REMARK 2 REMARK 2 RESOLUTION. 2.05 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0109 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) : 2.05 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2 REMARK 3 NUMBER OF REFLECTIONS : 266095 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : THIN SHELLS (SFTOOLS) REMARK 3 R VALUE (WORKING + TEST SET) : 0.224 REMARK 3 R VALUE (WORKING SET) : 0.223 REMARK 3 FREE R VALUE : 0.264 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.812 REMARK 3 FREE R VALUE TEST SET COUNT : 2162 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) : 2.05 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10 REMARK 3 REFLECTION IN BIN (WORKING SET) : 18210 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.35 REMARK 3 BIN R VALUE (WORKING SET) : 0.3260 REMARK 3 BIN FREE R VALUE SET COUNT : 0 REMARK 3 BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 29516 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 143 REMARK 3 SOLVENT ATOMS : 1275 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.03 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.95100 REMARK 3 B22 (A**2) : 0.53700 REMARK 3 B33 (A**2) : 2.17700 REMARK 3 B12 (A**2) : -0.24800 REMARK 3 B13 (A**2) : 0.07600 REMARK 3 B23 (A**2) : -2.48900 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.218 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.187 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.173 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.604 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 30607 ; 0.014 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 19833 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 41855 ; 1.267 ; 1.940 REMARK 3 BOND ANGLES OTHERS (DEGREES): 48541 ; 0.879 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3986 ; 7.101 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1173 ;34.294 ;24.015 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 4503 ;13.334 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 96 ;19.749 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 4694 ; 0.078 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 34555 ; 0.005 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): 6285 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL 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): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL 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): 19677 ; 0.760 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 7966 ; 0.175 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31700 ; 1.338 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 10930 ; 2.030 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 10115 ; 3.160 ; 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 : A -10 A 9999 REMARK 3 ORIGIN FOR THE GROUP (A): 20.7112 -85.4626 25.4689 REMARK 3 T TENSOR REMARK 3 T11: 0.2067 T22: 0.1803 REMARK 3 T33: 0.2335 T12: 0.0312 REMARK 3 T13: -0.0139 T23: -0.0739 REMARK 3 L TENSOR REMARK 3 L11: 1.7135 L22: 0.4248 REMARK 3 L33: 3.7174 L12: -0.0542 REMARK 3 L13: 2.0919 L23: -0.0264 REMARK 3 S TENSOR REMARK 3 S11: 0.2777 S12: 0.2657 S13: -0.3136 REMARK 3 S21: -0.0449 S22: -0.0455 S23: -0.0057 REMARK 3 S31: 0.4961 S32: 0.1549 S33: -0.2321 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 : B -10 B 9999 REMARK 3 ORIGIN FOR THE GROUP (A): 19.0732 -69.8856 34.2371 REMARK 3 T TENSOR REMARK 3 T11: 0.1217 T22: 0.1175 REMARK 3 T33: 0.0829 T12: 0.0115 REMARK 3 T13: 0.0315 T23: 0.0060 REMARK 3 L TENSOR REMARK 3 L11: 1.5988 L22: 0.3936 REMARK 3 L33: 1.6424 L12: 0.1010 REMARK 3 L13: 1.3304 L23: 0.1931 REMARK 3 S TENSOR REMARK 3 S11: -0.0296 S12: 0.0710 S13: -0.1227 REMARK 3 S21: 0.0239 S22: 0.0064 S23: 0.0930 REMARK 3 S31: 0.0151 S32: -0.0688 S33: 0.0232 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 : C -10 C 9999 REMARK 3 ORIGIN FOR THE GROUP (A): 41.3551 -81.3611 66.3620 REMARK 3 T TENSOR REMARK 3 T11: 0.3245 T22: 0.2645 REMARK 3 T33: 0.1526 T12: 0.0244 REMARK 3 T13: -0.1290 T23: 0.1089 REMARK 3 L TENSOR REMARK 3 L11: 5.1128 L22: 4.1474 REMARK 3 L33: 5.6146 L12: -1.2808 REMARK 3 L13: 1.7699 L23: 1.0464 REMARK 3 S TENSOR REMARK 3 S11: 0.2610 S12: -0.3723 S13: -0.4395 REMARK 3 S21: 0.4962 S22: 0.0581 S23: -0.2674 REMARK 3 S31: 0.7046 S32: 0.3462 S33: -0.3191 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 : D -10 D 9999 REMARK 3 ORIGIN FOR THE GROUP (A): 52.7396 -25.6486 35.0219 REMARK 3 T TENSOR REMARK 3 T11: 