REMARK 2 REMARK 2 RESOLUTION. 2.80 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) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.67 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0 REMARK 3 NUMBER OF REFLECTIONS : 55400 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) : 0.194 REMARK 3 R VALUE (WORKING SET) : 0.192 REMARK 3 FREE R VALUE : 0.239 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 2813 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) : 2.80 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3811 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.69 REMARK 3 BIN R VALUE (WORKING SET) : 0.2780 REMARK 3 BIN FREE R VALUE SET COUNT : 200 REMARK 3 BIN FREE R VALUE : 0.3000 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 9740 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 44 REMARK 3 SOLVENT ATOMS : 264 REMARK 3 REMARK 3 B VALUES. REMARK 3 B VALUE TYPE : LIKELY RESIDUAL REMARK 3 FROM WILSON PLOT (A**2) : 57.73 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.77 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.12000 REMARK 3 B22 (A**2) : -0.12000 REMARK 3 B33 (A**2) : 0.18000 REMARK 3 B12 (A**2) : -0.06000 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): 0.499 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.301 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.235 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.406 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.908 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9880 ; 0.008 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 6575 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13377 ; 1.063 ; 1.959 REMARK 3 BOND ANGLES OTHERS (DEGREES): 16023 ; 0.795 ; 3.001 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1251 ; 5.581 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 444 ;38.344 ;24.324 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1730 ;14.370 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 88 ;16.752 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1582 ; 0.062 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10953 ; 0.003 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1899 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1823 ; 0.203 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 6558 ; 0.188 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4704 ; 0.172 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 5585 ; 0.081 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 263 ; 0.152 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.003 ; 0.200 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): 19 ; 0.204 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 61 ; 0.193 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.210 ; 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): 8133 ; 0.430 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2587 ; 0.053 