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. 3.10 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) : 3.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.72 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7 REMARK 3 NUMBER OF REFLECTIONS : 38636 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) : 0.179 REMARK 3 R VALUE (WORKING SET) : 0.177 REMARK 3 FREE R VALUE : 0.217 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2044 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) : 3.10 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.18 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2679 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.58 REMARK 3 BIN R VALUE (WORKING SET) : 0.2920 REMARK 3 BIN FREE R VALUE SET COUNT : 140 REMARK 3 BIN FREE R VALUE : 0.3160 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 10348 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 240 REMARK 3 SOLVENT ATOMS : 98 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) : 3.21 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.04000 REMARK 3 B22 (A**2) : 1.04000 REMARK 3 B33 (A**2) : -1.56000 REMARK 3 B12 (A**2) : 0.52000 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): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.362 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.254 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 31.235 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.933 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10860 ; 0.006 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 7271 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14811 ; 1.001 ; 1.982 REMARK 3 BOND ANGLES OTHERS (DEGREES): 17626 ; 0.765 ; 3.005 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1348 ; 5.376 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 466 ;33.205 ;24.292 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1682 ;13.057 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 58 ;14.475 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1664 ; 0.058 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12050 ; 0.002 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 2134 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2083 ; 0.184 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 7418 ; 0.173 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5297 ; 0.173 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 5762 ; 0.081 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 310 ; 0.136 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.005 ; 0.200 REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 24 ; 0.113 ; 0.200 REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 12 ; 0.103 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 45 ; 0.147 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 7 ; 0.110 ; 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): 6945 ; 0.826 ; 5.000 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2727 ; 0.100 ; 5.000 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10816 ; 1.274 ;10.