: 0.0050 REMARK 3 S21: 0.4069 S22: 0.0092 S23: -0.0162 REMARK 3 S31: -0.4653 S32: 0.0500 S33: 0.0102 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): 102.9420 34.2690 96.2710 REMARK 3 T TENSOR REMARK 3 T11: 0.0616 T22: -0.0771 REMARK 3 T33: -0.1866 T12: -0.1855 REMARK 3 T13: 0.0258 T23: 0.0579 REMARK 3 L TENSOR REMARK 3 L11: 1.6648 L22: 1.6436 REMARK 3 L33: 2.3486 L12: -0.5337 REMARK 3 L13: -0.9118 L23: 0.0623 REMARK 3 S TENSOR REMARK 3 S11: 0.0554 S12: -0.3395 S13: 0.0796 REMARK 3 S21: 0.4529 S22: -0.0567 S23: -0.0784 REMARK 3 S31: -0.1301 S32: 0.2086 S33: 0.0012 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): 100.1960 22.6550 131.2830 REMARK 3 T TENSOR REMARK 3 T11: 0.1223 T22: -0.0895 REMARK 3 T33: -0.1368 T12: -0.0782 REMARK 3 T13: 0.1566 T23: 0.0112 REMARK 3 L TENSOR REMARK 3 L11: 2.7817 L22: 3.2226 REMARK 3 L33: 21.2278 L12: -1.8031 REMARK 3 L13: 7.6309 L23: -4.1690 REMARK 3 S TENSOR REMARK 3 S11: 0.6376 S12: 0.6941 S13: -0.5921 REMARK 3 S21: -0.1773 S22: 0.3031 S23: -0.0403 REMARK 3 S31: 1.0732 S32: 0.7841 S33: -0.9407 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): 109.3310 28.2480 149.4790 REMARK 3 T TENSOR REMARK 3 T11: 0.2681 T22: -0.4009 REMARK 3 T33: -0.2949 T12: -0.0832 REMARK 3 T13: -0.0198 T23: -0.0295 REMARK 3 L TENSOR REMARK 3 L11: 5.1708 L22: 2.1877 REMARK 3 L33: 20.4062 L12: -1.8739 REMARK 3 L13: 7.3523 L23: -2.0611 REMARK 3 S TENSOR REMARK 3 S11: -0.4202 S12: 0.8589 S13: 0.2560 REMARK 3 S21: 0.7676 S22: 0.4524 S23: -0.5348 REMARK 3 S31: -1.8752 S32: 1.6414 S33: -0.0322 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): 119.2080 31.4000 183.5950 REMARK 3 T TENSOR REMARK 3 T11: 1.6845 T22: 0.7793 REMARK 3 T33: 0.6585 T12: -0.0647 REMARK 3 T13: -0.7679 T23: -0.0324 REMARK 3 L TENSOR REMARK 3 L11: 3.3604 L22: 0.0157 REMARK 3 L33: 6.2798 L12: -0.2296 REMARK 3 L13: -4.5938 L23: 0.3138 REMARK 3 S TENSOR REMARK 3 S11: -1.5493 S12: -1.8097 S13: 0.5720 REMARK 3 S21: -0.1441 S22: -0.2731 S23: -0.6768 REMARK 3 S31: -2.6711 S32: 3.2783 S33: 1.8223 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): 89.7310 36.5670 33.4360 REMARK 3 T TENSOR REMARK 3 T11: -0.0172 T22: 0.0501 REMARK 3 T33: -0.1278 T12: -0.1955 REMARK 3 T13: -0.1387 T23: 0.0263 REMARK 3 L TENSOR REMARK 3 L11: 7.3175 L22: 8.3579 REMARK 3 L33: 10.4725 L12: -4.7524 REMARK 3 L13: 6.0528 L23: -8.2046 REMARK 3 S TENSOR REMARK 3 S11: 0.1507 S12: 0.4785 S13: -0.6326 REMARK 3 S21: -0.6786 S22: -0.0684 S23: 0.3654 REMARK 3 S31: 1.0500 S32: -0.2618 S33: -0.0823 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): 93.9370 41.9070 41.4650 REMARK 3 T TENSOR REMARK 3 T11: -0.1957 T22: -0.0093 REMARK 3 T33: -0.0769 T12: -0.0497 REMARK 3 T13: -0.0161 T23: 0.0877 REMARK 3 L