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. 2.90 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) : 2.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.19 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1 REMARK 3 NUMBER OF REFLECTIONS : 46249 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) : 0.166 REMARK 3 R VALUE (WORKING SET) : 0.163 REMARK 3 FREE R VALUE : 0.213 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2421 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) : 2.90 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3085 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2830 REMARK 3 BIN FREE R VALUE SET COUNT : 140 REMARK 3 BIN FREE R VALUE : 0.3470 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 10385 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 223 REMARK 3 SOLVENT ATOMS : 364 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) : 44.60 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.89000 REMARK 3 B22 (A**2) : 0.89000 REMARK 3 B33 (A**2) : -1.33000 REMARK 3 B12 (A**2) : 0.44000 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): 1.054 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.311 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.216 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.178 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957 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): 10884 ; 0.005 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 7291 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14848 ; 0.922 ; 1.983 REMARK 3 BOND ANGLES OTHERS (DEGREES): 17658 ; 0.759 ; 3.005 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1354 ; 5.174 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 466 ;31.968 ;24.356 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1685 ;11.724 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 57 ;13.632 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1670 ; 0.057 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12089 ; 0.002 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 2142 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1959 ; 0.178 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 7414 ; 0.170 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5286 ; 0.170 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 5662 ; 0.078 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 429 ; 0.128 ; 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 ; 0.133 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 51 ; 0.167 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 10 ; 0.128 ; 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): 6970 ; 1.302 ; 5.000 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10835 ; 2.140 ;10.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4568 ; 1.213 ; 5.