HEADER IMMUNE SYSTEM 02-DEC-21 7T1W TITLE CRYSTAL STRUCTURE OF HUMAN FAB A194-01 IN COMPLEX WITH ITS SYNTHETIC TITLE 2 TETRASACCHARIDE ARA4 EPITOPE (BSI110886) COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB A194-01 HEAVY CHAIN; COMPND 3 CHAIN: H, H2, H3, H4, H5; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB A194-01 LIGHT CHAIN; COMPND 7 CHAIN: L, L2, L3, L4, L5; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: EXPI293; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: HOSAA.20194.B.K13; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_COMMON: HUMAN; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM_STRAIN: EXPI293 KEYWDS SSGCID, TUBERCULOSIS INFECTION, DIAGNOSTIC ANTIBODY, A194-01, ARA4 KEYWDS 2 TETRASACCHARIDE, LIPOARABINOMANNAN, MANLAM, STRUCTURAL GENOMICS, KEYWDS 3 SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE, IMMUNE KEYWDS 4 SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID) JRNL AUTH J.ABENDROTH,D.M.DRANOW,A.PINTER,A.CHOUDHARY,W.J.HONNEN, JRNL AUTH 2 T.LOWARY,P.S.HORANYI,D.D.LORIMER,T.E.EDWARDS JRNL TITL CRYSTAL STRUCTURE OF HUMAN FAB A194-01 IN COMPLEX WITH ITS JRNL TITL 2 SYNTHETIC TETRASACCHARIDE ARA4 EPITOPE (BSI110886) JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.45 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.18RC1 3776 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) : 2.45 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.47 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 3 NUMBER OF REFLECTIONS : 102796 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.169 REMARK 3 R VALUE (WORKING SET) : 0.168 REMARK 3 FREE R VALUE : 0.218 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.930 REMARK 3 FREE R VALUE TEST SET COUNT : 1982 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 45.4700 - 5.9000 0.98 7278 141 0.1607 0.2043 REMARK 3 2 5.9000 - 4.6900 0.99 7252 141 0.1230 0.1596 REMARK 3 3 4.6900 - 4.0900 0.99 7199 143 0.1158 0.1556 REMARK 3 4 4.0900 - 3.7200 0.99 7218 150 0.1491 0.1975 REMARK 3 5 3.7200 - 3.4500 0.99 7211 161 0.1644 0.2255 REMARK 3 6 3.4500 - 3.2500 0.99 7246 121 0.1765 0.2222 REMARK 3 7 3.2500 - 3.0900 0.99 7186 146 0.1850 0.2221 REMARK 3 8 3.0900 - 2.9500 0.99 7200 119 0.1996 0.2475 REMARK 3 9 2.9500 - 2.8400 0.99 7202 150 0.2109 0.2848 REMARK 3 10 2.8400 - 2.7400 0.99 7183 127 0.2075 0.2852 REMARK 3 11 2.7400 - 2.6600 0.99 7162 149 0.2043 0.2795 REMARK 3 12 2.6600 - 2.5800 0.99 7153 149 0.2134 0.2781 REMARK 3 13 2.5800 - 2.5100 0.99 7188 139 0.2331 0.2566 REMARK 3 14 2.5100 - 2.4500 0.99 7136 146 0.2690 0.3390 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 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) : 0.321 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.542 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 41.19 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.03 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 : 0.004 16808 REMARK 3 ANGLE : 0.841 22909 REMARK 3 CHIRALITY : 0.052 2621 REMARK 3 PLANARITY : 0.005 2915 REMARK 3 DIHEDRAL : 18.261 5913 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 49 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 108 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.2665 -4.0254 -62.6678 REMARK 3 T TENSOR REMARK 3 T11: 0.2233 T22: 0.2214 REMARK 3 T33: 0.1932 T12: 0.0396 REMARK 3 T13: 0.0358 T23: -0.0344 REMARK 3 L TENSOR REMARK 3 L11: 0.8776 L22: 4.0805 REMARK 3 L33: 2.4799 L12: 0.2225 REMARK 3 L13: 0.1909 L23: -1.0093 REMARK 3 S TENSOR REMARK 3 S11: 0.0918 S12: 0.0864 S13: -0.0627 REMARK 3 S21: -0.1472 S22: -0.0224 S23: 0.1053 REMARK 3 S31: 0.0663 S32: 0.0300 S33: -0.0639 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 109 THROUGH 142 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.1905 -13.8106 -45.7217 REMARK 3 T TENSOR REMARK 3 T11: 0.2877 T22: 0.2227 REMARK 3 T33: 0.2856 T12: -0.0767 REMARK 3 T13: -0.0388 T23: -0.0541 REMARK 3 L TENSOR REMARK 3 L11: 2.0399 L22: 1.8395 REMARK 3 L33: 1.9549 L12: 0.3631 REMARK 3 L13: -0.9456 L23: -1.0930 REMARK 3 S TENSOR REMARK 3 S11: 0.1464 S12: -0.1842 S13: -0.1958 REMARK 3 S21: 0.0017 S22: -0.1482 S23: 0.2472 REMARK 3 S31: 0.1808 S32: -0.0578 S33: 0.0077 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 143 THROUGH 222 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.0522 -12.5126 -38.2124 REMARK 3 T TENSOR REMARK 3 T11: 0.2751 T22: 0.2925 REMARK 3 T33: 0.4295 T12: -0.0749 REMARK 3 T13: -0.0312 T23: -0.0354 REMARK 3 L TENSOR REMARK 3 L11: 2.5202 L22: 5.5350 REMARK 3 L33: 3.9588 L12: -0.3761 REMARK 3 L13: -0.2299 L23: 1.8234 REMARK 3 S TENSOR REMARK 3 S11: -0.0090 S12: 0.0026 S13: -0.0846 REMARK 3 S21: -0.1284 S22: -0.2228 S23: 0.5569 REMARK 3 S31: 0.1041 S32: -0.5316 S33: 0.2322 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.6049 8.7492 -39.2784 REMARK 3 T TENSOR REMARK 3 T11: 0.1587 T22: 0.1885 REMARK 3 T33: 0.2578 T12: -0.0233 REMARK 3 T13: -0.0380 T23: 0.0014 REMARK 3 L TENSOR REMARK 3 L11: 6.0145 L22: 0.6718 REMARK 3 L33: 4.2131 L12: 0.2132 REMARK 3 L13: -1.5699 L23: -1.5980 REMARK 3 S TENSOR REMARK 3 S11: -0.1493 S12: -0.3148 S13: -0.6062 REMARK 3 S21: 0.0131 S22: -0.2399 S23: 0.1204 REMARK 3 S31: 0.1756 S32: 0.2955 S33: 0.3767 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 19 THROUGH 38 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.9270 10.2294 -49.8665 REMARK 3 T TENSOR REMARK 3 T11: 0.2289 T22: 0.1764 REMARK 3 T33: 0.2375 T12: 0.0386 REMARK 3 T13: -0.0024 T23: -0.0686 REMARK 3 L TENSOR REMARK 3 L11: 5.8410 L22: 3.6155 REMARK 3 L33: 5.9251 L12: 1.3985 REMARK 3 L13: -1.3622 L23: -0.2714 REMARK 3 S TENSOR REMARK 3 S11: -0.0295 S12: 0.0323 S13: -0.2259 REMARK 3 S21: -0.1193 S22: 0.0731 S23: -0.3143 REMARK 3 S31: 0.1881 S32: 0.4549 S33: -0.0125 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 39 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.7611 14.0896 -48.2711 REMARK 3 T TENSOR REMARK 3 T11: 0.1983 T22: 0.1745 REMARK 3 T33: 0.1670 T12: -0.0332 REMARK 3 T13: 0.0127 T23: 0.0150 REMARK 3 L TENSOR REMARK 3 L11: 4.3832 L22: 3.4393 REMARK 3 L33: 3.7614 L12: -0.8579 REMARK 3 L13: 0.4662 L23: 0.4702 REMARK 3 S TENSOR REMARK 3 S11: -0.0216 S12: -0.0883 S13: 0.1733 REMARK 3 S21: 0.0723 S22: -0.0032 S23: 0.1106 REMARK 3 S31: 0.0688 S32: -0.2586 S33: 0.0230 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 76 THROUGH 112 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.4327 7.0065 -42.3832 REMARK 3 T TENSOR REMARK 3 T11: 0.2277 T22: 0.2693 REMARK 3 T33: 0.2759 T12: -0.0355 REMARK 3 T13: 0.0156 T23: -0.0316 REMARK 3 L TENSOR REMARK 3 L11: 0.8635 L22: 0.3319 REMARK 3 L33: 4.1611 L12: 0.1543 REMARK 3 L13: -1.4974 L23: -0.6160 REMARK 3 S TENSOR REMARK 3 S11: 0.0731 S12: 0.0684 S13: 0.0476 REMARK 3 S21: 0.0494 S22: 0.0289 S23: -0.0464 REMARK 3 S31: 0.0446 S32: -0.0077 S33: -0.0790 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 113 THROUGH 149 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.2406 -14.5278 -25.5391 REMARK 3 T TENSOR REMARK 3 T11: 0.3055 T22: 0.2657 REMARK 3 T33: 0.3347 T12: -0.0718 REMARK 3 T13: 0.0503 T23: -0.0253 REMARK 3 L TENSOR REMARK 3 L11: 2.6564 L22: 6.3781 REMARK 3 L33: 2.6374 L12: 2.4956 REMARK 3 L13: 0.6595 L23: 0.9130 REMARK 3 S TENSOR REMARK 3 S11: -0.0508 S12: 0.0541 S13: -0.1328 REMARK 3 S21: 0.0791 S22: 0.0570 S23: 0.2398 REMARK 3 S31: 0.4653 S32: -0.1903 S33: 0.0043 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 150 THROUGH 162 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.9715 -19.5432 -22.1698 REMARK 3 T TENSOR REMARK 3 T11: 0.5811 T22: 0.3393 REMARK 3 T33: 0.5542 T12: 0.0246 REMARK 3 T13: -0.1121 T23: 0.0115 REMARK 3 L TENSOR REMARK 3 L11: 2.4604 L22: 6.8928 REMARK 3 L33: 4.9980 L12: 1.5085 REMARK 3 L13: 0.5861 L23: -1.6009 REMARK 3 S TENSOR REMARK 3 S11: 0.0993 S12: -0.2611 S13: -0.5194 REMARK 3 S21: 0.9073 S22: -0.0718 S23: -0.6431 REMARK 3 S31: 0.4168 S32: 0.1749 S33: -0.0477 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 163 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.4190 -13.6734 -22.1392 REMARK 3 T TENSOR REMARK 3 T11: 0.3596 T22: 0.3046 REMARK 3 T33: 0.3730 T12: -0.0987 REMARK 3 T13: 0.0483 T23: 0.0267 REMARK 3 L TENSOR REMARK 3 L11: 1.7813 L22: 5.8895 REMARK 3 L33: 2.1239 L12: 1.5726 REMARK 3 L13: 0.4092 L23: 0.3020 REMARK 3 S TENSOR REMARK 3 S11: 0.2623 S12: -0.2783 S13: -0.2596 REMARK 3 S21: 0.5272 S22: -0.2110 S23: 0.2132 REMARK 3 S31: 0.6175 S32: -0.2253 S33: -0.0907 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'H2' AND (RESID 1 THROUGH 33 ) REMARK 3 ORIGIN FOR THE GROUP (A): -36.6773 10.3659 -7.8761 REMARK 3 T TENSOR REMARK 3 T11: 0.2772 T22: 0.4097 REMARK 3 T33: 0.3141 T12: -0.0179 REMARK 3 T13: -0.0546 T23: 0.0883 REMARK 3 L TENSOR REMARK 3 L11: 4.9958 L22: 4.4197 REMARK 3 L33: 2.8438 L12: -1.4406 REMARK 3 L13: -0.6184 L23: 0.8833 REMARK 3 S TENSOR REMARK 3 S11: 0.3717 S12: 0.2949 S13: -0.3243 REMARK 3 S21: -0.2230 S22: -0.3107 S23: 0.2080 REMARK 3 S31: -0.0134 S32: -0.0831 S33: -0.0389 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'H2' AND (RESID 34 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): -33.7916 16.5440 -2.9600 REMARK 3 T TENSOR REMARK 3 T11: 0.2535 T22: 0.3544 REMARK 3 T33: 0.3639 T12: -0.0551 REMARK 3 T13: -0.0631 T23: 0.1031 REMARK 3 L TENSOR REMARK 3 L11: 2.1907 L22: 3.1436 REMARK 3 L33: 2.5645 L12: -1.0237 REMARK 3 L13: -0.9043 L23: 0.2456 REMARK 3 S TENSOR REMARK 3 S11: -0.1420 S12: 0.1018 S13: 0.2398 REMARK 3 S21: -0.0739 S22: 0.0247 S23: -0.2305 REMARK 3 S31: -0.0742 S32: 0.1650 S33: 0.1126 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'H2' AND (RESID 120 THROUGH 222 ) REMARK 3 ORIGIN FOR THE GROUP (A): -28.1234 -14.7053 2.4727 REMARK 3 T TENSOR REMARK 3 T11: 0.3669 T22: 0.4093 REMARK 3 T33: 0.4255 T12: -0.1294 REMARK 3 T13: 0.0535 T23: -0.0174 REMARK 3 L TENSOR REMARK 3 L11: 5.3548 