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10151 ; 0.479 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4077 ; 0.752 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3226 ; 1.189 ; 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 : 2 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : A C E G REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 5 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 8 A 35 4 REMARK 3 1 C 8 C 35 4 REMARK 3 1 E 8 E 35 4 REMARK 3 1 G 8 G 35 4 REMARK 3 2 A 42 A 71 4 REMARK 3 2 C 42 C 71 4 REMARK 3 2 E 42 E 71 4 REMARK 3 2 G 42 G 71 4 REMARK 3 3 A 79 A 82 4 REMARK 3 3 C 79 C 82 4 REMARK 3 3 E 79 E 82 4 REMARK 3 3 G 79 G 82 4 REMARK 3 4 A 104 A 130 4 REMARK 3 4 C 104 C 130 4 REMARK 3 4 E 104 E 130 4 REMARK 3 4 G 104 G 130 4 REMARK 3 5 A 137 A 172 4 REMARK 3 5 C 137 C 172 4 REMARK 3 5 E 137 E 172 4 REMARK 3 5 G 137 G 172 4 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 1 A (A): 1572 ; 0.240 ; 0.500 REMARK 3 MEDIUM POSITIONAL 1 C (A): 1572 ; 0.250 ; 0.500 REMARK 3 MEDIUM POSITIONAL 1 E (A): 1572 ; 0.220 ; 0.500 REMARK 3 MEDIUM POSITIONAL 1 G (A): 1572 ; 0.220 ; 0.500 REMARK 3 MEDIUM THERMAL 1 A (A**2): 1572 ; 0.190 ; 2.000 REMARK 3 MEDIUM THERMAL 1 C (A**2): 1572 ; 0.220 ; 2.000 REMARK 3 MEDIUM THERMAL 1 E (A**2): 1572 ; 0.240 ; 2.000 REMARK 3 MEDIUM THERMAL 1 G (A**2): 1572 ; 0.210 ; 2.000 REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : B D F H REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 B 1 B 120 4 REMARK 3 1 D 1 D 120 4 REMARK 3 1 F 1 F 120 4 REMARK 3 1 H 1 H 120 4 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 MEDIUM POSITIONAL 2 B (A): 1512 ; 0.230 ; 0.500 REMARK 3 MEDIUM POSITIONAL 2 D (A): 1512 ; 0.300 ; 0.500 REMARK 3 MEDIUM POSITIONAL 2 F (A): 1512 ; 0.220 ; 0.500 REMARK 3 MEDIUM POSITIONAL 2 H (A): 1512 ; 0.220 ; 0.500 REMARK 3 MEDIUM THERMAL 2 B (A**2): 1512 ; 0.200 ; 2.000 REMARK 3 MEDIUM THERMAL 2 D (A**2): 1512 ; 0.210 ; 2.000 REMARK 3 MEDIUM THERMAL 2 F (A**2): 1512 ; 0.190 ; 2.000 REMARK 3 MEDIUM THERMAL 2 H (A**2): 1512 ; 0.210 ; 2.000 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 20 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 4 A 47 REMARK 3 ORIGIN FOR THE GROUP (A): 56.4420 -26.8220 28.6060 REMARK 3 T TENSOR REMARK 3 T11: -0.0993 T22: -0.1477 REMARK 3 T33: -0.0632 T12: 0.0007 REMARK 3 T13: -0.1190 T23: -0.0218 REMARK 3 L TENSOR REMARK 3 L11: 3.5520 L22: 11.5820 REMARK 3 L33: 4.7011 L12: -1.7862 REMARK 3 L13: -0.9947 L23: 2.3625 REMARK 3 S TENSOR REMARK 3 S11: -0.0837 S12: -0.4423 S13: -0.5741 REMARK 3 S21: 0.4345 S22: 0.4945 S23: -0.6341 REMARK 3 S31: 0.2650 S32: 0.6674 S33: -0.4108 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 48 A 153 REMARK 3 ORIGIN FOR THE GROUP (A): 48.0090 -24.6380 16.4160 REMARK 3 T TENSOR REMARK 3 T11: 0.0687 T22: -0.1530 REMARK 3 T33: 0.0762 T12: -0.0952 REMARK 3 T13: -0.0110 T23: -0.0777 REMARK 3 L TENSOR REMARK 3 L11: 2.3414 L22: 3.5596 REMARK 3 L33: 5.9199 L12: 