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. 2.75 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) : 2.75 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.99 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 95.1 REMARK 3 NUMBER OF REFLECTIONS : 53440 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) : 0.146 REMARK 3 R VALUE (WORKING SET) : 0.144 REMARK 3 FREE R VALUE : 0.191 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 2856 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) : 2.75 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.82 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3521 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2240 REMARK 3 BIN FREE R VALUE SET COUNT : 199 REMARK 3 BIN FREE R VALUE : 0.2880 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 10461 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 210 REMARK 3 SOLVENT ATOMS : 1129 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) : 36.91 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.26000 REMARK 3 B22 (A**2) : 1.26000 REMARK 3 B33 (A**2) : -1.89000 REMARK 3 B12 (A**2) : 0.63000 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): 0.562 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.256 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.167 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.066 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10960 ; 0.006 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 7349 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14972 ; 0.997 ; 1.979 REMARK 3 BOND ANGLES OTHERS (DEGREES): 17890 ; 0.767 ; 3.003 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1384 ; 5.498 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 476 ;32.846 ;24.286 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1725 ;12.280 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 61 ;14.624 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1686 ; 0.061 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12214 ; 0.002 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 2166 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2133 ; 0.182 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 7843 ; 0.175 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5316 ; 0.173 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 5753 ; 0.079 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 940 ; 0.135 ; 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): 22 ; 0.114 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 87 ; 0.172 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 37 ; 0.109 ; 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): 7018 ; 1.611 ; 5.000 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10945 ; 2.584 ;10.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4585 ; 1.593 ; 5.