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) : 42.64 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5 REMARK 3 NUMBER OF REFLECTIONS : 50725 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) : 0.164 REMARK 3 R VALUE (WORKING SET) : 0.161 REMARK 3 FREE R VALUE : 0.205 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 2713 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) : 2.87 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3343 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2520 REMARK 3 BIN FREE R VALUE SET COUNT : 198 REMARK 3 BIN FREE R VALUE : 0.3400 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 10403 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 210 REMARK 3 SOLVENT ATOMS : 612 REMARK 3 REMARK 3 B VALUES. REMARK 3 B VALUE TYPE : UNVERIFIED REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.09 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.21000 REMARK 3 B22 (A**2) : 1.21000 REMARK 3 B33 (A**2) : -1.82000 REMARK 3 B12 (A**2) : 0.61000 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): 0.648 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.279 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.187 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.783 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10895 ; 0.005 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 7298 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14875 ; 0.936 ; 1.979 REMARK 3 BOND ANGLES OTHERS (DEGREES): 17733 ; 0.758 ; 3.004 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1368 ; 5.264 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 473 ;32.211 ;24.271 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1698 ;11.618 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 60 ;13.472 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1675 ; 0.058 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12134 ; 0.002 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 2157 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2003 ; 0.179 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 7610 ; 0.171 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5306 ; 0.171 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 5668 ; 0.078 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 591 ; 0.124 ; 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): 17 ; 0.112 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 61 ; 0.152 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 15 ; 0.135 ; 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): 6993 ; 1.391 ; 5.000 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10878 ; 2.222 ;10.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4552 ; 1.293 ; 5.