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4006 ; 2.062 ;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): 133.9140 12.7020 77.9610 REMARK 3 T TENSOR REMARK 3 T11: 0.0741 T22: 0.2919 REMARK 3 T33: 0.1290 T12: 0.1219 REMARK 3 T13: 0.0155 T23: 0.4047 REMARK 3 L TENSOR REMARK 3 L11: 4.9855 L22: 9.2218 REMARK 3 L33: 1.6837 L12: -4.8724 REMARK 3 L13: 0.7602 L23: 0.4490 REMARK 3 S TENSOR REMARK 3 S11: 0.0479 S12: 0.0961 S13: -0.5040 REMARK 3 S21: 1.2353 S22: -0.4983 S23: -0.6348 REMARK 3 S31: 0.5142 S32: 0.9656 S33: 0.4504 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): 129.9430 22.2810 68.5970 REMARK 3 T TENSOR REMARK 3 T11: -0.1403 T22: 0.1670 REMARK 3 T33: -0.0070 T12: 0.0750 REMARK 3 T13: 0.0418 T23: 0.2707 REMARK 3 L TENSOR REMARK 3 L11: 3.0675 L22: 3.8727 REMARK 3 L33: 1.9525 L12: 1.1833 REMARK 3 L13: 0.3071 L23: -0.1314 REMARK 3 S TENSOR REMARK 3 S11: 0.1168 S12: 0.0476 S13: -0.2906 REMARK 3 S21: -0.1223 S22: -0.2987 S23: -0.4112 REMARK 3 S31: 0.2466 S32: 0.2622 S33: 0.1819 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): 119.3810 34.0160 63.9690 REMARK 3 T TENSOR REMARK 3 T11: -0.1781 T22: -0.1011 REMARK 3 T33: -0.1279 T12: -0.0454 REMARK 3 T13: -0.0172 T23: 0.1362 REMARK 3 L TENSOR REMARK 3 L11: 1.3431 L22: 2.1599 REMARK 3 L33: 2.0259 L12: -0.3139 REMARK 3 L13: 0.1043 L23: -1.3198 REMARK 3 S TENSOR REMARK 3 S11: -0.0709 S12: -0.0302 S13: -0.0328 REMARK 3 S21: 0.2200 S22: -0.1243 S23: -0.5053 REMARK 3 S31: 0.0133 S32: 0.4933 S33: 0.1951 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): 107.7010 36.4860 63.2270 REMARK 3 T TENSOR REMARK 3 T11: -0.1349 T22: -0.1423 REMARK 3 T33: -0.2223 T12: -0.0952 REMARK 3 T13: -0.0351 T23: 0.0818 REMARK 3 L TENSOR REMARK 3 L11: 3.8617 L22: 2.3473 REMARK 3 L33: 2.6343 L12: -0.5417 REMARK 3 L13: -1.5973 L23: 0.0084 REMARK 3 S TENSOR REMARK 3 S11: 0.0981 S12: 0.1861 S13: -0.0315 REMARK 3 S21: 0.0264 S22: -0.2348 S23: 0.0456 REMARK 3 S31: 0.0357 S32: -0.0262 S33: 0.1368 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): 106.8080 24.7820 63.4510 REMARK 3 T TENSOR REMARK 3 T11: -0.1385 T22: -0.1783 REMARK 3 T33: -0.1466 T12: -0.0658 REMARK 3 T13: 0.0007 T23: 0.0524 REMARK 3 L TENSOR REMARK 3 L11: 1.5632 L22: 1.6179 REMARK 3 L33: 2.6445 L12: 0.1690 REMARK 3 L13: -0.7929 L23: -1.1041 REMARK 3 S TENSOR REMARK 3 S11: 0.0140 S12: 0.1007 S13: -0.2452 REMARK 3 S21: 0.0345 S22: -0.1583 S23: -0.1005 REMARK 3 S31: 0.2552 S32: -0.1494 S33: 0.1443 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): 100.5390 13.2950 71.7960 REMARK 3 T TENSOR REMARK 3 T11: 0.0765 T22: -0.1502 REMARK 3 T33: -0.0882 T12: -0.1322 REMARK 3 T13: 0.0536 T23: 0.0406 REMARK 3 L TENSOR REMARK 3 L11: 1.8695 L22: 2.3561 REMARK 3 L33: 2.4832 L12: -0.2032 REMARK 3 L13: -0.1218 L23: 0.3641 REMARK 