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. 2.40 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) : 2.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.44 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 96.5 REMARK 3 NUMBER OF REFLECTIONS : 80277 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 : 0.193 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 4276 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) : 2.40 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46 REMARK 3 REFLECTION IN BIN (WORKING SET) : 5145 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2260 REMARK 3 BIN FREE R VALUE SET COUNT : 297 REMARK 3 BIN FREE R VALUE : 0.2810 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 10537 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 205 REMARK 3 SOLVENT ATOMS : 1142 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) : 43.58 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.13000 REMARK 3 B22 (A**2) : -0.13000 REMARK 3 B33 (A**2) : 0.19000 REMARK 3 B12 (A**2) : -0.06000 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): 0.220 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.183 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.127 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.822 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11037 ; 0.007 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 7400 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15084 ; 1.043 ; 1.979 REMARK 3 BOND ANGLES OTHERS (DEGREES): 18022 ; 0.790 ; 3.002 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1398 ; 5.725 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 482 ;34.156 ;24.315 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1739 ;12.173 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 62 ;14.711 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1698 ; 0.065 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12324 ; 0.003 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 2184 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1991 ; 0.183 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 7668 ; 0.181 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5312 ; 0.170 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 5756 ; 0.081 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 925 ; 0.154 ; 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 ; 0.116 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 77 ; 0.202 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 40 ; 0.162 ; 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): 7058 ; 1.901 ; 5.000 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11025 ; 2.897 ;10.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4619 ; 2.019 ; 5.