REMARK 2 REMARK 2 RESOLUTION. 3.39 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743) 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 : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.39 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.85 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 78.8 REMARK 3 NUMBER OF REFLECTIONS : 36404 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.261 REMARK 3 R VALUE (WORKING SET) : 0.260 REMARK 3 FREE R VALUE : 0.289 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1855 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 44.8571 - 7.9583 0.99 3619 173 0.2408 0.2712 REMARK 3 2 7.9583 - 6.3224 1.00 3430 192 0.2587 0.2881 REMARK 3 3 6.3224 - 5.5249 1.00 3401 178 0.2657 0.3559 REMARK 3 4 5.5249 - 5.0205 1.00 3365 196 0.2384 0.2758 REMARK 3 5 5.0205 - 4.6610 0.99 3360 159 0.2196 0.2515 REMARK 3 6 4.6610 - 4.3865 1.00 3342 175 0.2277 0.2435 REMARK 3 7 4.3865 - 4.1669 1.00 3311 178 0.2470 0.2510 REMARK 3 8 4.1669 - 3.9857 1.00 3324 174 0.2854 0.3122 REMARK 3 9 3.9857 - 3.8323 0.99 3298 198 0.3135 0.3267 REMARK 3 10 3.8323 - 3.7001 0.64 2128 105 0.3362 0.3450 REMARK 3 11 3.7001 - 3.5845 0.35 1149 71 0.3514 0.3041 REMARK 3 12 3.5845 - 3.4821 0.18 596 39 0.3794 0.4610 REMARK 3 13 3.4821 - 3.3904 0.07 226 17 0.4374 0.5115 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.83 REMARK 3 K_SOL : 0.29 REMARK 3 B_SOL : 28.70 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.840 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.640 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -10.04490 REMARK 3 B22 (A**2) : -10.04490 REMARK 3 B33 (A**2) : 20.08980 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 : 0.011 6201 REMARK 3 ANGLE : 1.674 8459 REMARK 3 CHIRALITY : 0.097 1031 REMARK 3 PLANARITY : 0.008 1062 REMARK 3 DIHEDRAL : 21.758 2138 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 19 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: chain 'A' and (resseq 18:50) REMARK 3 ORIGIN FOR THE GROUP (A): -27.3860 115.1749 -4.1543 REMARK 3 T TENSOR REMARK 3 T11: 0.5221 T22: 1.9083 REMARK 3 T33: 0.5707 T12: -0.2576 REMARK 3 T13: -0.0544 T23: -0.0188 REMARK 3 L TENSOR REMARK 3 L11: 4.9059 L22: 0.2571 REMARK 3 L33: 0.8975 L12: 0.0385 REMARK 3 L13: -1.1089 L23: -0.0503 REMARK 3 S TENSOR REMARK 3 S11: -0.0947 S12: -0.9621 S13: 0.1769 REMARK 3 S21: 0.0222 S22: -0.0908 S23: -0.5612 REMARK 3 S31: 0.0155 S32: 1.0737 S33: 0.0563 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: chain 'A' and (resseq 51:130) REMARK 3 ORIGIN FOR THE GROUP (A): 3.7017 117.2075 -25.6492 REMARK 3 T TENSOR REMARK 3 T11: 0.7718 T22: 2.3266 REMARK 3 T33: 0.9309 T12: -0.2332 REMARK 3 T13: 0.0770 T23: 0.1927 REMARK 3 L TENSOR REMARK 3 L11: 0.8077 L22: 2.7153 REMARK 3 L33: 5.4635 L12: 0.6115 REMARK 3 L13: -1.1589 L23: 0.9179 REMARK 3 S TENSOR REMARK 3 S11: 0.4723 S12: -0.4377 S13: 0.4955 REMARK 3 S21: 0.6452 S22: -0.2478 