L22: 3.8584 REMARK 3 L33: 3.4411 L12: 0.6504 REMARK 3 L13: -0.5568 L23: -0.8653 REMARK 3 S TENSOR REMARK 3 S11: -0.1916 S12: 0.3952 S13: -0.3612 REMARK 3 S21: -0.1849 S22: 0.1465 S23: 0.4380 REMARK 3 S31: 0.6024 S32: -0.7000 S33: -0.0088 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'L2' AND (RESID 1 THROUGH 25 ) REMARK 3 ORIGIN FOR THE GROUP (A): -32.2956 14.1683 22.9592 REMARK 3 T TENSOR REMARK 3 T11: 0.3163 T22: 0.4075 REMARK 3 T33: 0.3791 T12: -0.0340 REMARK 3 T13: -0.0981 T23: 0.0187 REMARK 3 L TENSOR REMARK 3 L11: 3.2531 L22: 2.3615 REMARK 3 L33: 0.6490 L12: -0.1468 REMARK 3 L13: 0.2171 L23: 1.2045 REMARK 3 S TENSOR REMARK 3 S11: -0.3229 S12: -0.1216 S13: 0.2452 REMARK 3 S21: 0.0451 S22: 0.0857 S23: -0.3525 REMARK 3 S31: 0.0291 S32: 0.1044 S33: 0.2013 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'L2' AND (RESID 26 THROUGH 38 ) REMARK 3 ORIGIN FOR THE GROUP (A): -36.6681 21.7216 13.7163 REMARK 3 T TENSOR REMARK 3 T11: 0.2785 T22: 0.3578 REMARK 3 T33: 0.2712 T12: 0.0039 REMARK 3 T13: -0.0657 T23: 0.0435 REMARK 3 L TENSOR REMARK 3 L11: 3.4942 L22: 9.1749 REMARK 3 L33: 4.7730 L12: 2.5181 REMARK 3 L13: 1.5732 L23: 6.0915 REMARK 3 S TENSOR REMARK 3 S11: -0.1851 S12: 0.1915 S13: 0.4070 REMARK 3 S21: -0.6105 S22: -0.0631 S23: 0.5720 REMARK 3 S31: -0.4655 S32: 0.2377 S33: 0.2423 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'L2' AND (RESID 39 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): -42.1559 14.7606 17.1991 REMARK 3 T TENSOR REMARK 3 T11: 0.3144 T22: 0.2930 REMARK 3 T33: 0.3462 T12: -0.0444 REMARK 3 T13: -0.0891 T23: 0.0760 REMARK 3 L TENSOR REMARK 3 L11: 4.4334 L22: 1.9601 REMARK 3 L33: 6.6220 L12: 0.1051 REMARK 3 L13: -0.4970 L23: 2.5857 REMARK 3 S TENSOR REMARK 3 S11: -0.0041 S12: -0.0873 S13: -0.1582 REMARK 3 S21: 0.4453 S22: -0.1501 S23: -0.0259 REMARK 3 S31: 0.4255 S32: -0.1122 S33: 0.1795 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'L2' AND (RESID 76 THROUGH 127 ) REMARK 3 ORIGIN FOR THE GROUP (A): -30.7654 0.3980 14.4850 REMARK 3 T TENSOR REMARK 3 T11: 0.3757 T22: 0.3099 REMARK 3 T33: 0.2852 T12: -0.0687 REMARK 3 T13: 0.0069 T23: 0.0480 REMARK 3 L TENSOR REMARK 3 L11: 2.0090 L22: 2.4496 REMARK 3 L33: 0.4478 L12: -1.6027 REMARK 3 L13: -0.0027 L23: 0.1537 REMARK 3 S TENSOR REMARK 3 S11: -0.1970 S12: -0.0694 S13: -0.0843 REMARK 3 S21: 0.0322 S22: 0.0355 S23: -0.0500 REMARK 3 S31: 0.1725 S32: 0.0138 S33: 0.1741 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'L2' AND (RESID 128 THROUGH 173 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.8289 -12.5092 17.5747 REMARK 3 T TENSOR REMARK 3 T11: 0.4347 T22: 0.3975 REMARK 3 T33: 0.4287 T12: -0.0579 REMARK 3 T13: 0.0196 T23: 0.1060 REMARK 3 L TENSOR REMARK 3 L11: 6.4603 L22: 4.0595 REMARK 3 L33: 1.5170 L12: -4.0691 REMARK 3 L13: -2.4708 L23: 1.4952 REMARK 3 S TENSOR REMARK 3 S11: -0.5256 S12: -0.4198 S13: -0.0889 REMARK 3 S21: 0.4412 S22: 0.2242 S23: -0.2889 REMARK 3 S31: 0.2791 S32: 0.1753 S33: 0.3160 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'L2' AND (RESID 174 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.1934 -22.6228 15.8720 REMARK 3 T TENSOR REMARK 3 T11: 0.4080 T22: 0.3430 REMARK 3 T33: 0.5214 T12: 0.0184 REMARK 3 T13: 0.0146 T23: 0.1285 REMARK 3 L TENSOR REMARK 3 L11: 5.8429 L22: 8.0841 REMARK 3 L33: 5.9334 L12: -3.9342 REMARK 3 L13: -2.0729 L23: 2.6178 REMARK 3 S TENSOR REMARK 3 S11: -0.2724 S12: -0.2680 S13: -0.4951 REMARK 3 S21: 0.4946 S22: 0.1822 S23: -0.4288 REMARK 3 S31: 0.8958 S32: 0.5262 S33: 0.1354 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'H3' AND (RESID 1 THROUGH 143 ) REMARK 3 ORIGIN FOR THE GROUP (A): -33.7521 -41.9010 -38.7902 REMARK 3 T TENSOR REMARK 3 T11: 0.2493 T22: 0.4113 REMARK 3 T33: 0.4724 T12: -0.0538 REMARK 3 T13: -0.0310 T23: -0.0882 REMARK 3 L TENSOR REMARK 3 L11: 2.4911 L22: 2.2731 REMARK 3 L33: 1.7889 L12: 0.7326 REMARK 3 L13: 1.0890 L23: 0.4951 REMARK 3 S TENSOR REMARK 3 S11: -0.2398 S12: 0.0554 S13: 0.3114 REMARK 3 S21: -0.0248 S22: 0.2272 S23: -0.3216 REMARK 3 S31: -0.2087 S32: 0.3556 S33: 0.0199 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'H3' AND (RESID 144 THROUGH 222 ) REMARK 3 ORIGIN FOR THE GROUP (A): -50.1830 -19.5207 -40.7746 REMARK 3 T TENSOR REMARK 3 T11: 0.8674 T22: 0.4713 REMARK 3 T33: 1.5112 T12: -0.0753 REMARK 3 T13: -0.7433 T23: -0.3733 REMARK 3 L TENSOR REMARK 3 L11: 4.0053 L22: 3.9574 REMARK 3 L33: 3.5304 L12: 0.6683 REMARK 3 L13: 2.9452 L23: -0.3077 REMARK 3 S TENSOR REMARK 3 S11: -1.2530 S12: -1.0999 S13: 1.7947 REMARK 3 S21: 1.5934 S22: 0.2999 S23: -1.3254 REMARK 3 S31: -0.9872 S32: -0.5601 S33: 0.5250 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'L3' AND (RESID 1 THROUGH 25 ) REMARK 3 ORIGIN FOR THE GROUP (A): -52.8088 -52.4196 -54.2143 REMARK 3 T TENSOR REMARK 3 T11: 0.3181 T22: 0.2987 REMARK 3 T33: 0.2821 T12: -0.0828 REMARK 3 T13: 0.0370 T23: -0.0171 REMARK 3 L TENSOR REMARK 3 L11: 2.7837 L22: 5.3007 REMARK 3 L33: 4.6608 L12: -3.2734 REMARK 3 L13: -2.3052 L23: 0.9054 REMARK 3 S TENSOR REMARK 3 S11: 0.0701 S12: 0.4973 S13: 0.4566 REMARK 3 S21: -0.5910 S22: -0.0264 S23: -0.4131 REMARK 3 S31: -0.0991 S32: 0.1302 S33: -0.0140 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'L3' AND (RESID 26 THROUGH 38 ) REMARK 3 ORIGIN FOR THE GROUP (A): -43.9413 -57.4274 -47.3444 REMARK 3 T TENSOR REMARK 3 T11: 0.2171 T22: 0.3220 REMARK 3 T33: 0.3632 T12: -0.0474 REMARK 3 T13: 0.0223 T23: -0.0556 REMARK 3 L TENSOR REMARK 3 L11: 2.1776 L22: 2.1410 REMARK 3 L33: 4.9181 L12: -0.9645 REMARK 3 L13: -0.6592 L23: 3.0859 REMARK 3 S TENSOR REMARK 3 S11: -0.1548 S12: 0.1345 S13: 0.1282 REMARK 3 S21: -0.1932 S22: 0.4226 S23: -0.6457 REMARK 3 S31: 0.0875 S32: 0.4070 S33: -0.2730 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'L3' AND (RESID 39 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): -52.2314 -55.2460 -42.8664 REMARK 3 T TENSOR REMARK 3 T11: 0.2100 T22: 0.2005 REMARK 3 T33: 0.2088 T12: -0.0355 REMARK 3 T13: -0.0235 T23: -0.0204 REMARK 3 L TENSOR REMARK 3 L11: 6.5118 L22: 2.1090 REMARK 3 L33: 5.0517 L12: 0.3514 REMARK 3 L13: -1.2901 L23: -1.0191 REMARK 3 S TENSOR REMARK 3 S11: -0.1701 S12: -0.0758 S13: 0.1261 REMARK 3 S21: -0.0668 S22: 0.0120 S23: 0.1464 REMARK 3 S31: -0.2779 S32: -0.0911 S33: 0.1958 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'L3' AND (RESID 76 THROUGH 127 ) REMARK 3 ORIGIN FOR THE GROUP (A): -52.6649 -37.6572 -48.4934 REMARK 3 T TENSOR REMARK 3 T11: 0.3252 T22: 0.2714 REMARK 3 T33: 0.5163 T12: -0.0771 REMARK 3 T13: -0.1102 T23: -0.0596 REMARK 3 L TENSOR REMARK 3 L11: 2.4635 L22: 1.1240 REMARK 3 L33: 0.8576 L12: 0.0013 REMARK 3 L13: 0.7294 L23: 0.1322 REMARK 3 S TENSOR REMARK 3 S11: -0.5726 S12: -0.1746 S13: 0.9256 REMARK 3 S21: 0.1194 S22: 0.3342 S23: -0.1452 REMARK 3 S31: -0.3187 S32: 0.1537 S33: 0.0646 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'L3' AND (RESID 128 THROUGH 149 ) REMARK 3 ORIGIN FOR THE GROUP (A): -58.1073 -22.0831 -55.8908 REMARK 3 T TENSOR REMARK 3 T11: 0.5027 T22: 0.4614 REMARK 3 T33: 1.0251 T12: -0.1205 REMARK 3 T13: -0.2402 T23: 0.1520 REMARK 3 L TENSOR REMARK 3 L11: 1.9162 L22: 3.1910 REMARK 3 L33: 2.3247 L12: 2.2527 REMARK 3 L13: -1.1711 L23: -0.4162 REMARK 3 S TENSOR REMARK 3 S11: -0.2035 S12: 0.2233 S13: 0.9765 REMARK 3 S21: 0.0137 S22: 0.0948 S23: -0.8450 REMARK 3 S31: -0.1179 S32: -0.0529 S33: 0.1665 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'L3' AND (RESID 150 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): -57.3317 -17.2826 -57.3531 REMARK 3 T TENSOR REMARK 3 T11: 0.6608 T22: 0.5238 REMARK 3 T33: 1.2423 T12: -0.1933 REMARK 3 T13: -0.2795 T23: 0.2082 REMARK 3 L TENSOR REMARK 3 L11: 0.2411 L22: 2.0104 REMARK 3 L33: 0.1842 L12: 0.2168 REMARK 3 L13: -0.0699 L23: 0.3248 REMARK 3 S TENSOR REMARK 3 S11: -0.4050 S12: 0.2088 S13: 1.1938 REMARK 3 S21: -0.2490 S22: -0.0403 S23: -0.6059 REMARK 3 S31: -0.4667 S32: 0.1362 S33: 0.2721 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'H4' AND (RESID 1 THROUGH 33 ) REMARK 3 ORIGIN FOR THE GROUP (A): -69.3001 35.9793 -49.3095 REMARK 3 T TENSOR REMARK 3 T11: 0.2554 T22: 0.2001 REMARK 3 T33: 0.1535 T12: 0.0117 REMARK 3 T13: -0.0123 T23: 0.0255 REMARK 3 L TENSOR REMARK 3 L11: 7.5737 L22: 8.2413 REMARK 3 L33: 2.3940 L12: 6.3240 REMARK 3 L13: 0.8308 L23: 1.5608 REMARK 3 S TENSOR REMARK 3 S11: -0.2359 S12: 0.3851 S13: -0.0293 REMARK 3 S21: -0.5897 S22: 0.2858 S23: 0.0246 REMARK 3 S31: 0.0073 S32: -0.0053 S33: -0.0272 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'H4' AND (RESID 34 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): -72.0356 38.7268 -41.7573 REMARK 3 T TENSOR REMARK 3 T11: 0.2229 T22: 0.1804 REMARK 3 T33: 0.1697 T12: 0.0092 REMARK 3 T13: 0.0077 T23: -0.0018 REMARK 3 L TENSOR REMARK 3 L11: 5.3542 L22: 2.9862 REMARK 3 L33: 1.4616 L12: 1.5180 REMARK 3 L13: 0.7520 L23: -0.2525 REMARK 3 S TENSOR REMARK 3 S11: -0.0205 S12: -0.1748 S13: 0.0503 REMARK 3 S21: 0.0056 S22: -0.0240 S23: -0.0219 REMARK 3 S31: -0.1257 S32: 0.0276 S33: 0.0483 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: CHAIN 'H4' AND (RESID 120 THROUGH 142 ) REMARK 3 ORIGIN FOR THE GROUP (A): -37.9265 39.2577 -45.9339 REMARK 3 T TENSOR REMARK 3 T11: 0.3856 T22: 0.6651 REMARK 3 T33: 0.3244 T12: 0.1121 REMARK 3 T13: 0.0315 T23: 0.0678 REMARK 3 L TENSOR REMARK 3 L11: 3.3554 L22: 1.1873 REMARK 3 L33: 1.3275 L12: 1.7060 REMARK 3 L13: -0.1571 L23: 0.4282 REMARK 3 S TENSOR REMARK 3 S11: -0.0152 S12: 0.2937 S13: 0.0843 REMARK 3 S21: 0.1902 S22: 0.0964 S23: -0.4705 REMARK 3 S31: 0.0560 S32: 0.8663 S33: -0.0598 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: CHAIN 'H4' AND (RESID 143 THROUGH 183 ) REMARK 3 ORIGIN FOR THE GROUP (A): -42.2096 34.2824 -42.9023 REMARK 3 T TENSOR REMARK 3 T11: 0.2555 T22: 0.4259 REMARK 3 T33: 0.2718 T12: 0.0206 REMARK 3 T13: 0.0317 T23: 0.0685 REMARK 3 L TENSOR REMARK 3 L11: 4.9234 L22: 