REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0019 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) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 94.4 REMARK 3 NUMBER OF REFLECTIONS : 43686 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) : 0.219 REMARK 3 R VALUE (WORKING SET) : 0.216 REMARK 3 FREE R VALUE : 0.271 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2278 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) : 2.48 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2586 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 76.94 REMARK 3 BIN R VALUE (WORKING SET) : 0.3180 REMARK 3 BIN FREE R VALUE SET COUNT : 127 REMARK 3 BIN FREE R VALUE : 0.4720 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 8770 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 43 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.43 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.91000 REMARK 3 B22 (A**2) : -3.52000 REMARK 3 B33 (A**2) : 5.43000 REMARK 3 B12 (A**2) : 0.00000 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): 0.569 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.314 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.239 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.240 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.895 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8992 ; 0.016 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 6023 ; 0.002 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12215 ; 1.587 ; 1.948 REMARK 3 BOND ANGLES OTHERS (DEGREES): 14669 ; 0.929 ; 3.003 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1133 ;13.475 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 375 ;33.536 ;24.133 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1435 ;17.229 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;16.152 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1344 ; 0.091 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10055 ; 0.007 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1821 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1460 ; 0.201 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5737 ; 0.203 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4204 ; 0.188 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 5031 ; 0.090 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 179 ; 0.152 ; 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 ; 0.163 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 41 ; 0.257 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 7 ; 0.102 ; 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): 7186 ; 0.841 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2320 ; 0.136 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9146 ; 1.050 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3978 ; 1.729 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3069 ; 2.454 ; 4.500 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 : 24 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 : E 1 E 35 REMARK 3 ORIGIN FOR THE GROUP (A): 60.7360 11.6470 137.4760 REMARK 3 T TENSOR REMARK 3 T11: 0.2461 T22: 0.1869 REMARK 3 T33: 0.0632 T12: 0.0292 REMARK 3 T13: 0.0443 T23: -0.0889 REMARK 3 L TENSOR REMARK 3 L11: 4.8279 L22: 2.8729 REMARK 3 L33: 6.1137 L12: -1.6516 REMARK 3 L13: 1.7120 L23: 0.0237 REMARK 3 S TENSOR REMARK 3 S11: 0.1496 S12: 1.1455 S13: 0.2440 REMARK 3 S21: -0.5273 S22: 0.0481 S23: 0.0033 REMARK 3 S31: -0.0696 S32: 0.0315 S33: -0.1976 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 : E 36 E 91 REMARK 3 ORIGIN FOR THE GROUP (A): 56.7290 17.5080 142.5250 REMARK 3 T TENSOR REMARK 3 T11: 0.1235 T22: 0.1087 REMARK 3 T33: -0.0466 T12: -0.0261 REMARK 3 T13: -0.0048 T23: -0.0349 REMARK 3 L TENSOR REMARK 3 L11: 3.8989 L22: 3.3714 REMARK 3 L33: 1.9101 L12: -0.9760 REMARK 3 L13: 1.3769 L23: -0.2181 REMARK 3 S TENSOR REMARK 3 S11: -0.0506 S12: -0.0042 S13: 0.0266 REMARK 3 S21: -0.1432 S22: 0.0417 S23: 0.0872 REMARK 3 S31: -0.1281 S32: 0.1050 S33: 0.0088 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 : E 92 E 125 REMARK 3 ORIGIN FOR THE GROUP (A): 59.9650 13.6700 151.3610 REMARK 3 T TENSOR REMARK 3 T11: 0.0802 T22: 0.1583 REMARK 3 T33: -0.0859 T12: -0.0719 REMARK 3 T13: -0.0106 T23: -0.0340 REMARK 3 L TENSOR REMARK 3 L11: 6.1074 L22: 9.4375 REMARK 3 L33: 2.8976 L12: -4.6498 REMARK 3 L13: 1.5395 L23: -0.9720 REMARK 3 S TENSOR REMARK 3 S11: -0.0312 S12: -0.3246 S13: -0.0270 REMARK 3 S21: 0.6154 S22: 0.1605 S23: 0.2719 REMARK 3 S31: 0.0261 S32: -0.1295 S33: -0.1294 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 : E 126 E 134 REMARK 3 ORIGIN FOR THE GROUP (A): 47.2900 30.3610 132.7160 REMARK 3 T TENSOR REMARK 3 T11: 0.2317 T22: 0.2673 REMARK 3 T33: 0.2363 T12: 0.0235 REMARK 3 T13: -0.0633 T23: 0.0580 REMARK 3 L TENSOR REMARK 3 L11: 2.3185 L22: 11.9229 REMARK 3 L33: 1.4382 L12: 3.0218 REMARK 3 L13: -1.8142 L23: -1.9803 REMARK 3 S TENSOR REMARK 3 S11: -0.3013 S12: 0.8417 S13: 1.4439 REMARK 3 S21: -0.3144 S22: -0.0317 S23: 0.7180 REMARK 3 S31: -0.5668 S32: -0.2991 S33: 0.3330 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 : E 135 E 176 REMARK 3 ORIGIN FOR THE GROUP (A): 64.3580 17.9580 143.7930 REMARK 3 T TENSOR REMARK 3 T11: 0.1114 T22: 0.1422 REMARK 3 T33: 0.0176 T12: -0.0563 REMARK 3 T13: -0.0001 T23: -0.0294 REMARK 3 L TENSOR REMARK 3 L11: 5.2905 L22: 3.7403 REMARK 3 L33: 2.4332 L12: -1.7912 REMARK 3 L13: -0.1403 L23: -0.2503 REMARK 3 S TENSOR REMARK 3 S11: -0.0002 S12: 0.3927 S13: 0.4257 REMARK 3 S21: -0.0594 S22: -0.1049 S23: -0.5136 REMARK 3 S31: -0.2046 S32: 0.2554 S33: 0.1051 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 : F 28 F 43 REMARK 3 ORIGIN FOR THE GROUP (A): 53.2010 41.7270 86.3340 REMARK 3 T TENSOR REMARK 3 T11: 0.2690 T22: 0.3218 REMARK 3 T33: 0.3109 T12: -0.0562 REMARK 3 T13: -0.2608 T23: 0.1294 REMARK 3 L TENSOR REMARK 3 L11: 4.2053 L22: 12.1161 REMARK 3 L33: 48.9931 L12: 2.6498 REMARK 3 