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3985 ; 2.093 ;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): 133.4040 12.4290 78.1640 REMARK 3 T TENSOR REMARK 3 T11: -0.1029 T22: 0.0070 REMARK 3 T33: -0.0580 T12: 0.0983 REMARK 3 T13: 0.0217 T23: 0.3594 REMARK 3 L TENSOR REMARK 3 L11: 9.8542 L22: 0.3473 REMARK 3 L33: 6.4696 L12: -1.7907 REMARK 3 L13: 2.3784 L23: -0.0729 REMARK 3 S TENSOR REMARK 3 S11: 0.0339 S12: 0.1518 S13: -0.7180 REMARK 3 S21: 0.5668 S22: -0.2769 S23: -1.0607 REMARK 3 S31: 1.0089 S32: 1.0814 S33: 0.2430 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): 129.4040 22.0220 68.7550 REMARK 3 T TENSOR REMARK 3 T11: -0.1418 T22: 0.0277 REMARK 3 T33: -0.0240 T12: 0.0489 REMARK 3 T13: 0.0390 T23: 0.2387 REMARK 3 L TENSOR REMARK 3 L11: 2.7069 L22: 3.1410 REMARK 3 L33: 1.8400 L12: -0.2144 REMARK 3 L13: -0.0018 L23: -0.3532 REMARK 3 S TENSOR REMARK 3 S11: -0.0892 S12: -0.1503 S13: -0.1357 REMARK 3 S21: -0.1263 S22: -0.0455 S23: -0.4889 REMARK 3 S31: 0.1904 S32: 0.3669 S33: 0.1348 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): 118.9160 33.7570 64.1670 REMARK 3 T TENSOR REMARK 3 T11: -0.0928 T22: 0.0068 REMARK 3 T33: 0.0256 T12: -0.0650 REMARK 3 T13: -0.0343 T23: 0.1521 REMARK 3 L TENSOR REMARK 3 L11: 0.9099 L22: 1.4825 REMARK 3 L33: 1.3487 L12: -0.5198 REMARK 3 L13: -0.6678 L23: -0.4323 REMARK 3 S TENSOR REMARK 3 S11: -0.0027 S12: -0.1389 S13: -0.0252 REMARK 3 S21: 0.1927 S22: -0.1496 S23: -0.3490 REMARK 3 S31: 0.0171 S32: 0.3760 S33: 0.1523 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): 107.3330 36.3070 63.4490 REMARK 3 T TENSOR REMARK 3 T11: -0.0715 T22: -0.0351 REMARK 3 T33: -0.0909 T12: -0.0901 REMARK 3 T13: -0.0449 T23: 0.0855 REMARK 3 L TENSOR REMARK 3 L11: 3.9776 L22: 1.9144 REMARK 3 L33: 2.2869 L12: -0.5619 REMARK 3 L13: -1.4956 L23: -0.2828 REMARK 3 S TENSOR REMARK 3 S11: 0.0639 S12: -0.0628 S13: -0.1976 REMARK 3 S21: 0.0128 S22: -0.2206 S23: 0.1439 REMARK 3 S31: -0.0167 S32: 0.0516 S33: 0.1567 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): 106.2780 24.6340 63.7060 REMARK 3 T TENSOR REMARK 3 T11: -0.0285 T22: -0.0524 REMARK 3 T33: -0.0262 T12: -0.0715 REMARK 3 T13: -0.0026 T23: 0.0657 REMARK 3 L TENSOR REMARK 3 L11: 0.8671 L22: 1.5963 REMARK 3 L33: 1.7222 L12: -0.0029 REMARK 3 L13: -0.6024 L23: -0.8380 REMARK 3 S TENSOR REMARK 3 S11: 0.0649 S12: 0.1272 S13: -0.0975 REMARK 3 S21: -0.0069 S22: -0.1357 S23: -0.0522 REMARK 3 S31: 0.2522 S32: -0.0776 S33: 0.0708 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): 100.0270 13.1980 72.0220 REMARK 3 T TENSOR REMARK 3 T11: 0.0021 T22: -0.1328 REMARK 3 T33: -0.0048 T12: -0.1155 REMARK 3 T13: 0.0785 T23: 0.0565 REMARK 3 L TENSOR REMARK 3 L11: 1.6649 L22: 2.9109 REMARK 3 L33: 3.6359 L12: -0.5156 REMARK 3 L13: -0.1259 L23: 0.2742 REMARK 3 S TENSOR REMARK 3 S11: -0.0958 S12: 0.0898 S13: -0.3031 REMARK 3 S21: -0.0647 S22: -0.1289 S23: 0.1013 REMARK 3 S31: 0.2493 S32: -0.1506 S33: 0.2247 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): 108.0460 7.3110 84.0410 REMARK 3 T TENSOR REMARK 3 T11: -0.0424 T22: -0.2635 REMARK 3 T33: -0.0313 T12: -0.0558 REMARK 3 T13: 0.0679 T23: 0.2231 REMARK 3 L TENSOR