3 S TENSOR REMARK 3 S11: -0.0452 S12: 0.0949 S13: -0.4164 REMARK 3 S21: -0.0916 S22: -0.0645 S23: -0.0366 REMARK 3 S31: 0.2632 S32: -0.2458 S33: 0.1097 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): 108.5830 7.4270 83.8650 REMARK 3 T TENSOR REMARK 3 T11: 0.0646 T22: -0.1805 REMARK 3 T33: 0.0388 T12: -0.0823 REMARK 3 T13: 0.0922 T23: 0.2006 REMARK 3 L TENSOR REMARK 3 L11: 3.1542 L22: 6.1962 REMARK 3 L33: 5.6722 L12: -0.9411 REMARK 3 L13: -0.5574 L23: 1.8602 REMARK 3 S TENSOR REMARK 3 S11: -0.1814 S12: -0.3245 S13: -0.5544 REMARK 3 S21: 0.5130 S22: -0.0657 S23: 0.0302 REMARK 3 S31: 0.7186 S32: -0.0028 S33: 0.2471 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): 111.4080 3.1730 78.2040 REMARK 3 T TENSOR REMARK 3 T11: 0.2222 T22: -0.1487 REMARK 3 T33: 0.0335 T12: 0.0237 REMARK 3 T13: 0.0872 T23: 0.2292 REMARK 3 L TENSOR REMARK 3 L11: 2.9228 L22: 3.7809 REMARK 3 L33: 4.2790 L12: -0.7369 REMARK 3 L13: -0.9643 L23: 0.6676 REMARK 3 S TENSOR REMARK 3 S11: -0.1397 S12: -0.0458 S13: -0.4506 REMARK 3 S21: -0.1773 S22: -0.2443 S23: -0.0388 REMARK 3 S31: 0.7635 S32: -0.0476 S33: 0.3840 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): 125.1880 7.8710 79.6450 REMARK 3 T TENSOR REMARK 3 T11: 0.1834 T22: 0.0608 REMARK 3 T33: 0.1523 T12: 0.1544 REMARK 3 T13: 0.0393 T23: 0.3154 REMARK 3 L TENSOR REMARK 3 L11: 3.2717 L22: 1.0976 REMARK 3 L33: 2.7013 L12: 0.2069 REMARK 3 L13: -0.7363 L23: -0.2083 REMARK 3 S TENSOR REMARK 3 S11: -0.1113 S12: -0.1350 S13: -0.5132 REMARK 3 S21: 0.1389 S22: -0.2413 S23: -0.5665 REMARK 3 S31: 0.6239 S32: 0.6057 S33: 0.3526 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): 107.1150 21.1420 168.6460 REMARK 3 T TENSOR REMARK 3 T11: 1.0878 T22: 0.1867 REMARK 3 T33: 0.1719 T12: 0.0182 REMARK 3 T13: -0.1511 T23: -0.0653 REMARK 3 L TENSOR REMARK 3 L11: 2.9026 L22: 2.8105 REMARK 3 L33: 6.8766 L12: -1.3309 REMARK 3 L13: 1.8520 L23: -2.1986 REMARK 3 S TENSOR REMARK 3 S11: -0.2105 S12: -0.6439 S13: -0.1235 REMARK 3 S21: 1.1271 S22: 0.3333 S23: -0.0826 REMARK 3 S31: -0.8495 S32: -0.7197 S33: -0.1228 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): 103.7000 29.7320 149.2830 REMARK 3 T TENSOR REMARK 3 T11: 0.8512 T22: 0.1488 REMARK 3 T33: -0.0191 T12: 0.1042 REMARK 3 T13: 0.0239 T23: -0.0062 REMARK 3 L TENSOR REMARK 3 L11: 11.9393 L22: 14.0434 REMARK 3 L33: 43.5833 L12: -8.3375 REMARK 3 L13: 21.8542 L23: -20.6866 REMARK 3 S TENSOR REMARK 3 S11: -0.5208 S12: -0.7923 S13: 0.1458 REMARK 3 S21: 1.5793 S22: 0.7725 S23: 0.3230 REMARK 3 S31: -2.5266 S32: -1.7268 S33: -0.2517 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): 97.9310 38.4100 103.8160 REMARK 3 T TENSOR REMARK 3 T11: 0.2682 T22: 0.0084 REMARK 3 T33: -0.1174 T12: -0.2419 REMARK 3 T13: 0.0310 T23: 0.0116 REMARK 3 L TENSOR REMARK 3 L11: 0.2464 L22: 0.5425 REMARK 3 L33: 3.8654 