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) : 46.23 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0 REMARK 3 NUMBER OF REFLECTIONS : 46776 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) : 0.169 REMARK 3 R VALUE (WORKING SET) : 0.167 REMARK 3 FREE R VALUE : 0.206 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2464 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) : 2.97 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3089 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2710 REMARK 3 BIN FREE R VALUE SET COUNT : 154 REMARK 3 BIN FREE R VALUE : 0.3330 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 10363 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 235 REMARK 3 SOLVENT ATOMS : 355 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) : 42.70 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.21000 REMARK 3 B22 (A**2) : 1.21000 REMARK 3 B33 (A**2) : -1.81000 REMARK 3 B12 (A**2) : 0.60000 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): 0.958 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.297 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.213 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.955 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10871 ; 0.005 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 7295 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14826 ; 0.925 ; 1.981 REMARK 3 BOND ANGLES OTHERS (DEGREES): 17675 ; 0.759 ; 3.005 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1353 ; 5.267 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 469 ;31.665 ;24.307 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1688 ;11.839 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 59 ;13.904 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1666 ; 0.057 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12068 ; 0.002 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 2138 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2008 ; 0.180 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 7548 ; 0.169 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5311 ; 0.170 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 5649 ; 0.080 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 453 ; 0.122 ; 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 ; 0.099 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 60 ; 0.148 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.113 ; 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): 6968 ; 1.244 ; 5.000 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10842 ; 2.056 ;10.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4547 ; 1.154 ; 5.