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4008 ; 2.497 ;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): 133.4480 12.4440 78.2360 REMARK 3 T TENSOR REMARK 3 T11: -0.1756 T22: 0.0682 REMARK 3 T33: -0.0983 T12: 0.1333 REMARK 3 T13: -0.0017 T23: 0.3306 REMARK 3 L TENSOR REMARK 3 L11: 8.2770 L22: 3.4378 REMARK 3 L33: 5.5052 L12: -3.1666 REMARK 3 L13: 0.3709 L23: -3.0986 REMARK 3 S TENSOR REMARK 3 S11: -0.0173 S12: 0.1942 S13: -0.4221 REMARK 3 S21: 0.4774 S22: -0.4391 S23: -1.3105 REMARK 3 S31: 0.9249 S32: 0.9499 S33: 0.4564 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): 129.4650 22.0450 68.8660 REMARK 3 T TENSOR REMARK 3 T11: -0.1885 T22: 0.0341 REMARK 3 T33: -0.0784 T12: 0.0526 REMARK 3 T13: 0.0168 T23: 0.2750 REMARK 3 L TENSOR REMARK 3 L11: 3.2149 L22: 3.7111 REMARK 3 L33: 2.9137 L12: 0.5069 REMARK 3 L13: -0.6259 L23: 0.5182 REMARK 3 S TENSOR REMARK 3 S11: -0.0669 S12: -0.1233 S13: -0.2335 REMARK 3 S21: -0.1148 S22: -0.1989 S23: -0.4937 REMARK 3 S31: 0.2182 S32: 0.3432 S33: 0.2658 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): 118.9410 33.7800 64.2700 REMARK 3 T TENSOR REMARK 3 T11: -0.1263 T22: 0.0134 REMARK 3 T33: -0.0020 T12: -0.0584 REMARK 3 T13: -0.0334 T23: 0.1512 REMARK 3 L TENSOR REMARK 3 L11: 0.6496 L22: 1.4775 REMARK 3 L33: 1.5406 L12: -0.4853 REMARK 3 L13: -0.5024 L23: -0.4728 REMARK 3 S TENSOR REMARK 3 S11: -0.0197 S12: -0.1339 S13: -0.0201 REMARK 3 S21: 0.1673 S22: -0.1461 S23: -0.3157 REMARK 3 S31: -0.0122 S32: 0.4246 S33: 0.1658 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): 107.3550 36.2950 63.5570 REMARK 3 T TENSOR REMARK 3 T11: -0.1032 T22: -0.0462 REMARK 3 T33: -0.1024 T12: -0.0794 REMARK 3 T13: -0.0429 T23: 0.0956 REMARK 3 L TENSOR REMARK 3 L11: 3.8324 L22: 1.7169 REMARK 3 L33: 2.8825 L12: -0.2806 REMARK 3 L13: -1.7908 L23: -0.0730 REMARK 3 S TENSOR REMARK 3 S11: 0.0556 S12: -0.0854 S13: -0.2132 REMARK 3 S21: -0.0749 S22: -0.2028 S23: 0.2063 REMARK 3 S31: -0.0167 S32: -0.0226 S33: 0.1472 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): 106.3390 24.6580 63.8120 REMARK 3 T TENSOR REMARK 3 T11: -0.0658 T22: -0.0549 REMARK 3 T33: -0.0443 T12: -0.0636 REMARK 3 T13: -0.0055 T23: 0.0767 REMARK 3 L TENSOR REMARK 3 L11: 1.2883 L22: 1.4837 REMARK 3 L33: 1.3090 L12: -0.0540 REMARK 3 L13: -0.7534 L23: -0.5347 REMARK 3 S TENSOR REMARK 3 S11: 0.0104 S12: 0.1658 S13: -0.0821 REMARK 3 S21: 0.0048 S22: -0.0978 S23: -0.0382 REMARK 3 S31: 0.2894 S32: -0.1506 S33: 0.0873 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): 100.0560 13.2450 72.1500 REMARK 3 T TENSOR REMARK 3 T11: -0.0254 T22: -0.1757 REMARK 3 T33: -0.0391 T12: -0.1106 REMARK 3 T13: 0.0759 T23: 0.0736 REMARK 3 L TENSOR REMARK 3 L11: 2.2491 L22: 2.6851 REMARK 3 L33: 3.5651 L12: -0.1755 REMARK 3 L13: -0.3379 L23: 0.5707 REMARK 3 S TENSOR REMARK 3 S11: -0.0595 S12: 0.1045 S13: -0.2600 REMARK 3 S21: -0.0256 S22: -0.1517 S23: 0.1196 REMARK 3 S31: 0.2357 S32: -0.2381 S33: 0.2111 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): 108.1080 7.2930 84.1810 REMARK 3 T TENSOR REMARK 3 T11: -0.0276 T22: -0.3071 REMARK 3 T33: -0.0622 T12: -0.0640 REMARK 3 T13: 