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. 2.59 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) : 2.59 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.63 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 92.2 REMARK 3 NUMBER OF REFLECTIONS : 60283 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) : 0.143 REMARK 3 R VALUE (WORKING SET) : 0.141 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 : 3207 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) : 2.59 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3171 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2560 REMARK 3 BIN FREE R VALUE SET COUNT : 172 REMARK 3 BIN FREE R VALUE : 0.3480 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 10515 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 205 REMARK 3 SOLVENT ATOMS : 1332 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) : 41.15 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.21000 REMARK 3 B22 (A**2) : -0.21000 REMARK 3 B33 (A**2) : 0.31000 REMARK 3 B12 (A**2) : -0.10000 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): 0.381 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.230 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.154 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.204 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11011 ; 0.007 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 7399 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15042 ; 1.043 ; 1.979 REMARK 3 BOND ANGLES OTHERS (DEGREES): 17995 ; 0.786 ; 3.004 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1392 ; 5.666 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 480 ;34.024 ;24.250 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1734 ;12.618 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 63 ;14.186 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1694 ; 0.063 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12275 ; 0.003 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 2182 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2167 ; 0.187 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 7952 ; 0.180 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5357 ; 0.174 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 5803 ; 0.081 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1064 ; 0.144 ; 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): 24 ; 0.109 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 93 ; 0.193 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 43 ; 0.155 ; 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): 7028 ; 1.831 ; 5.000 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10991 ; 2.920 ;10.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4613 ; 1.902 ; 5.