HEADER IMMUNE SYSTEM 14-SEP-23 8U70 TITLE CRYSTAL STRUCTURE OF MALARIA TRANSMISSION-BLOCKING ANTI-PFS48/45 TITLE 2 ANTIBODY RUPA-58. COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTIBODY RUPA-58 KAPPA CHAIN; COMPND 3 CHAIN: A, C, E, I, K, G; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ANTIBODY RUPA-58 HEAVY CHAIN; COMPND 7 CHAIN: B, D, F, J, L, H; 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_CELL_LINE: 293F; SOURCE 9 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1573; SOURCE 10 EXPRESSION_SYSTEM_TISSUE: EMBRYONIC KIDNEY; SOURCE 11 EXPRESSION_SYSTEM_CELL: EPITHELIAL; SOURCE 12 MOL_ID: 2; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_COMMON: HUMAN; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM_CELL_LINE: 239F; SOURCE 20 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1573; SOURCE 21 EXPRESSION_SYSTEM_TISSUE: EMBRYONIC KIDNEY; SOURCE 22 EXPRESSION_SYSTEM_CELL: EPITHELIAL KEYWDS PFS48/45, HUMAN TRANSMISSION-BLOCKING ANTIBODIES, MALARIA, IMMUNE KEYWDS 2 SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR S.HAILEMARIAM,D.IVANOCHKO,J.P.JULIEN REVDAT 1 18-SEP-24 8U70 0 JRNL AUTH I.KUCHARSKA,D.IVANOCHKO,S.HAILEMARIAM,M.R.INKLAAR,K.TEELEN, JRNL AUTH 2 R.STOTER,M.VAN DE VEGTE-BOLMER,G.J.VAN GEMERT,A.SEMESI, JRNL AUTH 3 B.MCLEOD,J.RUBINSTEIN,M.M.JORE,J.P.JULIEN JRNL TITL STRUCTURAL ELUCIDATION OF FULL-LENGTH PFS48/45 IN COMPLEX JRNL TITL 2 WITH POTENT MABS ISOLATED FROM A NATURALLY EXPOSED JRNL TITL 3 INDIVIDUAL. JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.09 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.09 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.46 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 51007 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.225 REMARK 3 R VALUE (WORKING SET) : 0.223 REMARK 3 FREE R VALUE : 0.263 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.530 REMARK 3 FREE R VALUE TEST SET COUNT : 1798 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 29.4600 - 7.2300 0.99 3764 129 0.1929 0.1974 REMARK 3 2 7.2300 - 5.7600 1.00 3784 139 0.2308 0.2445 REMARK 3 3 5.7500 - 5.0300 1.00 3807 150 0.1942 0.2378 REMARK 3 4 5.0300 - 4.5700 1.00 3783 138 0.1880 0.2350 REMARK 3 5 4.5700 - 4.2500 1.00 3824 135 0.1829 0.2392 REMARK 3 6 4.2500 - 4.0000 1.00 3763 136 0.2002 0.2550 REMARK 3 7 4.0000 - 3.8000 1.00 3780 146 0.2285 0.2481 REMARK 3 8 3.8000 - 3.6300 1.00 3778 133 0.2315 0.2714 REMARK 3 9 3.6300 - 3.4900 1.00 3820 138 0.2498 0.3073 REMARK 3 10 3.4900 - 3.3700 1.00 3762 148 0.2816 0.3610 REMARK 3 11 3.3700 - 3.2700 1.00 3850 134 0.3069 0.3871 REMARK 3 12 3.2700 - 3.1700 1.00 3755 136 0.3129 0.3774 REMARK 3 13 3.1700 - 3.0900 1.00 3739 136 0.3170 0.3530 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) : 0.470 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.660 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 51.70 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 20388 REMARK 3 ANGLE : 0.907 27720 REMARK 3 CHIRALITY : 0.056 3096 REMARK 3 PLANARITY : 0.007 3552 REMARK 3 DIHEDRAL : 14.350 7356 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 59 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.6930 24.6559 -8.3264 REMARK 3 T TENSOR REMARK 3 T11: 0.4748 T22: 0.4247 REMARK 3 T33: 0.2816 T12: 0.0368 REMARK 3 T13: -0.0377 T23: 0.0197 REMARK 3 L TENSOR REMARK 3 L11: 5.8239 L22: 2.1138 REMARK 3 L33: 4.4754 L12: 3.7400 REMARK 3 L13: 0.7989 L23: 2.1987 REMARK 3 S TENSOR REMARK 3 S11: 0.3480 S12: 0.1668 S13: 0.2077 REMARK 3 S21: 0.1215 S22: -0.5579 S23: 0.1771 REMARK 3 S31: -0.1949 S32: -0.0662 S33: 0.1554 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 19 THROUGH 38 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.8662 20.2810 -7.5144 REMARK 3 T TENSOR REMARK 3 T11: 0.5030 T22: 0.4182 REMARK 3 T33: 0.2985 T12: -0.0404 REMARK 3 T13: -0.0846 T23: 0.0094 REMARK 3 L TENSOR REMARK 3 L11: 4.5877 L22: 4.2050 REMARK 3 L33: 1.8717 L12: 1.7983 REMARK 3 L13: -1.5651 L23: -1.6329 REMARK 3 S TENSOR REMARK 3 S11: -0.4313 S12: 0.5196 S13: 0.0458 REMARK 3 S21: -0.8272 S22: 0.0812 S23: 0.0570 REMARK 3 S31: 0.0213 S32: -0.2083 S33: 0.1054 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 39 THROUGH 150 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.5175 27.9881 1.9196 REMARK 3 T TENSOR REMARK 3 T11: 0.4431 T22: 0.3937 REMARK 3 T33: 0.2956 T12: 0.0852 REMARK 3 T13: -0.0002 T23: 0.0362 REMARK 3 L TENSOR REMARK 3 L11: 3.2374 L22: 0.7751 REMARK 3 L33: 0.1858 L12: 1.1290 REMARK 3 L13: 0.1782 L23: 0.1982 REMARK 3 S TENSOR REMARK 3 S11: -0.0214 S12: -0.0344 S13: 0.0354 REMARK 3 S21: -0.0673 S22: -0.0775 S23: -0.0051 REMARK 3 S31: 0.1322 S32: 0.1331 S33: 0.0806 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 151 THROUGH 186 ) REMARK 3 ORIGIN FOR THE GROUP (A): 38.1333 26.3297 9.3455 REMARK 3 T TENSOR REMARK 3 T11: 0.4555 T22: 0.6027 REMARK 3 T33: 0.5890 T12: -0.0132 REMARK 3 T13: 0.0076 T23: 0.0912 REMARK 3 L TENSOR REMARK 3 L11: 6.2676 L22: 2.4420 REMARK 3 L33: 2.9746 L12: -1.8814 REMARK 3 L13: 2.7768 L23: -0.9439 REMARK 3 S TENSOR REMARK 3 S11: 0.0950 S12: 0.0322 S13: -0.5068 REMARK 3 S21: 0.3866 S22: -0.1578 S23: -0.1341 REMARK 3 S31: 0.2321 S32: 0.4993 S33: -0.1422 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 187 THROUGH 211 ) REMARK 3 ORIGIN FOR THE GROUP (A): 48.1149 30.9951 6.9950 REMARK 3 T TENSOR REMARK 3 T11: 0.3863 T22: 0.7463 REMARK 3 T33: 0.4390 T12: -0.0520 REMARK 3 T13: 0.0986 T23: 0.1376 REMARK 3 L TENSOR REMARK 3 L11: 6.0713 L22: 1.7892 REMARK 3 L33: 1.9877 L12: -1.8028 REMARK 3 L13: 2.7682 L23: -0.8916 REMARK 3 S TENSOR REMARK 3 S11: 0.2466 S12: 0.3714 S13: 0.6331 REMARK 3 S21: 0.2087 S22: -0.4914 S23: -0.4214 REMARK 3 S31: 0.3015 S32: 0.5539 S33: 0.2834 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.4597 75.6841 14.9914 REMARK 3 T TENSOR REMARK 3 T11: 0.5078 T22: 0.3650 REMARK 3 T33: 0.3926 T12: 0.0131 REMARK 3 T13: -0.0340 T23: 0.0252 REMARK 3 L TENSOR REMARK 3 L11: 2.8682 L22: 9.2659 REMARK 3 L33: 3.4394 L12: 0.1250 REMARK 3 L13: 2.7890 L23: 1.2866 REMARK 3 S TENSOR REMARK 3 S11: 0.1063 S12: -0.4010 S13: -0.4094 REMARK 3 S21: 0.8693 S22: -0.2142 S23: -0.1851 REMARK 3 S31: 0.1282 S32: -0.0269 S33: -0.0109 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 19 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): -23.4983 84.8347 11.7109 REMARK 3 T TENSOR REMARK 3 T11: 0.3464 T22: 0.4652 REMARK 3 T33: 0.3803 T12: -0.0992 REMARK 3 T13: 0.0251 T23: 0.0482 REMARK 3 L TENSOR REMARK 3 L11: 1.1118 L22: 5.7069 REMARK 3 L33: 3.0681 L12: -0.9112 REMARK 3 L13: 0.6643 L23: 1.1558 REMARK 3 