0.0861 T23: 0.2221 REMARK 3 L TENSOR REMARK 3 L11: 3.8946 L22: 6.2146 REMARK 3 L33: 7.3394 L12: -0.2963 REMARK 3 L13: -0.9735 L23: 3.4506 REMARK 3 S TENSOR REMARK 3 S11: -0.1523 S12: -0.2746 S13: -0.4420 REMARK 3 S21: 0.4741 S22: 0.0389 S23: 0.1051 REMARK 3 S31: 0.7217 S32: 0.1704 S33: 0.1134 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): 110.6780 2.9350 78.3060 REMARK 3 T TENSOR REMARK 3 T11: 0.1013 T22: -0.2549 REMARK 3 T33: -0.1025 T12: 0.0026 REMARK 3 T13: 0.0765 T23: 0.1982 REMARK 3 L TENSOR REMARK 3 L11: 2.8336 L22: 3.8076 REMARK 3 L33: 3.8208 L12: -0.4342 REMARK 3 L13: -0.8807 L23: 1.9030 REMARK 3 S TENSOR REMARK 3 S11: -0.1510 S12: 0.1308 S13: -0.2462 REMARK 3 S21: -0.0649 S22: -0.2816 S23: -0.0141 REMARK 3 S31: 0.7446 S32: 0.1146 S33: 0.4326 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): 124.6960 7.6970 79.9100 REMARK 3 T TENSOR REMARK 3 T11: -0.0191 T22: -0.1026 REMARK 3 T33: -0.0076 T12: 0.1149 REMARK 3 T13: 0.0303 T23: 0.2968 REMARK 3 L TENSOR REMARK 3 L11: 2.5948 L22: 2.5703 REMARK 3 L33: 2.7992 L12: 0.1463 REMARK 3 L13: -0.3990 L23: -0.0499 REMARK 3 S TENSOR REMARK 3 S11: -0.0165 S12: -0.1946 S13: -0.4404 REMARK 3 S21: 0.2131 S22: -0.3230 S23: -0.4663 REMARK 3 S31: 0.5102 S32: 0.6137 S33: 0.3395 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): 106.8630 21.1360 169.0610 REMARK 3 T TENSOR REMARK 3 T11: 0.4710 T22: -0.4175 REMARK 3 T33: -0.3736 T12: 0.0598 REMARK 3 T13: -0.1659 T23: -0.0937 REMARK 3 L TENSOR REMARK 3 L11: 4.0997 L22: 3.3231 REMARK 3 L33: 7.8111 L12: -2.1837 REMARK 3 L13: 2.6257 L23: -2.9229 REMARK 3 S TENSOR REMARK 3 S11: -0.2156 S12: -0.7802 S13: -0.0129 REMARK 3 S21: 1.0421 S22: 0.4400 S23: -0.2005 REMARK 3 S31: -0.9491 S32: -0.7747 S33: -0.2244 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 78 B 98 REMARK 3 ORIGIN FOR THE GROUP (A): 103.1230 30.1390 148.9770 REMARK 3 T TENSOR REMARK 3 T11: 0.7139 T22: -0.1714 REMARK 3 T33: -0.2518 T12: 0.2049 REMARK 3 T13: -0.0194 T23: -0.0105 REMARK 3 L TENSOR REMARK 3 L11: 9.8554 L22: 7.2095 REMARK 3 L33: 38.2042 L12: -4.4166 REMARK 3 L13: 16.5641 L23: -14.7858 REMARK 3 S TENSOR REMARK 3 S11: -0.8453 S12: -0.6184 S13: 0.6063 REMARK 3 S21: 1.1989 S22: 0.3624 S23: -0.5616 REMARK 3 S31: -2.9152 S32: -1.5318 S33: 0.4828 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): 97.6850 38.2560 104.2300 REMARK 3 T TENSOR REMARK 3 T11: 0.1644 T22: -0.0596 REMARK 3 T33: -0.1239 T12: -0.1686 REMARK 3 T13: 0.0413 T23: 0.0403 REMARK 3 L TENSOR REMARK 3 L11: 0.5255 L22: 0.5307 REMARK 3 L33: 2.8991 L12: -0.0459 REMARK 3 L13: -0.4335 L23: -1.1191 REMARK 3 S TENSOR REMARK 3 S11: 0.0017 S12: -0.1184 S13: 0.0116 REMARK 3 S21: 0.3632 S22: -0.0205 S23: 0.0084 REMARK 3 S31: -0.4546 S32: 0.0937 S33: 0.0188 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): 103.2000 34.3920 95.9580 REMARK 3 T TENSOR REMARK 3 T11: 0.0055 T22: -0.0804 REMARK 3 T33: -0.1513 T12: -0.1414 REMARK 3 T13: -0.0070 T23: 0.0843 REMARK 3 L TENSOR REMARK 3 L11: 1.7190 L22: 1.4292 REMARK 