REMARK 2 REMARK 2 RESOLUTION. 3.26 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.26 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 109.50 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.7 REMARK 3 NUMBER OF REFLECTIONS : 103139 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.240 REMARK 3 R VALUE (WORKING SET) : 0.239 REMARK 3 FREE R VALUE : 0.270 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 5157 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1109.5572 - 10.1277 0.96 3686 227 0.3380 0.3353 REMARK 3 2 10.1277 - 8.0394 1.00 3630 196 0.2068 0.2072 REMARK 3 3 8.0394 - 7.0234 1.00 3570 183 0.2149 0.2404 REMARK 3 4 7.0234 - 6.3813 0.99 3524 184 0.2245 0.3080 REMARK 3 5 6.3813 - 5.9239 0.98 3466 192 0.2336 0.2679 REMARK 3 6 5.9239 - 5.5747 0.98 3465 177 0.2236 0.2946 REMARK 3 7 5.5747 - 5.2955 0.98 3481 167 0.2062 0.2437 REMARK 3 8 5.2955 - 5.0650 0.99 3458 181 0.1904 0.2058 REMARK 3 9 5.0650 - 4.8700 0.98 3394 200 0.1694 0.2054 REMARK 3 10 4.8700 - 4.7020 0.98 3430 176 0.1678 0.2092 REMARK 3 11 4.7020 - 4.5549 0.99 3407 181 0.1773 0.2217 REMARK 3 12 4.5549 - 4.4247 0.98 3419 178 0.1851 0.2245 REMARK 3 13 4.4247 - 4.3082 0.98 3403 178 0.1918 0.2405 REMARK 3 14 4.3082 - 4.2031 0.98 3387 167 0.2047 0.2197 REMARK 3 15 4.2031 - 4.1076 0.97 3340 189 0.2071 0.1968 REMARK 3 16 4.1076 - 4.0202 0.96 3349 168 0.2185 0.2729 REMARK 3 17 4.0202 - 3.9397 0.95 3303 162 0.2367 0.3038 REMARK 3 18 3.9397 - 3.8654 0.95 3248 195 0.2466 0.2577 REMARK 3 19 3.8654 - 3.7964 0.93 3206 152 0.2546 0.2595 REMARK 3 20 3.7964 - 3.7320 0.94 3285 170 0.2667 0.3256 REMARK 3 21 3.7320 - 3.6718 0.93 3152 169 0.2739 0.2979 REMARK 3 22 3.6718 - 3.6153 0.91 3149 156 0.2767 0.3367 REMARK 3 23 3.6153 - 3.5621 0.90 3105 152 0.2876 0.3379 REMARK 3 24 3.5621 - 3.5120 0.88 3031 133 0.2979 0.3755 REMARK 3 25 3.5120 - 3.4645 0.88 3017 161 0.3046 0.2931 REMARK 3 26 3.4645 - 3.4195 0.86 2930 164 0.3267 0.3718 REMARK 3 27 3.4195 - 3.3767 0.84 2885 157 0.3447 0.4049 REMARK 3 28 3.3767 - 3.3361 0.83 2882 151 0.3473 0.3602 REMARK 3 29 3.3361 - 3.2973 0.81 2745 146 0.3636 0.4054 REMARK 3 30 3.2973 - 3.2600 0.76 2635 145 0.3956 0.4237 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 0.50 REMARK 3 SHRINKAGE RADIUS : 0.16 REMARK 3 K_SOL : 0.34 REMARK 3 B_SOL : 68.03 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.380 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 77.30 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 87.10 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.00000 REMARK 3 B22 (A**2) : 0.00000 REMARK 3 B33 (A**2) : 0.00000 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 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.004 29997 REMARK 3 ANGLE : 0.746 40955 REMARK 3 CHIRALITY : 0.049 4800 REMARK 3 PLANARITY : 0.003 5047 REMARK 3 DIHEDRAL : 14.013 10776 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 20 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN A AND RESID 1:340 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.1593 74.0954 38.5376 REMARK 3 T TENSOR REMARK 3 T11: 0.1872 T22: 0.2268 REMARK 3 T33: 0.2560 T12: -0.0267 REMARK 3 T13: 0.0122 T23: 0.0803 REMARK 3 L TENSOR REMARK 3 L11: -0.0604 L22: 0.9224 REMARK 3 L33: 0.0637 L12: -0.0185 REMARK 3 L13: 0.0290 L23: -0.2864 REMARK 3 S TENSOR REMARK 3 S11: -0.0078 S12: 0.0521 S13: 0.0431 REMARK 3 S21: 0.0908 S22: 0.1281 S23: 0.1551 REMARK 3 S31: -0.0225 S32: -0.0304 S33: -0.1071 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN B AND (RESID 1:340 OR RESID 400:400 ) ) REMARK 3 ORIGIN FOR THE GROUP (A): 23.0170 71.4861 35.1664 REMARK 3 T TENSOR REMARK 3 T11: 