S TENSOR REMARK 3 S11: -0.0560 S12: -0.1598 S13: -0.0817 REMARK 3 S21: 0.5140 S22: -0.2612 S23: 0.4403 REMARK 3 S31: 0.1039 S32: -0.0242 S33: 0.2497 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 76 THROUGH 90 ) REMARK 3 ORIGIN FOR THE GROUP (A): -26.5916 77.3236 8.8009 REMARK 3 T TENSOR REMARK 3 T11: 0.4196 T22: 0.5086 REMARK 3 T33: 0.3368 T12: 0.0506 REMARK 3 T13: -0.0184 T23: 0.0545 REMARK 3 L TENSOR REMARK 3 L11: 2.2894 L22: 7.6265 REMARK 3 L33: 2.4037 L12: 1.8980 REMARK 3 L13: -0.9430 L23: 1.5480 REMARK 3 S TENSOR REMARK 3 S11: 0.1321 S12: -0.0510 S13: 0.0008 REMARK 3 S21: 0.5930 S22: -0.3480 S23: 0.6607 REMARK 3 S31: 0.3227 S32: -0.5096 S33: 0.2188 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 91 THROUGH 128 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.3403 62.8331 1.1107 REMARK 3 T TENSOR REMARK 3 T11: 0.4265 T22: 0.4743 REMARK 3 T33: 0.3900 T12: -0.0342 REMARK 3 T13: 0.0096 T23: 0.0249 REMARK 3 L TENSOR REMARK 3 L11: 0.2858 L22: 5.0502 REMARK 3 L33: 1.7204 L12: 0.1949 REMARK 3 L13: 0.2827 L23: 2.6221 REMARK 3 S TENSOR REMARK 3 S11: 0.0455 S12: 0.1131 S13: -0.1045 REMARK 3 S21: 0.3760 S22: 0.0958 S23: 0.0908 REMARK 3 S31: 0.4476 S32: 0.0611 S33: -0.0771 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 129 THROUGH 150 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.8710 49.8026 2.0167 REMARK 3 T TENSOR REMARK 3 T11: 0.5958 T22: 0.5775 REMARK 3 T33: 0.6578 T12: 0.0113 REMARK 3 T13: 0.0099 T23: -0.0724 REMARK 3 L TENSOR REMARK 3 L11: 4.6120 L22: 3.4737 REMARK 3 L33: 2.5379 L12: -1.8062 REMARK 3 L13: -0.2087 L23: 2.8211 REMARK 3 S TENSOR REMARK 3 S11: -0.0557 S12: 0.0874 S13: -0.3553 REMARK 3 S21: 0.8394 S22: -0.0284 S23: -0.2568 REMARK 3 S31: 0.7340 S32: -0.2131 S33: -0.2261 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 151 THROUGH 172 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.5826 53.5291 1.4208 REMARK 3 T TENSOR REMARK 3 T11: 0.5178 T22: 0.4921 REMARK 3 T33: 0.5865 T12: -0.1301 REMARK 3 T13: -0.0455 T23: -0.1606 REMARK 3 L TENSOR REMARK 3 L11: 6.9046 L22: 6.4536 REMARK 3 L33: 3.8852 L12: -2.8468 REMARK 3 L13: 1.4052 L23: -2.2530 REMARK 3 S TENSOR REMARK 3 S11: 0.4145 S12: 0.6833 S13: -0.0743 REMARK 3 S21: -0.4726 S22: -0.3857 S23: 0.9927 REMARK 3 S31: 0.4898 S32: -0.0907 S33: 0.1280 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 173 THROUGH 186 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.5792 47.4293 -5.5875 REMARK 3 T TENSOR REMARK 3 T11: 0.2869 T22: 0.7600 REMARK 3 T33: 0.6635 T12: 0.0693 REMARK 3 T13: -0.0287 T23: -0.0850 REMARK 3 L TENSOR REMARK 3 L11: 1.2812 L22: 4.0860 REMARK 3 L33: 5.8797 L12: -0.4295 REMARK 3 L13: -1.9991 L23: 2.9970 REMARK 3 S TENSOR REMARK 3 S11: 0.3315 S12: -0.1226 S13: 0.0730 REMARK 3 S21: 0.1937 S22: 0.2668 S23: -1.3228 REMARK 3 S31: 0.0980 S32: 1.1747 S33: -0.5961 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 187 THROUGH 198 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.0434 39.7238 -0.6180 REMARK 3 T TENSOR REMARK 3 T11: 0.6956 T22: 0.6514 REMARK 3 T33: 0.4732 T12: 0.2129 REMARK 3 T13: 0.0337 T23: -0.0211 REMARK 3 L TENSOR REMARK 3 L11: 6.4021 L22: 7.5948 REMARK 3 L33: 6.5924 L12: -3.5968 REMARK 3 L13: -3.5061 L23: 3.9613 REMARK 3 S TENSOR REMARK 3 S11: -0.6142 S12: -0.7951 S13: -0.7647 REMARK 3 S21: 0.9286 S22: 0.8745 S23: -0.5205 REMARK 3 S31: 2.0087 S32: 0.9614 S33: 0.0147 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 199 THROUGH 211 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.5175 40.4064 3.6916 REMARK 3 T TENSOR REMARK 3 T11: 0.9633 T22: 0.5210 REMARK 3 T33: 0.6925 T12: 0.0010 REMARK 3 T13: 0.1155 T23: 0.1002 REMARK 3 L TENSOR REMARK 3 L11: 5.4508 L22: 6.1118 REMARK 3 L33: 8.0061 L12: -2.3457 REMARK 3 L13: -3.7047 L23: 3.3419 REMARK 3 S TENSOR REMARK 3 S11: -1.3010 S12: -0.2878 S13: -0.5060 REMARK 3 S21: 1.6016 S22: 0.3971 S23: 1.0265 REMARK 3 S31: 2.2136 S32: 0.5849 S33: 0.5887 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 1 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.9915 26.7975 62.4003 REMARK 3 T TENSOR REMARK 3 T11: 0.5861 T22: 0.5221 REMARK 3 T33: 0.4325 T12: 0.0144 REMARK 3 T13: 0.0213 T23: -0.0867 REMARK 3 L TENSOR REMARK 3 L11: 4.3040 L22: 2.9955 REMARK 3 L33: 2.0078 L12: -1.4267 REMARK 3 L13: -0.6292 L23: 0.5388 REMARK 3 S TENSOR REMARK 3 S11: 0.1523 S12: -0.2724 S13: 0.1889 REMARK 3 S21: -0.1403 S22: -0.8667 S23: 0.7403 REMARK 3 S31: -0.1408 S32: 0.9009 S33: 0.2009 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 19 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.6273 25.7845 59.0162 REMARK 3 T TENSOR REMARK 3 T11: 0.5030 T22: 0.4526 REMARK 3 T33: 0.3633 T12: -0.0337 REMARK 3 T13: -0.1079 T23: -0.0113 REMARK 3 L TENSOR REMARK 3 L11: 3.5087 L22: 3.4609 REMARK 3 L33: 1.2713 L12: -0.6380 REMARK 3 L13: -0.7215 L23: 0.2901 REMARK 3 S TENSOR REMARK 3 S11: -0.1891 S12: -0.3452 S13: 0.3205 REMARK 3 S21: 0.5218 S22: 0.0932 S23: -0.1091 REMARK 3 S31: -0.0764 S32: 0.1020 S33: 0.0437 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 76 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.2283 28.4367 56.9821 REMARK 3 T TENSOR REMARK 3 T11: 0.4716 T22: 0.3898 REMARK 3 T33: 0.3274 T12: 0.0357 REMARK 3 T13: -0.0472 T23: 0.0303 REMARK 3 L TENSOR REMARK 3 L11: 3.4673 L22: 3.7850 REMARK 3 L33: 1.6843 L12: -0.8963 REMARK 3 L13: -0.3099 L23: 1.4221 REMARK 3 S TENSOR REMARK 3 S11: -0.1792 S12: -0.3096 S13: 0.6377 REMARK 3 S21: -0.3323 S22: 0.2000 S23: 0.0723 REMARK 3 S31: -0.2686 S32: -0.0858 S33: 0.1642 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 114 THROUGH 150 ) REMARK 3 ORIGIN FOR THE GROUP (A): -36.8753 33.2515 46.2979 REMARK 3 T TENSOR REMARK 3 T11: 0.6154 T22: 0.3775 REMARK 3 T33: 0.8674 T12: -0.0245 REMARK 3 T13: -0.1048 T23: -0.0182 REMARK 3 L TENSOR REMARK 3 L11: 7.6799 L22: 0.2277 REMARK 3 L33: 1.7593 L12: 1.5026 REMARK 3 L13: 3.1661 L23: 0.4812 REMARK 3 S TENSOR REMARK 3 S11: -0.6617 S12: 0.4339 S13: 1.1524 REMARK 3 S21: -0.1267 S22: 0.0097 S23: 0.5964 REMARK 3 S31: -0.3015 S32: 0.4572 S33: 0.7670 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 151 THROUGH 186 ) REMARK 3 ORIGIN FOR THE GROUP (A): -33.8816 30.4041 48.0680 REMARK 3 T TENSOR REMARK 3 T11: 0.5697 T22: 0.4315 REMARK 3 T33: 0.5853 T12: 0.0212 REMARK 3 T13: -0.1192 T23: -0.0067 REMARK 3 L TENSOR REMARK 3 L11: 4.8020 L22: 3.4966 REMARK 3 L33: 2.8792 L12: 1.0859 REMARK 3 L13: 0.3722 L23: 1.4328 REMARK 3 S TENSOR REMARK 3 S11: -0.1727 S12: 0.0173 S13: 0.9257 REMARK 3 S21: -0.0511 S22: -0.2553 S23: 0.9919 REMARK 3 S31: -0.3296 S32: -0.2503 S33: 0.4190 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 