HEADER IMMUNE SYSTEM 09-AUG-24 9GFH TITLE BCR FAB FROM THE SUBSET 1 CHRONIC LYMPHOCYTIC LEUKAEMIA CASE P1173 COMPND MOL_ID: 1; COMPND 2 MOLECULE: BCR P1173 LIGHT CHAIN; COMPND 3 CHAIN: L, B, D, F; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: BCR P1173 HEAVY CHAIN; COMPND 7 CHAIN: A, H, C, E; 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 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM_CELL_LINE: HEK293 KEYWDS B-CELL RECEPTOR, FAB FRAGMENT, CHRONIC LYMPHOCYTIC LEUKAEMIA, IMMUNE KEYWDS 2 SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR P.G.COCOMAZZI,M.DEGANO REVDAT 1 20-AUG-25 9GFH 0 JRNL AUTH P.G.COCOMAZZI,A.IATROU,C.MINICI,M.DEGANO JRNL TITL DEFECTIVE CELL-AUTONOMOUS SIGNALLING AND ANTIGENIC JRNL TITL 2 POLYREACTIVITY OF B-CELL RECEPTORS FROM CHRONIC LYMPHOCYTIC JRNL TITL 3 LEUKAEMIA STEREOTYPED SUBSET 1 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.72 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 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) : 2.72 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 91.77 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 70.6 REMARK 3 NUMBER OF REFLECTIONS : 41879 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.215 REMARK 3 R VALUE (WORKING SET) : 0.214 REMARK 3 FREE R VALUE : 0.244 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.770 REMARK 3 FREE R VALUE TEST SET COUNT : 1997 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 91.7700 - 6.5500 1.00 4305 195 0.2396 0.2363 REMARK 3 2 6.5500 - 5.2000 1.00 4121 175 0.1917 0.1871 REMARK 3 3 5.2000 - 4.5400 1.00 4096 181 0.1455 0.1853 REMARK 3 4 4.5400 - 4.1200 1.00 4073 187 0.1570 0.1960 REMARK 3 5 4.1200 - 3.8300 1.00 4021 195 0.2025 0.2325 REMARK 3 6 3.8300 - 3.6000 0.70 2781 175 0.2338 0.2725 REMARK 3 7 3.6000 - 3.4200 0.62 2479 162 0.2517 0.3151 REMARK 3 8 3.4200 - 3.2700 0.96 3820 209 0.2750 0.3000 REMARK 3 9 3.2700 - 3.1500 0.77 3085 150 0.2833 0.3355 REMARK 3 10 3.1500 - 3.0400 0.65 2580 132 0.3052 0.3124 REMARK 3 11 3.0400 - 2.9400 0.52 2085 111 0.3174 0.3653 REMARK 3 12 2.9400 - 2.8600 0.33 1295 76 0.3259 0.3494 REMARK 3 13 2.8600 - 2.7800 0.19 758 37 0.3358 0.3218 REMARK 3 14 2.7800 - 2.7200 0.09 383 12 0.3596 0.3013 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) : 0.305 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.887 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 61.46 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 68.46 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 : 0.003 13507 REMARK 3 ANGLE : 0.645 18339 REMARK 3 CHIRALITY : 0.048 2039 REMARK 3 PLANARITY : 0.005 2331 REMARK 3 DIHEDRAL : 13.546 4876 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 16 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN 'H' AND RESID 1 THROUGH 120) REMARK 3 ORIGIN FOR THE GROUP (A): -21.0044 -41.5311 19.0497 REMARK 3 T TENSOR REMARK 3 T11: 0.1957 T22: 0.2491 REMARK 3 T33: 0.3231 T12: -0.0046 REMARK 3 T13: 0.0026 T23: -0.0264 REMARK 3 L TENSOR REMARK 3 L11: 4.5671 L22: 3.6065 REMARK 3 L33: 6.4322 L12: 1.3087 REMARK 3 L13: -0.1084 L23: -0.6810 REMARK 3 S TENSOR REMARK 3 S11: 0.0158 S12: -0.2931 S13: -0.1039 REMARK 3 S21: 0.2255 S22: -0.0030 S23: 0.3947 REMARK 3 S31: -0.0120 S32: -0.3344 S33: 0.0093 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN 'L' AND RESID 1 THROUGH 108) REMARK 3 ORIGIN FOR THE GROUP (A): 0.7562 -43.7436 14.4597 REMARK 3 T TENSOR REMARK 3 T11: 0.2274 T22: 0.1982 REMARK 3 T33: 0.2242 T12: -0.0512 REMARK 3 T13: -0.0375 T23: -0.0113 REMARK 3 L TENSOR REMARK 3 L11: 4.5183 L22: 4.4148 REMARK 3 L33: 4.5551 L12: -1.1352 REMARK 3 L13: 0.2906 L23: 0.0260 REMARK 3 S TENSOR REMARK 3 S11: 0.1960 S12: 0.2125 S13: -0.4483 REMARK 3 S21: -0.1401 S22: -0.0557 S23: 0.2018 REMARK 3 S31: 0.3564 S32: -0.2076 S33: -0.0632 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN 'A' AND RESID 1 THROUGH 120) REMARK 3 ORIGIN FOR THE GROUP (A): -52.2747 -52.0516 -8.2753 REMARK 3 T TENSOR REMARK 3 T11: 0.2010 T22: 0.4139 REMARK 3 T33: 0.3198 T12: 0.0654 REMARK 3 T13: -0.0516 T23: 0.0555 REMARK 3 L TENSOR REMARK 3 L11: 1.6082 L22: 9.8387 REMARK 3 L33: 2.1993 L12: 0.6344 REMARK 3 L13: 0.4668 L23: 0.1642 REMARK 3 S TENSOR REMARK 3 S11: 0.0430 S12: -0.0378 S13: -0.1505 REMARK 3 S21: 0.0999 S22: 0.0246 S23: 0.2306 REMARK 3 S31: 0.1027 S32: -0.0297 S33: -0.0779 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN 'B' AND RESID 2 THROUGH 108) REMARK 3 ORIGIN FOR THE GROUP (A): -30.2860 -47.6162 -11.9626 REMARK 3 T TENSOR REMARK 3 T11: 0.2007 T22: 0.2879 REMARK 3 T33: 0.3886 T12: 0.0606 REMARK 3 T13: -0.0905 T23: -0.0094 REMARK 3 L TENSOR REMARK 3 L11: 6.5680 L22: 4.3471 REMARK 3 L33: 3.3671 L12: -2.1067 REMARK 3 L13: -0.2708 L23: -0.5080 REMARK 3 S TENSOR REMARK 3 S11: 0.2152 S12: 0.2461 S13: 0.1141 REMARK 3 S21: -0.2474 S22: -0.1771 S23: -0.3746 REMARK 3 S31: -0.0833 S32: -0.1323 S33: -0.0578 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (CHAIN 'C' AND RESID 1 THROUGH 120) REMARK 3 ORIGIN FOR THE GROUP (A): 43.4562 -47.7883 29.3475 REMARK 3 T TENSOR REMARK 3 T11: 0.3000 T22: 0.4251 REMARK 3 T33: 0.5711 T12: 0.0707 REMARK 3 T13: 0.0066 T23: 0.0712 REMARK 3 L TENSOR REMARK 3 L11: 3.4911 L22: 3.7750 REMARK 3 L33: 4.7367 L12: 1.8655 REMARK 3 L13: 1.8839 L23: 1.6727 REMARK 3 S TENSOR REMARK 3 S11: 0.1186 S12: 0.3935 S13: -0.0647 REMARK 3 S21: -0.2258 S22: 0.0075 S23: -0.5047 REMARK 3 S31: 0.0688 S32: 0.3617 S33: -0.1068 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (CHAIN 'D' AND RESID 1 THROUGH 108) REMARK 3 ORIGIN FOR THE GROUP (A): 23.8862 -49.7958 18.3846 REMARK 3 T TENSOR REMARK 3 T11: 0.5119 T22: 0.2904 REMARK 3 T33: 0.2472 T12: -0.0435 REMARK 3 T13: -0.0283 T23: 0.0169 REMARK 3 L TENSOR REMARK 3 L11: 6.8064 L22: 4.2083 REMARK 3 L33: 5.4331 L12: -0.7386 REMARK 3 L13: -0.5941 L23: -0.0357 REMARK 3 S TENSOR REMARK 3 S11: -0.1090 S12: 0.4063 S13: 0.0058 REMARK 3 S21: -0.8258 S22: -0.1144 S23: -0.2293 REMARK 3 S31: 0.0573 S32: 0.5512 S33: 0.1930 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: (CHAIN 'E' AND RESID 1 THROUGH 120) REMARK 3 ORIGIN FOR THE GROUP (A): 50.4554 -67.9539 49.2857 REMARK 3 T TENSOR REMARK 3 T11: 0.2537 T22: 0.5890 REMARK 3 T33: 0.4398 T12: -0.0426 REMARK 3 T13: -0.0656 T23: 0.0334 REMARK 3 L TENSOR REMARK 3 L11: 5.8673 L22: 5.3520 REMARK 3 L33: 4.0591 L12: -1.5330 REMARK 3 L13: -0.2546 L23: 1.0578 REMARK 3 S TENSOR REMARK 3 S11: 0.0649 S12: 0.5795 S13: -0.3603 REMARK 3 S21: -0.1819 S22: -0.1456 S23: 0.0785 REMARK 3 S31: 0.2863 S32: -0.3873 S33: 0.0995 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: (CHAIN 'F' AND RESID 1 THROUGH 108) REMARK 3 ORIGIN FOR THE GROUP (A): 70.6107 -77.6968 48.0092 REMARK 3 T TENSOR REMARK 3 T11: 0.3543 T22: 0.3247 REMARK 3 T33: 0.4580 T12: 0.0780 REMARK 3 T13: 0.0086 T23: -0.0577 REMARK 3 L TENSOR REMARK 3 L11: 6.5705 L22: 6.0768 REMARK 3 L33: 5.2578 L12: 0.4680 REMARK 3 L13: -1.2199 L23: -0.5956 REMARK 3 S TENSOR REMARK 3 S11: -0.0848 S12: 0.1213 S13: -0.5577 REMARK 3 S21: -0.1515 S22: 0.0558 S23: 0.6890 REMARK 3 S31: 0.6783 S32: -0.1739 S33: 0.0498 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: (CHAIN 'H' AND RESID 121 THROUGH 224) REMARK 3 ORIGIN FOR THE GROUP (A): -8.5956 -19.7907 41.4607 REMARK 3 T TENSOR REMARK 3 T11: 0.6764 T22: 0.4582 REMARK 3 T33: 0.3534 T12: 0.1806 REMARK 3 T13: -0.0233 T23: -0.0064 REMARK 3 L TENSOR REMARK 3 L11: 2.5929 L22: 5.8205 REMARK 3 L33: 1.8336 L12: 0.6393 REMARK 3 L13: -0.2598 L23: 1.5712 REMARK 3 S TENSOR REMARK 3 S11: -0.1626 S12: -0.0303 S13: 0.3209 REMARK 3 S21: 0.2509 S22: 0.1432 S23: -0.0608 REMARK 3 S31: -0.1277 S32: -0.1698 S33: 0.0290 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: (CHAIN 'L' AND RESID 109 THROUGH 214) REMARK 3 ORIGIN FOR THE GROUP (A): 3.2854 -29.3228 49.4875 REMARK 3 T TENSOR REMARK 3 T11: 0.8449 T22: 0.3964 REMARK 3 T33: 0.4510 T12: 0.1083 REMARK 3 T13: -0.1714 T23: 0.0057 REMARK 3 L TENSOR REMARK 3 L11: 4.9593 L22: 0.7212 REMARK 3 L33: 6.5149 L12: 0.3444 REMARK 3 L13: -2.4827 L23: 0.4640 REMARK 3 S TENSOR REMARK 3 S11: -0.0362 S12: -0.8279 S13: -0.1654 REMARK 3 S21: 0.7051 S22: 0.0700 S23: -0.1489 REMARK 3 S31: -0.1465 S32: 0.2303 S33: 0.0034 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: (CHAIN 'A' AND RESID 121 THROUGH 224) REMARK 3 ORIGIN FOR THE GROUP (A): -38.7375 -74.4068 12.1160 REMARK 3 T TENSOR REMARK 3 T11: 0.6160 T22: 0.8928 REMARK 3 T33: 0.5145 T12: 0.0814 REMARK 3 T13: 0.0733 T23: 0.2092 REMARK 3 L TENSOR REMARK 3 L11: 3.7155 L22: 3.6235 REMARK 3 L33: 2.0340 L12: 0.1186 REMARK 3 L13: 0.0141 L23: -1.1539 REMARK 3 S TENSOR REMARK 3 S11: 0.1079 S12: -1.5409 S13: -0.2599 REMARK 3 S21: 0.7278 S22: 0.0349 S23: 0.0782 REMARK 3 S31: 0.0942 S32: -0.0319 S33: -0.2203 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: (CHAIN 'C' AND RESID 121 THROUGH 224) REMARK 3 ORIGIN FOR THE GROUP (A): 25.1444 -64.2291 52.3140 REMARK 3 T TENSOR REMARK 3 T11: 0.2961 T22: 0.4308 REMARK 3 T33: 0.3149 T12: 0.0566 REMARK 3 T13: -0.0016 T23: 0.1004 REMARK 3 L TENSOR REMARK 3 L11: 4.3498 L22: 7.3285 REMARK 3 L33: 4.3067 L12: 0.7605 REMARK 3 L13: -0.1774 L23: -1.1082 REMARK 3 S TENSOR REMARK 3 S11: -0.1383 S12: -0.3360 S13: -0.5780 REMARK 3 S21: 0.0613 S22: 0.0785 S23: -0.0655 REMARK 3 S31: 0.2889 S32: 0.2934 S33: 0.0307 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: (CHAIN 'B' AND RESID 109 THROUGH 214) REMARK 3 ORIGIN FOR THE GROUP (A): -26.5035 -81.9323 3.0877 REMARK 3 T TENSOR REMARK 3 T11: 0.6090 T22: 0.6616 REMARK 3 T33: 0.7584 T12: 0.1259 REMARK 3 T13: 0.0300 T23: 0.3269 REMARK 3 L TENSOR REMARK 3 L11: 3.5034 L22: 2.6311 REMARK 3 L33: 1.3238 L12: -0.4006 REMARK 3 L13: 0.4150 L23: -1.0195 REMARK 3 S TENSOR REMARK 3 S11: -0.0145 S12: -0.5425 S13: -1.0672 REMARK 3 S21: 0.1877 S22: -0.1241 S23: -0.1580 REMARK 3 S31: 0.4005 S32: 0.1430 S33: 0.1463 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: (CHAIN 'D' AND RESID 109 THROUGH 214) REMARK 3 ORIGIN FOR THE GROUP (A): 11.1986 -54.5122 54.1194 REMARK 3 T TENSOR REMARK 3 T11: 0.3696 T22: 0.2620 REMARK 3 T33: 0.4584 T12: 0.0304 REMARK 3 T13: -0.0047 T23: 0.0589 REMARK 3 L TENSOR REMARK 3 L11: 4.3107 L22: 1.8266 REMARK 3 L33: 6.7923 L12: 0.4105 REMARK 3 L13: 1.8409 L23: 0.5630 REMARK 3 S TENSOR REMARK 3 S11: -0.1693 S12: -0.5000 S13: 0.3299 REMARK 3 S21: 0.3277 S22: -0.0162 S23: 0.1384 REMARK 3 S31: -0.2244 S32: 0.0606 S33: 0.1766 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: (CHAIN 'E' AND RESID 121 THROUGH 224) REMARK 3 ORIGIN FOR THE GROUP (A): 68.2946 -43.4328 35.1947 REMARK 3 T TENSOR REMARK 3 T11: 0.3940 T22: 0.5853 REMARK 3 T33: 0.6322 T12: -0.0261 REMARK 3 T13: -0.0518 T23: 0.1940 REMARK 3 L TENSOR REMARK 3 L11: 4.0388 L22: 3.8430 REMARK 3 L33: 4.5286 L12: 0.0321 REMARK 3 L13: 0.3329 L23: 0.1335 REMARK 3 S TENSOR REMARK 3 S11: -0.3636 S12: 0.7661 S13: 0.2022 REMARK 3 S21: -0.3123 S22: 0.0935 S23: 0.0710 REMARK 3 S31: -0.2265 S32: 0.1460 S33: 0.2995 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: (CHAIN 'F' AND RESID 109 THROUGH 214) REMARK 3 ORIGIN FOR THE GROUP (A): 81.5100 -40.9949 45.5991 REMARK 3 T TENSOR REMARK 3 T11: 0.3445 T22: 0.5351 REMARK 3 T33: 0.5734 T12: 0.0023 REMARK 3 T13: 0.0124 T23: 0.1138 REMARK 3 L TENSOR REMARK 3 L11: 3.2407 L22: 6.0118 REMARK 3 L33: 2.7047 L12: -0.5255 REMARK 3 L13: -1.0180 L23: 0.9680 REMARK 3 S TENSOR REMARK 3 S11: -0.1035 S12: -0.0470 S13: 0.5087 REMARK 3 S21: -0.0869 S22: 0.0643 S23: -0.1835 REMARK 3 S31: -0.1720 S32: 0.3097 S33: 0.0164 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 2 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "A" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "C" and (resid 1 through 167 or REMARK 3 resid 175 through 198 or resid 203 REMARK 3 through 224 or resid 225)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "E" and (resid 1 through 167 or REMARK 3 resid 175 through 224 or resid 225)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "H" and (resid 1 through 167 or REMARK 3 resid 175 through 198 or resid 203 REMARK 3 through 224 or resid 225)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "B" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "D" and (resid 2 through 93 or REMARK 3 resid 96 through 214)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "F" and (resid 2 through 93 or REMARK 3 resid 96 through 214)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "L" and (resid 2 through 93 or REMARK 3 resid 96 through 214)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9GFH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-AUG-24. REMARK 100 THE DEPOSITION ID IS D_1292140879. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 28-SEP-20 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID23-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.972 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : STARANISO REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 123151 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.870 REMARK 200 RESOLUTION RANGE LOW (A) : 91.770 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2 REMARK 200 DATA REDUNDANCY : 13.40 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.87 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02 REMARK 200 COMPLETENESS FOR SHELL (%) : 81.5 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 : 1.700 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.42 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M CITRIC ACID PH 5 20% PEG 6,000, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 62.70800 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 67.32500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 64.25450 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 67.32500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 62.70800 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 64.25450 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 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 APPLY THE FOLLOWING TO CHAINS: L, H, G REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, E 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 CYS L 215 REMARK 465 GLU A 135 REMARK 465 ASN A 136 REMARK 465 SER A 137 REMARK 465 PRO A 138 REMARK 465 SER A 139 REMARK 465 ASP A 140 REMARK 465 THR A 141 REMARK 465 SER A 168 REMARK 465 ASP A 169 REMARK 465 ILE A 170 REMARK 465 SER A 171 REMARK 465 SER A 172 REMARK 465 THR A 173 REMARK 465 ARG A 174 REMARK 465 MET A 199 REMARK 465 GLN A 200 REMARK 465 GLY A 201 REMARK 465 THR A 202 REMARK 465 VAL A 225 REMARK 465 ASP B 1 REMARK 465 THR B 94 REMARK 465 PRO B 95 REMARK 465 CYS B 215 REMARK 465 CYS D 215 REMARK 465 CYS F 215 REMARK 465 GLU H 135 REMARK 465 ASN H 136 REMARK 465 SER H 137 REMARK 465 PRO H 138 REMARK 465 SER H 139 REMARK 465 ASP H 140 REMARK 465 THR H 141 REMARK 465 VAL H 225 REMARK 465 GLU C 135 REMARK 465 ASN C 136 REMARK 465 SER C 137 REMARK 465 PRO C 138 REMARK 465 SER C 139 REMARK 465 ASP C 140 REMARK 465 THR C 141 REMARK 465 MET C 199 REMARK 465 GLN C 200 REMARK 465 VAL C 225 REMARK 465 GLU E 135 REMARK 465 ASN E 136 REMARK 465 SER E 137 REMARK 465 PRO E 138 REMARK 465 SER E 139 REMARK 465 ASP E 140 REMARK 465 THR E 141 REMARK 465 MET E 199 REMARK 465 GLN E 200 REMARK 465 GLY E 201 REMARK 465 THR E 202 REMARK 465 VAL E 225 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 OE1 GLN C 82 H ASN E 216 1.56 REMARK 500 NZ LYS B 150 OE1 GLU B 196 2.13 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER L 30 -123.67 49.20 REMARK 500 LEU L 47 -61.40 -109.49 REMARK 500 ALA L 51 -34.46 84.73 REMARK 500 SER L 52 25.60 -152.73 REMARK 500 ALA L 84 -174.86 -172.76 REMARK 500 ASN L 139 71.65 51.75 REMARK 500 LYS A 43 -169.86 -118.37 REMARK 500 ALA A 92 -174.60 -174.09 REMARK 500 ARG A 181 114.90 -160.03 REMARK 500 SER B 30 -124.78 48.60 REMARK 500 ALA B 51 -33.43 81.70 REMARK 500 SER B 52 23.75 -150.03 REMARK 500 SER B 67 146.32 -171.48 REMARK 500 ALA B 84 -175.69 -173.18 REMARK 500 ASN B 139 71.41 51.72 REMARK 500 SER D 30 -123.22 48.84 REMARK 500 ALA D 51 -29.51 79.78 REMARK 500 SER D 52 20.46 -146.64 REMARK 500 ALA D 84 -176.17 -173.08 REMARK 500 ASN D 139 71.25 51.78 REMARK 500 SER F 30 -122.51 49.98 REMARK 500 ALA F 51 -31.63 81.12 REMARK 500 SER F 52 21.55 -147.33 REMARK 500 SER F 67 145.11 -170.79 REMARK 500 ALA F 84 -175.87 -173.50 REMARK 500 ASN F 139 72.19 52.04 REMARK 500 LYS H 43 -169.63 -118.80 REMARK 500 ALA H 92 -174.67 -173.21 REMARK 500 ASN H 167 15.76 51.10 REMARK 500 SER H 172 43.78 -90.51 REMARK 500 ALA C 92 -175.14 -173.66 REMARK 500 ASN C 166 31.67 -94.73 REMARK 500 ARG C 181 113.94 -160.61 REMARK 500 CYS E 22 107.61 -160.30 REMARK 500 LYS E 43 -169.86 -118.32 REMARK 500 ALA E 92 -175.62 -173.76 REMARK 500 ASN E 166 31.47 -94.52 REMARK 500 SER E 172 103.82 -55.46 REMARK 500 ARG E 181 115.14 -160.80 REMARK 500 REMARK 500 REMARK: NULL DBREF 9GFH L 1 215 PDB 9GFH 9GFH 1 215 DBREF 9GFH A 1 225 PDB 9GFH 9GFH 1 225 DBREF 9GFH B 1 215 PDB 9GFH 9GFH 1 215 DBREF 9GFH D 1 215 PDB 9GFH 9GFH 1 215 DBREF 9GFH F 1 215 PDB 9GFH 9GFH 1 215 DBREF 9GFH H 1 225 PDB 9GFH 9GFH 1 225 DBREF 9GFH C 1 225 PDB 9GFH 9GFH 1 225 DBREF 9GFH E 1 225 PDB 9GFH 9GFH 1 225 SEQRES 1 L 215 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 215 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 215 GLN SER ILE SER SER TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 L 215 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 L 215 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 215 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 215 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 L 215 TYR SER THR PRO PRO HIS THR PHE GLY GLN GLY THR LYS SEQRES 9 L 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 L 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 A 225 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 A 225 PRO GLY GLU SER LEU ARG ILE SER CYS LYS GLY SER GLY SEQRES 3 A 225 TYR SER PHE THR SER TYR TRP ILE THR TRP VAL ARG GLN SEQRES 4 A 225 MET PRO GLY LYS GLY LEU GLU TRP MET GLY ARG ILE ASP SEQRES 5 A 225 PRO SER ASP SER TYR THR ASN TYR SER PRO SER PHE GLN SEQRES 6 A 225 GLY HIS VAL THR ILE SER ALA ASP LYS SER ILE SER THR SEQRES 7 A 225 ALA TYR LEU GLN TRP SER SER LEU LYS ALA SER ASP THR SEQRES 8 A 225 ALA MET TYR TYR CYS ALA ARG GLU GLN TRP LEU GLY ILE SEQRES 9 A 225 LYS ASN PHE ASP TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 A 225 VAL SER SER GLY SER ALA SER ALA PRO THR LEU PHE PRO SEQRES 11 A 225 LEU VAL SER CYS GLU ASN SER PRO SER ASP THR SER SER SEQRES 12 A 225 VAL ALA VAL GLY CYS LEU ALA GLN ASP PHE LEU PRO ASP SEQRES 13 A 225 SER ILE THR PHE SER TRP LYS TYR LYS ASN ASN SER ASP SEQRES 14 A 225 ILE SER SER THR ARG GLY PHE PRO SER VAL LEU ARG GLY SEQRES 15 A 225 GLY LYS TYR ALA ALA THR SER GLN VAL LEU LEU PRO SER SEQRES 16 A 225 LYS ASP VAL MET GLN GLY THR ASP GLU HIS VAL VAL CYS SEQRES 17 A 225 LYS VAL GLN HIS PRO ASN GLY ASN LYS GLU LYS ASN VAL SEQRES 18 A 225 PRO LEU PRO VAL SEQRES 1 B 215 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 B 215 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 B 215 GLN SER ILE SER SER TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 B 215 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 B 215 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 B 215 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 B 215 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 B 215 TYR SER THR PRO PRO HIS THR PHE GLY GLN GLY THR LYS SEQRES 9 B 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 B 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 B 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 B 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 B 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 B 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 B 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 B 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 B 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 D 215 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 D 215 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 D 215 GLN SER ILE SER SER TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 D 215 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 D 215 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 D 215 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 D 215 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 D 215 TYR SER THR PRO PRO HIS THR PHE GLY GLN GLY THR LYS SEQRES 9 D 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 D 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 D 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 D 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 D 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 D 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 D 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 D 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 D 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 F 215 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 F 215 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 F 215 GLN SER ILE SER SER TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 F 215 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 F 215 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 F 215 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 F 215 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 F 215 TYR SER THR PRO PRO HIS THR PHE GLY GLN GLY THR LYS SEQRES 9 F 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 F 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 F 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 F 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 F 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 F 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 F 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 F 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 F 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 H 225 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 225 PRO GLY GLU SER LEU ARG ILE SER CYS LYS GLY SER GLY SEQRES 3 H 225 TYR SER PHE THR SER TYR TRP ILE THR TRP VAL ARG GLN SEQRES 4 H 225 MET PRO GLY LYS GLY LEU GLU TRP MET GLY ARG ILE ASP SEQRES 5 H 225 PRO SER ASP SER TYR THR ASN TYR SER PRO SER PHE GLN SEQRES 6 H 225 GLY HIS VAL THR ILE SER ALA ASP LYS SER ILE SER THR SEQRES 7 H 225 ALA TYR LEU GLN TRP SER SER LEU LYS ALA SER ASP THR SEQRES 8 H 225 ALA MET TYR TYR CYS ALA ARG GLU GLN TRP LEU GLY ILE SEQRES 9 H 225 LYS ASN PHE ASP TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 H 225 VAL SER SER GLY SER ALA SER ALA PRO THR LEU PHE PRO SEQRES 11 H 225 LEU VAL SER CYS GLU ASN SER PRO SER ASP THR SER SER SEQRES 12 H 225 VAL ALA VAL GLY CYS LEU ALA GLN ASP PHE LEU PRO ASP SEQRES 13 H 225 SER ILE THR PHE SER TRP LYS TYR LYS ASN ASN SER ASP SEQRES 14 H 225 ILE SER SER THR ARG GLY PHE PRO SER VAL LEU ARG GLY SEQRES 15 H 225 GLY LYS TYR ALA ALA THR SER GLN VAL LEU LEU PRO SER SEQRES 16 H 225 LYS ASP VAL MET GLN GLY THR ASP GLU HIS VAL VAL CYS SEQRES 17 H 225 LYS VAL GLN HIS PRO ASN GLY ASN LYS GLU LYS ASN VAL SEQRES 18 H 225 PRO LEU PRO VAL SEQRES 1 C 225 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 C 225 PRO GLY GLU SER LEU ARG ILE SER CYS LYS GLY SER GLY SEQRES 3 C 225 TYR SER PHE THR SER TYR TRP ILE THR TRP VAL ARG GLN SEQRES 4 C 225 MET PRO GLY LYS GLY LEU GLU TRP MET GLY ARG ILE ASP SEQRES 5 C 225 PRO SER ASP SER TYR THR ASN TYR SER PRO SER PHE GLN SEQRES 6 C 225 GLY HIS VAL THR ILE SER ALA ASP LYS SER ILE SER THR SEQRES 7 C 225 ALA TYR LEU GLN TRP SER SER LEU LYS ALA SER ASP THR SEQRES 8 C 225 ALA MET TYR TYR CYS ALA ARG GLU GLN TRP LEU GLY ILE SEQRES 9 C 225 LYS ASN PHE ASP TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 C 225 VAL SER SER GLY SER ALA SER ALA PRO THR LEU PHE PRO SEQRES 11 C 225 LEU VAL SER CYS GLU ASN SER PRO SER ASP THR SER SER SEQRES 12 C 225 VAL ALA VAL GLY CYS LEU ALA GLN ASP PHE LEU PRO ASP SEQRES 13 C 225 SER ILE THR PHE SER TRP LYS TYR LYS ASN ASN SER ASP SEQRES 14 C 225 ILE SER SER THR ARG GLY PHE PRO SER VAL LEU ARG GLY SEQRES 15 C 225 GLY LYS TYR ALA ALA THR SER GLN VAL LEU LEU PRO SER SEQRES 16 C 225 LYS ASP VAL MET GLN GLY THR ASP GLU HIS VAL VAL CYS SEQRES 17 C 225 LYS VAL GLN HIS PRO ASN GLY ASN LYS GLU LYS ASN VAL SEQRES 18 C 225 PRO LEU PRO VAL SEQRES 1 E 225 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 E 225 PRO GLY GLU SER LEU ARG ILE SER CYS LYS GLY SER GLY SEQRES 3 E 225 TYR SER PHE THR SER TYR TRP ILE THR TRP VAL ARG GLN SEQRES 4 E 225 MET PRO GLY LYS GLY LEU GLU TRP MET GLY ARG ILE ASP SEQRES 5 E 225 PRO SER ASP SER TYR THR ASN TYR SER PRO SER PHE GLN SEQRES 6 E 225 GLY HIS VAL THR ILE SER ALA ASP LYS SER ILE SER THR SEQRES 7 E 225 ALA TYR LEU GLN TRP SER SER LEU LYS ALA SER ASP THR SEQRES 8 E 225 ALA MET TYR TYR CYS ALA ARG GLU GLN TRP LEU GLY ILE SEQRES 9 E 225 LYS ASN PHE ASP TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 E 225 VAL SER SER GLY SER ALA SER ALA PRO THR LEU PHE PRO SEQRES 11 E 225 LEU VAL SER CYS GLU ASN SER PRO SER ASP THR SER SER SEQRES 12 E 225 VAL ALA VAL GLY CYS LEU ALA GLN ASP PHE LEU PRO ASP SEQRES 13 E 225 SER ILE THR PHE SER TRP LYS TYR LYS ASN ASN SER ASP SEQRES 14 E 225 ILE SER SER THR ARG GLY PHE PRO SER VAL LEU ARG GLY SEQRES 15 E 225 GLY LYS TYR ALA ALA THR SER GLN VAL LEU LEU PRO SER SEQRES 16 E 225 LYS ASP VAL MET GLN GLY THR ASP GLU HIS VAL VAL CYS SEQRES 17 E 225 LYS VAL GLN HIS PRO ASN GLY ASN LYS GLU LYS ASN VAL SEQRES 18 E 225 PRO LEU PRO VAL HET NAG G 1 25 HET NAG G 2 27 HET FUC G 3 20 HET NAG A 301 27 HET CIT H 301 18 HET NAG C 301 27 HET NAG E 301 27 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE HETNAM CIT CITRIC ACID HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L- HETSYN 2 FUC FUCOSE; FUCOSE FORMUL 9 NAG 5(C8 H15 N O6) FORMUL 9 FUC C6 H12 O5 FORMUL 11 CIT C6 H8 O7 FORMUL 14 HOH *14(H2 O) HELIX 1 AA1 GLN L 79 PHE L 83 5 5 HELIX 2 AA2 SER L 122 SER L 128 1 7 HELIX 3 AA3 LYS L 184 GLU L 188 1 5 HELIX 4 AA4 SER A 28 TYR A 32 5 5 HELIX 5 AA5 LYS A 74 ILE A 76 5 3 HELIX 6 AA6 LYS A 87 THR A 91 5 5 HELIX 7 AA7 GLN B 79 PHE B 83 5 5 HELIX 8 AA8 SER B 122 SER B 128 1 7 HELIX 9 AA9 LYS B 184 GLU B 188 1 5 HELIX 10 AB1 GLN D 79 PHE D 83 5 5 HELIX 11 AB2 SER D 122 SER D 128 1 7 HELIX 12 AB3 LYS D 184 GLU D 188 1 5 HELIX 13 AB4 GLN F 79 PHE F 83 5 5 HELIX 14 AB5 SER F 122 SER F 128 1 7 HELIX 15 AB6 LYS F 184 GLU F 188 1 5 HELIX 16 AB7 SER H 28 TYR H 32 5 5 HELIX 17 AB8 LYS H 74 ILE H 76 5 3 HELIX 18 AB9 LYS H 87 THR H 91 5 5 HELIX 19 AC1 SER H 195 GLN H 200 1 6 HELIX 20 AC2 SER C 28 TYR C 32 5 5 HELIX 21 AC3 LYS C 87 THR C 91 5 5 HELIX 22 AC4 SER E 28 TYR E 32 5 5 HELIX 23 AC5 LYS E 74 ILE E 76 5 3 HELIX 24 AC6 LYS E 87 THR E 91 5 5 SHEET 1 AA1 4 MET L 4 SER L 7 0 SHEET 2 AA1 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA1 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AA1 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AA212 SER L 53 LEU L 54 0 SHEET 2 AA212 LYS L 45 TYR L 49 -1 N TYR L 49 O SER L 53 SHEET 3 AA212 LEU L 33 GLN L 38 -1 N TRP L 35 O LEU L 47 SHEET 4 AA212 ALA L 84 GLN L 90 -1 O TYR L 87 N TYR L 36 SHEET 5 AA212 THR L 103 LYS L 108 -1 O VAL L 105 N ALA L 84 SHEET 6 AA212 SER L 10 SER L 14 1 N ALA L 13 O GLU L 106 SHEET 7 AA212 SER D 10 SER D 14 -1 O SER D 12 N SER L 10 SHEET 8 AA212 THR D 103 LYS D 108 1 O LYS D 108 N ALA D 13 SHEET 9 AA212 ALA D 84 GLN D 90 -1 N ALA D 84 O VAL D 105 SHEET 10 AA212 LEU D 33 GLN D 38 -1 N TYR D 36 O TYR D 87 SHEET 11 AA212 LYS D 45 TYR D 49 -1 O LEU D 47 N TRP D 35 SHEET 12 AA212 SER D 53 LEU D 54 -1 O SER D 53 N TYR D 49 SHEET 1 AA3 8 THR L 98 PHE L 99 0 SHEET 2 AA3 8 ALA L 84 GLN L 90 -1 N GLN L 90 O THR L 98 SHEET 3 AA3 8 THR L 103 LYS L 108 -1 O VAL L 105 N ALA L 84 SHEET 4 AA3 8 SER L 10 SER L 14 1 N ALA L 13 O GLU L 106 SHEET 5 AA3 8 SER D 10 SER D 14 -1 O SER D 12 N SER L 10 SHEET 6 AA3 8 THR D 103 LYS D 108 1 O LYS D 108 N ALA D 13 SHEET 7 AA3 8 ALA D 84 GLN D 90 -1 N ALA D 84 O VAL D 105 SHEET 8 AA3 8 THR D 98 PHE D 99 -1 O THR D 98 N GLN D 90 SHEET 1 AA4 4 SER L 115 PHE L 119 0 SHEET 2 AA4 4 THR L 130 PHE L 140 -1 O LEU L 136 N PHE L 117 SHEET 3 AA4 4 TYR L 174 SER L 183 -1 O LEU L 180 N VAL L 133 SHEET 4 AA4 4 SER L 160 VAL L 164 -1 N GLN L 161 O THR L 179 SHEET 1 AA5 4 ALA L 154 LEU L 155 0 SHEET 2 AA5 4 LYS L 146 VAL L 151 -1 N VAL L 151 O ALA L 154 SHEET 3 AA5 4 VAL L 192 THR L 198 -1 O GLU L 196 N GLN L 148 SHEET 4 AA5 4 VAL L 206 ASN L 211 -1 O VAL L 206 N VAL L 197 SHEET 1 AA6 4 GLN A 3 GLN A 6 0 SHEET 2 AA6 4 LEU A 18 SER A 25 -1 O LYS A 23 N VAL A 5 SHEET 3 AA6 4 THR A 78 TRP A 83 -1 O LEU A 81 N ILE A 20 SHEET 4 AA6 4 THR A 69 ASP A 73 -1 N ASP A 73 O THR A 78 SHEET 1 AA7 6 GLU A 10 LYS A 12 0 SHEET 2 AA7 6 THR A 114 VAL A 118 1 O LEU A 115 N GLU A 10 SHEET 3 AA7 6 ALA A 92 GLN A 100 -1 N ALA A 92 O VAL A 116 SHEET 4 AA7 6 TRP A 33 GLN A 39 -1 N VAL A 37 O TYR A 95 SHEET 5 AA7 6 LEU A 45 ILE A 51 -1 O MET A 48 N TRP A 36 SHEET 6 AA7 6 THR A 58 TYR A 60 -1 O ASN A 59 N ARG A 50 SHEET 1 AA8 4 GLU A 10 LYS A 12 0 SHEET 2 AA8 4 THR A 114 VAL A 118 1 O LEU A 115 N GLU A 10 SHEET 3 AA8 4 ALA A 92 GLN A 100 -1 N ALA A 92 O VAL A 116 SHEET 4 AA8 4 ASN A 106 TRP A 110 -1 O TYR A 109 N ARG A 98 SHEET 1 AA9 4 THR A 127 VAL A 132 0 SHEET 2 AA9 4 SER A 143 PHE A 153 -1 O LEU A 149 N PHE A 129 SHEET 3 AA9 4 LYS A 184 PRO A 194 -1 O ALA A 187 N ALA A 150 SHEET 4 AA9 4 VAL A 179 ARG A 181 -1 N ARG A 181 O LYS A 184 SHEET 1 AB1 3 THR A 159 LYS A 163 0 SHEET 2 AB1 3 HIS A 205 GLN A 211 -1 O VAL A 207 N LYS A 163 SHEET 3 AB1 3 LYS A 217 PRO A 222 -1 O VAL A 221 N VAL A 206 SHEET 1 AB2 4 MET B 4 SER B 7 0 SHEET 2 AB2 4 VAL B 19 ALA B 25 -1 O ARG B 24 N THR B 5 SHEET 3 AB2 4 ASP B 70 ILE B 75 -1 O LEU B 73 N ILE B 21 SHEET 4 AB2 4 PHE B 62 SER B 67 -1 N SER B 63 O THR B 74 SHEET 1 AB3 6 SER B 10 SER B 14 0 SHEET 2 AB3 6 THR B 103 LYS B 108 1 O LYS B 108 N ALA B 13 SHEET 3 AB3 6 ALA B 84 GLN B 90 -1 N ALA B 84 O VAL B 105 SHEET 4 AB3 6 LEU B 33 GLN B 38 -1 N TYR B 36 O TYR B 87 SHEET 5 AB3 6 LYS B 45 TYR B 49 -1 O ILE B 48 N TRP B 35 SHEET 6 AB3 6 SER B 53 LEU B 54 -1 O SER B 53 N TYR B 49 SHEET 1 AB4 4 SER B 115 PHE B 119 0 SHEET 2 AB4 4 THR B 130 PHE B 140 -1 O LEU B 136 N PHE B 117 SHEET 3 AB4 4 TYR B 174 SER B 183 -1 O LEU B 176 N LEU B 137 SHEET 4 AB4 4 SER B 160 VAL B 164 -1 N GLN B 161 O THR B 179 SHEET 1 AB5 4 ALA B 154 LEU B 155 0 SHEET 2 AB5 4 LYS B 146 VAL B 151 -1 N VAL B 151 O ALA B 154 SHEET 3 AB5 4 VAL B 192 THR B 198 -1 O GLU B 196 N GLN B 148 SHEET 4 AB5 4 VAL B 206 ASN B 211 -1 O VAL B 206 N VAL B 197 SHEET 1 AB6 4 MET D 4 SER D 7 0 SHEET 2 AB6 4 VAL D 19 ALA D 25 -1 O ARG D 24 N THR D 5 SHEET 3 AB6 4 ASP D 70 ILE D 75 -1 O LEU D 73 N ILE D 21 SHEET 4 AB6 4 PHE D 62 SER D 67 -1 N SER D 63 O THR D 74 SHEET 1 AB7 4 SER D 115 PHE D 119 0 SHEET 2 AB7 4 THR D 130 PHE D 140 -1 O LEU D 136 N PHE D 117 SHEET 3 AB7 4 TYR D 174 SER D 183 -1 O LEU D 182 N ALA D 131 SHEET 4 AB7 4 SER D 160 VAL D 164 -1 N GLN D 161 O THR D 179 SHEET 1 AB8 4 ALA D 154 LEU D 155 0 SHEET 2 AB8 4 LYS D 146 VAL D 151 -1 N VAL D 151 O ALA D 154 SHEET 3 AB8 4 VAL D 192 THR D 198 -1 O GLU D 196 N GLN D 148 SHEET 4 AB8 4 VAL D 206 ASN D 211 -1 O VAL D 206 N VAL D 197 SHEET 1 AB9 4 MET F 4 SER F 7 0 SHEET 2 AB9 4 VAL F 19 ALA F 25 -1 O ARG F 24 N THR F 5 SHEET 3 AB9 4 ASP F 70 ILE F 75 -1 O LEU F 73 N ILE F 21 SHEET 4 AB9 4 PHE F 62 SER F 67 -1 N SER F 63 O THR F 74 SHEET 1 AC1 6 SER F 10 SER F 14 0 SHEET 2 AC1 6 THR F 103 LYS F 108 1 O LYS F 108 N ALA F 13 SHEET 3 AC1 6 ALA F 84 GLN F 90 -1 N ALA F 84 O VAL F 105 SHEET 4 AC1 6 LEU F 33 GLN F 38 -1 N TYR F 36 O TYR F 87 SHEET 5 AC1 6 LYS F 45 TYR F 49 -1 O LEU F 47 N TRP F 35 SHEET 6 AC1 6 SER F 53 LEU F 54 -1 O SER F 53 N TYR F 49 SHEET 1 AC2 4 SER F 10 SER F 14 0 SHEET 2 AC2 4 THR F 103 LYS F 108 1 O LYS F 108 N ALA F 13 SHEET 3 AC2 4 ALA F 84 GLN F 90 -1 N ALA F 84 O VAL F 105 SHEET 4 AC2 4 THR F 98 PHE F 99 -1 O THR F 98 N GLN F 90 SHEET 1 AC3 4 SER F 115 PHE F 119 0 SHEET 2 AC3 4 THR F 130 PHE F 140 -1 O LEU F 136 N PHE F 117 SHEET 3 AC3 4 TYR F 174 SER F 183 -1 O LEU F 180 N VAL F 133 SHEET 4 AC3 4 SER F 160 VAL F 164 -1 N GLN F 161 O THR F 179 SHEET 1 AC4 4 ALA F 154 LEU F 155 0 SHEET 2 AC4 4 LYS F 146 VAL F 151 -1 N VAL F 151 O ALA F 154 SHEET 3 AC4 4 VAL F 192 THR F 198 -1 O GLU F 196 N GLN F 148 SHEET 4 AC4 4 VAL F 206 ASN F 211 -1 O VAL F 206 N VAL F 197 SHEET 1 AC5 4 GLN H 3 GLN H 6 0 SHEET 2 AC5 4 LEU H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AC5 4 THR H 78 TRP H 83 -1 O LEU H 81 N ILE H 20 SHEET 4 AC5 4 THR H 69 ASP H 73 -1 N ASP H 73 O THR H 78 SHEET 1 AC6 6 GLU H 10 LYS H 12 0 SHEET 2 AC6 6 THR H 114 VAL H 118 1 O LEU H 115 N GLU H 10 SHEET 3 AC6 6 ALA H 92 GLU H 99 -1 N ALA H 92 O VAL H 116 SHEET 4 AC6 6 TRP H 33 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AC6 6 LEU H 45 ILE H 51 -1 O MET H 48 N TRP H 36 SHEET 6 AC6 6 THR H 58 TYR H 60 -1 O ASN H 59 N ARG H 50 SHEET 1 AC7 4 GLU H 10 LYS H 12 0 SHEET 2 AC7 4 THR H 114 VAL H 118 1 O LEU H 115 N GLU H 10 SHEET 3 AC7 4 ALA H 92 GLU H 99 -1 N ALA H 92 O VAL H 116 SHEET 4 AC7 4 PHE H 107 TRP H 110 -1 O TYR H 109 N ARG H 98 SHEET 1 AC8 4 THR H 127 VAL H 132 0 SHEET 2 AC8 4 SER H 143 PHE H 153 -1 O LEU H 149 N PHE H 129 SHEET 3 AC8 4 LYS H 184 PRO H 194 -1 O ALA H 187 N ALA H 150 SHEET 4 AC8 4 THR H 173 GLY H 175 -1 N ARG H 174 O GLN H 190 SHEET 1 AC9 4 THR H 127 VAL H 132 0 SHEET 2 AC9 4 SER H 143 PHE H 153 -1 O LEU H 149 N PHE H 129 SHEET 3 AC9 4 LYS H 184 PRO H 194 -1 O ALA H 187 N ALA H 150 SHEET 4 AC9 4 VAL H 179 ARG H 181 -1 N ARG H 181 O LYS H 184 SHEET 1 AD1 3 THR H 159 LYS H 163 0 SHEET 2 AD1 3 HIS H 205 GLN H 211 -1 O LYS H 209 N SER H 161 SHEET 3 AD1 3 LYS H 217 PRO H 222 -1 O VAL H 221 N VAL H 206 SHEET 1 AD2 4 GLN C 3 GLN C 6 0 SHEET 2 AD2 4 LEU C 18 SER C 25 -1 O LYS C 23 N VAL C 5 SHEET 3 AD2 4 THR C 78 TRP C 83 -1 O LEU C 81 N ILE C 20 SHEET 4 AD2 4 THR C 69 ASP C 73 -1 N ASP C 73 O THR C 78 SHEET 1 AD3 6 GLU C 10 LYS C 12 0 SHEET 2 AD3 6 THR C 114 VAL C 118 1 O LEU C 115 N GLU C 10 SHEET 3 AD3 6 ALA C 92 GLU C 99 -1 N ALA C 92 O VAL C 116 SHEET 4 AD3 6 TRP C 33 GLN C 39 -1 N VAL C 37 O TYR C 95 SHEET 5 AD3 6 LEU C 45 ILE C 51 -1 O MET C 48 N TRP C 36 SHEET 6 AD3 6 THR C 58 TYR C 60 -1 O ASN C 59 N ARG C 50 SHEET 1 AD4 4 GLU C 10 LYS C 12 0 SHEET 2 AD4 4 THR C 114 VAL C 118 1 O LEU C 115 N GLU C 10 SHEET 3 AD4 4 ALA C 92 GLU C 99 -1 N ALA C 92 O VAL C 116 SHEET 4 AD4 4 PHE C 107 TRP C 110 -1 O TYR C 109 N ARG C 98 SHEET 1 AD5 4 THR C 127 VAL C 132 0 SHEET 2 AD5 4 SER C 143 PHE C 153 -1 O LEU C 149 N PHE C 129 SHEET 3 AD5 4 LYS C 184 PRO C 194 -1 O ALA C 187 N ALA C 150 SHEET 4 AD5 4 ARG C 174 GLY C 175 -1 N ARG C 174 O GLN C 190 SHEET 1 AD6 4 THR C 127 VAL C 132 0 SHEET 2 AD6 4 SER C 143 PHE C 153 -1 O LEU C 149 N PHE C 129 SHEET 3 AD6 4 LYS C 184 PRO C 194 -1 O ALA C 187 N ALA C 150 SHEET 4 AD6 4 VAL C 179 ARG C 181 -1 N ARG C 181 O LYS C 184 SHEET 1 AD7 3 THR C 159 LYS C 163 0 SHEET 2 AD7 3 HIS C 205 GLN C 211 -1 O LYS C 209 N SER C 161 SHEET 3 AD7 3 LYS C 217 PRO C 222 -1 O VAL C 221 N VAL C 206 SHEET 1 AD8 4 GLN E 3 GLN E 6 0 SHEET 2 AD8 4 LEU E 18 SER E 25 -1 O LYS E 23 N VAL E 5 SHEET 3 AD8 4 THR E 78 TRP E 83 -1 O LEU E 81 N ILE E 20 SHEET 4 AD8 4 THR E 69 ASP E 73 -1 N ASP E 73 O THR E 78 SHEET 1 AD9 6 GLU E 10 LYS E 12 0 SHEET 2 AD9 6 THR E 114 VAL E 118 1 O LEU E 115 N GLU E 10 SHEET 3 AD9 6 ALA E 92 GLU E 99 -1 N ALA E 92 O VAL E 116 SHEET 4 AD9 6 TRP E 33 GLN E 39 -1 N THR E 35 O ALA E 97 SHEET 5 AD9 6 GLU E 46 ILE E 51 -1 O MET E 48 N TRP E 36 SHEET 6 AD9 6 THR E 58 TYR E 60 -1 O ASN E 59 N ARG E 50 SHEET 1 AE1 4 GLU E 10 LYS E 12 0 SHEET 2 AE1 4 THR E 114 VAL E 118 1 O LEU E 115 N GLU E 10 SHEET 3 AE1 4 ALA E 92 GLU E 99 -1 N ALA E 92 O VAL E 116 SHEET 4 AE1 4 PHE E 107 TRP E 110 -1 O TYR E 109 N ARG E 98 SHEET 1 AE2 4 THR E 127 VAL E 132 0 SHEET 2 AE2 4 SER E 143 PHE E 153 -1 O LEU E 149 N PHE E 129 SHEET 3 AE2 4 LYS E 184 PRO E 194 -1 O VAL E 191 N VAL E 146 SHEET 4 AE2 4 ARG E 174 GLY E 175 -1 N ARG E 174 O GLN E 190 SHEET 1 AE3 4 THR E 127 VAL E 132 0 SHEET 2 AE3 4 SER E 143 PHE E 153 -1 O LEU E 149 N PHE E 129 SHEET 3 AE3 4 LYS E 184 PRO E 194 -1 O VAL E 191 N VAL E 146 SHEET 4 AE3 4 VAL E 179 ARG E 181 -1 N ARG E 181 O LYS E 184 SHEET 1 AE4 3 THR E 159 LYS E 163 0 SHEET 2 AE4 3 HIS E 205 GLN E 211 -1 O LYS E 209 N SER E 161 SHEET 3 AE4 3 LYS E 217 PRO E 222 -1 O VAL E 221 N VAL E 206 SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 2 CYS L 135 CYS L 195 1555 1555 2.04 SSBOND 3 CYS A 22 CYS A 96 1555 1555 2.03 SSBOND 4 CYS A 148 CYS A 208 1555 1555 2.04 SSBOND 5 CYS B 23 CYS B 88 1555 1555 2.04 SSBOND 6 CYS B 135 CYS B 195 1555 1555 2.04 SSBOND 7 CYS D 23 CYS D 88 1555 1555 2.04 SSBOND 8 CYS D 135 CYS D 195 1555 1555 2.04 SSBOND 9 CYS F 23 CYS F 88 1555 1555 2.04 SSBOND 10 CYS F 135 CYS F 195 1555 1555 2.04 SSBOND 11 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 12 CYS H 148 CYS H 208 1555 1555 2.04 SSBOND 13 CYS C 22 CYS C 96 1555 1555 2.04 SSBOND 14 CYS C 148 CYS C 208 1555 1555 2.04 SSBOND 15 CYS E 22 CYS E 96 1555 1555 2.04 SSBOND 16 CYS E 148 CYS E 208 1555 1555 2.03 LINK ND2 ASN A 166 C1 NAG A 301 1555 1555 1.44 LINK ND2 ASN H 166 C1 NAG G 1 1555 1555 1.45 LINK ND2 ASN C 166 C1 NAG C 301 1555 1555 1.44 LINK ND2 ASN E 166 C1 NAG E 301 1555 1555 1.44 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.45 LINK O6 NAG G 1 C1 FUC G 3 1555 1555 1.45 CISPEP 1 SER L 7 PRO L 8 0 -3.65 CISPEP 2 THR L 94 PRO L 95 0 -15.62 CISPEP 3 PRO L 95 PRO L 96 0 -9.87 CISPEP 4 TYR L 141 PRO L 142 0 3.33 CISPEP 5 LEU A 154 PRO A 155 0 5.49 CISPEP 6 SER B 7 PRO B 8 0 -2.24 CISPEP 7 TYR B 141 PRO B 142 0 4.11 CISPEP 8 SER D 7 PRO D 8 0 -3.83 CISPEP 9 THR D 94 PRO D 95 0 -22.14 CISPEP 10 PRO D 95 PRO D 96 0 -11.49 CISPEP 11 TYR D 141 PRO D 142 0 3.10 CISPEP 12 SER F 7 PRO F 8 0 -1.53 CISPEP 13 THR F 94 PRO F 95 0 -11.59 CISPEP 14 PRO F 95 PRO F 96 0 -14.00 CISPEP 15 TYR F 141 PRO F 142 0 3.93 CISPEP 16 LEU H 154 PRO H 155 0 5.76 CISPEP 17 LEU C 154 PRO C 155 0 5.85 CISPEP 18 LEU E 154 PRO E 155 0 5.93 CRYST1 125.416 128.509 134.650 90.00 90.00 90.00 P 21 21 21 16 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 0.007973 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007782 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007427 0.00000 MTRIX1 1 -0.941683 0.320730 0.101807 11.72806 1 MTRIX2 1 -0.198420 -0.284894 -0.937798 -80.80895 1 MTRIX3 1 -0.271776 -0.903309 0.331919 -29.04413 1 MTRIX1 2 0.966917 -0.247794 -0.060572 87.64545 1 MTRIX2 2 -0.210391 -0.908951 0.359921 -123.17159 1 MTRIX3 2 -0.144243 -0.335270 -0.931015 16.54156 1 MTRIX1 3 0.995883 -0.000306 -0.090646 30.23814 1 MTRIX2 3 0.090592 0.037757 0.995172 -26.62761 1 MTRIX3 3 0.003118 -0.999287 0.037629 -32.57341 1 MTRIX1 4 -0.965422 0.259367 0.026247 6.83353 1 MTRIX2 4 -0.106927 -0.302149 -0.947245 -79.14010 1 MTRIX3 4 -0.237754 -0.917297 0.319435 -28.44101 1 MTRIX1 5 0.982167 -0.187852 0.007753 92.03496 1 MTRIX2 5 -0.178058 -0.916135 0.359153 -122.08910 1 MTRIX3 5 -0.060364 -0.354129 -0.933246 17.85120 1 MTRIX1 6 0.998399 0.025147 -0.050665 31.97979 1 MTRIX2 6 0.049755 0.035598 0.998127 -28.20243 1 MTRIX3 6 0.026903 -0.999050 0.034289 -31.77201 1