L12: -0.1432 REMARK 3 L13: -0.1098 L23: -1.2601 REMARK 3 S TENSOR REMARK 3 S11: 0.0364 S12: -0.2941 S13: -0.0669 REMARK 3 S21: 0.4870 S22: -0.0583 S23: 0.0108 REMARK 3 S31: -0.5066 S32: 0.0906 S33: 0.0220 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): 103.5310 34.6290 95.6250 REMARK 3 T TENSOR REMARK 3 T11: 0.0561 T22: -0.0414 REMARK 3 T33: -0.1383 T12: -0.1824 REMARK 3 T13: -0.0178 T23: 0.0664 REMARK 3 L TENSOR REMARK 3 L11: 1.3934 L22: 1.4175 REMARK 3 L33: 2.2015 L12: -0.4453 REMARK 3 L13: -1.3438 L23: -0.0457 REMARK 3 S TENSOR REMARK 3 S11: 0.0434 S12: -0.3548 S13: 0.0643 REMARK 3 S21: 0.3429 S22: -0.1101 S23: -0.1166 REMARK 3 S31: -0.1569 S32: 0.2642 S33: 0.0667 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): 100.6320 22.6850 130.3420 REMARK 3 T TENSOR REMARK 3 T11: 0.5076 T22: 0.2072 REMARK 3 T33: 0.1591 T12: -0.0764 REMARK 3 T13: 0.0518 T23: 0.0018 REMARK 3 L TENSOR REMARK 3 L11: 3.1177 L22: 2.2141 REMARK 3 L33: 20.5282 L12: -1.5173 REMARK 3 L13: 7.9754 L23: -4.3130 REMARK 3 S TENSOR REMARK 3 S11: 0.6443 S12: 0.4708 S13: -0.3131 REMARK 3 S21: -0.1745 S22: 0.0185 S23: -0.1677 REMARK 3 S31: 1.6315 S32: 0.5024 S33: -0.6628 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): 109.8210 28.2090 148.5750 REMARK 3 T TENSOR REMARK 3 T11: 0.8908 T22: 0.0547 REMARK 3 T33: 0.2229 T12: -0.1159 REMARK 3 T13: -0.0965 T23: 0.0507 REMARK 3 L TENSOR REMARK 3 L11: 4.2130 L22: 1.2904 REMARK 3 L33: 16.2223 L12: -0.6957 REMARK 3 L13: 5.5377 L23: -1.5236 REMARK 3 S TENSOR REMARK 3 S11: -0.3261 S12: 0.4965 S13: 0.2656 REMARK 3 S21: 0.8408 S22: 0.2831 S23: -0.5380 REMARK 3 S31: -1.6856 S32: 0.9687 S33: 0.0430 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): 119.6500 31.2620 182.6750 REMARK 3 T TENSOR REMARK 3 T11: 2.1005 T22: 1.2511 REMARK 3 T33: 0.9544 T12: -0.3300 REMARK 3 T13: -0.5227 T23: -0.0140 REMARK 3 L TENSOR REMARK 3 L11: 3.1875 L22: 1.8536 REMARK 3 L33: 8.7346 L12: -0.6510 REMARK 3 L13: -4.4473 L23: -1.1780 REMARK 3 S TENSOR REMARK 3 S11: -1.1091 S12: -1.9628 S13: 0.8840 REMARK 3 S21: 0.8878 S22: 0.1138 S23: -1.2250 REMARK 3 S31: -1.3855 S32: 2.8896 S33: 0.9953 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): 90.5150 37.1100 32.7960 REMARK 3 T TENSOR REMARK 3 T11: -0.1012 T22: -0.0300 REMARK 3 T33: -0.0527 T12: -0.2240 REMARK 3 T13: -0.0841 T23: 0.0452 REMARK 3 L TENSOR REMARK 3 L11: 10.7631 L22: 10.5748 REMARK 3 L33: 9.3400 L12: -8.7827 REMARK 3 L13: 6.0039 L23: -6.1561 REMARK 3 S TENSOR REMARK 3 S11: 0.2710 S12: 0.7987 S13: -0.9500 REMARK 3 S21: -0.3808 S22: -0.0209 S23: 0.5736 REMARK 3 S31: 0.5936 S32: 0.1377 S33: -0.2501 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): 94.6590 42.4740 40.8070 REMARK 3 T TENSOR REMARK 3 T11: -0.2448 T22: -0.0867 REMARK 3 T33: -0.1817 T12: -0.0519 REMARK 3 T13: -0.0048 T23: 0.0592 REMARK 3 