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3979 ; 1.907 ;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): 133.1640 12.3590 78.5150 REMARK 3 T TENSOR REMARK 3 T11: 0.0426 T22: 0.1742 REMARK 3 T33: 0.0229 T12: 0.1713 REMARK 3 T13: 0.0326 T23: 0.3886 REMARK 3 L TENSOR REMARK 3 L11: 7.9623 L22: 6.1541 REMARK 3 L33: 2.9042 L12: -3.3784 REMARK 3 L13: 1.0282 L23: -1.7570 REMARK 3 S TENSOR REMARK 3 S11: -0.2017 S12: 0.0139 S13: -0.6761 REMARK 3 S21: 0.8316 S22: -0.2202 S23: -1.4399 REMARK 3 S31: 0.5505 S32: 0.8926 S33: 0.4220 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): 129.1830 21.8950 69.1370 REMARK 3 T TENSOR REMARK 3 T11: -0.1461 T22: 0.1027 REMARK 3 T33: -0.1593 T12: 0.0585 REMARK 3 T13: 0.0379 T23: 0.2725 REMARK 3 L TENSOR REMARK 3 L11: 3.1853 L22: 4.9013 REMARK 3 L33: 1.5567 L12: 1.4397 REMARK 3 L13: 0.4301 L23: -0.8645 REMARK 3 S TENSOR REMARK 3 S11: -0.0813 S12: 0.0068 S13: -0.2166 REMARK 3 S21: -0.0961 S22: -0.1640 S23: -0.4528 REMARK 3 S31: 0.3996 S32: 0.4212 S33: 0.2453 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): 118.6840 33.6410 64.5700 REMARK 3 T TENSOR REMARK 3 T11: -0.2020 T22: -0.0917 REMARK 3 T33: -0.2080 T12: -0.0562 REMARK 3 T13: -0.0519 T23: 0.1530 REMARK 3 L TENSOR REMARK 3 L11: 0.2918 L22: 2.4491 REMARK 3 L33: 1.8113 L12: -0.3883 REMARK 3 L13: -0.5044 L23: -0.6760 REMARK 3 S TENSOR REMARK 3 S11: -0.0771 S12: -0.0585 S13: -0.0452 REMARK 3 S21: 0.2667 S22: -0.1352 S23: -0.4412 REMARK 3 S31: 0.0308 S32: 0.4716 S33: 0.2123 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): 107.0400 36.1120 63.9220 REMARK 3 T TENSOR REMARK 3 T11: -0.1657 T22: -0.1398 REMARK 3 T33: -0.3337 T12: -0.0891 REMARK 3 T13: -0.0587 T23: 0.0761 REMARK 3 L TENSOR REMARK 3 L11: 4.6967 L22: 1.9635 REMARK 3 L33: 2.7361 L12: -0.7261 REMARK 3 L13: -1.7064 L23: -0.2838 REMARK 3 S TENSOR REMARK 3 S11: 0.0549 S12: 0.1301 S13: -0.2687 REMARK 3 S21: 0.1513 S22: -0.3274 S23: 0.1088 REMARK 3 S31: 0.1070 S32: -0.0594 S33: 0.2725 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): 106.1000 24.4980 64.1590 REMARK 3 T TENSOR REMARK 3 T11: -0.1738 T22: -0.1885 REMARK 3 T33: -0.2559 T12: -0.0437 REMARK 3 T13: 0.0008 T23: 0.0543 REMARK 3 L TENSOR REMARK 3 L11: 0.9343 L22: 1.7002 REMARK 3 L33: 2.3463 L12: -0.0784 REMARK 3 L13: -0.7169 L23: -1.0432 REMARK 3 S TENSOR REMARK 3 S11: 0.0041 S12: 0.1575 S13: -0.2321 REMARK 3 S21: -0.0494 S22: -0.1396 S23: 0.0029 REMARK 3 S31: 0.2176 S32: -0.1401 S33: 0.1355 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): 99.8230 13.0670 72.5500 REMARK 3 T TENSOR REMARK 3 T11: -0.0049 T22: -0.2317 REMARK 3 T33: -0.1685 T12: -0.1348 REMARK 3 T13: 0.0662 T23: 0.0830 REMARK 3 L TENSOR REMARK 3 L11: 2.7500 L22: 2.0947 REMARK 3 L33: 3.7555 L12: -0.5960 REMARK 3 L13: 0.0849 L23: 0.4358 REMARK 3 S TENSOR REMARK 3 S11: 0.0990 S12: 0.1378 S13: -0.4223 REMARK 3 S21: -0.0801 S22: -0.0930 S23: -0.0359 REMARK 3 S31: 0.4405 S32: -0.0801 S33: -0.0060 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): 107.9160 7.2120 84.5800 REMARK 3 T TENSOR REMARK 3 T11: 0.0920 T22: -0.1666 REMARK 3 T33: -0.1034 T12: -0.0212 REMARK 3 T13: 0.0797 T23: 0.2129 REMARK 3 L TENSOR REMARK 3 L11: 3.3487 L22: 6.0947 REMARK 3 L33: 6.8095 L12: -0.6427 REMARK 3 L13: -1.4262 L23: 4.5242 REMARK 3 S TENSOR REMARK 3 S11: -0.2663 S12: -0.3986 S13: -0.5138 REMARK 3 S21: 0.4917 S22: -0.0307 S23: 0.1057 REMARK 3 S31: 0.6801 S32: 0.1495 S33: 0.2970 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): 110.6190 2.9410 78.9130 REMARK 3 T TENSOR REMARK 3 T11: 0.2035 T22: -0.1732 REMARK 3 T33: -0.0876 T12: -0.0145 REMARK 3 T13: 0.0930 T23: 0.2434 REMARK 3 L TENSOR REMARK 3 L11: 1.7385 L22: 4.3235 REMARK 3 L33: 4.8754 L12: -0.9384 REMARK 3 L13: -1.1997 L23: 1.3342 REMARK 3 S TENSOR REMARK 3 S11: -0.1540 S12: 0.0756 S13: -0.3235 REMARK 3 S21: -0.0880 S22: -0.2533 S23: 0.0402 REMARK 3 S31: 0.8708 S32: -0.1205 S33: 0.4073 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): 124.4500 7.5290 80.2210 REMARK 3 T TENSOR REMARK 3 T11: 0.0932 T22: 0.0063 REMARK 3 T33: 0.0159 T12: 0.1323 REMARK 3 T13: 0.0518 T23: 0.3060 REMARK 3 L TENSOR REMARK 3 L11: 2.6329 L22: 3.3332 REMARK 3 L33: 2.7348 L12: -0.1035 REMARK 3 L13: -0.7219 L23: -0.0563 REMARK 3 S TENSOR REMARK 3 S11: -0.1290 S12: -0.1483 S13: -0.4486 REMARK 3 S21: 0.0701 S22: -0.2113 S23: -0.3182 REMARK 3 S31: 0.6129 S32: 0.4612 S33: 0.3403 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): 106.5340 21.2800 169.6670 REMARK 3 T TENSOR REMARK 3 T11: 1.0333 T22: 0.1420 REMARK 3 T33: 0.0702 T12: 0.0899 REMARK 3 T13: -0.1958 T23: -0.1354 REMARK 3 L TENSOR REMARK 3 L11: 3.4228 L22: 4.4598 REMARK 3 L33: 8.5569 L12: -2.1058 REMARK 3 L13: 2.9560 L23: -3.6053 REMARK 3 S TENSOR REMARK 3 S11: -0.2967 S12: -0.6181 S13: 0.0380 REMARK 3 S21: 1.4206 S22: 0.4282 S23: -0.2532 REMARK 3 S31: -1.0628 S32: -0.9177 S33: -0.1315 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 78 B 98 REMARK 3 ORIGIN FOR THE GROUP (A): 103.3390 29.8270 150.1690 REMARK 3 T TENSOR REMARK 3 T11: 0.7990 T22: 0.0967 REMARK 3 T33: 0.0161 T12: 0.1627 REMARK 3 T13: 0.0243 T23: -0.0128 REMARK 3 L TENSOR REMARK 3 L11: 10.9463 L22: 9.0368 REMARK 3 L33: 43.3190 L12: -5.4465 REMARK 3 L13: 19.4668 L23: -17.1049 REMARK 3 S TENSOR REMARK 3 S11: -0.5629 S12: -0.8826 S13: 0.5269 REMARK 3 S21: 1.1936 S22: 0.3049 S23: -0.5801 REMARK 3 S31: -2.3939 S32: -2.2572 S33: 0.2581 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): 97.6030 38.2510 104.6010 REMARK 3 T TENSOR REMARK 3 T11: 0.1970 T22: -0.0067 REMARK 3 T33: -0.2168 T12: -0.2150 REMARK 3 T13: 0.0066 T23: 0.0271 REMARK 3 L TENSOR REMARK 3 L11: 0.2053 L22: 0.7393 REMARK 3 L33: 2.9255 L12: -0.3104 REMARK 3 L13: 0.2147 L23: -1.1787 REMARK 3 S TENSOR REMARK 3 S11: 0.0140 S12: -0.3212 S13: -0.0586 REMARK 3 S21: 0.5553 S22: -0.0301 S23: 0.1005 REMARK 3 S31: -0.6181 S32: 0.0781 S33: 0.0161 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): 103.0920 34.3460 96.3200 