0.1864 T22: 0.1671 REMARK 3 T33: 0.4405 T12: -0.0279 REMARK 3 T13: 0.0246 T23: 0.0217 REMARK 3 L TENSOR REMARK 3 L11: 1.5263 L22: 1.5337 REMARK 3 L33: 2.6644 L12: 0.4334 REMARK 3 L13: -1.3408 L23: -1.1982 REMARK 3 S TENSOR REMARK 3 S11: 0.1468 S12: 0.0328 S13: 0.3013 REMARK 3 S21: 0.2127 S22: -0.0979 S23: 0.1402 REMARK 3 S31: -0.3954 S32: -0.0265 S33: -0.0489 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 -10 E 9999 REMARK 3 ORIGIN FOR THE GROUP (A): 54.9720 -42.9282 38.5963 REMARK 3 T TENSOR REMARK 3 T11: 0.1355 T22: 0.0907 REMARK 3 T33: 0.1954 T12: -0.0101 REMARK 3 T13: -0.0100 T23: 0.0133 REMARK 3 L TENSOR REMARK 3 L11: 1.9183 L22: 0.9081 REMARK 3 L33: 1.2083 L12: 0.5887 REMARK 3 L13: -0.9298 L23: -0.6199 REMARK 3 S TENSOR REMARK 3 S11: 0.0175 S12: -0.0542 S13: 0.3096 REMARK 3 S21: 0.0693 S22: 0.0298 S23: -0.0876 REMARK 3 S31: -0.0620 S32: 0.0547 S33: -0.0473 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 -10 F 9999 REMARK 3 ORIGIN FOR THE GROUP (A): 32.8315 -42.2177 71.7950 REMARK 3 T TENSOR REMARK 3 T11: 0.4863 T22: 0.5331 REMARK 3 T33: 0.3645 T12: -0.0130 REMARK 3 T13: 0.1491 T23: -0.1856 REMARK 3 L TENSOR REMARK 3 L11: 8.9910 L22: 4.0736 REMARK 3 L33: 10.8175 L12: 0.6408 REMARK 3 L13: 0.1945 L23: -1.0394 REMARK 3 S TENSOR REMARK 3 S11: 0.1643 S12: -0.9047 S13: 0.4426 REMARK 3 S21: 0.8648 S22: 0.1366 S23: 0.4843 REMARK 3 S31: -0.2568 S32: -0.4888 S33: -0.3009 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 : G -10 G 9999 REMARK 3 ORIGIN FOR THE GROUP (A): 58.9973 -84.6263 25.4648 REMARK 3 T TENSOR REMARK 3 T11: 0.1696 T22: 0.1774 REMARK 3 T33: 0.2671 T12: -0.0466 REMARK 3 T13: 0.0498 T23: -0.0898 REMARK 3 L TENSOR REMARK 3 L11: 1.5290 L22: 0.8080 REMARK 3 L33: 2.8183 L12: -0.3070 REMARK 3 L13: 0.7356 L23: -0.0369 REMARK 3 S TENSOR REMARK 3 S11: 0.0294 S12: 0.3267 S13: -0.3365 REMARK 3 S21: -0.0366 S22: -0.0143 S23: 0.0463 REMARK 3 S31: 0.2080 S32: 0.0861 S33: -0.0151 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 : H -10 H 9999 REMARK 3 ORIGIN FOR THE GROUP (A): 57.8435 -68.5695 34.5565 REMARK 3 T TENSOR REMARK 3 T11: 0.1455 T22: 0.1027 REMARK 3 T33: 0.0995 T12: -0.0472 REMARK 3 T13: 0.0280 T23: -0.0010 REMARK 3 L TENSOR REMARK 3 L11: 1.5218 L22: 0.4807 REMARK 3 L33: 1.8781 L12: -0.1410 REMARK 3 L13: 0.6769 L23: 0.3004 REMARK 3 S TENSOR REMARK 3 S11: -0.0826 S12: 0.0910 S13: -0.1383 REMARK 3 S21: 0.0557 S22: 0.0016 S23: 0.0909 REMARK 3 S31: 0.0509 S32: -0.0897 S33: 0.0811 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 : I -10 I 9999 REMARK 3 ORIGIN FOR THE GROUP (A): 77.2304 -82.0356 65.3309 REMARK 3 T TENSOR REMARK 3 T11: 0.4717 T22: 0.5130 REMARK 3 T33: 0.2145 T12: 0.0563 REMARK 3 T13: -0.1126 T23: 0.1585 REMARK 3 L TENSOR REMARK 3 L11: 5.5231 L22: 8.0967 REMARK 3 L33: 3.5075 L12: -0.2092 REMARK 3 L13: 0.3102 L23: 1.9290 REMARK 3 S TENSOR REMARK 3 S11: 0.2599 S12: -0.8666 S13: -0.5947 REMARK 3 S21: 0.8543 S22: 0.0357 S23: -0.8570 REMARK 3 S31: 0.5870 S32: 0.3513 S33: -0.2957 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 : J -10 J 9999 REMARK 3 ORIGIN FOR THE GROUP (A): 15.0383 -26.3050 35.0422 REMARK 3 T TENSOR REMARK 3 T11: 0.1441 T22: 0.1614 REMARK 3 T33: 0.4042 T12: 0.0073 REMARK 3 T13: -0.0299 T23: -0.0070 REMARK 3 L TENSOR REMARK 3 L11: 0.9803 L22: 1.7479 REMARK 3 L33: 2.9503 L12: 0.3574 REMARK 3 L13: -0.6393 L23: -1.4377 REMARK 3 S TENSOR REMARK 3 S11: 0.0077 S12: 0.1065 S13: 0.2798 REMARK 3 S21: 0.0830 S22: -0.1065 S23: 0.0882 REMARK 3 S31: -0.3013 S32: 0.0020 S33: 0.0988 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 : K -10 K 9999 REMARK 3 ORIGIN FOR THE GROUP (A): 15.9704 -44.4119 39.0012 REMARK 3 T TENSOR REMARK 3 T11: 0.1126 T22: 0.0818 REMARK 3 T33: 0.1515 T12: 0.0075 REMARK 3 T13: -0.0383 T23: 0.0066 REMARK 3 L TENSOR REMARK 3 L11: 1.8774 L22: 1.0152 REMARK 3 L33: 2.1297 L12: 0.3113 REMARK 3 L13: -1.2008 L23: -0.7644 REMARK 3 S TENSOR REMARK 3 S11: -0.0499 S12: -0.0910 S13: 0.3090 REMARK 3 S21: 0.0033 S22: 0.0018 S23: -0.1033 REMARK 3 S31: -0.0021 S32: 0.1828 S33: 0.0481 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 : L -10 L 9999 REMARK 3 ORIGIN FOR THE GROUP (A): -3.3584 -42.3370 72.1794 REMARK 3 T TENSOR REMARK 3 T11: 0.4906 T22: 0.5774 REMARK 3 T33: 0.3769 T12: 0.0459 REMARK 3 T13: 0.2978 T23: -0.1760 REMARK 3 L TENSOR REMARK 3 L11: 9.6694 L22: 8.1988 REMARK 3 L33: 10.4017 L12: -0.2432 REMARK 3 L13: -2.4691 L23: -1.3049 REMARK 3 S TENSOR REMARK 3 S11: 0.3281 S12: -1.0693 S13: 0.6806 REMARK 3 S21: 1.3932 S22: 