187 THROUGH 197 ) REMARK 3 ORIGIN FOR THE GROUP (A): -46.9515 30.6461 48.9969 REMARK 3 T TENSOR REMARK 3 T11: 0.6054 T22: 0.6319 REMARK 3 T33: 0.7320 T12: 0.1132 REMARK 3 T13: -0.1591 T23: -0.1343 REMARK 3 L TENSOR REMARK 3 L11: 3.3445 L22: 1.7390 REMARK 3 L33: 0.0104 L12: 1.7583 REMARK 3 L13: -0.0440 L23: -0.0496 REMARK 3 S TENSOR REMARK 3 S11: -0.1131 S12: 0.7702 S13: 0.7027 REMARK 3 S21: 0.1723 S22: -0.0960 S23: 0.9259 REMARK 3 S31: -0.1803 S32: 0.0389 S33: 0.5339 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 198 THROUGH 211 ) REMARK 3 ORIGIN FOR THE GROUP (A): -40.7707 37.9876 54.9879 REMARK 3 T TENSOR REMARK 3 T11: 0.5086 T22: 0.6693 REMARK 3 T33: 1.0418 T12: 0.1381 REMARK 3 T13: -0.0811 T23: -0.0620 REMARK 3 L TENSOR REMARK 3 L11: 7.0126 L22: 2.5804 REMARK 3 L33: 0.9617 L12: 3.7684 REMARK 3 L13: 1.8147 L23: 1.4495 REMARK 3 S TENSOR REMARK 3 S11: -0.4908 S12: -0.5263 S13: 0.7844 REMARK 3 S21: -0.0380 S22: -0.3666 S23: 1.0798 REMARK 3 S31: 0.0874 S32: -0.2810 S33: 0.6806 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 1 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): -57.2312 41.1234 17.5326 REMARK 3 T TENSOR REMARK 3 T11: 0.2799 T22: 0.5690 REMARK 3 T33: 0.4694 T12: 0.0422 REMARK 3 T13: 0.1113 T23: 0.0233 REMARK 3 L TENSOR REMARK 3 L11: 2.1046 L22: 4.2561 REMARK 3 L33: 5.5349 L12: -1.0098 REMARK 3 L13: 1.3113 L23: -0.1148 REMARK 3 S TENSOR REMARK 3 S11: -0.0490 S12: 0.4059 S13: -0.4075 REMARK 3 S21: -0.1287 S22: -0.1502 S23: -0.2309 REMARK 3 S31: 0.0352 S32: 0.5473 S33: 0.1371 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 76 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): -56.5479 33.8767 20.1109 REMARK 3 T TENSOR REMARK 3 T11: 0.4079 T22: 0.4127 REMARK 3 T33: 0.3894 T12: -0.0038 REMARK 3 T13: 0.0699 T23: 0.0838 REMARK 3 L TENSOR REMARK 3 L11: 3.7701 L22: 5.9129 REMARK 3 L33: 3.8739 L12: -4.4167 REMARK 3 L13: -2.1596 L23: 2.1380 REMARK 3 S TENSOR REMARK 3 S11: -0.2532 S12: -0.1453 S13: -0.0203 REMARK 3 S21: 0.2797 S22: 0.1207 S23: -0.0754 REMARK 3 S31: 0.4995 S32: 0.1769 S33: 0.2158 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 114 THROUGH 211 ) REMARK 3 ORIGIN FOR THE GROUP (A): -61.4771 5.2761 27.6445 REMARK 3 T TENSOR REMARK 3 T11: 0.6211 T22: 0.5027 REMARK 3 T33: 0.4600 T12: -0.0039 REMARK 3 T13: -0.0146 T23: -0.0918 REMARK 3 L TENSOR REMARK 3 L11: 4.8759 L22: 4.7402 REMARK 3 L33: 6.2385 L12: 1.5533 REMARK 3 L13: -1.3354 L23: -3.2246 REMARK 3 S TENSOR REMARK 3 S11: -0.1099 S12: 0.6404 S13: -0.2410 REMARK 3 S21: -0.3668 S22: 0.2953 S23: 0.0545 REMARK 3 S31: 1.0096 S32: -0.2427 S33: -0.1427 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 1 THROUGH 25 ) REMARK 3 ORIGIN FOR THE GROUP (A): -56.8621 56.4653 -4.5938 REMARK 3 T TENSOR REMARK 3 T11: 0.4848 T22: 0.4855 REMARK 3 T33: 0.4096 T12: -0.1361 REMARK 3 T13: 0.0541 T23: 0.0127 REMARK 3 L TENSOR REMARK 3 L11: 2.0231 L22: 6.2464 REMARK 3 L33: 4.3443 L12: 1.1579 REMARK 3 L13: 0.8163 L23: -0.4504 REMARK 3 S TENSOR REMARK 3 S11: -0.2915 S12: 0.4074 S13: 0.4768 REMARK 3 S21: 0.5098 S22: 0.1318 S23: -0.1421 REMARK 3 S31: -0.0828 S32: 0.3612 S33: -0.1805 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 26 THROUGH 102 ) REMARK 3 ORIGIN FOR THE GROUP (A): -57.3671 48.8169 -10.4209 REMARK 3 T TENSOR REMARK 3 T11: 0.3348 T22: 0.3769 REMARK 3 T33: 0.4297 T12: -0.0404 REMARK 3 T13: -0.0039 T23: 0.0584 REMARK 3 L TENSOR REMARK 3 L11: 4.5133 L22: 3.9429 REMARK 3 L33: 7.5387 L12: 0.5393 REMARK 3 L13: 1.3133 L23: 1.2387 REMARK 3 S TENSOR REMARK 3 S11: 0.0193 S12: 0.2315 S13: -0.4704 REMARK 3 S21: -0.1968 S22: 0.0483 S23: -0.6843 REMARK 3 S31: 0.0651 S32: 0.5983 S33: -0.0355 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 103 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): -41.9543 66.4003 -11.8011 REMARK 3 T TENSOR REMARK 3 T11: 0.8281 T22: 0.9007 REMARK 3 T33: 1.0836 T12: -0.5460 REMARK 3 T13: -0.1063 T23: 0.5115 REMARK 3 L TENSOR REMARK 3 L11: 1.7751 L22: 0.4671 REMARK 3 L33: 1.6722 L12: 0.2697 REMARK 3 L13: -0.3802 L23: 0.7680 REMARK 3 S TENSOR REMARK 3 S11: -0.2699 S12: -0.1111 S13: 0.3526 REMARK 3 S21: 0.4940 S22: -0.2042 S23: -0.3837 REMARK 3 S31: -1.2490 S32: 0.6281 S33: 0.0095 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 114 THROUGH 211 ) REMARK 3 ORIGIN FOR THE GROUP (A): -43.6186 81.7135 -26.7723 REMARK 3 T TENSOR REMARK 3 T11: 0.7635 T22: 0.5480 REMARK 3 T33: 0.8553 T12: -0.2049 REMARK 3 T13: 0.0712 T23: 0.0632 REMARK 3 L TENSOR REMARK 3 L11: 2.8777 L22: 3.7783 REMARK 3 L33: 3.4563 L12: 0.0695 REMARK 3 L13: -0.3050 L23: -2.5276 REMARK 3 S TENSOR REMARK 3 S11: 0.1910 S12: 0.1377 S13: 0.5151 REMARK 3 S21: 0.8777 S22: -0.0840 S23: -0.1670 REMARK 3 S31: -1.0657 S32: 0.2796 S33: -0.0997 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 145 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.7253 16.5988 14.3648 REMARK 3 T TENSOR REMARK 3 T11: 0.3651 T22: 0.3543 REMARK 3 T33: 0.2621 T12: 0.0046 REMARK 3 T13: 0.0207 T23: 0.0525 REMARK 3 L TENSOR REMARK 3 L11: 4.0785 L22: 1.6912 REMARK 3 L33: 1.7332 L12: 1.3467 REMARK 3 L13: 1.2379 L23: 0.5067 REMARK 3 S TENSOR REMARK 3 S11: 0.0222 S12: 0.1706 S13: 0.1217 REMARK 3 S21: 0.0466 S22: -0.1000 S23: -0.0113 REMARK 3 S31: -0.1230 S32: 0.1294 S33: 0.0762 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 146 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.7431 30.9592 22.3552 REMARK 3 T TENSOR REMARK 3 T11: 0.5652 T22: 0.5074 REMARK 3 T33: 0.4560 T12: -0.0425 REMARK 3 T13: -0.1058 T23: -0.0095 REMARK 3 L TENSOR REMARK 3 L11: 2.9076 L22: 7.6462 REMARK 3 L33: 1.7492 L12: 2.4411 REMARK 3 L13: -0.5154 L23: 0.0425 REMARK 3 S TENSOR REMARK 3 S11: 0.2494 S12: -0.5926 S13: 0.4628 REMARK 3 S21: 0.9217 S22: -0.3332 S23: -0.1976 REMARK 3 S31: -0.1146 S32: 0.0476 S33: 0.0447 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.0407 80.6779 -13.5506 REMARK 3 T TENSOR REMARK 3 T11: 0.4481 T22: 0.3443 REMARK 3 T33: 0.5435 T12: -0.0378 REMARK 3 T13: 0.0010 T23: 0.0005 REMARK 3 L TENSOR REMARK 3 L11: 2.9999 L22: 3.8032 REMARK 3 L33: 2.3580 L12: -1.8902 REMARK 3 L13: -0.5817 L23: 1.5437 REMARK 3 S TENSOR REMARK 3 S11: 0.6093 S12: 0.1170 S13: -0.1503 REMARK 3 S21: -0.5083 S22: -0.0946 S23: 0.1264 REMARK 3 S31: -0.1675 S32: -0.0269 S33: -0.1214 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 18 THROUGH 59 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.0601 90.2870 -6.0833 REMARK 3 T TENSOR REMARK 3 T11: 0.3288 T22: 0.3767 REMARK 3 T33: 0.4311 T12: -0.0274 REMARK 3 T13: 0.0376 T23: 0.0476 REMARK 3 L TENSOR REMARK 3 L11: 2.7046 L22: 2.7809 REMARK 3 L33: 