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4030 ; 2.953 ;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 : 26 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 32 REMARK 3 ORIGIN FOR THE GROUP (A): 129.9990 14.2740 71.9790 REMARK 3 T TENSOR REMARK 3 T11: -0.1787 T22: 0.0578 REMARK 3 T33: 0.0188 T12: 0.1115 REMARK 3 T13: 0.0870 T23: 0.2906 REMARK 3 L TENSOR REMARK 3 L11: 5.1519 L22: 5.0488 REMARK 3 L33: 3.6863 L12: -0.3678 REMARK 3 L13: 1.1721 L23: -0.3050 REMARK 3 S TENSOR REMARK 3 S11: -0.0385 S12: 0.4202 S13: -0.4221 REMARK 3 S21: -0.0407 S22: -0.3412 S23: -0.5086 REMARK 3 S31: 0.4757 S32: 0.8968 S33: 0.3797 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 33 A 54 REMARK 3 ORIGIN FOR THE GROUP (A): 126.9090 29.6390 71.6850 REMARK 3 T TENSOR REMARK 3 T11: -0.1973 T22: -0.0144 REMARK 3 T33: -0.1091 T12: 0.0036 REMARK 3 T13: -0.0214 T23: 0.1883 REMARK 3 L TENSOR REMARK 3 L11: 2.4012 L22: 13.1682 REMARK 3 L33: 3.3830 L12: 0.3354 REMARK 3 L13: -0.8020 L23: 3.7316 REMARK 3 S TENSOR REMARK 3 S11: 0.1791 S12: -0.3031 S13: 0.0000 REMARK 3 S21: -0.0964 S22: -0.3707 S23: -0.1127 REMARK 3 S31: -0.1689 S32: 0.0444 S33: 0.1915 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 55 A 115 REMARK 3 ORIGIN FOR THE GROUP (A): 121.1170 30.8140 64.9070 REMARK 3 T TENSOR REMARK 3 T11: -0.1370 T22: 0.0192 REMARK 3 T33: -0.0122 T12: -0.0652 REMARK 3 T13: -0.0353 T23: 0.1571 REMARK 3 L TENSOR REMARK 3 L11: 1.2436 L22: 1.4073 REMARK 3 L33: 1.7709 L12: -0.5960 REMARK 3 L13: -0.4862 L23: -0.7239 REMARK 3 S TENSOR REMARK 3 S11: -0.0851 S12: -0.1345 S13: 0.0430 REMARK 3 S21: 0.1812 S22: -0.1609 S23: -0.3336 REMARK 3 S31: 0.0019 S32: 0.4327 S33: 0.2460 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 164 REMARK 3 ORIGIN FOR THE GROUP (A): 107.2940 36.0800 63.0130 REMARK 3 T TENSOR REMARK 3 T11: -0.1120 T22: -0.0383 REMARK 3 T33: -0.0803 T12: -0.0791 REMARK 3 T13: -0.0354 T23: 0.0961 REMARK 3 L TENSOR REMARK 3 L11: 2.4072 L22: 1.5037 REMARK 3 L33: 2.5331 L12: 0.3592 REMARK 3 L13: -1.6436 L23: -0.2923 REMARK 3 S TENSOR REMARK 3 S11: 0.0072 S12: 0.0379 S13: -0.1503 REMARK 3 S21: -0.0011 S22: -0.2012 S23: 0.2352 REMARK 3 S31: -0.0055 S32: 0.0328 S33: 0.1940 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 165 A 243 REMARK 3 ORIGIN FOR THE GROUP (A): 105.7750 24.9610 64.1890 REMARK 3 T TENSOR REMARK 3 T11: -0.0788 T22: -0.0583 REMARK 3 T33: -0.0321 T12: -0.0571 REMARK 3 T13: 0.0054 T23: 0.0660 REMARK 3 L TENSOR REMARK 3 L11: 1.0567 L22: 1.2248 REMARK 3 L33: 2.1111 L12: 0.2732 REMARK 3 L13: -0.6243 L23: -0.6772 REMARK 3 S TENSOR REMARK 3 S11: 0.0165 S12: 0.1411 S13: -0.0951 REMARK 3 S21: 0.0331 S22: -0.1469 S23: -0.0012 REMARK 3 S31: 0.2090 S32: -0.1146 S33: 0.1304 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 315 REMARK 3 ORIGIN FOR THE GROUP (A): 102.4390 10.7280 73.6970 REMARK 3 T TENSOR REMARK 3 T11: 0.0473 T22: -0.1845 REMARK 3 T33: -0.0614 T12: -0.1151 REMARK 3 T13: 0.0776 T23: 0.0796 REMARK 3 L TENSOR REMARK 3 L11: 1.8569 L22: 2.1080 REMARK 3 L33: 1.9814 L12: -0.2102 REMARK 3 L13: 0.1843 L23: 0.4512 REMARK 3 S TENSOR REMARK 3 S11: -0.1105 S12: 0.1435 S13: -0.3214 REMARK 3 S21: -0.0541 S22: -0.1359 S23: 0.0494 REMARK 3 S31: 0.4135 S32: -0.1282 S33: 0.2465 