REMARK 3 L11: 3.7126 L22: 6.3929 REMARK 3 L33: 5.1977 L12: 0.0138 REMARK 3 L13: -0.3475 L23: 2.1607 REMARK 3 S TENSOR REMARK 3 S11: -0.0280 S12: -0.2419 S13: -0.4280 REMARK 3 S21: 0.3674 S22: 0.0743 S23: 0.0389 REMARK 3 S31: 0.5735 S32: 0.0404 S33: -0.0463 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): 110.8020 2.9720 78.3640 REMARK 3 T TENSOR REMARK 3 T11: 0.1381 T22: -0.2607 REMARK 3 T33: -0.0731 T12: 0.0115 REMARK 3 T13: 0.0688 T23: 0.2061 REMARK 3 L TENSOR REMARK 3 L11: 2.8436 L22: 3.5664 REMARK 3 L33: 3.9820 L12: 0.3144 REMARK 3 L13: -0.3963 L23: 1.3151 REMARK 3 S TENSOR REMARK 3 S11: -0.1009 S12: 0.0651 S13: -0.3432 REMARK 3 S21: -0.1734 S22: -0.2519 S23: -0.0339 REMARK 3 S31: 0.6679 S32: -0.0301 S33: 0.3528 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): 124.5510 7.7620 79.8450 REMARK 3 T TENSOR REMARK 3 T11: 0.0238 T22: -0.1271 REMARK 3 T33: 0.0063 T12: 0.1047 REMARK 3 T13: 0.0371 T23: 0.2581 REMARK 3 L TENSOR REMARK 3 L11: 2.7391 L22: 1.7804 REMARK 3 L33: 2.4070 L12: 0.0386 REMARK 3 L13: -0.3656 L23: -0.5098 REMARK 3 S TENSOR REMARK 3 S11: -0.0189 S12: -0.1973 S13: -0.3718 REMARK 3 S21: 0.2330 S22: -0.2935 S23: -0.4886 REMARK 3 S31: 0.5747 S32: 0.5560 S33: 0.3124 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): 106.8580 21.1190 168.7730 REMARK 3 T TENSOR REMARK 3 T11: 0.4843 T22: -0.3760 REMARK 3 T33: -0.3563 T12: 0.0725 REMARK 3 T13: -0.1775 T23: -0.1157 REMARK 3 L TENSOR REMARK 3 L11: 4.4435 L22: 3.4148 REMARK 3 L33: 7.2168 L12: -2.3896 REMARK 3 L13: 2.7182 L23: -3.0205 REMARK 3 S TENSOR REMARK 3 S11: -0.2317 S12: -0.7806 S13: -0.0312 REMARK 3 S21: 1.1365 S22: 0.3983 S23: -0.2074 REMARK 3 S31: -1.0758 S32: -0.7251 S33: -0.1666 REMARK 3 REMARK 3 TLS GROUP : 11 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 79 B 98 REMARK 3 ORIGIN FOR THE GROUP (A): 103.1110 30.0870 148.7500 REMARK 3 T TENSOR REMARK 3 T11: 0.5630 T22: -0.1505 REMARK 3 T33: -0.1705 T12: 0.1780 REMARK 3 T13: -0.0396 T23: 0.0256 REMARK 3 L TENSOR REMARK 3 L11: 9.1334 L22: 11.8711 REMARK 3 L33: 39.6766 L12: -5.9665 REMARK 3 L13: 18.4456 L23: -16.4466 REMARK 3 S TENSOR REMARK 3 S11: -1.2000 S12: -0.9643 S13: 0.5065 REMARK 3 S21: 1.4911 S22: 0.6796 S23: -0.6431 REMARK 3 S31: -3.3078 S32: -2.0432 S33: 0.5204 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): 97.6000 38.2160 104.0550 REMARK 3 T TENSOR REMARK 3 T11: 0.1784 T22: -0.0696 REMARK 3 T33: -0.0946 T12: -0.1777 REMARK 3 T13: 0.0296 T23: 0.0347 REMARK 3 L TENSOR REMARK 3 L11: 0.5361 L22: 0.4293 REMARK 3 L33: 3.0679 L12: -0.1732 REMARK 3 L13: -0.1769 L23: -1.0029 REMARK 3 S TENSOR REMARK 3 S11: -0.0258 S12: -0.1035 S13: -0.0277 REMARK 3 S21: 0.3452 S22: -0.0588 S23: -0.0048 REMARK 3 S31: -0.4315 S32: 0.0171 S33: 0.0846 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): 103.1110 34.3330 95.8090 REMARK 3 T TENSOR REMARK 3 T11: 0.0409 T22: -0.0734 REMARK 3 T33: -0.1158 T12: -0.1402 REMARK 3 T13: -0.0124 T23: 0.0631 REMARK 3 L TENSOR