0.1294 S23: 1.0526 REMARK 3 S31: -0.8044 S32: -0.5202 S33: -0.4575 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 : M -10 M 9999 REMARK 3 ORIGIN FOR THE GROUP (A): 59.0301 4.8896 -34.8301 REMARK 3 T TENSOR REMARK 3 T11: 0.2112 T22: 0.1932 REMARK 3 T33: 0.2717 T12: -0.0119 REMARK 3 T13: 0.0120 T23: -0.0823 REMARK 3 L TENSOR REMARK 3 L11: 1.6591 L22: 0.5962 REMARK 3 L33: 4.3072 L12: 0.2489 REMARK 3 L13: -2.0464 L23: -0.0738 REMARK 3 S TENSOR REMARK 3 S11: 0.2305 S12: -0.3114 S13: 0.3185 REMARK 3 S21: -0.0511 S22: -0.0248 S23: -0.0511 REMARK 3 S31: -0.4588 S32: 0.3006 S33: -0.2057 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 : N -10 N 9999 REMARK 3 ORIGIN FOR THE GROUP (A): 57.2080 -10.6684 -43.5640 REMARK 3 T TENSOR REMARK 3 T11: 0.1421 T22: 0.0956 REMARK 3 T33: 0.0771 T12: 0.0367 REMARK 3 T13: -0.0399 T23: 0.0174 REMARK 3 L TENSOR REMARK 3 L11: 1.8270 L22: 0.4552 REMARK 3 L33: 1.8093 L12: -0.0125 REMARK 3 L13: -1.2677 L23: 0.3822 REMARK 3 S TENSOR REMARK 3 S11: -0.0010 S12: -0.0992 S13: 0.1586 REMARK 3 S21: -0.0877 S22: 0.0106 S23: 0.0881 REMARK 3 S31: -0.0818 S32: 0.0553 S33: -0.0096 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 : O -10 O 9999 REMARK 3 ORIGIN FOR THE GROUP (A): 79.8039 0.5150 -75.4867 REMARK 3 T TENSOR REMARK 3 T11: 0.5763 T22: 0.4043 REMARK 3 T33: 0.3533 T12: -0.0747 REMARK 3 T13: 0.1739 T23: 0.0648 REMARK 3 L TENSOR REMARK 3 L11: 6.5175 L22: 3.9281 REMARK 3 L33: 6.0617 L12: 1.4124 REMARK 3 L13: -3.8572 L23: 0.9244 REMARK 3 S TENSOR REMARK 3 S11: 0.2439 S12: 0.5317 S13: 0.4679 REMARK 3 S21: -0.9059 S22: 0.1449 S23: -0.4769 REMARK 3 S31: -0.8084 S32: 0.2209 S33: -0.3888 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 : P -10 P 9999 REMARK 3 ORIGIN FOR THE GROUP (A): 20.6631 4.0992 -34.9049 REMARK 3 T TENSOR REMARK 3 T11: 0.1471 T22: 0.1869 REMARK 3 T33: 0.1834 T12: 0.0330 REMARK 3 T13: -0.0472 T23: -0.0567 REMARK 3 L TENSOR REMARK 3 L11: 1.3825 L22: 0.8205 REMARK 3 L33: 2.8742 L12: 0.1848 REMARK 3 L13: -1.0146 L23: -0.0391 REMARK 3 S TENSOR REMARK 3 S11: 0.0571 S12: -0.2700 S13: 0.2287 REMARK 3 S21: 0.0862 S22: -0.0230 S23: 0.0289 REMARK 3 S31: -0.2347 S32: -0.0295 S33: -0.0341 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 : Q -10 Q 9999 REMARK 3 ORIGIN FOR THE GROUP (A): 19.4479 -12.0272 -44.0250 REMARK 3 T TENSOR REMARK 3 T11: 0.1384 T22: 0.1220 REMARK 3 T33: 0.0726 T12: 0.0057 REMARK 3 T13: -0.0365 T23: 0.0074 REMARK 3 L TENSOR REMARK 3 L11: 1.3437 L22: 0.3736 REMARK 3 L33: 1.8770 L12: 0.0918 REMARK 3 L13: -0.9865 L23: 0.1549 REMARK 3 S TENSOR REMARK 3 S11: -0.0940 S12: -0.0361 S13: 0.0614 REMARK 3 S21: -0.0142 S22: -0.0060 S23: 0.1191 REMARK 3 S31: -0.0096 S32: -0.1617 S33: 0.0999 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 : R -10 R 9999 REMARK 3 ORIGIN FOR THE GROUP (A): 39.2619 0.7932 -75.9955 REMARK 3 T TENSOR REMARK 3 T11: 0.3583 T22: 0.2892 REMARK 3 T33: 0.1556 T12: -0.0125 REMARK 3 T13: 0.0923 T23: 0.0783 REMARK 3 L TENSOR REMARK 3 L11: 5.3243 L22: 5.0374 REMARK 3 L33: 5.3404 L12: 1.7925 REMARK 3 L13: -0.9289 L23: 1.4948 REMARK 3 S TENSOR REMARK 3 S11: 0.3193 S12: 0.5210 S13: 0.3686 REMARK 3 S21: -0.7776 S22: 0.0614 S23: -0.5062 REMARK 3 S31: -0.8703 S32: 0.4781 S33: -0.3807 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 : S -10 S 9999 REMARK 3 ORIGIN FOR THE GROUP (A): 14.5375 -54.9640 -44.7712 REMARK 3 T TENSOR REMARK 3 T11: 0.1851 T22: 0.1549 REMARK 3 T33: 0.3549 T12: 0.0205 REMARK 3 T13: -0.0301 T23: 0.0090 REMARK 3 L TENSOR REMARK 3 L11: 1.5933 L22: 1.5905 REMARK 3 L33: 2.4740 L12: -0.7700 REMARK 3 L13: 1.4056 L23: -1.5223 REMARK 3 S TENSOR REMARK 3 S11: 0.1973 S12: -0.0454 S13: -0.2799 REMARK 3 S21: -0.2163 S22: -0.1429 S23: 0.1787 REMARK 3 S31: 0.3992 S32: 0.0110 S33: -0.0545 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 : T -10 T 9999 REMARK 3 ORIGIN FOR THE GROUP (A): 16.5452 -37.5542 -48.0271 REMARK 3 T TENSOR REMARK 3 T11: 0.1174 T22: 0.1011 REMARK 3 T33: 0.1556 T12: -0.0131 REMARK 3 T13: 0.0071 T23: 0.0152 REMARK 3 L TENSOR REMARK 3 L11: 1.8814 L22: 0.8068 REMARK 3 L33: 1.2352 L12: -0.6097 REMARK 3 L13: 1.1376 L23: -0.5627 REMARK 3 S TENSOR REMARK 3 S11: 0.0008 S12: 0.0722 S13: -0.2918 REMARK 3 S21: -0.0201 S22: 0.0540 S23: -0.0926 REMARK 3 S31: -0.0064 S32: 0.1440 S33: -0.0548 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 : U -10 U 9999 REMARK 3 ORIGIN FOR THE GROUP (A): -5.6661 -38.3334 -81.4471 REMARK 3 T TENSOR REMARK 3 T11: 0.3450 T22: 0.4539 REMARK 3 T33: 0.2904 T12: 0.0377 