REMARK 3 T TENSOR REMARK 3 T11: 0.0199 T22: -0.0769 REMARK 3 T33: -0.2783 T12: -0.1510 REMARK 3 T13: -0.0181 T23: 0.0714 REMARK 3 L TENSOR REMARK 3 L11: 1.9689 L22: 1.2632 REMARK 3 L33: 2.2414 L12: -0.5951 REMARK 3 L13: -1.0307 L23: 0.2150 REMARK 3 S TENSOR REMARK 3 S11: 0.0106 S12: -0.3510 S13: 0.0774 REMARK 3 S21: 0.4131 S22: -0.0953 S23: -0.1755 REMARK 3 S31: -0.1418 S32: 0.2027 S33: 0.0847 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): 100.3330 22.6260 131.3020 REMARK 3 T TENSOR REMARK 3 T11: 0.3260 T22: 0.1693 REMARK 3 T33: 0.0074 T12: -0.0447 REMARK 3 T13: 0.0539 T23: 0.0249 REMARK 3 L TENSOR REMARK 3 L11: 2.7377 L22: 2.7689 REMARK 3 L33: 23.4941 L12: -2.0258 REMARK 3 L13: 8.0171 L23: -5.7854 REMARK 3 S TENSOR REMARK 3 S11: 0.6779 S12: 0.5086 S13: -0.8712 REMARK 3 S21: 0.0008 S22: 0.3372 S23: -0.1800 REMARK 3 S31: 1.2913 S32: 0.5944 S33: -1.0152 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): 109.4720 28.1270 149.7170 REMARK 3 T TENSOR REMARK 3 T11: 0.7095 T22: 0.1061 REMARK 3 T33: 0.1305 T12: -0.0481 REMARK 3 T13: -0.1040 T23: 0.0006 REMARK 3 L TENSOR REMARK 3 L11: 3.1437 L22: 2.0877 REMARK 3 L33: 13.2447 L12: -1.4581 REMARK 3 L13: 4.3235 L23: -2.6944 REMARK 3 S TENSOR REMARK 3 S11: -0.2974 S12: 0.4587 S13: 0.1675 REMARK 3 S21: 0.7784 S22: 0.4134 S23: -0.7168 REMARK 3 S31: -1.6823 S32: 1.2319 S33: -0.1160 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): 119.2510 31.1760 183.8100 REMARK 3 T TENSOR REMARK 3 T11: 2.3534 T22: 1.1338 REMARK 3 T33: 1.0922 T12: -0.1422 REMARK 3 T13: -1.0368 T23: 0.0285 REMARK 3 L TENSOR REMARK 3 L11: 0.0000 L22: 0.0000 REMARK 3 L33: 0.0000 L12: 0.0000 REMARK 3 L13: 0.0000 L23: 0.0000 REMARK 3 S TENSOR REMARK 3 S11: -0.3907 S12: -1.4030 S13: 0.1351 REMARK 3 S21: -0.1435 S22: 0.3542 S23: -0.3330 REMARK 3 S31: -1.2221 S32: 3.1313 S33: 0.0366 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): 89.7100 36.7560 33.5380 REMARK 3 T TENSOR REMARK 3 T11: -0.1793 T22: -0.0775 REMARK 3 T33: -0.2307 T12: -0.2355 REMARK 3 T13: 0.0060 T23: 0.0225 REMARK 3 L TENSOR REMARK 3 L11: 8.1816 L22: 17.3548 REMARK 3 L33: 15.6083 L12: -10.7108 REMARK 3 L13: 7.9651 L23: -11.7933 REMARK 3 S TENSOR REMARK 3 S11: 0.5947 S12: 0.5126 S13: -0.5792 REMARK 3 S21: -0.9268 S22: -0.6716 S23: 0.0908 REMARK 3 S31: 1.3108 S32: -0.0166 S33: 0.0769 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): 93.9500 42.1740 41.4690 REMARK 3 T TENSOR REMARK 3 T11: -0.2707 T22: -0.1826 REMARK 3 T33: -0.2838 T12: -0.0586 REMARK 3 T13: -0.0066 T23: 0.0412 REMARK 3 L TENSOR REMARK 3 L11: 4.0201 L22: 0.5460 REMARK 3 L33: 2.4272 L12: -0.6723 REMARK 3 L13: 1.6012 L23: 0.5885 REMARK 3 S TENSOR REMARK 3 S11: 0.0598 S12: -0.0241 S13: 0.0918 REMARK 3 S21: 0.0104 S22: 0.0496 S23: 0.2428 REMARK 3 S31: 0.3504 S32: -0.2838 S33: -0.1094 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): 93.7500 42.9750 