REMARK 3 L11: 1.7751 L22: 1.1894 REMARK 3 L33: 2.0008 L12: -0.3811 REMARK 3 L13: -0.9842 L23: -0.0941 REMARK 3 S TENSOR REMARK 3 S11: 0.0064 S12: -0.2674 S13: 0.0283 REMARK 3 S21: 0.3356 S22: -0.0664 S23: -0.1425 REMARK 3 S31: -0.0514 S32: 0.1559 S33: 0.0601 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): 100.2610 22.5570 130.5970 REMARK 3 T TENSOR REMARK 3 T11: 0.0767 T22: -0.1905 REMARK 3 T33: -0.1888 T12: -0.0218 REMARK 3 T13: 0.0455 T23: 0.0128 REMARK 3 L TENSOR REMARK 3 L11: 3.3791 L22: 3.1517 REMARK 3 L33: 23.7094 L12: -1.6520 REMARK 3 L13: 8.9365 L23: -4.7903 REMARK 3 S TENSOR REMARK 3 S11: 0.7051 S12: 0.4028 S13: -0.5122 REMARK 3 S21: -0.1137 S22: 0.1055 S23: -0.0459 REMARK 3 S31: 1.4974 S32: 0.4634 S33: -0.8106 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): 109.4840 28.0840 148.6830 REMARK 3 T TENSOR REMARK 3 T11: 0.3225 T22: -0.3978 REMARK 3 T33: -0.2316 T12: -0.1077 REMARK 3 T13: -0.0805 T23: 0.0332 REMARK 3 L TENSOR REMARK 3 L11: 4.5806 L22: 2.1046 REMARK 3 L33: 19.7418 L12: -1.1262 REMARK 3 L13: 7.3788 L23: -1.3520 REMARK 3 S TENSOR REMARK 3 S11: -0.2947 S12: 0.7425 S13: 0.0897 REMARK 3 S21: 0.7300 S22: 0.4744 S23: -0.7443 REMARK 3 S31: -1.8493 S32: 1.2909 S33: -0.1797 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): 119.4680 31.1090 182.6540 REMARK 3 T TENSOR REMARK 3 T11: 1.8135 T22: 0.5504 REMARK 3 T33: 0.4830 T12: -0.2024 REMARK 3 T13: -0.8420 T23: -0.2340 REMARK 3 L TENSOR REMARK 3 L11: 0.9676 L22: 13.5549 REMARK 3 L33: 9.1428 L12: 3.6215 REMARK 3 L13: -2.9743 L23: -11.1324 REMARK 3 S TENSOR REMARK 3 S11: -0.6064 S12: -2.1629 S13: 0.8326 REMARK 3 S21: 1.6236 S22: -0.1915 S23: -1.1158 REMARK 3 S31: -3.0834 S32: 3.1376 S33: 0.7979 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): 90.0490 36.8710 33.2470 REMARK 3 T TENSOR REMARK 3 T11: -0.0643 T22: 0.0136 REMARK 3 T33: 0.0524 T12: -0.2048 REMARK 3 T13: -0.0610 T23: 0.0391 REMARK 3 L TENSOR REMARK 3 L11: 7.2173 L22: 4.8143 REMARK 3 L33: 10.8333 L12: -5.1507 REMARK 3 L13: 5.8943 L23: -5.2659 REMARK 3 S TENSOR REMARK 3 S11: 0.3702 S12: 0.5788 S13: -0.7370 REMARK 3 S21: -0.6322 S22: -0.1115 S23: 0.2980 REMARK 3 S31: 0.8421 S32: 0.1383 S33: -0.2587 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): 94.2600 42.2240 41.1920 REMARK 3 T TENSOR REMARK 3 T11: -0.1649 T22: -0.0173 REMARK 3 T33: -0.0565 T12: -0.0440 REMARK 3 T13: -0.0016 T23: 0.0377 REMARK 3 L TENSOR REMARK 3 L11: 3.4314 L22: 2.5418 REMARK 3 L33: 3.0549 L12: -0.4056 REMARK 3 L13: 1.1968 L23: -0.8031 REMARK 3 S TENSOR REMARK 3 S11: -0.0082 S12: -0.1078 S13: -0.1308 REMARK 3 S21: 0.0984 S22: -0.0588 S23: 0.0604 REMARK 3 S31: 0.2327 S32: -0.1015 S33: 0.0670 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): 94.0800 43.0920 43.4110 REMARK 3 T TENSOR REMARK 3 T11: -0.1406 T22: -0.0459 REMARK 3 T33: -0.0318 T12: -0.0726 REMARK 3 T13: 0.0036 T23: 0.0467 REMARK 3 L TENSOR REMARK 3 L11: 3.5601 L22: 1.3828 REMARK 3 L33: 3.4154 L12: -0.7327 