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. 2.51 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) : 2.51 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.13 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3 REMARK 3 NUMBER OF REFLECTIONS : 71126 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 : 0.190 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 3807 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) : 2.51 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.57 REMARK 3 REFLECTION IN BIN (WORKING SET) : 4785 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2160 REMARK 3 BIN FREE R VALUE SET COUNT : 260 REMARK 3 BIN FREE R VALUE : 0.2890 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 10538 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 205 REMARK 3 SOLVENT ATOMS : 1043 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) : 51.55 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.03000 REMARK 3 B22 (A**2) : -0.03000 REMARK 3 B33 (A**2) : 0.05000 REMARK 3 B12 (A**2) : -0.02000 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): 0.266 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.199 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.131 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.761 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11034 ; 0.006 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 7394 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15073 ; 1.046 ; 1.979 REMARK 3 BOND ANGLES OTHERS (DEGREES): 18001 ; 0.789 ; 3.003 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1397 ; 5.497 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 481 ;33.588 ;24.324 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1735 ;12.148 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 61 ;13.892 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1698 ; 0.065 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12310 ; 0.003 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 2178 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1982 ; 0.183 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 7585 ; 0.179 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5314 ; 0.172 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 5775 ; 0.081 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 868 ; 0.137 ; 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): 18 ; 0.103 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 67 ; 0.177 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 34 ; 0.148 ; 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): 7079 ; 1.852 ; 5.000 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11024 ; 2.876 ;10.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4606 ; 1.939 ; 5.