0.3127 REMARK 3 L13: 1.7670 L23: 1.4329 REMARK 3 S TENSOR REMARK 3 S11: -0.2182 S12: -0.1099 S13: -0.1159 REMARK 3 S21: 0.0199 S22: 0.2961 S23: -0.0304 REMARK 3 S31: -0.0962 S32: 0.1299 S33: -0.0779 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 154 A 209 REMARK 3 ORIGIN FOR THE GROUP (A): 42.6890 -29.0980 -15.5620 REMARK 3 T TENSOR REMARK 3 T11: 0.1709 T22: 0.1133 REMARK 3 T33: 0.3065 T12: -0.2518 REMARK 3 T13: 0.0932 T23: -0.1756 REMARK 3 L TENSOR REMARK 3 L11: 0.1968 L22: 1.3012 REMARK 3 L33: 11.1990 L12: 0.0181 REMARK 3 L13: 0.1745 L23: -3.0254 REMARK 3 S TENSOR REMARK 3 S11: 0.0291 S12: 0.4248 S13: -0.0041 REMARK 3 S21: -0.0426 S22: 0.1746 S23: 0.3180 REMARK 3 S31: 0.9366 S32: -0.4502 S33: -0.2037 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 213 A 235 REMARK 3 ORIGIN FOR THE GROUP (A): 44.1180 -34.0290 -24.9940 REMARK 3 T TENSOR REMARK 3 T11: 0.2622 T22: -0.1153 REMARK 3 T33: 0.0622 T12: -0.2337 REMARK 3 T13: 0.3873 T23: -0.2809 REMARK 3 L TENSOR REMARK 3 L11: 23.2621 L22: 8.6319 REMARK 3 L33: 9.8309 L12: 1.7597 REMARK 3 L13: 1.1684 L23: 5.3168 REMARK 3 S TENSOR REMARK 3 S11: -0.5046 S12: -0.5052 S13: -1.4638 REMARK 3 S21: 0.6858 S22: 0.3581 S23: 0.3114 REMARK 3 S31: 2.1573 S32: -0.0189 S33: 0.1465 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 : B 1 B 120 REMARK 3 ORIGIN FOR THE GROUP (A): 29.7590 -14.4600 8.5890 REMARK 3 T TENSOR REMARK 3 T11: 0.1029 T22: -0.2192 REMARK 3 T33: 0.1062 T12: -0.1392 REMARK 3 T13: 0.0951 T23: 0.0004 REMARK 3 L TENSOR REMARK 3 L11: 5.1779 L22: 2.1753 REMARK 3 L33: 0.9038 L12: 0.0059 REMARK 3 L13: 0.7310 L23: -0.4373 REMARK 3 S TENSOR REMARK 3 S11: 0.1190 S12: -0.1633 S13: 0.1731 REMARK 3 S21: 0.5391 S22: 0.0096 S23: 0.3290 REMARK 3 S31: -0.1333 S32: -0.0485 S33: -0.1286 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 : C 4 C 47 REMARK 3 ORIGIN FOR THE GROUP (A): 47.8440 -11.8040 100.9780 REMARK 3 T TENSOR REMARK 3 T11: 0.0749 T22: -0.0944 REMARK 3 T33: -0.3001 T12: 0.1073 REMARK 3 T13: 0.3526 T23: 0.1923 REMARK 3 L TENSOR REMARK 3 L11: 11.3924 L22: 12.0573 REMARK 3 L33: 8.8285 L12: -5.1595 REMARK 3 L13: 3.5865 L23: -3.1500 REMARK 3 S TENSOR REMARK 3 S11: -0.2032 S12: -1.1298 S13: -0.2777 REMARK 3 S21: 1.4636 S22: 0.4670 S23: 0.8183 REMARK 3 S31: -0.7124 S32: -0.1419 S33: -0.2638 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 : C 48 C 153 REMARK 3 ORIGIN FOR THE GROUP (A): 49.6230 -8.3110 86.7270 REMARK 3 T TENSOR REMARK 3 T11: 0.0815 T22: -0.1285 REMARK 3 T33: -0.0546 T12: 0.1332 REMARK 3 T13: 0.1186 T23: 0.0941 REMARK 3 L TENSOR REMARK 3 L11: 3.7154 L22: 4.1338 REMARK 3 L33: 4.1624 L12: -1.5357 REMARK 3 L13: 1.1126 L23: -0.4208 REMARK 3 S TENSOR REMARK 3 S11: 0.1924 S12: -0.2296 S13: -0.2497 REMARK 3 S21: 0.4383 S22: -0.0117 S23: 0.4041 REMARK 3 S31: 0.1718 S32: 0.0016 S33: -0.1807 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 : C 154 C 209 REMARK 3 ORIGIN FOR THE GROUP (A): 37.6480 -6.9220 55.9090 REMARK 3 T TENSOR REMARK 3 