L TENSOR REMARK 3 L11: 2.7059 L22: 1.3993 REMARK 3 L33: 2.5079 L12: -0.3533 REMARK 3 L13: 0.6278 L23: -0.0456 REMARK 3 S TENSOR REMARK 3 S11: 0.0235 S12: 0.0187 S13: -0.0786 REMARK 3 S21: 0.0602 S22: 0.0609 S23: 0.2229 REMARK 3 S31: 0.1624 S32: -0.2265 S33: -0.0844 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): 94.4940 43.3160 43.0610 REMARK 3 T TENSOR REMARK 3 T11: -0.2045 T22: -0.0776 REMARK 3 T33: -0.1746 T12: -0.0707 REMARK 3 T13: 0.0298 T23: 0.0591 REMARK 3 L TENSOR REMARK 3 L11: 3.2980 L22: 1.0942 REMARK 3 L33: 2.9671 L12: -0.3585 REMARK 3 L13: 1.3480 L23: -0.7773 REMARK 3 S TENSOR REMARK 3 S11: -0.0631 S12: -0.0347 S13: 0.2173 REMARK 3 S21: -0.0140 S22: -0.0022 S23: -0.0036 REMARK 3 S31: 0.1608 S32: -0.2704 S33: 0.0654 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): 86.8450 48.0480 12.5840 REMARK 3 T TENSOR REMARK 3 T11: -0.2198 T22: 0.1293 REMARK 3 T33: -0.0197 T12: -0.1000 REMARK 3 T13: -0.0792 T23: 0.0490 REMARK 3 L TENSOR REMARK 3 L11: 1.0449 L22: 2.0594 REMARK 3 L33: 4.6427 L12: -1.1419 REMARK 3 L13: -0.3556 L23: 0.2789 REMARK 3 S TENSOR REMARK 3 S11: 0.1363 S12: 0.4371 S13: -0.0933 REMARK 3 S21: -0.1712 S22: -0.2546 S23: 0.0922 REMARK 3 S31: -0.3474 S32: -0.3744 S33: 0.1183 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): 93.0590 45.2150 4.4020 REMARK 3 T TENSOR REMARK 3 T11: 0.0633 T22: 0.0349 REMARK 3 T33: 0.0645 T12: 0.0880 REMARK 3 T13: -0.0303 T23: 0.0522 REMARK 3 L TENSOR REMARK 3 L11: 8.8200 L22: 0.8814 REMARK 3 L33: 11.3175 L12: -0.7058 REMARK 3 L13: -4.0960 L23: 2.8343 REMARK 3 S TENSOR REMARK 3 S11: 0.2447 S12: 0.4373 S13: -0.4141 REMARK 3 S21: -0.2231 S22: -0.1889 S23: -0.0897 REMARK 3 S31: 0.7652 S32: -0.0498 S33: -0.0558 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): 95.0420 47.9990 8.9230 REMARK 3 T TENSOR REMARK 3 T11: -0.0007 T22: -0.0215 REMARK 3 T33: -0.1159 T12: 0.0905 REMARK 3 T13: -0.0442 T23: 0.0315 REMARK 3 L TENSOR REMARK 3 L11: 7.5528 L22: 1.9816 REMARK 3 L33: 15.9061 L12: 1.6792 REMARK 3 L13: -3.9915 L23: -0.6047 REMARK 3 S TENSOR REMARK 3 S11: 0.3456 S12: -0.5333 S13: 0.2213 REMARK 3 S21: -0.4204 S22: -0.2084 S23: 0.0643 REMARK 3 S31: 0.4549 S32: 0.3780 S33: -0.1372 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): 94.4800 41.0480 -4.0220 REMARK 3 T TENSOR REMARK 3 T11: 0.8198 T22: 0.2833 REMARK 3 T33: 0.1518 T12: 0.2477 REMARK 3 T13: 0.0072 T23: -0.0266 REMARK 3 L TENSOR REMARK 3 L11: 4.9617 L22: 3.4247 REMARK 3 L33: 1.7704 L12: -1.3183 REMARK 3 L13: 1.2938 L23: 1.7552 REMARK 3 S TENSOR REMARK 3 S11: 0.2750 S12: 0.3984 S13: -1.2056 REMARK 3 S21: -0.3446 S22: -0.6613 S23: -0.0136 REMARK 3 S31: 0.8145 S32: 0.5732 S33: 0.3863 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): 86.6030 44.2030 -2.2430 REMARK 3 T TENSOR REMARK 3 T11: 0.1401 T22: 0.3192 REMARK 3 T33: 0.1443 T12: 0.0455 