7.5495 REMARK 3 L33: 4.0195 L12: -2.2864 REMARK 3 L13: 0.3885 L23: -1.1994 REMARK 3 S TENSOR REMARK 3 S11: 0.4246 S12: 0.2598 S13: 0.0764 REMARK 3 S21: -0.4817 S22: -0.3652 S23: 0.0948 REMARK 3 S31: 0.2171 S32: 0.4984 S33: -0.0917 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: CHAIN 'H4' AND (RESID 184 THROUGH 198 ) REMARK 3 ORIGIN FOR THE GROUP (A): -36.3569 26.2848 -42.3313 REMARK 3 T TENSOR REMARK 3 T11: 0.2995 T22: 0.5867 REMARK 3 T33: 0.3476 T12: 0.0803 REMARK 3 T13: 0.0296 T23: 0.0051 REMARK 3 L TENSOR REMARK 3 L11: 3.6638 L22: 1.4268 REMARK 3 L33: 4.9876 L12: 2.1194 REMARK 3 L13: 0.4686 L23: -0.5303 REMARK 3 S TENSOR REMARK 3 S11: -0.0945 S12: 0.4050 S13: 0.0210 REMARK 3 S21: -0.1859 S22: 0.3759 S23: -0.7900 REMARK 3 S31: 0.6562 S32: 0.6665 S33: -0.2830 REMARK 3 TLS GROUP : 33 REMARK 3 SELECTION: CHAIN 'H4' AND (RESID 199 THROUGH 222 ) REMARK 3 ORIGIN FOR THE GROUP (A): -39.4263 31.4115 -52.1516 REMARK 3 T TENSOR REMARK 3 T11: 0.6408 T22: 0.8324 REMARK 3 T33: 0.4377 T12: 0.2512 REMARK 3 T13: 0.0433 T23: 0.0353 REMARK 3 L TENSOR REMARK 3 L11: 7.9142 L22: 3.3477 REMARK 3 L33: 0.0134 L12: -4.4926 REMARK 3 L13: -0.4071 L23: 0.1923 REMARK 3 S TENSOR REMARK 3 S11: 0.6505 S12: 0.6548 S13: 0.1426 REMARK 3 S21: -1.2713 S22: -0.3123 S23: -0.2498 REMARK 3 S31: 0.5358 S32: 0.9562 S33: -0.1928 REMARK 3 TLS GROUP : 34 REMARK 3 SELECTION: CHAIN 'L4' AND (RESID 1 THROUGH 25 ) REMARK 3 ORIGIN FOR THE GROUP (A): -64.0112 28.2883 -19.6272 REMARK 3 T TENSOR REMARK 3 T11: 0.2651 T22: 0.3168 REMARK 3 T33: 0.3198 T12: -0.0727 REMARK 3 T13: -0.0165 T23: 0.0475 REMARK 3 L TENSOR REMARK 3 L11: 3.7483 L22: 0.3788 REMARK 3 L33: 2.7227 L12: -0.0609 REMARK 3 L13: -0.5556 L23: 0.7024 REMARK 3 S TENSOR REMARK 3 S11: 0.1752 S12: 0.0120 S13: 0.1059 REMARK 3 S21: 0.0824 S22: -0.1336 S23: -0.2990 REMARK 3 S31: -0.1693 S32: 0.3493 S33: -0.1019 REMARK 3 TLS GROUP : 35 REMARK 3 SELECTION: CHAIN 'L4' AND (RESID 26 THROUGH 38 ) REMARK 3 ORIGIN FOR THE GROUP (A): -73.8560 30.6571 -25.9453 REMARK 3 T TENSOR REMARK 3 T11: 0.2718 T22: 0.3107 REMARK 3 T33: 0.2550 T12: 0.0045 REMARK 3 T13: -0.0178 T23: 0.0404 REMARK 3 L TENSOR REMARK 3 L11: 4.5378 L22: 4.5800 REMARK 3 L33: 5.4566 L12: -1.6603 REMARK 3 L13: -4.9325 L23: 2.5255 REMARK 3 S TENSOR REMARK 3 S11: 0.2493 S12: 0.1620 S13: -0.0717 REMARK 3 S21: 0.2091 S22: -0.2405 S23: 0.1636 REMARK 3 S31: -0.3390 S32: -0.3786 S33: 0.0914 REMARK 3 TLS GROUP : 36 REMARK 3 SELECTION: CHAIN 'L4' AND (RESID 39 THROUGH 112 ) REMARK 3 ORIGIN FOR THE GROUP (A): -65.0930 24.6647 -27.3588 REMARK 3 T TENSOR REMARK 3 T11: 0.1991 T22: 0.2331 REMARK 3 T33: 0.2158 T12: -0.0180 REMARK 3 T13: 0.0339 T23: 0.0416 REMARK 3 L TENSOR REMARK 3 L11: 2.8739 L22: 0.9594 REMARK 3 L33: 1.1710 L12: -0.3408 REMARK 3 L13: 1.1198 L23: -0.2465 REMARK 3 S TENSOR REMARK 3 S11: 0.0705 S12: -0.0737 S13: -0.0736 REMARK 3 S21: 0.0913 S22: -0.0821 S23: -0.1601 REMARK 3 S31: -0.0606 S32: 0.1301 S33: 0.0033 REMARK 3 TLS GROUP : 37 REMARK 3 SELECTION: CHAIN 'L4' AND (RESID 113 THROUGH 127 ) REMARK 3 ORIGIN FOR THE GROUP (A): -28.2223 36.0618 -41.8609 REMARK 3 T TENSOR REMARK 3 T11: 0.4042 T22: 0.9129 REMARK 3 T33: 0.6604 T12: 0.0408 REMARK 3 T13: 0.0532 T23: 0.2020 REMARK 3 L TENSOR REMARK 3 L11: 7.2490 L22: 5.3399 REMARK 3 L33: 7.2521 L12: 4.9245 REMARK 3 L13: -3.2479 L23: -5.2591 REMARK 3 S TENSOR REMARK 3 S11: -0.0847 S12: 0.5269 S13: 0.5711 REMARK 3 S21: -0.5815 S22: -0.2682 S23: -0.7073 REMARK 3 S31: 0.0382 S32: 1.0639 S33: 0.2814 REMARK 3 TLS GROUP : 38 REMARK 3 SELECTION: CHAIN 'L4' AND (RESID 128 THROUGH 149 ) REMARK 3 ORIGIN FOR THE GROUP (A): -34.8775 32.2090 -29.1585 REMARK 3 T TENSOR REMARK 3 T11: 0.2183 T22: 0.4544 REMARK 3 T33: 0.4124 T12: 0.0041 REMARK 3 T13: -0.0607 T23: 0.0216 REMARK 3 L TENSOR REMARK 3 L11: 6.8416 L22: 8.1361 REMARK 3 L33: 6.4558 L12: 5.0501 REMARK 3 L13: -3.3863 L23: -4.7573 REMARK 3 S TENSOR REMARK 3 S11: 0.2641 S12: -0.3712 S13: 0.6586 REMARK 3 S21: 0.4189 S22: -0.1553 S23: -0.1742 REMARK 3 S31: -0.4149 S32: 0.5143 S33: -0.1439 REMARK 3 TLS GROUP : 39 REMARK 3 SELECTION: CHAIN 'L4' AND (RESID 150 THROUGH 173 ) REMARK 3 ORIGIN FOR THE GROUP (A): -38.4812 32.7850 -29.2980 REMARK 3 T TENSOR REMARK 3 T11: 0.2977 T22: 0.4423 REMARK 3 T33: 0.4185 T12: -0.0268 REMARK 3 T13: -0.0810 T23: 0.0206 REMARK 3 L TENSOR REMARK 3 L11: 5.2071 L22: 2.4706 REMARK 3 L33: 2.3981 L12: 0.2669 REMARK 3 L13: -0.7276 L23: -0.6282 REMARK 3 S TENSOR REMARK 3 S11: -0.0538 S12: -0.1107 S13: 0.3895 REMARK 3 S21: 0.3988 S22: 0.0487 S23: -0.6014 REMARK 3 S31: -0.3943 S32: 0.5708 S33: 0.0354 REMARK 3 TLS GROUP : 40 REMARK 3 SELECTION: CHAIN 'L4' AND (RESID 174 THROUGH 212 ) REMARK 3 ORIGIN FOR THE GROUP (A): -26.0548 35.5527 -31.2185 REMARK 3 T TENSOR REMARK 3 T11: 0.3727 T22: 0.9381 REMARK 3 T33: 0.7596 T12: -0.1781 REMARK 3 T13: -0.0595 T23: 0.1513 REMARK 3 L TENSOR REMARK 3 L11: 4.8697 L22: 2.0480 REMARK 3 L33: 0.2625 L12: 1.4562 REMARK 3 L13: -0.8680 L23: 0.0908 REMARK 3 S TENSOR REMARK 3 S11: 0.1719 S12: -0.1801 S13: 0.4360 REMARK 3 S21: 0.2491 S22: -0.5450 S23: -0.7094 REMARK 3 S31: -0.5481 S32: 1.1615 S33: 0.3555 REMARK 3 TLS GROUP : 41 REMARK 3 SELECTION: CHAIN 'H5' AND (RESID 1 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.6081 7.7505 -7.6125 REMARK 3 T TENSOR REMARK 3 T11: 0.2001 T22: 0.2953 REMARK 3 T33: 0.2141 T12: -0.0434 REMARK 3 T13: -0.0019 T23: 0.0380 REMARK 3 L TENSOR REMARK 3 L11: 2.3973 L22: 1.7428 REMARK 3 L33: 2.4355 L12: 0.3689 REMARK 3 L13: -1.1235 L23: -0.0680 REMARK 3 S TENSOR REMARK 3 S11: 0.0802 S12: -0.2764 S13: -0.0760 REMARK 3 S21: 0.1770 S22: -0.0468 S23: 0.0366 REMARK 3 S31: 0.0327 S32: 0.0213 S33: -0.0445 REMARK 3 TLS GROUP : 42 REMARK 3 SELECTION: CHAIN 'H5' AND (RESID 120 THROUGH 142 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.4445 23.5330 18.5291 REMARK 3 T TENSOR REMARK 3 T11: 0.4196 T22: 0.9632 REMARK 3 T33: 0.7953 T12: -0.1024 REMARK 3 T13: 0.0225 T23: -0.2889 REMARK 3 L TENSOR REMARK 3 L11: 3.1931 L22: 1.7560 REMARK 3 L33: 2.1990 L12: -1.0865 REMARK 3 L13: -1.0909 L23: 0.0868 REMARK 3 S TENSOR REMARK 3 S11: -0.0903 S12: 0.0353 S13: 0.4588 REMARK 3 S21: 0.4714 S22: -1.2025 S23: 1.5787 REMARK 3 S31: 0.0454 S32: -0.8427 S33: 1.2315 REMARK 3 TLS GROUP : 43 REMARK 3 SELECTION: CHAIN 'H5' AND (RESID 143 THROUGH 222 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.8962 27.9511 14.7150 REMARK 3 T TENSOR REMARK 3 T11: 0.4250 T22: 1.0479 REMARK 3 T33: 0.7785 T12: -0.0273 REMARK 3 T13: -0.0707 T23: -0.2731 REMARK 3 L TENSOR REMARK 3 L11: 8.8475 L22: 6.5879 REMARK 3 L33: 4.5178 L12: 1.1969 REMARK 3 L13: 0.3951 L23: -1.0127 REMARK 3 S TENSOR REMARK 3 S11: -0.4253 S12: 1.2256 S13: 0.4942 REMARK 3 S21: -0.4293 S22: -0.4665 S23: 0.9556 REMARK 3 S31: -0.1579 S32: -0.4178 S33: 0.8618 REMARK 3 TLS GROUP : 44 REMARK 3 SELECTION: CHAIN 'L5' AND (RESID 1 THROUGH 25 ) REMARK 3 ORIGIN FOR THE GROUP (A): 24.7007 11.2575 8.6177 REMARK 3 T TENSOR REMARK 3 T11: 0.3000 T22: 0.5513 REMARK 3 T33: 0.3724 T12: -0.0296 REMARK 3 T13: -0.0553 T23: 0.1377 REMARK 3 L TENSOR REMARK 3 L11: 1.8892 L22: 5.1697 REMARK 3 L33: 3.0338 L12: -0.0751 REMARK 3 L13: 0.7728 L23: 1.7891 REMARK 3 S TENSOR REMARK 3 S11: 0.0050 S12: -0.2562 S13: -0.1498 REMARK 3 S21: 0.5221 S22: 0.0999 S23: 0.0707 REMARK 3 S31: 0.2818 S32: 0.0487 S33: -0.1617 REMARK 3 TLS GROUP : 45 REMARK 3 SELECTION: CHAIN 'L5' AND (RESID 26 THROUGH 38 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.0654 7.0175 -2.2087 REMARK 3 T TENSOR REMARK 3 T11: 0.2443 T22: 0.4093 REMARK 3 T33: 0.3323 T12: -0.0506 REMARK 3 T13: -0.0706 T23: 0.0053 REMARK 3 L TENSOR REMARK 3 L11: 7.8127 L22: 8.8526 REMARK 3 L33: 2.5048 L12: -7.8895 REMARK 3 L13: -2.1759 L23: 1.1031 REMARK 3 S TENSOR REMARK 3 S11: 0.3857 S12: 0.2748 S13: -0.3982 REMARK 3 S21: -0.2497 S22: -0.5452 S23: 0.1155 REMARK 3 S31: 0.0800 S32: -0.0985 S33: 0.2040 REMARK 3 TLS GROUP : 46 REMARK 3 SELECTION: CHAIN 'L5' AND (RESID 39 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 23.6318 16.4539 -1.6520 REMARK 3 T TENSOR REMARK 3 T11: 0.1741 T22: 0.3656 REMARK 3 T33: 0.2621 T12: -0.0152 REMARK 3 T13: -0.0156 T23: 0.0201 REMARK 3 L TENSOR REMARK 3 L11: 1.5837 L22: 6.1623 REMARK 3 L33: 4.2084 L12: 2.8172 REMARK 3 L13: 0.5851 L23: 0.6695 REMARK 3 S TENSOR REMARK 3 S11: -0.0278 S12: -0.1651 S13: 0.2482 REMARK 3 S21: 0.0272 S22: -0.0490 S23: -0.2766 REMARK 3 S31: -0.0590 S32: 0.1574 S33: 0.0766 REMARK 3 TLS GROUP : 47 REMARK 3 SELECTION: CHAIN 'L5' AND (RESID 76 THROUGH 112 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.9153 16.0941 6.4506 REMARK 3 T TENSOR REMARK 3 T11: 0.1856 T22: 0.4641 REMARK 3 T33: 0.3280 T12: -0.0200 REMARK 3 T13: -0.0402 T23: 0.0318 REMARK 3 L TENSOR REMARK 3 L11: 0.4849 L22: 4.4387 REMARK 3 L33: 6.8138 L12: 0.6600 REMARK 3 L13: 1.1269 L23: 4.7485 REMARK 3 S TENSOR REMARK 3 S11: -0.0084 S12: -0.2993 S13: 0.0997 REMARK 3 S21: 0.2126 S22: -0.0963 S23: -0.0436 REMARK 3 S31: 0.2066 S32: 0.0349 S33: 0.0795 REMARK 3 TLS GROUP : 48 REMARK 3 SELECTION: CHAIN 'L5' AND (RESID 113 THROUGH 187 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.2740 24.4848 27.8893 REMARK 3 T TENSOR REMARK 3 T11: 0.4813 T22: 0.8840 REMARK 3 T33: 0.4797 T12: 0.0229 REMARK 3 T13: 0.0841 T23: -0.1312 REMARK 3 L TENSOR REMARK 3 L11: 7.2092 L22: 2.3104 REMARK 3 L33: 3.0777 L12: 0.6484 REMARK 3 L13: -3.2376 L23: -0.9576 REMARK 3 S TENSOR REMARK 3 S11: -0.4364 S12: -0.9970 S13: -0.0635 REMARK 3 S21: 0.5567 S22: 0.1606 S23: 0.3744 REMARK 3 S31: 0.0773 S32: -0.0302 S33: 0.2162 REMARK 3 TLS GROUP : 49 REMARK 3 SELECTION: CHAIN 'L5' AND (RESID 188 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.8673 29.8031 36.0012 REMARK 3 T TENSOR REMARK 3 T11: 0.6600 T22: 1.4393 REMARK 3 T33: 0.6445 T12: 0.0623 REMARK 3 T13: 0.1097 T23: -0.2913 REMARK 3 L TENSOR REMARK 3 L11: 7.3413 L22: 1.9365 REMARK 3 L33: 1.3820 L12: 0.4799 REMARK 3 L13: -2.8579 L23: -0.9616 REMARK 3 S TENSOR REMARK 3 S11: 0.1225 S12: -2.3799 S13: 0.9977 REMARK 3 S21: 0.4076 S22: 0.0275 S23: 0.5306 REMARK 3 S31: -0.1319 S32: 0.5038 S33: -0.1610 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 "H" and (resid 1 through 4 or REMARK 3 resid 6 through 12 or (resid 13 and (name REMARK 3 N or name CA or name C or name O or name REMARK 3 CB )) or resid 14 through 18 or resid 20 REMARK 3 or resid 22 through 42 or (resid 43 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 44 through 103 or REMARK 3 resid 105 through 112 or (resid 113 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 114 through 124 or REMARK 3 (resid 125 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 126 REMARK 3 through 135 or resid 143 through 166 or REMARK 3 (resid 167 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 168 REMARK 3 through 177 or (resid 178 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 179 through 182 or (resid 183 REMARK 3 and (name N or name CA or name C or name REMARK 3 O or name CB )) or resid 184 through 191 REMARK 3 or (resid 192 and (name N or name CA or REMARK 3 name C or name O or name CB )) or resid REMARK 3 193 through 196 or (resid 197 and (name N REMARK 3 or name CA or name C or name O or name CB REMARK 3 )) or resid 198 through 199 or (resid 200 REMARK 3 and (name N or name CA or name C or name REMARK 3 O or name CB )) or resid 201 through 206 REMARK 3 or (resid 207 and (name N or name CA or REMARK 3 name C or name O or name CB )) or resid REMARK 3 208 or (resid 209 and (name N or name CA REMARK 3 or name C or name O or name CB )) or REMARK 3 resid 210 through 211 or resid 213 REMARK 3 through 216 or (resid 217 through 218 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 219 or (resid 220 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 221 or (resid 222 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 300 through 302 or REMARK 3 resid 311)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "H2" and (resid 1 through 4 or REMARK 3 resid 6 through 12 or (resid 13 and (name REMARK 3 N or name CA or name C or name O or name REMARK 3 CB )) or resid 14 through 18 or resid 20 REMARK 3 or resid 22 through 42 or (resid 43 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 44 through 103 or REMARK 3 resid 105 through 112 or (resid 113 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 114 through 124 or REMARK 3 (resid 125 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 126 REMARK 3 through 135 or resid 143 through 166 or REMARK 3 (resid 167 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 168 REMARK 3 through 177 or (resid 178 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 179 through 182 or (resid 183 REMARK 3 and (name N or name CA or name C or name REMARK 3 O or name CB )) or resid 184 through 191 REMARK 3 or (resid 192 and (name N or name CA or REMARK 3 name C or name O or name CB )) or resid REMARK 3 193 through 196 or (resid 197 and (name N REMARK 3 or name CA or name C or name O or name CB REMARK 3 )) or resid 198 through 199 or (resid 200 REMARK 3 and (name N or name CA or name C or name REMARK 3 O or name CB )) or resid 201 through 206 REMARK 3 or (resid 207 and (name N or name CA or REMARK 3 name C or name O or name CB )) or resid REMARK 3 208 through 211 or resid 213 through 216 REMARK 3 or (resid 217 through 218 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 219 or (resid 220 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 221 through 302 or resid 311)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "H3" and (resid 1 through 4 or REMARK 3 resid 6 through 12 or (resid 13 and (name REMARK 3 N or name CA or name C or name O or name REMARK 3 CB )) or resid 14 through 18 or resid 20 REMARK 3 or resid 22 through 103 or resid 105 REMARK 3 through 124 or (resid 125 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 126 through 211 or resid 213 REMARK 3 through 302 or resid 311)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "H4" and (resid 1 through 4 or REMARK 3 resid 6 through 12 or (resid 13 and (name REMARK 3 N or name CA or name C or name O or name REMARK 3 CB )) or resid 14 through 18 or resid 20 REMARK 3 or resid 22 through 42 or (resid 43 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 44 through 103 or REMARK 3 resid 105 through 112 or (resid 113 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 114 through 124 or REMARK 3 (resid 125 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 126 REMARK 3 through 135 or resid 143 through 166 or REMARK 3 (resid 167 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 168 REMARK 3 through 177 or (resid 178 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 179 through 182 or (resid 183 REMARK 3 and (name N or name CA or name C or name REMARK 3 O or name CB )) or resid 184 through 191 REMARK 3 or (resid 192 and (name N or name CA or REMARK 3 name C or name O or name CB )) or resid REMARK 3 193 through 196 or (resid 197 and (name N REMARK 3 or name CA or name C or name O or name CB REMARK 3 )) or resid 198 through 199 or (resid 200 REMARK 3 and (name N or name CA or name C or name REMARK 3 O or name CB )) or resid 201 through 206 REMARK 3 or (resid 207 and (name N or name CA or REMARK 3 name C or name O or name CB )) or resid REMARK 3 208 or (resid 209 and (name N or name CA REMARK 3 or name C or name O or name CB )) or REMARK 3 resid 210 through 211 or resid 213 or REMARK 3 (resid 214 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 215 REMARK 3 through 216 or (resid 217 through 218 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 219 or (resid 220 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 221 through 302 or REMARK 3 resid 311)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 5 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "H5" and (resid 1 through 4 or REMARK 3 resid 6 through 18 or resid 20 or resid REMARK 3 22 through 42 or (resid 43 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 44 through 103 or resid 105 REMARK 3 through 135 or resid 143 through 166 or REMARK 3 (resid 167 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 168 REMARK 3 through 177 or (resid 178 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 179 through 196 or (resid 197 REMARK 3 and (name N or name CA or name C or name REMARK 3 O or name CB )) or resid 198 through 206 REMARK 3 or (resid 207 and (name N or name CA or REMARK 3 name C or name O or name CB )) or resid REMARK 3 208 through 211 or resid 213 or (resid REMARK 3 214 and (name N or name CA or name C or REMARK 3 name O or name CB )) or resid 215 through REMARK 3 302 or resid 311)) 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 "L" and (resid 1 through 12 or REMARK 3 resid 14 through 23 or (resid 24 through REMARK 3 25 and (name N or name CA or name C or REMARK 3 name O or name CB )) or resid 26 through REMARK 3 53 or resid 55 through 78 or resid 80 REMARK 3 through 101 or (resid 102 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 103 through 120 or (resid 121 REMARK 3 through 122 and (name N or name CA or REMARK 3 name C or name O or name CB )) or resid REMARK 3 123 through 124 or (resid 125 and (name N REMARK 3 or name CA or name C or name O or name CB REMARK 3 )) or resid 126 through 145 or (resid 146 REMARK 3 and (name N or name CA or name C or name REMARK 3 O or name CB )) or resid 147 through 152 REMARK 3 or (resid 153 and (name N or name CA or REMARK 3 name C or name O or name CB )) or resid REMARK 3 154 through 181 or (resid 182 through 183 REMARK 3 and (name N or name CA or name C or name REMARK 3 O or name CB )) or resid 184 through 193 REMARK 3 or (resid 194 and (name N or name CA or REMARK 3 name C or name O or name CB )) or resid REMARK 3 195 through 211 or (resid 212 and (name N REMARK 3 or name CA or name C or name O or name CB REMARK 3 )))) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "L2" and (resid 1 through 12 or REMARK 3 resid 14 through 53 or resid 55 through REMARK 3 78 or resid 80 through 101 or (resid 102 REMARK 3 and (name N or name CA or name C or name REMARK 3 O or name CB )) or resid 103 through 120 REMARK 3 or (resid 121 through 122 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 123 through 124 or (resid 125 REMARK 3 and (name N or name CA or name C or name REMARK 3 O or name CB )) or resid 126 through 145 REMARK 3 or (resid 146 and (name N or name CA or REMARK 3 name C or name O or name CB )) or resid REMARK 3 147 or (resid 148 and (name N or name CA REMARK 3 or name C or name O or name CB )) or REMARK 3 resid 149 through 152 or (resid 153 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 154 through 181 or REMARK 3 (resid 182 through 183 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 184 through 186 or (resid 187 REMARK 3 and (name N or name CA or name C or name REMARK 3 O or name CB )) or resid 188 or (resid REMARK 3 189 and (name N or name CA or name C or REMARK 3 name O or name CB )) or resid 190 through REMARK 3 193 or (resid 194 and (name N or name CA REMARK 3 or name C or name O or name CB )) or REMARK 3 resid 195 through 211 or (resid 212 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )))) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "L3" and (resid 1 through 12 or REMARK 3 resid 14 through 23 or (resid 24 through REMARK 3 25 and (name N or name CA or name C or REMARK 3 name O or name CB )) or resid 26 through REMARK 3 53 or resid 55 through 78 or resid 80 REMARK 3 through 120 or (resid 121 through 122 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 123 through 186 or REMARK 3 (resid 187 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 188 REMARK 3 through 193 or (resid 194 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 195 through 