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4028 ; 2.908 ;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): 132.9320 12.1020 78.3570 REMARK 3 T TENSOR REMARK 3 T11: -0.1882 T22: 0.0993 REMARK 3 T33: 0.0165 T12: 0.0713 REMARK 3 T13: -0.0553 T23: 0.4004 REMARK 3 L TENSOR REMARK 3 L11: 4.3390 L22: 13.4216 REMARK 3 L33: 3.7125 L12: -2.4833 REMARK 3 L13: -0.6286 L23: 0.0099 REMARK 3 S TENSOR REMARK 3 S11: -0.1973 S12: -0.0949 S13: -0.3419 REMARK 3 S21: 0.5329 S22: -0.1952 S23: -0.9466 REMARK 3 S31: 0.5544 S32: 0.8323 S33: 0.3925 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): 129.0170 21.6150 68.9240 REMARK 3 T TENSOR REMARK 3 T11: -0.2484 T22: -0.0629 REMARK 3 T33: -0.0864 T12: 0.0313 REMARK 3 T13: 0.0143 T23: 0.2485 REMARK 3 L TENSOR REMARK 3 L11: 3.1771 L22: 6.1405 REMARK 3 L33: 3.3315 L12: 0.0302 REMARK 3 L13: -0.1408 L23: 1.7500 REMARK 3 S TENSOR REMARK 3 S11: 0.0547 S12: -0.0095 S13: -0.1112 REMARK 3 S21: -0.1423 S22: -0.2830 S23: -0.5369 REMARK 3 S31: 0.1076 S32: 0.3626 S33: 0.2283 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): 118.5350 33.3710 64.2890 REMARK 3 T TENSOR REMARK 3 T11: -0.2743 T22: -0.1151 REMARK 3 T33: -0.1125 T12: -0.0931 REMARK 3 T13: -0.0503 T23: 0.1361 REMARK 3 L TENSOR REMARK 3 L11: 1.0076 L22: 1.6247 REMARK 3 L33: 2.1037 L12: -0.4411 REMARK 3 L13: -0.3526 L23: -0.6230 REMARK 3 S TENSOR REMARK 3 S11: 0.0394 S12: -0.0131 S13: 0.0086 REMARK 3 S21: 0.2021 S22: -0.2131 S23: -0.2712 REMARK 3 S31: -0.0583 S32: 0.3853 S33: 0.1737 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): 106.9730 35.9030 63.4940 REMARK 3 T TENSOR REMARK 3 T11: -0.2434 T22: -0.1651 REMARK 3 T33: -0.1988 T12: -0.0866 REMARK 3 T13: -0.0376 T23: 0.0904 REMARK 3 L TENSOR REMARK 3 L11: 2.8786 L22: 1.4552 REMARK 3 L33: 2.5665 L12: 0.4195 REMARK 3 L13: -1.9370 L23: -0.1162 REMARK 3 S TENSOR REMARK 3 S11: -0.0199 S12: 0.0112 S13: -0.1160 REMARK 3 S21: 0.0517 S22: -0.1345 S23: 0.2048 REMARK 3 S31: 0.0121 S32: -0.0421 S33: 0.1545 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): 105.9430 24.3110 63.8110 REMARK 3 T TENSOR REMARK 3 T11: -0.1889 T22: -0.1844 REMARK 3 T33: -0.1462 T12: -0.0824 REMARK 3 T13: -0.0100 T23: 0.0621 REMARK 3 L TENSOR REMARK 3 L11: 0.9301 L22: 0.9556 REMARK 3 L33: 1.9082 L12: -0.0965 REMARK 3 L13: -0.6960 L23: -0.4877 REMARK 3 S TENSOR REMARK 3 S11: 0.0272 S12: 0.1340 S13: -0.1451 REMARK 3 S21: 0.0620 S22: -0.1453 S23: -0.0107 REMARK 3 S31: 0.2669 S32: -0.1252 S33: 0.1181 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 244 A 290 REMARK 3 ORIGIN FOR THE GROUP (A): 99.5560 12.9550 72.2190 REMARK 3 T TENSOR REMARK 3 T11: -0.0511 T22: -0.2704 REMARK 3 T33: -0.0903 T12: -0.1386 REMARK 3 T13: 0.0535 T23: 0.0520 REMARK 3 L TENSOR REMARK 3 L11: 2.4651 L22: 2.1919 REMARK 3 L33: 3.8818 L12: 0.0965 REMARK 3 L13: -0.3252 L23: 0.5447 REMARK 3 S TENSOR REMARK 3 S11: -0.0558 S12: 0.1083 S13: -0.2652 REMARK 3 S21: -0.0325 S22: -0.1912 S23: 0.1392 REMARK 3 S31: 0.4367 S32: -0.2824 S33: 0.2470 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 291 A 326 REMARK 3 ORIGIN FOR THE GROUP (A): 107.6080 7.0420 84.2450 REMARK 3 T TENSOR REMARK 3 T11: 0.0178 T22: -0.2870 REMARK 3 T33: -0.0417 T12: -0.0921 REMARK 3 T13: 0.1011 T23: 0.2083 