L13: 6.0089 L23: 0.1479 REMARK 3 S TENSOR REMARK 3 S11: -1.0809 S12: 0.1440 S13: 1.1950 REMARK 3 S21: -0.2504 S22: 0.1981 S23: 1.0357 REMARK 3 S31: 0.5440 S32: 0.0573 S33: 0.8827 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 : F 44 F 79 REMARK 3 ORIGIN FOR THE GROUP (A): 57.5960 37.9120 72.1550 REMARK 3 T TENSOR REMARK 3 T11: 0.5616 T22: 0.4910 REMARK 3 T33: 0.1475 T12: -0.2353 REMARK 3 T13: -0.2279 T23: 0.1819 REMARK 3 L TENSOR REMARK 3 L11: 7.1746 L22: 5.6667 REMARK 3 L33: 12.5951 L12: -1.7569 REMARK 3 L13: 3.4678 L23: -2.0676 REMARK 3 S TENSOR REMARK 3 S11: -0.1132 S12: 0.9938 S13: 0.0622 REMARK 3 S21: -1.1059 S22: 0.0704 S23: 0.2284 REMARK 3 S31: 0.1300 S32: 0.4103 S33: 0.0428 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 : F 80 F 132 REMARK 3 ORIGIN FOR THE GROUP (A): 67.9030 36.0090 75.5610 REMARK 3 T TENSOR REMARK 3 T11: 0.5623 T22: 0.5407 REMARK 3 T33: 0.2123 T12: -0.2636 REMARK 3 T13: 0.0286 T23: 0.0800 REMARK 3 L TENSOR REMARK 3 L11: 5.8592 L22: 13.2816 REMARK 3 L33: 11.6844 L12: -0.7687 REMARK 3 L13: 1.3639 L23: -7.7083 REMARK 3 S TENSOR REMARK 3 S11: -0.7206 S12: 1.1789 S13: 0.1855 REMARK 3 S21: -1.6444 S22: -0.2397 S23: -1.0148 REMARK 3 S31: 0.0555 S32: 1.2677 S33: 0.9603 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 : F 133 F 142 REMARK 3 ORIGIN FOR THE GROUP (A): 66.0230 42.7320 84.7280 REMARK 3 T TENSOR REMARK 3 T11: 0.2987 T22: 0.3019 REMARK 3 T33: 0.3011 T12: -0.0166 REMARK 3 T13: 0.0148 T23: -0.0069 REMARK 3 L TENSOR REMARK 3 L11: 19.9572 L22: 70.4248 REMARK 3 L33: 57.7908 L12: 12.3176 REMARK 3 L13: 2.7252 L23: -37.6217 REMARK 3 S TENSOR REMARK 3 S11: -1.1885 S12: 0.7268 S13: 1.4518 REMARK 3 S21: -0.8643 S22: -0.1377 S23: -1.8602 REMARK 3 S31: -0.1759 S32: 0.5800 S33: 1.3261 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 : F 163 F 170 REMARK 3 ORIGIN FOR THE GROUP (A): 58.2840 43.8330 77.8060 REMARK 3 T TENSOR REMARK 3 T11: 0.3400 T22: 0.3791 REMARK 3 T33: 0.3100 T12: -0.1854 REMARK 3 T13: -0.0551 T23: 0.0988 REMARK 3 L TENSOR REMARK 3 L11: 2.5536 L22: 36.0368 REMARK 3 L33: 28.9216 L12: -7.4225 REMARK 3 L13: 6.8605 L23: -7.6249 REMARK 3 S TENSOR REMARK 3 S11: -0.5098 S12: 0.0117 S13: 0.7857 REMARK 3 S21: -1.2039 S22: -0.7732 S23: -0.4689 REMARK 3 S31: -0.4521 S32: -0.2490 S33: 1.2830 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 : H 1 H 213 REMARK 3 ORIGIN FOR THE GROUP (A): 15.1770 15.1610 117.3350 REMARK 3 T TENSOR REMARK 3 T11: 0.2017 T22: 0.2256 REMARK 3 T33: 0.0238 T12: 0.0003 REMARK 3 T13: -0.0236 T23: -0.0040 REMARK 3 L TENSOR REMARK 3 L11: 2.8317 L22: 0.6712 REMARK 3 L33: 0.4534 L12: 1.0757 REMARK 3 L13: 0.3612 L23: 0.1289 REMARK 3 S TENSOR REMARK 3 S11: -0.1911 S12: 0.3346 S13: 0.0156 REMARK 3 S21: -0.1090 S22: 0.1608 S23: 0.0183 REMARK 3 S31: -0.0111 S32: -0.0372 S33: 0.0304 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 : I 1 I 38 REMARK 3 ORIGIN FOR THE GROUP (A): 66.1870 13.9210 98.6230 REMARK 3 T TENSOR REMARK 3 T11: 0.3947 T22: 0.2535 