212)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "L4" and ((resid 1 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 2 through 12 or resid 14 through REMARK 3 23 or (resid 24 through 25 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 26 through 53 or resid 55 REMARK 3 through 78 or resid 80 through 101 or REMARK 3 (resid 102 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 103 REMARK 3 through 120 or (resid 121 through 122 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 123 through 145 or REMARK 3 (resid 146 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 147 REMARK 3 through 152 or (resid 153 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 154 through 181 or (resid 182 REMARK 3 through 183 and (name N or name CA or REMARK 3 name C or name O or name CB )) or resid REMARK 3 184 through 193 or (resid 194 and (name N REMARK 3 or name CA or name C or name O or name CB REMARK 3 )) or resid 195 through 212)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 5 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "L5" and ((resid 1 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 2 through 12 or resid 14 through REMARK 3 23 or (resid 24 through 25 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 26 through 53 or resid 55 REMARK 3 through 78 or resid 80 through 121 or REMARK 3 (resid 122 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 123 REMARK 3 through 145 or (resid 146 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 147 through 181 or (resid 182 REMARK 3 through 183 and (name N or name CA or REMARK 3 name C or name O or name CB )) or resid REMARK 3 184 through 186 or (resid 187 and (name N REMARK 3 or name CA or name C or name O or name CB REMARK 3 )) or resid 188 through 212)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 7T1W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000261517. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-OCT-19 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 21-ID-F REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 102834 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.450 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 200 DATA REDUNDANCY : 3.223 REMARK 200 R MERGE (I) : 0.08800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.4900 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.51 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8 REMARK 200 DATA REDUNDANCY IN SHELL : 3.25 REMARK 200 R MERGE FOR SHELL (I) : 0.59300 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.030 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: HUMAN FAB STRUCTURES REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 59.30 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: OPTIMIZATION SCREEN AROUND REMARK 280 RIGAKUREAGENTS JCSG+ B12, CONDITION D5: 200MM POTASSIUM CITRATE, REMARK 280 18.6% (W/V) PEG 3350: HOSAA.20194.B.K13.PC00170 AT 19.5MG/ML + REMARK 280 1MMYB-8-099 / BSI110866 CRYO: 20% EG + 1MM COMPOUND: TRAY: REMARK 280 312856D5: PUCK: ZMT3-1, PH 8.0, VAPOR DIFFUSION, SITTING DROP REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 74.50500 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5 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: H, L, A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H2, L2, 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: H3, L3, 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: H4, L4, D 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: 5 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H5, L5, 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 SER H 136 REMARK 465 LYS H 137 REMARK 465 SER H 138 REMARK 465 THR H 139 REMARK 465 SER H 140 REMARK 465 GLY H 141 REMARK 465 SER H 223 REMARK 465 CYS H 224 REMARK 465 ASP H 225 REMARK 465 LYS H 226 REMARK 465 THR H 227 REMARK 465 HIS H 228 REMARK 465 LYS H 137 REMARK 465 SER H 138 REMARK 465 THR H 139 REMARK 465 SER H 140 REMARK 465 GLY H 141 REMARK 465 SER H 223 REMARK 465 CYS H 224 REMARK 465 ASP H 225 REMARK 465 LYS H 226 REMARK 465 THR H 227 REMARK 465 HIS H 228 REMARK 465 SER H 136 REMARK 465 LYS H 137 REMARK 465 SER H 138 REMARK 465 THR H 139 REMARK 465 SER H 140 REMARK 465 GLY H 141 REMARK 465 GLY H 142 REMARK 465 SER H 223 REMARK 465 CYS H 224 REMARK 465 ASP H 225 REMARK 465 LYS H 226 REMARK 465 THR H 227 REMARK 465 HIS H 228 REMARK 465 LYS H 137 REMARK 465 SER H 138 REMARK 465 THR H 139 REMARK 465 SER H 140 REMARK 465 GLY H 141 REMARK 465 SER H 223 REMARK 465 CYS H 224 REMARK 465 ASP H 225 REMARK 465 LYS H 226 REMARK 465 THR H 227 REMARK 465 HIS H 228 REMARK 465 CYS L 213 REMARK 465 LYS H 137 REMARK 465 SER H 138 REMARK 465 THR H 139 REMARK 465 SER H 140 REMARK 465 GLY H 141 REMARK 465 SER H 223 REMARK 465 CYS H 224 REMARK 465 ASP H 225 REMARK 465 LYS H 226 REMARK 465 THR H 227 REMARK 465 HIS H 228 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 GLN H 1 CG CD OE1 NE2 REMARK 470 LYS H 214 CG CD CE NZ REMARK 470 GLU L 1 CG CD OE1 OE2 REMARK 470 LYS L 144 CG CD CE NZ REMARK 470 LYS L 148 CG CD CE NZ REMARK 470 LYS L 168 CG CD CE NZ REMARK 470 LYS L 187 CG CD CE NZ REMARK 470 LYS L 189 CG CD CE NZ REMARK 470 CYS L 213 SG REMARK 470 GLN H 1 CG CD OE1 NE2 REMARK 470 LYS H 209 CG CD CE NZ REMARK 470 LYS H 214 CG CD CE NZ REMARK 470 ARG H 218 CG CD NE CZ NH1 NH2 REMARK 470 LYS H 222 CG CD CE NZ REMARK 470 GLU L 1 CG CD OE1 OE2 REMARK 470 ARG L 24 CG CD NE CZ NH1 NH2 REMARK 470 LYS L 144 CG CD CE NZ REMARK 470 LYS L 168 CG CD CE NZ REMARK 470 CYS L 213 SG REMARK 470 GLN H 1 CG CD OE1 NE2 REMARK 470 LYS H 43 CG CD CE NZ REMARK 470 LYS H 113 CG CD CE NZ REMARK 470 LEU H 167 CG CD1 CD2 REMARK 470 LEU H 178 CG CD1 CD2 REMARK 470 LEU H 183 CG CD1 CD2 REMARK 470 VAL H 192 CG1 CG2 REMARK 470 LEU H 197 CG CD1 CD2 REMARK 470 GLN H 200 CG CD OE1 NE2 REMARK 470 ASN H 207 CG OD1 ND2 REMARK 470 LYS H 209 CG CD CE NZ REMARK 470 ASN H 212 CG OD1 ND2 REMARK 470 LYS H 214 CG CD CE NZ REMARK 470 LYS H 217 CG CD CE NZ REMARK 470 ARG H 218 CG CD NE CZ NH1 NH2 REMARK 470 GLU H 220 CG CD OE1 OE2 REMARK 470 LYS H 222 CG CD CE NZ REMARK 470 GLU L 1 CG CD OE1 OE2 REMARK 470 LYS L 102 CG CD CE NZ REMARK 470 GLU L 122 CG CD OE1 OE2 REMARK 470 LYS L 125 CG CD CE NZ REMARK 470 LYS L 144 CG CD CE NZ REMARK 470 GLN L 146 CG CD OE1 NE2 REMARK 470 LYS L 148 CG CD CE NZ REMARK 470 LEU L 153 CG CD1 CD2 REMARK 470 LYS L 168 CG CD CE NZ REMARK 470 LYS L 182 CG CD CE NZ REMARK 470 LYS L 189 CG CD CE NZ REMARK 470 GLU L 212 CG CD OE1 OE2 REMARK 470 CYS L 213 SG REMARK 470 GLN H 1 CG CD OE1 NE2 REMARK 470 LYS H 222 CG CD CE NZ REMARK 470 LYS L 125 CG CD CE NZ REMARK 470 LYS L 144 CG CD CE NZ REMARK 470 LYS L 148 CG CD CE NZ REMARK 470 LYS L 168 CG CD CE NZ REMARK 470 LYS L 187 CG CD CE NZ REMARK 470 LYS L 189 CG CD CE NZ REMARK 470 GLU L 212 CG CD OE1 OE2 REMARK 470 GLN H 1 CG CD OE1 NE2 REMARK 470 ARG H 13 CG CD NE CZ NH1 NH2 REMARK 470 LYS H 113 CG CD CE NZ REMARK 470 LYS H 125 CG CD CE NZ REMARK 470 LEU H 183 CG CD1 CD2 REMARK 470 VAL H 192 CG1 CG2 REMARK 470 GLN H 200 CG CD OE1 NE2 REMARK 470 LYS H 209 CG CD CE NZ REMARK 470 LYS H 217 CG CD CE NZ REMARK 470 ARG H 218 CG CD NE CZ NH1 NH2 REMARK 470 GLU H 220 CG CD OE1 OE2 REMARK 470 LYS H 222 CG CD CE NZ REMARK 470 LYS L 102 CG CD CE NZ REMARK 470 ASP L 121 CG OD1 OD2 REMARK 470 LYS L 125 CG CD CE NZ REMARK 470 LYS L 144 CG CD CE NZ REMARK 470 LYS L 148 CG CD CE NZ REMARK 470 LEU L 153 CG CD1 CD2 REMARK 470 LYS L 168 CG CD CE NZ REMARK 470 LYS L 189 CG CD CE NZ REMARK 470 GLU L 194 CG CD OE1 OE2 REMARK 470 GLU L 212 CG CD OE1 OE2 REMARK 470 CYS L 213 SG 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 C5 BXY C 1 C1 BXY C 2 1.96 REMARK 500 N GLNH5 1 O HOHH5 601 2.08 REMARK 500 OE1 GLNL3 159 O HOHL3 401 2.15 REMARK 500 N GLNH2 1 O HOHH2 601 2.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH H 698 O HOHL3 480 2454 2.16 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP H 99 -76.55 -116.59 REMARK 500 ARG H 102 -133.42 51.00 REMARK 500 LYS H 107 -72.37 -125.46 REMARK 500 ASP H 152 63.01 65.46 REMARK 500 ARG L 30 -121.62 54.41 REMARK 500 ALA L 51 -40.18 70.44 REMARK 500 TRP L 94 -141.26 54.37 REMARK 500 ASPH2 99 -75.95 -117.75 REMARK 500 ARGH2 102 -134.69 50.31 REMARK 500 ASPH2 104 -60.86 -92.90 REMARK 500 ASPH2 104 -62.64 -91.51 REMARK 500 LYSH2 107 -73.40 -125.04 REMARK 500 ASPH2 152 62.41 65.57 REMARK 500 ARGL2 30 -120.52 56.39 REMARK 500 ALAL2 51 -38.85 71.21 REMARK 500 TRPL2 94 -140.75 54.57 REMARK 500 ASPH3 99 -78.94 -117.49 REMARK 500 ARGH3 102 -131.93 49.28 REMARK 500 LYSH3 107 -74.27 -123.71 REMARK 500 ASPH3 152 62.62 62.55 REMARK 500 ARGL3 30 -120.04 55.11 REMARK 500 ALAL3 51 -40.42 71.29 REMARK 500 TRPL3 94 -141.56 53.97 REMARK 500 ASPH4 99 -80.25 -118.10 REMARK 500 ARGH4 102 -134.10 50.15 REMARK 500 LYSH4 107 -72.07 -123.16 REMARK 500 ASPH4 152 60.87 64.86 REMARK 500 ARGL4 30 -120.06 54.75 REMARK 500 ALAL4 51 -39.62 71.79 REMARK 500 TRPL4 94 -140.94 53.41 REMARK 500 ASPH5 99 -75.18 -116.38 REMARK 500 ARGH5 102 -133.59 49.45 REMARK 500 LYSH5 107 -74.77 -123.11 REMARK 500 ASPH5 152 65.25 63.54 REMARK 500 THRH5 199 -64.12 -101.63 REMARK 500 ARGL5 30 -118.64 55.79 REMARK 500 ALAL5 51 -41.37 71.23 REMARK 500 TRPL5 94 -141.46 55.92 REMARK 500 REMARK 500 REMARK: NULL DBREF 7T1W H 1 228 PDB 7T1W 7T1W 1 228 DBREF 7T1W L 1 213 PDB 7T1W 7T1W 1 213 DBREF 7T1WH2 1 228 PDB 7T1W 7T1W 1 228 DBREF 7T1WL2 1 213 PDB 7T1W 7T1W 1 213 DBREF 7T1WH3 1 228 PDB 7T1W 7T1W 1 228 DBREF 7T1WL3 1 213 PDB 7T1W 7T1W 1 213 DBREF 7T1WH4 1 228 PDB 7T1W 7T1W 1 228 DBREF 7T1WL4 1 213 PDB 7T1W 7T1W 1 213 DBREF 7T1WH5 1 228 PDB 7T1W 7T1W 1 228 DBREF 7T1WL5 1 213 PDB 7T1W 7T1W 1 213 SEQRES 1 H 228 GLN VAL GLN LEU LEU GLU SER GLY GLY GLY VAL VAL ARG SEQRES 2 H 228 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 228 PHE ASN PHE GLU ASP PHE GLY MET SER TRP VAL ARG GLN SEQRES 4 H 228 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER SER ILE SER SEQRES 5 H 228 TRP ASN GLY ALA ASN ILE GLY TYR VAL ASP SER VAL LYS SEQRES 6 H 228 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 H 228 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 228 ALA LEU TYR TYR CYS ALA ILE ASP TRP TYR ARG ASP ASP SEQRES 9 H 228 TYR TYR LYS MET ASP VAL TRP GLY LYS GLY THR THR VAL SEQRES 10 H 228 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 H 228 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 H 228 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 H 228 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 H 228 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 H 228 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 H 228 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 H 228 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 18 H 228 LYS SER CYS ASP LYS THR HIS SEQRES 1 L 213 GLU ILE VAL MET THR GLN SER PRO ALA THR LEU SER VAL SEQRES 2 L 213 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 213 ARG SER ILE ARG SER ALA LEU ALA TRP TYR GLN HIS LYS SEQRES 4 L 213 PRO GLY GLN ALA PRO ARG LEU LEU ILE PHE GLY ALA SER SEQRES 5 L 213 THR ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 L 213 GLY SER GLY THR ASP PHE THR LEU THR VAL SER SER ILE SEQRES 7 L 213 ARG SER GLU ASP SER ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8 L 213 ASP PHE TRP TYR THR PHE GLY GLN GLY THR LYS LEU GLU SEQRES 9 L 213 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10 L 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11 L 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12 L 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13 L 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14 L 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15 L 213 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16 L 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17 L 213 ASN ARG GLY GLU CYS SEQRES 1H2 228 GLN VAL GLN LEU LEU GLU SER GLY GLY GLY VAL VAL ARG SEQRES 2H2 228 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3H2 228 PHE ASN PHE GLU ASP PHE GLY MET SER TRP VAL ARG GLN SEQRES 4H2 228 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER SER ILE SER SEQRES 5H2 228 TRP ASN GLY ALA ASN ILE GLY TYR VAL ASP SER VAL LYS SEQRES 6H2 228 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7H2 228 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8H2 228 ALA LEU TYR TYR CYS ALA ILE ASP TRP TYR ARG ASP ASP SEQRES 9H2 228 TYR TYR LYS MET ASP VAL TRP GLY LYS GLY THR THR VAL SEQRES 10H2 228 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11H2 228 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12H2 228 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13H2 228 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14H2 228 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15H2 228 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16H2 228 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17H2 228 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 18H2 228 LYS SER CYS ASP LYS THR HIS SEQRES 1L2 213 GLU ILE VAL MET THR GLN SER PRO ALA THR LEU SER VAL SEQRES 2L2 213 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3L2 213 ARG SER ILE ARG SER ALA LEU ALA TRP TYR GLN HIS LYS SEQRES 4L2 213 PRO GLY GLN ALA PRO ARG LEU LEU ILE PHE GLY ALA SER SEQRES 5L2 213 THR ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6L2 213 GLY SER GLY THR ASP PHE THR LEU THR VAL SER SER ILE SEQRES 7L2 213 ARG SER GLU ASP SER ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8L2 213 ASP PHE TRP TYR THR PHE GLY GLN GLY THR LYS LEU GLU SEQRES 9L2 213 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10L2 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11L2 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12L2 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13L2 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14L2 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15L2 213 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16L2 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17L2 213 ASN ARG GLY GLU CYS SEQRES 1H3 228 GLN VAL GLN LEU LEU GLU SER GLY GLY GLY VAL VAL ARG SEQRES 2H3 228 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3H3 228 PHE ASN PHE GLU ASP PHE GLY MET SER TRP VAL ARG GLN SEQRES 4H3 228 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER SER ILE SER SEQRES 5H3 228 TRP ASN GLY ALA ASN ILE GLY TYR VAL ASP SER VAL LYS SEQRES 6H3 228 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7H3 228 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8H3 228 ALA LEU TYR TYR CYS ALA ILE ASP TRP TYR ARG ASP ASP SEQRES 9H3 228 TYR TYR LYS MET ASP VAL TRP GLY LYS GLY THR THR VAL SEQRES 10H3 228 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11H3 228 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12H3 228 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13H3 228 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14H3 228 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15H3 228 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16H3 228 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17H3 228 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 18H3 228 LYS SER CYS ASP LYS THR HIS SEQRES 1L3 213 GLU ILE VAL MET THR GLN SER PRO ALA THR LEU SER VAL SEQRES 2L3 213 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3L3 213 ARG SER ILE ARG SER ALA LEU ALA TRP TYR GLN HIS LYS SEQRES 4L3 213 PRO GLY GLN ALA PRO ARG LEU LEU ILE PHE GLY ALA SER SEQRES 5L3 213 THR ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6L3 213 GLY SER GLY THR ASP PHE THR LEU THR VAL SER SER ILE SEQRES 7L3 213 ARG SER GLU ASP SER ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8L3 213 ASP PHE TRP TYR THR PHE GLY GLN GLY THR LYS LEU GLU SEQRES 9L3 213 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10L3 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11L3 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12L3 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13L3 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14L3 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15L3 213 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16L3 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17L3 213 ASN ARG GLY GLU CYS SEQRES 1H4 228 GLN VAL GLN LEU LEU GLU SER GLY GLY GLY VAL VAL ARG SEQRES 2H4 228 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3H4 228 PHE ASN PHE GLU ASP PHE GLY MET SER TRP VAL ARG GLN SEQRES 4H4 228 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER SER ILE SER SEQRES 5H4 228 TRP ASN GLY ALA ASN ILE GLY TYR VAL ASP SER VAL LYS SEQRES 6H4 228 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7H4 228 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8H4 228 ALA LEU TYR TYR CYS ALA ILE ASP TRP TYR ARG ASP ASP SEQRES 9H4 228 TYR TYR LYS MET ASP VAL TRP GLY LYS GLY THR THR VAL SEQRES 10H4 228 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11H4 228 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12H4 228 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13H4 228 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14H4 228 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15H4 228 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16H4 228 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17H4 228 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 18H4 228 LYS SER CYS ASP LYS THR HIS SEQRES 1L4 213 GLU ILE VAL MET THR GLN SER PRO ALA THR LEU SER VAL SEQRES 2L4 213 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3L4 213 ARG SER ILE ARG SER ALA LEU ALA TRP TYR GLN HIS LYS SEQRES 4L4 213 PRO GLY GLN ALA PRO ARG LEU LEU ILE PHE GLY ALA SER SEQRES 5L4 213 THR ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6L4 213 GLY SER GLY THR ASP PHE THR LEU THR VAL SER SER ILE SEQRES 7L4 213 ARG SER GLU ASP SER ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8L4 213 ASP PHE TRP TYR THR PHE GLY GLN GLY THR LYS LEU GLU SEQRES 9L4 213 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10L4 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11L4 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12L4 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13L4 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14L4 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15L4 213 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16L4 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17L4 213 ASN ARG GLY GLU CYS SEQRES 1H5 228 GLN VAL GLN LEU LEU GLU SER GLY GLY GLY VAL VAL ARG SEQRES 2H5 228 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3H5 228 PHE ASN PHE GLU ASP PHE GLY MET SER TRP VAL ARG GLN SEQRES 4H5 228 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER SER ILE SER SEQRES 5H5 228 TRP ASN GLY ALA ASN ILE GLY TYR VAL ASP SER VAL LYS SEQRES 6H5 228 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7H5 228 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8H5 228 ALA LEU TYR TYR CYS ALA ILE ASP TRP TYR ARG ASP ASP SEQRES 9H5 228 TYR TYR LYS MET ASP VAL TRP GLY LYS GLY THR THR VAL SEQRES 10H5 228 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11H5 228 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12H5 228 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13H5 228 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14H5 228 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15H5 228 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16H5 228 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17H5 228 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 18H5 228 LYS SER CYS ASP LYS THR HIS SEQRES 1L5 213 GLU ILE VAL MET THR GLN SER PRO ALA THR LEU SER VAL SEQRES 2L5 213 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3L5 213 ARG SER ILE