REMARK 3 L TENSOR REMARK 3 L11: 3.1282 L22: 5.3829 REMARK 3 L33: 4.2387 L12: -0.3323 REMARK 3 L13: -0.8189 L23: 2.9501 REMARK 3 S TENSOR REMARK 3 S11: -0.1844 S12: -0.2593 S13: -0.4108 REMARK 3 S21: 0.5516 S22: -0.0453 S23: 0.1828 REMARK 3 S31: 0.9945 S32: 0.0143 S33: 0.2297 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): 110.1110 2.6630 78.4070 REMARK 3 T TENSOR REMARK 3 T11: 0.1302 T22: -0.2959 REMARK 3 T33: -0.0399 T12: -0.0369 REMARK 3 T13: 0.1245 T23: 0.1794 REMARK 3 L TENSOR REMARK 3 L11: 3.1018 L22: 3.3161 REMARK 3 L33: 3.5102 L12: 0.4561 REMARK 3 L13: -0.0668 L23: 1.5637 REMARK 3 S TENSOR REMARK 3 S11: -0.1560 S12: -0.0510 S13: -0.4472 REMARK 3 S21: -0.0115 S22: -0.3381 S23: -0.0598 REMARK 3 S31: 0.7308 S32: -0.0741 S33: 0.4941 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): 124.1760 7.3280 79.9870 REMARK 3 T TENSOR REMARK 3 T11: -0.0488 T22: -0.1037 REMARK 3 T33: 0.0185 T12: 0.1029 REMARK 3 T13: 0.0088 T23: 0.3095 REMARK 3 L TENSOR REMARK 3 L11: 2.9989 L22: 3.1486 REMARK 3 L33: 3.0821 L12: 0.7461 REMARK 3 L13: -0.5003 L23: 0.0210 REMARK 3 S TENSOR REMARK 3 S11: -0.1362 S12: -0.2629 S13: -0.4431 REMARK 3 S21: 0.2734 S22: -0.2923 S23: -0.3881 REMARK 3 S31: 0.5990 S32: 0.6262 S33: 0.4285 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): 106.2680 21.3490 169.1560 REMARK 3 T TENSOR REMARK 3 T11: 0.4446 T22: -0.3282 REMARK 3 T33: -0.3172 T12: 0.2057 REMARK 3 T13: -0.1188 T23: -0.0935 REMARK 3 L TENSOR REMARK 3 L11: 6.1423 L22: 4.0518 REMARK 3 L33: 12.2091 L12: -1.8839 REMARK 3 L13: 5.5295 L23: -2.9334 REMARK 3 S TENSOR REMARK 3 S11: -0.2719 S12: -0.7559 S13: -0.1586 REMARK 3 S21: 1.1934 S22: 0.3932 S23: -0.4537 REMARK 3 S31: -1.3284 S32: -1.1794 S33: -0.1213 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): 103.3770 29.3140 150.3420 REMARK 3 T TENSOR REMARK 3 T11: 0.6342 T22: -0.0747 REMARK 3 T33: -0.0889 T12: 0.2407 REMARK 3 T13: 0.0477 T23: -0.0627 REMARK 3 L TENSOR REMARK 3 L11: 9.6249 L22: 10.9980 REMARK 3 L33: 39.4491 L12: -4.3203 REMARK 3 L13: 18.1102 L23: -15.1056 REMARK 3 S TENSOR REMARK 3 S11: -0.8897 S12: -0.1758 S13: 0.7367 REMARK 3 S21: 1.1894 S22: 0.2821 S23: -0.3446 REMARK 3 S31: -3.5011 S32: -1.1316 S33: 0.6077 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): 97.2700 38.1520 104.2390 REMARK 3 T TENSOR REMARK 3 T11: 0.1489 T22: -0.0805 REMARK 3 T33: -0.1421 T12: -0.2200 REMARK 3 T13: 0.0447 T23: 0.0203 REMARK 3 L TENSOR REMARK 3 L11: 0.2900 L22: 0.6087 REMARK 3 L33: 1.4657 L12: -0.3639 REMARK 3 L13: 0.1069 L23: -0.6001 REMARK 3 S TENSOR REMARK 3 S11: -0.0295 S12: -0.1666 S13: 0.0278 REMARK 3 S21: 0.4045 S22: 0.0270 S23: -0.0117 REMARK 3 S31: -0.4364 S32: 0.0948 S33: 0.0025 REMARK 3 REMARK 3 TLS GROUP : 13 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 173 B 338 REMARK 3 ORIGIN FOR THE GROUP (A): 102.7660 34.2180 95.9670 REMARK 3 T TENSOR REMARK 3 T11: -0.0421 T22: -0.1583 REMARK 3 T33: -0.1993 T12: -0.1953 REMARK 3 T13: -0.0108 T23: 0.0529 REMARK 3 L TENSOR REMARK 3 L11: 1.4144 L22: 