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 316 A 337 REMARK 3 ORIGIN FOR THE GROUP (A): 104.1120 4.8050 86.1090 REMARK 3 T TENSOR REMARK 3 T11: 0.1279 T22: -0.1388 REMARK 3 T33: -0.0602 T12: -0.1425 REMARK 3 T13: 0.1305 T23: 0.1937 REMARK 3 L TENSOR REMARK 3 L11: 2.1365 L22: 7.1695 REMARK 3 L33: 9.1865 L12: -0.7694 REMARK 3 L13: -1.7963 L23: 6.6196 REMARK 3 S TENSOR REMARK 3 S11: -0.2291 S12: -0.3808 S13: -0.3685 REMARK 3 S21: 0.3813 S22: -0.5868 S23: 0.4293 REMARK 3 S31: 0.7645 S32: -0.9096 S33: 0.8159 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 338 A 376 REMARK 3 ORIGIN FOR THE GROUP (A): 113.6490 3.6330 79.6290 REMARK 3 T TENSOR REMARK 3 T11: 0.0745 T22: -0.2220 REMARK 3 T33: -0.0559 T12: 0.0157 REMARK 3 T13: 0.0675 T23: 0.2146 REMARK 3 L TENSOR REMARK 3 L11: 3.0515 L22: 3.2838 REMARK 3 L33: 2.6375 L12: -0.1103 REMARK 3 L13: -0.1449 L23: 0.3975 REMARK 3 S TENSOR REMARK 3 S11: -0.0857 S12: -0.0342 S13: -0.3666 REMARK 3 S21: -0.1005 S22: -0.1327 S23: -0.2389 REMARK 3 S31: 0.5976 S32: 0.2294 S33: 0.2183 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 377 A 452 REMARK 3 ORIGIN FOR THE GROUP (A): 124.5070 7.6770 80.1260 REMARK 3 T TENSOR REMARK 3 T11: -0.0093 T22: -0.0388 REMARK 3 T33: -0.0030 T12: 0.1191 REMARK 3 T13: 0.0202 T23: 0.2936 REMARK 3 L TENSOR REMARK 3 L11: 2.3363 L22: 2.7976 REMARK 3 L33: 2.4300 L12: 0.1782 REMARK 3 L13: -0.6420 L23: -0.1394 REMARK 3 S TENSOR REMARK 3 S11: -0.1123 S12: -0.2174 S13: -0.4054 REMARK 3 S21: 0.2705 S22: -0.2252 S23: -0.4257 REMARK 3 S31: 0.6046 S32: 0.6174 S33: 0.3375 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 28 REMARK 3 ORIGIN FOR THE GROUP (A): 113.8000 17.0360 172.1780 REMARK 3 T TENSOR REMARK 3 T11: 0.4486 T22: -0.4309 REMARK 3 T33: -0.2413 T12: 0.0164 REMARK 3 T13: -0.3453 T23: -0.0931 REMARK 3 L TENSOR REMARK 3 L11: 6.2350 L22: 14.3805 REMARK 3 L33: 5.1649 L12: -2.3156 REMARK 3 L13: 3.9937 L23: -1.2521 REMARK 3 S TENSOR REMARK 3 S11: -0.1259 S12: -0.1970 S13: -0.0384 REMARK 3 S21: 1.4073 S22: 0.3054 S23: -0.6692 REMARK 3 S31: -0.2736 S32: 0.2443 S33: -0.1795 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 29 B 72 REMARK 3 ORIGIN FOR THE GROUP (A): 102.3200 23.4350 167.4900 REMARK 3 T TENSOR REMARK 3 T11: 0.7302 T22: -0.0102 REMARK 3 T33: -0.3091 T12: 0.2532 REMARK 3 T13: -0.0327 T23: -0.0552 REMARK 3 L TENSOR REMARK 3 L11: 3.2746 L22: 2.0407 REMARK 3 L33: 2.2909 L12: -0.8174 REMARK 3 L13: 1.7191 L23: -0.6076 REMARK 3 S TENSOR REMARK 3 S11: -0.2260 S12: -0.8079 S13: -0.0066 REMARK 3 S21: 0.9678 S22: 0.5002 S23: -0.0709 REMARK 3 S31: -1.2238 S32: -1.5571 S33: -0.2742 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 79 B 100 REMARK 3 ORIGIN FOR THE GROUP (A): 102.3010 29.9010 148.3970 REMARK 3 T TENSOR REMARK 3 T11: 0.5258 T22: -0.0713 REMARK 3 T33: -0.3133 T12: 0.1662 REMARK 3 T13: 0.0410 T23: -0.0023 REMARK 3 L TENSOR REMARK 3 L11: 8.2655 L22: 7.6482 REMARK 3 L33: 36.7959 L12: -2.8276 REMARK 3 L13: 16.7047 L23: -10.2179 REMARK 3 S TENSOR REMARK 3 S11: -1.0577 S12: -0.6040 