S23: -0.4831 REMARK 3 S31: -0.8636 S32: 0.5929 S33: -0.1116 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: chain 'A' and (resseq 131:288) REMARK 3 ORIGIN FOR THE GROUP (A): -3.0722 109.3912 -15.8382 REMARK 3 T TENSOR REMARK 3 T11: 0.3602 T22: 2.9904 REMARK 3 T33: 0.9247 T12: -0.3576 REMARK 3 T13: 0.1755 T23: 0.1284 REMARK 3 L TENSOR REMARK 3 L11: 1.8406 L22: 1.0642 REMARK 3 L33: 0.6005 L12: -0.4845 REMARK 3 L13: -1.1241 L23: 0.4800 REMARK 3 S TENSOR REMARK 3 S11: 0.0621 S12: -0.1418 S13: -0.3267 REMARK 3 S21: 0.1095 S22: 0.2443 S23: -0.6462 REMARK 3 S31: 0.3449 S32: 0.9651 S33: 0.0097 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: chain 'A' and (resseq 289:317) REMARK 3 ORIGIN FOR THE GROUP (A): -40.0832 128.5438 -2.6280 REMARK 3 T TENSOR REMARK 3 T11: 0.6618 T22: 1.6246 REMARK 3 T33: 0.6145 T12: -0.4014 REMARK 3 T13: 0.0400 T23: -0.0609 REMARK 3 L TENSOR REMARK 3 L11: 1.5077 L22: 2.6549 REMARK 3 L33: 3.4437 L12: 0.5026 REMARK 3 L13: 0.3150 L23: -0.2161 REMARK 3 S TENSOR REMARK 3 S11: -0.4729 S12: -0.2345 S13: 0.3080 REMARK 3 S21: 0.2561 S22: -0.0583 S23: -0.1432 REMARK 3 S31: -0.4405 S32: 0.7108 S33: 0.2925 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: chain 'A' and (resseq 318:351) REMARK 3 ORIGIN FOR THE GROUP (A): -27.1888 120.4279 -1.0831 REMARK 3 T TENSOR REMARK 3 T11: 0.8104 T22: 2.0272 REMARK 3 T33: 0.5587 T12: -0.4648 REMARK 3 T13: 0.0430 T23: -0.0543 REMARK 3 L TENSOR REMARK 3 L11: 5.3885 L22: 2.5198 REMARK 3 L33: 2.6371 L12: -1.8752 REMARK 3 L13: -2.1631 L23: 2.5480 REMARK 3 S TENSOR REMARK 3 S11: -0.2183 S12: -0.2541 S13: 0.3135 REMARK 3 S21: 0.2136 S22: -0.1054 S23: -0.5296 REMARK 3 S31: -0.3551 S32: 1.0752 S33: 0.0858 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: chain 'A' and (resseq 352:405) REMARK 3 ORIGIN FOR THE GROUP (A): -46.8546 125.3679 -9.9288 REMARK 3 T TENSOR REMARK 3 T11: 0.5291 T22: 1.4772 REMARK 3 T33: 0.0968 T12: -0.5466 REMARK 3 T13: -0.3632 T23: -0.1165 REMARK 3 L TENSOR REMARK 3 L11: 2.2842 L22: 1.5291 REMARK 3 L33: 4.1509 L12: 0.9240 REMARK 3 L13: 1.7727 L23: 1.6804 REMARK 3 S TENSOR REMARK 3 S11: 0.0355 S12: 0.0697 S13: 0.6373 REMARK 3 S21: 0.1004 S22: -0.0575 S23: 0.2462 REMARK 3 S31: -1.0043 S32: 0.2914 S33: 0.2272 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: chain 'A' and (resseq 406:432) REMARK 3 ORIGIN FOR THE GROUP (A): -45.3628 117.1043 -16.5084 REMARK 3 T TENSOR REMARK 3 T11: 0.5904 T22: 1.5388 REMARK 3 T33: 0.2999 T12: -0.4455 REMARK 3 T13: -0.3192 T23: -0.0501 REMARK 3 L TENSOR REMARK 3 L11: 5.2255 L22: 3.2815 REMARK 3 L33: 5.6055 L12: 0.8736 REMARK 3 L13: 0.6274 L23: 0.2249 REMARK 3 S TENSOR REMARK 3 S11: -0.0315 S12: 0.2514 S13: -0.0519 REMARK 3 S21: -0.1814 S22: -0.0316 S23: -0.6398 REMARK 3 S31: 0.1220 S32: 0.7949 S33: 0.0590 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: chain 'H' and (resseq 1:120) REMARK 3 ORIGIN FOR THE GROUP (A): -52.0292 114.7911 21.4105 REMARK 