TENSOR REMARK 3 L11: 3.6793 L22: 2.3880 REMARK 3 L33: 2.8221 L12: -0.6181 REMARK 3 L13: 0.5816 L23: -0.0642 REMARK 3 S TENSOR REMARK 3 S11: -0.0116 S12: -0.0921 S13: -0.0013 REMARK 3 S21: 0.0963 S22: 0.1119 S23: 0.2024 REMARK 3 S31: 0.2083 S32: -0.3511 S33: -0.1003 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): 93.7630 42.7960 43.7020 REMARK 3 T TENSOR REMARK 3 T11: -0.1959 T22: 0.0085 REMARK 3 T33: -0.0572 T12: -0.0615 REMARK 3 T13: 0.0169 T23: 0.0916 REMARK 3 L TENSOR REMARK 3 L11: 3.4141 L22: 1.5081 REMARK 3 L33: 3.6057 L12: -0.5171 REMARK 3 L13: 1.6828 L23: -1.1660 REMARK 3 S TENSOR REMARK 3 S11: -0.0835 S12: -0.1248 S13: 0.1779 REMARK 3 S21: -0.0378 S22: 0.0488 S23: 0.0974 REMARK 3 S31: 0.1721 S32: -0.1946 S33: 0.0347 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): 86.1570 47.4620 13.1750 REMARK 3 T TENSOR REMARK 3 T11: -0.2719 T22: 0.1291 REMARK 3 T33: -0.0047 T12: -0.1559 REMARK 3 T13: -0.1212 T23: 0.0679 REMARK 3 L TENSOR REMARK 3 L11: 2.7787 L22: 1.9303 REMARK 3 L33: 3.4840 L12: -2.0125 REMARK 3 L13: -0.9340 L23: 1.9006 REMARK 3 S TENSOR REMARK 3 S11: 0.1384 S12: 0.1929 S13: -0.4538 REMARK 3 S21: 0.0418 S22: 0.0025 S23: 0.0133 REMARK 3 S31: -0.5796 S32: -1.0782 S33: -0.1409 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): 92.2880 44.5370 4.8800 REMARK 3 T TENSOR REMARK 3 T11: -0.1725 T22: -0.1351 REMARK 3 T33: -0.1671 T12: 0.0780 REMARK 3 T13: -0.1611 T23: 0.0649 REMARK 3 L TENSOR REMARK 3 L11: 8.1673 L22: 1.5066 REMARK 3 L33: 14.9147 L12: 0.7462 REMARK 3 L13: -6.6127 L23: 0.8251 REMARK 3 S TENSOR REMARK 3 S11: 0.2405 S12: 0.1712 S13: -0.4571 REMARK 3 S21: -0.1950 S22: 0.0166 S23: -0.1318 REMARK 3 S31: 1.3225 S32: -0.2606 S33: -0.2571 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): 94.3030 47.3030 9.4270 REMARK 3 T TENSOR REMARK 3 T11: -0.1524 T22: -0.1546 REMARK 3 T33: -0.2672 T12: 0.0947 REMARK 3 T13: -0.0659 T23: 0.0576 REMARK 3 L TENSOR REMARK 3 L11: 5.5770 L22: 1.3309 REMARK 3 L33: 14.6915 L12: 1.1195 REMARK 3 L13: -2.0782 L23: 0.0700 REMARK 3 S TENSOR REMARK 3 S11: 0.3327 S12: -0.3330 S13: 0.1400 REMARK 3 S21: -0.4781 S22: 0.0059 S23: 0.1540 REMARK 3 S31: 0.5629 S32: 0.3316 S33: -0.3386 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): 93.6610 40.3190 -3.5120 REMARK 3 T TENSOR REMARK 3 T11: 0.4975 T22: 0.0628 REMARK 3 T33: -0.0634 T12: 0.3075 REMARK 3 T13: -0.1417 T23: -0.1007 REMARK 3 L TENSOR REMARK 3 L11: 8.5970 L22: 1.3351 REMARK 3 L33: 4.3298 L12: -0.1422 REMARK 3 L13: -1.6085 L23: 1.2356 REMARK 3 S TENSOR REMARK 3 S11: 0.6915 S12: 0.0794 S13: -1.5153 REMARK 3 S21: -0.7848 S22: -0.5788 S23: 0.0704 REMARK 3 S31: 0.8112 S32: 1.2039 S33: -0.1127 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): 85.9060 