REMARK 3 T13: -0.2093 T23: -0.1222 REMARK 3 L TENSOR REMARK 3 L11: 9.1400 L22: 8.2982 REMARK 3 L33: 9.3269 L12: 2.1205 REMARK 3 L13: 1.2615 L23: 0.1760 REMARK 3 S TENSOR REMARK 3 S11: 0.1711 S12: 1.1910 S13: -0.6826 REMARK 3 S21: -0.7692 S22: 0.1853 S23: 0.7088 REMARK 3 S31: 0.3891 S32: -0.4342 S33: -0.3564 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 : V -10 V 9999 REMARK 3 ORIGIN FOR THE GROUP (A): 53.5826 -54.3088 -44.5016 REMARK 3 T TENSOR REMARK 3 T11: 0.1732 T22: 0.1466 REMARK 3 T33: 0.3738 T12: 0.0269 REMARK 3 T13: 0.0184 T23: 0.0123 REMARK 3 L TENSOR REMARK 3 L11: 1.2715 L22: 1.3844 REMARK 3 L33: 2.2605 L12: 0.1012 REMARK 3 L13: 0.4679 L23: -1.1822 REMARK 3 S TENSOR REMARK 3 S11: -0.0421 S12: -0.0990 S13: -0.2747 REMARK 3 S21: -0.1003 S22: -0.0547 S23: 0.0248 REMARK 3 S31: 0.2229 S32: -0.0701 S33: 0.0968 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 : W -10 W 9999 REMARK 3 ORIGIN FOR THE GROUP (A): 54.5996 -36.2847 -48.1297 REMARK 3 T TENSOR REMARK 3 T11: 0.1269 T22: 0.1017 REMARK 3 T33: 0.1494 T12: 0.0303 REMARK 3 T13: 0.0174 T23: 0.0159 REMARK 3 L TENSOR REMARK 3 L11: 1.6621 L22: 0.9614 REMARK 3 L33: 1.6748 L12: -0.1668 REMARK 3 L13: 0.8461 L23: -0.6988 REMARK 3 S TENSOR REMARK 3 S11: -0.0716 S12: 0.0405 S13: -0.2833 REMARK 3 S21: -0.0470 S22: 0.0449 S23: -0.0949 REMARK 3 S31: -0.0017 S32: 0.0690 S33: 0.0267 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 : X -10 X 9999 REMARK 3 ORIGIN FOR THE GROUP (A): 35.6627 -38.2592 -81.8332 REMARK 3 T TENSOR REMARK 3 T11: 0.5184 T22: 0.8383 REMARK 3 T33: 0.3892 T12: -0.1225 REMARK 3 T13: -0.2779 T23: -0.0073 REMARK 3 L TENSOR REMARK 3 L11: 7.9863 L22: 16.2259 REMARK 3 L33: 7.7128 L12: 3.9472 REMARK 3 L13: 2.9520 L23: 0.0481 REMARK 3 S TENSOR REMARK 3 S11: 0.0775 S12: 1.1918 S13: -0.3784 REMARK 3 S21: -1.1977 S22: 0.3396 S23: 1.2287 REMARK 3 S31: 0.5155 S32: -0.6518 S33: -0.4171 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL PLUS 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 U VALUES: WITH TLS ADDED. REMARK 4 REMARK 4 3PNW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-NOV-10. REMARK 100 THE RCSB ID CODE IS RCSB062603. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 18-AUG-10 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 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) : 0.97924 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000 REMARK 200 DATA SCALING SOFTWARE : HKL-3000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 266201 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4 REMARK 200 DATA REDUNDANCY : 2.500 REMARK 200 R MERGE (I) : 0.08600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12 REMARK 200 COMPLETENESS FOR SHELL (%) : 93.1 REMARK 200 DATA REDUNDANCY IN SHELL : 2.30 REMARK 200 R MERGE FOR SHELL (I) : 0.41400 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: PHASER REMARK 200 STARTING MODEL: PDB ENTRIES 2HFF (MODIFIED ON FFAS03 SERVER) AND REMARK 200 3PMT REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47.55 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG-3350, 0.05M CITRIC ACID, 0.05M REMARK 280 BIS-TRIS PROPANE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,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 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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 APPLY THE FOLLOWING TO CHAINS: D, 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 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I 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: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, K, 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: 5 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N, O 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: 6 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, Q, R 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: 7 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: S, T, U 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: 8 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: V, W, X 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 A 1 REMARK 465 GLY A 215 REMARK 465 GLU A 216 REMARK 465 CYS A 217 REMARK 465 GLY A 218 REMARK 465 GLY A 219 REMARK 465 SER A 220 REMARK 465 ASP A 221 REMARK 465 TYR A 222 REMARK 465 LYS A 223 REMARK 465 ASP A 224 REMARK 465 ASP A 225 REMARK 465 ASP A 226 REMARK 465 ASP A 227 REMARK 465 LYS A 228 REMARK 465 GLU B 1 REMARK 465 ILE B 2 REMARK 465 SER