1.5802 REMARK 3 L33: 2.1419 L12: -0.2922 REMARK 3 L13: -0.7488 L23: 0.1298 REMARK 3 S TENSOR REMARK 3 S11: 0.0546 S12: -0.2660 S13: 0.0958 REMARK 3 S21: 0.4302 S22: -0.0990 S23: -0.1348 REMARK 3 S31: -0.0602 S32: 0.2247 S33: 0.0444 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): 99.9420 22.6510 130.8710 REMARK 3 T TENSOR REMARK 3 T11: 0.2490 T22: -0.1016 REMARK 3 T33: -0.1234 T12: -0.1048 REMARK 3 T13: 0.0497 T23: -0.0054 REMARK 3 L TENSOR REMARK 3 L11: 3.7877 L22: 2.6048 REMARK 3 L33: 26.1509 L12: -2.7908 REMARK 3 L13: 9.7730 L23: -6.4844 REMARK 3 S TENSOR REMARK 3 S11: 0.6859 S12: 0.6576 S13: -0.4734 REMARK 3 S21: -0.3428 S22: 0.1939 S23: 0.1621 REMARK 3 S31: 1.4197 S32: 0.8471 S33: -0.8798 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): 109.1530 28.2510 149.0690 REMARK 3 T TENSOR REMARK 3 T11: 0.4274 T22: -0.3109 REMARK 3 T33: -0.1764 T12: -0.1030 REMARK 3 T13: -0.0343 T23: -0.0266 REMARK 3 L TENSOR REMARK 3 L11: 6.1854 L22: 2.3089 REMARK 3 L33: 23.1613 L12: -1.4769 REMARK 3 L13: 8.9390 L23: -1.7802 REMARK 3 S TENSOR REMARK 3 S11: -0.4599 S12: 0.6106 S13: 0.1900 REMARK 3 S21: 0.6233 S22: 0.4505 S23: -0.6388 REMARK 3 S31: -2.2981 S32: 1.6894 S33: 0.0094 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): 119.0870 31.3350 183.1630 REMARK 3 T TENSOR REMARK 3 T11: 1.9511 T22: 0.8137 REMARK 3 T33: 0.6802 T12: -0.1471 REMARK 3 T13: -0.8658 T23: -0.1889 REMARK 3 L TENSOR REMARK 3 L11: 3.7646 L22: 5.4692 REMARK 3 L33: 18.1237 L12: 4.5045 REMARK 3 L13: -6.9758 L23: -8.9896 REMARK 3 S TENSOR REMARK 3 S11: -0.2075 S12: -0.8478 S13: 1.0823 REMARK 3 S21: 2.1226 S22: -0.1486 S23: -1.9113 REMARK 3 S31: -4.3227 S32: 3.7870 S33: 0.3561 REMARK 3 REMARK 3 TLS GROUP : 17 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 1 H 13 REMARK 3 ORIGIN FOR THE GROUP (A): 89.7690 36.5350 33.1670 REMARK 3 T TENSOR REMARK 3 T11: -0.2245 T22: -0.0696 REMARK 3 T33: -0.0902 T12: -0.1700 REMARK 3 T13: -0.0138 T23: 0.0502 REMARK 3 L TENSOR REMARK 3 L11: 12.0138 L22: 17.6137 REMARK 3 L33: 11.8823 L12: -12.1686 REMARK 3 L13: 8.8313 L23: -9.6293 REMARK 3 S TENSOR REMARK 3 S11: 0.3507 S12: 0.3005 S13: -1.1269 REMARK 3 S21: -0.7807 S22: 0.1389 S23: 0.8024 REMARK 3 S31: 0.9651 S32: -0.1217 S33: -0.4896 REMARK 3 REMARK 3 TLS GROUP : 18 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 14 H 54 REMARK 3 ORIGIN FOR THE GROUP (A): 93.9400 41.8470 41.1790 REMARK 3 T TENSOR REMARK 3 T11: -0.2765 T22: -0.1044 REMARK 3 T33: -0.1415 T12: -0.0490 REMARK 3 T13: -0.0106 T23: 0.0860 REMARK 3 L TENSOR REMARK 3 L11: 2.8415 L22: 1.8079 REMARK 3 L33: 2.1204 L12: 0.2694 REMARK 3 L13: 0.3730 L23: -0.0486 REMARK 3 S TENSOR REMARK 3 S11: 0.0117 S12: 0.0100 S13: 0.0240 REMARK 3 S21: 0.0131 S22: 0.0321 S23: 0.1562 REMARK 3 S31: 0.2438 S32: -0.2276 S33: -0.0438 REMARK 3 REMARK 3 TLS GROUP : 19 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 55 H 110 REMARK 3 ORIGIN FOR THE GROUP (A): 93.7550 42.7160 43.4000 REMARK 3 T TENSOR REMARK 3 T11: -0.2598 T22: -0.1033 REMARK 3 T33: -0.1137 T12: -0.0739 REMARK 3 T13: -0.0109 T23: 0.0807 REMARK 3 L TENSOR REMARK 3 L11: 3.2994 L22: 0.4697 REMARK 3 L33: 2.9323 L12: -0.6681 REMARK 3 L13: 1.2150 L23: -0.8749 REMARK 3 S TENSOR REMARK 3 S11: -0.0618 S12: 0.0211 S13: 0.0989 REMARK 3 S21: -0.0239 S22: 0.0014 S23: 0.0234 REMARK 3 S31: 0.1811 S32: -0.3198 S33: 0.0604 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): 86.1990 47.5650 12.7000 REMARK 3 T TENSOR REMARK 3 T11: -0.3169 T22: 0.1195 REMARK 3 T33: -0.0732 T12: -0.0740 REMARK 3 T13: -0.0794 T23: 0.0470 REMARK 3 L TENSOR REMARK 3 L11: 1.2362 L22: 1.0957 REMARK 3 L33: 3.7495 L12: -1.1328 REMARK 3 L13: 0.2121 L23: 0.2679 REMARK 3 S TENSOR REMARK 3 S11: 0.2808 S12: -0.0405 S13: -0.2693 REMARK 3 S21: -0.0160 S22: -0.1528 S23: 0.0973 REMARK 3 S31: -0.0467 S32: -0.6355 S33: -0.1279 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): 92.2760 44.6200 4.6690 REMARK 3 T TENSOR REMARK 3 T11: -0.2932 T22: -0.1692 REMARK 3 T33: -0.2078 T12: 0.0717 REMARK 3 T13: -0.1150 T23: -0.0104 REMARK 3 L TENSOR REMARK 3 L11: 7.9266 L22: 1.0004 REMARK 3 L33: 14.2986 L12: -2.4433 REMARK 3 L13: -4.7739 L23: 1.6041 REMARK 3 S TENSOR REMARK 3 S11: 0.4514 S12: 0.2063 S13: -0.7114 REMARK 3 S21: -0.2674 S22: -0.3841 S23: 0.1243 REMARK 3 S31: 0.7970 S32: 0.2007 S33: -0.0672 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): 94.3010 47.3970 9.1790 REMARK 3 T TENSOR REMARK 3 T11: -0.3257 T22: -0.1987 REMARK 3 T33: -0.2788 T12: 0.1107 REMARK 3 T13: -0.0909 T23: 0.0562 REMARK 3 L TENSOR REMARK 3 L11: 10.6160 L22: 1.9983 REMARK 3 L33: 13.2310 L12: -0.4580 REMARK 3 L13: -3.7996 L23: -0.2035 REMARK 3 S TENSOR REMARK 3 S11: 0.4320 S12: -0.4239 S13: 0.0020 REMARK 3 S21: -0.3732 S22: -0.1038 S23: -0.0466 REMARK 3 S31: 0.6002 S32: 0.6535 S33: -0.3282 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): 93.7780 40.4300 -3.6580 REMARK 3 T TENSOR REMARK 3 T11: 0.1870 T22: -0.0426 REMARK 3 T33: -0.1476 T12: 0.2758 REMARK 3 T13: -0.0960 T23: -0.1315 REMARK 3 L TENSOR REMARK 3 L11: 7.7757 L22: 3.9136 REMARK 3 L33: 6.2447 L12: 0.4237 REMARK 3 L13: -2.4523 L23: -0.9758 REMARK 3 S TENSOR REMARK 3 S11: 0.6118 S12: 0.4813 S13: -1.2766 REMARK 3 S21: -0.8540 S22: -0.7092 S23: -0.0382 REMARK 3 S31: 0.5831 S32: 0.3961 S33: 0.0974 REMARK 3 REMARK 3 TLS GROUP : 24 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 207 H 221 REMARK 3 ORIGIN FOR THE GROUP (A): 85.8370 43.5500 -1.9310 REMARK 3 T TENSOR REMARK 3 T11: -0.1855 T22: 0.0345 REMARK 3 T33: -0.0956 T12: 0.0578 REMARK 3 T13: -0.2759 T23: -0.0964 REMARK 3 L TENSOR REMARK 3 L11: 6.9762 L22: 4.6661 REMARK 3 L33: 15.7770 L12: 2.5961 REMARK 3 L13: -8.4835 L23: -0.0704 REMARK 3 S TENSOR REMARK 3 S11: -0.3870 S12: 0.5271 S13: -0.6436 REMARK 3 S21: -1.3335 S22: 0.1229 S23: 0.8409 REMARK 3 S31: 1.9895 S32: -0.8019 S33: 0.2641 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): 114.1070 49.9490 35.1290 REMARK 3 T TENSOR REMARK 3 T11: -0.2726 T22: -0.0949 REMARK 3 T33: -0.0562 T12: 0.0350 REMARK 3 T13: 0.0170 T23: 0.1437 