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4036 ; 2.975 ;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 : 26 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 32 REMARK 3 ORIGIN FOR THE GROUP (A): 130.0750 14.1410 72.0520 REMARK 3 T TENSOR REMARK 3 T11: -0.1269 T22: 0.0924 REMARK 3 T33: 0.0326 T12: 0.0875 REMARK 3 T13: 0.0477 T23: 0.2903 REMARK 3 L TENSOR REMARK 3 L11: 3.5064 L22: 4.3405 REMARK 3 L33: 2.5191 L12: -0.1934 REMARK 3 L13: 1.0806 L23: -0.6442 REMARK 3 S TENSOR REMARK 3 S11: -0.0069 S12: 0.3691 S13: -0.2807 REMARK 3 S21: 0.0607 S22: -0.4708 S23: -0.6162 REMARK 3 S31: 0.4584 S32: 0.7992 S33: 0.4778 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 33 A 54 REMARK 3 ORIGIN FOR THE GROUP (A): 126.9940 29.3980 71.7420 REMARK 3 T TENSOR REMARK 3 T11: -0.1604 T22: -0.0221 REMARK 3 T33: -0.0250 T12: 0.0015 REMARK 3 T13: -0.0655 T23: 0.1856 REMARK 3 L TENSOR REMARK 3 L11: 1.9709 L22: 13.8415 REMARK 3 L33: 4.5553 L12: 0.4717 REMARK 3 L13: -1.3274 L23: 5.7691 REMARK 3 S TENSOR REMARK 3 S11: 0.1593 S12: -0.3785 S13: 0.0876 REMARK 3 S21: 0.1558 S22: -0.2124 S23: -0.5255 REMARK 3 S31: -0.1230 S32: 0.1724 S33: 0.0531 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 55 A 115 REMARK 3 ORIGIN FOR THE GROUP (A): 121.1530 30.7180 64.9890 REMARK 3 T TENSOR REMARK 3 T11: -0.1675 T22: 0.0085 REMARK 3 T33: -0.0365 T12: -0.0736 REMARK 3 T13: -0.0323 T23: 0.1680 REMARK 3 L TENSOR REMARK 3 L11: 0.6748 L22: 1.4259 REMARK 3 L33: 1.6692 L12: -0.3487 REMARK 3 L13: -0.1723 L23: -0.6809 REMARK 3 S TENSOR REMARK 3 S11: -0.0172 S12: 0.0122 S13: -0.0059 REMARK 3 S21: 0.1725 S22: -0.2646 S23: -0.3390 REMARK 3 S31: -0.0246 S32: 0.4267 S33: 0.2819 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 164 REMARK 3 ORIGIN FOR THE GROUP (A): 107.2880 35.9960 63.0630 REMARK 3 T TENSOR REMARK 3 T11: -0.1368 T22: -0.0888 REMARK 3 T33: -0.1041 T12: -0.0828 REMARK 3 T13: -0.0358 T23: 0.0938 REMARK 3 L TENSOR REMARK 3 L11: 2.4628 L22: 1.9926 REMARK 3 L33: 2.6118 L12: -0.4821 REMARK 3 L13: -1.9390 L23: 0.3968 REMARK 3 S TENSOR REMARK 3 S11: -0.0148 S12: -0.0157 S13: -0.1175 REMARK 3 S21: 0.0287 S22: -0.1446 S23: 0.1613 REMARK 3 S31: -0.0388 S32: 0.0315 S33: 0.1594 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 165 A 243 REMARK 3 ORIGIN FOR THE GROUP (A): 105.7730 24.8560 64.2490 REMARK 3 T TENSOR REMARK 3 T11: -0.0889 T22: -0.0820 REMARK 3 T33: -0.0649 T12: -0.0745 REMARK 3 T13: -0.0015 T23: 0.0563 REMARK 3 L TENSOR REMARK 3 L11: 1.1797 L22: 0.7734 REMARK 3 L33: 1.1158 L12: 0.1430 REMARK 3 L13: -0.4173 L23: -0.3648 REMARK 3 S TENSOR REMARK 3 S11: 0.0348 S12: 0.0918 S13: -0.1344 REMARK 3 S21: -0.0161 S22: -0.1999 S23: 0.0099 REMARK 3 S31: 0.2506 S32: -0.0894 S33: 0.1651 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 315 REMARK 3 ORIGIN FOR THE GROUP (A): 102.4170 10.6060 73.7810 REMARK 3 T TENSOR REMARK 3 T11: 0.0294 T22: -0.2023 REMARK 3 T33: -0.0917 T12: -0.1316 REMARK 3 T13: 0.0710 T23: 0.0591 REMARK 3 L TENSOR REMARK 3 L11: 1.5943 L22: 2.1065 REMARK 3 L33: 2.0306 L12: -0.0649 REMARK 3 L13: -0.0317 L23: 0.4859 REMARK 3 S TENSOR REMARK 3 S11: -0.1181 S12: 0.0774 S13: -0.2662 REMARK 3 S21: -0.0398 S22: -0.1491 S23: 0.0824 REMARK 3 S31: 0.3749 S32: -0.0648 