43.7550 REMARK 3 T TENSOR REMARK 3 T11: -0.2510 T22: -0.1151 REMARK 3 T33: -0.2512 T12: -0.0554 REMARK 3 T13: 0.0136 T23: 0.0647 REMARK 3 L TENSOR REMARK 3 L11: 2.3041 L22: 0.3230 REMARK 3 L33: 3.3734 L12: -0.5822 REMARK 3 L13: 1.8702 L23: -1.0438 REMARK 3 S TENSOR REMARK 3 S11: -0.0852 S12: 0.0687 S13: 0.1227 REMARK 3 S21: -0.0281 S22: 0.0130 S23: 0.0479 REMARK 3 S31: 0.1463 S32: -0.3266 S33: 0.0722 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): 86.1230 47.6040 13.2300 REMARK 3 T TENSOR REMARK 3 T11: -0.2031 T22: -0.0078 REMARK 3 T33: -0.1247 T12: -0.1126 REMARK 3 T13: -0.0713 T23: 0.0045 REMARK 3 L TENSOR REMARK 3 L11: 2.5317 L22: 1.4237 REMARK 3 L33: 3.3323 L12: -1.6794 REMARK 3 L13: -0.3464 L23: 1.2385 REMARK 3 S TENSOR REMARK 3 S11: 0.3246 S12: 0.3220 S13: -0.2627 REMARK 3 S21: -0.3160 S22: 0.0736 S23: 0.3332 REMARK 3 S31: -0.4413 S32: -0.7710 S33: -0.3982 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): 92.0910 44.5370 5.2110 REMARK 3 T TENSOR REMARK 3 T11: 0.0054 T22: 0.0508 REMARK 3 T33: -0.0683 T12: 0.1119 REMARK 3 T13: -0.1651 T23: 0.0214 REMARK 3 L TENSOR REMARK 3 L11: 9.7051 L22: 2.4121 REMARK 3 L33: 13.0263 L12: 0.0259 REMARK 3 L13: -6.4447 L23: 1.2276 REMARK 3 S TENSOR REMARK 3 S11: 0.1441 S12: 0.5591 S13: -0.1245 REMARK 3 S21: -0.3715 S22: 0.1636 S23: -0.2930 REMARK 3 S31: 1.1826 S32: -0.0728 S33: -0.3077 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): 94.2550 47.4110 9.4840 REMARK 3 T TENSOR REMARK 3 T11: -0.0471 T22: -0.1098 REMARK 3 T33: -0.1829 T12: 0.0869 REMARK 3 T13: -0.0635 T23: 0.0474 REMARK 3 L TENSOR REMARK 3 L11: 6.0081 L22: 1.2575 REMARK 3 L33: 17.7681 L12: 1.9584 REMARK 3 L13: -0.3067 L23: -3.4153 REMARK 3 S TENSOR REMARK 3 S11: 0.2738 S12: -0.0017 S13: 0.3364 REMARK 3 S21: -0.5594 S22: -0.2928 S23: 0.1853 REMARK 3 S31: 0.2544 S32: 0.7185 S33: 0.0190 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): 93.6550 40.4600 -3.3680 REMARK 3 T TENSOR REMARK 3 T11: 0.5256 T22: 0.2778 REMARK 3 T33: -0.0238 T12: 0.2891 REMARK 3 T13: 0.0261 T23: -0.0733 REMARK 3 L TENSOR REMARK 3 L11: 11.2833 L22: 2.6581 REMARK 3 L33: 3.2375 L12: 0.1457 REMARK 3 L13: -4.8146 L23: 1.7105 REMARK 3 S TENSOR REMARK 3 S11: 0.3197 S12: 0.0149 S13: -1.3704 REMARK 3 S21: -0.9467 S22: -0.5993 S23: -0.2013 REMARK 3 S31: 0.4162 S32: 1.2192 S33: 0.2797 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): 85.7150 43.6710 -1.7230 REMARK 3 T TENSOR REMARK 3 T11: 0.0462 T22: 0.3491 REMARK 3 T33: -0.0350 T12: -0.0228 REMARK 3 T13: -0.1806 T23: -0.0857 REMARK 3 L TENSOR REMARK 3 L11: 11.9914 L22: 6.2193 REMARK 3 L33: 22.8893 L12: 4.4986 REMARK 3 L13: -14.4984 L23: -3.8509 REMARK 3 S TENSOR REMARK 3 S11: -0.0924 S12: 0.6505 S13: 0.2201 REMARK 3 S21: -1.2402 S22: 0.5047 S23: 1.1632 REMARK 3 S31: 1.5531 S32: -1.0156 S33: -0.4123 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): 114.1160 50.1220 