B 3 REMARK 465 GLU B 4 REMARK 465 LYS B 230 REMARK 465 SER B 231 REMARK 465 CYS B 232 REMARK 465 ASP B 233 REMARK 465 LYS B 234 REMARK 465 THR B 235 REMARK 465 HIS B 236 REMARK 465 THR B 237 REMARK 465 GLY B 238 REMARK 465 GLY B 239 REMARK 465 SER B 240 REMARK 465 HIS B 241 REMARK 465 HIS B 242 REMARK 465 HIS B 243 REMARK 465 HIS B 244 REMARK 465 HIS B 245 REMARK 465 HIS B 246 REMARK 465 GLY C 539 REMARK 465 PRO C 540 REMARK 465 GLU C 541 REMARK 465 LYS C 542 REMARK 465 ILE C 543 REMARK 465 LEU C 544 REMARK 465 GLU C 545 REMARK 465 SER C 546 REMARK 465 SER C 547 REMARK 465 ILE C 548 REMARK 465 GLN C 609 REMARK 465 THR C 610 REMARK 465 GLU C 611 REMARK 465 ALA C 612 REMARK 465 TRP C 613 REMARK 465 GLU C 614 REMARK 465 GLU C 615 REMARK 465 SER D 1 REMARK 465 GLY D 215 REMARK 465 GLU D 216 REMARK 465 CYS D 217 REMARK 465 GLY D 218 REMARK 465 GLY D 219 REMARK 465 SER D 220 REMARK 465 ASP D 221 REMARK 465 TYR D 222 REMARK 465 LYS D 223 REMARK 465 ASP D 224 REMARK 465 ASP D 225 REMARK 465 ASP D 226 REMARK 465 ASP D 227 REMARK 465 LYS D 228 REMARK 465 GLU E 1 REMARK 465 ILE E 2 REMARK 465 SER E 3 REMARK 465 LYS E 230 REMARK 465 SER E 231 REMARK 465 CYS E 232 REMARK 465 ASP E 233 REMARK 465 LYS E 234 REMARK 465 THR E 235 REMARK 465 HIS E 236 REMARK 465 THR E 237 REMARK 465 GLY E 238 REMARK 465 GLY E 239 REMARK 465 SER E 240 REMARK 465 HIS E 241 REMARK 465 HIS E 242 REMARK 465 HIS E 243 REMARK 465 HIS E 244 REMARK 465 HIS E 245 REMARK 465 HIS E 246 REMARK 465 GLY F 539 REMARK 465 PRO F 540 REMARK 465 GLU F 541 REMARK 465 LYS F 542 REMARK 465 ILE F 543 REMARK 465 LEU F 544 REMARK 465 GLU F 545 REMARK 465 SER F 546 REMARK 465 SER F 547 REMARK 465 ILE F 548 REMARK 465 PRO F 549 REMARK 465 MET F 550 REMARK 465 GLU F 551 REMARK 465 TYR F 552 REMARK 465 ALA F 553 REMARK 465 LYS F 554 REMARK 465 MET F 555 REMARK 465 GLN F 609 REMARK 465 THR F 610 REMARK 465 GLU F 611 REMARK 465 ALA F 612 REMARK 465 TRP F 613 REMARK 465 GLU F 614 REMARK 465 GLU F 615 REMARK 465 SER G 1 REMARK 465 GLY G 215 REMARK 465 GLU G 216 REMARK 465 CYS G 217 REMARK 465 GLY G 218 REMARK 465 GLY G 219 REMARK 465 SER G 220 REMARK 465 ASP G 221 REMARK 465 TYR G 222 REMARK 465 LYS G 223 REMARK 465 ASP G 224 REMARK 465 ASP G 225 REMARK 465 ASP G 226 REMARK 465 ASP G 227 REMARK 465 LYS G 228 REMARK 465 GLU H 1 REMARK 465 ILE H 2 REMARK 465 SER H 3 REMARK 465 SER H 143 REMARK 465 SER H 144 REMARK 465 LYS H 145 REMARK 465 SER H 146 REMARK 465 THR H 147 REMARK 465 SER H 148 REMARK 465 GLY H 149 REMARK 465 GLY H 150 REMARK 465 LYS H 230 REMARK 465 SER H 231 REMARK 465 CYS H 232 REMARK 465 ASP H 233 REMARK 465 LYS H 234 REMARK 465 THR H 235 REMARK 465 HIS H 236 REMARK 465 THR H 237 REMARK 465 GLY H 238 REMARK 465 GLY H 239 REMARK 465 SER H 240 REMARK 465 HIS H 241 REMARK 465 HIS H 242 REMARK 465 HIS H 243 REMARK 465 HIS H 244 REMARK 465 HIS H 245 REMARK 465 HIS H 246 REMARK 465 GLY I 539 REMARK 465 PRO I 540 REMARK 465 GLU I 541 REMARK 465 LYS I 542 REMARK 465 ILE I 543 REMARK 465 LEU I 544 REMARK 465 GLU I 545 REMARK 465 SER I 546 REMARK 465 SER I 547 REMARK 465 ILE I 548 REMARK 465 PRO I 549 REMARK 465 MET I 550 REMARK 465 GLU I 551 REMARK 465 TYR I 552 REMARK 465 ALA I 553 REMARK 465 GLN I 609 REMARK 465 THR I 610 REMARK 465 GLU I 611 REMARK 465 ALA I 612 REMARK 465 TRP I 613 REMARK 465 GLU I 614 REMARK 465 GLU I 615 REMARK 465 SER J 1 REMARK 465 GLY J 215 REMARK 465 GLU J 216 REMARK 465 CYS J 217 REMARK 465 GLY J 218 REMARK 465 GLY J 219 REMARK 465 SER J 220 REMARK 465 ASP J 221 REMARK 465 TYR J 222 REMARK 465 LYS J 223 REMARK 465 ASP J 224 REMARK 465 ASP J 225 REMARK 465 ASP J 226 REMARK 465 ASP J 227 REMARK 465 LYS J 228 REMARK 465 GLU K 1 REMARK 465 ILE K 2 REMARK 465 SER K 3 REMARK 465 SER K 143 REMARK 465 SER K 144 REMARK 465 LYS K 145 REMARK 465 SER K 146 REMARK 465 THR K 147 REMARK 465 SER K 148 REMARK 465 GLY K 149 REMARK 465 GLY K 150 REMARK 465 LYS K 230 REMARK 465 SER K 231 REMARK 465 CYS K 232 REMARK 465 ASP K 233 REMARK 465 LYS K 234 REMARK 465 THR K 235 REMARK 465 HIS K 236 REMARK 465 THR K 237 REMARK 465 GLY K 238 REMARK 465 GLY K 239 REMARK 465 SER K 240 REMARK 465 HIS K 241 REMARK 465 HIS K 242 REMARK 465 HIS K 243 REMARK 465 HIS K 244 REMARK 465 HIS K 245 REMARK 465 HIS K 246 REMARK 465 GLY L 539 REMARK 465 PRO L 540 REMARK 465 GLU L 541 REMARK 465 LYS L 542 REMARK 465 ILE L 543 REMARK 465 LEU L 544 REMARK 465 GLU L 545 REMARK 465 SER L 546 REMARK 465 SER L 547 REMARK 465 ILE L 548 REMARK 465 PRO L 549 REMARK 465 MET L 550 