S33: 0.2672 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 316 A 337 REMARK 3 ORIGIN FOR THE GROUP (A): 104.1410 4.7230 86.1710 REMARK 3 T TENSOR REMARK 3 T11: 0.1631 T22: -0.1655 REMARK 3 T33: -0.0559 T12: -0.1631 REMARK 3 T13: 0.1289 T23: 0.1805 REMARK 3 L TENSOR REMARK 3 L11: 2.1531 L22: 8.1318 REMARK 3 L33: 16.7972 L12: -0.1188 REMARK 3 L13: -0.2936 L23: 10.7464 REMARK 3 S TENSOR REMARK 3 S11: -0.2019 S12: -0.3774 S13: -0.4574 REMARK 3 S21: 0.6581 S22: -0.6574 S23: 0.4486 REMARK 3 S31: 1.2820 S32: -1.1033 S33: 0.8593 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 338 A 376 REMARK 3 ORIGIN FOR THE GROUP (A): 113.6150 3.5190 79.6680 REMARK 3 T TENSOR REMARK 3 T11: 0.0749 T22: -0.2611 REMARK 3 T33: -0.0605 T12: 0.0068 REMARK 3 T13: 0.0582 T23: 0.1902 REMARK 3 L TENSOR REMARK 3 L11: 2.6664 L22: 2.9922 REMARK 3 L33: 2.0517 L12: 0.6866 REMARK 3 L13: -0.1091 L23: 0.9755 REMARK 3 S TENSOR REMARK 3 S11: -0.1760 S12: -0.0346 S13: -0.3178 REMARK 3 S21: -0.1309 S22: -0.1127 S23: -0.0294 REMARK 3 S31: 0.5339 S32: 0.1794 S33: 0.2887 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 377 A 452 REMARK 3 ORIGIN FOR THE GROUP (A): 124.5220 7.5450 80.1950 REMARK 3 T TENSOR REMARK 3 T11: -0.0457 T22: -0.0799 REMARK 3 T33: -0.0060 T12: 0.1004 REMARK 3 T13: 0.0291 T23: 0.2788 REMARK 3 L TENSOR REMARK 3 L11: 2.1574 L22: 2.4891 REMARK 3 L33: 2.9107 L12: 0.9162 REMARK 3 L13: -0.0147 L23: 0.2097 REMARK 3 S TENSOR REMARK 3 S11: -0.0909 S12: -0.2130 S13: -0.3615 REMARK 3 S21: 0.2477 S22: -0.2637 S23: -0.2917 REMARK 3 S31: 0.5424 S32: 0.6279 S33: 0.3546 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 28 REMARK 3 ORIGIN FOR THE GROUP (A): 113.7480 17.2440 172.2760 REMARK 3 T TENSOR REMARK 3 T11: 0.5332 T22: -0.3366 REMARK 3 T33: -0.2075 T12: 0.0516 REMARK 3 T13: -0.3938 T23: -0.0920 REMARK 3 L TENSOR REMARK 3 L11: 7.9758 L22: 11.6676 REMARK 3 L33: 5.5717 L12: -1.3380 REMARK 3 L13: 2.2247 L23: 0.9728 REMARK 3 S TENSOR REMARK 3 S11: -0.3184 S12: -0.3658 S13: -0.1020 REMARK 3 S21: 1.4565 S22: 0.5055 S23: -0.8356 REMARK 3 S31: -0.2894 S32: 0.4794 S33: -0.1870 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 29 B 72 REMARK 3 ORIGIN FOR THE GROUP (A): 102.2570 23.7020 167.5800 REMARK 3 T TENSOR REMARK 3 T11: 0.5100 T22: -0.0729 REMARK 3 T33: -0.4776 T12: 0.2875 REMARK 3 T13: -0.0447 T23: -0.0942 REMARK 3 L TENSOR REMARK 3 L11: 3.8787 L22: 3.2985 REMARK 3 L33: 10.9136 L12: -1.3853 REMARK 3 L13: 3.2330 L23: -2.3541 REMARK 3 S TENSOR REMARK 3 S11: -0.5732 S12: -0.8802 S13: -0.0411 REMARK 3 S21: 1.2774 S22: 0.7166 S23: -0.2468 REMARK 3 S31: -1.7546 S32: -2.0912 S33: -0.1434 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 79 B 100 REMARK 3 ORIGIN FOR THE GROUP (A): 102.3930 30.1130 148.4950 REMARK 3 T TENSOR REMARK 3 T11: 0.4310 T22: -0.1569 REMARK 3 T33: -0.5200 T12: 0.2131 REMARK 3 T13: 0.0115 T23: -0.0196 REMARK 3 L TENSOR REMARK 3 L11: 8.1355 L22: 8.2954 REMARK 3 L33: 35.8670 L12: -3.3482 REMARK 3 L13: 16.5444 L23: -10.7296 REMARK 3 S TENSOR