0.3158 T22: 0.3876 REMARK 3 T33: 0.3054 T12: -0.0330 REMARK 3 T13: -0.0348 T23: -0.0149 REMARK 3 L TENSOR REMARK 3 L11: 0.2770 L22: 0.5083 REMARK 3 L33: 0.0328 L12: -0.0762 REMARK 3 L13: -0.2025 L23: -0.2064 REMARK 3 S TENSOR REMARK 3 S11: 0.0512 S12: 0.1034 S13: 0.0779 REMARK 3 S21: -0.0639 S22: 0.0563 S23: -0.0149 REMARK 3 S31: 0.0634 S32: 0.1422 S33: -0.1037 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN C AND (RESID 1:339 OR RESID 400:400 ) ) REMARK 3 ORIGIN FOR THE GROUP (A): 34.5374 80.9192 55.7957 REMARK 3 T TENSOR REMARK 3 T11: 0.3511 T22: 0.3992 REMARK 3 T33: 0.4448 T12: -0.0072 REMARK 3 T13: -0.0109 T23: -0.0981 REMARK 3 L TENSOR REMARK 3 L11: 0.1656 L22: 0.1924 REMARK 3 L33: 0.0324 L12: -0.1686 REMARK 3 L13: 0.0898 L23: -0.1005 REMARK 3 S TENSOR REMARK 3 S11: -0.0665 S12: -0.0910 S13: 0.0944 REMARK 3 S21: 0.0460 S22: 0.1090 S23: -0.2419 REMARK 3 S31: 0.0098 S32: 0.1738 S33: -0.0424 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN D AND RESID 1:340 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.6220 89.4005 71.7684 REMARK 3 T TENSOR REMARK 3 T11: 0.4387 T22: 0.2973 REMARK 3 T33: 0.3413 T12: 0.0141 REMARK 3 T13: 0.0170 T23: -0.0898 REMARK 3 L TENSOR REMARK 3 L11: 0.2527 L22: 0.4591 REMARK 3 L33: 0.2571 L12: 0.3587 REMARK 3 L13: -0.0286 L23: -0.4643 REMARK 3 S TENSOR REMARK 3 S11: 0.1097 S12: -0.1096 S13: 0.0760 REMARK 3 S21: 0.0804 S22: 0.0441 S23: 0.0949 REMARK 3 S31: -0.0535 S32: 0.0177 S33: -0.1714 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (CHAIN E AND (RESID 1:340 OR RESID 400:400 ) ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.2201 85.1528 61.1804 REMARK 3 T TENSOR REMARK 3 T11: 0.3575 T22: 0.2992 REMARK 3 T33: 0.3945 T12: 0.0631 REMARK 3 T13: 0.0888 T23: 0.0063 REMARK 3 L TENSOR REMARK 3 L11: 0.2031 L22: 0.5322 REMARK 3 L33: 0.0602 L12: 0.1454 REMARK 3 L13: 0.0035 L23: -0.0836 REMARK 3 S TENSOR REMARK 3 S11: 0.0124 S12: -0.0838 S13: 0.1597 REMARK 3 S21: 0.0868 S22: -0.0062 S23: 0.0527 REMARK 3 S31: -0.0632 S32: -0.0253 S33: -0.0017 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (CHAIN B AND RESID 348:348 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.1267 92.0047 21.4362 REMARK 3 T TENSOR REMARK 3 T11: 0.4236 T22: 0.5590 REMARK 3 T33: 0.5633 T12: -0.0695 REMARK 3 T13: 0.0909 T23: 0.0233 REMARK 3 L TENSOR REMARK 3 L11: 0.0638 L22: 0.0148 REMARK 3 L33: 0.0096 L12: 0.0066 REMARK 3 L13: 0.0080 L23: -0.0111 REMARK 3 S TENSOR REMARK 3 S11: 0.1186 S12: -0.0026 S13: 0.2014 REMARK 3 S21: -0.0060 S22: -0.0324 S23: 0.0551 REMARK 3 S31: 0.0022 S32: 0.0643 S33: -0.0784 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: (CHAIN B AND RESID 349:349 ) REMARK 3 ORIGIN FOR THE GROUP (A): 34.8857 96.8513 33.4540 REMARK 3 T TENSOR REMARK 3 T11: 0.4962 T22: 0.7821 REMARK 3 T33: 0.7519 T12: -0.1433 REMARK 3 T13: 0.0333 T23: -0.0072 REMARK 3 L TENSOR REMARK 3 L11: 0.0250 L22: 0.1812 REMARK 3 L33: 0.0695 L12: 0.0135 REMARK 3 L13: -0.0339 L23: 0.0081 REMARK 3 S TENSOR REMARK 3 S11: 0.0336 S12: -0.0432 S13: 0.0150 REMARK 3 S21: -0.0253 S22: -0.0406 S23: -0.0367 REMARK 3 S31: 0.0093 S32: -0.0019 S33: 0.0097 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: (CHAIN D AND RESID 348:348 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.7981 108.6446 57.3221 REMARK 3 T TENSOR REMARK 3 T11: 0.8941 T22: 0.4783 REMARK 3 T33: 0.5681 T12: -0.0014 REMARK 3 T13: -0.0406 T23: -0.0569 REMARK 3 L TENSOR REMARK 3 L11: 0.1028 L22: 0.1449 REMARK 3 L33: -0.0003 L12: 0.0946 REMARK 3 L13: 0.0031 L23: 0.0059 REMARK 3 S TENSOR REMARK 3 S11: 0.0377 S12: 0.0217 S13: 0.0337 REMARK 3 S21: 0.0036 S22: -0.0801 S23: -0.0233 REMARK 3 S31: -0.0132 S32: 0.0104 S33: 0.0263 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: (CHAIN D AND RESID 349:349 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.9265 111.0533 60.1049 REMARK 3 T TENSOR REMARK 3 T11: 0.6748 T22: 0.4657 REMARK 3 T33: 0.7286 T12: -0.0319 REMARK 3 T13: 0.1424 T23: -0.0255 REMARK 3 L TENSOR REMARK 3 L11: 0.0551 L22: 0.2258 REMARK 3 L33: 0.1307 L12: 0.0182 REMARK 3 L13: -0.0042 L23: 0.0726 REMARK 3 S TENSOR REMARK 3 S11: -0.0668 S12: -0.0151 S13: 0.1053 REMARK 3 S21: 0.0448 S22: -0.1763 S23: -0.0281 REMARK 3 S31: -0.0149 S32: 0.0177 S33: 0.2207 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: (CHAIN A AND RESID 348:348 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.6518 100.7471 37.8683 REMARK 3 T TENSOR REMARK 3 T11: 0.5593 T22: 0.7575 REMARK 3 T33: 0.6682 T12: -0.0023 REMARK 3 T13: -0.0249 T23: 0.1100 REMARK 3 L TENSOR REMARK 3 L11: 0.0466 L22: 0.0527 REMARK 3 L33: 0.1731 L12: 0.0419 REMARK 3 L13: -0.0876 L23: -0.0676 REMARK 3 S TENSOR REMARK 3 S11: 0.1159 S12: -0.0252 S13: -0.0317 REMARK 3 S21: -0.0087 S22: 0.0728 S23: 0.0737 REMARK 3 S31: -0.0195 S32: -0.0456 S33: -0.1626 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: (CHAIN N AND RESID 1:108 ) OR (CHAIN F AND RESID 1: REMARK 3 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): 52.9138 46.8182 33.1915 REMARK 3 T TENSOR REMARK 3 T11: 0.3727 T22: 0.6670 REMARK 3 T33: 0.6496 T12: 0.0263 REMARK 3 T13: -0.0063 T23: -0.1998 REMARK 3 L TENSOR REMARK 3 L11: 0.3490 L22: 0.5067 REMARK 3 L33: 0.8852 L12: 0.0125 REMARK 3 L13: -0.5812 L23: 0.1305 REMARK 3 S TENSOR REMARK 3 S11: 0.0155 S12: 0.4546 S13: -0.1577 REMARK 3 S21: -0.0103 S22: -0.0163 S23: -0.3179 REMARK 3 S31: -0.0011 S32: 0.1081 S33: -0.0221 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: (CHAIN N AND RESID 113:185 ) OR (CHAIN F AND RESID REMARK 3 126:221 ) REMARK 3 ORIGIN FOR THE GROUP (A): 83.0449 36.7442 23.4876 REMARK 3 T TENSOR REMARK 3 T11: 0.7715 T22: 0.9879 REMARK 3 T33: 1.0232 T12: -0.0665 REMARK 3 T13: 0.0405 T23: -0.0417 REMARK 3 L TENSOR REMARK 3 L11: 0.3927 L22: 0.6020 REMARK 3 L33: 0.9795 L12: -0.0470 REMARK 3 L13: -0.6218 L23: 0.1882 REMARK 3 S TENSOR REMARK 3 S11: -0.2922 S12: 0.2681 S13: -0.0984 REMARK 3 S21: -0.0071 S22: -0.1113 S23: -0.0031 REMARK 3 S31: 0.0172 S32: -0.5283 S33: 0.5138 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: (CHAIN K AND RESID 1:108 ) OR (CHAIN G AND RESID 1: REMARK 3 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): 54.6561 73.5066 87.5068 REMARK 3 T TENSOR REMARK 3 T11: 0.4339 T22: 0.7315 REMARK 3 T33: 0.5072 T12: 0.1613 REMARK 3 T13: -0.1272 T23: -0.2616 REMARK 3 L TENSOR REMARK 3 L11: 0.4148 L22: 0.4963 REMARK 3 L33: 1.1688 L12: 0.2973 REMARK 3 L13: 0.6719 L23: 0.4598 REMARK 3 S TENSOR REMARK 3 S11: -0.1637 S12: 0.2202 S13: -0.1893 REMARK 3 S21: -0.0301 S22: 0.3252 S23: -0.0913 REMARK 3 S31: -0.1028 S32: 0.4620 S33: -0.1359 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: (CHAIN K AND RESID 113:210 ) OR (CHAIN G AND RESID REMARK 3 126:221 ) REMARK 3 ORIGIN FOR THE GROUP (A): 76.5164 71.5759 110.5711 REMARK 3 T TENSOR REMARK 3 T11: 0.7454 T22: 0.4769 REMARK 3 T33: 0.7290 T12: 0.0322 REMARK 3 T13: -0.1704 T23: -0.0592 REMARK 3 L TENSOR REMARK 3 L11: 1.6422 L22: 0.1605 REMARK 3 L33: 1.4669 L12: 0.5326 REMARK 3 L13: -0.4039 L23: -0.3121 REMARK 3 S TENSOR REMARK 3 S11: -0.1634 S12: -0.2074 S13: -0.6012 REMARK 3 S21: 0.0290 S22: -0.1084 S23: -0.3723 REMARK 3 S31: -0.0205 S32: 0.0469 S33: 0.2746 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: (CHAIN H AND RESID 1:120 ) OR (CHAIN L AND RESID 1: REMARK 3 108 