REMARK 3 L13: 1.4730 L23: -1.3824 REMARK 3 S TENSOR REMARK 3 S11: -0.0680 S12: -0.1130 S13: 0.1271 REMARK 3 S21: 0.0080 S22: 0.0136 S23: 0.0622 REMARK 3 S31: 0.1607 S32: -0.1866 S33: 0.0545 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): 86.4710 47.7740 12.7570 REMARK 3 T TENSOR REMARK 3 T11: -0.2089 T22: 0.1014 REMARK 3 T33: 0.0325 T12: -0.0759 REMARK 3 T13: -0.0732 T23: 0.0524 REMARK 3 L TENSOR REMARK 3 L11: 1.3523 L22: 1.3247 REMARK 3 L33: 3.5701 L12: -0.9360 REMARK 3 L13: -0.4568 L23: 1.2659 REMARK 3 S TENSOR REMARK 3 S11: 0.0522 S12: 0.2290 S13: -0.0788 REMARK 3 S21: -0.1586 S22: -0.0962 S23: 0.0927 REMARK 3 S31: -0.1893 S32: -0.5180 S33: 0.0440 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): 92.5870 44.8460 4.7260 REMARK 3 T TENSOR REMARK 3 T11: -0.1608 T22: -0.0882 REMARK 3 T33: -0.1118 T12: 0.0553 REMARK 3 T13: -0.0825 T23: 0.0011 REMARK 3 L TENSOR REMARK 3 L11: 5.5062 L22: 1.2383 REMARK 3 L33: 12.9400 L12: -0.3213 REMARK 3 L13: -4.1538 L23: 1.2934 REMARK 3 S TENSOR REMARK 3 S11: 0.1654 S12: 0.3948 S13: -0.4307 REMARK 3 S21: -0.1370 S22: 0.0601 S23: -0.2344 REMARK 3 S31: 1.2814 S32: -0.1713 S33: -0.2254 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): 94.5950 47.6160 9.2290 REMARK 3 T TENSOR REMARK 3 T11: -0.1571 T22: -0.1775 REMARK 3 T33: -0.1560 T12: 0.1001 REMARK 3 T13: -0.0247 T23: 0.0570 REMARK 3 L TENSOR REMARK 3 L11: 6.3813 L22: 3.4021 REMARK 3 L33: 13.2127 L12: 0.2307 REMARK 3 L13: -1.4830 L23: 0.5180 REMARK 3 S TENSOR REMARK 3 S11: 0.2216 S12: -0.0428 S13: 0.0009 REMARK 3 S21: -0.2578 S22: -0.1102 S23: 0.3331 REMARK 3 S31: 0.5495 S32: 0.1618 S33: -0.1114 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): 93.9740 40.6180 -3.6560 REMARK 3 T TENSOR REMARK 3 T11: 0.6228 T22: 0.0237 REMARK 3 T33: -0.0444 T12: 0.2667 REMARK 3 T13: -0.0145 T23: -0.0992 REMARK 3 L TENSOR REMARK 3 L11: 9.6159 L22: 2.2700 REMARK 3 L33: 8.2544 L12: -2.1416 REMARK 3 L13: -3.2842 L23: 4.3077 REMARK 3 S TENSOR REMARK 3 S11: 0.4565 S12: 0.4901 S13: -1.5845 REMARK 3 S21: -0.1981 S22: -1.0473 S23: -0.2150 REMARK 3 S31: 0.0962 S32: 0.4463 S33: 0.5908 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): 86.2090 44.2280 -2.4190 REMARK 3 T TENSOR REMARK 3 T11: -0.1162 T22: 0.1289 REMARK 3 T33: -0.2363 T12: 0.0370 REMARK 3 T13: -0.2522 T23: -0.0570 REMARK 3 L TENSOR REMARK 3 L11: 12.1279 L22: 9.6128 REMARK 3 L33: 24.7977 L12: 8.3666 REMARK 3 L13: -13.6939 L23: -6.4038 REMARK 3 S TENSOR REMARK 3 S11: -0.3114 S12: 0.9509 S13: -0.4901 REMARK 3 S21: -1.1936 S22: 0.3881 S23: 0.8933 REMARK 3 S31: 1.5849 S32: -1.4770 S33: -0.0768 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): 114.3650 50.3300 35.0740 REMARK 3 T TENSOR REMARK 3 T11: -0.1189 T22: 0.0431 REMARK 3 T33: 0.0581 T12: 0.0232 REMARK 3 T13: 0.0028 T23: 0.1284 REMARK 3 L TENSOR REMARK 3 L11: 1.0139 L22: 0.6984 REMARK 3 L33: 0.5101 L12: 0.6109 REMARK 3 L13: -0.3612 L23: -0.5726 REMARK 3 S TENSOR REMARK 3 S11: 0.0496 S12: 0.1401 