REMARK 465 GLU L 551 REMARK 465 TYR L 552 REMARK 465 ALA L 553 REMARK 465 LYS L 554 REMARK 465 GLN L 609 REMARK 465 THR L 610 REMARK 465 GLU L 611 REMARK 465 ALA L 612 REMARK 465 TRP L 613 REMARK 465 GLU L 614 REMARK 465 GLU L 615 REMARK 465 SER M 1 REMARK 465 GLU M 216 REMARK 465 CYS M 217 REMARK 465 GLY M 218 REMARK 465 GLY M 219 REMARK 465 SER M 220 REMARK 465 ASP M 221 REMARK 465 TYR M 222 REMARK 465 LYS M 223 REMARK 465 ASP M 224 REMARK 465 ASP M 225 REMARK 465 ASP M 226 REMARK 465 ASP M 227 REMARK 465 LYS M 228 REMARK 465 GLU N 1 REMARK 465 ILE N 2 REMARK 465 SER N 3 REMARK 465 LYS N 230 REMARK 465 SER N 231 REMARK 465 CYS N 232 REMARK 465 ASP N 233 REMARK 465 LYS N 234 REMARK 465 THR N 235 REMARK 465 HIS N 236 REMARK 465 THR N 237 REMARK 465 GLY N 238 REMARK 465 GLY N 239 REMARK 465 SER N 240 REMARK 465 HIS N 241 REMARK 465 HIS N 242 REMARK 465 HIS N 243 REMARK 465 HIS N 244 REMARK 465 HIS N 245 REMARK 465 HIS N 246 REMARK 465 GLY O 539 REMARK 465 PRO O 540 REMARK 465 GLU O 541 REMARK 465 LYS O 542 REMARK 465 ILE O 543 REMARK 465 LEU O 544 REMARK 465 GLU O 545 REMARK 465 SER O 546 REMARK 465 SER O 547 REMARK 465 GLN O 609 REMARK 465 THR O 610 REMARK 465 GLU O 611 REMARK 465 ALA O 612 REMARK 465 TRP O 613 REMARK 465 GLU O 614 REMARK 465 GLU O 615 REMARK 465 SER P 1 REMARK 465 GLY P 215 REMARK 465 GLU P 216 REMARK 465 CYS P 217 REMARK 465 GLY P 218 REMARK 465 GLY P 219 REMARK 465 SER P 220 REMARK 465 ASP P 221 REMARK 465 TYR P 222 REMARK 465 LYS P 223 REMARK 465 ASP P 224 REMARK 465 ASP P 225 REMARK 465 ASP P 226 REMARK 465 ASP P 227 REMARK 465 LYS P 228 REMARK 465 GLU Q 1 REMARK 465 ILE Q 2 REMARK 465 SER Q 3 REMARK 465 SER Q 143 REMARK 465 SER Q 144 REMARK 465 LYS Q 145 REMARK 465 SER Q 146 REMARK 465 THR Q 147 REMARK 465 SER Q 148 REMARK 465 GLY Q 149 REMARK 465 GLY Q 150 REMARK 465 LYS Q 230 REMARK 465 SER Q 231 REMARK 465 CYS Q 232 REMARK 465 ASP Q 233 REMARK 465 LYS Q 234 REMARK 465 THR Q 235 REMARK 465 HIS Q 236 REMARK 465 THR Q 237 REMARK 465 GLY Q 238 REMARK 465 GLY Q 239 REMARK 465 SER Q 240 REMARK 465 HIS Q 241 REMARK 465 HIS Q 242 REMARK 465 HIS Q 243 REMARK 465 HIS Q 244 REMARK 465 HIS Q 245 REMARK 465 HIS Q 246 REMARK 465 GLY R 539 REMARK 465 PRO R 540 REMARK 465 GLU R 541 REMARK 465 LYS R 542 REMARK 465 ILE R 543 REMARK 465 LEU R 544 REMARK 465 GLU R 545 REMARK 465 SER R 546 REMARK 465 SER R 547 REMARK 465 GLN R 609 REMARK 465 THR R 610 REMARK 465 GLU R 611 REMARK 465 ALA R 612 REMARK 465 TRP R 613 REMARK 465 GLU R 614 REMARK 465 GLU R 615 REMARK 465 SER S 1 REMARK 465 GLU S 216 REMARK 465 CYS S 217 REMARK 465 GLY S 218 REMARK 465 GLY S 219 REMARK 465 SER S 220 REMARK 465 ASP S 221 REMARK 465 TYR S 222 REMARK 465 LYS S 223 REMARK 465 ASP S 224 REMARK 465 ASP S 225 REMARK 465 ASP S 226 REMARK 465 ASP S 227 REMARK 465 LYS S 228 REMARK 465 GLU T 1 REMARK 465 ILE T 2 REMARK 465 SER T 3 REMARK 465 GLU T 4 REMARK 465 LYS T 230 REMARK 465 SER T 231 REMARK 465 CYS T 232 REMARK 465 ASP T 233 REMARK 465 LYS T 234 REMARK 465 THR T 235 REMARK 465 HIS T 236 REMARK 465 THR T 237 REMARK 465 GLY T 238 REMARK 465 GLY T 239 REMARK 465 SER T 240 REMARK 465 HIS T 241 REMARK 465 HIS T 242 REMARK 465 HIS T 243 REMARK 465 HIS T 244 REMARK 465 HIS T 245 REMARK 465 HIS T 246 REMARK 465 GLY U 539 REMARK 465 PRO U 540 REMARK 465 GLU U 541 REMARK 465 LYS U 542 REMARK 465 ILE U 543 REMARK 465 LEU U 544 REMARK 465 GLU U 545 REMARK 465 SER U 546 REMARK 465 SER U 547 REMARK 465 ILE U 548 REMARK 465 PRO U 549 REMARK 465 MET U 550 REMARK 465 GLU U 551 REMARK 465 TYR U 552 REMARK 465 ALA U 553 REMARK 465 LYS U 554 REMARK 465 GLN U 609 REMARK 465 THR U 610 REMARK 465 GLU U 611 REMARK 465 ALA U 612 REMARK 465 TRP U 613 REMARK 465 GLU U 614 REMARK 465 GLU U 615 REMARK 465 SER V 1 REMARK 465 ASP V 2 REMARK 465 GLY V 215 REMARK 465 GLU V 216 REMARK 465 CYS V 217 REMARK 465 GLY V 218 REMARK 465 GLY V 219 REMARK 465 SER V 220 REMARK 465 ASP V 221 REMARK 465 TYR V 222 REMARK 465 LYS V 223 REMARK 465 ASP V 224 REMARK 465 ASP V 225 REMARK 465 ASP V 226 REMARK 465 ASP V 227 REMARK 465 LYS V 228 REMARK 465 GLU W 1 REMARK 465 ILE W 2 REMARK 465 SER W 3 REMARK 465 SER W 143 REMARK 465 SER W 144 REMARK 465 LYS W 145 REMARK 465 SER W 146 REMARK 465 THR W 147 REMARK 465 SER W 148 REMARK 465 LYS W 230 REMARK 465 SER W 231 REMARK 465 CYS W 232 REMARK 465 ASP W 233 REMARK 465 LYS W 234 REMARK 465 THR W 235 REMARK 465 HIS W 236 REMARK 465 THR W 237 REMARK 465 GLY W 238 REMARK 465 GLY W 239 REMARK 465 SER W 240 REMARK 465 HIS