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4563 ; 0.955 ; 5.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3992 ; 1.692 ;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): 133.5730 13.0120 78.0960 REMARK 3 T TENSOR REMARK 3 T11: 0.0406 T22: 0.1421 REMARK 3 T33: 0.0197 T12: 0.1444 REMARK 3 T13: -0.0308 T23: 0.3019 REMARK 3 L TENSOR REMARK 3 L11: 9.7233 L22: 9.8242 REMARK 3 L33: 4.7945 L12: -7.8655 REMARK 3 L13: 0.8507 L23: -4.7303 REMARK 3 S TENSOR REMARK 3 S11: -0.0457 S12: 0.0475 S13: -0.3473 REMARK 3 S21: 0.5761 S22: -0.6331 S23: -1.2072 REMARK 3 S31: 1.0696 S32: 0.9782 S33: 0.6789 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): 129.5560 22.2700 68.7960 REMARK 3 T TENSOR REMARK 3 T11: -0.1030 T22: 0.0917 REMARK 3 T33: -0.0742 T12: 0.0991 REMARK 3 T13: 0.0537 T23: 0.2708 REMARK 3 L TENSOR REMARK 3 L11: 3.8477 L22: 3.4879 REMARK 3 L33: 1.8232 L12: 1.3684 REMARK 3 L13: -0.2222 L23: -0.9387 REMARK 3 S TENSOR REMARK 3 S11: 0.0212 S12: 0.0194 S13: -0.3973 REMARK 3 S21: -0.1557 S22: -0.1482 S23: -0.4809 REMARK 3 S31: 0.3790 S32: 0.1561 S33: 0.1271 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): 119.0040 33.9930 64.2150 REMARK 3 T TENSOR REMARK 3 T11: -0.1919 T22: -0.1192 REMARK 3 T33: -0.1711 T12: -0.0474 REMARK 3 T13: 0.0058 T23: 0.1445 REMARK 3 L TENSOR REMARK 3 L11: 0.9567 L22: 3.1950 REMARK 3 L33: 1.6406 L12: -0.5012 REMARK 3 L13: 0.0272 L23: -0.8960 REMARK 3 S TENSOR REMARK 3 S11: -0.0842 S12: -0.0768 S13: -0.0439 REMARK 3 S21: 0.1416 S22: -0.0189 S23: -0.5303 REMARK 3 S31: 0.0429 S32: 0.3906 S33: 0.1031 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): 107.4350 36.4570 63.5140 REMARK 3 T TENSOR REMARK 3 T11: -0.1325 T22: -0.1544 REMARK 3 T33: -0.2854 T12: -0.1121 REMARK 3 T13: -0.0522 T23: 0.1009 REMARK 3 L TENSOR REMARK 3 L11: 5.6353 L22: 2.0276 REMARK 3 L33: 3.4132 L12: -1.1640 REMARK 3 L13: -2.7311 L23: 0.1694 REMARK 3 S TENSOR REMARK 3 S11: -0.0299 S12: -0.0699 S13: -0.3453 REMARK 3 S21: -0.0464 S22: -0.1007 S23: 0.1070 REMARK 3 S31: 0.0081 S32: -0.1374 S33: 0.1306 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): 106.4540 24.8460 63.7150 REMARK 3 T TENSOR REMARK 3 T11: -0.0865 T22: -0.2450 REMARK 3 T33: -0.2032 T12: -0.0433 REMARK 3 T13: 0.0069 T23: 0.0893 REMARK 3 L TENSOR REMARK 3 L11: 1.8596 L22: 1.5553 REMARK 3 L33: 2.3250 L12: 0.3821 REMARK 3 L13: -0.7449 L23: -1.0472 REMARK 3 S TENSOR REMARK 3 S11: 0.0033 S12: 0.0563 S13: -0.2640 REMARK 3 S21: -0.0753 S22: -0.0986 S23: 0.0355 REMARK 3 S31: 0.1975 S32: -0.2109 S33: 0.0953 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): 100.2240 13.4080 72.0960 REMARK 3 T TENSOR REMARK 3 T11: 0.0212 T22: -0.1514 REMARK 3 T33: -0.1321 T12: -0.1647 REMARK 3 T13: 0.0524 T23: 0.0636 REMARK 3 L TENSOR REMARK 3 L11: 0.9028 L22: 3.7926 REMARK 3 L33: 4.2225 L12: 0.1094 REMARK 3 L13: 0.5209 L23: -0.1050 REMARK 3 S TENSOR REMARK 3 S11: -0.0504 S12: 0.1696 S13: -0.4334 REMARK 3 S21: -0.0438 S22: -0.1123 S23: 0.0084 REMARK 3 