S13: 0.0766 REMARK 3 S21: -0.1047 S22: -0.0864 S23: -0.0197 REMARK 3 S31: -0.0230 S32: 0.1315 S33: 0.0369 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): 113.7050 39.4180 36.1360 REMARK 3 T TENSOR REMARK 3 T11: -0.0513 T22: 0.0310 REMARK 3 T33: 0.0104 T12: 0.0151 REMARK 3 T13: -0.0065 T23: 0.0383 REMARK 3 L TENSOR REMARK 3 L11: 3.8357 L22: 1.4014 REMARK 3 L33: 2.2041 L12: -0.0739 REMARK 3 L13: -0.2406 L23: -1.7459 REMARK 3 S TENSOR REMARK 3 S11: 0.1034 S12: 0.4733 S13: -0.2887 REMARK 3 S21: -0.1626 S22: 0.0390 S23: -0.0393 REMARK 3 S31: 0.6029 S32: 0.2706 S33: -0.1424 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): 112.4640 45.9050 35.5200 REMARK 3 T TENSOR REMARK 3 T11: -0.1338 T22: -0.0267 REMARK 3 T33: -0.0288 T12: 0.0048 REMARK 3 T13: -0.0446 T23: 0.0868 REMARK 3 L TENSOR REMARK 3 L11: 4.6879 L22: 0.6861 REMARK 3 L33: 4.2853 L12: 0.1199 REMARK 3 L13: -2.2718 L23: -0.4841 REMARK 3 S TENSOR REMARK 3 S11: -0.0925 S12: 0.2550 S13: -0.1202 REMARK 3 S21: -0.0392 S22: -0.0480 S23: 0.0748 REMARK 3 S31: 0.2667 S32: 0.0928 S33: 0.1406 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): 100.4580 53.2970 8.1810 REMARK 3 T TENSOR REMARK 3 T11: -0.1323 T22: 0.1424 REMARK 3 T33: -0.0170 T12: 0.0601 REMARK 3 T13: 0.0212 T23: 0.0559 REMARK 3 L TENSOR REMARK 3 L11: 1.6319 L22: 2.1707 REMARK 3 L33: 7.5284 L12: -1.6304 REMARK 3 L13: 3.2544 L23: -2.5014 REMARK 3 S TENSOR REMARK 3 S11: 0.5145 S12: 0.2071 S13: -0.2084 REMARK 3 S21: -0.3897 S22: -0.3058 S23: 0.1412 REMARK 3 S31: 0.7217 S32: 0.2342 S33: -0.2087 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): 101.6260 59.8920 8.8210 REMARK 3 T TENSOR REMARK 3 T11: -0.2183 T22: 0.2243 REMARK 3 T33: -0.1287 T12: 0.0129 REMARK 3 T13: -0.0081 T23: 0.0596 REMARK 3 L TENSOR REMARK 3 L11: 5.4667 L22: 7.7987 REMARK 3 L33: 2.5708 L12: -5.4148 REMARK 3 L13: 3.2560 L23: -1.9850 REMARK 3 S TENSOR REMARK 3 S11: -0.1138 S12: -0.1298 S13: 0.5189 REMARK 3 S21: 0.1965 S22: -0.0814 S23: -0.3896 REMARK 3 S31: -0.0436 S32: 0.4265 S33: 0.1953 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): 95.1450 60.2460 2.9720 REMARK 3 T TENSOR REMARK 3 T11: -0.2195 T22: 0.0943 REMARK 3 T33: -0.1534 T12: 0.0339 REMARK 3 T13: 0.0068 T23: 0.0477 REMARK 3 L TENSOR REMARK 3 L11: 7.5391 L22: 3.8034 REMARK 3 L33: 3.8771 L12: -3.3657 REMARK 3 L13: 2.8744 L23: -1.4300 REMARK 3 S TENSOR REMARK 3 S11: -0.0818 S12: 0.3458 S13: 0.0266 REMARK 3 S21: -0.2967 S22: -0.0848 S23: -0.0051 REMARK 3 S31: 0.0326 S32: 0.0873 S33: 0.1666 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): 102.9720 62.6710 -2.0370 REMARK 3 T TENSOR REMARK 3 T11: -0.2154 T22: 0.2462 REMARK 3 T33: -0.1136 T12: 0.1244 REMARK 3 T13: 0.0726 T23: 0.1676 REMARK 3 L TENSOR REMARK 3 L11: 2.2961 L22: 6.0706 REMARK 3 L33: 4.4701 L12: -1.4101 REMARK 3 L13: -1.7455 L23: -2.9727 REMARK 3 S TENSOR REMARK 3 S11: -0.0966 S12: 1.5287 S13: 0.2088 REMARK 3 S21: -0.3934 S22: -0.5259 S23: -0.2768 REMARK 3 S31: -0.3359 S32: 1.2219 S33: 0.6225 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 1TY3. 