REMARK 3 S11: -0.9467 S12: -0.5715 S13: 0.4243 REMARK 3 S21: 0.8436 S22: 0.2787 S23: -0.9191 REMARK 3 S31: -2.9333 S32: -1.3429 S33: 0.6679 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 101 B 137 REMARK 3 ORIGIN FOR THE GROUP (A): 93.9390 37.0620 108.1200 REMARK 3 T TENSOR REMARK 3 T11: 0.2266 T22: -0.0377 REMARK 3 T33: -0.1198 T12: -0.2305 REMARK 3 T13: 0.0402 T23: -0.0115 REMARK 3 L TENSOR REMARK 3 L11: 1.0231 L22: 0.7196 REMARK 3 L33: 4.3347 L12: -0.6844 REMARK 3 L13: 0.3406 L23: -1.2790 REMARK 3 S TENSOR REMARK 3 S11: -0.1203 S12: -0.2716 S13: 0.1423 REMARK 3 S21: 0.4935 S22: -0.0394 S23: 0.0483 REMARK 3 S31: -0.3848 S32: 0.1777 S33: 0.1596 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 138 B 201 REMARK 3 ORIGIN FOR THE GROUP (A): 101.2760 43.1080 94.9320 REMARK 3 T TENSOR REMARK 3 T11: 0.0956 T22: -0.1204 REMARK 3 T33: -0.1042 T12: -0.2048 REMARK 3 T13: 0.0137 T23: 0.0047 REMARK 3 L TENSOR REMARK 3 L11: 1.2712 L22: 0.7980 REMARK 3 L33: 4.2329 L12: 0.0412 REMARK 3 L13: -1.3445 L23: -0.4346 REMARK 3 S TENSOR REMARK 3 S11: 0.1659 S12: -0.2002 S13: 0.1686 REMARK 3 S21: 0.3609 S22: -0.0854 S23: -0.0598 REMARK 3 S31: -0.5642 S32: 0.2230 S33: -0.0805 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 202 B 342 REMARK 3 ORIGIN FOR THE GROUP (A): 102.4650 31.4470 97.1540 REMARK 3 T TENSOR REMARK 3 T11: 0.0599 T22: -0.0974 REMARK 3 T33: -0.1573 T12: -0.1865 REMARK 3 T13: -0.0210 T23: 0.0605 REMARK 3 L TENSOR REMARK 3 L11: 1.5295 L22: 1.5569 REMARK 3 L33: 1.9793 L12: -0.7815 REMARK 3 L13: -0.6696 L23: 0.4022 REMARK 3 S TENSOR REMARK 3 S11: -0.0347 S12: -0.2959 S13: 0.0719 REMARK 3 S21: 0.4684 S22: -0.0655 S23: -0.1139 REMARK 3 S31: 0.0011 S32: 0.2328 S33: 0.1002 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 343 B 390 REMARK 3 ORIGIN FOR THE GROUP (A): 101.5840 21.7460 133.1160 REMARK 3 T TENSOR REMARK 3 T11: 0.2415 T22: -0.0509 REMARK 3 T33: -0.1708 T12: -0.0519 REMARK 3 T13: 0.0301 T23: -0.0191 REMARK 3 L TENSOR REMARK 3 L11: 2.5801 L22: 3.0602 REMARK 3 L33: 24.4817 L12: -1.9241 REMARK 3 L13: 7.8241 L23: -4.7267 REMARK 3 S TENSOR REMARK 3 S11: 0.7802 S12: 0.7670 S13: -0.4658 REMARK 3 S21: -0.3422 S22: 0.1905 S23: -0.1241 REMARK 3 S31: 1.5879 S32: 1.0544 S33: -0.9706 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 : B 391 B 441 REMARK 3 ORIGIN FOR THE GROUP (A): 108.5290 28.6310 149.9560 REMARK 3 T TENSOR REMARK 3 T11: 0.4680 T22: -0.3329 REMARK 3 T33: -0.1853 T12: -0.0742 REMARK 3 T13: -0.0323 T23: 0.0098 REMARK 3 L TENSOR REMARK 3 L11: 5.4165 L22: 2.5646 REMARK 3 L33: 22.3065 L12: -1.4135 REMARK 3 L13: 8.1958 L23: -2.0718 REMARK 3 S TENSOR REMARK 3 S11: -0.5095 S12: 0.3702 S13: 0.1596 REMARK 3 S21: 0.7477 S22: 0.4255 S23: -0.4918 REMARK 3 S31: -2.2382 S32: 1.1673 S33: 0.0840 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 : B 442 B 461 REMARK 3 ORIGIN FOR THE GROUP (A): 120.0640 31.0660 184.4760 REMARK 3 T TENSOR REMARK 3 T11: 2.5715 T22: 1.5098 REMARK 3 T33: 1.1120 T12: -0.3991 REMARK 3 T13: -0.9833 T23: -0.1423 REMARK 3 L TENSOR REMARK 3 L11: 3.9298 L22: 20.6503 REMARK 3 L33: 2.2601 L12: -9.0084 REMARK 3 L13: 2.9802 L23: -6.8316 REMARK 3 S TENSOR REMARK 3 S11: -1.0021 S12: -1.2108 S13: 0.2598 REMARK 3 S21: 3.2835 S22: -0.8862 S23: -4.0040 REMARK 3 S31: -1.2283 S32: 5.1978 S33: 1.8883 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 1 H 31 REMARK 3 ORIGIN FOR THE GROUP (A): 89.6610 36.1380 38.0710 REMARK 3 T TENSOR REMARK 3 T11: -0.1914 T22: -0.0108 REMARK 3 T33: -0.0695 T12: -0.1378 REMARK 3 T13: -0.0130 T23: 0.0532 REMARK 3 L TENSOR REMARK 3 L11: 4.2002 L22: 5.3786 REMARK 3 L33: 6.3577 L12: -2.0402 REMARK 3 L13: 3.7337 L23: -3.5323 REMARK 3 S TENSOR REMARK 3 S11: 0.2521 S12: 0.1840 S13: -0.3798 REMARK 3 S21: -0.2607 S22: -0.0368 S23: 0.2724 REMARK 3 S31: 0.6521 S32: -0.1354 S33: -0.2153 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 32 H 122 REMARK 3 ORIGIN FOR THE GROUP (A): 93.5780 43.8020 41.1100 REMARK 3 T TENSOR REMARK 3 T11: -0.1935 T22: -0.0055 REMARK 3 T33: -0.0610 T12: -0.0491 REMARK 3 T13: -0.0061 T23: 0.0749 REMARK 3 L TENSOR REMARK 3 L11: 2.1847 L22: 0.6209 REMARK 3 L33: 2.8509 L12: -0.2202 REMARK 3 L13: 0.9068 L23: -0.4825 REMARK 3 S TENSOR REMARK 3 S11: 0.0132 S12: 0.1078 S13: 0.0779 REMARK 3 S21: 0.0097 S22: -0.0627 S23: 0.0597 REMARK 3 S31: 0.0714 S32: -0.2312 S33: 0.0495 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 123 H 185 REMARK 3 ORIGIN FOR THE GROUP (A): 91.8280 46.8260 5.7190 REMARK 3 T TENSOR REMARK 3 T11: -0.1922 T22: -0.1133 REMARK 3 T33: -0.1513 T12: 0.0959 REMARK 3 T13: -0.0724 T23: 0.0146 REMARK 3 L TENSOR REMARK 3 L11: 6.3694 L22: 1.8655 REMARK 3 L33: 11.1482 L12: -0.7554 REMARK 3 L13: -1.4707 L23: -0.1040 REMARK 3 S TENSOR REMARK 3 S11: 0.2059 S12: 0.2741 S13: -0.2516 REMARK 3 S21: -0.3223 S22: -0.1127 S23: -0.0020 REMARK 3 S31: 0.7386 S32: -0.0914 S33: -0.0932 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 186 H 221 REMARK 3 ORIGIN FOR THE GROUP (A): 90.7630 42.3920 -2.7960 REMARK 3 T TENSOR REMARK 3 T11: 0.1336 T22: -0.0298 REMARK 3 T33: -0.2082 T12: 0.1508 REMARK 3 T13: -0.1592 T23: -0.1394 REMARK 3 L TENSOR REMARK 3 L11: 5.7071 L22: 2.7947 REMARK 3 L33: 8.7499 L12: -1.0243 REMARK 3 L13: -2.6669 L23: 1.0027 REMARK 3 S TENSOR REMARK 3 S11: 0.1302 S12: 0.4186 S13: -0.8154 REMARK 3 S21: -0.9514 S22: -0.3258 S23: 0.3098 REMARK 3 S31: 1.5176 S32: 0.1092 S33: 0.1957 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 : L 1 L 104 REMARK 3 ORIGIN FOR THE GROUP (A): 112.9620 45.3290 35.3670 REMARK 3 T TENSOR REMARK 3 T11: -0.1844 T22: -0.0069 REMARK 3 T33: -0.0566 T12: 0.0158 REMARK 3 T13: -0.0080 T23: 0.1042 REMARK 3 L TENSOR REMARK 3 L11: 2.1897 L22: 0.7050 REMARK 3 L33: 2.2925 L12: 0.2270 REMARK 3 L13: -0.6823 L23: -0.3964 REMARK 3 S TENSOR REMARK 3 S11: 0.0672 S12: 0.3263 S13: 0.0725 REMARK 3 S21: -0.0973 S22: -0.0077 S23: -0.0337 REMARK 3 S31: 0.1397 S32: -0.0045 S33: -0.0595 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 : L 105 L 160 REMARK 3 ORIGIN FOR THE GROUP (A): 