REMARK 3 T33: 0.0206 T12: -0.0861 REMARK 3 T13: -0.0370 T23: -0.0650 REMARK 3 L TENSOR REMARK 3 L11: 3.9117 L22: 3.0953 REMARK 3 L33: 6.6559 L12: 0.4899 REMARK 3 L13: -1.1658 L23: -2.5548 REMARK 3 S TENSOR REMARK 3 S11: -0.2460 S12: 0.3635 S13: -0.1448 REMARK 3 S21: -0.7631 S22: -0.1909 S23: -0.2846 REMARK 3 S31: 0.3635 S32: 0.4143 S33: 0.4369 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 : I 39 I 57 REMARK 3 ORIGIN FOR THE GROUP (A): 59.1010 21.2070 100.1070 REMARK 3 T TENSOR REMARK 3 T11: 0.3647 T22: 0.2602 REMARK 3 T33: 0.3100 T12: -0.0445 REMARK 3 T13: -0.1164 T23: 0.0760 REMARK 3 L TENSOR REMARK 3 L11: 5.2462 L22: 0.7118 REMARK 3 L33: 9.2654 L12: -1.0761 REMARK 3 L13: 4.9051 L23: 0.5098 REMARK 3 S TENSOR REMARK 3 S11: 0.7907 S12: -0.6983 S13: -0.0364 REMARK 3 S21: -0.0312 S22: -0.4136 S23: 0.1605 REMARK 3 S31: -0.3762 S32: -0.2830 S33: -0.3771 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 : I 58 I 119 REMARK 3 ORIGIN FOR THE GROUP (A): 62.9860 21.1030 98.7220 REMARK 3 T TENSOR REMARK 3 T11: 0.3474 T22: 0.2201 REMARK 3 T33: -0.0187 T12: -0.0952 REMARK 3 T13: -0.0895 T23: -0.0169 REMARK 3 L TENSOR REMARK 3 L11: 1.7819 L22: 3.0930 REMARK 3 L33: 5.3316 L12: 0.3831 REMARK 3 L13: 1.2397 L23: -3.4015 REMARK 3 S TENSOR REMARK 3 S11: -0.0761 S12: 0.1152 S13: 0.0757 REMARK 3 S21: 0.0755 S22: 0.0467 S23: -0.0955 REMARK 3 S31: -0.2611 S32: 0.1795 S33: 0.0294 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 : I 120 I 213 REMARK 3 ORIGIN FOR THE GROUP (A): 48.9940 -10.6200 102.6160 REMARK 3 T TENSOR REMARK 3 T11: 0.2961 T22: 0.4384 REMARK 3 T33: 0.1895 T12: -0.0802 REMARK 3 T13: -0.0404 T23: -0.1094 REMARK 3 L TENSOR REMARK 3 L11: 3.2482 L22: 4.0066 REMARK 3 L33: 2.2465 L12: 1.9855 REMARK 3 L13: 1.5306 L23: 1.6933 REMARK 3 S TENSOR REMARK 3 S11: -0.1431 S12: 0.3629 S13: -0.4660 REMARK 3 S21: -0.3526 S22: 0.2036 S23: 0.0896 REMARK 3 S31: 0.2014 S32: 0.0052 S33: -0.0605 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 : I 215 I 221 REMARK 3 ORIGIN FOR THE GROUP (A): 53.5660 -16.9830 105.4510 REMARK 3 T TENSOR REMARK 3 T11: 0.3098 T22: 0.2980 REMARK 3 T33: 0.3106 T12: -0.0403 REMARK 3 T13: -0.0774 T23: -0.0605 REMARK 3 L TENSOR REMARK 3 L11: 18.0065 L22: 20.1332 REMARK 3 L33: 9.0447 L12: 12.3715 REMARK 3 L13: 6.5565 L23: 9.3081 REMARK 3 S TENSOR REMARK 3 S11: 0.7180 S12: -0.0527 S13: -1.8513 REMARK 3 S21: 0.3044 S22: -0.5239 S23: -0.1755 REMARK 3 S31: 1.0473 S32: 0.1177 S33: -0.1940 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 : L 1 L 84 REMARK 3 ORIGIN FOR THE GROUP (A): 33.4110 5.7390 130.3980 REMARK 3 T TENSOR REMARK 3 T11: 0.1070 T22: 0.0836 REMARK 3 T33: 0.0603 T12: -0.0068 REMARK 3 T13: 0.0040 T23: -0.0006 REMARK 3 L TENSOR REMARK 3 L11: 3.7749 L22: 2.1269 REMARK 3 L33: 2.8864 L12: 0.1224 REMARK 3 L13: -1.4067 L23: -0.5808 REMARK 3 S TENSOR REMARK 3 S11: -0.0009 S12: 0.0490 S13: -0.3892 REMARK 3 S21: -0.0883 S22: 0.0675 S23: -0.0418 REMARK 3 S31: 0.1720 S32: 0.0741 S33: -0.0667 