S31: 0.2764 S32: -0.1615 S33: 0.1627 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): 108.2260 7.5310 84.1150 REMARK 3 T TENSOR REMARK 3 T11: 0.0854 T22: -0.1632 REMARK 3 T33: -0.0551 T12: -0.0628 REMARK 3 T13: 0.0531 T23: 0.2434 REMARK 3 L TENSOR REMARK 3 L11: 3.2237 L22: 6.0694 REMARK 3 L33: 9.9055 L12: -0.3869 REMARK 3 L13: -1.0962 L23: 3.7616 REMARK 3 S TENSOR REMARK 3 S11: -0.3077 S12: -0.3149 S13: -0.4480 REMARK 3 S21: 0.4591 S22: -0.0723 S23: 0.1755 REMARK 3 S31: 0.4973 S32: -0.3913 S33: 0.3800 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): 110.9950 3.2570 78.4320 REMARK 3 T TENSOR REMARK 3 T11: 0.2313 T22: -0.2002 REMARK 3 T33: -0.0587 T12: -0.0160 REMARK 3 T13: 0.0364 T23: 0.2428 REMARK 3 L TENSOR REMARK 3 L11: 2.6463 L22: 4.9412 REMARK 3 L33: 5.4110 L12: -0.9434 REMARK 3 L13: -1.6576 L23: 1.7060 REMARK 3 S TENSOR REMARK 3 S11: -0.0747 S12: -0.0630 S13: -0.4393 REMARK 3 S21: -0.0460 S22: -0.3097 S23: 0.1195 REMARK 3 S31: 0.8004 S32: -0.0954 S33: 0.3844 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): 124.7340 8.0010 79.9050 REMARK 3 T TENSOR REMARK 3 T11: 0.1271 T22: -0.0060 REMARK 3 T33: 0.0458 T12: 0.1278 REMARK 3 T13: 0.0306 T23: 0.3077 REMARK 3 L TENSOR REMARK 3 L11: 2.9086 L22: 3.7805 REMARK 3 L33: 2.8693 L12: 0.1687 REMARK 3 L13: -0.3903 L23: 0.6711 REMARK 3 S TENSOR REMARK 3 S11: -0.0591 S12: -0.1427 S13: -0.5477 REMARK 3 S21: 0.2430 S22: -0.2263 S23: -0.3451 REMARK 3 S31: 0.5283 S32: 0.4294 S33: 0.2853 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): 106.9090 20.9570 168.9110 REMARK 3 T TENSOR REMARK 3 T11: 1.0168 T22: 0.2120 REMARK 3 T33: 0.2082 T12: 0.0805 REMARK 3 T13: -0.1474 T23: -0.0599 REMARK 3 L TENSOR REMARK 3 L11: 2.6266 L22: 2.1911 REMARK 3 L33: 5.5584 L12: -0.8147 REMARK 3 L13: 0.8506 L23: -1.3765 REMARK 3 S TENSOR REMARK 3 S11: -0.1874 S12: -0.6527 S13: 0.0518 REMARK 3 S21: 1.1439 S22: 0.3860 S23: -0.0331 REMARK 3 S31: -1.1070 S32: -0.5534 S33: -0.1986 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 77 B 98 REMARK 3 ORIGIN FOR THE GROUP (A): 103.1860 29.9910 148.8370 REMARK 3 T TENSOR REMARK 3 T11: 0.8430 T22: 0.1847 REMARK 3 T33: 0.0081 T12: 0.1245 REMARK 3 T13: 0.0110 T23: 0.0411 REMARK 3 L TENSOR REMARK 3 L11: 13.7237 L22: 13.2644 REMARK 3 L33: 51.5541 L12: -8.7802 REMARK 3 L13: 24.8373 L23: -22.9964 REMARK 3 S TENSOR REMARK 3 S11: -1.0104 S12: -0.5707 S13: 0.8636 REMARK 3 S21: 1.0820 S22: 0.4117 S23: -0.6305 REMARK 3 S31: -2.3692 S32: -1.7584 S33: 0.5988 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): 97.8460 38.4080 104.1600 REMARK 3 T TENSOR REMARK 3 T11: 0.2278 T22: 0.0291 REMARK 3 T33: -0.1668 T12: -0.2152 REMARK 3 T13: 0.0546 T23: 0.0217 REMARK 3 L TENSOR REMARK 3 L11: 0.5819 L22: 1.2467 REMARK 3 L33: 4.5437 L12: -0.0224 REMARK 3 L13: -0.8880 L23: -1.9589 REMARK 3 S TENSOR REMARK 3 S11: 0.0381 S12: -0.3156 S13: -0.0585 REMARK 3 S21: 0.6503 S22: -0.1325 S23: 0.1323 REMARK 3 S31: -0.8019 S32: 0.0002 S33: 0.0944 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): 103.3900 34.6080 95.9020 