1.7211 L12: -0.9008 REMARK 3 L13: 0.8337 L23: 1.1705 REMARK 3 S TENSOR REMARK 3 S11: -0.0204 S12: -0.1606 S13: 0.0170 REMARK 3 S21: -0.3389 S22: 0.1683 S23: 0.0087 REMARK 3 S31: -0.1270 S32: -0.1283 S33: -0.1203 REMARK 3 TLS GROUP : 33 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 60 THROUGH 72 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.7960 90.3369 -7.0100 REMARK 3 T TENSOR REMARK 3 T11: 0.4705 T22: 0.5294 REMARK 3 T33: 0.5951 T12: -0.0601 REMARK 3 T13: 0.0114 T23: -0.0198 REMARK 3 L TENSOR REMARK 3 L11: 3.1899 L22: 3.5613 REMARK 3 L33: 1.3501 L12: -1.2772 REMARK 3 L13: 0.3031 L23: 0.5646 REMARK 3 S TENSOR REMARK 3 S11: 0.0375 S12: -0.2453 S13: 0.4942 REMARK 3 S21: -0.5809 S22: -0.1094 S23: -1.0249 REMARK 3 S31: -0.4786 S32: 0.1659 S33: -0.2163 REMARK 3 TLS GROUP : 34 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 73 THROUGH 87 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.0041 84.9681 -11.4408 REMARK 3 T TENSOR REMARK 3 T11: 0.3664 T22: 0.4213 REMARK 3 T33: 0.5521 T12: -0.1305 REMARK 3 T13: 0.0134 T23: 0.0453 REMARK 3 L TENSOR REMARK 3 L11: 3.1092 L22: 3.6338 REMARK 3 L33: 1.7128 L12: -1.7449 REMARK 3 L13: 0.3422 L23: 0.4522 REMARK 3 S TENSOR REMARK 3 S11: -0.0061 S12: 0.1973 S13: 0.2105 REMARK 3 S21: 0.1333 S22: -0.1843 S23: -0.4328 REMARK 3 S31: -0.0108 S32: 0.4267 S33: -0.1626 REMARK 3 TLS GROUP : 35 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 88 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.8982 84.3923 -4.8477 REMARK 3 T TENSOR REMARK 3 T11: 0.3713 T22: 0.4143 REMARK 3 T33: 0.4107 T12: -0.0448 REMARK 3 T13: -0.0023 T23: 0.0346 REMARK 3 L TENSOR REMARK 3 L11: 2.1956 L22: 2.5264 REMARK 3 L33: 1.5855 L12: -0.5317 REMARK 3 L13: -0.2817 L23: 0.4895 REMARK 3 S TENSOR REMARK 3 S11: -0.1180 S12: -0.1381 S13: 0.1498 REMARK 3 S21: 0.6027 S22: 0.1442 S23: 0.0206 REMARK 3 S31: 0.2216 S32: -0.0314 S33: -0.0547 REMARK 3 TLS GROUP : 36 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 120 THROUGH 145 ) REMARK 3 ORIGIN FOR THE GROUP (A): -21.8227 48.9761 -11.0207 REMARK 3 T TENSOR REMARK 3 T11: 0.5717 T22: 0.5420 REMARK 3 T33: 0.8097 T12: -0.1487 REMARK 3 T13: -0.1754 T23: -0.0023 REMARK 3 L TENSOR REMARK 3 L11: 1.8012 L22: 4.7724 REMARK 3 L33: 3.6130 L12: 0.1296 REMARK 3 L13: -0.0285 L23: 0.9944 REMARK 3 S TENSOR REMARK 3 S11: 0.1658 S12: -0.1079 S13: -0.4575 REMARK 3 S21: 0.0773 S22: -0.0801 S23: 1.0428 REMARK 3 S31: 0.9189 S32: -0.6168 S33: -0.0510 REMARK 3 TLS GROUP : 37 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 146 THROUGH 188 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.7210 58.4345 -11.2418 REMARK 3 T TENSOR REMARK 3 T11: 0.3330 T22: 0.4454 REMARK 3 T33: 0.6340 T12: -0.0660 REMARK 3 T13: -0.0514 T23: -0.0468 REMARK 3 L TENSOR REMARK 3 L11: 1.0741 L22: 4.9377 REMARK 3 L33: 4.6404 L12: 0.8358 REMARK 3 L13: -0.9278 L23: 0.5964 REMARK 3 S TENSOR REMARK 3 S11: 0.2431 S12: -0.3662 S13: -0.2494 REMARK 3 S21: -0.2885 S22: -0.1846 S23: 0.5484 REMARK 3 S31: 0.3802 S32: -0.5347 S33: -0.1557 REMARK 3 TLS GROUP : 38 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 189 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): -23.3473 55.4691 -20.7466 REMARK 3 T TENSOR REMARK 3 T11: 0.5596 T22: 0.5737 REMARK 3 T33: 0.6592 T12: -0.0631 REMARK 3 T13: -0.1903 T23: -0.0404 REMARK 3 L TENSOR REMARK 3 L11: 0.4113 L22: 4.5608 REMARK 3 L33: 3.6332 L12: 0.1828 REMARK 3 L13: -0.8079 L23: 0.4955 REMARK 3 S TENSOR REMARK 3 S11: -0.0482 S12: 0.3178 S13: 0.0827 REMARK 3 S21: -0.5713 S22: 0.2152 S23: 0.9172 REMARK 3 S31: 0.5051 S32: -0.4645 S33: -0.0947 REMARK 3 TLS GROUP : 39 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 1 THROUGH 111 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.4780 14.3398 40.6553 REMARK 3 T TENSOR REMARK 3 T11: 0.4626 T22: 0.3771 REMARK 3 T33: 0.2472 T12: -0.0048 REMARK 3 T13: -0.0197 T23: 0.0087 REMARK 3 L TENSOR REMARK 3 L11: 4.6460 L22: 2.6005 REMARK 3 L33: 1.0127 L12: 0.1522 REMARK 3 L13: 1.4911 L23: 0.1226 REMARK 3 S TENSOR REMARK 3 S11: 0.0596 S12: -0.0859 S13: -0.1236 REMARK 3 S21: -0.0840 S22: -0.0063 S23: -0.1185 REMARK 3 S31: -0.2325 S32: -0.1510 S33: -0.0182 REMARK 3 TLS GROUP : 40 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 112 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): -30.0284 35.0198 34.7221 REMARK 3 T TENSOR REMARK 3 T11: 0.7130 T22: 0.6160 REMARK 3 T33: 0.7761 T12: -0.0184 REMARK 3 T13: -0.0904 T23: 0.1797 REMARK 3 L TENSOR REMARK 3 L11: 4.6157 L22: 2.7870 REMARK 3 L33: 4.0964 L12: -0.8348 REMARK 3 L13: -0.0624 L23: 0.8466 REMARK 3 S TENSOR REMARK 3 S11: 0.0573 S12: 0.5731 S13: 0.8852 REMARK 3 S21: -0.8119 S22: -0.0773 S23: 0.4071 REMARK 3 S31: -1.0496 S32: -0.1791 S33: -0.0397 REMARK 3 TLS GROUP : 41 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -65.7982 37.0895 43.5193 REMARK 3 T TENSOR REMARK 3 T11: 0.4040 T22: 0.4043 REMARK 3 T33: 0.4131 T12: -0.0062 REMARK 3 T13: 0.0768 T23: 0.0165 REMARK 3 L TENSOR REMARK 3 L11: 1.4217 L22: 4.8938 REMARK 3 L33: 1.0842 L12: 0.5709 REMARK 3 L13: 0.6005 L23: -0.1595 REMARK 3 S TENSOR REMARK 3 S11: 0.1746 S12: -0.4407 S13: -0.2808 REMARK 3 S21: 0.4666 S22: -0.2157 S23: -0.4206 REMARK 3 S31: -0.3310 S32: -0.1154 S33: 0.0265 REMARK 3 TLS GROUP : 42 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 18 THROUGH 59 ) REMARK 3 ORIGIN FOR THE GROUP (A): -68.2984 46.2633 36.1427 REMARK 3 T TENSOR REMARK 3 T11: 0.2634 T22: 0.4545 REMARK 3 T33: 0.2780 T12: -0.0186 REMARK 3 T13: 0.0382 T23: 0.0073 REMARK 3 L TENSOR REMARK 3 L11: 2.6292 L22: 4.2483 REMARK 3 L33: 1.1268 L12: 0.7808 REMARK 3 L13: 0.1816 L23: -1.0067 REMARK 3 S TENSOR REMARK 3 S11: -0.0378 S12: 0.0224 S13: 0.1940 REMARK 3 S21: 0.0190 S22: 0.1655 S23: 0.2082 REMARK 3 S31: 0.1081 S32: -0.0400 S33: -0.0136 REMARK 3 TLS GROUP : 43 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 60 THROUGH 95 ) REMARK 3 ORIGIN FOR THE GROUP (A): -72.6371 41.5767 38.6071 REMARK 3 T TENSOR REMARK 3 T11: 0.4368 T22: 0.4186 REMARK 3 T33: 0.3675 T12: 0.0570 REMARK 3 T13: 0.0644 T23: -0.0496 REMARK 3 L TENSOR REMARK 3 L11: 1.7933 L22: 4.2139 REMARK 3 L33: -0.0085 L12: 0.7815 REMARK 3 L13: 0.0014 L23: -0.6430 REMARK 3 S TENSOR REMARK 3 S11: -0.0722 S12: 0.1026 S13: 0.1451 REMARK 3 S21: 0.0292 S22: 0.1785 S23: 0.3977 REMARK 3 S31: 0.1427 S32: 0.1658 S33: -0.0434 REMARK 3 TLS GROUP : 44 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 96 THROUGH 145 ) REMARK 3 ORIGIN FOR THE GROUP (A): -60.3392 24.9591 35.6469 REMARK 3 T TENSOR REMARK 3 T11: 0.3197 T22: 0.4846 REMARK 3 T33: 0.2282 T12: 0.0843 REMARK 3 T13: 0.0008 T23: -0.0033 REMARK 3 L TENSOR REMARK 3 L11: 1.4344 L22: 7.2915 REMARK 3 L33: 1.6700 L12: -0.5436 REMARK 3 L13: 0.5380 L23: -1.4177 REMARK 3 S TENSOR REMARK 3 S11: 0.0922 S12: 0.1285 S13: -0.2439 REMARK 3 S21: -0.3101 S22: -0.0605 S23: -0.2421 REMARK 3 S31: 0.2835 S32: 0.1419 S33: 0.0284 REMARK 3 TLS GROUP : 45 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 146 THROUGH 165 ) REMARK 3 ORIGIN FOR THE GROUP (A): -51.6309 14.9951 41.8229 REMARK 3 T TENSOR REMARK 3 T11: 0.6122 T22: 0.3975 REMARK 3 T33: 0.5147 T12: -0.0304 REMARK 3 T13: -0.1127 T23: -0.0541 REMARK 3 L TENSOR REMARK 3 L11: 2.9855 L22: 2.8263 REMARK 3 L33: 3.6790 L12: 2.5770 REMARK 3 L13: -1.1348 L23: 0.3143 REMARK 3 S TENSOR REMARK 3 S11: 0.0381 S12: 0.0870 S13: 0.0538 REMARK 3 S21: -0.3537 S22: 0.2585 S23: -0.2931 REMARK 3 S31: -0.1654 S32: 0.5847 S33: -0.2683 REMARK 3 TLS GROUP : 46 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 166 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): -55.0243 9.4777 42.6602 REMARK 3 T TENSOR REMARK 3 T11: 0.5147 T22: 0.3750 REMARK 3 T33: 0.4385 T12: 0.0568 REMARK 3 T13: -0.0008 T23: -0.0239 REMARK 3 L TENSOR REMARK 3 L11: 3.1388 L22: 3.0999 REMARK 3 L33: 3.8800 L12: 2.8191 REMARK 3 L13: -0.3942 L23: 0.1452 REMARK 3 S TENSOR REMARK 3 S11: 0.1907 S12: 0.0956 S13: -0.4016 REMARK 3 S21: 0.3855 S22: -0.0166 S23: -0.3360 REMARK 3 S31: 0.4302 S32: 0.1154 S33: -0.1053 REMARK 3 TLS GROUP : 47 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -64.8356 55.2117 -34.2180 REMARK 3 T TENSOR REMARK 3 T11: 0.4168 T22: 0.5086 REMARK 3 T33: 0.3934 T12: -0.1305 REMARK 3 T13: 0.0505 T23: -0.0802 REMARK 3 L TENSOR REMARK 3 L11: 2.1817 L22: 6.8123 REMARK 3 L33: 2.6736 L12: 0.5406 REMARK 3 L13: -0.9731 L23: -1.8225 REMARK 3 S TENSOR REMARK 3 S11: -0.1402 S12: 1.0007 S13: 0.6444 REMARK 3 S21: -0.4661 S22: 0.0797 S23: -0.9670 REMARK 3 S31: 0.6110 S32: -0.2218 S33: 0.0048 REMARK 3 TLS GROUP : 48 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 18 THROUGH 72 ) REMARK 3 ORIGIN FOR THE GROUP (A): -70.6371 47.2165 -27.0437 REMARK 3 T TENSOR REMARK 3 T11: 0.3105 T22: 0.3831 REMARK 3 T33: 0.2819 T12: -0.0179 REMARK 3 T13: -0.0518 T23: -0.0154 REMARK 3 L TENSOR REMARK 3 L11: 2.4266 L22: 5.6765 REMARK 3 L33: 1.6817 L12: 0.6699 REMARK 3 L13: -0.9811 L23: -2.1838 REMARK 3 S TENSOR REMARK 3 S11: 0.1022 S12: -0.0390 S13: 0.0419 REMARK 3 S21: 0.0273 S22: -0.0161 S23: 0.0657 REMARK 3 S31: -0.0608 S32: 0.2882 S33: -0.1425 REMARK 3 TLS GROUP : 49 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 73 THROUGH 87 ) REMARK 3 ORIGIN FOR THE GROUP (A): -72.0846 53.6003 -32.2129 REMARK 3 T TENSOR REMARK 3 T11: 0.3719 T22: 0.3201 REMARK 3 T33: 0.2819 T12: -0.1331 REMARK 3 T13: -0.0258 T23: 0.0395 REMARK 3 L TENSOR REMARK 3 L11: 3.2208 L22: 6.6388 REMARK 3 L33: 1.6475 L12: 0.1661 REMARK 3 L13: -0.1367 L23: -2.1038 REMARK 3 S TENSOR REMARK 3 S11: 0.0475 S12: -0.0087 S13: 0.2167 REMARK 3 S21: -0.1118 S22: 0.1787 S23: 0.3156 REMARK 3 S31: 0.1732 S32: 0.0027 S33: -0.2350 REMARK 3 TLS GROUP : 50 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 88 THROUGH 111 ) REMARK 3 ORIGIN FOR THE GROUP (A): -63.1345 45.9653 -23.0200 REMARK 3 T TENSOR REMARK 3 T11: 0.4353 T22: 0.4588 REMARK 3 T33: 0.3907 T12: 0.0159 REMARK 3 T13: -0.0718 T23: 0.0217 REMARK 3 L TENSOR REMARK 3 L11: 2.5659 L22: 2.5798 REMARK 3 L33: 0.3901 L12: 0.1885 REMARK 3 L13: -0.4694 L23: 0.7645 REMARK 3 S TENSOR REMARK 3 S11: -0.2475 S12: -0.2483 S13: -0.3196 REMARK 3 S21: 0.5403 S22: 0.1011 S23: -0.6007 REMARK 3 S31: 0.0809 S32: -0.0168 S33: 0.1593 REMARK 3 TLS GROUP : 51 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 112 THROUGH 145 ) REMARK 3 ORIGIN FOR THE GROUP (A): -46.8046 74.4664 -36.0553 REMARK 3 T TENSOR REMARK 3 T11: 0.5308 T22: 0.5514 REMARK 3 T33: 0.7483 T12: -0.0721 REMARK 3 T13: 0.1174 T23: 0.1319 REMARK 3 L TENSOR REMARK 3 L11: 1.3488 L22: 4.2937 REMARK 3 L33: 2.1068 L12: 0.9234 REMARK 3 L13: -2.1447 L23: -0.7200 REMARK 3 S TENSOR REMARK 3 S11: -0.4854 S12: -0.5141 S13: 0.4783 REMARK 3 S21: -0.2962 S22: 0.0772 S23: -0.7205 REMARK 3 S31: -0.2470 S32: 0.5191 S33: 0.0218 REMARK 3 TLS GROUP : 52 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 146 THROUGH 188 ) REMARK 3 ORIGIN FOR THE GROUP (A): -47.7814 68.4629 -33.4178 REMARK 3 T TENSOR REMARK 3 T11: 0.4032 T22: 0.4860 REMARK 3 T33: 0.5855 T12: 0.0086 REMARK 3 T13: 0.0982 T23: 0.1232 REMARK 3 L TENSOR REMARK 3 L11: 3.2307 L22: 6.1919 REMARK 3 L33: 4.2285 L12: 2.5039 REMARK 3 L13: -1.5315 L23: -0.4362 REMARK 3 S TENSOR REMARK 3 S11: 0.0800 S12: -0.1618 S13: 0.0750 REMARK 3 S21: -0.4549 S22: -0.0503 S23: -0.8593 REMARK 3 S31: 0.0641 S32: 0.4398 S33: -0.0019 REMARK 3 TLS GROUP : 53 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 189 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): -45.6237 67.2878 -43.3585 REMARK 3 T TENSOR REMARK 3 T11: 0.7290 T22: 0.6840 REMARK 3 T33: 0.5885 T12: -0.0862 REMARK 3 T13: 0.1399 T23: 0.1676 REMARK 3 L TENSOR REMARK 3 L11: 6.0908 L22: 6.2127 REMARK 3 L33: 3.9709 L12: 2.6775 REMARK 3 L13: -3.6672 L23: -1.2249 REMARK 3 S TENSOR REMARK 3 S11: 0.1257 S12: 0.1070 S13: -0.0076 REMARK 3 S21: -1.0706 S22: -0.3109 S23: -1.0302 REMARK 3 S31: 0.3125 S32: -0.0000 S33: 0.0659 REMARK 3 TLS GROUP : 54 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 1 THROUGH 38 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.6158 75.0299 5.5820 REMARK 3 T TENSOR REMARK 3 T11: 0.7201 T22: 0.6639 REMARK 3 T33: 0.5900 T12: 0.2392 REMARK 3 T13: -0.1443 T23: -0.1291 REMARK 3 L TENSOR REMARK 3 L11: 1.3522 L22: 6.3039 REMARK 3 L33: 4.9308 L12: 2.9039 REMARK 3 L13: 0.6065 L23: -0.3443 REMARK 3 S TENSOR REMARK 3 S11: 0.1367 S12: 0.4873 S13: -0.3083 REMARK 3 S21: -0.4434 S22: -0.0413 S23: 0.2821 REMARK 3 S31: 0.9108 S32: 0.3586 S33: -0.0672 REMARK 3 TLS GROUP : 55 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 39 THROUGH 150 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.5549 62.8214 14.6557 REMARK 3 T TENSOR REMARK 3 T11: 0.9717 T22: 0.7499 REMARK 3 T33: 0.9076 T12: 0.1255 REMARK 3 T13: -0.1739 T23: -0.2157 REMARK 3 L TENSOR REMARK 3 L11: 1.2169 L22: 4.6171 REMARK 3 L33: 1.3210 L12: 1.8806 REMARK 3 L13: -0.8810 L23: -1.9922 REMARK 3 S TENSOR REMARK 3 S11: -0.0332 S12: 0.2267 S13: -0.7136 REMARK 3 S21: -0.2876 S22: -0.2569 S23: -0.2693 REMARK 3 S31: 0.6010 S32: -0.0644 S33: 0.2818 REMARK 3 TLS GROUP : 56 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 151 THROUGH 197 ) REMARK 3 ORIGIN FOR THE GROUP (A): -4.1433 46.8109 21.3425 REMARK 3 T TENSOR REMARK 3 T11: 0.9580 T22: 0.7333 REMARK 3 T33: 1.2360 T12: -0.0116 REMARK 3 T13: -0.0442 T23: -0.1252 REMARK 3 L TENSOR REMARK 3 L11: 2.9834 L22: 2.2593 REMARK 3 L33: 3.0760 L12: 1.8672 REMARK 3 L13: -1.9467 L23: -1.3610 REMARK 3 S TENSOR REMARK 3 S11: -0.8624 S12: 0.7550 S13: -0.5189 REMARK 3 S21: -0.5139 S22: 0.6300 S23: 0.2178 REMARK 3 S31: 0.3005 S32: -0.7155 S33: 0.1230 REMARK 3 TLS GROUP : 57 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 198 THROUGH 211 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.0701 38.1397 15.1909 REMARK 3 T TENSOR REMARK 3 T11: 1.9961 T22: 0.5638 REMARK 3 T33: 1.1493 T12: -0.1543 REMARK 3 T13: -0.1960 T23: -0.0854 REMARK 3 L TENSOR REMARK 3 L11: 7.3612 L22: 2.6088 REMARK 3 L33: 3.7506 L12: 2.6791 REMARK 3 L13: -3.7348 L23: -1.8395 REMARK 3 S TENSOR REMARK 3 S11: -1.8980 S12: 2.1233 S13: -0.9039 REMARK 3 S21: -2.1864 S22: 1.8306 S23: -0.3685 REMARK 3 S31: 0.4595 S32: -1.0354 S33: 0.8847 REMARK 3 TLS GROUP : 58 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.1807 83.0378 27.4724 REMARK 3 T TENSOR REMARK 3 T11: 0.4089 T22: 0.3146 REMARK 3 T33: 0.4321 T12: 0.0621 REMARK 3 T13: -0.0591 T23: -0.0683 REMARK 3 L TENSOR REMARK 3 L11: 4.3970 L22: 2.5601 REMARK 3 L33: 3.0609 L12: -0.5661 REMARK 3 L13: 0.3296 L23: 0.3422 REMARK 3 S TENSOR REMARK 3 S11: 0.2395 S12: 0.2723 S13: -0.6196 REMARK 3 S21: 0.0235 S22: -0.0731 S23: 0.0203 REMARK 3 S31: 0.3953 S32: 0.1414 S33: -0.1578 REMARK 3 TLS GROUP : 59 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 120 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.9319 49.7397 34.1206 REMARK 3 T TENSOR REMARK 3 T11: 1.0621 T22: 0.6675 REMARK 3 T33: 1.8349 T12: -0.0199 REMARK 3 T13: -0.3821 T23: 0.1649 REMARK 3 L TENSOR REMARK 3 L11: 2.2337 L22: 0.4002 REMARK 3 L33: 2.1941 L12: 0.5599 REMARK 3 L13: -0.0341 L23: -1.0733 REMARK 3 S TENSOR REMARK 3 S11: 0.2356 S12: -0.2187 S13: -1.2875 REMARK 3 S21: -0.3024 S22: -0.1480 S23: 0.7316 REMARK 3 S31: 0.7302 S32: 0.2355 S33: -0.1535 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 8U70 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-SEP-23. REMARK 100 THE DEPOSITION ID IS D_1000277154. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 25-JUN-22 REMARK 200 TEMPERATURE (KELVIN) : 80 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.03320 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51007 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.090 REMARK 200 RESOLUTION RANGE LOW (A) : 29.460 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 9.500 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 3.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.09 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.20 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0 REMARK 200 DATA REDUNDANCY IN SHELL : 9.00 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.04 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM ACETATE, 30% PEG 8000, REMARK 280 0.1 M SODIUM CACODYLATE, 20% ETHYLENE GLYCOL, PH 6.5, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.51733 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 30.75867 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3580 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19530 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3440 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19720 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3430 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20020 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3470 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19840 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3470 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19380 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 6 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3540 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19930 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H 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 GLY A 212 REMARK 465 GLU A 213 REMARK 465 CYS A 214 REMARK 465 GLY C 212 REMARK 465 GLU C 213 REMARK 465 CYS C 214 REMARK 465 GLY E 212 REMARK 465 GLU E 213 REMARK 465 CYS E 214 REMARK 465 GLY I 212 REMARK 465 GLU I 213 REMARK 465 CYS I 214 REMARK 465 GLY K 212 REMARK 465 GLU K 213 REMARK 465 CYS K 214 REMARK 465 LYS B 214 REMARK 465 SER B 215 REMARK 465 CYS B 216 REMARK 465 LYS D 214 REMARK 465 SER D 215 REMARK 465 CYS D 216 REMARK 465 LYS F 214 REMARK 465 SER F 215 REMARK 465 CYS F 216 REMARK 465 LYS J 214 REMARK 465 SER J 215 REMARK 465 CYS J 216 REMARK 465 LYS L 214 REMARK 465 SER L 215 REMARK 465 CYS L 216 REMARK 465 GLY G 212 REMARK 465 GLU G 213 REMARK 465 CYS G 214 REMARK 465 LYS H 214 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER A 30 -70.17 -64.97 REMARK 500 ALA A 51 -9.67 69.12 REMARK 500 SER A 52 -5.71 -142.17 REMARK 500 SER C 30 -71.83 -78.01 REMARK 500 THR C 31 23.27 -141.15 REMARK 500 ALA C 51 -10.03 69.09 REMARK 500 SER C 52 -5.76 -142.45 REMARK 500 THR E 31 21.44 -143.18 REMARK 500 ALA E 51 -9.20 67.78 REMARK 500 SER E 52 -8.34 -141.65 REMARK 500 ASN E 138 64.54 60.02 REMARK 500 SER I 30 -71.63 -60.85 REMARK 500 THR I 31 22.12 -141.79 REMARK 500 ALA I 51 -9.81 68.91 REMARK 500 SER I 52 -5.93 -142.19 REMARK 500 ALA K 51 -8.68 69.51 REMARK 500 SER K 52 -5.37 -141.74 REMARK 500 SER B 127 -158.34 -146.64 REMARK 500 SER B 132 16.24 55.41 REMARK 500 ASP B 144 67.10 60.65 REMARK 500 CYS D 22 118.72 -161.31 REMARK 500 THR D 98 31.18 -90.78 REMARK 500 SER D 127 -157.07 -144.71 REMARK 500 LYS D 129 18.50 -140.29 REMARK 500 ASP D 144 67.54 60.24 REMARK 500 CYS F 22 117.65 -161.04 REMARK 500 SER F 132 15.36 56.32 REMARK 500 ASP F 144 67.18 61.53 REMARK 500 SER J 127 -158.27 -147.95 REMARK 500 SER J 132 25.55 -143.23 REMARK 500 ASP J 144 67.70 61.09 REMARK 500 SER L 127 -156.77 -149.77 REMARK 500 SER L 128 92.94 -69.69 REMARK 500 ASP L 144 67.05 60.88 REMARK 500 ILE G 2 55.75 -109.34 REMARK 500 ALA G 51 -8.36 67.95 REMARK 500 SER G 52 -8.39 -141.27 REMARK 500 ASN G 138 63.98 62.09 REMARK 500 CYS H 22 117.48 -160.50 REMARK 500 ASP H 144 69.49 60.41 REMARK 500 REMARK 500 REMARK: NULL DBREF 8U70 A 1 214 PDB 8U70 8U70 1 214 DBREF 8U70 C 1 214 PDB 8U70 8U70 1 214 DBREF 8U70 E 1 214 PDB 8U70 8U70 1 214 DBREF 8U70 I 1 214 PDB 8U70 8U70 1 214 DBREF 8U70 K 1 214 PDB 8U70 8U70 1 214 DBREF 8U70 B 1 216 PDB 8U70 8U70 1 216 DBREF 8U70 D 1 216 PDB 8U70 8U70 1 216 DBREF 8U70 F 1 216 PDB 8U70 8U70 1 216 DBREF 8U70 J 1 216 PDB 8U70 8U70 1 216 DBREF 8U70 L 1 216 PDB 8U70 8U70 1 216 DBREF 8U70 G 1 214 PDB 8U70 8U70 1 214 DBREF 8U70 H 1 216 PDB 8U70 8U70 1 216 SEQRES 1 A 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 