99.6910 57.8230 5.3960 REMARK 3 T TENSOR REMARK 3 T11: -0.2449 T22: 0.1861 REMARK 3 T33: -0.1904 T12: 0.0720 REMARK 3 T13: 0.0349 T23: 0.0425 REMARK 3 L TENSOR REMARK 3 L11: 4.8369 L22: 4.0411 REMARK 3 L33: 4.0935 L12: -3.7715 REMARK 3 L13: 3.0199 L23: -2.8696 REMARK 3 S TENSOR REMARK 3 S11: 0.1404 S12: 0.2287 S13: 0.2401 REMARK 3 S21: -0.1237 S22: -0.2792 S23: -0.1870 REMARK 3 S31: 0.1924 S32: 0.4300 S33: 0.1389 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 161 L 192 REMARK 3 ORIGIN FOR THE GROUP (A): 95.7610 57.3740 5.3830 REMARK 3 T TENSOR REMARK 3 T11: -0.2702 T22: 0.0630 REMARK 3 T33: -0.2088 T12: 0.0479 REMARK 3 T13: 0.0041 T23: -0.0010 REMARK 3 L TENSOR REMARK 3 L11: 8.7788 L22: 5.5380 REMARK 3 L33: 5.1761 L12: -5.5046 REMARK 3 L13: 4.5810 L23: -3.5699 REMARK 3 S TENSOR REMARK 3 S11: 0.1019 S12: 0.1531 S13: -0.1716 REMARK 3 S21: -0.0784 S22: -0.0803 S23: 0.1474 REMARK 3 S31: 0.0835 S32: 0.2213 S33: -0.0216 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 193 L 214 REMARK 3 ORIGIN FOR THE GROUP (A): 102.7210 62.5240 -1.3470 REMARK 3 T TENSOR REMARK 3 T11: -0.2592 T22: 0.2045 REMARK 3 T33: -0.1120 T12: 0.1302 REMARK 3 T13: 0.0453 T23: 0.1559 REMARK 3 L TENSOR REMARK 3 L11: 15.0175 L22: 4.2715 REMARK 3 L33: 9.5348 L12: -4.4939 REMARK 3 L13: 7.5253 L23: -5.1262 REMARK 3 S TENSOR REMARK 3 S11: 0.2547 S12: 1.2658 S13: 0.3870 REMARK 3 S21: -0.3362 S22: -0.6392 S23: -0.4028 REMARK 3 S31: 0.0022 S32: 0.9662 S33: 0.3846 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 2VDR 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-34089. 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 : NULL 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 : 609049 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.40 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 (%) : 99.7 REMARK 200 DATA REDUNDANCY : 6.9 REMARK 200 R MERGE (I) : 0.09 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 17.30 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.57 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.30 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 117.86200 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 58.93100 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 58.93100 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 117.86200 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: 11570 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 72130 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.6 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 400 REMARK 400 COMPOUND REMARK 400 ENGINEERED RESIDUE IN CHAIN C, ALA 396 TO ARG 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 C 404 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 4194 O HOH A 4195 2.20 REMARK 500 O HOH B 4029 O HOH A 4258 2.15 REMARK 500 O HOH B 4122 O HOH A 4258 2.09 REMARK 500 O HOH L 4014 O HOH L 4137 2.00 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 -124.46 51.48 REMARK 500 LYS A 118 -120.91 51.92 REMARK 