T11: 0.2250 T22: 0.0389 REMARK 3 T33: 0.3413 T12: 0.2855 REMARK 3 T13: -0.0821 T23: -0.0100 REMARK 3 L TENSOR REMARK 3 L11: 1.1271 L22: 0.0947 REMARK 3 L33: 17.6468 L12: 0.2687 REMARK 3 L13: 4.1112 L23: 0.6948 REMARK 3 S TENSOR REMARK 3 S11: 0.0061 S12: -0.0529 S13: -0.2990 REMARK 3 S21: -0.2005 S22: 0.0541 S23: 0.1185 REMARK 3 S31: -0.6874 S32: -0.5101 S33: -0.0603 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 : C 214 C 235 REMARK 3 ORIGIN FOR THE GROUP (A): 29.0970 -7.0610 49.0140 REMARK 3 T TENSOR REMARK 3 T11: 0.0012 T22: -0.1956 REMARK 3 T33: 0.2657 T12: 0.1350 REMARK 3 T13: -0.1101 T23: -0.1153 REMARK 3 L TENSOR REMARK 3 L11: 10.8239 L22: 10.0193 REMARK 3 L33: 15.3859 L12: -2.7761 REMARK 3 L13: 4.7072 L23: -7.1154 REMARK 3 S TENSOR REMARK 3 S11: -0.4119 S12: -0.9504 S13: 0.1024 REMARK 3 S21: 1.1866 S22: 0.1876 S23: 0.9721 REMARK 3 S31: -0.3615 S32: -0.8345 S33: 0.2243 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 : D 1 D 120 REMARK 3 ORIGIN FOR THE GROUP (A): 63.4280 0.5370 71.5150 REMARK 3 T TENSOR REMARK 3 T11: -0.0692 T22: -0.1240 REMARK 3 T33: 0.0272 T12: 0.1324 REMARK 3 T13: 0.0371 T23: 0.0390 REMARK 3 L TENSOR REMARK 3 L11: 1.4987 L22: 5.2540 REMARK 3 L33: 2.9944 L12: -0.2020 REMARK 3 L13: -1.3155 L23: -1.6277 REMARK 3 S TENSOR REMARK 3 S11: 0.0337 S12: -0.0971 S13: 0.2383 REMARK 3 S21: 0.2286 S22: 0.0355 S23: -0.5018 REMARK 3 S31: -0.0803 S32: 0.1660 S33: -0.0692 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 : E 4 E 47 REMARK 3 ORIGIN FOR THE GROUP (A): 70.7490 -21.2920 -18.4760 REMARK 3 T TENSOR REMARK 3 T11: -0.2385 T22: -0.0613 REMARK 3 T33: 0.0779 T12: -0.0711 REMARK 3 T13: 0.1484 T23: -0.2652 REMARK 3 L TENSOR REMARK 3 L11: 5.5715 L22: 9.9164 REMARK 3 L33: 4.8332 L12: 2.0430 REMARK 3 L13: 2.3178 L23: 3.6483 REMARK 3 S TENSOR REMARK 3 S11: -0.0014 S12: 0.7915 S13: -0.3320 REMARK 3 S21: -0.1189 S22: 0.4747 S23: -1.2466 REMARK 3 S31: 0.2750 S32: 0.2507 S33: -0.4732 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 : E 48 E 152 REMARK 3 ORIGIN FOR THE GROUP (A): 60.8770 -13.5950 -10.7950 REMARK 3 T TENSOR REMARK 3 T11: -0.0319 T22: -0.0730 REMARK 3 T33: 0.1240 T12: -0.1324 REMARK 3 T13: 0.0549 T23: -0.1139 REMARK 3 L TENSOR REMARK 3 L11: 2.7131 L22: 5.8857 REMARK 3 L33: 3.9253 L12: -0.5889 REMARK 3 L13: 0.1529 L23: 4.6611 REMARK 3 S TENSOR REMARK 3 S11: 0.0295 S12: 0.3319 S13: 0.1337 REMARK 3 S21: -0.0570 S22: -0.0662 S23: -0.0696 REMARK 3 S31: 0.0550 S32: -0.0596 S33: 0.0367 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 : E 153 E 217 REMARK 3 ORIGIN FOR THE GROUP (A): 51.5730 -0.1880 18.6000 REMARK 3 T TENSOR REMARK 3 T11: 0.5448 T22: -0.1539 REMARK 3 T33: 0.3995 T12: -0.1053 REMARK 3 T13: 0.0371 T23: -0.0911 REMARK 3 L TENSOR REMARK 3 L11: 5.0055 L22: 0.5159 REMARK 3 L33: 18.7018 L12: -1.5859 REMARK 3 L13: -9.4978 L23: 3.1048 REMARK 3 S TENSOR REMARK 3 S11: 0.2516 S12: 0.0091 S13: 0.6413 REMARK 3 S21: -0.1377 S22: 0.5323 S23: 0.0978 REMARK 3 S31: -0.4672 S32: 0.1517 S33: -0.7839 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 : E 222 E 235 REMARK 3 ORIGIN FOR THE GROUP (A): 55.0630 5.2480 29.0350 REMARK 3 T TENSOR REMARK 3 T11: -0.0029 T22: -0.2423 REMARK 3 T33: 0.4337 T12: -0.1278 REMARK 3 T13: 0.1676 T23: 0.0536 REMARK 3 L TENSOR REMARK 3 L11: 20.4152 L22: 13.8727 REMARK 3 L33: 18.4249 L12: -3.8878 REMARK 3 L13: -13.9002 L23: -8.2006 REMARK 3 S TENSOR REMARK 3 S11: 0.4199 S12: -1.1599 S13: 0.2020 REMARK 3 S21: -1.1090 S22: -0.9098 S23: -2.5181 REMARK 3 S31: -1.2132 S32: 2.9828 S33: 0.4899 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 : F 1 F 120 REMARK 3 ORIGIN FOR THE GROUP (A): 42.0240 -1.5230 -11.6230 REMARK 3 T TENSOR REMARK 3 T11: -0.0533 T22: -0.1213 REMARK 3 T33: 0.1026 T12: -0.2188 REMARK 3 T13: 0.0608 T23: -0.0062 REMARK 3 L TENSOR REMARK 3 L11: 3.6885 L22: 4.7556 REMARK 3 L33: 0.9676 L12: -1.2129 REMARK 3 L13: 0.0044 L23: 0.0903 REMARK 3 S TENSOR REMARK 3 S11: -0.1187 S12: 0.4032 S13: 0.1278 REMARK 3 S21: -0.1867 S22: 0.1677 S23: 0.0424 REMARK 3 S31: -0.0321 S32: -0.0629 S33: -0.0490 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 : G 4 G 47 REMARK 3 ORIGIN FOR THE GROUP (A): 29.9090 -34.8380 60.4930 REMARK 3 T TENSOR REMARK 3 T11: -0.2091 T22: -0.1629 REMARK 3 T33: 0.8522 T12: -0.1116 REMARK 3 T13: -0.1546 T23: 0.0028 REMARK 3 L TENSOR REMARK 3 L11: 9.7176 L22: 7.7660 REMARK 3 L33: 6.6136 L12: -1.6610 REMARK 3 L13: 3.2685 L23: -0.3703 REMARK 3 S TENSOR REMARK 3 S11: 0.1243 S12: -0.0141 S13: -0.8360 REMARK 3 S21: -0.7641 S22: 0.1648 S23: 2.4260 REMARK 3 S31: 0.3272 S32: -0.7852 S33: -0.2891 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 : G 48 G 126 REMARK 3 ORIGIN FOR THE GROUP (A): 42.0160 -28.7340 62.6200 REMARK 3 T TENSOR REMARK 3 T11: -0.0271 T22: -0.1270 REMARK 3 T33: 0.1933 T12: 0.0960 REMARK 3 T13: -0.0178 T23: 0.0312 REMARK 3 L TENSOR REMARK 3 L11: 5.5342 L22: 5.1992 REMARK 3 L33: 2.4273 L12: -1.5522 REMARK 3 L13: 1.1675 L23: -0.6709 REMARK 3 S TENSOR REMARK 3 S11: -0.1558 S12: 0.0812 S13: -0.2737 REMARK 3 S21: -0.4194 S22: -0.0005 S23: 0.8306 REMARK 3 S31: 0.0440 S32: -0.2418 S33: 0.1564 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 : G 127 G 163 REMARK 3 ORIGIN FOR THE GROUP (A): 49.9810 -32.6460 68.4300 REMARK 3 T TENSOR REMARK 3 T11: 0.0014 T22: -0.1674 REMARK 3 T33: 0.0483 T12: 0.1118 REMARK 3 T13: 0.0619 T23: 0.0810 REMARK 3 L TENSOR REMARK 3 L11: 5.7124 L22: 9.3931 REMARK 3 L33: 2.1124 L12: -0.2013 REMARK 3 L13: 1.2979 L23: 1.2694 REMARK 3 S TENSOR REMARK 3 S11: -0.3202 S12: -0.0345 S13: -0.5045 REMARK 3 S21: 0.3676 S22: 0.2279 S23: 0.5650 REMARK 3 S31: 0.4736 S32: 0.0216 S33: 0.0923 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 : G 164 G 235 REMARK 3 ORIGIN FOR THE GROUP (A): 73.3420 -22.3810 90.6820 REMARK 3 T TENSOR REMARK 3 T11: 0.2445 T22: -0.0175 REMARK 3 T33: 0.0792 T12: 0.3280 REMARK 3 T13: -0.1552 T23: -0.0444 REMARK 3 L TENSOR REMARK 3 L11: 13.5347 L22: 11.0026 REMARK 3 L33: 