S13: 0.5160 REMARK 3 S21: 1.3068 S22: 0.4407 S23: -0.3001 REMARK 3 S31: -3.3040 S32: -1.3657 S33: 0.6170 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 101 B 137 REMARK 3 ORIGIN FOR THE GROUP (A): 93.9350 37.0550 108.0790 REMARK 3 T TENSOR REMARK 3 T11: 0.2543 T22: -0.0724 REMARK 3 T33: -0.1020 T12: -0.2006 REMARK 3 T13: 0.0686 T23: 0.0119 REMARK 3 L TENSOR REMARK 3 L11: 1.1865 L22: 0.6094 REMARK 3 L33: 5.4983 L12: -0.7332 REMARK 3 L13: 0.7916 L23: -1.3706 REMARK 3 S TENSOR REMARK 3 S11: -0.1074 S12: -0.1572 S13: 0.0511 REMARK 3 S21: 0.4877 S22: -0.0865 S23: 0.0445 REMARK 3 S31: -0.4282 S32: 0.1160 S33: 0.1940 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 138 B 201 REMARK 3 ORIGIN FOR THE GROUP (A): 101.2600 43.1150 94.8760 REMARK 3 T TENSOR REMARK 3 T11: 0.1063 T22: -0.1225 REMARK 3 T33: -0.1318 T12: -0.1774 REMARK 3 T13: 0.0201 T23: 0.0130 REMARK 3 L TENSOR REMARK 3 L11: 1.2960 L22: 0.9821 REMARK 3 L33: 4.6923 L12: 0.0436 REMARK 3 L13: -1.5197 L23: -0.5624 REMARK 3 S TENSOR REMARK 3 S11: 0.1561 S12: -0.1548 S13: 0.1829 REMARK 3 S21: 0.4261 S22: -0.0306 S23: -0.0659 REMARK 3 S31: -0.5996 S32: 0.2147 S33: -0.1255 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 202 B 342 REMARK 3 ORIGIN FOR THE GROUP (A): 102.4620 31.5100 97.1020 REMARK 3 T TENSOR REMARK 3 T11: 0.0491 T22: -0.0650 REMARK 3 T33: -0.1562 T12: -0.1644 REMARK 3 T13: -0.0101 T23: 0.0660 REMARK 3 L TENSOR REMARK 3 L11: 1.5493 L22: 1.8464 REMARK 3 L33: 2.0068 L12: -0.5912 REMARK 3 L13: -0.8140 L23: 0.1812 REMARK 3 S TENSOR REMARK 3 S11: -0.0193 S12: -0.3055 S13: 0.0652 REMARK 3 S21: 0.4279 S22: -0.0598 S23: -0.0981 REMARK 3 S31: 0.0238 S32: 0.2493 S33: 0.0791 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 343 B 390 REMARK 3 ORIGIN FOR THE GROUP (A): 101.5280 21.6940 133.0120 REMARK 3 T TENSOR REMARK 3 T11: 0.2288 T22: -0.1804 REMARK 3 T33: -0.2087 T12: -0.0399 REMARK 3 T13: 0.0243 T23: -0.0084 REMARK 3 L TENSOR REMARK 3 L11: 2.8048 L22: 2.5615 REMARK 3 L33: 19.7061 L12: -1.6337 REMARK 3 L13: 6.6871 L23: -4.2707 REMARK 3 S TENSOR REMARK 3 S11: 0.7710 S12: 0.5888 S13: -0.4580 REMARK 3 S21: -0.3756 S22: 0.0546 S23: -0.1430 REMARK 3 S31: 1.5450 S32: 0.9774 S33: -0.8256 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 : B 391 B 441 REMARK 3 ORIGIN FOR THE GROUP (A): 108.4880 28.4820 149.8610 REMARK 3 T TENSOR REMARK 3 T11: 0.4416 T22: -0.3811 REMARK 3 T33: -0.2293 T12: -0.0648 REMARK 3 T13: -0.0475 T23: 0.0318 REMARK 3 L TENSOR REMARK 3 L11: 3.3091 L22: 1.7811 REMARK 3 L33: 16.7006 L12: -0.6451 REMARK 3 L13: 5.0743 L23: -0.9941 REMARK 3 S TENSOR REMARK 3 S11: -0.2339 S12: 0.4819 S13: 0.1202 REMARK 3 S21: 0.6757 S22: 0.3232 S23: -0.3835 REMARK 3 S31: -1.7264 S32: 0.9200 S33: -0.0893 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 : B 442 B 461 REMARK 3 ORIGIN FOR THE GROUP (A): 119.6940 30.8980 184.5140 REMARK 3 T TENSOR REMARK 3 T11: 1.7696 T22: 1.0824 REMARK 3 T33: 0.6805 T12: -0.3199 REMARK 3 T13: -0.6514 T23: -0.0787 REMARK 3 L TENSOR REMARK 3 L11: 6.4814 