REMARK 3 T13: -0.2251 T23: -0.0227 REMARK 3 L TENSOR REMARK 3 L11: 9.4750 L22: 6.4648 REMARK 3 L33: 23.1076 L12: 6.2846 REMARK 3 L13: -10.3215 L23: -2.8090 REMARK 3 S TENSOR REMARK 3 S11: -0.2018 S12: 0.5481 S13: -0.5947 REMARK 3 S21: -1.0733 S22: 0.1217 S23: 0.6778 REMARK 3 S31: 1.3684 S32: -1.0390 S33: 0.0800 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): 114.8860 50.6330 34.8420 REMARK 3 T TENSOR REMARK 3 T11: -0.2433 T22: -0.0627 REMARK 3 T33: -0.0695 T12: 0.0312 REMARK 3 T13: 0.0206 T23: 0.1525 REMARK 3 L TENSOR REMARK 3 L11: 0.9107 L22: 2.3350 REMARK 3 L33: 6.3748 L12: 0.0216 REMARK 3 L13: -2.1006 L23: 1.8397 REMARK 3 S TENSOR REMARK 3 S11: 0.0884 S12: 0.1963 S13: 0.1455 REMARK 3 S21: -0.1132 S22: -0.0406 S23: -0.0389 REMARK 3 S31: -0.1329 S32: 0.3619 S33: -0.0478 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): 114.2270 39.6750 35.8120 REMARK 3 T TENSOR REMARK 3 T11: -0.2451 T22: -0.1093 REMARK 3 T33: -0.1654 T12: 0.0717 REMARK 3 T13: -0.0167 T23: 0.0182 REMARK 3 L TENSOR REMARK 3 L11: 3.4978 L22: 3.1030 REMARK 3 L33: 2.4328 L12: 1.1665 REMARK 3 L13: -0.9176 L23: -2.6462 REMARK 3 S TENSOR REMARK 3 S11: 0.1351 S12: 0.3906 S13: -0.3091 REMARK 3 S21: -0.1364 S22: -0.0271 S23: -0.0959 REMARK 3 S31: 0.5094 S32: 0.0894 S33: -0.1080 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): 112.9810 46.2130 35.2670 REMARK 3 T TENSOR REMARK 3 T11: -0.2454 T22: -0.1343 REMARK 3 T33: -0.1267 T12: -0.0050 REMARK 3 T13: -0.0466 T23: 0.0999 REMARK 3 L TENSOR REMARK 3 L11: 4.1778 L22: 1.3949 REMARK 3 L33: 3.1205 L12: -0.5453 REMARK 3 L13: -2.0312 L23: -0.4520 REMARK 3 S TENSOR REMARK 3 S11: -0.0156 S12: 0.3796 S13: -0.0023 REMARK 3 S21: -0.0853 S22: -0.0458 S23: 0.0195 REMARK 3 S31: 0.3116 S32: -0.1002 S33: 0.0614 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): 100.9480 53.6840 7.8740 REMARK 3 T TENSOR REMARK 3 T11: -0.1510 T22: 0.2026 REMARK 3 T33: -0.0835 T12: 0.0293 REMARK 3 T13: 0.0314 T23: 0.1054 REMARK 3 L TENSOR REMARK 3 L11: 1.1735 L22: 2.4344 REMARK 3 L33: 5.7867 L12: -1.4497 REMARK 3 L13: 2.4174 L23: -2.2656 REMARK 3 S TENSOR REMARK 3 S11: 0.4944 S12: 0.3350 S13: -0.3131 REMARK 3 S21: -0.2805 S22: -0.2248 S23: 0.2381 REMARK 3 S31: 0.6417 S32: 0.2813 S33: -0.2695 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): 102.1040 60.2780 8.5740 REMARK 3 T TENSOR REMARK 3 T11: -0.2120 T22: 0.2860 REMARK 3 T33: -0.1393 T12: 0.0109 REMARK 3 T13: 0.0212 T23: 0.1055 REMARK 3 L TENSOR REMARK 3 L11: 6.8060 L22: 8.4501 REMARK 3 L33: 3.3075 L12: -5.3615 REMARK 3 L13: 4.4004 L23: -2.0685 REMARK 3 S TENSOR REMARK 3 S11: -0.0895 S12: -0.3425 S13: 0.6247 REMARK 3 S21: 0.0447 S22: -0.1484 S23: -0.5572 REMARK 3 S31: 0.1363 S32: 0.2823 S33: 0.2379 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): 95.6180 60.6510 2.6970 REMARK 3 T TENSOR REMARK 3 