2.5716 L12: 1.6944 REMARK 3 L13: -0.7625 L23: -2.3197 REMARK 3 S TENSOR REMARK 3 S11: -0.4453 S12: 0.2087 S13: -0.0255 REMARK 3 S21: 0.3100 S22: 0.4553 S23: -0.9450 REMARK 3 S31: -0.1378 S32: 0.2098 S33: -0.0099 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 1 H 120 REMARK 3 ORIGIN FOR THE GROUP (A): 61.8870 -20.2400 54.4110 REMARK 3 T TENSOR REMARK 3 T11: 0.0790 T22: -0.1562 REMARK 3 T33: -0.0500 T12: 0.1351 REMARK 3 T13: 0.0676 T23: 0.0430 REMARK 3 L TENSOR REMARK 3 L11: 4.0365 L22: 3.2511 REMARK 3 L33: 0.8768 L12: -0.6322 REMARK 3 L13: -0.6921 L23: -0.1371 REMARK 3 S TENSOR REMARK 3 S11: -0.0674 S12: 0.1484 S13: -0.1636 REMARK 3 S21: -0.4349 S22: -0.0405 S23: -0.1790 REMARK 3 S31: -0.0118 S32: -0.0853 S33: 0.1078 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3EZJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-NOV-08. REMARK 100 THE RCSB ID CODE IS RCSB049958. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 08-MAY-07 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 : SSRL REMARK 200 BEAMLINE : BL9-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 86152 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 91.7 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.08600 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) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90 REMARK 200 COMPLETENESS FOR SHELL (%) : 91.7 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.76700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.200 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD REMARK 200 SOFTWARE USED: SHELXD REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 65.09 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.52 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M NA/K PHOSPHATE, PH 5.0, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+2/3 REMARK 290 6555 -X,-X+Y,-Z+1/3 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 134.03333 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 268.06667 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 268.06667 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 134.03333 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 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: BIOLOGICAL UNIT IS A DODECAMER, IT IS UNKNOWN AT THE MOMENT REMARK 300 HOW INDIVIDUAL SUBUNITS ARE ASSEMBLED IN VIVO 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7850 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 29980 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 APPLY THE FOLLOWING TO CHAINS: E, F REMARK 350 BIOMT1 2 -0.500000 0.866025 0.000000 49.26000 REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 -85.32082 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 8210 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 29620 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F 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: 3 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7810 