3 L33: 1.9033 L12: -0.2640 REMARK 3 L13: -0.9250 L23: 0.0035 REMARK 3 S TENSOR REMARK 3 S11: 0.0167 S12: -0.2567 S13: -0.0075 REMARK 3 S21: 0.3687 S22: -0.0968 S23: -0.1372 REMARK 3 S31: -0.0556 S32: 0.1618 S33: 0.0801 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): 100.3770 22.6130 130.7940 REMARK 3 T TENSOR REMARK 3 T11: 0.1440 T22: -0.1938 REMARK 3 T33: -0.1672 T12: -0.0449 REMARK 3 T13: 0.0628 T23: 0.0107 REMARK 3 L TENSOR REMARK 3 L11: 2.8352 L22: 3.2159 REMARK 3 L33: 21.5841 L12: -2.0142 REMARK 3 L13: 7.8112 L23: -5.2121 REMARK 3 S TENSOR REMARK 3 S11: 0.6442 S12: 0.4442 S13: -0.4782 REMARK 3 S21: -0.2629 S22: 0.1397 S23: -0.0388 REMARK 3 S31: 1.5513 S32: 0.4544 S33: -0.7839 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): 109.5360 28.1050 148.9570 REMARK 3 T TENSOR REMARK 3 T11: 0.3224 T22: -0.4391 REMARK 3 T33: -0.2543 T12: -0.1263 REMARK 3 T13: -0.0445 T23: 0.0600 REMARK 3 L TENSOR REMARK 3 L11: 4.6347 L22: 2.3749 REMARK 3 L33: 21.3191 L12: -1.6700 REMARK 3 L13: 7.3714 L23: -1.4969 REMARK 3 S TENSOR REMARK 3 S11: -0.2175 S12: 0.6241 S13: 0.2653 REMARK 3 S21: 0.8418 S22: 0.3000 S23: -0.5600 REMARK 3 S31: -1.6418 S32: 1.3732 S33: -0.0825 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): 119.4190 31.2240 182.9780 REMARK 3 T TENSOR REMARK 3 T11: 1.8950 T22: 1.2423 REMARK 3 T33: 1.0367 T12: -0.0741 REMARK 3 T13: -0.7764 T23: -0.2894 REMARK 3 L TENSOR REMARK 3 L11: 0.3997 L22: 1.9223 REMARK 3 L33: 7.1076 L12: 0.8765 REMARK 3 L13: -1.6854 L23: -3.6963 REMARK 3 S TENSOR REMARK 3 S11: 0.0493 S12: -2.5590 S13: 1.5405 REMARK 3 S21: -0.0851 S22: -0.2903 S23: -0.5016 REMARK 3 S31: -1.6858 S32: 3.4624 S33: 0.2410 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): 90.0950 36.8750 33.2610 REMARK 3 T TENSOR REMARK 3 T11: -0.0455 T22: -0.0111 REMARK 3 T33: -0.0442 T12: -0.2050 REMARK 3 T13: -0.0025 T23: 0.0014 REMARK 3 L TENSOR REMARK 3 L11: 9.3653 L22: 7.9854 REMARK 3 L33: 10.6333 L12: -6.4844 REMARK 3 L13: 7.7869 L23: -6.5637 REMARK 3 S TENSOR REMARK 3 S11: 0.4278 S12: 0.2920 S13: -0.8284 REMARK 3 S21: -0.9524 S22: 0.0172 S23: 0.3480 REMARK 3 S31: 0.9204 S32: -0.0049 S33: -0.4450 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): 94.2650 42.2440 41.2560 REMARK 3 T TENSOR REMARK 3 T11: -0.1646 T22: -0.0201 REMARK 3 T33: -0.0857 T12: -0.0586 REMARK 3 T13: -0.0100 T23: 0.0547 REMARK 3 L TENSOR REMARK 3 L11: 3.0779 L22: 1.6746 REMARK 3 L33: 2.7407 L12: -0.5306 REMARK 3 L13: 1.5035 L23: -0.1858 REMARK 3 S TENSOR REMARK 3 S11: -0.0010 S12: -0.1711 S13: -0.0180 REMARK 3 S21: 0.0974 S22: -0.0130 S23: 0.1166 REMARK 3 S31: 0.2336 S32: -0.1644 S33: 0.0140 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): 94.0930 43.1090 43.4950 REMARK 3 T TENSOR REMARK 3 T11: -0.1560 T22: -0.0532 REMARK 3 T33: -0.0198 T12: -0.0542 REMARK 3 T13: -0.0028 T23: 0.0515 REMARK 3 L TENSOR REMARK 3 L11: 3.0131 L22: 0.4930 REMARK 3 L33: 3.4497 L12: -0.1166 REMARK 3 L13: 1.0781 L23: -1.1469 REMARK 3 S TENSOR REMARK 3 S11: -0.0849 S12: -0.1109 