A 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 A 214 GLN ILE ILE SER THR TYR LEU ASN TRP TYR GLN HIS LYS SEQRES 4 A 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE LYS SER ALA SER SEQRES 5 A 214 THR LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 A 214 GLY SER GLY THR ASP PHE THR LEU THR ILE THR SER LEU SEQRES 7 A 214 GLN PRO GLU ASP PHE ALA THR PHE TYR CYS GLN GLN SER SEQRES 8 A 214 TYR ARG ASP PRO ILE THR PHE GLY GLN GLY THR ARG LEU SEQRES 9 A 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 A 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 A 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 A 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 A 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 A 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 A 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 A 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 A 214 PHE ASN ARG GLY GLU CYS SEQRES 1 C 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 C 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 C 214 GLN ILE ILE SER THR TYR LEU ASN TRP TYR GLN HIS LYS SEQRES 4 C 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE LYS SER ALA SER SEQRES 5 C 214 THR LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 C 214 GLY SER GLY THR ASP PHE THR LEU THR ILE THR SER LEU SEQRES 7 C 214 GLN PRO GLU ASP PHE ALA THR PHE TYR CYS GLN GLN SER SEQRES 8 C 214 TYR ARG ASP PRO ILE THR PHE GLY GLN GLY THR ARG LEU SEQRES 9 C 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 C 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 C 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 C 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 C 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 C 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 C 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 C 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 C 214 PHE ASN ARG GLY GLU CYS SEQRES 1 E 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 E 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 E 214 GLN ILE ILE SER THR TYR LEU ASN TRP TYR GLN HIS LYS SEQRES 4 E 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE LYS SER ALA SER SEQRES 5 E 214 THR LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 E 214 GLY SER GLY THR ASP PHE THR LEU THR ILE THR SER LEU SEQRES 7 E 214 GLN PRO GLU ASP PHE ALA THR PHE TYR CYS GLN GLN SER SEQRES 8 E 214 TYR ARG ASP PRO ILE THR PHE GLY GLN GLY THR ARG LEU SEQRES 9 E 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 E 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 E 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 E 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 E 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 E 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 E 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 E 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 E 214 PHE ASN ARG GLY GLU CYS SEQRES 1 I 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 I 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 I 214 GLN ILE ILE SER THR TYR LEU ASN TRP TYR GLN HIS LYS SEQRES 4 I 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE LYS SER ALA SER SEQRES 5 I 214 THR LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 I 214 GLY SER GLY THR ASP PHE THR LEU THR ILE THR SER LEU SEQRES 7 I 214 GLN PRO GLU ASP PHE ALA THR PHE TYR CYS GLN GLN SER SEQRES 8 I 214 TYR ARG ASP PRO ILE THR PHE GLY GLN GLY THR ARG LEU SEQRES 9 I 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 I 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 I 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 I 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 I 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 I 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 I 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 I 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 I 214 PHE ASN ARG GLY GLU CYS SEQRES 1 K 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 K 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 K 214 GLN ILE ILE SER THR TYR LEU ASN TRP TYR GLN HIS LYS SEQRES 4 K 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE LYS SER ALA SER SEQRES 5 K 214 THR LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 K 214 GLY SER GLY THR ASP PHE THR LEU THR ILE THR SER LEU SEQRES 7 K 214 GLN PRO GLU ASP PHE ALA THR PHE TYR CYS GLN GLN SER SEQRES 8 K 214 TYR ARG ASP PRO ILE THR PHE GLY GLN GLY THR ARG LEU SEQRES 9 K 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 K 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 K 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 K 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 K 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 K 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 K 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 K 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 K 214 PHE ASN ARG GLY GLU CYS SEQRES 1 B 227 GLN VAL GLN LEU VAL GLN SER GLY PRO GLU ALA LYS LYS SEQRES 2 B 227 PRO GLY ALA SER VAL LYS VAL SER CYS GLN ALA SER GLY SEQRES 3 B 227 TYR PRO PHE SER GLY TYR TYR MET HIS TRP LEU ARG GLN SEQRES 4 B 227 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP MET ASN SEQRES 5 B 227 PRO ASN SER GLY GLY THR LYS TYR ALA GLN ARG PHE GLN SEQRES 6 B 227 GLY ARG VAL THR MET THR ARG ASP THR SER ILE SER THR SEQRES 7 B 227 ALA HIS MET GLU LEU ARG GLY LEU ARG SER ASP ASP THR SEQRES 8 B 227 ALA VAL TYR TYR CYS ALA ARG ASP TYR CYS THR GLY SER SEQRES 9 B 227 SER CYS TYR ARG THR ASP TYR ASP TYR TRP GLY GLN GLY SEQRES 10 B 227 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 B 227 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 B 227 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 B 227 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 B 227 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 B 227 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 B 227 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 B 227 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 18 B 227 VAL GLU PRO LYS SER CYS SEQRES 1 D 227 GLN VAL GLN LEU VAL GLN SER GLY PRO GLU ALA LYS LYS SEQRES 2 D 227 PRO GLY ALA SER VAL LYS VAL SER CYS GLN ALA SER GLY SEQRES 3 D 227 TYR PRO PHE SER GLY TYR TYR MET HIS TRP LEU ARG GLN SEQRES 4 D 227 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP MET ASN SEQRES 5 D 227 PRO ASN SER GLY GLY THR LYS TYR ALA GLN ARG PHE GLN SEQRES 6 D 227 GLY ARG VAL THR MET THR ARG ASP THR SER ILE SER THR SEQRES 7 