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 30170 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D 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 APPLY THE FOLLOWING TO CHAINS: G, H REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 49.26000 REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 85.32082 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 134.03333 REMARK 350 REMARK 350 BIOMOLECULE: 4 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 8230 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 29740 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, G, H 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 A -3 REMARK 465 ALA A -2 REMARK 465 MET A -1 REMARK 465 ALA A 0 REMARK 465 GLU A 1 REMARK 465 GLU A 2 REMARK 465 GLY A 32 REMARK 465 PRO A 33 REMARK 465 GLY A 34 REMARK 465 SER A 81 REMARK 465 ALA A 82 REMARK 465 ALA A 83 REMARK 465 LYS A 84 REMARK 465 VAL A 85 REMARK 465 GLU A 86 REMARK 465 PRO A 87 REMARK 465 LEU A 88 REMARK 465 PRO A 89 REMARK 465 LEU A 90 REMARK 465 VAL A 91 REMARK 465 GLY A 92 REMARK 465 GLU A 93 REMARK 465 GLY A 94 REMARK 465 SER A 95 REMARK 465 ASP A 96 REMARK 465 ASN A 97 REMARK 465 TYR A 98 REMARK 465 ALA A 99 REMARK 465 LYS A 192 REMARK 465 ASN A 193 REMARK 465 SER A 194 REMARK 465 GLY A 195 REMARK 465 GLU A 196 REMARK 465 ASN A 197 REMARK 465 GLN A 198 REMARK 465 PRO A 199 REMARK 465 ALA A 200 REMARK 465 THR A 201 REMARK 465 LEU A 202 REMARK 465 LYS A 203 REMARK 465 SER A 204 REMARK 465 SER A 236 REMARK 465 GLU A 237 REMARK 465 GLY C -3 REMARK 465 ALA C -2 REMARK 465 MET C -1 REMARK 465 ALA C 0 REMARK 465 GLU C 1 REMARK 465 GLU C 2 REMARK 465 GLY C 32 REMARK 465 PRO C 33 REMARK 465 GLY C 34 REMARK 465 LYS C 79 REMARK 465 SER C 80 REMARK 465 SER C 81 REMARK 465 ALA C 82 REMARK 465 ALA C 83 REMARK 465 LYS C 84 REMARK 465 VAL C 85 REMARK 465 GLU C 86 REMARK 465 PRO C 87 REMARK 465 LEU C 88 REMARK 465 PRO C 89 REMARK 465 LEU C 90 REMARK 465 VAL C 91 REMARK 465 GLY C 92 REMARK 465 GLU C 93 REMARK 465 GLY C 94 REMARK 465 SER C 95 REMARK 465 ASP C 96 REMARK 465 ASN C 97 REMARK 465 TYR C 98 REMARK 465 LYS C 192 REMARK 465 ASN C 193 REMARK 465 SER C 194 REMARK 465 GLY C 195 REMARK 465 GLU C 196 REMARK 465 ASN C 197 REMARK 465 GLN C 198 REMARK 465 PRO C 199 REMARK 465 ALA C 200 REMARK 465 THR C 201 REMARK 465 LEU C 202 REMARK 465 LYS C 203 REMARK 465 SER C 204 REMARK 465 SER C 236 REMARK 465 GLU C 237 REMARK 465 GLY E -3 REMARK 465 ALA E -2 REMARK 465 MET E -1 REMARK 465 ALA E 0 REMARK 465 GLU E 1 REMARK 465 GLU E 2 REMARK 465 ALA E 3 REMARK 465 PRO E 33 REMARK 465 GLY E 34 REMARK 465 LYS E 79 REMARK 465 SER E 80 REMARK 465 SER E 81 REMARK 465 ALA E 82 REMARK 465 ALA E 83 REMARK 465 LYS E 84 REMARK 465 VAL E 85 REMARK 465 GLU E 86 REMARK 465 PRO E 87 REMARK 465 LEU E 88 REMARK 465 PRO E 89 REMARK 465 LEU E 90 REMARK 465 VAL E 91 REMARK 465 GLY E 92 REMARK 465 GLU E 93 REMARK 465 GLY E 94 REMARK 465 SER E 95 REMARK 