S13: 0.1063 REMARK 3 S21: -0.0234 S22: 0.0512 S23: 0.0495 REMARK 3 S31: 0.1767 S32: -0.2434 S33: 0.0336 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): 86.4970 47.8270 12.7870 REMARK 3 T TENSOR REMARK 3 T11: -0.1988 T22: -0.0003 REMARK 3 T33: -0.0634 T12: -0.0961 REMARK 3 T13: -0.0877 T23: 0.0493 REMARK 3 L TENSOR REMARK 3 L11: 2.3774 L22: 0.6648 REMARK 3 L33: 5.0433 L12: -0.7257 REMARK 3 L13: -1.0720 L23: 0.7615 REMARK 3 S TENSOR REMARK 3 S11: 0.1390 S12: 0.3391 S13: -0.1471 REMARK 3 S21: -0.1606 S22: -0.0248 S23: 0.1003 REMARK 3 S31: -0.3052 S32: -0.7344 S33: -0.1142 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): 92.5960 44.8960 4.7390 REMARK 3 T TENSOR REMARK 3 T11: -0.1549 T22: -0.1581 REMARK 3 T33: -0.1652 T12: 0.0344 REMARK 3 T13: -0.0791 T23: -0.0260 REMARK 3 L TENSOR REMARK 3 L11: 8.1228 L22: 1.1577 REMARK 3 L33: 12.1449 L12: -1.4310 REMARK 3 L13: -4.5295 L23: 1.9535 REMARK 3 S TENSOR REMARK 3 S11: 0.1123 S12: 0.2144 S13: -0.4454 REMARK 3 S21: -0.2062 S22: -0.0823 S23: -0.0984 REMARK 3 S31: 1.2922 S32: -0.0178 S33: -0.0300 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): 94.6030 47.6800 9.2620 REMARK 3 T TENSOR REMARK 3 T11: -0.2097 T22: -0.1947 REMARK 3 T33: -0.2593 T12: 0.0968 REMARK 3 T13: -0.0594 T23: 0.0490 REMARK 3 L TENSOR REMARK 3 L11: 6.9767 L22: 2.0551 REMARK 3 L33: 11.7254 L12: 1.3117 REMARK 3 L13: -1.7022 L23: -1.8286 REMARK 3 S TENSOR REMARK 3 S11: 0.4007 S12: -0.0964 S13: 0.3780 REMARK 3 S21: -0.5129 S22: -0.0404 S23: 0.0403 REMARK 3 S31: 0.5116 S32: 0.2411 S33: -0.3603 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): 93.9970 40.6350 -3.6340 REMARK 3 T TENSOR REMARK 3 T11: 0.4133 T22: -0.0060 REMARK 3 T33: -0.1111 T12: 0.1906 REMARK 3 T13: -0.0220 T23: -0.0353 REMARK 3 L TENSOR REMARK 3 L11: 4.8896 L22: 3.3784 REMARK 3 L33: 5.7450 L12: -1.2913 REMARK 3 L13: -0.3663 L23: 2.5541 REMARK 3 S TENSOR REMARK 3 S11: 0.2515 S12: 0.0875 S13: -1.3867 REMARK 3 S21: -0.9505 S22: -0.8000 S23: -0.1055 REMARK 3 S31: 0.4070 S32: 0.6858 S33: 0.5485 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): 86.2460 44.2590 -2.4320 REMARK 3 T TENSOR REMARK 3 T11: -0.0256 T22: 0.1195 REMARK 3 T33: -0.1362 T12: -0.0089 REMARK 3 T13: -0.2839 T23: -0.0365 REMARK 3 L TENSOR REMARK 3 L11: 13.9065 L22: 5.8130 REMARK 3 L33: 17.3841 L12: 6.1813 REMARK 3 L13: -11.5919 L23: -0.2873 REMARK 3 S TENSOR REMARK 3 S11: -0.3615 S12: 0.8343 S13: -0.1730 REMARK 3 S21: -1.3596 S22: 0.5363 S23: 0.8244 REMARK 3 S31: 1.7555 S32: -1.3424 S33: -0.1748 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): 114.3960 50.3810 35.1590 REMARK 3 T TENSOR REMARK 3 T11: -0.1629 T22: 0.0070 REMARK 3 T33: 0.0032 T12: 0.0347 REMARK 3 T13: 0.0211 T23: 0.1498 REMARK 3 L TENSOR REMARK 3 L11: 1.8566 L22: 1.6429 REMARK 3 L33: 2.2684 L12: 0.2974 REMARK 3 L13: -0.7531 L23: 0.7780 REMARK 3 S TENSOR REMARK 3 S11: 0.1303 S12: 0.2128 S13: 0.1628 REMARK 3 S21: -0.0587 S22: -0.0941 S23: -0.0148 REMARK 3 S31: -0.1025 S32: 0.1427 S33: -0.0362 