REMARK 3 T TENSOR REMARK 3 T11: 0.0580 T22: -0.0636 REMARK 3 T33: -0.1926 T12: -0.1628 REMARK 3 T13: -0.0154 T23: 0.1176 REMARK 3 L TENSOR REMARK 3 L11: 2.0073 L22: 1.2509 REMARK 3 L33: 2.7756 L12: -0.3685 REMARK 3 L13: -1.6745 L23: 0.3476 REMARK 3 S TENSOR REMARK 3 S11: 0.0685 S12: -0.3889 S13: 0.0811 REMARK 3 S21: 0.4148 S22: -0.0218 S23: -0.0591 REMARK 3 S31: -0.1479 S32: 0.1494 S33: -0.0467 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): 100.4480 22.5980 130.6160 REMARK 3 T TENSOR REMARK 3 T11: 0.5002 T22: 0.0555 REMARK 3 T33: 0.1507 T12: -0.0530 REMARK 3 T13: 0.0692 T23: 0.0297 REMARK 3 L TENSOR REMARK 3 L11: 2.5283 L22: 2.3465 REMARK 3 L33: 23.1227 L12: -1.9371 REMARK 3 L13: 7.5971 L23: -5.3163 REMARK 3 S TENSOR REMARK 3 S11: 0.6399 S12: 0.4877 S13: -0.7756 REMARK 3 S21: 0.0116 S22: 0.2666 S23: -0.0774 REMARK 3 S31: 1.3751 S32: 0.5835 S33: -0.9065 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): 109.5880 27.9880 148.8070 REMARK 3 T TENSOR REMARK 3 T11: 0.8653 T22: 0.0843 REMARK 3 T33: 0.2600 T12: -0.0824 REMARK 3 T13: -0.0783 T23: 0.0791 REMARK 3 L TENSOR REMARK 3 L11: 4.3730 L22: 1.7347 REMARK 3 L33: 14.5426 L12: -0.1485 REMARK 3 L13: 5.5094 L23: 0.2158 REMARK 3 S TENSOR REMARK 3 S11: -0.1767 S12: 0.5676 S13: 0.2948 REMARK 3 S21: 1.0943 S22: 0.2611 S23: -0.5232 REMARK 3 S31: -1.2100 S32: 1.3723 S33: -0.0844 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): 119.5790 31.0630 182.8940 REMARK 3 T TENSOR REMARK 3 T11: 1.8212 T22: 1.3637 REMARK 3 T33: 1.0727 T12: -0.0828 REMARK 3 T13: -0.5430 T23: -0.1406 REMARK 3 L TENSOR REMARK 3 L11: 0.6357 L22: 0.6411 REMARK 3 L33: 4.4959 L12: 0.6384 REMARK 3 L13: -1.6906 L23: -1.6977 REMARK 3 S TENSOR REMARK 3 S11: -1.4228 S12: -1.8904 S13: 1.1246 REMARK 3 S21: -0.1932 S22: 0.8610 S23: -1.1110 REMARK 3 S31: -1.0563 S32: 1.7807 S33: 0.5618 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): 90.3620 36.9200 33.2110 REMARK 3 T TENSOR REMARK 3 T11: -0.1189 T22: -0.1249 REMARK 3 T33: -0.0849 T12: -0.3076 REMARK 3 T13: -0.0191 T23: 0.0922 REMARK 3 L TENSOR REMARK 3 L11: 15.6157 L22: 3.7773 REMARK 3 L33: 10.2503 L12: -6.9231 REMARK 3 L13: 4.0389 L23: 0.7624 REMARK 3 S TENSOR REMARK 3 S11: 0.3154 S12: 0.6752 S13: -1.2006 REMARK 3 S21: -0.6069 S22: -0.2291 S23: 0.4775 REMARK 3 S31: 0.8967 S32: 0.0558 S33: -0.0863 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): 94.3930 42.4780 41.0960 REMARK 3 T TENSOR REMARK 3 T11: -0.2340 T22: -0.1544 REMARK 3 T33: -0.2586 T12: -0.0319 REMARK 3 T13: -0.0294 T23: 0.0565 REMARK 3 L TENSOR REMARK 3 L11: 5.2194 L22: 0.6976 REMARK 3 L33: 2.1765 L12: -0.4427 REMARK 3 L13: 0.8341 L23: 1.0906 REMARK 3 S TENSOR REMARK 3 S11: 0.0398 S12: -0.0652 S13: -0.0167 REMARK 3 S21: 0.2409 S22: 0.1420 S23: 0.3545 REMARK 3 S31: 0.1822 S32: -0.2283 S33: -0.1818 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): 94.1990 43.2560 43.3680 REMARK 3 T TENSOR REMARK 3 T11: -0.2006 T22: -0.1311 REMARK 3 T33: -0.1666 T12: -0.0833 REMARK 3 T13: -0.0021 T23: 0.0852 REMARK 3 L TENSOR REMARK 3 L11: 