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 : L 85 L 129 REMARK 3 ORIGIN FOR THE GROUP (A): 18.0470 1.1000 117.8310 REMARK 3 T TENSOR REMARK 3 T11: 0.2333 T22: 0.2454 REMARK 3 T33: 0.1949 T12: -0.0315 REMARK 3 T13: 0.0377 T23: -0.0766 REMARK 3 L TENSOR REMARK 3 L11: 4.4974 L22: 1.4644 REMARK 3 L33: 0.7928 L12: 1.9534 REMARK 3 L13: 1.4491 L23: 0.9138 REMARK 3 S TENSOR REMARK 3 S11: -0.2276 S12: 0.4314 S13: -0.4957 REMARK 3 S21: -0.2349 S22: 0.1588 S23: -0.0613 REMARK 3 S31: 0.0943 S32: 0.0057 S33: 0.0688 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 : L 130 L 148 REMARK 3 ORIGIN FOR THE GROUP (A): 10.2720 -9.5800 114.7300 REMARK 3 T TENSOR REMARK 3 T11: 0.4004 T22: 0.3486 REMARK 3 T33: 0.4841 T12: -0.0544 REMARK 3 T13: 0.2164 T23: -0.0411 REMARK 3 L TENSOR REMARK 3 L11: 3.8042 L22: 1.2151 REMARK 3 L33: 8.6477 L12: 1.9399 REMARK 3 L13: 1.8846 L23: 2.2810 REMARK 3 S TENSOR REMARK 3 S11: -0.1296 S12: 0.6301 S13: -1.1318 REMARK 3 S21: 0.0632 S22: 0.2670 S23: -0.7371 REMARK 3 S31: 0.2314 S32: 0.8993 S33: -0.1374 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 : L 149 L 214 REMARK 3 ORIGIN FOR THE GROUP (A): 6.2650 -10.8490 108.6290 REMARK 3 T TENSOR REMARK 3 T11: 0.3083 T22: 0.3802 REMARK 3 T33: 0.4096 T12: -0.0896 REMARK 3 T13: 0.1680 T23: -0.2095 REMARK 3 L TENSOR REMARK 3 L11: 3.9086 L22: 3.8997 REMARK 3 L33: 5.9853 L12: 0.2870 REMARK 3 L13: 2.9181 L23: 0.5320 REMARK 3 S TENSOR REMARK 3 S11: -0.0707 S12: 0.5405 S13: -0.7215 REMARK 3 S21: -0.7218 S22: 0.1386 S23: -0.2483 REMARK 3 S31: 0.3943 S32: -0.1277 S33: -0.0680 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 : M 1 M 84 REMARK 3 ORIGIN FOR THE GROUP (A): 45.4500 19.5600 85.6270 REMARK 3 T TENSOR REMARK 3 T11: 0.4056 T22: 0.3517 REMARK 3 T33: -0.0083 T12: -0.2294 REMARK 3 T13: -0.1566 T23: 0.0472 REMARK 3 L TENSOR REMARK 3 L11: 4.4030 L22: 7.3457 REMARK 3 L33: 3.2367 L12: 2.3695 REMARK 3 L13: 1.7120 L23: -0.4898 REMARK 3 S TENSOR REMARK 3 S11: -0.2870 S12: 0.0629 S13: 0.0068 REMARK 3 S21: -0.6827 S22: 0.4657 S23: 0.5213 REMARK 3 S31: 0.2628 S32: -0.4920 S33: -0.1787 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 : M 85 M 121 REMARK 3 ORIGIN FOR THE GROUP (A): 42.2930 8.4840 94.3620 REMARK 3 T TENSOR REMARK 3 T11: 0.3380 T22: 0.4064 REMARK 3 T33: 0.2067 T12: -0.1586 REMARK 3 T13: -0.1697 T23: 0.0364 REMARK 3 L TENSOR REMARK 3 L11: 0.4172 L22: 5.2942 REMARK 3 L33: 1.3423 L12: 1.4042 REMARK 3 L13: -0.7352 L23: -2.3117 REMARK 3 S TENSOR REMARK 3 S11: -0.1184 S12: 0.1633 S13: -0.1077 REMARK 3 S21: -0.2313 S22: 0.4291 S23: 0.3056 REMARK 3 S31: 0.0683 S32: -0.3173 S33: -0.3107 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 : M 122 M 193 REMARK 3 ORIGIN FOR THE GROUP (A): 35.0190 -9.5630 106.4620 REMARK 3 T TENSOR REMARK 3 T11: 0.1921 T22: 0.3246 REMARK 3 T33: 0.2884 T12: -0.0751 REMARK 3 T13: -0.1017 T23: -0.0102 REMARK 3 L TENSOR REMARK 3 L11: 3.4428 L22: 5.5953 REMARK 3 L33: 7.9764 L12: 2.6796 REMARK 3 L13: -0.3816 L23: -2.4798 