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): 113.7230 39.4260 36.2060 REMARK 3 T TENSOR REMARK 3 T11: -0.1263 T22: -0.0284 REMARK 3 T33: -0.0685 T12: 0.0353 REMARK 3 T13: 0.0130 T23: 0.0638 REMARK 3 L TENSOR REMARK 3 L11: 4.6703 L22: 2.5915 REMARK 3 L33: 2.5238 L12: 0.2058 REMARK 3 L13: -0.0946 L23: -1.5106 REMARK 3 S TENSOR REMARK 3 S11: 0.0693 S12: 0.2481 S13: -0.4668 REMARK 3 S21: -0.1593 S22: 0.1211 S23: -0.1745 REMARK 3 S31: 0.6021 S32: 0.1664 S33: -0.1904 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): 112.4860 45.9480 35.6140 REMARK 3 T TENSOR REMARK 3 T11: -0.1421 T22: -0.0470 REMARK 3 T33: -0.0483 T12: -0.0060 REMARK 3 T13: -0.0345 T23: 0.0766 REMARK 3 L TENSOR REMARK 3 L11: 4.4393 L22: 0.8187 REMARK 3 L33: 4.2633 L12: -0.1322 REMARK 3 L13: -1.9572 L23: -0.2816 REMARK 3 S TENSOR REMARK 3 S11: -0.1780 S12: 0.2907 S13: -0.1592 REMARK 3 S21: -0.0159 S22: -0.0523 S23: 0.0379 REMARK 3 S31: 0.3042 S32: 0.1331 S33: 0.2303 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): 100.4950 53.3550 8.2120 REMARK 3 T TENSOR REMARK 3 T11: -0.1326 T22: 0.1439 REMARK 3 T33: -0.0458 T12: 0.0555 REMARK 3 T13: 0.0173 T23: 0.0549 REMARK 3 L TENSOR REMARK 3 L11: 2.0533 L22: 2.0924 REMARK 3 L33: 6.8677 L12: -1.6156 REMARK 3 L13: 3.7309 L23: -2.6660 REMARK 3 S TENSOR REMARK 3 S11: 0.4332 S12: 0.1455 S13: -0.3293 REMARK 3 S21: -0.3148 S22: -0.1380 S23: 0.2364 REMARK 3 S31: 0.5271 S32: 0.0949 S33: -0.2952 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): 101.6350 59.9270 8.8580 REMARK 3 T TENSOR REMARK 3 T11: -0.2093 T22: 0.1630 REMARK 3 T33: -0.1733 T12: 0.0093 REMARK 3 T13: -0.0147 T23: 0.0464 REMARK 3 L TENSOR REMARK 3 L11: 6.7331 L22: 6.0580 REMARK 3 L33: 2.1273 L12: -4.6104 REMARK 3 L13: 2.8185 L23: -1.5305 REMARK 3 S TENSOR REMARK 3 S11: -0.1925 S12: -0.1843 S13: 0.5345 REMARK 3 S21: 0.1639 S22: -0.1165 S23: -0.2984 REMARK 3 S31: -0.0524 S32: 0.2574 S33: 0.3090 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): 95.1990 60.2780 2.9690 REMARK 3 T TENSOR REMARK 3 T11: -0.2584 T22: 0.0834 REMARK 3 T33: -0.1815 T12: 0.0245 REMARK 3 T13: 0.0061 T23: 0.0414 REMARK 3 L TENSOR REMARK 3 L11: 6.9623 L22: 4.9284 REMARK 3 L33: 5.2017 L12: -4.1842 REMARK 3 L13: 4.0956 L23: -3.0694 REMARK 3 S TENSOR REMARK 3 S11: 0.0433 S12: 0.3875 S13: 0.0694 REMARK 3 S21: -0.3655 S22: -0.1511 S23: -0.0314 REMARK 3 S31: 0.0575 S32: 0.1447 S33: 0.1078 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): 103.0350 62.6820 -2.0170 REMARK 3 T TENSOR REMARK 3 T11: -0.2287 T22: 0.1106 REMARK 3 T33: -0.2355 T12: 0.1473 REMARK 3 T13: 0.1259 T23: 0.1392 REMARK 3 L TENSOR REMARK 3 L11: 5.1710 L22: 5.7268 REMARK 3 L33: 6.0140 L12: -2.2754 REMARK 3 L13: 1.1443 L23: -3.5125 REMARK 3 S TENSOR REMARK 3 S11: 0.2111 S12: 1.2002 S13: 0.0786 REMARK 3 S21: -0.3692 S22: -0.4667 S23: -0.3222 REMARK 3 S31: -0.1882 S32: 1.0733 S33: 0.2556 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. THESE ARE RE-REFINED COORDINATES OF THE REMARK 3 PREVIOUS WWPDB SUBMISSION 1TXV. THE STARTING MODEL WAS A 2.4 REMARK 3 ANGSTROM STRUCTURE WITH A DIFFERENT BOUND LIGAND. THE MODEL IS REMARK 3 REFINED TO LOWER RFREE. ONE SEQUENCE MISTAKE IN THE AIIB REMARK 3 SUBUNIT IS CORRECTED. MORE OF BETA SUBUNIT DOMAIN I-EGF1 IS REMARK 3 BUILT. MISTAKES IN CARBOHYDRATE ANOMERIC LINKAGES ARE REMARK 3 CORRECTED. REMARK 4 REMARK 4 2VDL 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-34077. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-AUG-03 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) : 0.9793 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 : 62512 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.75 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 (%) : 99.9 REMARK 200 DATA REDUNDANCY : 7.1 REMARK 200 R MERGE (I) : 0.14 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.10 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.60 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.00 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: PDB ENTRY 1JV2 REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 66.8 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.7 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 117.59867 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 58.79933 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 58.79933 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 117.59867 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PQS REMARK 350 TOTAL BURIED SURFACE AREA: 10480 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 71680 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.8 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 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 A 4058 O HOH A 4242 2.18 REMARK 500 O HOH A 4062 O HOH A 4064 2.20 REMARK 500 O HOH B 4016 O HOH B 4100 2.18 REMARK 500 O HOH L 4038 O HOH L 4055 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER A 101 -124.71 50.76 REMARK 500 LYS A 118 -123.59 56.15 REMARK 500 GLU A 123 135.73 98.51 REMARK 500 LEU A 212 -48.01 71.97 REMARK 500 SER A 222 -169.82 -73.60 REMARK 500 SER A 261 71.48 51.07 REMARK 500 THR B 7 48.18 -91.37 REMARK 500 ARG B 8 73.28 -153.66 REMARK 500 VAL B 10 71.36 38.19 REMARK 500 VAL B 80 92.76 62.02 REMARK 500 ASN B 148 33.71 -98.01 REMARK 500 VAL B 157 -82.70 -125.03 REMARK 500 SER B 213 -152.86 -114.62 REMARK 500 LYS B 253 171.22 -54.33 REMARK 500 LEU B 258 -7.91 86.50 REMARK 500 LYS B 410 -20.04 76.49 REMARK 500 GLU B 442 71.85 57.72 REMARK 500 HIS B 446 -63.01 70.27 REMARK 500 THR B 454 145.51 66.75 REMARK 500 ASP H 179 -8.63 67.77 REMARK 500 SER L 30 60.17 30.28 REMARK 500 SER L 43 -159.88 -88.02 REMARK 500 SER L 77 74.13 62.70 REMARK 500 LYS L 169 -65.00 -92.61 REMARK 500 ASN L 212 81.76 54.50 REMARK 500 REMARK 500 REMARK: NULL REMARK 600 REMARK 600 HETEROGEN REMARK 600 CACODYLATE ION (CAC): CACODYLATE IS FOUND IN THE LIGAND REMARK 600 BINDING SITE. BASED ON IMPURITIES IN CACODYLATE AND REMARK 600 HYDROGEN BOND DONORS NEAR THE CACODYLATE, IT IS POSSIBLE REMARK 600 THAT ONE OR TWO METHYL GROUPS HAVE BEEN LOST. 