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 ALSO REMARK 3 CORRECTED. REMARK 4 REMARK 4 2VDK 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-34076. 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 : 55875 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 (%) : 99.9 REMARK 200 DATA REDUNDANCY : 7.5 REMARK 200 R MERGE (I) : 0.13 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.00 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.68 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.10 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 1TXV 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 117.42467 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 58.71233 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 58.71233 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 117.42467 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: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 10550 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 71610 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.7 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 SER B 78 REMARK 465 GLY H 135 REMARK 465 ASP H 136 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O HOH B 4024 O HOH B 4109 1.93 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 ASN A 2 46.65 -141.69 REMARK 500 SER A 101 -120.66 48.01 REMARK 500 LYS A 118 -127.49 50.98 REMARK 500 GLU A 123 134.62 105.31 REMARK 500 SER A 144 72.46 -150.75 REMARK 500 LEU A 212 -45.97 74.62 REMARK 500 THR B 7 50.25 -95.32 REMARK 500 ARG B 8 66.06 -154.57 REMARK 500 VAL B 10 73.84 40.72 REMARK 500 ASP B 47 30.22 -99.46 REMARK 500 PHE B 56 79.48 -151.35 REMARK 500 ASP B 66 58.11 -146.54 REMARK 500 VAL B 80 96.62 64.05 REMARK 500 ASN B 148 37.22 -94.27 REMARK 500 VAL B 157 -83.55 -126.48 REMARK 500 SER B 213 -154.20 -117.05 REMARK 500 LYS B 253 172.18 -57.91 REMARK 500 LEU B 258 -8.38 86.48 REMARK 500 LYS B 410 -28.71 76.14 REMARK 500 GLU B 442 71.57 57.74 REMARK 500 HIS B 446 -65.03 68.36 REMARK 500 THR B 454 120.18 66.08 REMARK 500 TYR H 101 -59.04 -122.06 REMARK 500 SER L 30 65.63 24.50 REMARK 500 SER L 77 73.98 56.10 REMARK 500 LYS L 169 -64.61 -95.34 REMARK 500 ASN L 212 70.80 49.56 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 110.9 REMARK 620 3 CAC B1462 O2 110.3 106.7 REMARK 620 4 CAC B1462 C1 108.9 110.5 109.5 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 48.4 REMARK 620 3 ASP A 245 OD2 120.7 72.4 REMARK 620 4 ASP A 247 O 74.5 71.8 92.1 REMARK 620 5 THR A 250 C 91.8 139.1 146.9 90.8 REMARK 620 6 THR A 250 O 71.2 118.3 165.2 82.5 20.8 REMARK 620 7 THR A 250 OG1 142.2 145.2 87.9 80.7 60.1 77.7 REMARK 620 8 GLU A 252 OE1 81.2 79.1 85.4 150.2 107.2 106.0 128.8 REMARK 620 9 GLU A 252 OE2 123.7 125.6 85.2 159.9 80.9 95.1 79.3 49.6 REMARK 620 N 1 2 3 4 5 6 7 8 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 