2.7901 L22: 1.1798 REMARK 3 L33: 2.7387 L12: -0.8617 REMARK 3 L13: 1.4035 L23: -0.3516 REMARK 3 S TENSOR REMARK 3 S11: -0.1055 S12: -0.1157 S13: 0.3006 REMARK 3 S21: -0.1011 S22: 0.0216 S23: 0.0924 REMARK 3 S31: 0.2079 S32: -0.2820 S33: 0.0838 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): 86.5420 47.8560 12.7660 REMARK 3 T TENSOR REMARK 3 T11: -0.1842 T22: 0.0386 REMARK 3 T33: -0.0562 T12: -0.1326 REMARK 3 T13: -0.1222 T23: 0.0501 REMARK 3 L TENSOR REMARK 3 L11: 2.7396 L22: 1.4694 REMARK 3 L33: 3.1798 L12: -0.9205 REMARK 3 L13: -0.0720 L23: 1.5262 REMARK 3 S TENSOR REMARK 3 S11: 0.0753 S12: 0.4461 S13: -0.2291 REMARK 3 S21: -0.2657 S22: 0.1350 S23: 0.3114 REMARK 3 S31: -0.2434 S32: -1.0382 S33: -0.2103 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): 92.6920 45.0410 4.6570 REMARK 3 T TENSOR REMARK 3 T11: 0.1143 T22: 0.0222 REMARK 3 T33: 0.0276 T12: 0.0048 REMARK 3 T13: -0.1524 T23: 0.0460 REMARK 3 L TENSOR REMARK 3 L11: 10.1294 L22: 3.7238 REMARK 3 L33: 9.2798 L12: -0.7088 REMARK 3 L13: -4.8806 L23: 1.3913 REMARK 3 S TENSOR REMARK 3 S11: -0.0047 S12: 0.6207 S13: -0.1050 REMARK 3 S21: -0.3107 S22: 0.2086 S23: -0.2041 REMARK 3 S31: 1.4446 S32: -0.6714 S33: -0.2039 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): 94.7300 47.7230 9.1520 REMARK 3 T TENSOR REMARK 3 T11: 0.0135 T22: -0.0854 REMARK 3 T33: -0.1461 T12: -0.0064 REMARK 3 T13: -0.0922 T23: 0.0120 REMARK 3 L TENSOR REMARK 3 L11: 4.0626 L22: 2.9704 REMARK 3 L33: 12.5899 L12: 2.0444 REMARK 3 L13: -0.0379 L23: -4.9632 REMARK 3 S TENSOR REMARK 3 S11: 0.3822 S12: 0.0532 S13: 0.1687 REMARK 3 S21: -0.2039 S22: -0.3684 S23: 0.1098 REMARK 3 S31: 0.5898 S32: 0.0894 S33: -0.0138 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): 94.1900 40.8090 -3.7300 REMARK 3 T TENSOR REMARK 3 T11: 0.7315 T22: 0.1663 REMARK 3 T33: 0.0508 T12: 0.1744 REMARK 3 T13: 0.0128 T23: -0.0490 REMARK 3 L TENSOR REMARK 3 L11: 4.3736 L22: 1.7869 REMARK 3 L33: 2.7151 L12: 0.9340 REMARK 3 L13: 3.2775 L23: 1.3412 REMARK 3 S TENSOR REMARK 3 S11: 0.3938 S12: 0.2796 S13: -1.3141 REMARK 3 S21: -0.5929 S22: -0.4154 S23: -0.2270 REMARK 3 S31: 1.0547 S32: 0.8618 S33: 0.0216 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): 86.3360 44.3670 -2.5030 REMARK 3 T TENSOR REMARK 3 T11: -0.0010 T22: 0.3618 REMARK 3 T33: 0.0811 T12: -0.0702 REMARK 3 T13: -0.1904 T23: -0.0206 REMARK 3 L TENSOR REMARK 3 L11: 10.7952 L22: 6.2133 REMARK 3 L33: 32.6049 L12: 5.8294 REMARK 3 L13: -14.4785 L23: -4.3254 REMARK 3 S TENSOR REMARK 3 S11: -0.5702 S12: 1.3446 S13: -0.6410 REMARK 3 S21: -0.8986 S22: 0.5851 S23: 0.2749 REMARK 3 S31: 1.4070 S32: -2.0539 S33: -0.0149 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): 114.4560 50.5550 35.1330 REMARK 3 T TENSOR REMARK 3 T11: -0.1884 T22: -0.1083 REMARK 3 T33: -0.1098 T12: 0.0423 REMARK 3 T13: 0.0295 T23: 0.1703 REMARK 3 L TENSOR REMARK 3 L11: 0.6978 L22: 0.3574 REMARK 3 L33: 2.9377 L12: 0.4710 REMARK 3 L13: -0.3573 L23: 0.0887 REMARK 3 S TENSOR REMARK 3 S11: 0.0911 S12: 0.1926 S13: 0.1162 REMARK 3 S21: -0.2027 S22: 0.0378 S23: -0.1679 REMARK 3 S31: -0.3464 S32: 0.1982 S33: -0.1290 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): 113.8320 39.6160 36.1270 REMARK 3 T TENSOR REMARK 3 T11: -0.2829 T22: -0.1124 REMARK 3 T33: -0.2001 T12: 0.0902 REMARK 3 T13: 0.0222 T23: 0.0404 REMARK 3 L TENSOR REMARK 3 L11: 3.6082 L22: 3.7429 REMARK 3 L33: 4.0307 L12: 1.3607 REMARK 3 L13: -1.6574 L23: -3.6655 REMARK 3 S TENSOR REMARK 3 S11: 0.1565 S12: 0.3113 S13: -0.4732 REMARK 3 S21: -0.1702 S22: -0.0498 S23: -0.1436 REMARK 3 S31: 0.7711 S32: 0.2183 S33: -0.1067 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): 112.5820 46.1410 35.5600 REMARK 3 T TENSOR REMARK 3 T11: -0.1940 T22: -0.2109 REMARK 3 T33: -0.1760 T12: -0.0120 REMARK 3 T13: -0.0262 T23: 0.0923 REMARK 3 L TENSOR REMARK 3 L11: 5.1547 L22: 1.4421 REMARK 3 L33: 2.9263 L12: -1.1239 REMARK 3 L13: -2.7280 L23: -0.7374 REMARK 3 S TENSOR REMARK 3 S11: -0.1533 S12: 0.2545 S13: -0.1397 REMARK 3 S21: -0.0668 S22: 0.0076 S23: 0.0528 REMARK 3 S31: 0.3393 S32: 0.3336 S33: 0.1458 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): 100.6090 53.4350 8.1630 REMARK 3 T TENSOR REMARK 3 T11: -0.1981 T22: 0.2513 REMARK 3 T33: -0.1768 T12: 0.0042 REMARK 3 T13: 0.0317 T23: 0.1328 REMARK 3 L TENSOR REMARK 3 L11: 1.2059 L22: 2.2758 REMARK 3 L33: 5.6946 L12: -1.4027 REMARK 3 L13: 2.3516 L23: -1.8903 REMARK 3 S TENSOR REMARK 3 S11: 0.5744 S12: 0.2390 S13: -0.3818 REMARK 3 S21: -0.4121 S22: -0.2004 S23: 0.2705 REMARK 3 S31: 0.7065 S32: 0.1935 S33: -0.3740 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): 101.6810 60.0070 8.8170 REMARK 3 T TENSOR REMARK 3 T11: -0.2038 T22: 0.2081 REMARK 3 T33: -0.2617 T12: -0.0624 REMARK 3 T13: 0.0266 T23: 0.0411 REMARK 3 L TENSOR REMARK 3 L11: 7.7846 L22: 7.4661 REMARK 3 L33: 6.0809 L12: -6.2128 REMARK 3 L13: 5.2356 L23: -3.7835 REMARK 3 S TENSOR REMARK 3 S11: -0.1581 S12: -0.4119 S13: 0.5810 REMARK 3 S21: 0.2693 S22: -0.2019 S23: -0.3453 REMARK 3 S31: -0.0676 S32: 0.1376 S33: 0.3600 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): 95.2340 60.4010 2.9270 REMARK 3 T TENSOR REMARK 3 T11: -0.2156 T22: 0.0992 REMARK 3 T33: -0.1868 T12: -0.0002 REMARK 3 T13: 0.0136 T23: 0.0212 REMARK 3 L TENSOR REMARK 3 L11: 7.3176 L22: 3.5028 REMARK 3 L33: 4.2091 L12: -2.8159 REMARK 3 L13: 3.1881 L23: -0.5187 REMARK 3 S TENSOR REMARK 3 S11: 0.0192 S12: 0.4584 S13: 0.0094 REMARK 3 S21: -0.3992 S22: -0.2128 S23: -0.1515 REMARK 3 S31: -0.0987 S32: 0.0315 S33: 0.1936 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): 103.0900 62.8590 -2.0080 REMARK 3 T TENSOR REMARK 3 T11: -0.0357 T22: 0.1675 REMARK 3 T33: -0.2103 T12: 0.0375 REMARK 3 T13: 0.0838 T23: 0.2321 REMARK 3 L TENSOR REMARK 3 L11: 9.3513 L22: 5.5826 REMARK 3 L33: 3.0088 L12: -5.6862 REMARK 3 L13: 0.1143 L23: -1.4314 REMARK 3 S TENSOR REMARK 3 S11: -0.0542 S12: 1.2485 S13: -0.0894 REMARK 3 S21: -0.3307 S22: -0.1808 S23: 0.0457 REMARK 3 S31: -0.3978 S32: 0.5631 S33: 0.2350 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 2VC2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-SEP-07. REMARK 100 THE PDBE ID CODE IS EBI-33829. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-OCT-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 : CHESS REMARK 200 BEAMLINE : A-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9760 REMARK 200 MONOCHROMATOR : RH-COATED SI REMARK 200 OPTICS : MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41563 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.10 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 : 7.0 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) : 3.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.20 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7 REMARK 200 DATA REDUNDANCY IN SHELL : 6.00 REMARK 200 R MERGE FOR SHELL (I) : 0.56 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.70 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 (%): 68 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.9 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10-12% PEG 3350, 0.7 M REMARK 280 MAGNESIUM ACETATE, 0.1 M IMIDAZOLE, PH 6.5, VAPOR REMARK 280 DIFFUSION, 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 117.47800 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 58.73900 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 58.73900 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 117.47800 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: 11050 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 71730 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.0 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 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 4005 O HOH B 4023 2.10 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 28.36 -149.03 REMARK 500 GLN A 47 18.25 58.57 REMARK 500 SER A 101 -114.25 46.75 REMARK 500 LYS A 118 -134.50 54.43 REMARK 500 GLU A 123 129.92 91.47 REMARK 500 LEU A 212 -61.32 69.98 REMARK 500 SER A 261 72.36 44.97 REMARK 500 THR B 7 39.28 -90.81 REMARK 500 ARG B 8 72.41 -150.77 REMARK 500 ASP B 47 42.43 -97.57 REMARK 500 ASN B 48 15.40 59.46 REMARK 500 PHE B 56 78.44 -151.84 REMARK 500 VAL B 63 96.14 -64.13 REMARK 500 ASP B 66 55.01 -140.39 REMARK 500 SER B 78 -68.13 -151.36 REMARK 500 VAL B 80 93.70 64.26 REMARK 500 ASP B 95 -21.26 65.90 REMARK 500 ASN B 148 40.13 -95.31 REMARK 500 VAL B 157 -83.81 -127.14 REMARK 500 LEU B 196 108.41 -48.47 REMARK 500 SER B 213 -152.56 -112.60 REMARK 500 LEU B 258 -6.23 86.33 REMARK 500 ASN B 303 60.41 60.06 REMARK 500 ALA B 309 75.10 -108.40 REMARK 500 LYS B 410 -25.47 72.43 REMARK 500 GLU B 442 70.16 53.05 REMARK 500 HIS B 446 -54.43 74.06 REMARK 500 THR B 454 150.11 70.31 REMARK 500 THR H 91 96.68 -66.62 REMARK 500 TYR H 101 -60.46 -124.83 REMARK 500 SER L 30 71.65 17.14 REMARK 500 SER L 43 -155.59 -84.60 REMARK 500 SER L 77 78.56 54.16 REMARK 500 ASN L 138 76.56 53.13 REMARK 500 ASN L 212 72.98 50.97 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 46.3 REMARK 620 3 ASP A 245 OD2 111.0 65.8 REMARK 620 4 ASP A 247 O 81.0 68.4 85.6 REMARK 620 