W 241 REMARK 465 HIS W 242 REMARK 465 HIS W 243 REMARK 465 HIS W 244 REMARK 465 HIS W 245 REMARK 465 HIS W 246 REMARK 465 GLY X 539 REMARK 465 PRO X 540 REMARK 465 GLU X 541 REMARK 465 LYS X 542 REMARK 465 ILE X 543 REMARK 465 LEU X 544 REMARK 465 GLU X 545 REMARK 465 SER X 546 REMARK 465 SER X 547 REMARK 465 ILE X 548 REMARK 465 PRO X 549 REMARK 465 MET X 550 REMARK 465 GLU X 551 REMARK 465 TYR X 552 REMARK 465 ALA X 553 REMARK 465 LYS X 554 REMARK 465 ILE X 608 REMARK 465 GLN X 609 REMARK 465 THR X 610 REMARK 465 GLU X 611 REMARK 465 ALA X 612 REMARK 465 TRP X 613 REMARK 465 GLU X 614 REMARK 465 GLU X 615 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ASP A 2 CG OD1 OD2 REMARK 470 GLN A 4 CG CD OE1 NE2 REMARK 470 ARG A 25 CD NE CZ NH1 NH2 REMARK 470 SER A 29 OG REMARK 470 SER A 31 OG REMARK 470 LYS A 43 CE NZ REMARK 470 LYS A 46 CE NZ REMARK 470 SER A 61 OG REMARK 470 LYS A 129 CG CD CE NZ REMARK 470 LYS A 148 CE NZ REMARK 470 LYS A 172 CD CE NZ REMARK 470 LYS A 186 NZ REMARK 470 GLU A 190 CD OE1 OE2 REMARK 470 LYS A 191 NZ REMARK 470 SER A 205 OG REMARK 470 SER A 206 OG REMARK 470 SER B 106 OG REMARK 470 LYS B 107 CE NZ REMARK 470 LYS B 108 CG CD CE NZ REMARK 470 LYS B 145 CG CD CE NZ REMARK 470 LYS B 222 CG CD CE NZ REMARK 470 LYS B 226 CG CD CE NZ REMARK 470 MET C 550 CG SD CE REMARK 470 LYS C 554 CG CD CE NZ REMARK 470 ARG C 574 CG CD NE CZ NH1 NH2 REMARK 470 ASP D 2 CG OD1 OD2 REMARK 470 ARG D 19 CG CD NE CZ NH1 NH2 REMARK 470 GLN D 28 CG CD OE1 NE2 REMARK 470 SER D 29 OG REMARK 470 SER D 31 OG REMARK 470 SER D 57 OG REMARK 470 SER D 61 OG REMARK 470 ARG D 67 NE CZ NH1 NH2 REMARK 470 SER D 68 OG REMARK 470 THR D 70 OG1 CG2 REMARK 470 ILE D 76 CG1 CD1 REMARK 470 LYS D 106 CE NZ REMARK 470 ILE D 109 CG1 CG2 CD1 REMARK 470 LYS D 129 CG CD CE NZ REMARK 470 LYS D 148 CE NZ REMARK 470 LYS D 172 CG CD CE NZ REMARK 470 LYS D 193 CE NZ REMARK 470 GLU E 4 CG CD OE1 OE2 REMARK 470 LYS E 107 CE NZ REMARK 470 LYS E 108 CG CD CE NZ REMARK 470 LYS E 217 CD CE NZ REMARK 470 LYS E 226 CE NZ REMARK 470 LYS F 557 CE NZ REMARK 470 ARG F 574 CG CD NE CZ NH1 NH2 REMARK 470 ASP G 2 CG OD1 OD2 REMARK 470 GLN G 4 CG CD OE1 NE2 REMARK 470 SER G 29 OG REMARK 470 LYS G 43 CE NZ REMARK 470 GLN G 103 CD OE1 NE2 REMARK 470 LYS G 129 CG CD CE NZ REMARK 470 ASN G 155 CG OD1 ND2 REMARK 470 LYS G 172 CD CE NZ REMARK 470 LYS G 191 CG CD CE NZ REMARK 470 LYS G 193 CE NZ REMARK 470 SER H 106 OG REMARK 470 LYS H 107 CE NZ REMARK 470 LYS H 108 CG CD CE NZ REMARK 470 LYS H 217 CD CE NZ REMARK 470 LYS H 222 CD CE NZ REMARK 470 LYS H 226 CE NZ REMARK 470 LYS I 554 CG CD CE NZ REMARK 470 MET I 555 CG SD CE REMARK 470 LYS I 557 CD CE NZ REMARK 470 ARG I 574 CG CD NE CZ NH1 NH2 REMARK 470 LYS I 606 CE NZ REMARK 470 ASP J 2 CG OD1 OD2 REMARK 470 GLN J 4 CG CD OE1 NE2 REMARK 470 SER J 29 OG REMARK 470 LYS J 46 CD CE NZ REMARK 470 ARG J 67 CG CD NE CZ NH1 NH2 REMARK 470 LYS J 129 CD CE NZ REMARK 470 LYS J 172 CG CD CE NZ REMARK 470 LYS J 193 CE NZ REMARK 470 SER K 106 OG REMARK 470 LYS K 107 CE NZ REMARK 470 LYS K 108 CG CD CE NZ REMARK 470 LYS K 217 CD CE NZ REMARK 470 LYS K 222 CE NZ REMARK 470 LYS K 226 CG CD CE NZ REMARK 470 GLU K 228 CG CD OE1 OE2 REMARK 470 MET L 555 CG SD CE REMARK 470 LYS L 557 CG CD CE NZ REMARK 470 PHE L 563 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG L 574 CG CD NE CZ NH1 NH2 REMARK 470 LYS L 606 CD CE NZ REMARK 470 ASP M 2 CG OD1 OD2 REMARK 470 ARG M 25 CD NE CZ NH1 NH2 REMARK 470 SER M 29 OG REMARK 470 SER M 32 OG REMARK 470 LYS M 43 CE NZ REMARK 470 LYS M 129 CG CD CE NZ REMARK 470 LYS M 148 CE NZ REMARK 470 SER M 171 OG REMARK 470 LYS M 172 CG CD CE NZ REMARK 470 GLU M 190 CD OE1 OE2 REMARK 470 LYS M 193 CE NZ REMARK 470 GLU N 4 CG CD OE1 OE2 REMARK 470 SER N 106 OG REMARK 470 LYS N 107 CD CE NZ REMARK 470 LYS N 108 CG CD CE NZ REMARK 470 LYS N 145 CG CD CE NZ REMARK 470 LYS N 217 CD CE NZ REMARK 470 LYS N 222 CD CE NZ REMARK 470 LYS N 226 CG CD CE NZ REMARK 470 ILE O 548 CG1 CG2 CD1 REMARK 470 MET O 550 CG SD CE REMARK 470 LYS O 554 CG CD CE NZ REMARK 470 LYS O 571 CE NZ REMARK 470 ARG O 574 CG CD NE CZ NH1 NH2 REMARK 470 MET O 585 CG SD CE REMARK 470 LYS O 606 CD CE NZ REMARK 470 ILE O 608 CG1 CG2 CD1 REMARK 470 ASP P 2 CG OD1 OD2 REMARK 470 SER P 29 OG REMARK 470 LYS P 43 CE NZ REMARK 470 LYS P 46 NZ REMARK 470 SER P 68 OG REMARK 470 LYS P 129 CG CD CE NZ REMARK 470 LYS P 148 CE NZ REMARK 470 LYS P 172 CG CD CE NZ REMARK 470 LYS P 191 CD CE NZ REMARK 470 LYS P 193 CE NZ REMARK 