L22: 12.9537 REMARK 3 L33: 5.8462 L12: -8.7206 REMARK 3 L13: 5.7023 L23: -8.6783 REMARK 3 S TENSOR REMARK 3 S11: -0.4790 S12: -0.3372 S13: 0.7357 REMARK 3 S21: 2.5891 S22: -0.9301 S23: -2.9384 REMARK 3 S31: -0.4542 S32: 3.0396 S33: 1.4091 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 1 H 31 REMARK 3 ORIGIN FOR THE GROUP (A): 89.7040 36.1840 37.9770 REMARK 3 T TENSOR REMARK 3 T11: -0.1584 T22: -0.0427 REMARK 3 T33: -0.0594 T12: -0.1632 REMARK 3 T13: -0.0325 T23: 0.0509 REMARK 3 L TENSOR REMARK 3 L11: 6.2129 L22: 6.5952 REMARK 3 L33: 6.4030 L12: -3.7054 REMARK 3 L13: 3.2611 L23: -3.7758 REMARK 3 S TENSOR REMARK 3 S11: 0.1135 S12: 0.2041 S13: -0.4749 REMARK 3 S21: -0.1797 S22: 0.0011 S23: 0.2137 REMARK 3 S31: 0.6590 S32: -0.1045 S33: -0.1146 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 32 H 122 REMARK 3 ORIGIN FOR THE GROUP (A): 93.5980 43.8570 41.0650 REMARK 3 T TENSOR REMARK 3 T11: -0.1500 T22: -0.0201 REMARK 3 T33: -0.0549 T12: -0.0551 REMARK 3 T13: -0.0069 T23: 0.0745 REMARK 3 L TENSOR REMARK 3 L11: 2.5888 L22: 0.5146 REMARK 3 L33: 2.9964 L12: -0.2564 REMARK 3 L13: 0.8972 L23: -0.7348 REMARK 3 S TENSOR REMARK 3 S11: -0.0770 S12: 0.0424 S13: 0.0811 REMARK 3 S21: -0.0244 S22: 0.0011 S23: 0.0408 REMARK 3 S31: 0.1133 S32: -0.1712 S33: 0.0759 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 123 H 185 REMARK 3 ORIGIN FOR THE GROUP (A): 91.7810 46.9000 5.7420 REMARK 3 T TENSOR REMARK 3 T11: -0.1853 T22: -0.1288 REMARK 3 T33: -0.1833 T12: 0.0971 REMARK 3 T13: -0.0786 T23: 0.0153 REMARK 3 L TENSOR REMARK 3 L11: 5.6097 L22: 2.1076 REMARK 3 L33: 10.5564 L12: -0.0641 REMARK 3 L13: -1.3610 L23: -0.1894 REMARK 3 S TENSOR REMARK 3 S11: 0.2233 S12: 0.0699 S13: -0.2752 REMARK 3 S21: -0.2555 S22: -0.0670 S23: 0.0416 REMARK 3 S31: 0.7554 S32: -0.1287 S33: -0.1563 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 186 H 221 REMARK 3 ORIGIN FOR THE GROUP (A): 90.7430 42.4610 -2.8470 REMARK 3 T TENSOR REMARK 3 T11: 0.1559 T22: -0.0254 REMARK 3 T33: -0.1917 T12: 0.1211 REMARK 3 T13: -0.1144 T23: -0.1121 REMARK 3 L TENSOR REMARK 3 L11: 6.3754 L22: 2.3729 REMARK 3 L33: 9.1575 L12: -0.2426 REMARK 3 L13: -3.2760 L23: 1.4832 REMARK 3 S TENSOR REMARK 3 S11: -0.0017 S12: 0.4591 S13: -0.8232 REMARK 3 S21: -0.9248 S22: -0.2149 S23: 0.1839 REMARK 3 S31: 1.3992 S32: 0.0136 S33: 0.2166 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 : L 1 L 104 REMARK 3 ORIGIN FOR THE GROUP (A): 112.9200 45.4330 35.3160 REMARK 3 T TENSOR REMARK 3 T11: -0.1527 T22: -0.0198 REMARK 3 T33: -0.0507 T12: 0.0129 REMARK 3 T13: -0.0032 T23: 0.1030 REMARK 3 L TENSOR REMARK 3 L11: 2.8916 L22: 0.8321 REMARK 3 L33: 3.1132 L12: 0.4356 REMARK 3 L13: -0.6627 L23: -0.2977 REMARK 3 S TENSOR REMARK 3 S11: 0.0485 S12: 0.3396 S13: 0.0734 REMARK 3 S21: -0.1143 S22: 0.0269 S23: -0.0932 REMARK 3 S31: 0.1940 S32: -0.0075 S33: -0.0753 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 : L 105 L 160 REMARK 3 ORIGIN FOR THE GROUP (A): 99.5950 57.8730 5.3460 REMARK 3 T TENSOR REMARK 3 T11: -0.2398 