465 ASP E 96 REMARK 465 ASN E 97 REMARK 465 TYR E 98 REMARK 465 LYS E 192 REMARK 465 ASN E 193 REMARK 465 SER E 194 REMARK 465 GLY E 195 REMARK 465 GLU E 196 REMARK 465 ASN E 197 REMARK 465 GLN E 198 REMARK 465 PRO E 199 REMARK 465 ALA E 200 REMARK 465 THR E 201 REMARK 465 LEU E 202 REMARK 465 LYS E 203 REMARK 465 SER E 204 REMARK 465 SER E 236 REMARK 465 GLU E 237 REMARK 465 GLY G -3 REMARK 465 ALA G -2 REMARK 465 MET G -1 REMARK 465 ALA G 0 REMARK 465 GLU G 1 REMARK 465 GLU G 2 REMARK 465 GLY G 32 REMARK 465 PRO G 33 REMARK 465 GLY G 34 REMARK 465 SER G 81 REMARK 465 ALA G 82 REMARK 465 ALA G 83 REMARK 465 LYS G 84 REMARK 465 VAL G 85 REMARK 465 GLU G 86 REMARK 465 PRO G 87 REMARK 465 LEU G 88 REMARK 465 PRO G 89 REMARK 465 LEU G 90 REMARK 465 VAL G 91 REMARK 465 GLY G 92 REMARK 465 GLU G 93 REMARK 465 GLY G 94 REMARK 465 SER G 95 REMARK 465 ASP G 96 REMARK 465 ASN G 97 REMARK 465 TYR G 98 REMARK 465 LYS G 192 REMARK 465 ASN G 193 REMARK 465 SER G 194 REMARK 465 GLY G 195 REMARK 465 GLU G 196 REMARK 465 ASN G 197 REMARK 465 GLN G 198 REMARK 465 PRO G 199 REMARK 465 ALA G 200 REMARK 465 THR G 201 REMARK 465 LEU G 202 REMARK 465 LYS G 203 REMARK 465 SER G 204 REMARK 465 SER G 236 REMARK 465 GLU G 237 REMARK 465 HIS B 121 REMARK 465 HIS B 122 REMARK 465 HIS B 123 REMARK 465 HIS B 124 REMARK 465 HIS B 125 REMARK 465 HIS B 126 REMARK 465 HIS D 121 REMARK 465 HIS D 122 REMARK 465 HIS D 123 REMARK 465 HIS D 124 REMARK 465 HIS D 125 REMARK 465 HIS D 126 REMARK 465 HIS F 121 REMARK 465 HIS F 122 REMARK 465 HIS F 123 REMARK 465 HIS F 124 REMARK 465 HIS F 125 REMARK 465 HIS F 126 REMARK 465 HIS H 121 REMARK 465 HIS H 122 REMARK 465 HIS H 123 REMARK 465 HIS H 124 REMARK 465 HIS H 125 REMARK 465 HIS H 126 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 GLU A 71 115.80 -33.29 REMARK 500 ASN A 72 61.31 69.52 REMARK 500 ASN A 141 50.99 71.94 REMARK 500 ASN A 177 -58.94 -123.61 REMARK 500 ASN A 213 61.89 39.95 REMARK 500 LEU A 234 41.35 -87.86 REMARK 500 GLU C 71 139.72 -35.22 REMARK 500 ASN C 141 43.14 75.79 REMARK 500 GLU E 71 132.85 -32.57 REMARK 500 ASN E 72 60.23 26.59 REMARK 500 ASN E 141 40.75 76.67 REMARK 500 ASN G 72 44.50 70.15 REMARK 500 ASN G 141 43.45 70.08 REMARK 500 ASN G 167 39.40 -156.88 REMARK 500 ASN G 213 46.27 37.00 REMARK 500 VAL F 48 -60.86 -97.22 REMARK 500 SER H 33 147.53 -176.36 REMARK 500 ALA H 91 166.24 172.29 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 238 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 238 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 238 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 G 238 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 127 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 127 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 128 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 F 127 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 128 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 H 127