HEADER IMMUNE SYSTEM 17-SEP-25 9WU2 TITLE CRYSTAL STRUCTURE OF CZ22-FAB IN COMPLEX WITH LEFT-HANDED DC(GC)3 DNA COMPND MOL_ID: 1; COMPND 2 MOLECULE: CZ22-FAB HEAVY CHAIN; COMPND 3 CHAIN: A, C, G, I, M, O; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: CZ22-FAB LIGHT CHAIN; COMPND 7 CHAIN: B, D, H, J, N, P; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: DNA (5'-D(*CP*GP*CP*GP*CP*GP*C)-3'); COMPND 11 CHAIN: E, F, K, L, Q, R; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_TAXID: 10090; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM: SYNTHESIUM; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 638370 KEYWDS ANTIBODY, Z-DNA, COMPLEX, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR C.C.LEE,S.F.HSU,T.P.KO,A.H.J.WANG REVDAT 1 18-FEB-26 9WU2 0 JRNL AUTH C.C.LEE,S.F.HSU,Y.W.CHANG,Y.W.CHEN,M.R.HO,H.SUGIYAMA, JRNL AUTH 2 A.H.J.WANG JRNL TITL STRUCTURAL BASIS OF B-TO-Z DNA TRANSITION DRIVEN BY AN JRNL TITL 2 ANTI-Z-DNA ANTIBODY JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.35 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) : 2.35 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 17.92 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0 REMARK 3 NUMBER OF REFLECTIONS : 155585 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.171 REMARK 3 R VALUE (WORKING SET) : 0.169 REMARK 3 FREE R VALUE : 0.210 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980 REMARK 3 FREE R VALUE TEST SET COUNT : 7751 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 17.9200 - 7.1500 0.99 4947 274 0.1463 0.1604 REMARK 3 2 7.1500 - 5.7400 1.00 4956 316 0.1670 0.1899 REMARK 3 3 5.7400 - 5.0300 0.99 4995 262 0.1380 0.1731 REMARK 3 4 5.0300 - 4.5800 1.00 5058 238 0.1175 0.1450 REMARK 3 5 4.5800 - 4.2600 1.00 5003 274 0.1159 0.1384 REMARK 3 6 4.2600 - 4.0100 1.00 5018 257 0.1321 0.1747 REMARK 3 7 4.0100 - 3.8100 1.00 5067 233 0.1472 0.1756 REMARK 3 8 3.8100 - 3.6400 1.00 5002 253 0.1540 0.1901 REMARK 3 9 3.6400 - 3.5100 1.00 5050 271 0.1514 0.2020 REMARK 3 10 3.5100 - 3.3900 1.00 5072 210 0.1621 0.1964 REMARK 3 11 3.3800 - 3.2800 1.00 5018 245 0.1768 0.2341 REMARK 3 12 3.2800 - 3.1900 1.00 4991 263 0.1802 0.2290 REMARK 3 13 3.1900 - 3.1000 1.00 5029 270 0.1773 0.2298 REMARK 3 14 3.1000 - 3.0300 1.00 5063 238 0.1925 0.2425 REMARK 3 15 3.0300 - 2.9600 1.00 5029 252 0.1930 0.2455 REMARK 3 16 2.9600 - 2.9000 1.00 4963 289 0.1986 0.2595 REMARK 3 17 2.9000 - 2.8400 1.00 4981 302 0.1981 0.2439 REMARK 3 18 2.8400 - 2.7900 1.00 4964 278 0.1971 0.2451 REMARK 3 19 2.7900 - 2.7400 0.99 4950 314 0.1972 0.2507 REMARK 3 20 2.7400 - 2.6900 0.99 4988 305 0.2049 0.2515 REMARK 3 21 2.6900 - 2.6500 1.00 5041 230 0.2089 0.2441 REMARK 3 22 2.6500 - 2.6100 0.99 4941 278 0.2170 0.2822 REMARK 3 23 2.6100 - 2.5700 0.99 4997 288 0.2150 0.2797 REMARK 3 24 2.5700 - 2.5300 0.99 5009 253 0.2283 0.2824 REMARK 3 25 2.5300 - 2.5000 0.98 4959 201 0.2276 0.2757 REMARK 3 26 2.5000 - 2.4700 0.97 4872 287 0.2288 0.2704 REMARK 3 27 2.4700 - 2.4300 0.98 4970 202 0.2312 0.2818 REMARK 3 28 2.4300 - 2.4100 0.94 4748 238 0.2411 0.2858 REMARK 3 29 2.4100 - 2.3800 0.88 4465 211 0.2447 0.2681 REMARK 3 30 2.3800 - 2.3500 0.74 3688 219 0.2442 0.3031 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) : 0.265 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.163 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 32.08 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.18 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 : 0.011 21093 REMARK 3 ANGLE : 1.218 28798 REMARK 3 CHIRALITY : 0.073 3215 REMARK 3 PLANARITY : 0.012 3533 REMARK 3 DIHEDRAL : 14.226 7672 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 51 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 4 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): 81.3597 31.2550 9.5334 REMARK 3 T TENSOR REMARK 3 T11: 0.2076 T22: 0.2932 REMARK 3 T33: 0.3521 T12: -0.0148 REMARK 3 T13: -0.0976 T23: 0.0862 REMARK 3 L TENSOR REMARK 3 L11: 0.1846 L22: 0.4507 REMARK 3 L33: 0.1756 L12: 0.0043 REMARK 3 L13: 0.1519 L23: 0.0613 REMARK 3 S TENSOR REMARK 3 S11: 0.0481 S12: 0.2117 S13: 0.2120 REMARK 3 S21: 0.2448 S22: -0.1046 S23: -0.1067 REMARK 3 S31: -0.1103 S32: 0.2624 S33: -0.1149 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 121 THROUGH 222 ) REMARK 3 ORIGIN FOR THE GROUP (A): 88.5661 -0.9382 19.4897 REMARK 3 T TENSOR REMARK 3 T11: 0.2890 T22: 0.3385 REMARK 3 T33: 0.3335 T12: 0.0162 REMARK 3 T13: 0.0444 T23: 0.0784 REMARK 3 L TENSOR REMARK 3 L11: 0.1639 L22: 0.0821 REMARK 3 L33: 0.3244 L12: -0.0907 REMARK 3 L13: 0.2372 L23: -0.1243 REMARK 3 S TENSOR REMARK 3 S11: -0.1327 S12: -0.0552 S13: 0.1514 REMARK 3 S21: 0.0754 S22: -0.2083 S23: -0.2191 REMARK 3 S31: -0.0628 S32: 0.4891 S33: -0.1036 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 90 ) REMARK 3 ORIGIN FOR THE GROUP (A): 68.7505 18.3140 -4.4479 REMARK 3 T TENSOR REMARK 3 T11: 0.2773 T22: 0.3268 REMARK 3 T33: 0.3407 T12: 0.0739 REMARK 3 T13: -0.1584 T23: -0.0216 REMARK 3 L TENSOR REMARK 3 L11: 0.2068 L22: 0.1719 REMARK 3 L33: 0.1062 L12: 0.0803 REMARK 3 L13: -0.0676 L23: -0.0267 REMARK 3 S TENSOR REMARK 3 S11: 0.2660 S12: 0.3946 S13: -0.0958 REMARK 3 S21: -0.1685 S22: -0.0761 S23: 0.2889 REMARK 3 S31: 0.3105 S32: 0.0612 S33: 0.3130 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 91 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): 68.6547 13.6434 2.1683 REMARK 3 T TENSOR REMARK 3 T11: 0.2983 T22: 0.2770 REMARK 3 T33: 0.3452 T12: -0.0241 REMARK 3 T13: -0.0866 T23: 0.0033 REMARK 3 L TENSOR REMARK 3 L11: 0.0112 L22: 0.0011 REMARK 3 L33: 0.1128 L12: -0.0021 REMARK 3 L13: -0.0476 L23: -0.0008 REMARK 3 S TENSOR REMARK 3 S11: -0.0003 S12: 0.0641 S13: 0.0393 REMARK 3 S21: 0.0187 S22: 0.0379 S23: 0.0504 REMARK 3 S31: 0.2102 S32: -0.2322 S33: -0.0036 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 114 THROUGH 150 ) REMARK 3 ORIGIN FOR THE GROUP (A): 76.8473 -8.8020 20.9147 REMARK 3 T TENSOR REMARK 3 T11: 0.3963 T22: 0.3323 REMARK 3 T33: 0.2308 T12: 0.0007 REMARK 3 T13: 0.0432 T23: -0.0153 REMARK 3 L TENSOR REMARK 3 L11: 0.0186 L22: 0.0485 REMARK 3 L33: 0.0252 L12: 0.0251 REMARK 3 L13: -0.0211 L23: -0.0211 REMARK 3 S TENSOR REMARK 3 S11: -0.1725 S12: -0.1999 S13: -0.0023 REMARK 3 S21: -0.0271 S22: -0.1796 S23: 0.0842 REMARK 3 S31: 0.1812 S32: -0.1036 S33: -0.0007 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 151 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 73.5274 -10.4328 21.4535 REMARK 3 T TENSOR REMARK 3 T11: 0.4256 T22: 0.3888 REMARK 3 T33: 0.2231 T12: -0.0910 REMARK 3 T13: 0.0902 T23: -0.0258 REMARK 3 L TENSOR REMARK 3 L11: 0.3111 L22: 0.1175 REMARK 3 L33: 0.0796 L12: 0.1005 REMARK 3 L13: 0.0949 L23: -0.0291 REMARK 3 S TENSOR REMARK 3 S11: -0.1956 S12: -0.2648 S13: 0.0977 REMARK 3 S21: 0.0656 S22: -0.1589 S23: 0.0090 REMARK 3 S31: 0.3550 S32: -0.6306 S33: -0.2242 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 4 THROUGH 62 ) REMARK 3 ORIGIN FOR THE GROUP (A): 60.2744 61.8614 -19.5499 REMARK 3 T TENSOR REMARK 3 T11: 0.1702 T22: 0.2218 REMARK 3 T33: 0.2502 T12: -0.0372 REMARK 3 T13: -0.0230 T23: 0.0432 REMARK 3 L TENSOR REMARK 3 L11: 0.0612 L22: 0.1605 REMARK 3 L33: 0.0844 L12: -0.0275 REMARK 3 L13: -0.0411 L23: -0.0491 REMARK 3 S TENSOR REMARK 3 S11: -0.0353 S12: 0.1080 S13: 0.1109 REMARK 3 S21: 0.0342 S22: 0.0018 S23: -0.1645 REMARK 3 S31: -0.0275 S32: 0.0058 S33: 0.0088 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 63 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): 58.8481 61.0945 -20.8094 REMARK 3 T TENSOR REMARK 3 T11: 0.2295 T22: 0.2289 REMARK 3 T33: 0.2457 T12: -0.0004 REMARK 3 T13: -0.0016 T23: 0.0270 REMARK 3 L TENSOR REMARK 3 L11: 0.1003 L22: 0.0602 REMARK 3 L33: 0.0859 L12: -0.0555 REMARK 3 L13: 0.0213 L23: -0.0639 REMARK 3 S TENSOR REMARK 3 S11: 0.0001 S12: 0.0524 S13: 0.0500 REMARK 3 S21: 0.0243 S22: -0.0399 S23: -0.1185 REMARK 3 S31: -0.0459 S32: 0.0290 S33: 0.0000 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 121 THROUGH 223 ) REMARK 3 ORIGIN FOR THE GROUP (A): 35.7298 80.5685 -30.6015 REMARK 3 T TENSOR REMARK 3 T11: 0.2244 T22: 0.2254 REMARK 3 T33: 0.2901 T12: -0.1026 REMARK 3 T13: 0.0398 T23: -0.0492 REMARK 3 L TENSOR REMARK 3 L11: 0.2441 L22: 0.1613 REMARK 3 L33: 0.3221 L12: -0.0872 REMARK 3 L13: -0.0068 L23: -0.0962 REMARK 3 S TENSOR REMARK 3 S11: 0.1521 S12: -0.0760 S13: 0.2395 REMARK 3 S21: -0.0297 S22: -0.0801 S23: 0.0557 REMARK 3 S31: -0.1767 S32: 0.1656 S33: 0.0313 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): 36.5510 52.7651 -9.8353 REMARK 3 T TENSOR REMARK 3 T11: 0.2132 T22: 0.3993 REMARK 3 T33: 0.2741 T12: -0.0204 REMARK 3 T13: 0.0131 T23: -0.0167 REMARK 3 L TENSOR REMARK 3 L11: 0.0189 L22: 0.0275 REMARK 3 L33: 0.0053 L12: 0.0237 REMARK 3 L13: -0.0032 L23: 0.0053 REMARK 3 S TENSOR REMARK 3 S11: 0.0435 S12: -0.0713 S13: -0.1570 REMARK 3 S21: -0.1225 S22: 0.0586 S23: -0.0594 REMARK 3 S31: 0.0636 S32: -0.1769 S33: -0.0006 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 19 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 45.4357 55.0776 -4.4295 REMARK 3 T TENSOR REMARK 3 T11: 0.1951 T22: 0.2702 REMARK 3 T33: 0.2486 T12: 0.0284 REMARK 3 T13: 0.0227 T23: 0.0455 REMARK 3 L TENSOR REMARK 3 L11: 0.0974 L22: 0.0165 REMARK 3 L33: 0.0442 L12: -0.0104 REMARK 3 L13: -0.0669 L23: 0.0102 REMARK 3 S TENSOR REMARK 3 S11: -0.0071 S12: -0.3114 S13: -0.0053 REMARK 3 S21: 0.0646 S22: 0.0438 S23: -0.0487 REMARK 3 S31: 0.0764 S32: -0.1193 S33: 0.0000 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 76 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): 39.0112 58.8949 -10.2150 REMARK 3 T TENSOR REMARK 3 T11: 0.1769 T22: 0.2824 REMARK 3 T33: 0.2249 T12: 0.0107 