REMARK 3 S TENSOR REMARK 3 S11: -0.0765 S12: -0.0210 S13: 0.0145 REMARK 3 S21: -0.0054 S22: 0.0455 S23: 0.4501 REMARK 3 S31: -0.1156 S32: 0.0760 S33: 0.0310 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 : M 194 M 214 REMARK 3 ORIGIN FOR THE GROUP (A): 26.7350 -14.2500 102.6430 REMARK 3 T TENSOR REMARK 3 T11: 0.3629 T22: 0.3762 REMARK 3 T33: 0.3479 T12: -0.0921 REMARK 3 T13: -0.0329 T23: -0.0242 REMARK 3 L TENSOR REMARK 3 L11: 5.0484 L22: 13.8817 REMARK 3 L33: 16.2120 L12: 1.7441 REMARK 3 L13: 3.0023 L23: -9.0886 REMARK 3 S TENSOR REMARK 3 S11: 0.1776 S12: 0.3418 S13: -0.3618 REMARK 3 S21: -0.6691 S22: 0.0862 S23: 1.1217 REMARK 3 S31: 0.6973 S32: 0.1329 S33: -0.2638 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 RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3SKJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUL-11. REMARK 100 THE RCSB ID CODE IS RCSB066315. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-NOV-09 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 31-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793 REMARK 200 MONOCHROMATOR : CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60701 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 90.0 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASES REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 48.49 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 0.1 M SODIUM ACETATE, REMARK 280 0.2 M AMMONIUM ACETATE, PH 5.0, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z 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 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 143.11900 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 143.11900 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 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 39.47000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 60.42950 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 39.47000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 60.42950 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 143.11900 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 39.47000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 60.42950 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 143.11900 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 39.47000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 60.42950 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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 300 REMARK: TWO BIOLOGICAL ENSEMBLES ARE PRESENTED IN THE ASYMMETRIC REMARK 300 UNIT. 