3 T TENSOR REMARK 3 T11: -0.3954 T22: 1.1951 REMARK 3 T33: 0.3467 T12: -0.9590 REMARK 3 T13: 0.0388 T23: -0.1005 REMARK 3 L TENSOR REMARK 3 L11: 3.5729 L22: 2.7144 REMARK 3 L33: 1.9225 L12: 1.3414 REMARK 3 L13: -1.8665 L23: -0.5645 REMARK 3 S TENSOR REMARK 3 S11: -0.0407 S12: -0.8114 S13: 0.2860 REMARK 3 S21: 0.1767 S22: 0.1318 S23: -0.2275 REMARK 3 S31: -1.2264 S32: 0.4052 S33: -0.1237 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: chain 'H' and (resseq 121:152) REMARK 3 ORIGIN FOR THE GROUP (A): -64.1051 91.1719 44.4523 REMARK 3 T TENSOR REMARK 3 T11: 0.9785 T22: 1.0908 REMARK 3 T33: 0.4637 T12: -0.6388 REMARK 3 T13: -0.0244 T23: 0.1917 REMARK 3 L TENSOR REMARK 3 L11: 6.2220 L22: 3.0399 REMARK 3 L33: 7.1552 L12: 0.6378 REMARK 3 L13: 0.5136 L23: -0.0942 REMARK 3 S TENSOR REMARK 3 S11: 0.2007 S12: -1.2884 S13: -1.3170 REMARK 3 S21: 1.3408 S22: 0.0885 S23: 0.5036 REMARK 3 S31: 1.3315 S32: -0.3138 S33: -0.2890 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: chain 'H' and (resseq 153:168) REMARK 3 ORIGIN FOR THE GROUP (A): -58.4829 98.9213 40.2823 REMARK 3 T TENSOR REMARK 3 T11: 0.3867 T22: 1.0533 REMARK 3 T33: 0.5737 T12: -0.7231 REMARK 3 T13: -0.0336 T23: 0.0066 REMARK 3 L TENSOR REMARK 3 L11: 5.4765 L22: 9.5974 REMARK 3 L33: 5.7480 L12: -0.6051 REMARK 3 L13: 1.0252 L23: -2.1083 REMARK 3 S TENSOR REMARK 3 S11: -0.0303 S12: -0.2710 S13: -0.1208 REMARK 3 S21: 0.4789 S22: -0.3305 S23: -0.5442 REMARK 3 S31: 0.4083 S32: 0.8564 S33: 0.0767 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: chain 'H' and (resseq 169:190) REMARK 3 ORIGIN FOR THE GROUP (A): -63.5834 93.8798 35.7809 REMARK 3 T TENSOR REMARK 3 T11: 0.6761 T22: 0.8712 REMARK 3 T33: 0.5624 T12: -0.7512 REMARK 3 T13: 0.1372 T23: 0.0059 REMARK 3 L TENSOR REMARK 3 L11: 2.0031 L22: 8.1059 REMARK 3 L33: 8.3865 L12: -4.3301 REMARK 3 L13: 6.3772 L23: -2.6254 REMARK 3 S TENSOR REMARK 3 S11: 0.3648 S12: 0.2396 S13: -0.4839 REMARK 3 S21: -0.0447 S22: -0.0424 S23: 0.0454 REMARK 3 S31: 0.3260 S32: 0.3159 S33: -0.0590 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: chain 'H' and (resseq 191:220) REMARK 3 ORIGIN FOR THE GROUP (A): -56.1965 94.2158 48.0385 REMARK 3 T TENSOR REMARK 3 T11: 0.8651 T22: 1.1689 REMARK 3 T33: 0.8238 T12: -0.4016 REMARK 3 T13: -0.1803 T23: 0.1269 REMARK 3 L TENSOR REMARK 3 L11: 5.3564 L22: 4.0520 REMARK 3 L33: 4.3053 L12: -0.4066 REMARK 3 L13: -0.2802 L23: 2.0479 REMARK 3 S TENSOR REMARK 3 S11: 0.3261 S12: -1.0622 S13: -0.4582 REMARK 3 S21: 1.4336 S22: -0.4310 S23: -1.0247 REMARK 3 S31: 0.8725 S32: 0.7027 S33: 0.0277 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: chain 'L' and (resseq 21:51) REMARK 3 ORIGIN FOR THE GROUP (A): -50.6365 96.9416 3.8955 REMARK 3 T TENSOR REMARK 3 T11: 0.6616 T22: 1.1118 REMARK 3 T33: 0.3779 T12: -0.4261 REMARK 3 T13: 0.1692 T23: -0.0755 REMARK 3 L TENSOR REMARK 3 L11: 4.6400 L22: 7.4523 REMARK 3 L33: 6.2243 L12: -0.0401 REMARK 3 L13: -0.1808 L23: -0.9978 REMARK 3 S TENSOR REMARK 3 S11: -0.3983 S12: 0.3864 S13: -0.0650 REMARK 3 S21: -1.3149 S22: 0.3702 S23: 0.2347 REMARK 3 S31: 0.7970 S32: 0.6251 S33: 0.1287 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: chain 'L' and (resseq 52:67) REMARK 3 ORIGIN FOR THE GROUP (A): -47.3033 98.8226 17.0394 REMARK 3 T TENSOR REMARK 3 T11: -0.0562 T22: 1.0463 REMARK 3 T33: 0.5551 T12: -0.6110 REMARK 3 T13: 0.3434 T23: 0.1449 REMARK 3 L TENSOR REMARK 3 L11: 6.7440 L22: 5.6789 REMARK 3 L33: 1.5394 L12: 1.5029 REMARK 3 L13: -2.3069 L23: 1.1264 REMARK 3 S TENSOR REMARK 3 S11: -0.0261 S12: -0.7573 S13: -0.0345 REMARK 3 S21: 0.4033 S22: 0.1060 S23: -0.0849 REMARK 3 S31: 0.3023 S32: 1.1256 S33: 0.0597 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: chain 'L' and (resseq 68:118) REMARK 3 ORIGIN FOR THE GROUP (A): -44.5327 97.9010 9.6709 REMARK 3 T TENSOR REMARK 3 T11: 0.6438 T22: 1.1483 REMARK 3 T33: 0.5045 T12: -0.2870 REMARK 3 T13: 0.1732 T23: -0.1737 REMARK 3 L TENSOR REMARK 3 L11: 2.2109 L22: 4.5027 REMARK 3 L33: 5.7519 L12: -0.1698 REMARK 3 L13: -1.3947 L23: -1.4596 REMARK 3 S TENSOR REMARK 3 S11: -0.3138 S12: -0.2244 S13: -0.1750 REMARK 3 S21: -0.3500 S22: 0.0731 S23: -0.7417 REMARK 3 S31: 0.7910 S32: 1.5170 S33: 0.2899 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: chain 'L' and (resseq 119:155) REMARK 3 ORIGIN FOR THE GROUP (A): -65.0205 85.9602 35.0687 REMARK 3 T TENSOR REMARK 3 T11: 1.0236 T22: 0.8868 REMARK 3 T33: 0.7009 T12: -0.8595 REMARK 3 T13: 0.4295 T23: 0.1312 REMARK 3 L TENSOR REMARK 3 L11: 2.9171 L22: 0.7596 REMARK 3 L33: 5.1237 L12: 0.2662 REMARK 3 L13: -2.3678 L23: -1.9377 REMARK 3 S TENSOR REMARK 3 S11: -0.1589 S12: -0.3171 S13: -0.3622 REMARK 3 S21: 0.5758 S22: -0.2651 S23: -0.0965 REMARK 3 S31: 1.1078 S32: 0.1564 S33: 0.3716 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: chain 'L' and (resseq 156:181) REMARK 3 ORIGIN FOR THE GROUP (A): -72.3404 81.7854 31.6890 REMARK 3 T TENSOR REMARK 3 T11: 1.4481 T22: 1.1497 REMARK 3 T33: 0.8257 T12: -0.6842 REMARK 3 T13: 0.0829 T23: -0.1750 REMARK 3 L TENSOR REMARK 3 L11: 5.5044 L22: 1.1358 REMARK 3 L33: 7.9870 L12: -1.2914 REMARK 3 L13: -4.1503 L23: 1.7511 REMARK 3 S TENSOR REMARK 3 S11: -0.4484 S12: 0.2261 S13: -1.1416 REMARK 3 S21: 0.0812 S22: -0.1368 S23: 0.1965 REMARK 3 S31: 0.8642 S32: -0.9498 S33: 0.7117 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: chain 'L' and (resseq 182:210) REMARK 3 ORIGIN FOR THE GROUP (A): -70.2908 85.6356 36.7742 REMARK 3 T TENSOR REMARK 3 T11: 1.2794 T22: 0.9572 REMARK 3 T33: 0.7486 T12: -0.4971 REMARK 3 T13: 0.1648 T23: -0.0282 REMARK 3 L TENSOR REMARK 3 L11: 3.8594 L22: 1.6938 REMARK 3 L33: 6.2847 L12: -0.9777 REMARK 3 L13: -2.1043 L23: 1.3651 REMARK 3 S TENSOR REMARK 3 S11: -0.2583 S12: -0.3894 S13: -0.6054 REMARK 3 S21: 0.1327 S22: -0.2486 S23: 0.0304 REMARK 3 S31: 0.2746 S32: -0.3342 S33: 0.3316 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: chain 'L' and (resseq 211:233) REMARK 3 ORIGIN FOR THE GROUP (A): -70.2763 77.2105 39.9931 REMARK 3 T TENSOR REMARK 3 T11: 1.6605 T22: 0.9236 REMARK 3 T33: 0.9488 T12: -0.4977 REMARK 3 T13: 0.2134 T23: 0.0811 REMARK 3 L TENSOR REMARK 3 L11: 9.5954 L22: 2.0196 REMARK 3 L33: 0.2971 L12: 2.1076 REMARK 3 L13: -0.0377 L23: -1.7405 REMARK 3 S TENSOR REMARK 3 S11: -0.0847 S12: -0.3284 S13: -0.8648 REMARK 3 S21: 0.7733 S22: 0.1758 S23: 0.8132 REMARK 3 S31: 2.1780 S32: -1.3219 S33: -0.1469 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 4DAG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JAN-12. REMARK 100 THE RCSB ID CODE IS RCSB070084. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-OCT-08 REMARK 200 TEMPERATURE (KELVIN) : 112 REMARK 200 PH : 5.6 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 8.3.1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000 REMARK 200 MONOCHROMATOR : DOUBLE FLAT CRYSTAL, SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36420 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200 REMARK 200 RESOLUTION RANGE LOW (A) : 224.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 72.7 REMARK 200 DATA REDUNDANCY : 6.000 REMARK 200 R MERGE (I) : 0.17900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR REMARK 200 SOFTWARE USED: SHARP REMARK 200 STARTING MODEL: B20-4 FAB MODEL, PDB ENTRY 2FJH REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 5000 MME, 15% GLYCEROL, 100 MM REMARK 280 CITRATE PH 5.6. CRYSTALS APPEARED AFTER 7-15 DAYS WITH TWO REMARK 280 DISTINCT MORPHOLOGIES: A SQUARE-LIKE CRYSTAL AND A LONGER, REMARK 280 POINTED CRYSTAL FORM., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+1/2 REMARK 290 6555 X-Y,X,Z+1/2 REMARK 290 7555 Y,X,-Z REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,-Z REMARK 290 10555 -Y,-X,-Z+1/2 REMARK 290 11555 -X+Y,Y,-Z+1/2 REMARK 290 12555 X,X-Y,-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 -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 0.00000 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 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 83.68000 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 83.68000 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 83.68000 REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 83.68000 REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 83.68000 REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 83.68000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 300 REMARK: DS7 HEAVY CHAIN H RESIDUES 1-220 REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7000 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 40930 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 16590 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 79270 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 0.00000 REMARK 350 BIOMT3 2 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 