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.0424 41.8554 17.6646 REMARK 3 T TENSOR REMARK 3 T11: 0.3098 T22: 0.3972 REMARK 3 T33: 0.3924 T12: 0.0048 REMARK 3 T13: -0.0621 T23: -0.0323 REMARK 3 L TENSOR REMARK 3 L11: 0.9789 L22: 0.6820 REMARK 3 L33: 1.4492 L12: 0.5223 REMARK 3 L13: 0.3699 L23: 0.5977 REMARK 3 S TENSOR REMARK 3 S11: 0.0969 S12: 0.2008 S13: -0.2357 REMARK 3 S21: -0.0590 S22: -0.1379 S23: -0.0329 REMARK 3 S31: -0.1351 S32: -0.0183 S33: 0.0150 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: (CHAIN H AND RESID 126:221 ) OR (CHAIN L AND RESID REMARK 3 113:210 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.0919 20.4447 -7.3653 REMARK 3 T TENSOR REMARK 3 T11: 0.4886 T22: 0.6361 REMARK 3 T33: 0.6730 T12: -0.0532 REMARK 3 T13: -0.1074 T23: -0.2155 REMARK 3 L TENSOR REMARK 3 L11: 0.8010 L22: 0.5922 REMARK 3 L33: 0.1216 L12: 0.4573 REMARK 3 L13: 0.0003 L23: -0.0938 REMARK 3 S TENSOR REMARK 3 S11: 0.0105 S12: 0.3541 S13: -0.2818 REMARK 3 S21: 0.0251 S22: 0.1103 S23: -0.0388 REMARK 3 S31: 0.1108 S32: -0.1906 S33: -0.0685 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: (CHAIN I AND RESID 1:120 ) OR (CHAIN O AND RESID 1: REMARK 3 108 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.2351 84.0130 105.6171 REMARK 3 T TENSOR REMARK 3 T11: 0.6462 T22: 0.7400 REMARK 3 T33: 0.4734 T12: -0.1766 REMARK 3 T13: 0.1691 T23: -0.2027 REMARK 3 L TENSOR REMARK 3 L11: 0.5284 L22: 0.4375 REMARK 3 L33: 1.1596 L12: 0.0349 REMARK 3 L13: 0.2112 L23: 0.7179 REMARK 3 S TENSOR REMARK 3 S11: 0.3091 S12: -0.3169 S13: 0.1562 REMARK 3 S21: 0.1221 S22: -0.1993 S23: 0.0235 REMARK 3 S31: 0.2141 S32: 0.0464 S33: -0.1205 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: (CHAIN I AND RESID 126:221 ) OR (CHAIN O AND RESID REMARK 3 113:208 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.6662 84.7093 138.6892 REMARK 3 T TENSOR REMARK 3 T11: 1.1168 T22: 1.3487 REMARK 3 T33: 0.7712 T12: -0.3399 REMARK 3 T13: 0.2222 T23: -0.1451 REMARK 3 L TENSOR REMARK 3 L11: 1.3282 L22: 0.4308 REMARK 3 L33: 1.0071 L12: 0.1629 REMARK 3 L13: -1.1748 L23: -0.1349 REMARK 3 S TENSOR REMARK 3 S11: -0.1769 S12: -0.2931 S13: -0.0258 REMARK 3 S21: -0.0225 S22: 0.3680 S23: -0.0415 REMARK 3 S31: -0.2742 S32: 0.3494 S33: -0.2746 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: (CHAIN J AND RESID 1:120 ) OR (CHAIN M AND RESID 1: REMARK 3 108 ) REMARK 3 ORIGIN FOR THE GROUP (A): -38.7979 63.9626 62.0546 REMARK 3 T TENSOR REMARK 3 T11: 0.3555 T22: 0.3538 REMARK 3 T33: 0.4995 T12: -0.0131 REMARK 3 T13: 0.1331 T23: 0.0738 REMARK 3 L TENSOR REMARK 3 L11: 0.7185 L22: 0.1359 REMARK 3 L33: 0.3341 L12: 0.1724 REMARK 3 L13: 0.3495 L23: 0.2070 REMARK 3 S TENSOR REMARK 3 S11: 0.0046 S12: 0.0521 S13: 0.2095 REMARK 3 S21: 0.0091 S22: -0.0073 S23: 0.1603 REMARK 3 S31: -0.0064 S32: 0.0780 S33: 0.0304 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: (CHAIN J AND RESID 126:221 ) OR (CHAIN M AND RESID REMARK 3 113:210 ) REMARK 3 ORIGIN FOR THE GROUP (A): -68.4760 49.7970 65.6056 REMARK 3 T TENSOR REMARK 3 T11: 0.4660 T22: 0.5420 REMARK 3 T33: 0.8667 T12: 0.0915 REMARK 3 T13: 0.1061 T23: 0.0836 REMARK 3 L TENSOR REMARK 3 L11: -0.0001 L22: 1.6065 REMARK 3 L33: 1.6795 L12: -0.0787 REMARK 3 L13: -0.0516 L23: 1.0560 REMARK 3 S TENSOR REMARK 3 S11: -0.0518 S12: -0.0072 S13: 0.0255 REMARK 3 S21: 0.0494 S22: -0.2172 S23: 0.7315 REMARK 3 S31: 0.1345 S32: -0.2106 S33: 0.2997 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 4 REMARK 3 NCS GROUP : 1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: chain A and (resseq 1:340 ) and (not REMARK 3 element H) REMARK 3 SELECTION : chain B and (resseq 1:340 ) and (not REMARK 3 element H) REMARK 3 ATOM PAIRS NUMBER : 2716 REMARK 3 RMSD : 0.014 REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: chain A and (resseq 1:340 ) and (not REMARK 3 element H) REMARK 3 SELECTION : chain C and (resseq 1:339 ) and (not REMARK 3 element H) REMARK 3 ATOM PAIRS NUMBER : 2706 REMARK 3 RMSD : 0.016 REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: chain A and (resseq 1:340 ) and (not REMARK 3 element H) REMARK 3 SELECTION : chain D and (resseq 1:340 ) and (not REMARK 3 element H) REMARK 3 ATOM PAIRS NUMBER : 2716 REMARK 3 RMSD : 0.014 REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: chain A and (resseq 1:340 ) and (not REMARK 3 element H) REMARK 3 SELECTION : chain E and (resseq 1:340 ) and (not REMARK 3 element H) REMARK 3 ATOM PAIRS NUMBER : 2716 REMARK 3 RMSD : 0.016 REMARK 3 NCS GROUP : 2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: chain F and (resseq 1:120 ) and (not REMARK 3 element H) REMARK 3 SELECTION : chain G and (resseq 1:120 ) and (not REMARK 3 element H) REMARK 3 ATOM PAIRS NUMBER : 949 REMARK 3 RMSD : 0.025 REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: chain F and (resseq 1:120 ) and (not REMARK 3 element H) REMARK 3 SELECTION : chain H and (resseq 1:120 ) and (not REMARK 3 element H) REMARK 3 ATOM PAIRS NUMBER : 949 REMARK 3 RMSD : 0.014 REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: chain F and (resseq 1:120 ) and (not REMARK 3 element H) REMARK 3 SELECTION : chain I and (resseq 1:120 ) and (not REMARK 3 element H) REMARK 3 ATOM PAIRS NUMBER : 949 REMARK 3 RMSD : 0.010 REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: chain F and (resseq 1:120 ) and (not REMARK 3 element H) REMARK 3 SELECTION : chain J and (resseq 1:120 ) and (not REMARK 3 element H) REMARK 3 ATOM PAIRS NUMBER : 949 REMARK 3 RMSD : 0.012 REMARK 3 NCS GROUP : 3 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: chain K and (resseq 1:108 ) and (not REMARK 3 element H) REMARK 3 SELECTION : chain L and (resseq 1:108 ) and (not REMARK 3 element H) REMARK 3 ATOM PAIRS NUMBER : 804 REMARK 3 RMSD : 0.014 REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: chain K and (resseq 1:108 ) and (not REMARK 3 element H) REMARK 3 SELECTION : chain M and (resseq 1:108 ) and (not REMARK 3 element H) REMARK 3 ATOM PAIRS NUMBER : 804 REMARK 3 RMSD : 0.012 REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: chain K and (resseq 1:108 ) and (not REMARK 3 element H) REMARK 3 SELECTION : chain N and (resseq 1:108 ) and (not REMARK 3 element H) REMARK 3 ATOM PAIRS NUMBER : 804 REMARK 3 RMSD : 0.011 REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: chain K and (resseq 1:108 ) and (not REMARK 3 element H) REMARK 3 SELECTION : chain O and (resseq 1:108 ) and (not REMARK 3 element H) REMARK 3 ATOM PAIRS NUMBER : 804 REMARK 3 RMSD : 0.047 REMARK 3 NCS GROUP : 4 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: B348 REMARK 3 SELECTION : B349 REMARK 3 ATOM PAIRS NUMBER : 62 REMARK 3 RMSD : 0.009 REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: B348 REMARK 3 SELECTION : D348 REMARK 3 ATOM PAIRS NUMBER : 62 REMARK 3 RMSD : 0.009 REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: B348 REMARK 3 SELECTION : D349 REMARK 3 ATOM PAIRS NUMBER : 62 REMARK 3 RMSD : 0.010 REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: B348 REMARK 3 SELECTION : A348 REMARK 3 ATOM PAIRS NUMBER : 62 REMARK 3 RMSD : 0.009 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3RHW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-APR-11. REMARK 100 THE RCSB ID CODE IS RCSB064950. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-APR-10 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 24-ID-C REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979 REMARK 200 MONOCHROMATOR : CRYO-COOLED DOUBLE SI(111) REMARK 200 CRYSTAL MONOCHROMATOR REMARK 200 OPTICS : MIRRORS: BENT CYLINDERS, STRIPES REMARK 200 OF PT, RH AND CLEAR REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 REMARK 200 DATA SCALING SOFTWARE : XIA2 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 109734 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.260 REMARK 200 RESOLUTION RANGE LOW (A) : 110.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 7.200 REMARK 200 R MERGE (I) : 0.13800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.26 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.34 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.9 REMARK 200 DATA REDUNDANCY IN SHELL : 7.20 REMARK 200 R MERGE FOR SHELL (I) : 1.18300 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.700 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: HOMOLOGY MODEL DERIVED FROM PDB ENTRY 3EHZ REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 69.23 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.00 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 21-23% PEG 400, 50 MM SODIUM CITRATE REMARK 280 PH 4.5, 70 MM SODIUM CHLORIDE, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2 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 -Y+1/2,X+1/2,Z+3/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 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 287.30500 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 77.42500 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 77.42500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 430.95750 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 77.42500 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 77.42500 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 143.65250 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 77.42500 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 77.42500 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 430.95750 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 77.42500 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 77.42500 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 143.65250 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 287.30500 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTADECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, REMARK 350 AND CHAINS: J, K, L, 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 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 HIS A 341 REMARK 465 HIS A 342 REMARK 465 HIS A 343 REMARK 465 HIS A 344 REMARK 465 HIS A 345 REMARK 465 HIS A 346 REMARK 465 HIS A 347 REMARK 465 HIS B 341 REMARK 465 HIS B 342 REMARK 465 HIS B 343 REMARK 465 HIS B 344 REMARK 465 HIS B 345 REMARK 465 HIS B 346 REMARK 465 HIS B 347 REMARK 465 HIS C 340 REMARK 465 HIS C 341 REMARK 465 HIS C 342 REMARK 465 HIS C 343 REMARK 465 HIS C 344 REMARK 465 HIS C 345 REMARK 465 HIS C 346 REMARK 465 HIS C 347 REMARK 465 HIS D 341 REMARK 465 HIS D 342 REMARK 465 HIS D 343 REMARK 465 HIS D 344 REMARK 465 HIS D 345 REMARK 465 HIS D 346 REMARK 465 HIS D 347 REMARK 465 HIS E 341 REMARK 465 HIS E 342 REMARK 465 HIS E 343 REMARK 465 HIS E 344 REMARK 465 HIS E 345 REMARK 465 HIS E 346 REMARK 465 HIS E 347 REMARK 465 ALA F 134 REMARK 465 PRO F 135 REMARK 465 GLY F 136 REMARK 465 SER F 137 REMARK 465 ALA F 138 REMARK 465 ALA F 139 REMARK 465 GLN F 140 REMARK 465 THR F 141 REMARK 465 ASN F 142 REMARK 465 SER F 143 REMARK 465 MET F 144 REMARK 465 VAL F 145 REMARK 465 THR F 146 REMARK 465 LEU F 147 REMARK 465 GLY F 148 REMARK 465 SER F 188 REMARK 465 SER F 189 REMARK 465 VAL F 190 REMARK 465 THR F 191 REMARK 465 VAL F 192 REMARK 465 PRO F 193 REMARK 465 SER F 194 REMARK 465 SER F 195 REMARK 465 THR F 196 REMARK 465 TRP F 197 REMARK 465 PRO F 198 REMARK 465 SER F 199 REMARK 465 GLU F 200 REMARK 465 THR F 201 REMARK 465 VAL F 202 REMARK 465 GLY G 136 REMARK 465 SER G 137 REMARK 465 ALA G 138 REMARK 465 ALA G 139 REMARK 465 GLN G 140 REMARK 465 THR G 141 REMARK 465 ASN G 142 REMARK 465 SER G 143 REMARK 465 MET G 144 REMARK 465 VAL G 145 REMARK 465 THR G 146 REMARK 465 LEU G 147 REMARK 465 VAL G 192 REMARK 465 PRO G 193 REMARK 465 SER G 194 REMARK 465 SER G 195 REMARK 465 THR G 196 REMARK 465 TRP G 197 REMARK 465 PRO G 198 REMARK 465 SER G 199 REMARK 465 GLU G 200 REMARK 465 GLY I 136 REMARK 465 SER I 137 REMARK 465 ALA I 138 REMARK 465 ALA I 139 REMARK 465 GLN I 140 REMARK 465 THR I 141 REMARK 465 ASN I 142 REMARK 465 PHE I 155 REMARK 465 PRO I 156 REMARK 465 GLU I 157 REMARK 465 PRO I 158 REMARK 465 VAL I 159 REMARK 465 THR I 160 REMARK 465 VAL I 161 REMARK 465 THR I 162 REMARK 465 TRP I 163 REMARK 465 ASN I 164 REMARK 465 SER I 165 REMARK 465 GLY I 166 REMARK 465 SER I 167 REMARK 465 LEU I 168 REMARK 465 SER I 169 REMARK 465 ALA J 138 REMARK 465 ALA J 139 REMARK 465 GLN J 140 REMARK 465 THR J 141 REMARK 465 ASN J 142 REMARK 465 SER J 143 REMARK 465 ALA K 185 REMARK 465 ARG K 186 REMARK 465 ALA K 187 REMARK 465 TRP K 188 REMARK 465 GLU K 189 REMARK 465 ARG K 190 REMARK 465 HIS K 191 REMARK 465 SER K 192 REMARK 465 SER K 193 REMARK 465 TYR K 194 REMARK 465 SER K 195 REMARK 465 GLU N 126 REMARK 465 GLU N 127 REMARK 465 LEU N 128 REMARK 465 GLU N 129 REMARK 465 THR N 130 REMARK 465 ASN N 131 REMARK 465 LYS N 132 REMARK 465 ALA N 133 REMARK 465 THR N 148 REMARK 465 VAL N 149 REMARK 465 ASP N 150 REMARK 465 TRP N 151 REMARK 465 LYS N 152 REMARK 465 VAL N 153 REMARK 465 ASP N 154 REMARK 465 GLY N 155 REMARK 465 THR N 156 REMARK 465 PRO N 157 REMARK 465 VAL N 158 REMARK 465 ASN N 172 REMARK 465 ASN N 173 REMARK 465 LYS N 174 REMARK 465 TYR N 175 REMARK 465 MET N 176 REMARK 465 TYR N 180 REMARK 465 LEU N 181 REMARK 465 THR N 182 REMARK 465 ARG N 186 REMARK 465 ALA N 187 REMARK 465 TRP N 188 REMARK 465 GLU N 189 REMARK 465 ARG N 190 REMARK 465 HIS N 191 REMARK 465 SER N 192 REMARK 465 SER N 193 REMARK 465 TYR N 194 REMARK 465 SER N 195 REMARK 465 CYS N 196 REMARK 465 GLN N 197 REMARK 465 VAL N 198 REMARK 465 THR N 199 REMARK 465 HIS N 200 REMARK 465 GLU N 201 REMARK 465 GLY N 202 REMARK 465 HIS N 203 REMARK 465 THR N 204 REMARK 465 VAL N 205 REMARK 465 GLU N 206 REMARK 465 LYS N 207 REMARK 465 SER N 208 REMARK 465 LEU N 209 REMARK 465 SER N 210 REMARK 465 LYS O 152 REMARK 465 VAL O 153 REMARK 465 ASP O 154 REMARK 465 GLY O 155 REMARK 465 THR O 156 REMARK 465 PRO O 157 REMARK 465 VAL O 158 REMARK 465 THR O 159 REMARK 465 GLN O 160 REMARK 465 ARG O 190 REMARK 465 HIS O 191 REMARK 465 SER O 192 REMARK 465 SER O 193 REMARK 465 LEU O 209 REMARK 465 SER O 210 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 LYS A 69 CG CD CE NZ REMARK 470 LYS A 105 CG CD CE NZ REMARK 470 LYS B 69 CG CD CE NZ REMARK 470 LYS B 105 CG CD CE NZ REMARK 470 LYS C 69 CG CD CE NZ REMARK 470 LYS C 105 CG CD CE NZ REMARK 470 LYS D 69 CG CD CE NZ REMARK 470 LYS D 105 CG CD CE NZ REMARK 470 LYS E 69 CG CD CE NZ REMARK 470 LYS E 105 CG CD CE NZ REMARK 470 LYS G 214 CG CD CE NZ REMARK 470 MET J 144 CG SD CE REMARK 470 ARG M 186 CG CD NE CZ NH1 NH2 REMARK 470 GLU O 129 CG CD OE1 OE2 REMARK 470 LYS O 132 