REMARK 3 L TENSOR REMARK 3 L11: 2.0134 L22: 0.7562 REMARK 3 L33: 2.1007 L12: 0.7360 REMARK 3 L13: -0.5759 L23: 0.4119 REMARK 3 S TENSOR REMARK 3 S11: 0.1040 S12: 0.2783 S13: 0.2746 REMARK 3 S21: -0.0646 S22: -0.0411 S23: 0.0119 REMARK 3 S31: -0.0664 S32: 0.0992 S33: -0.0630 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): 113.4010 39.0080 36.1690 REMARK 3 T TENSOR REMARK 3 T11: -0.2137 T22: -0.1133 REMARK 3 T33: -0.1353 T12: 0.0267 REMARK 3 T13: -0.0125 T23: 0.0945 REMARK 3 L TENSOR REMARK 3 L11: 4.5345 L22: 1.8099 REMARK 3 L33: 2.2669 L12: 0.3649 REMARK 3 L13: -0.0669 L23: -0.8368 REMARK 3 S TENSOR REMARK 3 S11: -0.0157 S12: 0.3718 S13: -0.2639 REMARK 3 S21: -0.1599 S22: 0.1330 S23: -0.0711 REMARK 3 S31: 0.5319 S32: 0.1353 S33: -0.1174 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): 112.1810 45.5600 35.6380 REMARK 3 T TENSOR REMARK 3 T11: -0.2667 T22: -0.1490 REMARK 3 T33: -0.1319 T12: -0.0084 REMARK 3 T13: -0.0302 T23: 0.0966 REMARK 3 L TENSOR REMARK 3 L11: 3.9213 L22: 0.9542 REMARK 3 L33: 5.4599 L12: -0.7525 REMARK 3 L13: -1.7655 L23: 0.0516 REMARK 3 S TENSOR REMARK 3 S11: -0.0217 S12: 0.3695 S13: -0.0510 REMARK 3 S21: -0.0058 S22: -0.0539 S23: 0.1147 REMARK 3 S31: 0.3861 S32: -0.1419 S33: 0.0755 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): 100.3050 52.9530 8.0760 REMARK 3 T TENSOR REMARK 3 T11: -0.2881 T22: 0.0465 REMARK 3 T33: -0.1507 T12: 0.0622 REMARK 3 T13: 0.0160 T23: 0.0590 REMARK 3 L TENSOR REMARK 3 L11: 2.2854 L22: 1.9437 REMARK 3 L33: 5.8958 L12: -1.9374 REMARK 3 L13: 3.5235 L23: -2.6131 REMARK 3 S TENSOR REMARK 3 S11: 0.4621 S12: 0.3527 S13: -0.2704 REMARK 3 S21: -0.2924 S22: -0.3435 S23: 0.1354 REMARK 3 S31: 0.4835 S32: 0.3681 S33: -0.1186 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): 101.4590 59.6270 8.7240 REMARK 3 T TENSOR REMARK 3 T11: -0.3834 T22: 0.1493 REMARK 3 T33: -0.2440 T12: 0.0510 REMARK 3 T13: -0.0031 T23: 0.0308 REMARK 3 L TENSOR REMARK 3 L11: 6.6961 L22: 5.2547 REMARK 3 L33: 2.8572 L12: -4.4602 REMARK 3 L13: 2.9753 L23: -2.3522 REMARK 3 S TENSOR REMARK 3 S11: -0.1208 S12: -0.1972 S13: 0.5044 REMARK 3 S21: 0.1206 S22: -0.1868 S23: -0.4294 REMARK 3 S31: -0.0663 S32: 0.3298 S33: 0.3076 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): 95.1880 59.8360 2.9730 REMARK 3 T TENSOR REMARK 3 T11: -0.3512 T22: -0.0006 REMARK 3 T33: -0.2585 T12: 0.0468 REMARK 3 T13: -0.0067 T23: 0.0134 REMARK 3 L TENSOR REMARK 3 L11: 9.7968 L22: 4.3387 REMARK 3 L33: 4.7133 L12: -5.0596 REMARK 3 L13: 4.5306 L23: -2.6858 REMARK 3 S TENSOR REMARK 3 S11: 0.0511 S12: 0.2758 S13: 0.0881 REMARK 3 S21: -0.2341 S22: -0.1424 S23: -0.0250 REMARK 3 S31: 0.0375 S32: 0.2784 S33: 0.0913 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): 102.6600 62.2790 -2.3980 REMARK 3 T TENSOR REMARK 3 T11: -0.3440 T22: 0.1709 REMARK 3 T33: -0.1917 T12: 0.1622 REMARK 3 T13: 0.0901 T23: 0.1440 REMARK 3 L TENSOR REMARK 3 L11: 14.1961 L22: 5.2787 REMARK 3 L33: 12.6441 L12: -4.6242 REMARK 3 L13: 9.7312 L23: -5.3059 REMARK 3 S TENSOR REMARK 3 S11: 0.5371 S12: 1.5211 S13: 0.3215 REMARK 3 S21: -0.5150 S22: -0.7958 S23: -0.3958 REMARK 3 S31: 0.2665 S32: 1.2939 S33: 0.2587 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 : 1.40 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 2VDO 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-34088. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-DEC-04 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 19-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.07223 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : CUSTOM (SBC2 3K) REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 557015 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 (%) : 99.8 REMARK 200 DATA REDUNDANCY : 7.2 REMARK 200 R MERGE (I) : 0.11 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 16.20 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.62 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.80 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER REMARK 200 SOFTWARE USED: CNS REMARK 200 STARTING MODEL: NONE REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 67.2 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.8 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 11% PEG 3350, 0.7 M MAGNESIUM REMARK 280 ACETATE, 0.1 M SODIUM CACODYLATE, PH 6.5, VAPOR DIFFUSION, REMARK 280 HANGING DROP, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+1/3 REMARK 290 6555 -X,-X+Y,-Z+2/3 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 117.71133 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 58.85567 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 58.85567 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 117.71133 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: 11960 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 72750 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.9 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 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 4100 O HOH A 4252 2.04 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 -122.75 50.05 REMARK 500 LYS A 118 -122.03 51.68 REMARK 500 GLU A 123 134.43 99.29 REMARK 500 LEU A 212 -46.37 71.52 REMARK 500 SER A 222 -176.60 -68.49 REMARK 500 SER A 261 70.41 53.50 REMARK 500 PRO A 337 20.70 -78.97 REMARK 500 VAL B 10 72.70 41.75 REMARK 500 PHE B 56 79.46 -151.14 REMARK 500 ASP B 71 -158.49 -114.49 REMARK 500 VAL B 80 103.48 66.94 REMARK 500 ASP B 95 15.65 59.99 REMARK 500 VAL B 157 -87.56 -125.17 REMARK 500 SER B 213 -156.57 -114.46 REMARK 500 ASP B 241 51.69 -111.55 REMARK 500 LEU B 258 -12.59 83.66 REMARK 500 VAL B 275 -84.29 -91.16 REMARK 500 CYS B 374 -158.98 -95.87 REMARK 500 LYS B 410 -23.04 75.11 REMARK 500 GLU B 442 82.06 55.65 REMARK 500 HIS B 446 -63.52 67.44 REMARK 500 ASN B 452 -60.71 -106.21 REMARK 500 THR B 454 147.91 69.28 REMARK 500 HIS C 401 -56.05 -145.80 REMARK 500 LEU C 402 -11.91 -160.62 REMARK 500 GLN C 407 70.24 -114.72 REMARK 500 ASP H 179 -16.30 77.13 REMARK 500 SER L 30 58.49 31.85 