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5660 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 28080 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6030 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 24570 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, I, M 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 SER H 129A REMARK 465 THR H 129B REMARK 465 SER H 129C REMARK 465 LYS I 128A REMARK 465 SER I 128B REMARK 465 THR I 128C REMARK 465 ALA E -27 REMARK 465 PRO E -26 REMARK 465 GLU E -25 REMARK 465 HIS E -24 REMARK 465 HIS E -23 REMARK 465 HIS E -22 REMARK 465 HIS E -21 REMARK 465 HIS E -20 REMARK 465 HIS E -19 REMARK 465 ASP E -18 REMARK 465 TYR E -17 REMARK 465 ASP E -16 REMARK 465 ILE E -15 REMARK 465 PRO E -14 REMARK 465 THR E -13 REMARK 465 THR E -12 REMARK 465 GLU E -11 REMARK 465 ASN E -10 REMARK 465 LEU E -9 REMARK 465 TYR E -8 REMARK 465 PHE E -7 REMARK 465 GLN E -6 REMARK 465 GLY E -5 REMARK 465 ALA E -4 REMARK 465 MET E -3 REMARK 465 ASP E -2 REMARK 465 ALA E -1 REMARK 465 ALA E 0 REMARK 465 CYS E 177 REMARK 465 PRO E 178 REMARK 465 ALA F -27 REMARK 465 PRO F -26 REMARK 465 GLU F -25 REMARK 465 HIS F -24 REMARK 465 HIS F -23 REMARK 465 HIS F -22 REMARK 465 HIS F -21 REMARK 465 HIS F -20 REMARK 465 HIS F -19 REMARK 465 ASP F -18 REMARK 465 TYR F -17 REMARK 465 ASP F -16 REMARK 465 ILE F -15 REMARK 465 PRO F -14 REMARK 465 THR F -13 REMARK 465 THR F -12 REMARK 465 GLU F -11 REMARK 465 ASN F -10 REMARK 465 LEU F -9 REMARK 465 TYR F -8 REMARK 465 PHE F -7 REMARK 465 GLN F -6 REMARK 465 GLY F -5 REMARK 465 ALA F -4 REMARK 465 MET F -3 REMARK 465 ASP F -2 REMARK 465 ALA F -1 REMARK 465 ALA F 0 REMARK 465 GLN F 1 REMARK 465 GLY F 2 REMARK 465 LYS F 3 REMARK 465 GLU F 4 REMARK 465 VAL F 5 REMARK 465 VAL F 6 REMARK 465 LEU F 7 REMARK 465 LEU F 8 REMARK 465 ASP F 9 REMARK 465 PHE F 10 REMARK 465 ALA F 11 REMARK 465 ALA F 12 REMARK 465 ALA F 13 REMARK 465 GLY F 14 REMARK 465 GLY F 15 REMARK 465 GLU F 16 REMARK 465 LEU F 17 REMARK 465 GLY F 18 REMARK 465 TRP F 19 REMARK 465 LEU F 20 REMARK 465 THR F 21 REMARK 465 HIS F 22 REMARK 465 PRO F 23 REMARK 465 TYR F 24 REMARK 465 GLY F 25 REMARK 465 LYS F 26 REMARK 465 GLY F 27 REMARK 465 THR F 59 REMARK 465 ASN F 60 REMARK 465 TRP F 61 REMARK 465 VAL F 62 REMARK 465 TYR F 63 REMARK 465 ARG F 64 REMARK 465 GLY F 65 REMARK 465 GLU F 66 REMARK 465 ALA F 67 REMARK 465 GLU F 68 REMARK 465 ARG F 69 REMARK 465 ILE F 70 REMARK 465 PHE F 71 REMARK 465 ILE F 72 REMARK 465 GLU F 73 REMARK 465 LEU F 97 REMARK 465 TYR F 98 REMARK 465 TYR F 99 REMARK 465 ALA F 100 REMARK 465 GLU F 101 REMARK 465 SER F 102 REMARK 465 ASP F 103 REMARK 465 LEU F 104 REMARK 465 ASP F 105 REMARK 465 TYR F 106 REMARK 465 GLY F 107 REMARK 465 THR F 108 REMARK 465 ASN F 109 REMARK 465 PHE F 110 REMARK 465 GLN F 111 REMARK 465 LYS F 112 REMARK 465 ARG F 113 REMARK 465 LEU F 114 REMARK 465 PHE F 115 REMARK 465 THR F 116 REMARK 465 LYS F 117 REMARK 465 ILE F 118 REMARK 465 ASP F 119 REMARK 465 THR F 120 REMARK 465 GLU F 143 REMARK 465 ARG F 144 REMARK 465 SER F 145 REMARK 465 VAL F 146 REMARK 465 GLY F 147 REMARK 465 PRO F 148 REMARK 465 LEU F 149 REMARK 465 THR F 150 REMARK 465 ARG F 151 REMARK 465 LYS F 152 REMARK 465 GLY F 153 REMARK 465 PHE F 154 REMARK 465 TYR F 155 REMARK 465 LEU F 156 REMARK 465 ALA F 157 REMARK 465 PHE F 158 REMARK 465 GLN F 159 REMARK 