T22: 0.1780 REMARK 3 T33: -0.2300 T12: 0.0632 REMARK 3 T13: 0.0286 T23: 0.0310 REMARK 3 L TENSOR REMARK 3 L11: 4.8024 L22: 4.6700 REMARK 3 L33: 4.5960 L12: -3.8360 REMARK 3 L13: 3.5112 L23: -3.0959 REMARK 3 S TENSOR REMARK 3 S11: 0.1552 S12: 0.1478 S13: 0.3314 REMARK 3 S21: -0.1327 S22: -0.2888 S23: -0.2126 REMARK 3 S31: 0.2817 S32: 0.4145 S33: 0.1335 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 161 L 192 REMARK 3 ORIGIN FOR THE GROUP (A): 95.9170 57.1970 5.4750 REMARK 3 T TENSOR REMARK 3 T11: -0.2553 T22: 0.0716 REMARK 3 T33: -0.2129 T12: 0.0159 REMARK 3 T13: -0.0046 T23: 0.0069 REMARK 3 L TENSOR REMARK 3 L11: 7.1771 L22: 4.3622 REMARK 3 L33: 4.8740 L12: -4.0231 REMARK 3 L13: 3.0620 L23: -2.4983 REMARK 3 S TENSOR REMARK 3 S11: 0.0387 S12: 0.0186 S13: -0.2004 REMARK 3 S21: -0.1131 S22: 0.0112 S23: 0.1335 REMARK 3 S31: 0.0200 S32: 0.1143 S33: -0.0499 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 193 L 214 REMARK 3 ORIGIN FOR THE GROUP (A): 102.6440 62.6170 -1.3920 REMARK 3 T TENSOR REMARK 3 T11: -0.1754 T22: 0.2033 REMARK 3 T33: -0.1359 T12: 0.1658 REMARK 3 T13: 0.0558 T23: 0.1594 REMARK 3 L TENSOR REMARK 3 L11: 13.4686 L22: 4.4340 REMARK 3 L33: 9.1253 L12: -5.5279 REMARK 3 L13: 7.4256 L23: -5.0830 REMARK 3 S TENSOR REMARK 3 S11: 0.4608 S12: 1.3891 S13: -0.0285 REMARK 3 S21: -0.4251 S22: -0.6294 S23: -0.4311 REMARK 3 S31: -0.0613 S32: 1.0102 S33: 0.1686 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE REMARK 3 RIDING POSITIONS. REMARK 4 REMARK 4 2VDQ 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-34087. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 28-FEB-05 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 : 416764 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.60 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 (%) : 98.5 REMARK 200 DATA REDUNDANCY : 6 REMARK 200 R MERGE (I) : 0.08 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 19.10 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70 REMARK 200 COMPLETENESS FOR SHELL (%) : 87.4 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.43 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.20 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: 11580 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 71880 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.3 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 400 REMARK 400 COMPOUND REMARK 400 ENGINEERED RESIDUE IN CHAIN C, ALA 396 TO ARG 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 HIS C 400 REMARK 465 HIS C 401 REMARK 465 LEU C 402 REMARK 465 GLY C 403 REMARK 465 GLY C 404 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 A 4142 O HOH A 4314 2.18 REMARK 500 O HOH B 4165 O HOH A 4278 1.88 REMARK 500 O HOH L 4014 O HOH H 4078 2.11 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 -125.76 49.72 REMARK 500 LYS A 118 -123.27 51.84 REMARK 500 GLU A 123 135.55 99.31 REMARK 500 LEU A 212 -46.13 72.93 REMARK 500 THR A 296 140.06 -170.58 REMARK 500 PRO A 337 44.63 -83.60 REMARK 500 THR B 7 35.71 -97.31 REMARK 500 PHE B 56 81.80 -156.64 REMARK 500 ASP B 71 -159.68 -122.94 REMARK 500 VAL B 80 104.38 68.02 REMARK 500 VAL B 157 -83.91 -124.12 REMARK 500 SER B 213 -154.40 -110.90 REMARK 500 LEU B 258 -15.36 88.12 REMARK 500 VAL B 275 -86.25 -88.22 REMARK 500 LYS B 410 -27.77 71.05 REMARK 500 HIS B 446 -60.00 70.22 REMARK 500 THR B 454 154.18 68.38 REMARK 500 VAL H 133 -156.65 -76.82 REMARK 500 ASP H 179 -12.92 77.12 REMARK 500 SER L 30 57.58 28.03 REMARK 500 SER L 77 79.43 67.13 REMARK 500 ASN L 212 80.57 50.95 REMARK 500 GLU L 213 90.84 -164.37 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 51.3 REMARK 620 3 ASP A 245 OD2 121.5 70.9 REMARK 620 4 ASP A 247 O 76.2 78.1 84.5 REMARK 620 5 THR A 250 C 92.6 143.1 141.0 86.3 REMARK 620 6 THR A 250 O 72.0 122.5 156.5 80.4 20.7 REMARK 620 7 THR A 250 OG1 137.9 137.4 79.1 69.4 62.2 78.8 REMARK 620 8 GLU A 252 OE1 89.9 79.0 87.4 157.1 112.9 113.0 129.9 REMARK 620 9 GLU A 252 OE2 132.9 129.3 88.8 147.4 79.1 94.3 78.0 53.4 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 78.5 REMARK 620 3 ASP A 297 OD1 82.3 78.4 REMARK 620 4 ARG A 303 O 160.1 89.5 79.8 REMARK 620 5 ASP A 305 OD1 117.3 148.0 128.8 81.0 REMARK 620 6 ASP A 305 OD2 90.9 161.5 85.2 96.1 50.5 REMARK 620 7 HOH A4359 O 94.5 83.1 161.5 99.8 68.8 113.1 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 79.3 REMARK 620 3 TYR A 371 O 73.2 81.7 REMARK 620 4 ASP A 367 OD1 90.9 92.5 163.8 REMARK 620 5 HOH A4391 O 145.5 69.4 88.0 104.2 REMARK 620 6 ASP A 373 OD1 94.7 173.9 97.5 86.5 116.6 REMARK 620 7 ASP A 373 OD2 130.8 135.8 79.1 114.7 70.4 49.5 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 89.7 REMARK 620 3 ASP A 426 OD1 80.3 89.2 REMARK 620 4 ASP A 428 OD1 158.0 92.4 77.9 REMARK 620 5 ASP A 434 OD1 98.3 170.9 87.9 78.6 REMARK 620 6 ASP A 434 OD2 82.3 136.7 130.5 110.4 49.6 REMARK 620 7 HOH A4436 O 130.8 86.2 148.5 71.2 91.7 68.3 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 27.9 REMARK 620 3 HOH C4013 O 101.0 79.5 REMARK 620 4 ASP B 251 OD2 105.4 127.2 101.0 REMARK 620 5 GOL B1462 O1 48.9 58.2 75.0 70.8 REMARK 620 6 SER B 123 O 177.6 150.0 78.2 77.0 132.6 REMARK 620 7 ASP B 126 OD1 106.5 86.6 83.5 146.2 141.2 71.2 REMARK 620 8 ASP B 127 OD1 82.1 99.8 168.8 88.4 114.3 98.3 85.3 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 158 OD2 REMARK 620 2 ASN B 215 OD1 98.2 REMARK 620 3 ASP B 217 O 165.7 92.4 REMARK 620 4 ASP B 217 OD1 92.5 96.1 76.7 REMARK 620 5 PRO B 219 O 83.9 166.3 88.2 97.3 REMARK 620 6 GLU B 220 OE2 101.9 79.7 89.4 165.4 86.6 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 B4148 O REMARK 620 2 SER B 123 OG 94.7 REMARK 620 3 GLU B 220 OE1 88.2 175.4 REMARK 620 4 HOH B4057 O 94.3 83.2 100.2 REMARK 620 5 ASP C 410 OD1 95.1 86.1 90.1 166.3 REMARK 620 6 SER B 121 OG 172.4 90.6 86.8 81.0 90.6 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: 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. THERE IS A A408R MUTATION 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