REMARK 500 SER L 77 75.63 58.09 REMARK 500 ASN L 212 70.10 51.30 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 52.0 REMARK 620 3 ASP A 245 OD2 122.3 70.3 REMARK 620 4 ASP A 247 O 78.0 77.3 90.7 REMARK 620 5 THR A 250 O 76.3 126.9 158.1 81.7 REMARK 620 6 THR A 250 OG1 145.2 139.5 80.4 75.7 77.8 REMARK 620 7 GLU A 252 OE1 88.8 81.6 82.5 158.9 111.4 122.3 REMARK 620 8 GLU A 252 OE2 132.1 126.1 80.3 148.5 95.6 73.1 49.8 REMARK 620 N 1 2 3 4 5 6 7 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A2005 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH A4304 O REMARK 620 2 ASN A 299 OD1 96.2 REMARK 620 3 ASP A 301 OD1 82.8 81.5 REMARK 620 4 ASP A 297 OD1 162.9 79.1 80.2 REMARK 620 5 ARG A 303 O 98.6 161.9 90.1 83.7 REMARK 620 6 ASP A 305 OD1 69.0 112.9 149.1 128.0 82.3 REMARK 620 7 ASP A 305 OD2 113.0 85.7 160.7 83.2 97.9 50.0 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 75.7 REMARK 620 3 TYR A 371 O 75.6 87.2 REMARK 620 4 ASP A 367 OD1 87.3 93.6 162.2 REMARK 620 5 HOH A4342 O 151.4 76.2 97.8 99.6 REMARK 620 6 ASP A 373 OD1 93.6 164.0 101.7 73.8 115.1 REMARK 620 7 ASP A 373 OD2 129.0 147.5 80.7 106.9 75.7 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 86.3 REMARK 620 3 HOH A4381 O 134.6 88.6 REMARK 620 4 ASP A 426 OD1 78.2 83.8 145.8 REMARK 620 5 ASP A 428 OD1 157.6 93.8 67.8 79.5 REMARK 620 6 ASP A 434 OD1 100.4 170.8 91.2 91.2 77.6 REMARK 620 7 ASP A 434 OD2 82.1 138.2 72.2 131.9 111.4 50.0 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 27.8 REMARK 620 3 HOH C4014 O 95.7 81.6 REMARK 620 4 ASP B 127 OD1 82.0 92.4 170.6 REMARK 620 5 ASP B 251 OD2 99.2 126.0 104.6 84.7 REMARK 620 6 GOL B1462 O1 46.8 62.8 70.2 113.5 69.3 REMARK 620 7 SER B 123 O 177.1 155.0 86.0 96.8 78.0 132.1 REMARK 620 8 ASP B 126 OD1 105.1 80.8 88.6 83.3 151.0 139.6 77.3 REMARK 620 N 1 2 3 4 5 6 7 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B2003 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 217 O REMARK 620 2 ASP B 158 OD2 164.1 REMARK 620 3 ASN B 215 OD1 96.3 95.5 REMARK 620 4 ASP B 217 OD1 76.8 91.5 94.8 REMARK 620 5 PRO B 219 O 89.1 81.8 166.7 98.3 REMARK 620 6 GLU B 220 OE2 92.4 100.0 81.4 168.1 86.2 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 ASP C 410 OD1 REMARK 620 2 HOH B4088 O 92.1 REMARK 620 3 SER B 121 OG 90.3 176.5 REMARK 620 4 SER B 123 OG 79.3 89.3 88.7 REMARK 620 5 GLU B 220 OE1 93.6 90.9 91.5 172.9 REMARK 620 6 HOH B4022 O 154.7 98.7 78.1 78.1 108.9 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 900 RELATED ID: 2VC2 RELATED DB: PDB REMARK 900 RE-REFINEMENT OF INTEGRIN ALPHAIIBBETA3 REMARK 900 HEADPIECE BOUND TO ANTAGONIST L-739758 REMARK 999 REMARK 999 SEQUENCE REMARK 999 ACCORDING TO THE AUTHORS THE CORRECT CHAIN A SEQUENCE IS REMARK 999 ANNOTATED IN NCBI ENTRY GI 88758615 WHICH SHOULD BE USED REMARK 999 IN PLACE OF P08514. REMARK 999 ACCORDING TO THE AUTHORS THE CORRECT CHAIN C SEQUENCE IS REMARK 999 ANNOTATED IN NCBI ENTRY GI 70906437 WHICH CORRESPONDS TO REMARK 999 THE UNIPROT ENTRY Q53Y18