ILE A 95 REMARK 465 GLU A 96 REMARK 465 ASN A 97 REMARK 465 PRO A 98 REMARK 465 ARG A 99 REMARK 465 GLN A 100 REMARK 465 SER A 101 REMARK 465 ARG A 102 REMARK 465 PHE A 103 REMARK 465 VAL A 104 REMARK 465 LEU A 105 REMARK 465 GLY A 106 REMARK 465 ALA A 107 REMARK 465 ILE A 108 REMARK 465 ALA A 109 REMARK 465 LEU A 110 REMARK 465 GLY A 111 REMARK 465 VAL A 112 REMARK 465 ALA A 113 REMARK 465 LEU A 165 REMARK 465 LYS A 166 REMARK 465 GLU A 167 REMARK 465 PHE A 168 REMARK 465 VAL A 169 REMARK 465 SER A 170 REMARK 465 LYS A 171 REMARK 465 ASN A 172 REMARK 465 LEU A 173 REMARK 465 THR A 174 REMARK 465 SER A 175 REMARK 465 ALA A 176 REMARK 465 ILE A 177 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 PHE A 48 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR A 49 OG1 CG2 REMARK 470 LEU A 50 CG CD1 CD2 REMARK 470 GLU A 51 CG CD OE1 OE2 REMARK 470 LYS A 75 CG CD CE NZ REMARK 470 GLU A 80 CG CD OE1 OE2 REMARK 470 LYS A 82 CG CD CE NZ REMARK 470 ASP A 87 CG OD1 OD2 REMARK 470 GLN A 88 CG CD OE1 NE2 REMARK 470 GLU A 93 CG CD OE1 OE2 REMARK 470 LYS A 126 CG CD CE NZ REMARK 470 LYS A 138 CG CD CE NZ REMARK 470 LEU A 141 CG CD1 CD2 REMARK 470 LYS A 142 CG CD CE NZ REMARK 470 LEU A 158 CG CD1 CD2 REMARK 470 THR A 160 OG1 CG2 REMARK 470 GLU A 164 CG CD OE1 OE2 REMARK 470 ASP A 186 CG OD1 OD2 REMARK 470 GLN A 195 CG CD OE1 NE2 REMARK 470 ARG A 198 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 199 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 209 CG OD1 OD2 REMARK 470 MET A 222 CG SD CE REMARK 470 LYS A 242 CG CD CE NZ REMARK 470 GLU A 246 CG CD OE1 OE2 REMARK 470 LYS A 254 CG CD CE NZ REMARK 470 PHE A 256 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU A 259 CG CD1 CD2 REMARK 470 ILE A 260 CG1 CG2 CD1 REMARK 470 ILE A 268 CG1 CG2 CD1 REMARK 470 SER A 293 OG REMARK 470 GLU A 294 CG CD OE1 OE2 REMARK 470 GLU A 305 CG CD OE1 OE2 REMARK 470 LYS A 324 CG CD CE NZ REMARK 470 ASP A 325 CG OD1 OD2 REMARK 470 GLU A 327 CG CD OE1 OE2 REMARK 470 ARG A 329 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 367 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 405 CG CD CE NZ REMARK 470 ILE A 420 CG1 CG2 CD1 REMARK 470 ASP A 421 CG OD1 OD2 REMARK 470 ASN A 422 CG OD1 ND2 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 SG CYS H 149 CB CYS H 205 1.48 REMARK 500 O PRO H 132 OG SER L 141 1.91 REMARK 500 OG SER L 71 O GLY L 83 1.92 REMARK 500 O LEU L 47 N LYS L 50 1.97 REMARK 500 SG CYS A 283 CB CYS A 311 2.02 REMARK 500 OG SER A 27 OG SER A 29 2.04 REMARK 500 SG CYS A 384 CB CYS A 390 2.07 REMARK 500 SG CYS A 292 CB CYS A 301 2.08 REMARK 500 OE2 GLU A 33 NH2 ARG H 101 2.11 REMARK 500 OG SER A 237 OE1 GLN A 240 2.11 REMARK 500 O2 BMA A 503 O5 MAN A 505 2.12 REMARK 500 O GLY H 143 N SER H 195 2.14 REMARK 500 ND2 ASN A 57 C2 NAG A 501 2.15 REMARK 500 O VAL A 118 N ILE A 122 2.19 REMARK 500 OH TYR H 33 O GLY H 104 2.19 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 