43.9930 -2.2810 REMARK 3 T TENSOR REMARK 3 T11: -0.2611 T22: 0.1164 REMARK 3 T33: -0.1512 T12: -0.0110 REMARK 3 T13: -0.3487 T23: -0.0377 REMARK 3 L TENSOR REMARK 3 L11: 11.9463 L22: 11.0363 REMARK 3 L33: 26.3478 L12: 6.4023 REMARK 3 L13: -17.4415 L23: -6.7556 REMARK 3 S TENSOR REMARK 3 S11: -0.6070 S12: 0.6738 S13: -0.6419 REMARK 3 S21: -1.4601 S22: 0.4788 S23: 0.5999 REMARK 3 S31: 2.1393 S32: -1.7296 S33: 0.1282 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): 114.1110 49.9240 35.3410 REMARK 3 T TENSOR REMARK 3 T11: -0.1448 T22: 0.0275 REMARK 3 T33: 0.0038 T12: 0.0487 REMARK 3 T13: 0.0484 T23: 0.1657 REMARK 3 L TENSOR REMARK 3 L11: 1.6173 L22: 0.7314 REMARK 3 L33: 2.4751 L12: 0.5313 REMARK 3 L13: -0.1080 L23: 0.4539 REMARK 3 S TENSOR REMARK 3 S11: 0.1224 S12: 0.1503 S13: 0.2079 REMARK 3 S21: -0.0825 S22: -0.0736 S23: -0.0461 REMARK 3 S31: -0.2068 S32: 0.2741 S33: -0.0488 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): 113.3850 38.9760 36.4110 REMARK 3 T TENSOR REMARK 3 T11: -0.1109 T22: -0.0153 REMARK 3 T33: -0.0673 T12: 0.0530 REMARK 3 T13: 0.0000 T23: 0.0381 REMARK 3 L TENSOR REMARK 3 L11: 5.7369 L22: 2.2959 REMARK 3 L33: 4.0459 L12: 1.4300 REMARK 3 L13: 0.0299 L23: -1.5042 REMARK 3 S TENSOR REMARK 3 S11: 0.0381 S12: 0.3908 S13: -0.3509 REMARK 3 S21: -0.1819 S22: 0.0470 S23: -0.0521 REMARK 3 S31: 0.7805 S32: 0.2280 S33: -0.0851 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): 112.2070 45.4970 35.8190 REMARK 3 T TENSOR REMARK 3 T11: -0.1484 T22: -0.0428 REMARK 3 T33: -0.0533 T12: 0.0151 REMARK 3 T13: -0.0583 T23: 0.1187 REMARK 3 L TENSOR REMARK 3 L11: 4.6233 L22: 1.8136 REMARK 3 L33: 6.5969 L12: -0.5726 REMARK 3 L13: -2.2635 L23: 0.4388 REMARK 3 S TENSOR REMARK 3 S11: -0.0520 S12: 0.3054 S13: -0.0968 REMARK 3 S21: -0.0765 S22: -0.0371 S23: 0.0860 REMARK 3 S31: 0.3511 S32: -0.0137 S33: 0.0891 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): 100.2590 52.9530 8.3390 REMARK 3 T TENSOR REMARK 3 T11: -0.1465 T22: 0.2390 REMARK 3 T33: -0.0864 T12: 0.0824 REMARK 3 T13: 0.0171 T23: 0.0899 REMARK 3 L TENSOR REMARK 3 L11: 1.8825 L22: 3.0048 REMARK 3 L33: 6.5979 L12: -2.0081 REMARK 3 L13: 3.3815 L23: -2.9352 REMARK 3 S TENSOR REMARK 3 S11: 0.5267 S12: 0.2634 S13: -0.3226 REMARK 3 S21: -0.4485 S22: -0.2840 S23: 0.1670 REMARK 3 S31: 0.7147 S32: 0.2319 S33: -0.2426 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): 101.4740 59.5600 9.0220 REMARK 3 T TENSOR REMARK 3 T11: -0.2253 T22: 0.2441 REMARK 3 T33: -0.2343 T12: 0.0376 REMARK 3 T13: -0.0148 T23: 0.0669 REMARK 3 L TENSOR REMARK 3 L11: 6.7928 L22: 7.7301 REMARK 3 L33: 2.4874 L12: -4.7425 REMARK 3 L13: 2.8914 L23: -2.1068 REMARK 3 S TENSOR REMARK 3 S11: 0.0030 S12: -0.2065 S13: 0.5781 