77.7 REMARK 620 3 ARG A 303 O 167.0 98.3 REMARK 620 4 ASP A 297 OD1 84.8 77.2 82.3 REMARK 620 5 ASP A 305 OD1 101.7 150.6 87.8 132.2 REMARK 620 6 ASP A 305 OD2 78.2 152.6 102.3 87.9 48.8 REMARK 620 7 HOH A4180 O 89.1 77.2 102.1 154.4 73.4 115.2 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A2006 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 365 OD2 REMARK 620 2 ASP A 369 OD1 80.5 REMARK 620 3 TYR A 371 O 74.3 87.4 REMARK 620 4 ASP A 367 OD1 87.8 98.5 160.1 REMARK 620 5 HOH A4206 O 149.3 69.5 97.5 102.4 REMARK 620 6 ASP A 373 OD1 95.9 171.8 98.7 73.9 114.7 REMARK 620 7 ASP A 373 OD2 131.3 139.4 80.3 106.1 74.0 47.8 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 91.6 REMARK 620 3 ASP A 426 OD1 73.4 86.1 REMARK 620 4 ASP A 428 OD1 150.1 87.0 76.7 REMARK 620 5 ASP A 434 OD1 102.4 163.3 89.1 76.3 REMARK 620 6 ASP A 434 OD2 89.2 142.1 130.0 109.9 48.6 REMARK 620 7 HOH A4217 O 141.6 84.6 143.8 67.9 89.9 71.9 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 O2 REMARK 620 2 HOH B4125 O 94.7 REMARK 620 3 ASP B 127 OD1 85.5 178.3 REMARK 620 4 ASP B 251 OD2 121.7 89.9 88.6 REMARK 620 5 GOL B1463 O1 62.2 67.8 110.9 66.4 REMARK 620 6 SER B 123 O 158.4 85.5 94.9 79.9 136.0 REMARK 620 7 ASP B 126 OD1 83.6 101.8 79.9 151.5 142.1 75.3 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B2003 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 217 O REMARK 620 2 ASP B 158 OD2 158.2 REMARK 620 3 ASN B 215 OD1 96.1 100.5 REMARK 620 4 ASP B 217 OD1 73.3 92.3 90.8 REMARK 620 5 PRO B 219 O 84.2 80.4 175.2 93.8 REMARK 620 6 GLU B 220 OE2 94.4 101.2 83.9 166.1 91.3 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 B4060 O 84.0 REMARK 620 3 SER B 121 OG 86.2 169.0 REMARK 620 4 SER B 123 OG 172.5 95.5 94.9 REMARK 620 5 HOH B4014 O 101.2 94.2 82.9 86.4 REMARK 620 6 CAC B1462 O1 92.6 100.3 85.1 80.1 161.0 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 GOL A1453 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2004 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2005 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2006 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2007 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A3015 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A3249 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC B1462 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1463 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B2001 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2002 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2003 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3099 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF REMARK 800 SUGAR BOUND TO ASN B 320 RESIDUES 3320 TO 3324 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF REMARK 800 SUGAR BOUND TO ASN B 371 RESIDUES 3371 TO 3377 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: 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.