470 GLU Q 4 CG CD OE1 OE2 REMARK 470 SER Q 106 OG REMARK 470 LYS Q 107 CE NZ REMARK 470 LYS Q 108 CG CD CE NZ REMARK 470 LYS Q 217 CD CE NZ REMARK 470 LYS Q 226 CG CD CE NZ REMARK 470 ILE R 548 CG1 CG2 CD1 REMARK 470 MET R 550 CG SD CE REMARK 470 LYS R 554 CG CD CE NZ REMARK 470 LYS R 557 CE NZ REMARK 470 LYS R 571 CE NZ REMARK 470 ARG R 574 CG CD NE CZ NH1 NH2 REMARK 470 ASP S 2 CG OD1 OD2 REMARK 470 GLN S 4 CG CD OE1 NE2 REMARK 470 SER S 29 OG REMARK 470 SER S 31 OG REMARK 470 LYS S 43 NZ REMARK 470 SER S 61 OG REMARK 470 ARG S 67 CZ NH1 NH2 REMARK 470 SER S 68 OG REMARK 470 GLN S 103 CD OE1 NE2 REMARK 470 LYS S 129 CD CE NZ REMARK 470 ARG S 145 CD NE CZ NH1 NH2 REMARK 470 LYS S 148 NZ REMARK 470 LYS S 152 CE NZ REMARK 470 LYS S 172 CG CD CE NZ REMARK 470 SER S 185 OG REMARK 470 LYS S 191 NZ REMARK 470 LYS S 193 CE NZ REMARK 470 LYS T 46 CE NZ REMARK 470 LYS T 68 CD CE NZ REMARK 470 GLU T 92 CD OE1 OE2 REMARK 470 LYS T 107 CE NZ REMARK 470 LYS T 108 CG CD CE NZ REMARK 470 SER T 143 OG REMARK 470 LYS T 145 CE NZ REMARK 470 LYS T 217 CD CE NZ REMARK 470 LYS T 226 CE NZ REMARK 470 MET U 555 CG SD CE REMARK 470 LYS U 557 CD CE NZ REMARK 470 GLU U 578 CG CD OE1 OE2 REMARK 470 LYS U 606 CE NZ REMARK 470 GLN V 4 CD OE1 NE2 REMARK 470 LEU V 12 CD1 CD2 REMARK 470 ARG V 25 CD NE CZ NH1 NH2 REMARK 470 GLN V 28 CD OE1 NE2 REMARK 470 SER V 31 OG REMARK 470 LYS V 43 CE NZ REMARK 470 LYS V 46 CD CE NZ REMARK 470 SER V 61 OG REMARK 470 ARG V 67 NE CZ NH1 NH2 REMARK 470 SER V 68 OG REMARK 470 ASP V 125 CG OD1 OD2 REMARK 470 LYS V 129 CG CD CE NZ REMARK 470 ARG V 145 CD NE CZ NH1 NH2 REMARK 470 LYS V 172 CG CD CE NZ REMARK 470 SER V 185 OG REMARK 470 LYS V 191 NZ REMARK 470 LYS V 193 CE NZ REMARK 470 ARG W 90 CZ NH1 NH2 REMARK 470 SER W 106 OG REMARK 470 LYS W 107 CD CE NZ REMARK 470 LYS W 108 CG CD CE NZ REMARK 470 LYS W 217 CD CE NZ REMARK 470 LYS W 222 NZ REMARK 470 LYS W 226 CD CE NZ REMARK 470 MET X 555 CG SD CE REMARK 470 LYS X 557 CG CD CE NZ REMARK 470 ASP X 560 CG OD1 OD2 REMARK 470 LEU X 565 CD1 CD2 REMARK 470 GLU X 568 CD OE1 OE2 REMARK 470 LYS X 571 CG CD CE NZ REMARK 470 ARG X 574 CG CD NE CZ NH1 NH2 REMARK 470 ASP X 593 CG OD1 OD2 REMARK 470 TYR X 594 CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS X 606 CG CD CE NZ 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 OG1 THR E 147 UNK UNX E 1815 1.05 REMARK 500 OG SER E 143 UNK UNX E 1814 1.42 REMARK 500 OG SER G 64 UNK UNX G 1820 1.48 REMARK 500 O PHE M 84 UNK UNX M 1952 1.77 REMARK 500 O ARG J 62 UNK UNX J 1821 2.01 REMARK 500 O THR M 181 UNK UNX M 1966 2.07 REMARK 500 O PHE A 84 UNK UNX A 1972 2.08 REMARK 500 UNK UNX N 1967 UNK UNX N 1968 2.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER A 32 -18.35 -150.91 REMARK 500 ALA A 52 -52.86 78.55 REMARK 500 PHE A 95 -24.46 77.60 REMARK 500 ASN A 141 70.32 48.17 REMARK 500 ASP B 160 61.23 70.68 REMARK 500 SER D 32 -7.36 -155.25 REMARK 500 ALA D 52 -42.85 77.10 REMARK 500 ALA D 85 -169.68 -166.49 REMARK 500 PHE D 95 -23.48 76.09 REMARK 500 ASN D 141 70.50 57.19 REMARK 500 LYS D 193 -62.07 -103.75 REMARK 500 ASP E 160 61.63 74.00 REMARK 500 SER G 32 -19.64 -152.35 REMARK 500 ALA G 52 -56.62 71.69 REMARK 500 ALA G 85 -178.54 -176.27 REMARK 500 PHE G 95 -36.19 76.13 REMARK 500 SER G 130 47.30 -100.44 REMARK 500 ASN G 141 67.89 62.92 REMARK 500 LYS G 193 -54.27 -123.53 REMARK 500 ALA H 95 156.42 175.76 REMARK 500 PHE H 111 -3.92 70.11 REMARK 500 ASP H 160 60.80 67.45 REMARK 500 SER J 32 -14.45 -140.25 REMARK 500 ALA J 52 -54.08 75.90 REMARK 500 PHE J 95 -25.06 74.33 REMARK 500 LYS J 193 -60.68 -95.91 REMARK 500 SER K 88 52.18 38.57 REMARK 500 ALA K 95 157.32 179.51 REMARK 500 ASP K 160 66.77 65.60 REMARK 500 SER M 32 -17.99 -150.78 REMARK 500 ALA M 52 -49.38 82.84 REMARK 500 ALA M 85 -178.28 179.95 REMARK 500 PHE M 95 -19.22 75.18 REMARK 500 ASN M 141 75.49 42.15 REMARK 500 ASN M 155 -5.58 72.90 REMARK 500 SER N 88 54.15 34.91 REMARK 500 ALA N 95 159.27 177.89 REMARK 500 ASP N 160 61.01 69.23 REMARK 500 PRO O 549 166.47 -47.79 REMARK 500 SER P 32 -13.52 -153.72 REMARK 500 ALA P 52 -54.44 77.50 REMARK 500 ALA P 85 -178.02 -177.24 REMARK 500 PHE P 95 -32.52 80.24 REMARK 500 ASN P 141 66.52 62.68 REMARK 500 ALA Q 95 158.85 178.52 REMARK 500 PHE Q 111 -1.72 63.65 REMARK 500 ASP Q 160 62.42 66.56 REMARK 500 SER S 32 -20.64 -143.60 REMARK 500 ALA S 33 61.82 -68.49 REMARK 500 LEU S 48 -62.60 -96.81 REMARK 500 REMARK 500 THIS ENTRY HAS 66 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL