HEADER IMMUNE SYSTEM 11-FEB-25 9IAT TITLE BC8.121 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: BC8.121-FAB_IGH; COMPND 3 CHAIN: B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: BC8.121-FAB_IGL; COMPND 7 CHAIN: A; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS FAB-ANTIGEN COMPLEX, HBV, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR A.E.MECHALY,A.HAOUZ,M.BERETTA,C.CAILLET-SAGUY,H.MOUQUET REVDAT 1 26-NOV-25 9IAT 0 JRNL AUTH M.BERETTA,A.HAOUZ,A.E.MECHALY,C.CAILLET-SAGUY,C.PLANCHAIS, JRNL AUTH 2 N.SZERMAN,Y.ARONTHIPPAITOON,M.-N.UNGEHEUER,S.POL, JRNL AUTH 3 C.GAUDY-GRAFFIN,C.SUREAU,M.BOURGINE,H.MOUQUET JRNL TITL IN VIVO EFFICACY OF HUMAN ANTI-PRES2 HBV NEUTRALIZING JRNL TITL 2 ANTIBODIES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.54 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21.2_5419 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.54 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.72 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1 REMARK 3 NUMBER OF REFLECTIONS : 69528 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.201 REMARK 3 R VALUE (WORKING SET) : 0.199 REMARK 3 FREE R VALUE : 0.232 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990 REMARK 3 FREE R VALUE TEST SET COUNT : 3470 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 39.7200 - 4.5000 1.00 2866 163 0.1514 0.1714 REMARK 3 2 4.5000 - 3.5800 1.00 2749 159 0.1484 0.1893 REMARK 3 3 3.5800 - 3.1200 1.00 2717 157 0.1784 0.2230 REMARK 3 4 3.1200 - 2.8400 1.00 2679 147 0.1976 0.2178 REMARK 3 5 2.8400 - 2.6300 1.00 2712 136 0.2127 0.2303 REMARK 3 6 2.6300 - 2.4800 1.00 2688 123 0.2200 0.2576 REMARK 3 7 2.4800 - 2.3600 1.00 2686 131 0.2158 0.2944 REMARK 3 8 2.3600 - 2.2500 0.98 2601 154 0.2313 0.2618 REMARK 3 9 2.2500 - 2.1700 0.98 2616 139 0.2396 0.2944 REMARK 3 10 2.1700 - 2.0900 1.00 2614 165 0.2280 0.2476 REMARK 3 11 2.0900 - 2.0300 1.00 2671 121 0.2309 0.2867 REMARK 3 12 2.0300 - 1.9700 1.00 2672 115 0.2252 0.2901 REMARK 3 13 1.9700 - 1.9200 0.97 2595 135 0.2548 0.2732 REMARK 3 14 1.9200 - 1.8700 0.97 2581 111 0.2788 0.2984 REMARK 3 15 1.8700 - 1.8300 1.00 2627 155 0.2346 0.2714 REMARK 3 16 1.8300 - 1.7900 1.00 2651 134 0.2561 0.3058 REMARK 3 17 1.7900 - 1.7500 1.00 2637 139 0.2689 0.2596 REMARK 3 18 1.7500 - 1.7200 1.00 2605 165 0.2843 0.3228 REMARK 3 19 1.7200 - 1.6900 1.00 2609 160 0.3016 0.3474 REMARK 3 20 1.6900 - 1.6600 1.00 2658 127 0.2948 0.3445 REMARK 3 21 1.6600 - 1.6300 1.00 2652 118 0.3027 0.3242 REMARK 3 22 1.6300 - 1.6100 1.00 2631 137 0.2958 0.3251 REMARK 3 23 1.6100 - 1.5800 0.99 2626 128 0.3037 0.3330 REMARK 3 24 1.5800 - 1.5600 0.97 2593 104 0.3070 0.3326 REMARK 3 25 1.5600 - 1.5400 0.90 2322 147 0.3315 0.3502 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 : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.239 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.434 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 29.08 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.35 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL 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 : 0.006 3313 REMARK 3 ANGLE : 0.843 4519 REMARK 3 CHIRALITY : 0.054 512 REMARK 3 PLANARITY : 0.006 580 REMARK 3 DIHEDRAL : 15.963 1177 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 15 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.4035 -20.1223 6.2114 REMARK 3 T TENSOR REMARK 3 T11: 0.1181 T22: 0.9629 REMARK 3 T33: 0.4141 T12: 0.1979 REMARK 3 T13: -0.1685 T23: -0.3051 REMARK 3 L TENSOR REMARK 3 L11: 4.1945 L22: 1.6157 REMARK 3 L33: 5.5756 L12: 0.6992 REMARK 3 L13: 4.4994 L23: 1.8600 REMARK 3 S TENSOR REMARK 3 S11: 0.0632 S12: -0.0879 S13: -0.2773 REMARK 3 S21: 0.0794 S22: -0.8948 S23: 0.7964 REMARK 3 S31: 0.2809 S32: -1.7154 S33: -0.6623 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 18 THROUGH 73 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.3659 -11.5136 8.9541 REMARK 3 T TENSOR REMARK 3 T11: 0.2673 T22: 0.4715 REMARK 3 T33: 0.2205 T12: 0.1552 REMARK 3 T13: 0.0015 T23: 0.0001 REMARK 3 L TENSOR REMARK 3 L11: 1.1853 L22: 2.3720 REMARK 3 L33: 3.6064 L12: 0.3368 REMARK 3 L13: 0.3180 L23: 2.4497 REMARK 3 S TENSOR REMARK 3 S11: 0.2751 S12: 0.0479 S13: 0.1047 REMARK 3 S21: -0.3285 S22: -0.5138 S23: 0.0692 REMARK 3 S31: -0.5439 S32: -0.8870 S33: 0.2617 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 74 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.8079 -17.9365 3.3461 REMARK 3 T TENSOR REMARK 3 T11: 0.2683 T22: 0.6360 REMARK 3 T33: 0.2424 T12: 0.2042 REMARK 3 T13: -0.0558 T23: -0.0349 REMARK 3 L TENSOR REMARK 3 L11: 0.3612 L22: 1.9938 REMARK 3 L33: 2.2430 L12: 1.2420 REMARK 3 L13: 1.5287 L23: 2.2777 REMARK 3 S TENSOR REMARK 3 S11: 0.1898 S12: -0.2429 S13: 0.1072 REMARK 3 S21: -0.4281 S22: -0.4641 S23: 0.2376 REMARK 3 S31: -0.6434 S32: -1.0408 S33: 0.3477 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 120 THROUGH 134 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.7159 -34.7911 -34.5499 REMARK 3 T TENSOR REMARK 3 T11: 0.4119 T22: 0.5148 REMARK 3 T33: 0.5039 T12: 0.0648 REMARK 3 T13: 0.1463 T23: 0.0263 REMARK 3 L TENSOR REMARK 3 L11: 1.8285 L22: 3.3727 REMARK 3 L33: 3.6980 L12: 1.1889 REMARK 3 L13: 2.2651 L23: 0.0240 REMARK 3 S TENSOR REMARK 3 S11: 0.2118 S12: 0.8607 S13: -0.0307 REMARK 3 S21: -0.9078 S22: 0.0272 S23: -0.9841 REMARK 3 S31: -0.1801 S32: 0.8503 S33: -0.3282 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 135 THROUGH 216 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.4915 -36.9101 -24.4236 REMARK 3 T TENSOR REMARK 3 T11: 0.2281 T22: 0.2431 REMARK 3 T33: 0.2712 T12: 0.0247 REMARK 3 T13: 0.0015 T23: 0.0701 REMARK 3 L TENSOR REMARK 3 L11: 1.7401 L22: 2.4224 REMARK 3 L33: 3.7588 L12: 0.0279 REMARK 3 L13: -0.2817 L23: 1.2427 REMARK 3 S TENSOR REMARK 3 S11: 0.0395 S12: 0.0440 S13: 0.1123 REMARK 3 S21: -0.0995 S22: 0.0862 S23: -0.1438 REMARK 3 S31: -0.1242 S32: -0.1284 S33: -0.1041 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 23 ) REMARK 3 ORIGIN FOR THE GROUP (A): 31.1552 -24.8194 -2.6065 REMARK 3 T TENSOR REMARK 3 T11: 0.2036 T22: 0.2474 REMARK 3 T33: 0.3548 T12: 0.0256 REMARK 3 T13: 0.0395 T23: 0.0107 REMARK 3 L TENSOR REMARK 3 L11: 1.0193 L22: 1.9920 REMARK 3 L33: 3.1968 L12: 0.7455 REMARK 3 L13: -0.3622 L23: 0.6418 REMARK 3 S TENSOR REMARK 3 S11: 0.2294 S12: 0.1065 S13: 0.1059 REMARK 3 S21: -0.1978 S22: 0.0622 S23: -0.3505 REMARK 3 S31: -0.1539 S32: 0.1188 S33: -0.1644 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 24 THROUGH 49 ) REMARK 3 ORIGIN FOR THE GROUP (A): 24.2485 -18.3900 5.6019 REMARK 3 T TENSOR REMARK 3 T11: 0.2028 T22: 0.2011 REMARK 3 T33: 0.3238 T12: 0.0367 REMARK 3 T13: 0.0515 T23: 0.0114 REMARK 3 L TENSOR REMARK 3 L11: 1.8519 L22: 1.7153 REMARK 3 L33: 3.6999 L12: -0.1250 REMARK 3 L13: -0.0543 L23: 0.3578 REMARK 3 S TENSOR REMARK 3 S11: 0.3594 S12: 0.0688 S13: 0.1985 REMARK 3 S21: -0.0404 S22: -0.0893 S23: -0.2528 REMARK 3 S31: -0.3229 S32: -0.0973 S33: -0.0794 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 50 THROUGH 62 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.5556 -24.1143 14.3051 REMARK 3 T TENSOR REMARK 3 T11: 0.2711 T22: 0.2607 REMARK 3 T33: 0.3224 T12: 0.0363 REMARK 3 T13: -0.0299 T23: 0.0022 REMARK 3 L TENSOR REMARK 3 L11: 1.4130 L22: 2.2992 REMARK 3 L33: 3.2191 L12: 0.1608 REMARK 3 L13: 0.2627 L23: 1.3621 REMARK 3 S TENSOR REMARK 3 S11: 0.1069 S12: -0.3106 S13: 0.0897 REMARK 3 S21: 0.3863 S22: 0.0987 S23: -0.1905 REMARK 3 S31: 0.2805 S32: 0.1552 S33: -0.1556 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 63 THROUGH 76 ) REMARK 3 ORIGIN FOR THE GROUP (A): 34.1840 -19.7615 5.2912 REMARK 3 T TENSOR REMARK 3 T11: 0.2204 T22: 0.2552 REMARK 3 T33: 0.4038 T12: -0.0040 REMARK 3 T13: 0.0509 T23: -0.0410 REMARK 3 L TENSOR REMARK 3 L11: 0.8255 L22: 5.0379 REMARK 3 L33: 3.4008 L12: 0.8396 REMARK 3 L13: 0.1900 L23: -1.6091 REMARK 3 S TENSOR REMARK 3 S11: 0.1781 S12: 0.1673 S13: 0.1265 REMARK 3 S21: 0.0894 S22: 0.1166 S23: -0.3528 REMARK 3 S31: -0.3036 S32: 0.2841 S33: -0.1513 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 77 THROUGH 93 ) REMARK 3 ORIGIN FOR THE GROUP (A): 25.7768 -26.1747 3.5319 REMARK 3 T TENSOR REMARK 3 T11: 0.1854 T22: 0.2490 REMARK 3 T33: 0.2947 T12: 0.0178 REMARK 3 T13: 0.0173 T23: 0.0261 REMARK 3 L TENSOR REMARK 3 L11: 1.1082 L22: 2.5905 REMARK 3 L33: 2.8349 L12: -0.3609 REMARK 3 L13: -0.4287 L23: 1.0597 REMARK 3 S TENSOR REMARK 3 S11: 0.1557 S12: 0.0516 S13: -0.0354 REMARK 3 S21: -0.1566 S22: -0.0313 S23: 0.0358 REMARK 3 S31: 0.1018 S32: -0.0324 S33: -0.1514 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 94 THROUGH 117 ) REMARK 3 ORIGIN FOR THE GROUP (A): 25.5995 -24.7484 -4.3118 REMARK 3 T TENSOR REMARK 3 T11: 0.1820 T22: 0.2448 REMARK 3 T33: 0.2686 T12: 0.0330 REMARK 3 T13: 0.0089 T23: 0.0374 REMARK 3 L TENSOR REMARK 3 L11: 0.8309 L22: 0.2581 REMARK 3 L33: 2.3176 L12: -0.0046 REMARK 3 L13: -0.6466 L23: 0.0532 REMARK 3 S TENSOR REMARK 3 S11: 0.0992 S12: 0.1026 S13: 0.0983 REMARK 3 S21: -0.0470 S22: 0.0463 S23: -0.0533 REMARK 3 S31: -0.1559 S32: -0.0997 S33: -0.1474 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 118 THROUGH 133 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.8635 -25.6988 -30.9801 REMARK 3 T TENSOR REMARK 3 T11: 0.2776 T22: 0.3158 REMARK 3 T33: 0.3083 T12: -0.0088 REMARK 3 T13: -0.0423 T23: 0.0674 REMARK 3 L TENSOR REMARK 3 L11: 4.9979 L22: 2.1511 REMARK 3 L33: 3.7590 L12: -1.2665 REMARK 3 L13: 1.9222 L23: -0.3290 REMARK 3 S TENSOR REMARK 3 S11: 0.1365 S12: 0.5517 S13: 0.2712 REMARK 3 S21: -0.3695 S22: -0.1406 S23: 0.1532 REMARK 3 S31: -0.1047 S32: -0.2101 S33: -0.0160 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 134 THROUGH 154 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.4342 -27.6239 -19.8332 REMARK 3 T TENSOR REMARK 3 T11: 0.2270 T22: 0.2634 REMARK 3 T33: 0.3129 T12: 0.0125 REMARK 3 T13: 0.0263 T23: 0.0404 REMARK 3 L TENSOR REMARK 3 L11: 1.3437 L22: 2.1123 REMARK 3 L33: 3.1432 L12: -0.6833 REMARK 3 L13: 0.8234 L23: -0.3908 REMARK 3 S TENSOR REMARK 3 S11: 0.0066 S12: 0.1966 S13: 0.1269 REMARK 3 S21: 0.0120 S22: 0.0193 S23: 0.0232 REMARK 3 S31: -0.2012 S32: 0.1761 S33: -0.0705 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 155 THROUGH 191 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.5912 -24.5142 -21.5313 REMARK 3 T TENSOR REMARK 3 T11: 0.2575 T22: 0.2471 REMARK 3 T33: 0.3201 T12: 0.0086 REMARK 3 T13: -0.0049 T23: 0.0362 REMARK 3 L TENSOR REMARK 3 L11: 1.8054 L22: 1.9159 REMARK 3 L33: 2.8821 L12: 0.3915 REMARK 3 L13: 0.2509 L23: -0.0827 REMARK 3 S TENSOR REMARK 3 S11: -0.1403 S12: 0.1643 S13: 0.3127 REMARK 3 S21: -0.0625 S22: 0.1941 S23: 0.1612 REMARK 3 S31: -0.3093 S32: -0.2163 S33: -0.0388 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 192 THROUGH 215 ) REMARK 3 ORIGIN FOR THE GROUP (A): 23.0429 -22.7933 -28.0048 REMARK 3 T TENSOR REMARK 3 T11: 0.2871 T22: 0.3225 REMARK 3 T33: 0.3300 T12: -0.0502 REMARK 3 T13: -0.0151 T23: 0.0912 REMARK 3 L TENSOR REMARK 3 L11: 3.8365 L22: 3.6621 REMARK 3 L33: 6.5929 L12: -1.2442 REMARK 3 L13: 2.0901 L23: -1.9795 REMARK 3 S TENSOR REMARK 3 S11: 0.1164 S12: 0.5208 S13: 0.3132 REMARK 3 S21: -0.3899 S22: -0.0203 S23: 0.1677 REMARK 3 S31: -0.2581 S32: 0.2071 S33: -0.1024 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 9IAT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-FEB-25. REMARK 100 THE DEPOSITION ID IS D_1292145355. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-FEB-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-002 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.54 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70168 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.540 REMARK 200 RESOLUTION RANGE LOW (A) : 39.720 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 8.400 REMARK 200 R MERGE (I) : 0.07600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.54 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.56 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.59 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10% (W/V) PEG 6K, 10 MM SODIUM REMARK 280 ACETATE, 30% (W/V) ETOH, VAPOR DIFFUSION, TEMPERATURE 292K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+2/3 REMARK 290 6555 -X,-X+Y,-Z+1/3 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.23133 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 102.46267 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 102.46267 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 51.23133 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4010 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18970 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH B 498 LIES ON A SPECIAL POSITION. 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 ASP B 217 REMARK 465 LYS B 218 REMARK 465 THR B 219 REMARK 465 HIS B 220 REMARK 465 HIS B 221 REMARK 465 HIS B 222 REMARK 465 HIS B 223 REMARK 465 HIS B 224 REMARK 465 HIS B 225 REMARK 465 GLN A 1 REMARK 465 SER A 216 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 O HOH B 510 O HOH B 542 1.58 REMARK 500 O HOH A 535 O HOH A 543 1.68 REMARK 500 O ALA B 114 O HOH B 401 1.99 REMARK 500 OH TYR B 80 O HOH B 402 1.99 REMARK 500 O SER B 85 O HOH B 403 1.99 REMARK 500 O HOH B 447 O HOH B 512 2.01 REMARK 500 OG SER A 157 O HOH A 401 2.03 REMARK 500 O SER B 17 O HOH B 404 2.10 REMARK 500 NH1 ARG B 19 O HOH B 405 2.14 REMARK 500 O HOH A 433 O HOH A 511 2.16 REMARK 500 O HOH A 554 O HOH A 566 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH B 404 O HOH B 404 4555 1.93 REMARK 500 O HOH B 434 O HOH B 434 6555 2.03 REMARK 500 O HOH B 410 O HOH A 404 4655 2.16 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 B 99 -124.73 47.82 REMARK 500 SER B 132 -65.32 -95.42 REMARK 500 ASN A 28 -91.09 -116.92 REMARK 500 ASN A 52 -44.30 69.74 REMARK 500 ASP A 53 13.72 -151.66 REMARK 500 ASP A 155 -111.48 52.91 REMARK 500 GLU A 202 -116.64 55.31 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 572 DISTANCE = 7.37 ANGSTROMS DBREF 9IAT B 1 225 PDB 9IAT 9IAT 1 225 DBREF 9IAT A 1 216 PDB 9IAT 9IAT 1 216 SEQRES 1 B 225 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 225 PRO GLY GLY SER LEU ARG LEU SER CYS VAL ALA SER GLY SEQRES 3 B 225 PHE THR PHE SER ARG PHE GLU MET ASN TRP VAL ARG GLN SEQRES 4 B 225 