500 GLU A 123 134.02 98.17 REMARK 500 LEU A 212 -48.68 72.16 REMARK 500 THR A 296 143.95 -171.71 REMARK 500 VAL B 10 75.08 40.69 REMARK 500 PHE B 56 81.67 -153.35 REMARK 500 ASP B 71 -157.00 -112.18 REMARK 500 VAL B 80 97.55 68.35 REMARK 500 VAL B 157 -87.45 -127.66 REMARK 500 SER B 213 -154.96 -107.16 REMARK 500 ASP B 241 48.86 -107.62 REMARK 500 LEU B 258 -11.85 84.06 REMARK 500 VAL B 275 -77.27 -87.01 REMARK 500 LYS B 410 -25.51 72.80 REMARK 500 GLN B 440 54.66 -105.22 REMARK 500 GLU B 442 78.14 53.27 REMARK 500 HIS B 446 -57.96 70.17 REMARK 500 THR B 454 158.85 69.16 REMARK 500 ASP H 179 -16.14 75.75 REMARK 500 SER L 30 56.30 31.29 REMARK 500 SER L 77 79.31 64.31 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 50.9 REMARK 620 3 ASP A 245 OD2 118.1 67.2 REMARK 620 4 ASP A 247 O 79.2 77.8 85.5 REMARK 620 5 THR A 250 O 75.7 125.5 159.8 82.7 REMARK 620 6 THR A 250 OG1 144.6 142.9 84.9 76.0 76.5 REMARK 620 7 GLU A 252 OE1 84.2 82.0 91.4 159.2 105.3 124.3 REMARK 620 8 GLU A 252 OE2 128.6 129.3 91.4 148.6 90.2 72.6 51.9 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 80.0 REMARK 620 3 ASP A 297 OD1 82.4 79.5 REMARK 620 4 ARG A 303 O 160.9 86.2 82.2 REMARK 620 5 ASP A 305 OD1 119.4 144.0 129.9 79.3 REMARK 620 6 ASP A 305 OD2 94.1 165.0 86.0 96.0 50.7 REMARK 620 7 HOH A4317 O 89.6 80.3 159.3 101.0 70.5 113.7 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 75.8 REMARK 620 3 TYR A 371 O 77.1 89.5 REMARK 620 4 ASP A 367 OD1 86.1 90.1 162.8 REMARK 620 5 HOH A4361 O 149.7 73.9 102.2 94.3 REMARK 620 6 ASP A 373 OD1 94.1 161.6 103.3 73.7 115.2 REMARK 620 7 ASP A 373 OD2 133.9 147.5 86.4 102.9 75.5 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 87.0 REMARK 620 3 ASP A 426 OD1 78.8 86.3 REMARK 620 4 ASP A 428 OD1 156.7 88.6 78.1 REMARK 620 5 ASP A 434 OD1 99.5 171.7 90.0 83.4 REMARK 620 6 ASP A 434 OD2 85.6 135.3 134.8 113.1 51.0 REMARK 620 7 HOH A4399 O 131.6 80.0 145.3 69.8 99.1 72.6 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 28.0 REMARK 620 3 ASP B 251 OD2 100.4 127.7 REMARK 620 4 GOL B1462 O1 46.4 64.8 67.9 REMARK 620 5 HOH C4011 O 100.4 84.8 107.7 80.0 REMARK 620 6 SER B 123 O 178.6 152.8 79.0 134.1 80.9 REMARK 620 7 ASP B 126 OD1 104.6 79.5 151.0 141.0 81.9 75.6 REMARK 620 8 ASP B 127 OD1 82.3 91.3 86.4 111.8 164.6 96.4 82.7 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 161.5 REMARK 620 3 ASN B 215 OD1 94.4 98.5 REMARK 620 4 ASP B 217 OD1 75.5 90.1 95.5 REMARK 620 5 PRO B 219 O 89.2 80.0 171.1 93.3 REMARK 620 6 GLU B 220 OE2 91.1 103.0 85.5 166.6 86.3 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 HOH B4112 O REMARK 620 2 SER B 123 OG 95.5 REMARK 620 3 GLU B 220 OE1 87.1 177.4 REMARK 620 4 HOH B4041 O 99.5 80.5 99.2 REMARK 620 5 ASP C 410 OD1 96.3 88.3 91.4 161.3 REMARK 620 6 SER B 121 OG 171.8 89.9 87.6 75.2 90.0 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 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. THERE IS A A408R MUTATION 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