REMARK 3 S21: 0.0780 S22: -0.2879 S23: -0.4460 REMARK 3 S31: -0.0240 S32: 0.2947 S33: 0.2849 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): 95.0250 59.9230 3.1640 REMARK 3 T TENSOR REMARK 3 T11: -0.2568 T22: 0.1091 REMARK 3 T33: -0.1990 T12: 0.0406 REMARK 3 T13: 0.0296 T23: 0.0185 REMARK 3 L TENSOR REMARK 3 L11: 9.0169 L22: 3.7924 REMARK 3 L33: 5.9187 L12: -3.6192 REMARK 3 L13: 4.4036 L23: -2.1424 REMARK 3 S TENSOR REMARK 3 S11: -0.0098 S12: 0.2426 S13: 0.2185 REMARK 3 S21: -0.2741 S22: -0.1478 S23: -0.0086 REMARK 3 S31: -0.0331 S32: 0.1472 S33: 0.1577 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): 102.9160 62.2880 -1.9010 REMARK 3 T TENSOR REMARK 3 T11: -0.2516 T22: 0.2085 REMARK 3 T33: -0.2139 T12: 0.1333 REMARK 3 T13: 0.0801 T23: 0.1488 REMARK 3 L TENSOR REMARK 3 L11: 17.6041 L22: 6.7983 REMARK 3 L33: 5.6105 L12: -6.6274 REMARK 3 L13: 6.1128 L23: -4.5203 REMARK 3 S TENSOR REMARK 3 S11: 0.5004 S12: 1.4644 S13: -0.1356 REMARK 3 S21: -0.5864 S22: -0.5404 S23: -0.1399 REMARK 3 S31: -0.0577 S32: 1.0525 S33: 0.0400 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 : 1.20 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 2VDP 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-34116. 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 : 55536 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 (%) : 99.4 REMARK 200 DATA REDUNDANCY : 6.5 REMARK 200 R MERGE (I) : 0.11 REMARK 200 R SYM (I) : NULL REMARK 200 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 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 118.10667 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 59.05333 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 59.05333 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 118.10667 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: 11720 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 72080 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.4 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 LEU C 402 REMARK 465 GLY C 403 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 4054 O HOH A 4138 2.09 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 -124.95 57.37 REMARK 500 LYS A 118 -120.64 54.01 REMARK 500 GLU A 123 131.39 95.90 REMARK 500 LEU A 212 -47.91 70.94 REMARK 500 SER A 261 73.01 52.65 REMARK 500 THR A 296 138.86 -171.68 REMARK 500 THR B 7 44.43 -97.90 REMARK 500 ASP B 47 33.83 -97.44 REMARK 500 VAL B 80 96.25 67.48 REMARK 500 ASP B 95 -2.36 62.04 REMARK 500 ASN B 148 30.72 -91.73 REMARK 500 VAL B 157 -82.97 -127.51 REMARK 500 SER B 213 -154.33 -116.15 REMARK 500 LEU B 258 -8.34 82.77 REMARK 500 VAL B 275 -79.59 -99.04 REMARK 500 ALA B 309 79.01 -106.93 REMARK 500 CYS B 374 -155.17 -92.48 REMARK 500 LYS B 410 -23.84 73.48 REMARK 500 GLU B 442 81.99 60.40 REMARK 500 HIS B 446 -61.38 70.66 REMARK 500 THR B 454 164.32 69.90 REMARK 500 GLN C 407 76.95 -118.96 REMARK 500 ASP H 179 -6.23 72.94 REMARK 500 SER L 30 57.70 34.59 REMARK 500 SER L 77 74.38 52.02 REMARK 500 ASN L 212 77.51 51.55 REMARK 500 GLU L 213 77.21 -153.08 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 51.7 REMARK 620 3 ASP A 245 OD2 124.0 72.7 REMARK 620 4 ASP A 247 O 79.4 76.1 95.7 REMARK 620 5 THR A 250 O 72.0 121.8 163.1 80.9 REMARK 620 6 THR A 250 OG1 143.1 143.1 86.1 76.4 77.0 REMARK 620 7 GLU A 252 OE1 81.6 86.4 88.8 159.6 100.1 123.8 REMARK 620 8 GLU A 252 OE2 128.4 129.9 80.0 149.0 94.3 72.7 51.3 REMARK 620 N 1 2 3 4 5 6 7 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A2005 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN A 299 OD1 REMARK 620 2 ASP A 301 OD1 79.3 REMARK 620 3 ASP A 297 OD1 84.0 76.7 REMARK 620 4 ARG A 303 O 164.6 92.3 81.4 REMARK 620 5 ASP A 305 OD1 113.2 150.3 129.7 80.3 REMARK 620 6 ASP A 305 OD2 85.5 159.2 87.8 99.0 49.9 REMARK 620 7 HOH A4187 O 102.3 77.9 152.1 88.4 73.2 119.6 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 80.7 REMARK 620 3 TYR A 371 O 79.1 80.7 REMARK 620 4 ASP A 367 OD1 94.1 99.9 173.0 REMARK 620 5 HOH A4200 O 148.2 69.2 86.1 100.8 REMARK 620 6 ASP A 373 OD1 99.9 177.5 101.8 77.6 110.7 REMARK 620 7 ASP A 373 OD2 134.7 132.1 77.6 106.6 67.1 49.0 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 87.8 REMARK 620 3 ASP A 426 OD1 73.4 78.0 REMARK 620 4 ASP A 428 OD1 146.5 84.9 73.1 REMARK 620 5 ASP A 434 OD1 106.8 160.9 94.0 76.1 REMARK 620 6 ASP A 434 OD2 89.4 142.6 136.2 115.5 52.1 REMARK 620 7 HOH A4218 O 140.3 84.4 141.5 71.4 91.5 74.3 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 O2 REMARK 620 2 HOH C4006 O 96.3 REMARK 620 3 ASP B 251 OD2 123.6 106.0 REMARK 620 4 GOL B1462 O1 63.6 74.2 73.7 REMARK 620 5 SER B 123 O 158.7 87.0 75.0 136.9 REMARK 620 6 ASP B 126 OD1 83.4 94.1 142.9 142.8 75.4 REMARK 620 7 ASP B 127 OD1 81.4 169.7 83.5 113.1 91.7 75.7 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 158 OD2 REMARK 620 2 ASN B 215 OD1 100.0 REMARK 620 3 ASP B 217 O 158.7 96.5 REMARK 620 4 ASP B 217 OD1 90.7 91.6 75.4 REMARK 620 5 PRO B 219 O 80.4 173.8 84.7 94.6 REMARK 620 6 GLU B 220 OE2 101.4 87.0 92.7 167.8 86.8 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 HOH B4046 O REMARK 620 2 SER B 123 OG 90.3 REMARK 620 3 GLU B 220 OE1 83.7 166.2 REMARK 620 4 HOH B4012 O 94.7 86.9 105.9 REMARK 620 5 ASP C 410 OD1 91.3 77.5 90.1 163.4 REMARK 620 6 SER B 121 OG 174.6 94.7 91.0 87.7 87.8 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: 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