REMARK 3 T13: 0.0151 T23: 0.0329 REMARK 3 L TENSOR REMARK 3 L11: 0.0230 L22: 0.0397 REMARK 3 L33: -0.0069 L12: 0.0301 REMARK 3 L13: -0.0038 L23: -0.0054 REMARK 3 S TENSOR REMARK 3 S11: -0.0094 S12: -0.1090 S13: -0.0144 REMARK 3 S21: 0.0747 S22: 0.0052 S23: -0.0439 REMARK 3 S31: 0.0880 S32: -0.1839 S33: -0.0047 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 114 THROUGH 150 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.5612 75.1986 -31.6085 REMARK 3 T TENSOR REMARK 3 T11: 0.1761 T22: 0.3430 REMARK 3 T33: 0.2290 T12: -0.0290 REMARK 3 T13: -0.0102 T23: 0.0491 REMARK 3 L TENSOR REMARK 3 L11: 0.0253 L22: 0.0226 REMARK 3 L33: 0.0223 L12: -0.0119 REMARK 3 L13: -0.0119 L23: 0.0009 REMARK 3 S TENSOR REMARK 3 S11: 0.0350 S12: 0.0521 S13: 0.1770 REMARK 3 S21: -0.0389 S22: 0.0012 S23: 0.1761 REMARK 3 S31: -0.0192 S32: -0.0608 S33: -0.0003 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 151 THROUGH 163 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.5766 68.0843 -36.4513 REMARK 3 T TENSOR REMARK 3 T11: 0.2130 T22: 0.3916 REMARK 3 T33: 0.2038 T12: -0.0868 REMARK 3 T13: -0.0528 T23: -0.0244 REMARK 3 L TENSOR REMARK 3 L11: 0.0043 L22: 0.0237 REMARK 3 L33: 0.0030 L12: 0.0104 REMARK 3 L13: -0.0022 L23: -0.0040 REMARK 3 S TENSOR REMARK 3 S11: -0.1078 S12: 0.0948 S13: -0.0128 REMARK 3 S21: -0.0786 S22: -0.0197 S23: -0.0704 REMARK 3 S31: -0.0039 S32: -0.0909 S33: -0.0189 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 164 THROUGH 197 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.3506 73.4347 -31.5657 REMARK 3 T TENSOR REMARK 3 T11: 0.1640 T22: 0.4354 REMARK 3 T33: 0.2128 T12: -0.0558 REMARK 3 T13: -0.0218 T23: 0.0198 REMARK 3 L TENSOR REMARK 3 L11: 0.0545 L22: 0.0143 REMARK 3 L33: 0.0494 L12: 0.0300 REMARK 3 L13: -0.0484 L23: -0.0258 REMARK 3 S TENSOR REMARK 3 S11: 0.0628 S12: 0.0846 S13: 0.0427 REMARK 3 S21: -0.0193 S22: 0.0051 S23: 0.1667 REMARK 3 S31: 0.0103 S32: -0.1682 S33: 0.0299 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 198 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.9113 76.7284 -29.6511 REMARK 3 T TENSOR REMARK 3 T11: 0.0908 T22: 0.5059 REMARK 3 T33: 0.3179 T12: -0.0335 REMARK 3 T13: -0.0902 T23: 0.1107 REMARK 3 L TENSOR REMARK 3 L11: 0.0044 L22: 0.0514 REMARK 3 L33: 0.0405 L12: -0.0078 REMARK 3 L13: 0.0057 L23: 0.0162 REMARK 3 S TENSOR REMARK 3 S11: 0.0205 S12: 0.0667 S13: 0.0854 REMARK 3 S21: -0.0495 S22: -0.1077 S23: 0.0833 REMARK 3 S31: -0.0270 S32: -0.1046 S33: -0.0962 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 1 THROUGH 7 ) REMARK 3 ORIGIN FOR THE GROUP (A): 66.3322 45.4600 -7.9871 REMARK 3 T TENSOR REMARK 3 T11: 0.2286 T22: 0.3657 REMARK 3 T33: 0.3084 T12: 0.0385 REMARK 3 T13: -0.0102 T23: 0.0479 REMARK 3 L TENSOR REMARK 3 L11: 0.0141 L22: 0.0050 REMARK 3 L33: 0.0060 L12: -0.0095 REMARK 3 L13: 0.0081 L23: -0.0024 REMARK 3 S TENSOR REMARK 3 S11: 0.0364 S12: -0.0006 S13: -0.0105 REMARK 3 S21: -0.0138 S22: -0.0319 S23: -0.0055 REMARK 3 S31: -0.0388 S32: 0.1102 S33: 0.0000 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 1 THROUGH 7 ) REMARK 3 ORIGIN FOR THE GROUP (A): 67.6800 43.8393 -1.7291 REMARK 3 T TENSOR REMARK 3 T11: 0.4249 T22: 0.3902 REMARK 3 T33: 0.3149 T12: 0.0779 REMARK 3 T13: 0.0035 T23: 0.1529 REMARK 3 L TENSOR REMARK 3 L11: 0.0257 L22: 0.0131 REMARK 3 L33: 0.0175 L12: 0.0096 REMARK 3 L13: 0.0210 L23: 0.0016 REMARK 3 S TENSOR REMARK 3 S11: -0.0117 S12: -0.0383 S13: -0.0727 REMARK 3 S21: 0.2101 S22: -0.1222 S23: -0.1394 REMARK 3 S31: -0.1385 S32: 0.0272 S33: -0.0425 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 4 THROUGH 62 ) REMARK 3 ORIGIN FOR THE GROUP (A): 34.3726 6.0953 38.3438 REMARK 3 T TENSOR REMARK 3 T11: 0.3489 T22: 0.2753 REMARK 3 T33: 0.4050 T12: 0.0229 REMARK 3 T13: 0.0768 T23: -0.1182 REMARK 3 L TENSOR REMARK 3 L11: 0.1304 L22: 0.1881 REMARK 3 L33: 0.4094 L12: -0.0928 REMARK 3 L13: 0.1946 L23: -0.2309 REMARK 3 S TENSOR REMARK 3 S11: 0.2913 S12: -0.1649 S13: 0.1341 REMARK 3 S21: -0.0431 S22: 0.0117 S23: 0.2006 REMARK 3 S31: 0.1158 S32: -0.1042 S33: 0.1447 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 63 THROUGH 108 ) REMARK 3 ORIGIN FOR THE GROUP (A): 34.4039 4.4360 40.2241 REMARK 3 T TENSOR REMARK 3 T11: 0.3988 T22: 0.2975 REMARK 3 T33: 0.3872 T12: -0.0002 REMARK 3 T13: 0.0799 T23: -0.1026 REMARK 3 L TENSOR REMARK 3 L11: 0.0328 L22: 0.0465 REMARK 3 L33: 0.0884 L12: 0.0340 REMARK 3 L13: 0.0415 L23: 0.0287 REMARK 3 S TENSOR REMARK 3 S11: 0.3514 S12: -0.1489 S13: 0.0877 REMARK 3 S21: 0.0452 S22: -0.1297 S23: 0.1457 REMARK 3 S31: 0.1316 S32: -0.1470 S33: 0.0069 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 109 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): 41.6784 10.3874 37.6407 REMARK 3 T TENSOR REMARK 3 T11: 0.4520 T22: 0.2305 REMARK 3 T33: 0.4142 T12: -0.0451 REMARK 3 T13: 0.0859 T23: -0.1184 REMARK 3 L TENSOR REMARK 3 L11: 0.0476 L22: 0.0072 REMARK 3 L33: 0.0608 L12: -0.0088 REMARK 3 L13: 0.0094 L23: 0.0052 REMARK 3 S TENSOR REMARK 3 S11: 0.1271 S12: -0.0458 S13: 0.0265 REMARK 3 S21: -0.1196 S22: -0.0245 S23: 0.0347 REMARK 3 S31: -0.0122 S32: 0.0512 S33: 0.0010 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 121 THROUGH 194 ) REMARK 3 ORIGIN FOR THE GROUP (A): 59.4889 23.9109 49.8121 REMARK 3 T TENSOR REMARK 3 T11: 0.2929 T22: 0.2260 REMARK 3 T33: 0.2501 T12: 0.0875 REMARK 3 T13: 0.0049 T23: 0.0668 REMARK 3 L TENSOR REMARK 3 L11: 0.0517 L22: 0.1443 REMARK 3 L33: 0.2002 L12: 0.0371 REMARK 3 L13: -0.0019 L23: 0.1497 REMARK 3 S TENSOR REMARK 3 S11: 0.0077 S12: 0.1657 S13: 0.1360 REMARK 3 S21: 0.1473 S22: -0.0996 S23: -0.0524 REMARK 3 S31: -0.1278 S32: -0.0874 S33: -0.0430 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 195 THROUGH 212 ) REMARK 3 ORIGIN FOR THE GROUP (A): 59.7564 34.0079 46.9389 REMARK 3 T TENSOR REMARK 3 T11: 0.3716 T22: 0.1810 REMARK 3 T33: 0.3635 T12: 0.1042 REMARK 3 T13: 0.0354 T23: 0.1275 REMARK 3 L TENSOR REMARK 3 L11: 0.0004 L22: 0.0248 REMARK 3 L33: 0.0557 L12: 0.0050 REMARK 3 L13: 0.0066 L23: 0.0367 REMARK 3 S TENSOR REMARK 3 S11: -0.1150 S12: -0.0314 S13: 0.0472 REMARK 3 S21: 0.0793 S22: 0.0330 S23: 0.0174 REMARK 3 S31: -0.1455 S32: -0.0465 S33: -0.0363 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 213 THROUGH 223 ) REMARK 3 ORIGIN FOR THE GROUP (A): 58.6340 34.3038 53.0357 REMARK 3 T TENSOR REMARK 3 T11: 0.5499 T22: 0.3020 REMARK 3 T33: 0.4452 T12: 0.1352 REMARK 3 T13: 0.0427 T23: 0.0357 REMARK 3 L TENSOR REMARK 3 L11: 0.2671 L22: 0.0322 REMARK 3 L33: 0.0057 L12: 0.0569 REMARK 3 L13: 0.0034 L23: 0.0054 REMARK 3 S TENSOR REMARK 3 S11: -0.0091 S12: -0.0170 S13: 0.0283 REMARK 3 S21: 0.0336 S22: -0.0198 S23: -0.1447 REMARK 3 S31: -0.1499 S32: 0.0636 S33: -0.0001 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): 59.0488 -1.1715 29.6979 REMARK 3 T TENSOR REMARK 3 T11: 0.4756 T22: 0.6691 REMARK 3 T33: 0.3936 T12: 0.2634 REMARK 3 T13: 0.0496 T23: -0.1771 REMARK 3 L TENSOR REMARK 3 L11: 0.1851 L22: 0.0155 REMARK 3 L33: 0.0638 L12: -0.0087 REMARK 3 L13: -0.0412 L23: -0.0273 REMARK 3 S TENSOR REMARK 3 S11: 0.0926 S12: -0.0366 S13: -0.0192 REMARK 3 S21: 0.0185 S22: 0.1888 S23: -0.0989 REMARK 3 S31: 0.0601 S32: 0.2967 S33: 0.1191 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 19 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 50.0851 -0.2525 23.9510 REMARK 3 T TENSOR REMARK 3 T11: 0.3629 T22: 0.0652 REMARK 3 T33: 0.0956 T12: 0.4252 REMARK 3 T13: 0.2103 T23: -0.5827 REMARK 3 L TENSOR REMARK 3 L11: 0.0040 L22: 0.0662 REMARK 3 L33: 0.0666 L12: 0.0150 REMARK 3 L13: -0.0095 L23: 0.0657 REMARK 3 S TENSOR REMARK 3 S11: 0.1120 S12: 0.1223 S13: -0.0624 REMARK 3 S21: -0.0707 S22: 0.1554 S23: -0.2336 REMARK 3 S31: 0.3027 S32: 0.4123 S33: 0.3148 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 76 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): 56.1677 4.3649 29.5335 REMARK 3 T TENSOR REMARK 3 T11: 0.4281 T22: 0.3962 REMARK 3 T33: 0.3475 T12: 0.1118 REMARK 3 T13: 0.0491 T23: -0.1488 REMARK 3 L TENSOR REMARK 3 L11: 0.0345 L22: 0.1131 REMARK 3 L33: 0.1650 L12: -0.0214 REMARK 3 L13: 0.0890 L23: -0.0621 REMARK 3 S TENSOR REMARK 3 S11: 0.1149 S12: 0.0374 S13: -0.0147 REMARK 3 S21: -0.1545 S22: -0.0283 S23: -0.0933 REMARK 3 S31: 0.2645 S32: 0.4214 S33: 0.1952 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 114 THROUGH 174 ) REMARK 3 ORIGIN FOR THE GROUP (A): 71.5654 18.9512 48.7731 REMARK 3 T TENSOR REMARK 3 T11: 0.3323 T22: 0.4828 REMARK 3 T33: 0.3690 T12: 0.0715 REMARK 3 T13: -0.0653 T23: 0.0032 REMARK 3 L TENSOR REMARK 3 L11: 0.0789 L22: 0.1233 REMARK 3 L33: 0.0470 L12: 0.0646 REMARK 3 L13: -0.0547 L23: -0.0091 REMARK 3 S TENSOR REMARK 3 S11: -0.0165 S12: 0.0737 S13: -0.0693 REMARK 3 S21: 0.1882 S22: -0.0620 S23: -0.4631 REMARK 3 S31: -0.0014 S32: 0.2677 S33: -0.0025 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 175 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 78.2787 21.1340 55.0712 REMARK 3 T TENSOR REMARK 3 T11: 0.2350 T22: 0.7250 REMARK 3 T33: 0.4092 T12: 0.0805 REMARK 3 T13: -0.2263 T23: -0.0257 REMARK 3 L TENSOR REMARK 3 L11: 0.0101 L22: 0.1593 REMARK 3 L33: 0.0158 L12: 0.0137 REMARK 3 L13: 0.0012 L23: -0.0264 REMARK 3 S TENSOR REMARK 3 S11: 0.0269 S12: -0.1185 S13: -0.0384 REMARK 3 S21: 0.2156 S22: -0.0496 S23: -0.2898 REMARK 3 S31: -0.0010 S32: 0.1883 S33: -0.0010 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 4 THROUGH 62 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.0314 -27.4192 10.3120 REMARK 3 T TENSOR REMARK 3 T11: 0.4496 T22: 0.2775 REMARK 3 T33: 0.3088 T12: 0.1298 REMARK 3 T13: -0.1081 T23: -0.1095 REMARK 3 L TENSOR REMARK 3 L11: 0.0633 L22: 0.0605 REMARK 3 L33: 0.0561 L12: -0.0098 REMARK 3 L13: 0.0575 L23: -0.0304 REMARK 3 S TENSOR