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 CAC B1462 AS REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CAC B1462 C2 REMARK 620 2 CAC B1462 O1 110.4 REMARK 620 3 CAC B1462 O2 112.1 105.9 REMARK 620 4 CAC B1462 C1 106.7 109.5 112.4 REMARK 620 N 1 2 3 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 50.0 REMARK 620 3 ASP A 245 OD2 120.0 70.9 REMARK 620 4 ASP A 247 O 79.5 73.0 93.7 REMARK 620 5 THR A 250 O 69.3 117.3 169.8 83.4 REMARK 620 6 THR A 250 OG1 142.5 147.0 92.5 80.2 77.3 REMARK 620 7 GLU A 252 OE1 77.1 77.6 82.1 150.1 105.2 129.5 REMARK 620 8 GLU A 252 OE2 119.3 125.7 85.0 158.8 94.1 78.8 50.8 REMARK 620 N 1 2 3 4 5 6 7 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A2005 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN A 299 OD1 REMARK 620 2 ASP A 301 OD1 79.6 REMARK 620 3 ARG A 303 O 164.7 98.9 REMARK 620 4 ASP A 297 OD1 83.2 80.6 81.5 REMARK 620 5 ASP A 305 OD1 104.6 151.7 84.0 127.5 REMARK 620 6 ASP A 305 OD2 78.8 154.7 98.5 84.0 48.8 REMARK 620 7 HOH A4332 O 96.5 82.0 98.4 162.3 69.8 113.3 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 367 OD1 93.4 REMARK 620 3 ASP A 369 OD1 81.7 98.1 REMARK 620 4 TYR A 371 O 76.3 169.8 80.5 REMARK 620 5 HOH A4362 O 144.6 106.9 67.2 82.0 REMARK 620 6 ASP A 373 OD1 99.8 84.3 177.1 97.5 110.6 REMARK 620 7 ASP A 373 OD2 132.4 113.9 128.0 74.2 64.9 49.2 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 87.9 REMARK 620 3 ASP A 426 OD1 75.9 88.1 REMARK 620 4 ASP A 428 OD1 153.0 90.5 77.0 REMARK 620 5 ASP A 434 OD1 103.3 168.0 90.4 77.5 REMARK 620 6 ASP A 434 OD2 88.1 136.8 132.2 110.9 49.5 REMARK 620 7 HOH A4402 O 136.6 86.6 146.7 70.1 88.2 67.8 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B2002 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GOL B1463 C2 REMARK 620 2 GOL B1463 O2 26.6 REMARK 620 3 HOH B4231 O 98.3 87.7 REMARK 620 4 ASP B 251 OD2 98.9 124.8 99.2 REMARK 620 5 GOL B1463 O1 46.7 63.3 70.3 67.9 REMARK 620 6 SER B 123 O 178.0 154.0 83.7 80.9 134.6 REMARK 620 7 ASP B 126 OD1 103.2 79.1 90.8 154.1 137.8 76.6 REMARK 620 8 ASP B 127 OD1 79.2 85.4 168.9 91.9 113.8 98.8 79.3 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 159.0 REMARK 620 3 ASN B 215 OD1 98.2 96.8 REMARK 620 4 ASP B 217 OD1 74.3 90.8 91.5 REMARK 620 5 PRO B 219 O 86.7 80.3 171.6 96.4 REMARK 620 6 GLU B 220 OE2 93.4 102.8 83.7 166.0 89.3 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 GLU B 220 OE1 REMARK 620 2 HOH B4101 O 84.0 REMARK 620 3 SER B 123 OG 177.4 93.4 REMARK 620 4 HOH B4033 O 95.7 91.4 84.4 REMARK 620 5 CAC B1462 O1 93.7 100.8 86.7 165.3 REMARK 620 6 SER B 121 OG 84.6 165.8 97.9 81.2 88.4 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 CAC B1462 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1453 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1463 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: 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.