GLY L 118 N - CA - C ANGL. DEV. = -16.1 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 THR A 41 -70.40 -117.28 REMARK 500 PRO A 64 45.69 -83.79 REMARK 500 LYS A 68 -138.67 48.07 REMARK 500 THR A 69 -118.02 56.21 REMARK 500 GLU A 70 18.75 57.64 REMARK 500 ASP A 87 -73.29 -114.84 REMARK 500 LEU A 89 -72.09 -104.81 REMARK 500 ALA A 117 -74.37 -113.73 REMARK 500 ALA A 136 -122.69 62.65 REMARK 500 LEU A 141 -75.00 -58.29 REMARK 500 THR A 143 -131.48 48.00 REMARK 500 LYS A 179 65.92 62.12 REMARK 500 ALA A 185 167.39 173.64 REMARK 500 MET A 189 -77.01 -46.94 REMARK 500 SER A 194 170.73 171.41 REMARK 500 GLN A 195 13.63 56.72 REMARK 500 ALA A 211 60.33 60.39 REMARK 500 THR A 236 -67.77 -130.87 REMARK 500 VAL A 262 -66.72 -129.96 REMARK 500 TYR A 263 -140.62 54.57 REMARK 500 GLU A 294 74.85 50.38 REMARK 500 ASP A 325 -11.35 78.99 REMARK 500 LYS A 386 -137.87 54.09 REMARK 500 ILE A 392 -168.91 -122.97 REMARK 500 ILE A 400 -58.28 -120.86 REMARK 500 ASP A 416 -69.53 -128.05 REMARK 500 ASP A 421 68.92 73.55 REMARK 500 THR H 28 -173.55 -69.28 REMARK 500 SER H 49 165.38 178.47 REMARK 500 SER H 53 -2.67 74.35 REMARK 500 ARG H 66 -72.49 -115.02 REMARK 500 SER H 74 -63.32 -125.08 REMARK 500 ARG H 101 -121.79 61.28 REMARK 500 ALA H 102 -60.92 -125.40 REMARK 500 ASP H 107 -80.07 -123.00 REMARK 500 SER H 141 -75.66 -47.60 REMARK 500 ASP H 153 72.71 44.16 REMARK 500 ASN H 164 -128.40 52.55 REMARK 500 SER H 170 -177.53 -67.62 REMARK 500 THR H 200 -65.53 -93.82 REMARK 500 ASP L 45 -132.49 35.05 REMARK 500 TYR L 68 -80.82 -115.81 REMARK 500 ASP L 70 155.47 173.03 REMARK 500 THR L 97 71.54 48.98 REMARK 500 ALA L 103 -178.72 -170.91 REMARK 500 SER L 112 -122.97 44.06 REMARK 500 THR L 114 158.95 175.38 REMARK 500 SER L 157 159.40 179.48 REMARK 500 TYR L 160 142.20 -178.97 REMARK 500 HIS L 217 -78.01 -103.87 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 LEU A 66 ILE A 67 141.29 REMARK 500 LYS A 68 THR A 69 -144.32 REMARK 500 ILE A 137 LYS A 138 -147.20 REMARK 500 ASN A 145 GLU A 146 148.74 REMARK 500 ALA A 185 ASP A 186 149.79 REMARK 500 GLN A 195 PHE A 196 145.16 REMARK 500 SER A 293 GLU A 294 144.36 REMARK 500 ILE A 420 ASP A 421 -141.12 REMARK 500 GLN L 69 ASP L 70 143.06 REMARK 500 GLY L 120 THR L 121 -138.25 REMARK 500 LEU L 126 GLY L 127 -31.15 REMARK 500 THR L 229 GLU L 230 148.23 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 NAG A 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 502 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 503 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 504 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 505 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 506 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 507 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 508 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 509 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 510