T11: -0.2016 T22: 0.1759 REMARK 3 T33: -0.1957 T12: -0.0230 REMARK 3 T13: 0.0497 T23: 0.0363 REMARK 3 L TENSOR REMARK 3 L11: 9.3678 L22: 4.9817 REMARK 3 L33: 3.6254 L12: -4.6469 REMARK 3 L13: 3.5673 L23: -1.0830 REMARK 3 S TENSOR REMARK 3 S11: -0.0239 S12: 0.3217 S13: -0.0162 REMARK 3 S21: -0.3210 S22: -0.1381 S23: -0.0136 REMARK 3 S31: -0.0503 S32: 0.3352 S33: 0.1621 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): 103.4940 63.0850 -2.2930 REMARK 3 T TENSOR REMARK 3 T11: -0.0608 T22: 0.2465 REMARK 3 T33: -0.1685 T12: 0.1398 REMARK 3 T13: 0.1358 T23: 0.1423 REMARK 3 L TENSOR REMARK 3 L11: 11.7744 L22: 7.2184 REMARK 3 L33: 6.1378 L12: -5.9583 REMARK 3 L13: 1.4024 L23: -4.6122 REMARK 3 S TENSOR REMARK 3 S11: 0.4725 S12: 1.6877 S13: -0.3658 REMARK 3 S21: -0.8299 S22: -0.6015 S23: -0.3561 REMARK 3 S31: -0.1131 S32: 1.0988 S33: 0.1290 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 1TY6. 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 2VDN 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-34085. 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 : 50647 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.90 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 (%) : 100.0 REMARK 200 DATA REDUNDANCY : 7 REMARK 200 R MERGE (I) : 0.15 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.90 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 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 : 2.70 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 (%): 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 IMIDAZOLE, PH 6.5, VAPOR DIFFUSION, HANGING REMARK 280 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 117.12200 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 58.56100 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 58.56100 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 117.12200 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: 11630 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 72070 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.7 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 4043 O HOH A 4101 1.88 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 -119.60 52.38 REMARK 500 LYS A 118 -127.86 52.43 REMARK 500 GLU A 123 133.66 95.61 REMARK 500 LEU A 212 -49.05 72.36 REMARK 500 SER A 261 72.78 45.60 REMARK 500 TYR A 353 17.68 59.36 REMARK 500 THR B 7 42.63 -101.12 REMARK 500 ARG B 8 68.57 -151.29 REMARK 500 VAL B 10 77.26 37.18 REMARK 500 PHE B 56 81.39 -158.61 REMARK 500 ASP B 66 47.07 -142.34 REMARK 500 ASP B 71 -168.73 -127.95 REMARK 500 VAL B 80 108.09 70.77 REMARK 500 ASN B 148 31.75 -96.85 REMARK 500 VAL B 157 -84.50 -122.78 REMARK 500 LEU B 196 109.93 -48.03 REMARK 500 SER B 213 -151.33 -112.66 REMARK 500 LEU B 258 -5.77 82.60 REMARK 500 VAL B 275 -80.12 -105.97 REMARK 