5 THR A 250 C 96.7 138.1 150.8 90.0 REMARK 620 6 THR A 250 O 75.2 116.5 165.5 82.5 22.0 REMARK 620 7 THR A 250 OG1 149.4 136.9 87.9 76.5 63.1 81.4 REMARK 620 8 GLU A 252 OE1 76.1 85.4 89.3 153.0 106.7 105.1 129.8 REMARK 620 9 GLU A 252 OE2 124.7 132.6 90.1 153.5 81.2 97.0 77.2 52.7 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 79.2 REMARK 620 3 ARG A 303 O 150.1 86.1 REMARK 620 4 ASP A 297 OD1 75.7 73.7 75.2 REMARK 620 5 ASP A 305 OD1 107.2 163.8 94.2 122.1 REMARK 620 6 ASP A 305 OD2 76.3 147.5 105.2 79.8 47.7 REMARK 620 N 1 2 3 4 5 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 76.8 REMARK 620 3 TYR A 371 O 68.1 85.8 REMARK 620 4 ASP A 367 OD1 81.1 95.6 148.1 REMARK 620 5 ASP A 373 OD1 85.5 160.1 96.0 72.5 REMARK 620 6 ASP A 373 OD2 121.7 150.6 81.6 109.1 48.6 REMARK 620 N 1 2 3 4 5 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 83.1 REMARK 620 3 ASP A 426 OD1 75.1 86.4 REMARK 620 4 ASP A 428 OD1 141.9 82.4 68.9 REMARK 620 5 ASP A 434 OD1 112.1 164.1 93.2 82.7 REMARK 620 6 ASP A 434 OD2 94.9 138.1 133.7 119.0 48.2 REMARK 620 7 HOH A4029 O 133.9 83.6 147.3 78.9 88.3 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 B1478 O2 REMARK 620 2 HOH B4025 O 93.9 REMARK 620 3 ASP B 251 OD2 120.3 116.9 REMARK 620 4 GOL B1478 O1 60.6 73.6 79.7 REMARK 620 5 SER B 123 O 147.6 101.2 77.7 151.3 REMARK 620 6 ASP B 126 OD1 85.0 87.7 140.9 138.6 67.4 REMARK 620 7 ASP B 127 OD1 73.4 157.4 85.7 113.5 82.3 73.0 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 159.2 REMARK 620 3 ASN B 215 OD1 87.6 109.0 REMARK 620 4 ASP B 217 OD1 70.9 94.5 94.7 REMARK 620 5 PRO B 219 O 86.3 78.6 170.6 89.9 REMARK 620 6 GLU B 220 OE2 88.9 104.2 86.9 159.6 86.0 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 B4024 O REMARK 620 2 SER B 123 OG 78.1 REMARK 620 3 GLU B 220 OE1 118.8 160.8 REMARK 620 4 HOH B4006 O 89.9 78.9 91.4 REMARK 620 5 180 B1477 O1 109.9 79.5 101.3 146.8 REMARK 620 6 SER B 121 OG 152.7 77.1 84.4 74.4 76.4 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 MG A1460 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1461 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2004 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2005 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2006 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2007 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A3015 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A3249 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 180 B1477 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1478 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B2001 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2002 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2003 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3099 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 320 RESIDUES 3320 TO 3324 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC7 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: 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.