35.4450 REMARK 3 T TENSOR REMARK 3 T11: -0.2215 T22: -0.0965 REMARK 3 T33: -0.1972 T12: 0.0119 REMARK 3 T13: 0.0297 T23: 0.1222 REMARK 3 L TENSOR REMARK 3 L11: 0.5417 L22: 0.9300 REMARK 3 L33: 0.8988 L12: -0.0735 REMARK 3 L13: -0.4865 L23: 0.2195 REMARK 3 S TENSOR REMARK 3 S11: 0.0885 S12: 0.2293 S13: 0.0792 REMARK 3 S21: -0.1718 S22: -0.0168 S23: -0.0873 REMARK 3 S31: -0.3125 S32: 0.0307 S33: -0.0718 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): 113.3910 39.1540 36.4690 REMARK 3 T TENSOR REMARK 3 T11: -0.2520 T22: -0.1628 REMARK 3 T33: -0.2684 T12: 0.0695 REMARK 3 T13: 0.0014 T23: 0.0119 REMARK 3 L TENSOR REMARK 3 L11: 3.5522 L22: 2.9398 REMARK 3 L33: 2.6791 L12: 1.5928 REMARK 3 L13: -2.0217 L23: -1.8266 REMARK 3 S TENSOR REMARK 3 S11: 0.1147 S12: 0.4019 S13: -0.4701 REMARK 3 S21: -0.1858 S22: 0.0051 S23: -0.1938 REMARK 3 S31: 0.5192 S32: 0.1627 S33: -0.1198 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): 112.1560 45.7340 35.9360 REMARK 3 T TENSOR REMARK 3 T11: -0.2388 T22: -0.1602 REMARK 3 T33: -0.2579 T12: 0.0128 REMARK 3 T13: -0.0384 T23: 0.0771 REMARK 3 L TENSOR REMARK 3 L11: 4.1283 L22: 0.6033 REMARK 3 L33: 3.0316 L12: 0.8981 REMARK 3 L13: -2.0588 L23: -1.3523 REMARK 3 S TENSOR REMARK 3 S11: -0.0883 S12: 0.2990 S13: 0.0348 REMARK 3 S21: -0.0327 S22: 0.0652 S23: -0.0341 REMARK 3 S31: 0.3772 S32: 0.1340 S33: 0.0232 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): 100.2520 53.0350 8.4270 REMARK 3 T TENSOR REMARK 3 T11: -0.1953 T22: 0.1394 REMARK 3 T33: -0.2383 T12: 0.0251 REMARK 3 T13: 0.0047 T23: 0.0856 REMARK 3 L TENSOR REMARK 3 L11: 0.7660 L22: 2.9411 REMARK 3 L33: 5.2173 L12: -1.5009 REMARK 3 L13: 1.3547 L23: -2.6727 REMARK 3 S TENSOR REMARK 3 S11: 0.5295 S12: 0.2929 S13: -0.1838 REMARK 3 S21: -0.4829 S22: -0.3074 S23: 0.1587 REMARK 3 S31: 0.6646 S32: 0.2299 S33: -0.2221 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): 101.4510 59.6550 9.0630 REMARK 3 T TENSOR REMARK 3 T11: -0.2381 T22: 0.1879 REMARK 3 T33: -0.2675 T12: 0.0085 REMARK 3 T13: -0.0086 T23: 0.0154 REMARK 3 L TENSOR REMARK 3 L11: 6.3505 L22: 5.3999 REMARK 3 L33: 4.6282 L12: -3.1331 REMARK 3 L13: 3.0704 L23: -2.8094 REMARK 3 S TENSOR REMARK 3 S11: -0.0607 S12: -0.2293 S13: 0.4613 REMARK 3 S21: 0.3239 S22: -0.1691 S23: -0.1658 REMARK 3 S31: -0.0545 S32: 0.2802 S33: 0.2298 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): 95.0700 59.9320 3.1960 REMARK 3 T TENSOR REMARK 3 T11: -0.2355 T22: 0.0884 REMARK 3 T33: -0.2127 T12: -0.0190 REMARK 3 T13: 0.0513 T23: 0.0518 REMARK 3 L TENSOR REMARK 3 L11: 8.2964 L22: 3.7263 REMARK 3 L33: 4.8336 L12: -4.4909 REMARK 3 L13: 3.9596 L23: -1.2337 REMARK 3 S TENSOR REMARK 3 S11: 0.0154 S12: 0.2544 S13: -0.0390 REMARK 3 S21: -0.4880 S22: -0.0491 S23: -0.1207 REMARK 3 S31: 0.0183 S32: 0.2025 S33: 0.0337 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): 102.8900 62.3000 -1.8740 