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 ND2 ASN C 185 C2 NAG C 400 1.89 REMARK 500 ND2 ASN B 185 C2 NAG B 400 2.00 REMARK 500 CG ASN C 185 C1 NAG C 400 2.16 REMARK 500 REMARK 500 REMARK: NULL 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 VAL O 3 CB VAL O 3 CG2 0.170 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 VAL O 3 CG1 - CB - CG2 ANGL. DEV. = 11.7 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 VAL A 68 -115.09 50.94 REMARK 500 ASP A 71 -0.25 61.86 REMARK 500 ASP A 104 -125.55 57.84 REMARK 500 MET A 139 65.40 -115.77 REMARK 500 SER A 166 72.94 40.32 REMARK 500 LEU A 220 -61.07 -129.58 REMARK 500 VAL B 68 -115.00 51.15 REMARK 500 ASP B 104 -125.88 58.20 REMARK 500 MET B 139 64.95 -115.53 REMARK 500 SER B 166 72.97 40.62 REMARK 500 LEU B 220 -60.33 -129.21 REMARK 500 VAL C 68 -115.25 50.99 REMARK 500 ASP C 104 -126.31 59.30 REMARK 500 MET C 139 65.25 -115.75 REMARK 500 SER C 166 73.02 40.81 REMARK 500 LEU C 220 -59.42 -129.22 REMARK 500 VAL D 68 -115.13 51.29 REMARK 500 ASP D 104 -126.98 58.98 REMARK 500 MET D 139 65.60 -115.66 REMARK 500 SER D 166 72.95 40.66 REMARK 500 LEU D 220 -60.40 -129.72 REMARK 500 VAL E 68 -115.05 50.98 REMARK 500 ASP E 104 -126.69 59.36 REMARK 500 MET E 139 65.54 -114.64 REMARK 500 SER E 166 73.02 40.52 REMARK 500 LEU E 220 -60.32 -129.07 REMARK 500 SER F 28 99.04 -63.78 REMARK 500 ASN F 44 -159.58 -82.70 REMARK 500 LYS F 65 103.52 -56.99 REMARK 500 ALA F 92 -169.87 -161.51 REMARK 500 ASP F 110 -100.65 -97.08 REMARK 500 SER F 167 -72.69 -51.81 REMARK 500 LEU F 168 99.32 -61.87 REMARK 500 VAL F 178 -155.72 -85.68 REMARK 500 SER G 28 99.14 -63.57 REMARK 500 ASN G 44 -159.41 -83.08 REMARK 500 LYS G 65 103.29 -56.91 REMARK 500 ASP G 110 -100.37 -97.33 REMARK 500 THR G 125 109.94 -54.73 REMARK 500 LEU G 168 92.83 -69.93 REMARK 500 ASP G 182 -2.12 80.20 REMARK 500 THR G 185 119.09 -162.38 REMARK 500 VAL G 202 118.02 -162.12 REMARK 500 SER H 28 99.04 -64.01 REMARK 500 ASN H 44 -159.61 -82.85 REMARK 500 LYS H 65 104.49 -57.13 REMARK 500 ASP H 110 -100.45 -97.11 REMARK 500 PHE H 155 141.83 -179.91 REMARK 500 LEU H 168 92.25 -63.56 REMARK 500 GLU H 200 -150.98 -100.26 REMARK 500 REMARK 500 THIS ENTRY HAS 126 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 LMT A 349 REMARK 610 LMT B 350 REMARK 610 LMT A 350 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 400 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 400 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 400 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IVM B 348 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IVM B 349 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IVM D 348 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IVM D 349 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IVM A 348 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT A 349 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT B 350 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT A 350 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OCT D 350 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OCT E 348 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OCT B 351 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UND B 352 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3RI5 RELATED DB: PDB REMARK 900 THE SAME PROTEIN BUT IN THE PRESENCE OF THE LIGAND REMARK 900 PICROTOXIN AND IN THE ABSENCE OF THE LIGAND GLUTAMATE REMARK 900 RELATED ID: 3RIA RELATED DB: PDB REMARK 900 THE SAME PROTEIN BUT IN THE PRESENCE OF IODIDE AND IN THE REMARK 900 ABSENCE OF THE LIGAND GLUTAMATE REMARK 900 RELATED ID: 3RIF RELATED DB: PDB