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER TYR ILE SER SEQRES 5 B 225 ASN SER GLY GLU THR GLN TYR TYR ALA ASP SER VAL LYS SEQRES 6 B 225 GLY ARG PHE ILE VAL SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 B 225 LEU TYR LEU GLN MET ASN SER LEU ARG ALA ASP ASP THR SEQRES 8 B 225 ALA ILE TYR TYR CYS LEU VAL VAL LEU ASP TYR TRP GLY SEQRES 9 B 225 GLN GLY ALA LEU VAL THR VAL SER SER ALA SER THR LYS SEQRES 10 B 225 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 11 B 225 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 12 B 225 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 13 B 225 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 14 B 225 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 15 B 225 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 16 B 225 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 17 B 225 LYS LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS HIS SEQRES 18 B 225 HIS HIS HIS HIS SEQRES 1 A 216 GLN SER VAL LEU THR GLN ALA PRO SER ALA SER GLY THR SEQRES 2 A 216 PRO GLY GLN GLY VAL THR ILE ALA CYS SER GLY SER ASN SEQRES 3 A 216 SER ASN ILE GLY ASN ASN TYR VAL TYR TRP TYR HIS GLN SEQRES 4 A 216 LEU PRO GLY THR ALA PRO LYS LEU ILE ILE TYR THR ASN SEQRES 5 A 216 ASP GLN ARG PRO SER GLY VAL PRO ASP ARG PHE SER GLY SEQRES 6 A 216 SER LYS SER GLY THR SER ALA SER LEU ALA ILE SER GLY SEQRES 7 A 216 LEU ARG SER GLU ASP GLU GLY ASP TYR TYR CYS ALA ALA SEQRES 8 A 216 TRP ASP ASP SER LEU SER SER VAL LEU PHE GLY GLY GLY SEQRES 9 A 216 THR LYS LEU THR VAL LEU ARG GLN PRO LYS ALA ALA PRO SEQRES 10 A 216 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 A 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 A 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SEQRES 13 A 216 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER SEQRES 14 A 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 A 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SEQRES 16 A 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 A 216 THR VAL ALA PRO THR GLU CYS SER HET EDO B 301 4 HET EDO B 302 4 HET EDO A 301 4 HETNAM EDO 1,2-ETHANEDIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 3 EDO 3(C2 H6 O2) FORMUL 6 HOH *319(H2 O) HELIX 1 AA1 THR B 28 PHE B 32 5 5 HELIX 2 AA2 ARG B 87 THR B 91 5 5 HELIX 3 AA3 SER B 127 SER B 132 5 6 HELIX 4 AA4 SER B 156 ALA B 158 5 3 HELIX 5 AA5 SER B 187 LEU B 189 5 3 HELIX 6 AA6 LYS B 201 ASN B 204 5 4 HELIX 7 AA7 ARG A 80 GLU A 84 5 5 HELIX 8 AA8 SER A 125 ALA A 131 1 7 HELIX 9 AA9 THR A 185 HIS A 192 1 8 SHEET 1 AA1 4 GLN B 3 SER B 7 0 SHEET 2 AA1 4 LEU B 18 SER B 25 -1 O SER B 21 N SER B 7 SHEET 3 AA1 4 SER B 78 MET B 83 -1 O LEU B 79 N CYS B 22 SHEET 4 AA1 4 PHE B 68 ASP B 73 -1 N ILE B 69 O GLN B 82 SHEET 1 AA2 6 GLY B 10 VAL B 12 0 SHEET 2 AA2 6 ALA B 107 VAL B 111 1 O THR B 110 N VAL B 12 SHEET 3 AA2 6 ALA B 92 VAL B 