465 ASP F 160 REMARK 465 ILE F 161 REMARK 465 GLY F 162 REMARK 465 ARG F 171 REMARK 465 VAL F 172 REMARK 465 TYR F 173 REMARK 465 TYR F 174 REMARK 465 LYS F 175 REMARK 465 LYS F 176 REMARK 465 CYS F 177 REMARK 465 PRO F 178 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 CYS L 23 CB CYS L 23 SG -0.103 REMARK 500 CYS L 194 CB CYS L 194 SG -0.101 REMARK 500 PRO H 100G CD PRO H 100G N 0.254 REMARK 500 CYS I 213 C CYS I 213 OXT 0.150 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ASP L 81 CB - CG - OD1 ANGL. DEV. = -5.4 DEGREES REMARK 500 PRO H 100G N - CA - CB ANGL. DEV. = 9.3 DEGREES REMARK 500 PRO H 100G C - N - CA ANGL. DEV. = 13.0 DEGREES REMARK 500 PRO H 100G C - N - CD ANGL. DEV. = -13.9 DEGREES REMARK 500 LEU H 135 CA - CB - CG ANGL. DEV. = 15.6 DEGREES REMARK 500 ARG M 24 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES 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 L 30 -143.21 46.11 REMARK 500 SER L 52 -7.94 169.10 REMARK 500 SER L 127 -4.44 -56.06 REMARK 500 ASN L 138 74.31 40.01 REMARK 500 TYR L 140 -156.85 -90.52 REMARK 500 PRO L 141 133.29 -8.41 REMARK 500 LYS L 169 -70.98 -77.50 REMARK 500 LYS L 190 -64.52 -123.41 REMARK 500 SER H 82B 58.51 36.77 REMARK 500 PRO H 126 -158.83 -91.08 REMARK 500 SER H 127 -65.20 -131.21 REMARK 500 SER H 128 84.65 155.77 REMARK 500 ASP H 141 61.56 67.36 REMARK 500 GLU H 145 179.43 -50.72 REMARK 500 THR H 188 -44.67 -130.02 REMARK 500 ILE M 2 94.28 65.46 REMARK 500 PRO M 8 174.53 -46.75 REMARK 500 SER M 30 -136.67 58.82 REMARK 500 ALA M 51 -1.63 70.28 REMARK 500 SER M 52 -9.31 -162.63 REMARK 500 ARG M 61 -8.85 -59.79 REMARK 500 ASN M 138 60.31 60.78 REMARK 500 TYR M 140 111.51 -162.46 REMARK 500 PRO M 141 -169.96 -108.50 REMARK 500 LYS M 190 -64.45 -92.92 REMARK 500 VAL I 48 -59.30 -120.35 REMARK 500 ALA I 88 163.93 175.13 REMARK 500 ALA I 100H -160.50 -111.13 REMARK 500 SER I 127 136.05 161.61 REMARK 500 ASP I 141 62.86 61.90 REMARK 500 PRO I 144 177.56 -58.31 REMARK 500 GLU I 145 172.78 -54.46 REMARK 500 THR I 157 -32.72 -133.30 REMARK 500 SER I 212 102.75 -37.71 REMARK 500 PRO E 23 136.31 -27.94 REMARK 500 CYS E 46 48.23 -144.45 REMARK 500 ASP F 37 -1.51 66.14 REMARK 500 MET F 42 130.70 -170.85 REMARK 500 CYS F 46 59.84 -159.17 REMARK 500 SER F 50 -83.62 -72.15 REMARK 500 ASP F 54 75.83 -155.56 REMARK 500 ALA F 88 -50.62 -29.20 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 SER L 7 PRO L 8 -40.05 REMARK 500 TYR L 140 PRO L 141 -123.03 REMARK 500 PHE H 143 PRO H 144 -46.74 REMARK 500 GLU H 145 PRO H 146 -49.76 REMARK 500 SER M 7 PRO M 8 -50.25 REMARK 500 TYR M 140 PRO M 141 54.37 REMARK 500 SER I 53 GLY I 54 -149.99 REMARK 500 PHE I 143 PRO I 144 -41.05 REMARK 500 GLU I 145 PRO I 146 -38.98 REMARK 500 HIS E 22 PRO E 23 -50.43 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 SER L 7 -11.08 REMARK 500 PHE H 143 -10.41 REMARK 500 GLU H 145 -11.47 REMARK 500 PHE I 143 -10.91 REMARK 500 GLU I 145 -10.58 REMARK 500 REMARK 500 REMARK: NULL