REMARK 3 S11: -0.0089 S12: 0.0129 S13: 0.1057 REMARK 3 S21: -0.1803 S22: -0.1311 S23: 0.0953 REMARK 3 S31: -0.2881 S32: -0.1678 S33: -0.0947 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 63 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.3681 -28.3230 9.1040 REMARK 3 T TENSOR REMARK 3 T11: 0.4673 T22: 0.2681 REMARK 3 T33: 0.2952 T12: 0.0840 REMARK 3 T13: -0.1072 T23: -0.0665 REMARK 3 L TENSOR REMARK 3 L11: 0.0295 L22: 0.0732 REMARK 3 L33: 0.0562 L12: 0.0520 REMARK 3 L13: 0.0282 L23: 0.0379 REMARK 3 S TENSOR REMARK 3 S11: -0.0176 S12: -0.0191 S13: 0.0278 REMARK 3 S21: -0.2159 S22: -0.1382 S23: 0.1414 REMARK 3 S31: -0.3589 S32: -0.2308 S33: -0.0040 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 121 THROUGH 223 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.6869 -58.2471 -0.6095 REMARK 3 T TENSOR REMARK 3 T11: 0.2321 T22: 0.3647 REMARK 3 T33: 0.2462 T12: 0.0225 REMARK 3 T13: 0.0047 T23: -0.0401 REMARK 3 L TENSOR REMARK 3 L11: 0.0430 L22: 0.1397 REMARK 3 L33: 0.2614 L12: 0.0749 REMARK 3 L13: 0.0762 L23: 0.1746 REMARK 3 S TENSOR REMARK 3 S11: -0.1487 S12: -0.0880 S13: 0.0415 REMARK 3 S21: -0.1682 S22: -0.1205 S23: 0.0682 REMARK 3 S31: -0.1282 S32: -0.4357 S33: -0.0443 REMARK 3 TLS GROUP : 33 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 1 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 32.8872 -38.5694 24.1388 REMARK 3 T TENSOR REMARK 3 T11: 0.3715 T22: 0.1937 REMARK 3 T33: 0.2782 T12: 0.0153 REMARK 3 T13: -0.0832 T23: -0.0357 REMARK 3 L TENSOR REMARK 3 L11: 0.0492 L22: 0.1045 REMARK 3 L33: 0.0709 L12: -0.0683 REMARK 3 L13: 0.0311 L23: -0.0583 REMARK 3 S TENSOR REMARK 3 S11: -0.0357 S12: -0.1124 S13: 0.0133 REMARK 3 S21: 0.1572 S22: 0.0313 S23: -0.0669 REMARK 3 S31: 0.0711 S32: 0.0934 S33: 0.0000 REMARK 3 TLS GROUP : 34 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 76 THROUGH 128 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.4627 -51.0097 12.0975 REMARK 3 T TENSOR REMARK 3 T11: 0.3329 T22: 0.2023 REMARK 3 T33: 0.2350 T12: -0.0038 REMARK 3 T13: -0.0533 T23: -0.0068 REMARK 3 L TENSOR REMARK 3 L11: 0.1009 L22: 0.0642 REMARK 3 L33: 0.1021 L12: 0.0160 REMARK 3 L13: -0.1265 L23: 0.0006 REMARK 3 S TENSOR REMARK 3 S11: -0.0739 S12: 0.0492 S13: 0.0305 REMARK 3 S21: 0.0823 S22: 0.0288 S23: 0.0420 REMARK 3 S31: -0.0127 S32: -0.0449 S33: -0.0002 REMARK 3 TLS GROUP : 35 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 129 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 28.6387 -67.8915 -1.0598 REMARK 3 T TENSOR REMARK 3 T11: 0.3062 T22: 0.2635 REMARK 3 T33: 0.1989 T12: 0.0171 REMARK 3 T13: 0.0420 T23: 0.0103 REMARK 3 L TENSOR REMARK 3 L11: 0.1669 L22: 0.1762 REMARK 3 L33: 0.0631 L12: -0.1183 REMARK 3 L13: 0.0763 L23: -0.0992 REMARK 3 S TENSOR REMARK 3 S11: -0.1140 S12: 0.0876 S13: 0.0491 REMARK 3 S21: -0.0355 S22: 0.0555 S23: -0.0648 REMARK 3 S31: 0.2294 S32: 0.2061 S33: -0.0381 REMARK 3 TLS GROUP : 36 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 1 THROUGH 7 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.5005 -14.2651 21.9633 REMARK 3 T TENSOR REMARK 3 T11: 0.7904 T22: 0.2392 REMARK 3 T33: 0.3217 T12: 0.0705 REMARK 3 T13: -0.0816 T23: -0.0657 REMARK 3 L TENSOR REMARK 3 L11: 0.0362 L22: 0.0050 REMARK 3 L33: 0.0287 L12: -0.0104 REMARK 3 L13: 0.0332 L23: -0.0095 REMARK 3 S TENSOR REMARK 3 S11: 0.0110 S12: 0.0079 S13: 0.0078 REMARK 3 S21: -0.0666 S22: 0.0051 S23: 0.0121 REMARK 3 S31: -0.0590 S32: 0.0047 S33: -0.0016 REMARK 3 TLS GROUP : 37 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 7 ) REMARK 3 ORIGIN FOR THE GROUP (A): 30.6606 -12.0347 27.7373 REMARK 3 T TENSOR REMARK 3 T11: 0.6700 T22: 0.3075 REMARK 3 T33: 0.3878 T12: -0.0455 REMARK 3 T13: -0.0971 T23: -0.0529 REMARK 3 L TENSOR REMARK 3 L11: 0.0048 L22: 0.0068 REMARK 3 L33: 0.0056 L12: -0.0012 REMARK 3 L13: -0.0030 L23: 0.0047 REMARK 3 S TENSOR REMARK 3 S11: 0.1355 S12: -0.1342 S13: 0.1848 REMARK 3 S21: 0.0653 S22: -0.0190 S23: -0.0536 REMARK 3 S31: 0.0495 S32: -0.1410 S33: 0.0000 REMARK 3 TLS GROUP : 38 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 4 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.6212 86.2900 9.5788 REMARK 3 T TENSOR REMARK 3 T11: 0.2109 T22: 0.2574 REMARK 3 T33: 0.3230 T12: 0.0684 REMARK 3 T13: -0.0363 T23: -0.0585 REMARK 3 L TENSOR REMARK 3 L11: 0.0715 L22: 0.4813 REMARK 3 L33: 0.1556 L12: 0.1019 REMARK 3 L13: 0.0642 L23: -0.0731 REMARK 3 S TENSOR REMARK 3 S11: -0.0126 S12: -0.0395 S13: 0.1797 REMARK 3 S21: -0.1926 S22: 0.0247 S23: 0.1419 REMARK 3 S31: -0.2022 S32: -0.1494 S33: -0.0029 REMARK 3 TLS GROUP : 39 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 121 THROUGH 222 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.5518 54.8588 -0.3792 REMARK 3 T TENSOR REMARK 3 T11: 0.1442 T22: 0.4704 REMARK 3 T33: 0.3042 T12: -0.1002 REMARK 3 T13: 0.0439 T23: 0.0607 REMARK 3 L TENSOR REMARK 3 L11: 0.0671 L22: 0.0985 REMARK 3 L33: 0.1319 L12: 0.0983 REMARK 3 L13: 0.0239 L23: 0.0421 REMARK 3 S TENSOR REMARK 3 S11: -0.0453 S12: -0.0358 S13: 0.1493 REMARK 3 S21: -0.0341 S22: 0.0376 S23: 0.3080 REMARK 3 S31: 0.0497 S32: -0.4438 S33: -0.1848 REMARK 3 TLS GROUP : 40 REMARK 3 SELECTION: CHAIN 'N' AND (RESID 1 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.1455 73.5962 23.7044 REMARK 3 T TENSOR REMARK 3 T11: 0.2101 T22: 0.2724 REMARK 3 T33: 0.2899 T12: 0.0101 REMARK 3 T13: -0.1002 T23: -0.0358 REMARK 3 L TENSOR REMARK 3 L11: 0.2711 L22: 0.1280 REMARK 3 L33: 0.2514 L12: -0.0438 REMARK 3 L13: 0.0383 L23: 0.0616 REMARK 3 S TENSOR REMARK 3 S11: 0.1204 S12: -0.1556 S13: -0.0126 REMARK 3 S21: 0.2152 S22: 0.0208 S23: -0.2653 REMARK 3 S31: 0.2042 S32: 0.0582 S33: 0.1673 REMARK 3 TLS GROUP : 41 REMARK 3 SELECTION: CHAIN 'N' AND (RESID 76 THROUGH 128 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.3735 61.5945 11.9450 REMARK 3 T TENSOR REMARK 3 T11: 0.2227 T22: 0.2713 REMARK 3 T33: 0.2275 T12: -0.0375 REMARK 3 T13: -0.0748 T23: -0.0025 REMARK 3 L TENSOR REMARK 3 L11: 0.1290 L22: 0.1742 REMARK 3 L33: 0.2575 L12: -0.0569 REMARK 3 L13: -0.1966 L23: 0.1025 REMARK 3 S TENSOR REMARK 3 S11: -0.0210 S12: -0.0268 S13: 0.0304 REMARK 3 S21: 0.0238 S22: 0.0742 S23: -0.1031 REMARK 3 S31: 0.1403 S32: -0.1056 S33: 0.0094 REMARK 3 TLS GROUP : 42 REMARK 3 SELECTION: CHAIN 'N' AND (RESID 129 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.0578 44.3624 -1.1743 REMARK 3 T TENSOR REMARK 3 T11: 0.3936 T22: 0.3172 REMARK 3 T33: 0.2388 T12: -0.0304 REMARK 3 T13: 0.0394 T23: 0.0124 REMARK 3 L TENSOR REMARK 3 L11: 0.1230 L22: 0.1355 REMARK 3 L33: 0.0397 L12: -0.0763 REMARK 3 L13: 0.0195 L23: -0.0702 REMARK 3 S TENSOR REMARK 3 S11: -0.1161 S12: 0.0283 S13: 0.0483 REMARK 3 S21: -0.1264 S22: -0.0028 S23: -0.0536 REMARK 3 S31: 0.3563 S32: 0.0223 S33: -0.0062 REMARK 3 TLS GROUP : 43 REMARK 3 SELECTION: CHAIN 'O' AND (RESID 4 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): 38.0892 115.3007 39.2512 REMARK 3 T TENSOR REMARK 3 T11: 0.2669 T22: 0.2756 REMARK 3 T33: 0.2669 T12: 0.0497 REMARK 3 T13: -0.0255 T23: -0.0807 REMARK 3 L TENSOR REMARK 3 L11: 0.1528 L22: 0.1994 REMARK 3 L33: 0.1361 L12: 0.1311 REMARK 3 L13: -0.0233 L23: 0.0775 REMARK 3 S TENSOR REMARK 3 S11: -0.0414 S12: -0.2103 S13: 0.1295 REMARK 3 S21: 0.0340 S22: -0.0122 S23: 0.1844 REMARK 3 S31: 0.0246 S32: 0.0823 S33: -0.0051 REMARK 3 TLS GROUP : 44 REMARK 3 SELECTION: CHAIN 'O' AND (RESID 121 THROUGH 223 ) REMARK 3 ORIGIN FOR THE GROUP (A): 63.3214 132.6423 49.7289 REMARK 3 T TENSOR REMARK 3 T11: 0.2600 T22: 0.4618 REMARK 3 T33: 0.3094 T12: 0.1508 REMARK 3 T13: -0.0551 T23: 0.0207 REMARK 3 L TENSOR REMARK 3 L11: 0.0608 L22: 0.1460 REMARK 3 L33: 0.1861 L12: 0.0895 REMARK 3 L13: 0.0855 L23: 0.1685 REMARK 3 S TENSOR REMARK 3 S11: 0.1272 S12: -0.2378 S13: 0.2151 REMARK 3 S21: -0.0174 S22: -0.3049 S23: -0.0148 REMARK 3 S31: -0.2689 S32: -0.3695 S33: -0.1181 REMARK 3 TLS GROUP : 45 REMARK 3 SELECTION: CHAIN 'P' AND (RESID 1 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): 60.4654 104.8812 29.0232 REMARK 3 T TENSOR REMARK 3 T11: 0.2754 T22: 0.4773 REMARK 3 T33: 0.3949 T12: 0.0724 REMARK 3 T13: 0.0086 T23: -0.0431 REMARK 3 L TENSOR REMARK 3 L11: 0.0442 L22: 0.0094 REMARK 3 L33: 0.0071 L12: -0.0059 REMARK 3 L13: -0.0152 L23: -0.0034 REMARK 3 S TENSOR REMARK 3 S11: 0.0067 S12: 0.0532 S13: -0.0643 REMARK 3 S21: 0.0983 S22: 0.1570 S23: -0.0196 REMARK 3 S31: 0.0927 S32: 0.2771 S33: 0.0028 REMARK 3 TLS GROUP : 46 REMARK 3 SELECTION: CHAIN 'P' AND (RESID 19 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 51.7472 107.7620 23.6201 REMARK 3 T TENSOR REMARK 3 T11: 0.2743 T22: 0.3120 REMARK 3 T33: 0.2768 T12: 0.0244 REMARK 3 T13: 0.0267 T23: -0.0807 REMARK 3 L TENSOR REMARK 3 L11: 0.1258 L22: 0.0312 REMARK 3 L33: 0.0508 L12: 0.0034 REMARK 3 L13: -0.0513 L23: 0.0046 REMARK 3 S TENSOR REMARK 3 S11: -0.0922 S12: 0.2312 S13: 0.0002 REMARK 3 S21: -0.2078 S22: 0.1387 S23: -0.0055 REMARK 3 S31: 0.0152 S32: 0.2102 S33: 0.0003 REMARK 3 TLS GROUP : 47 REMARK 3 SELECTION: CHAIN 'P' AND (RESID 76 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): 58.4176 111.1530 29.3571 REMARK 3 T TENSOR REMARK 3 T11: 0.2309 T22: 0.3599 REMARK 3 T33: 0.2876 T12: 0.0216 REMARK 3 T13: 0.0161 T23: -0.0530 REMARK 3 L TENSOR REMARK 3 L11: 0.0117 L22: 0.0241 REMARK 3 L33: 0.0120 L12: -0.0125 REMARK 3 L13: 0.0255 L23: -0.0286 REMARK 3 S TENSOR REMARK 3 S11: -0.0275 S12: 0.0814 S13: -0.0532 REMARK 3 S21: -0.0575 S22: 0.0083 S23: 0.0214 REMARK 3 S31: 0.2039 S32: 0.2700 S33: -0.0066 REMARK 3 TLS GROUP : 48 REMARK 3 SELECTION: CHAIN 'P' AND (RESID 114 THROUGH 163 ) REMARK 3 ORIGIN FOR THE GROUP (A): 76.3299 124.2137 51.9093 REMARK 3 T TENSOR REMARK 3 T11: 0.2999 T22: 0.3962 REMARK 3 T33: 0.3073 T12: 0.0836 REMARK 3 T13: -0.0796 T23: -0.0162 REMARK 3 L TENSOR REMARK 3 L11: 0.0455 L22: 0.0399 REMARK 3 L33: 0.0263 L12: 0.0414 REMARK 3 L13: -0.0276 L23: -0.0239 REMARK 3 S TENSOR REMARK 3 S11: -0.0351 S12: -0.0645 S13: 0.0504 REMARK 3 S21: 0.1113 S22: -0.0965 S23: -0.2302 REMARK 3 S31: 0.0182 S32: 0.0269 S33: -0.0005 REMARK 3 TLS GROUP : 49 REMARK 3 SELECTION: CHAIN 'P' AND (RESID 164 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 78.9896 124.8970 50.1466 REMARK 3 T TENSOR REMARK 3 T11: 0.2262 T22: 0.4148 REMARK 3 T33: 0.3096 T12: 0.0539 REMARK 3 T13: -0.0940 T23: -0.0074 REMARK 3 L TENSOR REMARK 3 L11: 0.0419 L22: 0.0125 REMARK 3 L33: 0.0537 L12: -0.0188 REMARK 3 L13: -0.0250 L23: 0.0094 REMARK 3 S TENSOR REMARK 3 S11: 0.1286 S12: 0.0179 S13: 0.0624 REMARK 3 S21: 0.1126 S22: -0.1501 S23: -0.2330 REMARK 3 S31: 0.0642 S32: 0.0848 S33: 0.0009 REMARK 3 TLS GROUP : 50 REMARK 3 SELECTION: CHAIN 'Q' AND (RESID 1 THROUGH 7 ) REMARK 3 ORIGIN FOR THE GROUP (A): 30.3360 99.9240 26.8129 REMARK 3 T TENSOR REMARK 3 T11: 0.3589 T22: 0.3352 REMARK 3 T33: 0.2846 T12: -0.0083 REMARK 3 T13: -0.0348 T23: -0.0799 REMARK 3 L TENSOR REMARK 3 L11: 0.0110 L22: 0.0092 REMARK 3 L33: 0.0090 L12: 0.0084 REMARK 3 L13: 0.0076 L23: 0.0100 REMARK 3 S TENSOR REMARK 3 S11: 0.0506 S12: -0.0371 S13: 0.0010 REMARK 3 S21: 0.0585 S22: -0.0640 S23: 0.0420 REMARK 3 S31: 0.0544 S32: -0.0934 S33: 0.0000 REMARK 3 TLS GROUP : 51 REMARK 3 SELECTION: CHAIN 'R' AND (RESID 1 THROUGH 7 ) REMARK 3 ORIGIN FOR THE GROUP (A): 28.6665 98.0730 21.1563 REMARK 3 T TENSOR REMARK 3 T11: 0.4494 T22: 0.3119 REMARK 3 T33: 0.3240 T12: -0.0332 REMARK 3 T13: 0.0027 T23: -0.1100 REMARK 3 L TENSOR REMARK 3 L11: 0.0078 L22: 0.0133 REMARK 3 L33: 0.0110 L12: 0.0091 REMARK 3 L13: 0.0056 L23: 0.0067 REMARK 3 S TENSOR REMARK 3 S11: 0.0173 S12: 0.0866 S13: -0.1313 REMARK 3 S21: -0.1305 S22: -0.0604 S23: 0.1288 REMARK 3 S31: -0.1378 S32: 0.0414 S33: 0.0001 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 3 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "A" and (resid 3 through 123 or REMARK 3 resid 125 through 135 or resid 143 REMARK 3 through 222)) 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 3 through 123 or REMARK 3 resid 125 through 222)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "G" and (resid 3 through 123 or REMARK 3 resid 125 through 222)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "I" and (resid 3 through 123 or REMARK 3 resid 125 through 222)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 5 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "M" and (resid 3 through 123 or REMARK 3 resid 125 through 222)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 6 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "O" and (resid 3 through 123 or REMARK 3 resid 125 through 222)) 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" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "H" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "J" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 5 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "N" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 6 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "P" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_3 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "E" and (resid 1 or resid 4 REMARK 3 through 7)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "F" and (resid 1 or resid 4 REMARK 3 through 7)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "K" and (resid 1 or resid 4 REMARK 3 through 7)) 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 1 or resid 4 REMARK 3 through 7)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 5 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "Q" and (resid 1 or resid 4 REMARK 3 through 7)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 6 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "R" and (resid 1 or resid 4 REMARK 3 through 7)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9WU2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-SEP-25. REMARK 100 THE DEPOSITION ID IS D_1300063807. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-DEC-24 REMARK 200 TEMPERATURE (KELVIN) : 112 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSRRC REMARK 200 BEAMLINE : TPS 05A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300HE REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000 REMARK 200 DATA SCALING SOFTWARE : HKL-3000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 156195 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350 REMARK 200 RESOLUTION RANGE LOW (A) : 18.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 5.300 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 22.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.43 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: MOLREP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 61.58 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 12% (W/V) PEG 3,350, 0.1 M SODIUM REMARK 280 MALONATE, PH 5.0, 0.01% 1,2-DIAMINOCYCLOHEXANE SULFATE, 0.01% 1, REMARK 280 4-CYCLOHEXANEDICARBOXYLIC ACID, 0.01% METHYLENEDIPHOSPHONIC ACID, REMARK 280 0.01% SULFANILIC ACID, AND 0.001 M HEPES SODIUM, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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 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 29.79833 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 59.59667 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I, J, K, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N, O, P, Q, R REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 LYS A 1 REMARK 465 VAL A 2 REMARK 465 SER A 137 REMARK 465 LYS A 138 REMARK 465 SER A 139 REMARK 465 THR A 140 REMARK 465 SER A 141 REMARK 465 GLY A 142 REMARK 465 LYS A 223 REMARK 465 SER A 224 REMARK 465 CYS A 225 REMARK 465 ASP A 226 REMARK 465 LYS A 227 REMARK 465 THR A 228 REMARK 465 HIS A 229 REMARK 465 HIS A 230 REMARK 465 HIS A 231 REMARK 465 HIS A 232 REMARK 465 HIS A 233 REMARK 465 HIS A 234 REMARK 465 HIS A 235 REMARK 465 HIS A 236 REMARK 465 CYS B 214 REMARK 465 LYS C 1 REMARK 465 VAL C 2 REMARK 465 SER C 136 REMARK 465 SER C 137 REMARK 465 LYS C 138 REMARK 465 SER C 139 REMARK 465 THR C 140 REMARK 465 SER C 141 REMARK 465 GLY C 142 REMARK 465 SER C 224 REMARK 465 CYS C 225 REMARK 465 ASP C 226 REMARK 465 LYS C 227 REMARK 465 THR C 228 REMARK 465 HIS C 229 REMARK 465 HIS C 230 REMARK 465 HIS C 231 REMARK 465 HIS C 232 REMARK 465 HIS C 233 REMARK 465 HIS C 234 REMARK 465 HIS C 235 REMARK 465 HIS C 236 REMARK 465 CYS D 214 REMARK 465 LYS G 1 REMARK 465 VAL G 2 REMARK 465 SER G 136 REMARK 465 SER G 137 REMARK 465 LYS G 138 REMARK 465 SER G 139 REMARK 465 THR G 140 REMARK 465 SER G 141 REMARK 465 GLY G 142 REMARK 465 SER G 224 REMARK 465 CYS G 225 REMARK 465 ASP G 226 REMARK 465 LYS G 227 REMARK 465 THR G 228 REMARK 465 HIS G 229 REMARK 465 HIS G 230 REMARK 465 HIS G 231 REMARK 465 HIS G 232 REMARK 465 HIS G 233 REMARK 465 HIS G 234 REMARK 465 HIS G 235 REMARK 465 HIS G 236 REMARK 465 CYS H 214 REMARK 465 LYS I 1 REMARK 465 VAL I 2 REMARK 465 SER I 136 REMARK 465 SER I 137 REMARK 465 LYS I 138 REMARK 465 SER I 139 REMARK 465 THR I 140 REMARK 465 SER I 141 REMARK 465 GLY I 142 REMARK 465 SER I 224 REMARK 465 CYS I 225 REMARK 465 ASP I 226 REMARK 465 LYS I 227 REMARK 465 THR I 228 REMARK 465 HIS I 229 REMARK 465 HIS I 230 REMARK 465 HIS I 231 REMARK 465 HIS I 232 REMARK 465 HIS I 233 REMARK 465 HIS I 234 REMARK 465 HIS I 235 REMARK 465 HIS I 236 REMARK 465 CYS J 214 REMARK 465 LYS M 1 REMARK 465 VAL M 2 REMARK 465 SER M 136 REMARK 465 SER M 137 REMARK 465 LYS M 138 REMARK 465 SER M 139 REMARK 465 THR M 140 REMARK 465 SER M 141 REMARK 465 GLY M 142 REMARK 465 LYS M 223 REMARK 465 SER M 224 REMARK 465 CYS M 225 REMARK 465 ASP M 226 REMARK 465 LYS M 227 REMARK 465 THR M 228 REMARK 465 HIS M 229 REMARK 465 HIS M 230 REMARK 465 HIS M 231 REMARK 465 HIS M 232 REMARK 465 HIS M 233 REMARK 465 HIS M 234 REMARK 465 HIS M 235 REMARK 465 HIS M 236 REMARK 465 CYS N 214 REMARK 465 LYS O 1 REMARK 465 VAL O 2 REMARK 465 SER O 136 REMARK 465 SER O 137 REMARK 465 LYS O 138 REMARK 465 SER O 139 REMARK 465 THR O 140 REMARK 465 SER O 141 REMARK 465 GLY O 142 REMARK 465 SER O 224 REMARK 465 CYS O 225 REMARK 465 ASP O 226 REMARK 465 LYS O 227 REMARK 465 THR O 228 REMARK 465 HIS O 229 REMARK 465 HIS O 230 REMARK 465 HIS O 231 REMARK 465 HIS O 232 REMARK 465 HIS O 233 REMARK 465 HIS O 234 REMARK 465 HIS O 235 REMARK 465 HIS O 236 REMARK 465 CYS P 214 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 SER O 124 OG 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 C 492 O HOH C 548 1.93 REMARK 500 O HOH D 472 O HOH M 534 2.00 REMARK 500 O HOH J 310 O HOH J 331 2.04 REMARK 500 O HOH O 506 O HOH O 517 2.05 REMARK 500 O HOH J 341 O HOH J 428 2.08 REMARK 500 O HOH N 345 O HOH N 427 2.09 REMARK 500 O3 GOL G 302 O HOH G 401 2.10 REMARK 500 O HOH I 479 O HOH I 509 2.10 REMARK 500 OE1 GLU G 157 O HOH G 402 2.11 REMARK 500 O HOH J 336 O HOH J 412 2.11 REMARK 500 O HOH K 117 O HOH L 112 2.12 REMARK 500 O HOH O 464 O HOH O 500 2.12 REMARK 500 O HOH D 409 O HOH D 434 2.12 REMARK 500 O HOH M 515 O HOH M 525 2.12 REMARK 500 O HOH M 494 O HOH M 497 2.12 REMARK 500 NZ LYS D 45 O HOH D 301 2.14 REMARK 500 O HOH G 496 O HOH H 378 2.14 REMARK 500 OE1 GLN C 201 O HOH C 401 2.15 REMARK 500 O HOH N 370 O HOH N 408 2.15 REMARK 500 O HOH O 468 O HOH O 495 2.16 REMARK 500 O HOH D 326 O HOH M 460 2.16 REMARK 500 O HOH D 366 O HOH D 429 2.17 REMARK 500 NH2 ARG N 53 O5' DC Q 1 2.19 REMARK 500 O HOH G 402 O HOH G 461 2.19 REMARK 500 O HOH D 373 O HOH D 426 2.19 REMARK 500 O GLY J 28 O HOH J 301 2.19 REMARK 500 O HOH M 472 O HOH M 524 2.19 REMARK 500 O HOH D 442 O HOH D 455 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 DG F 4 O3' DG F 4 C3' -0.038 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 DC E 1 C3' - O3' - P ANGL. DEV. = 9.5 DEGREES REMARK 500 DC Q 1 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES REMARK 500 DC Q 3 O4' - C1' - N1 ANGL. DEV. = 2.0 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 ASP A 153 60.64 64.94 REMARK 500 SER A 197 33.33 -95.01 REMARK 500 THR B 51 -49.69 69.48 REMARK 500 ALA B 84 -178.90 -173.36 REMARK 500 ASN B 138 75.17 57.85 REMARK 500 ASN B 212 -70.00 -63.70 REMARK 500 ASP C 153 60.78 64.43 REMARK 500 SER C 197 32.73 -90.75 REMARK 500 THR D 51 -50.25 70.30 REMARK 500 ASN D 77 71.80 41.81 REMARK 500 ASN D 138 74.90 56.60 REMARK 500 LYS D 169 -61.20 -92.57 REMARK 500 ASN D 212 -73.20 -65.31 REMARK 500 SER G 197 32.38 -91.54 REMARK 500 THR H 51 -49.52 69.26 REMARK 500 ASN H 138 74.74 56.17 REMARK 500 LYS H 169 -60.46 -90.62 REMARK 500 ASP I 153 62.49 65.57 REMARK 500 SER I 197 34.44 -94.31 REMARK 500 THR J 51 -50.05 71.19 REMARK 500 ASN J 138 75.08 58.47 REMARK 500 ASP M 153 60.11 65.44 REMARK 500 SER M 197 33.86 -93.81 REMARK 500 THR N 51 -50.45 70.24 REMARK 500 ALA N 84 -178.87 -173.35 REMARK 500 ASN N 138 74.89 57.35 REMARK 500 LYS N 169 -60.76 -92.48 REMARK 500 ASP O 153 62.10 65.27 REMARK 500 SER O 197 32.12 -91.73 REMARK 500 THR P 51 -49.79 70.74 REMARK 500 ASN P 138 75.04 56.72 REMARK 500 LYS P 169 -61.47 -92.96 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG J 53 0.17 SIDE CHAIN REMARK 500 ARG J 211 0.12 SIDE CHAIN 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 514 DISTANCE = 6.41 ANGSTROMS REMARK 525 HOH C 578 DISTANCE = 6.67 ANGSTROMS REMARK 525 HOH D 475 DISTANCE = 6.32 ANGSTROMS REMARK 525 HOH D 476 DISTANCE = 6.79 ANGSTROMS REMARK 525 HOH D 477 DISTANCE = 7.18 ANGSTROMS REMARK 525 HOH I 527 DISTANCE = 6.14 ANGSTROMS REMARK 525 HOH I 528 DISTANCE = 6.17 ANGSTROMS REMARK 525 HOH I 529 DISTANCE = 7.32 ANGSTROMS REMARK 525 HOH J 464 DISTANCE = 7.92 ANGSTROMS REMARK 525 HOH J 465 DISTANCE = 7.97 ANGSTROMS REMARK 525 HOH M 544 DISTANCE = 5.88 ANGSTROMS REMARK 525 HOH M 545 DISTANCE = 6.24 ANGSTROMS REMARK 525 HOH O 520 DISTANCE = 7.38 ANGSTROMS DBREF 9WU2 A 1 236 PDB 9WU2 9WU2 1 236 DBREF 9WU2 B 1 214 PDB 9WU2 9WU2 1 214 DBREF 9WU2 C 1 236 PDB 9WU2 9WU2 1 236 DBREF 9WU2 D 1 214 PDB 9WU2 9WU2 1 214 DBREF 9WU2 E 1 7 PDB 9WU2 9WU2 1 7 DBREF 9WU2 F 1 7 PDB 9WU2 9WU2 1 7 DBREF 9WU2 G 1 236 PDB 9WU2 9WU2 1 236 DBREF 9WU2 H 1 214 PDB 9WU2 9WU2 1 214 DBREF 9WU2 I 1 236 PDB 9WU2 9WU2 1 236 DBREF 9WU2 J 1 214 PDB 9WU2 9WU2 1 214 DBREF 9WU2 K 1 7 PDB 9WU2 9WU2 1 7 DBREF 9WU2 L 1 7 PDB 9WU2 9WU2 1 7 DBREF 9WU2 M 1 236 PDB 9WU2 9WU2 1 236 DBREF 9WU2 N 1 214 PDB 9WU2 9WU2 1 214 DBREF 9WU2 O 1 236 PDB 9WU2 9WU2 1 236 DBREF 9WU2 P 1 214 PDB 9WU2 9WU2 1 214 DBREF 9WU2 Q 1 7 PDB 9WU2 9WU2 1 7 DBREF 9WU2 R 1 7 PDB 9WU2 9WU2 1 7 SEQRES 1 A 236 LYS VAL PCA LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 236 PRO LYS GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 A 236 PHE ASN PHE ASN THR TYR ALA MET ASN TRP VAL ARG GLN SEQRES 4 A 236 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ARG SEQRES 5 A 236 SER LYS SER ASN ASN TYR ALA THR TYR TYR ALA ASP SER SEQRES 6 A 236 MET LYS ASP ARG PHE THR ILE SER ARG ASP ASP SER GLU SEQRES 7 A 236 ASN MET LEU TYR LEU GLN MET ILE ASN LEU LYS ALA GLU SEQRES 8 A 236 ASP THR ALA MET TYR TYR CYS VAL ARG GLN ALA TYR SER SEQRES 9 A 236 ASN TYR GLY ALA MET ASP TYR TRP GLY GLN GLY ILE SER SEQRES 10 A 236 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 A 236 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 A 236 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 A 236 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 A 236 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 A 236 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 A 236 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 A 236 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS ALA GLU SEQRES 18 A 236 PRO LYS SER CYS ASP LYS THR HIS HIS HIS HIS HIS HIS SEQRES 19 A 236 HIS HIS SEQRES 1 B 214 ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA SEQRES 2 B 214 SER LEU GLY ASP ARG VAL THR ILE SER CYS SER ALA SER SEQRES 3 B 214 GLN GLY ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 B 214 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5 B 214 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 B 214 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7 B 214 GLU PRO GLU ASP ILE ALA THR TYR PHE CYS GLN GLN TYR SEQRES 8 B 214 SER LYS PHE PRO PHE THR PHE GLY SER GLY THR LYS LEU SEQRES 9 B 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 B 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 B 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 B 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 B 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 B 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 B 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 B 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 B 214 PHE ASN ARG ASN GLU CYS SEQRES 1 C 236 LYS VAL PCA LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 236 PRO LYS GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 C 236 PHE ASN PHE ASN THR TYR ALA MET ASN TRP VAL ARG GLN SEQRES 4 C 236 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ARG SEQRES 5 C 236 SER LYS SER ASN ASN TYR ALA THR TYR TYR ALA ASP SER SEQRES 6 C 236 MET LYS ASP ARG PHE THR ILE SER ARG ASP ASP SER GLU SEQRES 7 C 236 ASN MET LEU TYR LEU GLN MET ILE ASN LEU LYS ALA GLU SEQRES 8 C 236 ASP THR ALA MET TYR TYR CYS VAL ARG GLN ALA TYR SER SEQRES 9 C 236 ASN TYR GLY ALA MET ASP TYR TRP GLY GLN GLY ILE SER SEQRES 10 C 236 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 C 236 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 C 236 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 C 236 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 C 236 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 C 236 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 C 236 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 C 236 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS ALA GLU SEQRES 18 C 236 PRO LYS SER CYS ASP LYS THR HIS HIS HIS HIS HIS HIS SEQRES 19 C 236 HIS HIS SEQRES 1 D 214 ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA SEQRES 2 D 214 SER LEU GLY ASP ARG VAL THR ILE SER CYS SER ALA SER SEQRES 3 D 214 GLN GLY ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 D 214 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5 D 214 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 D 214 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7 D 214 GLU PRO GLU ASP ILE ALA THR TYR PHE CYS GLN GLN TYR SEQRES 8 D 214 SER LYS PHE PRO PHE THR PHE GLY SER GLY THR LYS LEU SEQRES 9 D 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 D 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 D 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 D 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 D 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 D 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 D 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 D 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 D 214 PHE ASN ARG ASN GLU CYS SEQRES 1 E 7 DC DG DC DG DC DG DC SEQRES 1 F 7 DC DG DC DG DC DG DC SEQRES 1 G 236 LYS VAL PCA LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 G 236 PRO LYS GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 G 236 PHE ASN PHE ASN THR TYR ALA MET ASN TRP VAL ARG GLN SEQRES 4 G 236 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ARG SEQRES 5 G 236 SER LYS SER ASN ASN TYR ALA THR TYR TYR ALA ASP SER SEQRES 6 G 236 MET LYS ASP ARG PHE THR ILE SER ARG ASP ASP SER GLU SEQRES 7 G 236 ASN MET LEU TYR LEU GLN MET ILE ASN LEU LYS ALA GLU SEQRES 8 G 236 ASP THR ALA MET TYR TYR CYS VAL ARG GLN ALA TYR SER SEQRES 9 G 236 ASN TYR GLY ALA MET ASP TYR TRP GLY GLN GLY ILE SER SEQRES 10 G 236 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 G 236 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 G 236 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 G 236 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 G 236 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 G 236 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 G 236 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 G 236 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS ALA GLU SEQRES 18 G 236 PRO LYS SER CYS ASP LYS THR HIS HIS HIS HIS HIS HIS SEQRES 19 G 236 HIS HIS SEQRES 1 H 214 ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA SEQRES 2 H 214 SER LEU GLY ASP ARG VAL THR ILE SER CYS SER ALA SER SEQRES 3 H 214 GLN GLY ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 H 214 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5 H 214 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 H 214 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7 H 214 GLU PRO GLU ASP ILE ALA THR TYR PHE CYS GLN GLN TYR SEQRES 8 H 214 SER LYS PHE PRO PHE THR PHE GLY SER GLY THR LYS LEU SEQRES 9 H 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 H 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 H 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 H 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 H 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 H 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 H 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 H 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 H 214 PHE ASN ARG ASN GLU CYS SEQRES 1 I 236 LYS VAL PCA LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 I 236 PRO LYS GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 I 236 PHE ASN PHE ASN THR TYR ALA MET ASN TRP VAL ARG GLN SEQRES 4 I 236 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ARG SEQRES 5 I 236 SER LYS SER ASN ASN TYR ALA THR TYR TYR ALA ASP SER SEQRES 6 I 236 MET LYS ASP ARG PHE THR ILE SER ARG ASP ASP SER GLU SEQRES 7 I 236 ASN MET LEU TYR LEU GLN MET ILE ASN LEU LYS ALA GLU SEQRES 8 I 236 ASP THR ALA MET TYR TYR CYS VAL ARG GLN ALA TYR SER SEQRES 9 I 236 ASN TYR GLY ALA MET ASP TYR TRP GLY GLN GLY ILE SER SEQRES 10 I 236 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 I 236 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 I 236 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 I 236 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 I 236 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 I 236 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 I 236 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 I 236 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS ALA GLU SEQRES 18 I 236 PRO LYS SER CYS ASP LYS THR HIS HIS HIS HIS HIS HIS SEQRES 19 I 236 HIS HIS SEQRES 1 J 214 ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA SEQRES 2 J 214 SER LEU GLY ASP ARG VAL THR ILE SER CYS SER ALA SER SEQRES 3 J 214 GLN GLY ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 J 214 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5 J 214 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 J 214 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7 J 214 GLU PRO GLU ASP ILE ALA THR TYR PHE CYS GLN GLN TYR SEQRES 8 J 214 SER LYS PHE PRO PHE THR PHE GLY SER GLY THR LYS LEU SEQRES 9 J 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 J 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 J 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 J 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 J 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 J 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 J 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 J 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 J 214 PHE ASN ARG ASN GLU CYS SEQRES 1 K 7 DC DG DC DG DC DG DC SEQRES 1 L 7 DC DG DC DG DC DG DC SEQRES 1 M 236 LYS VAL PCA LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 M 236 PRO LYS GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 M 236 PHE ASN PHE ASN THR TYR ALA MET ASN TRP VAL ARG GLN SEQRES 4 M 236 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ARG SEQRES 5 M 236 SER LYS SER ASN ASN TYR ALA THR TYR TYR ALA ASP SER SEQRES 6 M 236 MET LYS ASP ARG PHE THR ILE SER ARG ASP ASP SER GLU SEQRES 7 M 236 ASN MET LEU TYR LEU GLN MET ILE ASN LEU LYS ALA GLU SEQRES 8 M 236 ASP THR ALA MET TYR TYR CYS VAL ARG GLN ALA TYR SER SEQRES 9 M 236 ASN TYR GLY ALA MET ASP TYR TRP GLY GLN GLY ILE SER SEQRES 10 M 236 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 M 236 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 M 236 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 M 236 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 M 236 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 M 236 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 M 236 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 M 236 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS ALA GLU SEQRES 18 M 236 PRO LYS SER CYS ASP LYS THR HIS HIS HIS HIS HIS HIS SEQRES 19 M 236 HIS HIS SEQRES 1 N 214 ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA SEQRES 2 N 214 SER LEU GLY ASP ARG VAL THR ILE SER CYS SER ALA SER SEQRES 3 N 214 GLN GLY ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 N 214 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5 N 214 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 N 214 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7 N 214 GLU PRO GLU ASP ILE ALA THR TYR PHE CYS GLN GLN TYR SEQRES 8 N 214 SER LYS PHE PRO PHE THR PHE GLY SER GLY THR LYS LEU SEQRES 9 N 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 N 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 N 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 N 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 N 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 N 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 N 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 N 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 N 214 PHE ASN ARG ASN GLU CYS SEQRES 1 O 236 LYS VAL PCA LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 O 236 PRO LYS GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 O 236 PHE ASN PHE ASN THR TYR ALA MET ASN TRP VAL ARG GLN SEQRES 4 O 236 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ARG SEQRES 5 O 236 SER LYS SER ASN ASN TYR ALA THR TYR TYR ALA ASP SER SEQRES 6 O 236 MET LYS ASP ARG PHE THR ILE SER ARG ASP ASP SER GLU SEQRES 7 O 236 ASN MET LEU TYR LEU GLN MET ILE ASN LEU LYS ALA GLU SEQRES 8 O 236 ASP THR ALA MET TYR TYR CYS VAL ARG GLN ALA TYR SER SEQRES 9 O 236 ASN TYR GLY ALA MET ASP TYR TRP GLY GLN GLY ILE SER SEQRES 10 O 236 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 O 236 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 O 236 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 O 236 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 O 236 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 O 236 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 O 236 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 O 236 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS ALA GLU SEQRES 18 O 236 PRO LYS SER CYS ASP LYS THR HIS HIS HIS HIS HIS HIS SEQRES 19 O 236 HIS HIS SEQRES 1 P 214 ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA SEQRES 2 P 214 SER LEU GLY ASP ARG VAL THR ILE SER CYS SER ALA SER SEQRES 3 P 214 GLN GLY ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 P 214 PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER SEQRES 5 P 214 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 P 214 GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU SEQRES 7 P 214 GLU PRO GLU ASP ILE ALA THR TYR PHE CYS GLN GLN TYR SEQRES 8 P 214 SER LYS PHE PRO PHE THR PHE GLY SER GLY THR LYS LEU SEQRES 9 P 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 P 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 P 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 P 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 P 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 P 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 P 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 P 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 P 214 PHE ASN ARG ASN GLU CYS SEQRES 1 Q 7 DC DG DC DG DC DG DC SEQRES 1 R 7 DC DG DC DG DC DG DC HET PCA A 3 8 HET PCA C 3 8 HET PCA G 3 8 HET PCA I 3 8 HET PCA M 3 8 HET PCA O 3 8 HET GOL A 301 6 HET GOL C 301 6 HET GOL G 301 6 HET GOL G 302 6 HET GOL G 303 6 HET GOL I 301 6 HET GOL M 301 6 HET GOL O 301 6 HETNAM PCA PYROGLUTAMIC ACID HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 1 PCA 6(C5 H7 N O3) FORMUL 19 GOL 8(C3 H8 O3) FORMUL 27 HOH *1734(H2 O) HELIX 1 AA1 ASN A 28 TYR A 32 5 5 HELIX 2 AA2 SER A 53 ASN A 57 5 5 HELIX 3 AA3 ASP A 64 LYS A 67 5 4 HELIX 4 AA4 LYS A 89 THR A 93 5 5 HELIX 5 AA5 SER A 165 ALA A 167 5 3 HELIX 6 AA6 LYS A 210 ASN A 213 5 4 HELIX 7 AA7 GLU B 79 ILE B 83 5 5 HELIX 8 AA8 SER B 121 SER B 127 1 7 HELIX 9 AA9 LYS B 183 LYS B 188 1 6 HELIX 10 AB1 ASN C 28 TYR C 32 5 5 HELIX 11 AB2 SER C 53 ASN C 57 5 5 HELIX 12 AB3 ASP C 64 LYS C 67 5 4 HELIX 13 AB4 ASP C 76 GLU C 78 5 3 HELIX 14 AB5 LYS C 89 THR C 93 5 5 HELIX 15 AB6 SER C 165 ALA C 167 5 3 HELIX 16 AB7 SER C 196 GLY C 199 5 4 HELIX 17 AB8 LYS C 210 ASN C 213 5 4 HELIX 18 AB9 GLU D 79 ILE D 83 5 5 HELIX 19 AC1 SER D 121 SER D 127 1 7 HELIX 20 AC2 LYS D 183 LYS D 188 1 6 HELIX 21 AC3 ASN G 28 TYR G 32 5 5 HELIX 22 AC4 SER G 53 ASN G 57 5 5 HELIX 23 AC5 ASP G 64 LYS G 67 5 4 HELIX 24 AC6 LYS G 89 THR G 93 5 5 HELIX 25 AC7 SER G 196 GLY G 199 5 4 HELIX 26 AC8 LYS G 210 ASN G 213 5 4 HELIX 27 AC9 GLU H 79 ILE H 83 5 5 HELIX 28 AD1 SER H 121 SER H 127 1 7 HELIX 29 AD2 LYS H 183 LYS H 188 1 6 HELIX 30 AD3 ASN I 28 TYR I 32 5 5 HELIX 31 AD4 SER I 53 ASN I 57 5 5 HELIX 32 AD5 ASP I 64 LYS I 67 5 4 HELIX 33 AD6 LYS I 89 THR I 93 5 5 HELIX 34 AD7 SER I 165 ALA I 167 5 3 HELIX 35 AD8 LYS I 210 ASN I 213 5 4 HELIX 36 AD9 GLU J 79 ILE J 83 5 5 HELIX 37 AE1 SER J 121 SER J 127 1 7 HELIX 38 AE2 LYS J 183 LYS J 188 1 6 HELIX 39 AE3 ASN M 28 TYR M 32 5 5 HELIX 40 AE4 SER M 53 ASN M 57 5 5 HELIX 41 AE5 ASP M 64 LYS M 67 5 4 HELIX 42 AE6 LYS M 89 THR M 93 5 5 HELIX 43 AE7 SER M 165 ALA M 167 5 3 HELIX 44 AE8 SER M 196 GLY M 199 5 4 HELIX 45 AE9 LYS M 210 ASN M 213 5 4 HELIX 46 AF1 GLU N 79 ILE N 83 5 5 HELIX 47 AF2 SER N 121 SER N 127 1 7 HELIX 48 AF3 LYS N 183 LYS N 188 1 6 HELIX 49 AF4 ASN O 28 TYR O 32 5 5 HELIX 50 AF5 SER O 53 ASN O 57 5 5 HELIX 51 AF6 ASP O 64 LYS O 67 5 4 HELIX 52 AF7 LYS O 89 THR O 93 5 5 HELIX 53 AF8 SER O 196 GLY O 199 5 4 HELIX 54 AF9 LYS O 210 ASN O 213 5 4 HELIX 55 AG1 GLU P 79 ILE P 83 5 5 HELIX 56 AG2 SER P 121 SER P 127 1 7 HELIX 57 AG3 LYS P 183 LYS P 188 1 6 SHEET 1 AA1 4 LEU A 4 SER A 7 0 SHEET 2 AA1 4 LEU A 18 ALA A 24 -1 O ALA A 23 N VAL A 5 SHEET 3 AA1 4 MET A 80 MET A 85 -1 O MET A 85 N LEU A 18 SHEET 4 AA1 4 PHE A 70 ASP A 75 -1 N THR A 71 O GLN A 84 SHEET 1 AA2 6 GLY A 10 VAL A 12 0 SHEET 2 AA2 6 ILE A 116 VAL A 120 1 O SER A 117 N GLY A 10 SHEET 3 AA2 6 ALA A 94 GLN A 101 -1 N TYR A 96 O ILE A 116 SHEET 4 AA2 6 MET A 34 GLN A 39 -1 N VAL A 37 O TYR A 97 SHEET 5 AA2 6 LEU A 45 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AA2 6 THR A 60 TYR A 62 -1 O TYR A 61 N ARG A 50 SHEET 1 AA3 4 GLY A 10 VAL A 12 0 SHEET 2 AA3 4 ILE A 116 VAL A 120 1 O SER A 117 N GLY A 10 SHEET 3 AA3 4 ALA A 94 GLN A 101 -1 N TYR A 96 O ILE A 116 SHEET 4 AA3 4 MET A 109 TRP A 112 -1 O TYR A 111 N ARG A 100 SHEET 1 AA4 4 SER A 129 LEU A 133 0 SHEET 2 AA4 4 THR A 144 TYR A 154 -1 O LYS A 152 N SER A 129 SHEET 3 AA4 4 TYR A 185 PRO A 194 -1 O TYR A 185 N TYR A 154 SHEET 4 AA4 4 VAL A 172 THR A 174 -1 N HIS A 173 O VAL A 190 SHEET 1 AA5 4 SER A 129 LEU A 133 0 SHEET 2 AA5 4 THR A 144 TYR A 154 -1 O LYS A 152 N SER A 129 SHEET 3 AA5 4 TYR A 185 PRO A 194 -1 O TYR A 185 N TYR A 154 SHEET 4 AA5 4 VAL A 178 LEU A 179 -1 N VAL A 178 O SER A 186 SHEET 1 AA6 3 THR A 160 TRP A 163 0 SHEET 2 AA6 3 ILE A 204 HIS A 209 -1 O ASN A 206 N SER A 162 SHEET 3 AA6 3 THR A 214 LYS A 219 -1 O VAL A 216 N VAL A 207 SHEET 1 AA7 4 MET B 4 THR B 5 0 SHEET 2 AA7 4 VAL B 19 ALA B 25 -1 O SER B 24 N THR B 5 SHEET 3 AA7 4 ASP B 70 ILE B 75 -1 O LEU B 73 N ILE B 21 SHEET 4 AA7 4 PHE B 62 SER B 67 -1 N SER B 63 O THR B 74 SHEET 1 AA8 6 SER B 10 ALA B 13 0 SHEET 2 AA8 6 THR B 102 ILE B 106 1 O GLU B 105 N LEU B 11 SHEET 3 AA8 6 THR B 85 GLN B 90 -1 N TYR B 86 O THR B 102 SHEET 4 AA8 6 LEU B 33 GLN B 38 -1 N GLN B 38 O THR B 85 SHEET 5 AA8 6 VAL B 44 TYR B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AA8 6 ARG B 53 LEU B 54 -1 O ARG B 53 N TYR B 49 SHEET 1 AA9 4 SER B 10 ALA B 13 0 SHEET 2 AA9 4 THR B 102 ILE B 106 1 O GLU B 105 N LEU B 11 SHEET 3 AA9 4 THR B 85 GLN B 90 -1 N TYR B 86 O THR B 102 SHEET 4 AA9 4 THR B 97 PHE B 98 -1 O THR B 97 N GLN B 90 SHEET 1 AB1 4 SER B 114 PHE B 118 0 SHEET 2 AB1 4 THR B 129 PHE B 139 -1 O LEU B 135 N PHE B 116 SHEET 3 AB1 4 TYR B 173 SER B 182 -1 O LEU B 175 N LEU B 136 SHEET 4 AB1 4 SER B 159 VAL B 163 -1 N SER B 162 O SER B 176 SHEET 1 AB2 4 ALA B 153 LEU B 154 0 SHEET 2 AB2 4 LYS B 145 VAL B 150 -1 N VAL B 150 O ALA B 153 SHEET 3 AB2 4 VAL B 191 THR B 197 -1 O THR B 197 N LYS B 145 SHEET 4 AB2 4 VAL B 205 ASN B 210 -1 O VAL B 205 N VAL B 196 SHEET 1 AB3 4 LEU C 4 SER C 7 0 SHEET 2 AB3 4 LEU C 18 ALA C 24 -1 O SER C 21 N SER C 7 SHEET 3 AB3 4 MET C 80 MET C 85 -1 O MET C 85 N LEU C 18 SHEET 4 AB3 4 PHE C 70 ASP C 75 -1 N THR C 71 O GLN C 84 SHEET 1 AB4 6 GLY C 10 VAL C 12 0 SHEET 2 AB4 6 ILE C 116 VAL C 120 1 O THR C 119 N GLY C 10 SHEET 3 AB4 6 ALA C 94 GLN C 101 -1 N TYR C 96 O ILE C 116 SHEET 4 AB4 6 MET C 34 GLN C 39 -1 N VAL C 37 O TYR C 97 SHEET 5 AB4 6 LEU C 45 ILE C 51 -1 O GLU C 46 N ARG C 38 SHEET 6 AB4 6 THR C 60 TYR C 62 -1 O TYR C 61 N ARG C 50 SHEET 1 AB5 4 GLY C 10 VAL C 12 0 SHEET 2 AB5 4 ILE C 116 VAL C 120 1 O THR C 119 N GLY C 10 SHEET 3 AB5 4 ALA C 94 GLN C 101 -1 N TYR C 96 O ILE C 116 SHEET 4 AB5 4 MET C 109 TRP C 112 -1 O TYR C 111 N ARG C 100 SHEET 1 AB6 4 SER C 129 LEU C 133 0 SHEET 2 AB6 4 THR C 144 TYR C 154 -1 O LEU C 150 N PHE C 131 SHEET 3 AB6 4 TYR C 185 PRO C 194 -1 O LEU C 187 N VAL C 151 SHEET 4 AB6 4 VAL C 172 THR C 174 -1 N HIS C 173 O VAL C 190 SHEET 1 AB7 4 SER C 129 LEU C 133 0 SHEET 2 AB7 4 THR C 144 TYR C 154 -1 O LEU C 150 N PHE C 131 SHEET 3 AB7 4 TYR C 185 PRO C 194 -1 O LEU C 187 N VAL C 151 SHEET 4 AB7 4 VAL C 178 LEU C 179 -1 N VAL C 178 O SER C 186 SHEET 1 AB8 3 THR C 160 TRP C 163 0 SHEET 2 AB8 3 ILE C 204 HIS C 209 -1 O ASN C 206 N SER C 162 SHEET 3 AB8 3 THR C 214 LYS C 219 -1 O VAL C 216 N VAL C 207 SHEET 1 AB9 4 MET D 4 THR D 5 0 SHEET 2 AB9 4 VAL D 19 ALA D 25 -1 O SER D 24 N THR D 5 SHEET 3 AB9 4 ASP D 70 ILE D 75 -1 O TYR D 71 N CYS D 23 SHEET 4 AB9 4 PHE D 62 SER D 67 -1 N SER D 63 O THR D 74 SHEET 1 AC1 6 SER D 10 SER D 14 0 SHEET 2 AC1 6 THR D 102 LYS D 107 1 O LYS D 107 N ALA D 13 SHEET 3 AC1 6 ALA D 84 GLN D 90 -1 N ALA D 84 O LEU D 104 SHEET 4 AC1 6 LEU D 33 GLN D 38 -1 N GLN D 38 O THR D 85 SHEET 5 AC1 6 VAL D 44 TYR D 49 -1 O LEU D 47 N TRP D 35 SHEET 6 AC1 6 ARG D 53 LEU D 54 -1 O ARG D 53 N TYR D 49 SHEET 1 AC2 4 SER D 10 SER D 14 0 SHEET 2 AC2 4 THR D 102 LYS D 107 1 O LYS D 107 N ALA D 13 SHEET 3 AC2 4 ALA D 84 GLN D 90 -1 N ALA D 84 O LEU D 104 SHEET 4 AC2 4 THR D 97 PHE D 98 -1 O THR D 97 N GLN D 90 SHEET 1 AC3 4 SER D 114 PHE D 118 0 SHEET 2 AC3 4 THR D 129 PHE D 139 -1 O LEU D 135 N PHE D 116 SHEET 3 AC3 4 TYR D 173 SER D 182 -1 O LEU D 179 N VAL D 132 SHEET 4 AC3 4 SER D 159 VAL D 163 -1 N GLN D 160 O THR D 178 SHEET 1 AC4 4 ALA D 153 LEU D 154 0 SHEET 2 AC4 4 LYS D 145 VAL D 150 -1 N VAL D 150 O ALA D 153 SHEET 3 AC4 4 VAL D 191 THR D 197 -1 O GLU D 195 N GLN D 147 SHEET 4 AC4 4 VAL D 205 ASN D 210 -1 O VAL D 205 N VAL D 196 SHEET 1 AC5 4 LEU G 4 SER G 7 0 SHEET 2 AC5 4 LEU G 18 ALA G 24 -1 O SER G 21 N SER G 7 SHEET 3 AC5 4 MET G 80 MET G 85 -1 O MET G 85 N LEU G 18 SHEET 4 AC5 4 PHE G 70 ASP G 75 -1 N THR G 71 O GLN G 84 SHEET 1 AC6 6 GLY G 10 VAL G 12 0 SHEET 2 AC6 6 ILE G 116 VAL G 120 1 O THR G 119 N GLY G 10 SHEET 3 AC6 6 ALA G 94 GLN G 101 -1 N TYR G 96 O ILE G 116 SHEET 4 AC6 6 MET G 34 GLN G 39 -1 N VAL G 37 O TYR G 97 SHEET 5 AC6 6 LEU G 45 ILE G 51 -1 O GLU G 46 N ARG G 38 SHEET 6 AC6 6 THR G 60 TYR G 62 -1 O TYR G 61 N ARG G 50 SHEET 1 AC7 4 GLY G 10 VAL G 12 0 SHEET 2 AC7 4 ILE G 116 VAL G 120 1 O THR G 119 N GLY G 10 SHEET 3 AC7 4 ALA G 94 GLN G 101 -1 N TYR G 96 O ILE G 116 SHEET 4 AC7 4 MET G 109 TRP G 112 -1 O TYR G 111 N ARG G 100 SHEET 1 AC8 4 SER G 129 LEU G 133 0 SHEET 2 AC8 4 THR G 144 TYR G 154 -1 O LEU G 150 N PHE G 131 SHEET 3 AC8 4 TYR G 185 PRO G 194 -1 O LEU G 187 N VAL G 151 SHEET 4 AC8 4 VAL G 172 THR G 174 -1 N HIS G 173 O VAL G 190 SHEET 1 AC9 4 SER G 129 LEU G 133 0 SHEET 2 AC9 4 THR G 144 TYR G 154 -1 O LEU G 150 N PHE G 131 SHEET 3 AC9 4 TYR G 185 PRO G 194 -1 O LEU G 187 N VAL G 151 SHEET 4 AC9 4 VAL G 178 LEU G 179 -1 N VAL G 178 O SER G 186 SHEET 1 AD1 3 THR G 160 TRP G 163 0 SHEET 2 AD1 3 ILE G 204 HIS G 209 -1 O ASN G 206 N SER G 162 SHEET 3 AD1 3 THR G 214 LYS G 219 -1 O VAL G 216 N VAL G 207 SHEET 1 AD2 4 MET H 4 THR H 5 0 SHEET 2 AD2 4 VAL H 19 ALA H 25 -1 O SER H 24 N THR H 5 SHEET 3 AD2 4 ASP H 70 ILE H 75 -1 O LEU H 73 N ILE H 21 SHEET 4 AD2 4 PHE H 62 SER H 67 -1 N SER H 63 O THR H 74 SHEET 1 AD3 6 SER H 10 ALA H 13 0 SHEET 2 AD3 6 THR H 102 ILE H 106 1 O GLU H 105 N LEU H 11 SHEET 3 AD3 6 THR H 85 GLN H 90 -1 N TYR H 86 O THR H 102 SHEET 4 AD3 6 LEU H 33 GLN H 38 -1 N GLN H 38 O THR H 85 SHEET 5 AD3 6 VAL H 44 TYR H 49 -1 O LEU H 47 N TRP H 35 SHEET 6 AD3 6 ARG H 53 LEU H 54 -1 O ARG H 53 N TYR H 49 SHEET 1 AD4 4 SER H 10 ALA H 13 0 SHEET 2 AD4 4 THR H 102 ILE H 106 1 O GLU H 105 N LEU H 11 SHEET 3 AD4 4 THR H 85 GLN H 90 -1 N TYR H 86 O THR H 102 SHEET 4 AD4 4 THR H 97 PHE H 98 -1 O THR H 97 N GLN H 90 SHEET 1 AD5 4 SER H 114 PHE H 118 0 SHEET 2 AD5 4 THR H 129 PHE H 139 -1 O LEU H 135 N PHE H 116 SHEET 3 AD5 4 TYR H 173 SER H 182 -1 O LEU H 179 N VAL H 132 SHEET 4 AD5 4 SER H 159 VAL H 163 -1 N SER H 162 O SER H 176 SHEET 1 AD6 4 ALA H 153 LEU H 154 0 SHEET 2 AD6 4 LYS H 145 VAL H 150 -1 N VAL H 150 O ALA H 153 SHEET 3 AD6 4 VAL H 191 THR H 197 -1 O GLU H 195 N GLN H 147 SHEET 4 AD6 4 VAL H 205 ASN H 210 -1 O VAL H 205 N VAL H 196 SHEET 1 AD7 4 LEU I 4 SER I 7 0 SHEET 2 AD7 4 LEU I 18 ALA I 24 -1 O SER I 21 N SER I 7 SHEET 3 AD7 4 MET I 80 MET I 85 -1 O MET I 85 N LEU I 18 SHEET 4 AD7 4 PHE I 70 ASP I 75 -1 N THR I 71 O GLN I 84 SHEET 1 AD8 6 GLY I 10 VAL I 12 0 SHEET 2 AD8 6 ILE I 116 VAL I 120 1 O SER I 117 N GLY I 10 SHEET 3 AD8 6 ALA I 94 GLN I 101 -1 N TYR I 96 O ILE I 116 SHEET 4 AD8 6 MET I 34 GLN I 39 -1 N VAL I 37 O TYR I 97 SHEET 5 AD8 6 LEU I 45 ILE I 51 -1 O GLU I 46 N ARG I 38 SHEET 6 AD8 6 THR I 60 TYR I 62 -1 O TYR I 61 N ARG I 50 SHEET 1 AD9 4 GLY I 10 VAL I 12 0 SHEET 2 AD9 4 ILE I 116 VAL I 120 1 O SER I 117 N GLY I 10 SHEET 3 AD9 4 ALA I 94 GLN I 101 -1 N TYR I 96 O ILE I 116 SHEET 4 AD9 4 MET I 109 TRP I 112 -1 O TYR I 111 N ARG I 100 SHEET 1 AE1 4 SER I 129 LEU I 133 0 SHEET 2 AE1 4 THR I 144 TYR I 154 -1 O LEU I 150 N PHE I 131 SHEET 3 AE1 4 TYR I 185 PRO I 194 -1 O TYR I 185 N TYR I 154 SHEET 4 AE1 4 VAL I 172 THR I 174 -1 N HIS I 173 O VAL I 190 SHEET 1 AE2 4 SER I 129 LEU I 133 0 SHEET 2 AE2 4 THR I 144 TYR I 154 -1 O LEU I 150 N PHE I 131 SHEET 3 AE2 4 TYR I 185 PRO I 194 -1 O TYR I 185 N TYR I 154 SHEET 4 AE2 4 VAL I 178 LEU I 179 -1 N VAL I 178 O SER I 186 SHEET 1 AE3 3 THR I 160 TRP I 163 0 SHEET 2 AE3 3 ILE I 204 HIS I 209 -1 O ASN I 206 N SER I 162 SHEET 3 AE3 3 THR I 214 LYS I 219 -1 O VAL I 216 N VAL I 207 SHEET 1 AE4 4 MET J 4 THR J 5 0 SHEET 2 AE4 4 VAL J 19 ALA J 25 -1 O SER J 24 N THR J 5 SHEET 3 AE4 4 ASP J 70 ILE J 75 -1 O LEU J 73 N ILE J 21 SHEET 4 AE4 4 PHE J 62 SER J 67 -1 N SER J 63 O THR J 74 SHEET 1 AE5 6 SER J 10 SER J 14 0 SHEET 2 AE5 6 THR J 102 LYS J 107 1 O LYS J 107 N ALA J 13 SHEET 3 AE5 6 ALA J 84 GLN J 90 -1 N ALA J 84 O LEU J 104 SHEET 4 AE5 6 LEU J 33 GLN J 38 -1 N GLN J 38 O THR J 85 SHEET 5 AE5 6 VAL J 44 TYR J 49 -1 O LEU J 47 N TRP J 35 SHEET 6 AE5 6 ARG J 53 LEU J 54 -1 O ARG J 53 N TYR J 49 SHEET 1 AE6 4 SER J 10 SER J 14 0 SHEET 2 AE6 4 THR J 102 LYS J 107 1 O LYS J 107 N ALA J 13 SHEET 3 AE6 4 ALA J 84 GLN J 90 -1 N ALA J 84 O LEU J 104 SHEET 4 AE6 4 THR J 97 PHE J 98 -1 O THR J 97 N GLN J 90 SHEET 1 AE7 4 SER J 114 PHE J 118 0 SHEET 2 AE7 4 THR J 129 PHE J 139 -1 O LEU J 135 N PHE J 116 SHEET 3 AE7 4 TYR J 173 SER J 182 -1 O LEU J 181 N ALA J 130 SHEET 4 AE7 4 SER J 159 VAL J 163 -1 N SER J 162 O SER J 176 SHEET 1 AE8 4 ALA J 153 LEU J 154 0 SHEET 2 AE8 4 LYS J 145 VAL J 150 -1 N VAL J 150 O ALA J 153 SHEET 3 AE8 4 VAL J 191 THR J 197 -1 O ALA J 193 N LYS J 149 SHEET 4 AE8 4 VAL J 205 ASN J 210 -1 O VAL J 205 N VAL J 196 SHEET 1 AE9 4 LEU M 4 SER M 7 0 SHEET 2 AE9 4 LEU M 18 ALA M 24 -1 O ALA M 23 N VAL M 5 SHEET 3 AE9 4 MET M 80 MET M 85 -1 O MET M 85 N LEU M 18 SHEET 4 AE9 4 PHE M 70 ASP M 75 -1 N THR M 71 O GLN M 84 SHEET 1 AF1 6 GLY M 10 VAL M 12 0 SHEET 2 AF1 6 ILE M 116 VAL M 120 1 O SER M 117 N GLY M 10 SHEET 3 AF1 6 ALA M 94 GLN M 101 -1 N TYR M 96 O ILE M 116 SHEET 4 AF1 6 MET M 34 GLN M 39 -1 N VAL M 37 O TYR M 97 SHEET 5 AF1 6 LEU M 45 ILE M 51 -1 O GLU M 46 N ARG M 38 SHEET 6 AF1 6 THR M 60 TYR M 62 -1 O TYR M 61 N ARG M 50 SHEET 1 AF2 4 GLY M 10 VAL M 12 0 SHEET 2 AF2 4 ILE M 116 VAL M 120 1 O SER M 117 N GLY M 10 SHEET 3 AF2 4 ALA M 94 GLN M 101 -1 N TYR M 96 O ILE M 116 SHEET 4 AF2 4 MET M 109 TRP M 112 -1 O TYR M 111 N ARG M 100 SHEET 1 AF3 4 SER M 129 LEU M 133 0 SHEET 2 AF3 4 THR M 144 TYR M 154 -1 O LYS M 152 N SER M 129 SHEET 3 AF3 4 TYR M 185 PRO M 194 -1 O LEU M 187 N VAL M 151 SHEET 4 AF3 4 VAL M 172 THR M 174 -1 N HIS M 173 O VAL M 190 SHEET 1 AF4 4 SER M 129 LEU M 133 0 SHEET 2 AF4 4 THR M 144 TYR M 154 -1 O LYS M 152 N SER M 129 SHEET 3 AF4 4 TYR M 185 PRO M 194 -1 O LEU M 187 N VAL M 151 SHEET 4 AF4 4 VAL M 178 LEU M 179 -1 N VAL M 178 O SER M 186 SHEET 1 AF5 3 THR M 160 TRP M 163 0 SHEET 2 AF5 3 ILE M 204 HIS M 209 -1 O ASN M 206 N SER M 162 SHEET 3 AF5 3 THR M 214 LYS M 219 -1 O VAL M 216 N VAL M 207 SHEET 1 AF6 4 MET N 4 THR N 5 0 SHEET 2 AF6 4 VAL N 19 ALA N 25 -1 O SER N 24 N THR N 5 SHEET 3 AF6 4 ASP N 70 ILE N 75 -1 O LEU N 73 N ILE N 21 SHEET 4 AF6 4 PHE N 62 SER N 67 -1 N SER N 63 O THR N 74 SHEET 1 AF7 6 SER N 10 ALA N 13 0 SHEET 2 AF7 6 THR N 102 ILE N 106 1 O LYS N 103 N LEU N 11 SHEET 3 AF7 6 THR N 85 GLN N 90 -1 N TYR N 86 O THR N 102 SHEET 4 AF7 6 LEU N 33 GLN N 38 -1 N GLN N 38 O THR N 85 SHEET 5 AF7 6 VAL N 44 TYR N 49 -1 O LEU N 47 N TRP N 35 SHEET 6 AF7 6 ARG N 53 LEU N 54 -1 O ARG N 53 N TYR N 49 SHEET 1 AF8 4 SER N 10 ALA N 13 0 SHEET 2 AF8 4 THR N 102 ILE N 106 1 O LYS N 103 N LEU N 11 SHEET 3 AF8 4 THR N 85 GLN N 90 -1 N TYR N 86 O THR N 102 SHEET 4 AF8 4 THR N 97 PHE N 98 -1 O THR N 97 N GLN N 90 SHEET 1 AF9 4 SER N 114 PHE N 118 0 SHEET 2 AF9 4 THR N 129 PHE N 139 -1 O ASN N 137 N SER N 114 SHEET 3 AF9 4 TYR N 173 SER N 182 -1 O LEU N 179 N VAL N 132 SHEET 4 AF9 4 SER N 159 VAL N 163 -1 N GLN N 160 O THR N 178 SHEET 1 AG1 4 ALA N 153 LEU N 154 0 SHEET 2 AG1 4 LYS N 145 VAL N 150 -1 N VAL N 150 O ALA N 153 SHEET 3 AG1 4 VAL N 191 THR N 197 -1 O GLU N 195 N GLN N 147 SHEET 4 AG1 4 VAL N 205 ASN N 210 -1 O VAL N 205 N VAL N 196 SHEET 1 AG2 4 LEU O 4 SER O 7 0 SHEET 2 AG2 4 LEU O 18 ALA O 24 -1 O SER O 21 N SER O 7 SHEET 3 AG2 4 MET O 80 MET O 85 -1 O MET O 85 N LEU O 18 SHEET 4 AG2 4 PHE O 70 ASP O 75 -1 N SER O 73 O TYR O 82 SHEET 1 AG3 6 GLY O 10 VAL O 12 0 SHEET 2 AG3 6 ILE O 116 VAL O 120 1 O THR O 119 N GLY O 10 SHEET 3 AG3 6 ALA O 94 GLN O 101 -1 N TYR O 96 O ILE O 116 SHEET 4 AG3 6 MET O 34 GLN O 39 -1 N VAL O 37 O TYR O 97 SHEET 5 AG3 6 LEU O 45 ILE O 51 -1 O GLU O 46 N ARG O 38 SHEET 6 AG3 6 THR O 60 TYR O 62 -1 O TYR O 61 N ARG O 50 SHEET 1 AG4 4 GLY O 10 VAL O 12 0 SHEET 2 AG4 4 ILE O 116 VAL O 120 1 O THR O 119 N GLY O 10 SHEET 3 AG4 4 ALA O 94 GLN O 101 -1 N TYR O 96 O ILE O 116 SHEET 4 AG4 4 MET O 109 TRP O 112 -1 O TYR O 111 N ARG O 100 SHEET 1 AG5 4 SER O 129 LEU O 133 0 SHEET 2 AG5 4 THR O 144 TYR O 154 -1 O LEU O 150 N PHE O 131 SHEET 3 AG5 4 TYR O 185 PRO O 194 -1 O LEU O 187 N VAL O 151 SHEET 4 AG5 4 VAL O 172 THR O 174 -1 N HIS O 173 O VAL O 190 SHEET 1 AG6 4 SER O 129 LEU O 133 0 SHEET 2 AG6 4 THR O 144 TYR O 154 -1 O LEU O 150 N PHE O 131 SHEET 3 AG6 4 TYR O 185 PRO O 194 -1 O LEU O 187 N VAL O 151 SHEET 4 AG6 4 VAL O 178 LEU O 179 -1 N VAL O 178 O SER O 186 SHEET 1 AG7 3 THR O 160 TRP O 163 0 SHEET 2 AG7 3 ILE O 204 HIS O 209 -1 O ASN O 206 N SER O 162 SHEET 3 AG7 3 THR O 214 LYS O 219 -1 O VAL O 216 N VAL O 207 SHEET 1 AG8 4 MET P 4 THR P 5 0 SHEET 2 AG8 4 VAL P 19 ALA P 25 -1 O SER P 24 N THR P 5 SHEET 3 AG8 4 ASP P 70 ILE P 75 -1 O TYR P 71 N CYS P 23 SHEET 4 AG8 4 PHE P 62 SER P 67 -1 N SER P 63 O THR P 74 SHEET 1 AG9 6 SER P 10 SER P 14 0 SHEET 2 AG9 6 THR P 102 LYS P 107 1 O GLU P 105 N LEU P 11 SHEET 3 AG9 6 ALA P 84 GLN P 90 -1 N ALA P 84 O LEU P 104 SHEET 4 AG9 6 LEU P 33 GLN P 38 -1 N GLN P 38 O THR P 85 SHEET 5 AG9 6 VAL P 44 TYR P 49 -1 O LEU P 47 N TRP P 35 SHEET 6 AG9 6 ARG P 53 LEU P 54 -1 O ARG P 53 N TYR P 49 SHEET 1 AH1 4 SER P 10 SER P 14 0 SHEET 2 AH1 4 THR P 102 LYS P 107 1 O GLU P 105 N LEU P 11 SHEET 3 AH1 4 ALA P 84 GLN P 90 -1 N ALA P 84 O LEU P 104 SHEET 4 AH1 4 THR P 97 PHE P 98 -1 O THR P 97 N GLN P 90 SHEET 1 AH2 4 SER P 114 PHE P 118 0 SHEET 2 AH2 4 THR P 129 PHE P 139 -1 O LEU P 135 N PHE P 116 SHEET 3 AH2 4 TYR P 173 SER P 182 -1 O TYR P 173 N PHE P 139 SHEET 4 AH2 4 SER P 159 VAL P 163 -1 N GLN P 160 O THR P 178 SHEET 1 AH3 4 ALA P 153 LEU P 154 0 SHEET 2 AH3 4 LYS P 145 VAL P 150 -1 N VAL P 150 O ALA P 153 SHEET 3 AH3 4 VAL P 191 THR P 197 -1 O ALA P 193 N LYS P 149 SHEET 4 AH3 4 VAL P 205 ASN P 210 -1 O VAL P 205 N VAL P 196 SSBOND 1 CYS A 22 CYS A 98 1555 1555 2.13 SSBOND 2 CYS A 149 CYS A 205 1555 1555 2.07 SSBOND 3 CYS B 23 CYS B 88 1555 1555 2.16 SSBOND 4 CYS B 134 CYS B 194 1555 1555 2.03 SSBOND 5 CYS C 22 CYS C 98 1555 1555 2.08 SSBOND 6 CYS C 149 CYS C 205 1555 1555 2.04 SSBOND 7 CYS D 23 CYS D 88 1555 1555 2.13 SSBOND 8 CYS D 134 CYS D 194 1555 1555 2.09 SSBOND 9 CYS G 22 CYS G 98 1555 1555 2.09 SSBOND 10 CYS G 149 CYS G 205 1555 1555 2.06 SSBOND 11 CYS H 23 CYS H 88 1555 1555 2.14 SSBOND 12 CYS H 134 CYS H 194 1555 1555 2.07 SSBOND 13 CYS I 22 CYS I 98 1555 1555 2.10 SSBOND 14 CYS I 149 CYS I 205 1555 1555 2.06 SSBOND 15 CYS J 23 CYS J 88 1555 1555 2.11 SSBOND 16 CYS J 134 CYS J 194 1555 1555 2.06 SSBOND 17 CYS M 22 CYS M 98 1555 1555 2.10 SSBOND 18 CYS M 149 CYS M 205 1555 1555 2.07 SSBOND 19 CYS N 23 CYS N 88 1555 1555 2.15 SSBOND 20 CYS N 134 CYS N 194 1555 1555 2.05 SSBOND 21 CYS O 22 CYS O 98 1555 1555 2.07 SSBOND 22 CYS O 149 CYS O 205 1555 1555 2.06 SSBOND 23 CYS P 23 CYS P 88 1555 1555 2.12 SSBOND 24 CYS P 134 CYS P 194 1555 1555 2.06 LINK C PCA A 3 N LEU A 4 1555 1555 1.33 LINK C PCA C 3 N LEU C 4 1555 1555 1.32 LINK C PCA G 3 N LEU G 4 1555 1555 1.33 LINK C PCA I 3 N LEU I 4 1555 1555 1.33 LINK C PCA M 3 N LEU M 4 1555 1555 1.32 LINK C PCA O 3 N LEU O 4 1555 1555 1.32 CISPEP 1 PHE A 155 PRO A 156 0 -3.13 CISPEP 2 GLU A 157 PRO A 158 0 -2.37 CISPEP 3 PHE B 94 PRO B 95 0 -0.13 CISPEP 4 TYR B 140 PRO B 141 0 1.40 CISPEP 5 PHE C 155 PRO C 156 0 -3.45 CISPEP 6 GLU C 157 PRO C 158 0 -0.85 CISPEP 7 PHE D 94 PRO D 95 0 -0.37 CISPEP 8 TYR D 140 PRO D 141 0 3.17 CISPEP 9 PHE G 155 PRO G 156 0 -3.38 CISPEP 10 GLU G 157 PRO G 158 0 -2.35 CISPEP 11 PHE H 94 PRO H 95 0 0.24 CISPEP 12 TYR H 140 PRO H 141 0 1.06 CISPEP 13 PHE I 155 PRO I 156 0 -3.31 CISPEP 14 GLU I 157 PRO I 158 0 -2.14 CISPEP 15 PHE J 94 PRO J 95 0 -0.14 CISPEP 16 TYR J 140 PRO J 141 0 -0.25 CISPEP 17 PHE M 155 PRO M 156 0 -3.27 CISPEP 18 GLU M 157 PRO M 158 0 -1.83 CISPEP 19 PHE N 94 PRO N 95 0 -0.21 CISPEP 20 TYR N 140 PRO N 141 0 2.26 CISPEP 21 PHE O 155 PRO O 156 0 -2.77 CISPEP 22 GLU O 157 PRO O 158 0 -2.36 CISPEP 23 PHE P 94 PRO P 95 0 -0.93 CISPEP 24 TYR P 140 PRO P 141 0 2.16 CRYST1 195.566 195.566 89.395 90.00 90.00 120.00 P 31 18 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 0.005113 0.002952 0.000000 0.00000 SCALE2 0.000000 0.005904 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011186 0.00000 MTRIX1 1 0.453532 0.891029 -0.019377 -4.27004 1 MTRIX2 1 0.887841 -0.453592 -0.077413 3.63376 1 MTRIX3 1 -0.077766 0.017906 -0.996811 -4.62679 1 MTRIX1 2 -0.479033 -0.877665 -0.015210 101.52815 1 MTRIX2 2 0.877787 -0.478874 -0.013034 -50.61972 1 MTRIX3 2 0.004156 -0.019595 0.999799 29.76441 1 MTRIX1 3 -0.996756 -0.041518 0.068944 100.53392 1 MTRIX2 3 -0.040387 0.999027 0.017719 -55.17005 1 MTRIX3 3 -0.069612 0.014877 -0.997463 24.67962 1 MTRIX1 4 -0.997764 0.065883 0.011276 93.69364 1 MTRIX2 4 0.065869 0.997827 -0.001611 49.79020 1 MTRIX3 4 -0.011358 -0.000865 -0.999935 20.06862 1 MTRIX1 5 -0.384584 -0.923055 0.008053 97.38370 1 MTRIX2 5 0.920039 -0.384007 -0.077890 52.77705 1 MTRIX3 5 0.074989 -0.022546 0.996929 24.03463 1 MTRIX1 6 0.454744 0.890584 0.008295 -4.85069 1 MTRIX2 6 0.890612 -0.454673 -0.009103 2.89836 1 MTRIX3 6 -0.004335 0.011527 -0.999924 -10.22266 1 MTRIX1 7 -0.485896 -0.873989 -0.007001 102.10174 1 MTRIX2 7 0.874005 -0.485915 0.001229 -50.38752 1 MTRIX3 7 -0.004476 -0.005521 0.999975 30.26511 1 MTRIX1 8 -0.998642 -0.051280 -0.009200 101.60756 1 MTRIX2 8 -0.051417 0.998560 0.015304 -54.48023 1 MTRIX3 8 0.008402 0.015756 -0.999841 18.68711 1 MTRIX1 9 -0.997737 0.067194 0.002601 93.68563 1 MTRIX2 9 0.067180 0.997727 -0.005336 49.52331 1 MTRIX3 9 -0.002953 -0.005150 -0.999982 19.36301 1 MTRIX1 10 -0.381736 -0.924151 -0.014939 97.54914 1 MTRIX2 10 0.924266 -0.381626 -0.009739 51.72937 1 MTRIX3 10 0.003299 -0.017525 0.999841 29.48976 1 MTRIX1 11 0.324802 0.944479 -0.049627 2.71808 1 MTRIX2 11 0.943847 -0.327046 -0.046849 -4.07893 1 MTRIX3 11 -0.060478 -0.031624 -0.997668 -4.07404 1 MTRIX1 12 -0.464783 -0.885265 0.016786 100.95749 1 MTRIX2 12 0.885320 -0.464937 -0.006574 -51.76908 1 MTRIX3 12 0.013625 0.011805 0.999837 28.15127 1 MTRIX1 13 -0.985786 -0.155181 0.064387 103.51333 1 MTRIX2 13 -0.157517 0.986967 -0.032919 -46.87084 1 MTRIX3 13 -0.058439 -0.042594 -0.997382 25.73815 1 MTRIX1 14 -0.998473 0.051488 0.020013 94.36301 1 MTRIX2 14 0.051377 0.998661 -0.006002 50.76757 1 MTRIX3 14 -0.020295 -0.004964 -0.999782 20.75947 1 MTRIX1 15 -0.268388 -0.962590 0.037255 90.85007 1 MTRIX2 15 0.961874 -0.269899 -0.044190 46.28607 1 MTRIX3 15 0.052592 0.023974 0.998328 24.19637 1