REMARK 3 T TENSOR REMARK 3 T11: -0.0746 T22: 0.1750 REMARK 3 T33: -0.1636 T12: 0.0868 REMARK 3 T13: 0.1183 T23: 0.1123 REMARK 3 L TENSOR REMARK 3 L11: 13.3494 L22: 7.9082 REMARK 3 L33: 9.2264 L12: -8.1549 REMARK 3 L13: 5.9917 L23: -6.5288 REMARK 3 S TENSOR REMARK 3 S11: 0.1642 S12: 1.6823 S13: -1.0121 REMARK 3 S21: -0.5470 S22: 0.0535 S23: 0.1836 REMARK 3 S31: -0.3750 S32: 1.0167 S33: -0.2176 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 1TY5. 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. THE ARRANGEMENT OF ATOMS AT CENTERS IN THE LIGAND THAT REMARK 3 ARE FREE TO REARRANGE IN SOLVENT IS CHANGED. MISTAKES IN REMARK 3 CARBOHYDRATE ANOMERIC LINKAGES ARE ALSO CORRECTED. REMARK 4 REMARK 4 2VDM 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-34060. 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 : CUSTOM (SBC2 3K) REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50516 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 (%) : 99.8 REMARK 200 DATA REDUNDANCY : 7.00 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) : 2.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2 REMARK 200 DATA REDUNDANCY IN SHELL : 6.00 REMARK 200 R MERGE FOR SHELL (I) : 0.58 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.00 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 (%): 67.5 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.8 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10-12% PEG3350, 0.7 M MAGNESIUM REMARK 280 ACETATE, 0.1 M IMIDAZOLE, 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 118.15933 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 59.07967 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 59.07967 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 118.15933 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: PQS REMARK 350 TOTAL BURIED SURFACE AREA: 10970 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 71810 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.7 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY B 73 REMARK 465 SER B 74 REMARK 465 GLY B 75 REMARK 465 ASP B 76 REMARK 465 SER B 77 REMARK 465 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 4035 O HOH B 4037 2.20 REMARK 500 O HOH H 4020 O HOH H 4022 2.17 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 29.11 -140.09 REMARK 500 SER A 101 -129.84 50.26 REMARK 500 LYS A 118 -130.36 52.78 REMARK 500 GLU A 123 129.73 99.33 REMARK 500 LEU A 212 -52.09 77.55 REMARK 500 SER A 261 70.65 48.18 REMARK 500 THR B 7 54.79 -96.81 REMARK 500 ARG B 8 66.56 -154.05 REMARK 500 VAL B 10 73.90 43.29 REMARK 500 ASP B 47 38.20 -99.88 REMARK 500 ASP B 66 49.08 -142.48 REMARK 500 VAL B 80 91.25 62.47 REMARK 500 PRO B 94 121.59 -33.79 REMARK 500 ASP B 95 -8.17 64.89 REMARK 500 VAL B 157 -81.24 -125.69 REMARK 500 SER B 213 -154.15 -117.99 REMARK 500 LEU B 258 -3.08 87.71 