98 -1 N TYR B 94 O ALA B 107 SHEET 4 AA2 6 MET B 34 GLN B 39 -1 N VAL B 37 O TYR B 95 SHEET 5 AA2 6 GLU B 46 ILE B 51 -1 O GLU B 46 N ARG B 38 SHEET 6 AA2 6 GLN B 58 TYR B 60 -1 O TYR B 59 N TYR B 50 SHEET 1 AA3 4 GLY B 10 VAL B 12 0 SHEET 2 AA3 4 ALA B 107 VAL B 111 1 O THR B 110 N VAL B 12 SHEET 3 AA3 4 ALA B 92 VAL B 98 -1 N TYR B 94 O ALA B 107 SHEET 4 AA3 4 TYR B 102 TRP B 103 -1 O TYR B 102 N VAL B 98 SHEET 1 AA4 4 SER B 120 LEU B 124 0 SHEET 2 AA4 4 THR B 135 TYR B 145 -1 O LYS B 143 N SER B 120 SHEET 3 AA4 4 TYR B 176 PRO B 185 -1 O TYR B 176 N TYR B 145 SHEET 4 AA4 4 VAL B 163 THR B 165 -1 N HIS B 164 O VAL B 181 SHEET 1 AA5 4 SER B 120 LEU B 124 0 SHEET 2 AA5 4 THR B 135 TYR B 145 -1 O LYS B 143 N SER B 120 SHEET 3 AA5 4 TYR B 176 PRO B 185 -1 O TYR B 176 N TYR B 145 SHEET 4 AA5 4 VAL B 169 LEU B 170 -1 N VAL B 169 O SER B 177 SHEET 1 AA6 3 THR B 151 TRP B 154 0 SHEET 2 AA6 3 ILE B 195 HIS B 200 -1 O ASN B 197 N SER B 153 SHEET 3 AA6 3 THR B 205 LYS B 210 -1 O VAL B 207 N VAL B 198 SHEET 1 AA7 5 SER A 9 GLY A 12 0 SHEET 2 AA7 5 THR A 105 VAL A 109 1 O LYS A 106 N ALA A 10 SHEET 3 AA7 5 GLY A 85 ASP A 93 -1 N GLY A 85 O LEU A 107 SHEET 4 AA7 5 VAL A 34 GLN A 39 -1 N GLN A 39 O ASP A 86 SHEET 5 AA7 5 LYS A 46 ILE A 49 -1 O ILE A 48 N TRP A 36 SHEET 1 AA8 4 SER A 9 GLY A 12 0 SHEET 2 AA8 4 THR A 105 VAL A 109 1 O LYS A 106 N ALA A 10 SHEET 3 AA8 4 GLY A 85 ASP A 93 -1 N GLY A 85 O LEU A 107 SHEET 4 AA8 4 SER A 98 PHE A 101 -1 O LEU A 100 N ALA A 91 SHEET 1 AA9 3 VAL A 18 SER A 23 0 SHEET 2 AA9 3 SER A 71 ILE A 76 -1 O LEU A 74 N ILE A 20 SHEET 3 AA9 3 PHE A 63 SER A 68 -1 N SER A 64 O ALA A 75 SHEET 1 AB1 4 SER A 118 PHE A 122 0 SHEET 2 AB1 4 ALA A 134 PHE A 143 -1 O LEU A 139 N THR A 120 SHEET 3 AB1 4 TYR A 176 LEU A 184 -1 O SER A 180 N CYS A 138 SHEET 4 AB1 4 VAL A 163 THR A 165 -1 N GLU A 164 O TYR A 181 SHEET 1 AB2 4 SER A 118 PHE A 122 0 SHEET 2 AB2 4 ALA A 134 PHE A 143 -1 O LEU A 139 N THR A 120 SHEET 3 AB2 4 TYR A 176 LEU A 184 -1 O SER A 180 N CYS A 138 SHEET 4 AB2 4 SER A 169 LYS A 170 -1 N SER A 169 O ALA A 177 SHEET 1 AB3 4 SER A 157 VAL A 159 0 SHEET 2 AB3 4 THR A 149 ALA A 154 -1 N ALA A 154 O SER A 157 SHEET 3 AB3 4 TYR A 195 HIS A 201 -1 O GLN A 198 N ALA A 151 SHEET 4 AB3 4 SER A 204 VAL A 210 -1 O VAL A 206 N VAL A 199 SSBOND 1 CYS B 22 CYS B 96 1555 1555 2.06 SSBOND 2 CYS B 140 CYS B 196 1555 1555 2.04 SSBOND 3 CYS B 216 CYS A 215 1555 1555 2.04 SSBOND 4 CYS A 22 CYS A 89 1555 1555 2.04 SSBOND 5 CYS A 138 CYS A 197 1555 1555 2.05 CISPEP 1 PHE B 146 PRO B 147 0 -9.64 CISPEP 2 GLU B 148 PRO B 149 0 -0.69 CISPEP 3 TYR A 144 PRO A 145 0 -0.61 CRYST1 72.638 72.638 153.694 90.00 90.00 120.00 P 31 2 1 6 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.013767 0.007948 0.000000 0.00000 SCALE2 0.000000 0.015897 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006506 0.00000