500 LYS B 410 -32.04 74.84 REMARK 500 GLU B 442 73.81 55.83 REMARK 500 HIS B 446 -60.66 73.41 REMARK 500 THR B 454 154.29 67.68 REMARK 500 SER L 30 56.23 33.90 REMARK 500 SER L 31 7.31 59.73 REMARK 500 SER L 77 88.22 64.03 REMARK 500 ASN L 212 76.54 52.59 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 MG B2001 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP C 4 OD2 REMARK 620 2 HOH B4035 O 104.0 REMARK 620 3 SER B 121 OG 87.0 169.0 REMARK 620 4 SER B 123 OG 91.2 90.0 90.8 REMARK 620 5 GLU B 220 OE1 91.6 94.2 84.3 174.3 REMARK 620 6 HOH B4005 O 166.8 88.4 80.8 84.0 92.2 REMARK 620 N 1 2 3 4 5 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 49.1 REMARK 620 3 ASP A 245 OD2 112.1 64.8 REMARK 620 4 ASP A 247 O 87.2 77.3 92.7 REMARK 620 5 THR A 250 C 102.6 149.0 145.3 90.4 REMARK 620 6 THR A 250 O 82.0 127.7 165.4 83.8 21.4 REMARK 620 7 THR A 250 OG1 157.0 141.4 86.8 78.7 59.9 78.6 REMARK 620 8 GLU A 252 OE1 81.3 80.9 74.5 157.9 110.5 112.9 117.7 REMARK 620 9 GLU A 252 OE2 125.5 126.1 80.2 146.9 78.5 95.0 68.7 49.9 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 ASP A 297 OD1 REMARK 620 2 ASN A 299 OD1 86.7 REMARK 620 3 ASP A 301 OD1 77.5 75.1 REMARK 620 4 HOH A4124 O 153.7 90.1 76.4 REMARK 620 5 ARG A 303 O 82.2 168.3 98.6 98.1 REMARK 620 6 ASP A 305 OD1 139.8 94.9 141.6 66.5 96.0 REMARK 620 7 ASP A 305 OD2 94.3 73.5 147.9 109.8 111.2 48.8 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 70.8 REMARK 620 3 TYR A 371 O 64.7 84.2 REMARK 620 4 ASP A 367 OD1 83.7 87.9 148.3 REMARK 620 5 ASP A 373 OD1 91.0 156.4 102.0 74.8 REMARK 620 6 ASP A 373 OD2 128.6 153.0 88.7 110.8 50.6 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 94.6 REMARK 620 3 HOH A4138 O 133.5 85.1 REMARK 620 4 ASP A 426 OD1 77.2 84.8 148.4 REMARK 620 5 ASP A 428 OD1 151.0 87.4 75.5 74.1 REMARK 620 6 ASP A 434 OD1 106.6 158.6 82.5 96.8 72.7 REMARK 620 7 ASP A 434 OD2 85.0 139.1 67.0 134.1 112.0 48.6 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B2002 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GOL B1462 O1 REMARK 620 2 HOH B4040 O 70.0 REMARK 620 3 ASP B 127 OD1 106.7 161.5 REMARK 620 4 ASP B 251 OD2 107.3 76.9 87.1 REMARK 620 5 SER B 123 O 155.1 85.3 97.8 68.9 REMARK 620 6 ASP B 126 OD1 124.3 117.7 79.6 128.4 64.1 REMARK 620 N 1 2 3 4 5 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 162.4 REMARK 620 3 ASN B 215 OD1 90.6 101.4 REMARK 620 4 ASP B 217 OD1 73.5 93.7 88.7 REMARK 620 5 PRO B 219 O 89.2 78.8 179.8 91.2 REMARK 620 6 GLU B 220 OE2 87.9 105.7 85.8 160.6 94.2 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 MPT C 1 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1453 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL 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: 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.