REMARK 500 VAL B 275 -75.46 -95.73 REMARK 500 ASN B 303 60.95 61.46 REMARK 500 CYS B 374 -158.88 -91.59 REMARK 500 LYS B 410 -30.44 77.62 REMARK 500 GLU B 442 76.08 57.35 REMARK 500 HIS B 446 -59.26 70.85 REMARK 500 THR B 454 153.28 67.52 REMARK 500 ASP H 179 -13.54 70.49 REMARK 500 SER L 30 67.08 24.91 REMARK 500 SER L 77 81.64 59.56 REMARK 500 ASN L 212 85.37 52.13 REMARK 500 GLU L 213 57.88 -147.41 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 47.0 REMARK 620 3 ASP A 245 OD2 114.1 68.5 REMARK 620 4 ASP A 247 O 79.8 69.2 90.7 REMARK 620 5 THR A 250 C 92.4 135.8 153.2 89.8 REMARK 620 6 THR A 250 O 72.3 115.6 170.1 82.9 20.5 REMARK 620 7 THR A 250 OG1 144.3 143.5 94.8 79.3 59.0 76.7 REMARK 620 8 GLU A 252 OE1 76.5 85.2 87.5 153.0 103.7 101.7 127.7 REMARK 620 9 GLU A 252 OE2 123.1 130.9 86.6 155.8 82.1 96.2 77.0 50.9 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 ASN A 299 OD1 REMARK 620 2 ASP A 301 OD1 77.7 REMARK 620 3 ASP A 297 OD1 81.3 76.4 REMARK 620 4 ARG A 303 O 161.6 92.6 81.2 REMARK 620 5 ASP A 305 OD1 106.9 152.9 130.4 88.9 REMARK 620 6 ASP A 305 OD2 81.1 155.4 88.1 104.0 47.4 REMARK 620 7 HOH A4120 O 97.2 76.1 152.1 95.5 76.9 119.3 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 79.8 REMARK 620 3 TYR A 371 O 71.0 83.4 REMARK 620 4 ASP A 367 OD1 78.3 98.7 148.3 REMARK 620 5 ASP A 373 OD1 86.8 163.4 101.5 68.8 REMARK 620 6 ASP A 373 OD2 122.3 150.1 85.5 105.2 46.5 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 90.2 REMARK 620 3 ASP A 426 OD1 77.5 83.6 REMARK 620 4 ASP A 428 OD1 151.5 84.0 74.2 REMARK 620 5 ASP A 434 OD1 107.1 160.8 92.1 76.9 REMARK 620 6 ASP A 434 OD2 91.1 142.3 133.3 110.4 48.0 REMARK 620 7 HOH A4134 O 138.3 84.6 142.2 69.0 87.6 69.9 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B2002 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GOL B1463 O2 REMARK 620 2 HOH B4009 O 102.1 REMARK 620 3 ASP B 127 OD1 69.1 170.0 REMARK 620 4 ASP B 251 OD2 116.5 95.2 85.1 REMARK 620 5 GOL B1463 O1 63.4 74.9 96.4 63.5 REMARK 620 6 SER B 123 O 161.8 84.0 105.9 79.4 134.6 REMARK 620 7 ASP B 126 OD1 84.5 100.5 83.7 150.5 145.0 77.6 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 162.4 REMARK 620 3 ASN B 215 OD1 89.6 100.8 REMARK 620 4 ASP B 217 OD1 75.8 90.1 88.5 REMARK 620 5 PRO B 219 O 88.3 82.8 173.7 96.8 REMARK 620 6 GLU B 220 OE2 89.7 105.4 83.7 163.7 90.3 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG B2001 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH B4028 O REMARK 620 2 SER B 123 OG 90.9 REMARK 620 3 GLU B 220 OE1 77.6 162.8 REMARK 620 4 HOH B4008 O 97.1 88.2 105.7 REMARK 620 5 AGG B1462 OXT 90.6 79.3 88.0 165.4 REMARK 620 6 SER B 121 OG 163.7 96.7 91.5 97.6 76.7 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 AGG B1462 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 B1463 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.