ARG SER ALA LEU ALA TRP TYR GLN HIS LYS SEQRES 4L5 213 PRO GLY GLN ALA PRO ARG LEU LEU ILE PHE GLY ALA SER SEQRES 5L5 213 THR ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6L5 213 GLY SER GLY THR ASP PHE THR LEU THR VAL SER SER ILE SEQRES 7L5 213 ARG SER GLU ASP SER ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8L5 213 ASP PHE TRP TYR THR PHE GLY GLN GLY THR LYS LEU GLU SEQRES 9L5 213 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10L5 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11L5 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12L5 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13L5 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14L5 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15L5 213 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16L5 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17L5 213 ASN ARG GLY GLU CYS HET EDO H 501 4 HET EDO H 502 8 HET EDO L 301 4 HET EDO H2 501 4 HET EDO H2 502 4 HET EDO H3 501 4 HET EDO H3 502 4 HET EDO L3 301 4 HET EDO L3 302 4 HET EDO H4 501 4 HET EDO H4 502 4 HET CIT L4 301 13 HET EDO L4 302 4 HET EDO H5 501 4 HET BXY A 1 10 HET BXY A 2 9 HET BXY A 3 9 HET BXX A 4 9 HET BXY B 1 10 HET BXY B 2 9 HET BXY B 3 9 HET BXX B 4 9 HET BXY C 1 10 HET BXY C 2 9 HET BXY C 3 9 HET BXX C 4 9 HET BXY D 1 19 HET BXY D 2 9 HET BXY D 3 9 HET BXX D 4 9 HET BXY E 1 10 HET BXY E 2 9 HET BXY E 3 9 HET BXX E 4 9 HETNAM EDO 1,2-ETHANEDIOL HETNAM CIT CITRIC ACID HETNAM BXY ALPHA-D-ARABINOFURANOSE HETNAM BXX BETA-D-ARABINOFURANOSE HETSYN EDO ETHYLENE GLYCOL FORMUL 11 EDO 13(C2 H6 O2) FORMUL 22 CIT C6 H8 O7 FORMUL 25 BXY 15(C5 H10 O5) FORMUL 25 BXX 5(C5 H10 O5) FORMUL 30 HOH *1131(H2 O) HELIX 1 AA1 ASN H 28 GLU H 30 5 3 HELIX 2 AA2 ASP H 62 LYS H 65 5 4 HELIX 3 AA3 ASN H 74 LYS H 76 5 3 HELIX 4 AA4 ARG H 87 THR H 91 5 5 HELIX 5 AA5 SER H 164 ALA H 166 5 3 HELIX 6 AA6 SER H 195 THR H 199 5 5 HELIX 7 AA7 LYS H 209 ASN H 212 5 4 HELIX 8 AA8 ARG L 79 SER L 83 5 5 HELIX 9 AA9 SER L 120 LYS L 125 1 6 HELIX 10 AB1 LYS L 182 HIS L 188 1 7 HELIX 11 AB2 ASNH2 28 GLUH2 30 5 3 HELIX 12 AB3 ASPH2 62 LYSH2 65 5 4 HELIX 13 AB4 ASNH2 74 LYSH2 76 5 3 HELIX 14 AB5 ARGH2 87 THRH2 91 5 5 HELIX 15 AB6 SERH2 164 ALAH2 166 5 3 HELIX 16 AB7 SERH2 195 GLYH2 198 5 4 HELIX 17 AB8 LYSH2 209 ASNH2 212 5 4 HELIX 18 AB9 ARGL2 79 SERL2 83 5 5 HELIX 19 AC1 SERL2 120 SERL2 126 1 7 HELIX 20 AC2 LYSL2 182 LYSL2 187 1 6 HELIX 21 AC3 ASNH3 28 GLUH3 30 5 3 HELIX 22 AC4 ASPH3 62 LYSH3 65 5 4 HELIX 23 AC5 ASNH3 74 LYSH3 76 5 3 HELIX 24 AC6 ARGH3 87 THRH3 91 5 5 HELIX 25 AC7 PROH3 193 GLYH3 198 5 6 HELIX 26 AC8 LYSH3 209 ASNH3 212 5 4 HELIX 27 AC9 ARGL3 79 SERL3 83 5 5 HELIX 28 AD1 SERL3 120 LYSL3 125 1 6 HELIX 29 AD2 LYSL3 182 GLUL3 186 1 5 HELIX 30 AD3 ASNH4 28 GLUH4 30 5 3 HELIX 31 AD4 ASPH4 62 LYSH4 65 5 4 HELIX 32 AD5 ASNH4 74 LYSH4 76 5 3 HELIX 33 AD6 ARGH4 87 THRH4 91 5 5 HELIX 34 AD7 SERH4 164 ALAH4 166 5 3 HELIX 35 AD8 SERH4 195 THRH4 199 5 5 HELIX 36 AD9 LYSH4 209 ASNH4 212 5 4 HELIX 37 AE1 ARGL4 79 SERL4 83 5 5 HELIX 38 AE2 SERL4 120 SERL4 126 1 7 HELIX 39 AE3 LYSL4 182 HISL4 188 1 7 HELIX 40 AE4 ASNH5 28 GLUH5 30 5 3 HELIX 41 AE5 ASPH5 62 LYSH5 65 5 4 HELIX 42 AE6 ASNH5 74 LYSH5 76 5 3 HELIX 43 AE7 ARGH5 87 THRH5 91 5 5 HELIX 44 AE8 SERH5 164 ALAH5 166 5 3 HELIX 45 AE9 SERH5 195 GLYH5 198 5 4 HELIX 46 AF1 LYSH5 209 ASNH5 212 5 4 HELIX 47 AF2 ARGL5 79 SERL5 83 5 5 HELIX 48 AF3 SERL5 120 SERL5 126 1 7 HELIX 49 AF4 LYSL5 182 GLUL5 186 1 5 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O SER H 21 N SER H 7 SHEET 3 AA1 4 SER H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 AA1 4 PHE H 68 ASP H 73 -1 N SER H 71 O TYR H 80 SHEET 1 AA2 6 GLY H 10 VAL H 12 0 SHEET 2 AA2 6 THR H 115 VAL H 119 1 O THR H 118 N GLY H 10 SHEET 3 AA2 6 ALA H 92 TYR H 101 -1 N TYR H 94 O THR H 115 SHEET 4 AA2 6 PHE H 32 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O VAL H 48 N TRP H 36 SHEET 6 AA2 6 ILE H 58 TYR H 60 -1 O GLY H 59 N SER H 50 SHEET 1 AA3 4 GLY H 10 VAL H 12 0 SHEET 2 AA3 4 THR H 115 VAL H 119 1 O THR H 118 N GLY H 10 SHEET 3 AA3 4 ALA H 92 TYR H 101 -1 N TYR H 94 O THR H 115 SHEET 4 AA3 4 TYR H 105 TYR H 106 -1 O TYR H 105 N TYR H 101 SHEET 1 AA4 4 SER H 128 LEU H 132 0 SHEET 2 AA4 4 THR H 143 TYR H 153 -1 O LEU H 149 N PHE H 130 SHEET 3 AA4 4 TYR H 184 PRO H 193 -1 O TYR H 184 N TYR H 153 SHEET 4 AA4 4 VAL H 171 THR H 173 -1 N HIS H 172 O VAL H 189 SHEET 1 AA5 4 SER H 128 LEU H 132 0 SHEET 2 AA5 4 THR H 143 TYR H 153 -1 O LEU H 149 N PHE H 130 SHEET 3 AA5 4 TYR H 184 PRO H 193 -1 O TYR H 184 N TYR H 153 SHEET 4 AA5 4 VAL H 177 LEU H 178 -1 N VAL H 177 O SER H 185 SHEET 1 AA6 3 THR H 159 TRP H 162 0 SHEET 2 AA6 3 ILE H 203 HIS H 208 -1 O ASN H 205 N SER H 161 SHEET 3 AA6 3 THR H 213 ARG H 218 -1 O VAL H 215 N VAL H 206 SHEET 1 AA7 4 MET L 4 SER L 7 0 SHEET 2 AA7 4 ALA L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA7 4 ASP L 70 VAL L 75 -1 O LEU L 73 N LEU L 21 SHEET 4 AA7 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AA8 6 THR L 10 VAL L 13 0 SHEET 2 AA8 6 THR L 101 ILE L 105 1 O GLU L 104 N LEU L 11 SHEET 3 AA8 6 ALA L 84 GLN L 90 -1 N ALA L 84 O LEU L 103 SHEET 4 AA8 6 LEU L 33 HIS L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AA8 6 ARG L 45 PHE L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA8 6 THR L 53 ARG L 54 -1 O THR L 53 N PHE L 49 SHEET 1 AA9 4 THR L 10 VAL L 13 0 SHEET 2 AA9 4 THR L 101 ILE L 105 1 O GLU L 104 N LEU L 11 SHEET 3 AA9 4 ALA L 84 GLN L 90 -1 N ALA L 84 O LEU L 103 SHEET 4 AA9 4 THR L 96 PHE L 97 -1 O THR L 96 N GLN L 90 SHEET 1 AB1 4 SER L 113 PHE L 117 0 SHEET 2 AB1 4 THR L 128 PHE L 138 -1 O LEU L 134 N PHE L 115 SHEET 3 AB1 4 TYR L 172 SER L 181 -1 O LEU L 178 N VAL L 131 SHEET 4 AB1 4 SER L 158 VAL L 162 -1 N GLN L 159 O THR L 177 SHEET 1 AB2 4 ALA L 152 LEU L 153 0 SHEET 2 AB2 4 LYS L 144 VAL L 149 -1 N VAL L 149 O ALA L 152 SHEET 3 AB2 4 VAL L 190 THR L 196 -1 O GLU L 194 N GLN L 146 SHEET 4 AB2 4 VAL L 204 ASN L 209 -1 O VAL L 204 N VAL L 195 SHEET 1 AB3 4 GLNH2 3 SERH2 7 0 SHEET 2 AB3 4 LEUH2 18 SERH2 25 -1 O ALAH2 23 N LEUH2 5 SHEET 3 AB3 4 SERH2 78 METH2 83 -1 O METH2 83 N LEUH2 18 SHEET 4 AB3 4 PHEH2 68 ASPH2 73 -1 N THRH2 69 O GLNH2 82 SHEET 1 AB4 6 GLYH2 10 VALH2 12 0 SHEET 2 AB4 6 THRH2 115 VALH2 119 1 O THRH2 118 N GLYH2 10 SHEET 3 AB4 6 ALAH2 92 TYRH2 101 -1 N TYRH2 94 O THRH2 115 SHEET 4 AB4 6 PHEH2 32 GLNH2 39 -1 N VALH2 37 O TYRH2 95 SHEET 5 AB4 6 LEUH2 45 ILEH2 51 -1 O GLUH2 46 N ARGH2 38 SHEET 6 AB4 6 ILEH2 58 TYRH2 60 -1 O GLYH2 59 N SERH2 50 SHEET 1 AB5 4 GLYH2 10 VALH2 12 0 SHEET 2 AB5 4 THRH2 115 VALH2 119 1 O THRH2 118 N GLYH2 10 SHEET 3 AB5 4 ALAH2 92 TYRH2 101 -1 N TYRH2 94 O THRH2 115 SHEET 4 AB5 4 TYRH2 105 TYRH2 106 -1 O TYRH2 105 N TYRH2 101 SHEET 1 AB6 4 SERH2 128 LEUH2 132 0 SHEET 2 AB6 4 THRH2 143 TYRH2 153 -1 O LEUH2 149 N PHEH2 130 SHEET 3 AB6 4 TYRH2 184 PROH2 193 -1 O VALH2 192 N ALAH2 144 SHEET 4 AB6 4 VALH2 171 THRH2 173 -1 N HISH2 172 O VALH2 189 SHEET 1 AB7 4 SERH2 128 LEUH2 132 0 SHEET 2 AB7 4 THRH2 143 TYRH2 153 -1 O LEUH2 149 N PHEH2 130 SHEET 3 AB7 4 TYRH2 184 PROH2 193 -1 O VALH2 192 N ALAH2 144 SHEET 4 AB7 4 VALH2 177 LEUH2 178 -1 N VALH2 177 O SERH2 185 SHEET 1 AB8 3 THRH2 159 TRPH2 162 0 SHEET 2 AB8 3 ILEH2 203 HISH2 208 -1 O ASNH2 205 N SERH2 161 SHEET 3 AB8 3 THRH2 213 ARGH2 218 -1 O THRH2 213 N HISH2 208 SHEET 1 AB9 4 METL2 4 SERL2 7 0 SHEET 2 AB9 4 ALAL2 19 ALAL2 25 -1 O ARGL2 24 N THRL2 5 SHEET 3 AB9 4 ASPL2 70 VALL2 75 -1 O LEUL2 73 N LEUL2 21 SHEET 4 AB9 4 PHEL2 62 SERL2 67 -1 N SERL2 63 O THRL2 74 SHEET 1 AC1 6 THRL2 10 VALL2 13 0 SHEET 2 AC1 6 THRL2 101 ILEL2 105 1 O GLUL2 104 N LEUL2 11 SHEET 3 AC1 6 ALAL2 84 GLNL2 90 -1 N ALAL2 84 O LEUL2 103 SHEET 4 AC1 6 LEUL2 33 HISL2 38 -1 N TYRL2 36 O TYRL2 87 SHEET 5 AC1 6 ARGL2 45 PHEL2 49 -1 O LEUL2 47 N TRPL2 35 SHEET 6 AC1 6 THRL2 53 ARGL2 54 -1 O THRL2 53 N PHEL2 49 SHEET 1 AC2 4 THRL2 10 VALL2 13 0 SHEET 2 AC2 4 THRL2 101 ILEL2 105 1 O GLUL2 104 N LEUL2 11 SHEET 3 AC2 4 ALAL2 84 GLNL2 90 -1 N ALAL2 84 O LEUL2 103 SHEET 4 AC2 4 THRL2 96 PHEL2 97 -1 O THRL2 96 N GLNL2 90 SHEET 1 AC3 4 SERL2 113 PHEL2 117 0 SHEET 2 AC3 4 THRL2 128 PHEL2 138 -1 O LEUL2 134 N PHEL2 115 SHEET 3 AC3 4 TYRL2 172 SERL2 181 -1 O LEUL2 178 N VALL2 131 SHEET 4 AC3 4 SERL2 158 VALL2 162 -1 N GLNL2 159 O THRL2 177 SHEET 1 AC4 4 ALAL2 152 LEUL2 153 0 SHEET 2 AC4 4 LYSL2 144 VALL2 149 -1 N VALL2 149 O ALAL2 152 SHEET 3 AC4 4 VALL2 190 THRL2 196 -1 O GLUL2 194 N GLNL2 146 SHEET 4 AC4 4 VALL2 204 ASNL2 209 -1 O VALL2 204 N VALL2 195 SHEET 1 AC5 4 GLNH3 3 SERH3 7 0 SHEET 2 AC5 4 LEUH3 18 SERH3 25 -1 O ALAH3 23 N LEUH3 5 SHEET 3 AC5 4 SERH3 78 METH3 83 -1 O METH3 83 N LEUH3 18 SHEET 4 AC5 4 PHEH3 68 ASPH3 73 -1 N SERH3 71 O TYRH3 80 SHEET 1 AC6 6 GLYH3 10 VALH3 12 0 SHEET 2 AC6 6 THRH3 115 VALH3 119 1 O THRH3 118 N GLYH3 10 SHEET 3 AC6 6 ALAH3 92 TYRH3 101 -1 N TYRH3 94 O THRH3 115 SHEET 4 AC6 6 PHEH3 32 GLNH3 39 -1 N VALH3 37 O TYRH3 95 SHEET 5 AC6 6 LEUH3 45 ILEH3 51 -1 O VALH3 48 N TRPH3 36 SHEET 6 AC6 6 ILEH3 58 TYRH3 60 -1 O GLYH3 59 N SERH3 50 SHEET 1 AC7 4 GLYH3 10 VALH3 12 0 SHEET 2 AC7 4 THRH3 115 VALH3 119 1 O THRH3 118 N GLYH3 10 SHEET 3 AC7 4 ALAH3 92 TYRH3 101 -1 N TYRH3 94 O THRH3 115 SHEET 4 AC7 4 TYRH3 105 TYRH3 106 -1 O TYRH3 105 N TYRH3 101 SHEET 1 AC8 4 SERH3 128 LEUH3 132 0 SHEET 2 AC8 4 ALAH3 144 TYRH3 153 -1 O LEUH3 149 N PHEH3 130 SHEET 3 AC8 4 TYRH3 184 VALH3 192 -1 O TYRH3 184 N TYRH3 153 SHEET 4 AC8 4 VALH3 171 THRH3 173 -1 N HISH3 172 O VALH3 189 SHEET 1 AC9 4 SERH3 128 LEUH3 132 0 SHEET 2 AC9 4 ALAH3 144 TYRH3 153 -1 O LEUH3 149 N PHEH3 130 SHEET 3 AC9 4 TYRH3 184 VALH3 192 -1 O TYRH3 184 N TYRH3 153 SHEET 4 AC9 4 VALH3 177 LEUH3 178 -1 N VALH3 177 O SERH3 185 SHEET 1 AD1 3 THRH3 159 TRPH3 162 0 SHEET 2 AD1 3 ILEH3 203 HISH3 208 -1 O ASNH3 205 N SERH3 161 SHEET 3 AD1 3 THRH3 213 ARGH3 218 -1 O THRH3 213 N HISH3 208 SHEET 1 AD2 4 METL3 4 SERL3 7 0 SHEET 2 AD2 4 ALAL3 19 ALAL3 25 -1 O SERL3 22 N SERL3 7 SHEET 3 AD2 4 ASPL3 70 VALL3 75 -1 O LEUL3 73 N LEUL3 21 SHEET 4 AD2 4 PHEL3 62 SERL3 67 -1 N SERL3 63 O THRL3 74 SHEET 1 AD3 6 THRL3 10 VALL3 13 0 SHEET 2 AD3 6 THRL3 101 ILEL3 105 1 O GLUL3 104 N LEUL3 11 SHEET 3 AD3 6 ALAL3 84 GLNL3 90 -1 N ALAL3 84 O LEUL3 103 SHEET 4 AD3 6 LEUL3 33 HISL3 38 -1 N TYRL3 36 O TYRL3 87 SHEET 5 AD3 6 ARGL3 45 PHEL3 49 -1 O LEUL3 47 N TRPL3 35 SHEET 6 AD3 6 THRL3 53 ARGL3 54 -1 O THRL3 53 N PHEL3 49 SHEET 1 AD4 4 THRL3 10 VALL3 13 0 SHEET 2 AD4 4 THRL3 101 ILEL3 105 1 O GLUL3 104 N LEUL3 11 SHEET 3 AD4 4 ALAL3 84 GLNL3 90 -1 N ALAL3 84 O LEUL3 103 SHEET 4 AD4 4 THRL3 96 PHEL3 97 -1 O THRL3 96 N GLNL3 90 SHEET 1 AD5 4 SERL3 113 PHEL3 117 0 SHEET 2 AD5 4 THRL3 128 PHEL3 138 -1 O LEUL3 134 N PHEL3 115 SHEET 3 AD5 4 TYRL3 172 SERL3 181 -1 O LEUL3 174 N LEUL3 135 SHEET 4 AD5 4 SERL3 158 VALL3 162 -1 N GLNL3 159 O THRL3 177 SHEET 1 AD6 4 ALAL3 152 LEUL3 153 0 SHEET 2 AD6 4 LYSL3 144 VALL3 149 -1 N VALL3 149 O ALAL3 152 SHEET 3 AD6 4 VALL3 190 THRL3 196 -1 O ALAL3 192 N LYSL3 148 SHEET 4 AD6 4 VALL3 204 ASNL3 209 -1 O VALL3 204 N VALL3 195 SHEET 1 AD7 4 GLNH4 3 SERH4 7 0 SHEET 2 AD7 4 LEUH4 18 SERH4 25 -1 O SERH4 21 N SERH4 7 SHEET 3 AD7 4 SERH4 78 METH4 83 -1 O METH4 83 N LEUH4 18 SHEET 4 AD7 4 PHEH4 68 ASPH4 73 -1 N THRH4 69 O GLNH4 82 SHEET 1 AD8 6 GLYH4 10 VALH4 12 0 SHEET 2 AD8 6 THRH4 115 VALH4 119 1 O THRH4 118 N VALH4 12 SHEET 3 AD8 6 ALAH4 92 TYRH4 101 -1 N TYRH4 94 O THRH4 115 SHEET 4 AD8 6 PHEH4 32 GLNH4 39 -1 N VALH4 37 O TYRH4 95 SHEET 5 AD8 6 LEUH4 45 ILEH4 51 -1 O GLUH4 46 N ARGH4 38 SHEET 6 AD8 6 ILEH4 58 TYRH4 60 -1 O GLYH4 59 N SERH4 50 SHEET 1 AD9 4 GLYH4 10 VALH4 12 0 SHEET 2 AD9 4 THRH4 115 VALH4 119 1 O THRH4 118 N VALH4 12 SHEET 3 AD9 4 ALAH4 92 TYRH4 101 -1 N TYRH4 94 O THRH4 115 SHEET 4 AD9 4 TYRH4 105 TYRH4 106 -1 O TYRH4 105 N TYRH4 101 SHEET 1 AE1 4 SERH4 128 LEUH4 132 0 SHEET 2 AE1 4 THRH4 143 TYRH4 153 -1 O LEUH4 149 N PHEH4 130 SHEET 3 AE1 4 TYRH4 184 PROH4 193 -1 O LEUH4 186 N VALH4 150 SHEET 4 AE1 4 VALH4 171 THRH4 173 -1 N HISH4 172 O VALH4 189 SHEET 1 AE2 4 SERH4 128 LEUH4 132 0 SHEET 2 AE2 4 THRH4 143 TYRH4 153 -1 O LEUH4 149 N PHEH4 130 SHEET 3 AE2 4 TYRH4 184 PROH4 193 -1 O LEUH4 186 N VALH4 150 SHEET 4 AE2 4 VALH4 177 LEUH4 178 -1 N VALH4 177 O SERH4 185 SHEET 1 AE3 3 THRH4 159 TRPH4 162 0 SHEET 2 AE3 3 TYRH4 202 HISH4 208 -1 O ASNH4 205 N SERH4 161 SHEET 3 AE3 3 THRH4 213 VALH4 219 -1 O VALH4 215 N VALH4 206 SHEET 1 AE4 4 METL4 4 SERL4 7 0 SHEET 2 AE4 4 ALAL4 19 ALAL4 25 -1 O ARGL4 24 N THRL4 5 SHEET 3 AE4 4 ASPL4 70 VALL4 75 -1 O LEUL4 73 N LEUL4 21 SHEET 4 AE4 4 PHEL4 62 SERL4 67 -1 N SERL4 63 O THRL4 74 SHEET 1 AE5 6 THRL4 10 VALL4 13 0 SHEET 2 AE5 6 THRL4 101 ILEL4 105 1 O GLUL4 104 N LEUL4 11 SHEET 3 AE5 6 ALAL4 84 GLNL4 90 -1 N ALAL4 84 O LEUL4 103 SHEET 4 AE5 6 LEUL4 33 HISL4 38 -1 N ALAL4 34 O GLNL4 89 SHEET 5 AE5 6 ARGL4 45 PHEL4 49 -1 O LEUL4 47 N TRPL4 35 SHEET 6 AE5 6 THRL4 53 ARGL4 54 -1 O THRL4 53 N PHEL4 49 SHEET 1 AE6 4 THRL4 10 VALL4 13 0 SHEET 2 AE6 4 THRL4 101 ILEL4 105 1 O GLUL4 104 N LEUL4 11 SHEET 3 AE6 4 ALAL4 84 GLNL4 90 -1 N ALAL4 84 O LEUL4 103 SHEET 4 AE6 4 THRL4 96 PHEL4 97 -1 O THRL4 96 N GLNL4 90 SHEET 1 AE7 4 SERL4 113 PHEL4 117 0 SHEET 2 AE7 4 THRL4 128 PHEL4 138 -1 O LEUL4 134 N PHEL4 115 SHEET 3 AE7 4 TYRL4 172 SERL4 181 -1 O LEUL4 178 N VALL4 131 SHEET 4 AE7 4 SERL4 158 VALL4 162 -1 N GLNL4 159 O THRL4 177 SHEET 1 AE8 4 ALAL4 152 LEUL4 153 0 SHEET 2 AE8 4 LYSL4 144 VALL4 149 -1 N VALL4 149 O ALAL4 152 SHEET 3 AE8 4 VALL4 190 THRL4 196 -1 O ALAL4 192 N LYSL4 148 SHEET 4 AE8 4 VALL4 204 ASNL4 209 -1 O LYSL4 206 N CYSL4 193 SHEET 1 AE9 4 GLNH5 3 SERH5 7 0 SHEET 2 AE9 4 LEUH5 18 SERH5 25 -1 O SERH5 21 N SERH5 7 SHEET 3 AE9 4 SERH5 78 METH5 83 -1 O METH5 83 N LEUH5 18 SHEET 4 AE9 4 PHEH5 68 ASPH5 73 -1 N THRH5 69 O GLNH5 82 SHEET 1 AF1 6 GLYH5 10 VALH5 12 0 SHEET 2 AF1 6 THRH5 115 VALH5 119 1 O THRH5 118 N GLYH5 10 SHEET 3 AF1 6 ALAH5 92 TYRH5 101 -1 N TYRH5 94 O THRH5 115 SHEET 4 AF1 6 PHEH5 32 GLNH5 39 -1 N VALH5 37 O TYRH5 95 SHEET 5 AF1 6 LEUH5 45 ILEH5 51 -1 O VALH5 48 N TRPH5 36 SHEET 6 AF1 6 ILEH5 58 TYRH5 60 -1 O GLYH5 59 N SERH5 50 SHEET 1 AF2 4 GLYH5 10 VALH5 12 0 SHEET 2 AF2 4 THRH5 115 VALH5 119 1 O THRH5 118 N GLYH5 10 SHEET 3 AF2 4 ALAH5 92 TYRH5 101 -1 N TYRH5 94 O THRH5 115 SHEET 4 AF2 4 TYRH5 105 TYRH5 106 -1 O TYRH5 105 N TYRH5 101 SHEET 1 AF3 4 SERH5 128 LEUH5 132 0 SHEET 2 AF3 4 THRH5 143 TYRH5 153 -1 O GLYH5 147 N LEUH5 132 SHEET 3 AF3 4 TYRH5 184 PROH5 193 -1 O TYRH5 184 N TYRH5 153 SHEET 4 AF3 4 VALH5 171 THRH5 173 -1 N HISH5 172 O VALH5 189 SHEET 1 AF4 4 SERH5 128 LEUH5 132 0 SHEET 2 AF4 4 THRH5 143 TYRH5 153 -1 O GLYH5 147 N LEUH5 132 SHEET 3 AF4 4 TYRH5 184 PROH5 193 -1 O TYRH5 184 N TYRH5 153 SHEET 4 AF4 4 VALH5 177 LEUH5 178 -1 N VALH5 177 O SERH5 185 SHEET 1 AF5 3 THRH5 159 TRPH5 162 0 SHEET 2 AF5 3 ILEH5 203 HISH5 208 -1 O ASNH5 205 N SERH5 161 SHEET 3 AF5 3 THRH5 213 ARGH5 218 -1 O THRH5 213 N HISH5 208 SHEET 1 AF6 4 METL5 4 SERL5 7 0 SHEET 2 AF6 4 ALAL5 19 ALAL5 25 -1 O ARGL5 24 N THRL5 5 SHEET 3 AF6 4 ASPL5 70 VALL5 75 -1 O LEUL5 73 N LEUL5 21 SHEET 4 AF6 4 PHEL5 62 SERL5 67 -1 N SERL5 63 O THRL5 74 SHEET 1 AF7 6 THRL5 10 VALL5 13 0 SHEET 2 AF7 6 THRL5 101 ILEL5 105 1 O GLUL5 104 N LEUL5 11 SHEET 3 AF7 6 ALAL5 84 GLNL5 90 -1 N ALAL5 84 O LEUL5 103 SHEET 4 AF7 6 LEUL5 33 HISL5 38 -1 N TYRL5 36 O TYRL5 87 SHEET 5 AF7 6 ARGL5 45 PHEL5 49 -1 O LEUL5 47 N TRPL5 35 SHEET 6 AF7 6 THRL5 53 ARGL5 54 -1 O THRL5 53 N PHEL5 49 SHEET 1 AF8 4 THRL5 10 VALL5 13 0 SHEET 2 AF8 4 THRL5 101 ILEL5 105 1 O GLUL5 104 N LEUL5 11 SHEET 3 AF8 4 ALAL5 84 GLNL5 90 -1 N ALAL5 84 O LEUL5 103 SHEET 4 AF8 4 THRL5 96 PHEL5 97 -1 O THRL5 96 N GLNL5 90 SHEET 1 AF9 4 SERL5 113 PHEL5 117 0 SHEET 2 AF9 4 THRL5 128 PHEL5 138 -1 O LEUL5 134 N PHEL5 115 SHEET 3 AF9 4 TYRL5 172 SERL5 181 -1 O LEUL5 178 N VALL5 131 SHEET 4 AF9 4 SERL5 158 VALL5 162 -1 N SERL5 161 O SERL5 175 SHEET 1 AG1 4 ALAL5 152 LEUL5 153 0 SHEET 2 AG1 4 LYSL5 144 VALL5 149 -1 N VALL5 149 O ALAL5 152 SHEET 3 AG1 4 VALL5 190 THRL5 196 -1 O ALAL5 192 N LYSL5 148 SHEET 4 AG1 4 VALL5 204 ASNL5 209 -1 O VALL5 204 N VALL5 195 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 2 CYS H 148 CYS H 204 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.06 SSBOND 4 CYS L 133 CYS L 193 1555 1555 2.02 SSBOND 5 CYSH2 22 CYSH2 96 1555 1555 2.02 SSBOND 6 CYSH2 148 CYSH2 204 1555 1555 2.03 SSBOND 7 CYSL2 23 CYSL2 88 1555 1555 2.06 SSBOND 8 CYSL2 133 CYSL2 193 1555 1555 2.03 SSBOND 9 CYSH3 22 CYSH3 96 1555 1555 2.03 SSBOND 10 CYSH3 148 CYSH3 204 1555 1555 2.03 SSBOND 11 CYSL3 23 CYSL3 88 1555 1555 2.07 SSBOND 12 CYSL3 133 CYSL3 193 1555 1555 2.04 SSBOND 13 CYSH4 22 CYSH4 96 1555 1555 2.04 SSBOND 14 CYSH4 148 CYSH4 204 1555 1555 2.03 SSBOND 15 CYSL4 23 CYSL4 88 1555 1555 2.07 SSBOND 16 CYSL4 133 CYSL4 193 1555 1555 2.03 SSBOND 17 CYSH5 22 CYSH5 96 1555 1555 2.04 SSBOND 18 CYSH5 148 CYSH5 204 1555 1555 2.04 SSBOND 19 CYSL5 23 CYSL5 88 1555 1555 2.07 SSBOND 20 CYSL5 133 CYSL5 193 1555 1555 2.02 LINK O5 BXY A 1 C1 BXY A 2 1555 1555 1.44 LINK O5 BXY A 2 C1 BXY A 3 1555 1555 1.43 LINK O2 BXY A 3 C1 BXX A 4 1555 1555 1.43 LINK O5 BXY B 1 C1 BXY B 2 1555 1555 1.44 LINK O5 BXY B 2 C1 BXY B 3 1555 1555 1.43 LINK O2 BXY B 3 C1 BXX B 4 1555 1555 1.44 LINK O5 BXY C 1 C1 BXY C 2 1555 1555 1.43 LINK O5 BXY C 2 C1 BXY C 3 1555 1555 1.43 LINK O2 BXY C 3 C1 BXX C 4 1555 1555 1.44 LINK O5 BXY D 1 C1 BXY D 2 1555 1555 1.44 LINK O5 BXY D 2 C1 BXY D 3 1555 1555 1.42 LINK O2 BXY D 3 C1 BXX D 4 1555 1555 1.43 LINK O5 BXY E 1 C1 BXY E 2 1555 1555 1.43 LINK O5 BXY E 2 C1 BXY E 3 1555 1555 1.43 LINK O2 BXY E 3 C1 BXX E 4 1555 1555 1.44 CISPEP 1 PHE H 154 PRO H 155 0 -2.91 CISPEP 2 GLU H 156 PRO H 157 0 -0.49 CISPEP 3 SER L 7 PRO L 8 0 -4.50 CISPEP 4 TYR L 139 PRO L 140 0 2.92 CISPEP 5 PHEH2 154 PROH2 155 0 -2.41 CISPEP 6 GLUH2 156 PROH2 157 0 0.39 CISPEP 7 SERL2 7 PROL2 8 0 -4.79 CISPEP 8 TYRL2 139 PROL2 140 0 3.56 CISPEP 9 PHEH3 154 PROH3 155 0 -5.03 CISPEP 10 GLUH3 156 PROH3 157 0 3.00 CISPEP 11 SERL3 7 PROL3 8 0 -5.01 CISPEP 12 TYRL3 139 PROL3 140 0 2.96 CISPEP 13 PHEH4 154 PROH4 155 0 -3.14 CISPEP 14 GLUH4 156 PROH4 157 0 0.56 CISPEP 15 SERL4 7 PROL4 8 0 -4.57 CISPEP 16 TYRL4 139 PROL4 140 0 2.79 CISPEP 17 PHEH5 154 PROH5 155 0 -4.57 CISPEP 18 GLUH5 156 PROH5 157 0 0.65 CISPEP 19 SERL5 7 PROL5 8 0 -3.69 CISPEP 20 TYRL5 139 PROL5 140 0 3.14 CRYST1 85.620 149.010 114.530 90.00 99.51 90.00 P 1 21 1 10 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 0.011680 0.000000 0.001956 0.00000 SCALE2 0.000000 0.006711 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008853 0.00000 MTRIX1 1 0.538815 -0.761999 0.359216 -14.33628 1 MTRIX2 1 0.782260 0.294315 -0.549043 -16.54405 1 MTRIX3 1 0.312648 0.576832 0.754663 45.28816 1 MTRIX1 2 0.348922 -0.616053 -0.706209 -78.05159 1 MTRIX2 2 -0.546679 -0.745871 0.380550 -25.17523 1 MTRIX3 2 -0.761180 0.253288 -0.597035 -75.36112 1 MTRIX1 3 -0.421348 -0.437452 0.794419 -24.22292 1 MTRIX2 3 0.552163 -0.818641 -0.157931 26.30044 1 MTRIX3 3 0.719431 0.372105 0.586478 -4.48265 1 MTRIX1 4 0.448725 0.854674 0.261111 23.65576 1 MTRIX2 4 -0.874882 0.360525 0.323425 27.67836 1 MTRIX3 4 0.182285 -0.373570 0.909515 48.01745 1 MTRIX1 5 0.534771 -0.767583 0.353322 -14.71174 1 MTRIX2 5 0.782410 0.291873 -0.550132 -16.46919 1 MTRIX3 5 0.319147 0.570637 0.756650 45.46850 1 MTRIX1 6 0.311198 -0.610424 -0.728381 -78.93455 1 MTRIX2 6 -0.579754 -0.729241 0.363447 -26.65336 1 MTRIX3 6 -0.753022 0.309177 -0.580834 -74.68057 1 MTRIX1 7 -0.423285 -0.460697 0.780120 -24.98399 1 MTRIX2 7 0.489531 -0.840847 -0.230945 22.69000 1 MTRIX3 7 0.762358 0.284138 0.581444 -4.46420 1 MTRIX1 8 0.485176 0.825695 0.287805 25.27044 1 MTRIX2 8 -0.855649 0.380485 0.350851 28.77105 1 MTRIX3 8 0.180190 -0.416485 0.891107 47.12411 1