D 227 ALA HIS MET GLU LEU ARG GLY LEU ARG SER ASP ASP THR SEQRES 8 D 227 ALA VAL TYR TYR CYS ALA ARG ASP TYR CYS THR GLY SER SEQRES 9 D 227 SER CYS TYR ARG THR ASP TYR ASP TYR TRP GLY GLN GLY SEQRES 10 D 227 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 D 227 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 D 227 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 D 227 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 D 227 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 D 227 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 D 227 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 D 227 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 18 D 227 VAL GLU PRO LYS SER CYS SEQRES 1 F 227 GLN VAL GLN LEU VAL GLN SER GLY PRO GLU ALA LYS LYS SEQRES 2 F 227 PRO GLY ALA SER VAL LYS VAL SER CYS GLN ALA SER GLY SEQRES 3 F 227 TYR PRO PHE SER GLY TYR TYR MET HIS TRP LEU ARG GLN SEQRES 4 F 227 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP MET ASN SEQRES 5 F 227 PRO ASN SER GLY GLY THR LYS TYR ALA GLN ARG PHE GLN SEQRES 6 F 227 GLY ARG VAL THR MET THR ARG ASP THR SER ILE SER THR SEQRES 7 F 227 ALA HIS MET GLU LEU ARG GLY LEU ARG SER ASP ASP THR SEQRES 8 F 227 ALA VAL TYR TYR CYS ALA ARG ASP TYR CYS THR GLY SER SEQRES 9 F 227 SER CYS TYR ARG THR ASP TYR ASP TYR TRP GLY GLN GLY SEQRES 10 F 227 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 F 227 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 F 227 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 F 227 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 F 227 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 F 227 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 F 227 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 F 227 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 18 F 227 VAL GLU PRO LYS SER CYS SEQRES 1 J 227 GLN VAL GLN LEU VAL GLN SER GLY PRO GLU ALA LYS LYS SEQRES 2 J 227 PRO GLY ALA SER VAL LYS VAL SER CYS GLN ALA SER GLY SEQRES 3 J 227 TYR PRO PHE SER GLY TYR TYR MET HIS TRP LEU ARG GLN SEQRES 4 J 227 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP MET ASN SEQRES 5 J 227 PRO ASN SER GLY GLY THR LYS TYR ALA GLN ARG PHE GLN SEQRES 6 J 227 GLY ARG VAL THR MET THR ARG ASP THR SER ILE SER THR SEQRES 7 J 227 ALA HIS MET GLU LEU ARG GLY LEU ARG SER ASP ASP THR SEQRES 8 J 227 ALA VAL TYR TYR CYS ALA ARG ASP TYR CYS THR GLY SER SEQRES 9 J 227 SER CYS TYR ARG THR ASP TYR ASP TYR TRP GLY GLN GLY SEQRES 10 J 227 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 J 227 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 J 227 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 J 227 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 J 227 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 J 227 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 J 227 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 J 227 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 18 J 227 VAL GLU PRO LYS SER CYS SEQRES 1 L 227 GLN VAL GLN LEU VAL GLN SER GLY PRO GLU ALA LYS LYS SEQRES 2 L 227 PRO GLY ALA SER VAL LYS VAL SER CYS GLN ALA SER GLY SEQRES 3 L 227 TYR PRO PHE SER GLY TYR TYR MET HIS TRP LEU ARG GLN SEQRES 4 L 227 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP MET ASN SEQRES 5 L 227 PRO ASN SER GLY GLY THR LYS TYR ALA GLN ARG PHE GLN SEQRES 6 L 227 GLY ARG VAL THR MET THR ARG ASP THR SER ILE SER THR SEQRES 7 L 227 ALA HIS MET GLU LEU ARG GLY LEU ARG SER ASP ASP THR SEQRES 8 L 227 ALA VAL TYR TYR CYS ALA ARG ASP TYR CYS THR GLY SER SEQRES 9 L 227 SER CYS TYR ARG THR ASP TYR ASP TYR TRP GLY GLN GLY SEQRES 10 L 227 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 L 227 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 L 227 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 L 227 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 L 227 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 L 227 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 L 227 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 L 227 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 18 L 227 VAL GLU PRO LYS SER CYS SEQRES 1 G 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 G 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 G 214 GLN ILE ILE SER THR TYR LEU ASN TRP TYR GLN HIS LYS SEQRES 4 G 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE LYS SER ALA SER SEQRES 5 G 214 THR LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 G 214 GLY SER GLY THR ASP PHE THR LEU THR ILE THR SER LEU SEQRES 7 G 214 GLN PRO GLU ASP PHE ALA THR PHE TYR CYS GLN GLN SER SEQRES 8 G 214 TYR ARG ASP PRO ILE THR PHE GLY GLN GLY THR ARG LEU SEQRES 9 G 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 G 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 G 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 G 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 G 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 G 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 G 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 G 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 G 214 PHE ASN ARG GLY GLU CYS SEQRES 1 H 227 GLN VAL GLN LEU VAL GLN SER GLY PRO GLU ALA LYS LYS SEQRES 2 H 227 PRO GLY ALA SER VAL LYS VAL SER CYS GLN ALA SER GLY SEQRES 3 H 227 TYR PRO PHE SER GLY TYR TYR MET HIS TRP LEU ARG GLN SEQRES 4 H 227 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP MET ASN SEQRES 5 H 227 PRO ASN SER GLY GLY THR LYS TYR ALA GLN ARG PHE GLN SEQRES 6 H 227 GLY ARG VAL THR MET THR ARG ASP THR SER ILE SER THR SEQRES 7 H 227 ALA HIS MET GLU LEU ARG GLY LEU ARG SER ASP ASP THR SEQRES 8 H 227 ALA VAL TYR TYR CYS ALA ARG ASP TYR CYS THR GLY SER SEQRES 9 H 227 SER CYS TYR ARG THR ASP TYR ASP TYR TRP GLY GLN GLY SEQRES 10 H 227 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 H 227 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 H 227 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 H 227 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 H 227 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 H 227 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 H 227 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 H 227 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 18 H 227 VAL GLU PRO LYS SER CYS HELIX 1 AA1 GLN A 79 PHE A 83 5 5 HELIX 2 AA2 SER A 121 LYS A 126 1 6 HELIX 3 AA3 LYS A 183 GLU A 187 1 5 HELIX 4 AA4 GLN C 79 PHE C 83 5 5 HELIX 5 AA5 SER C 121 LYS C 126 1 6 HELIX 6 AA6 LYS C 183 GLU C 187 1 5 HELIX 7 AA7 GLN E 79 PHE E 83 5 5 HELIX 8 AA8 SER E 121 SER E 127 1 7 HELIX 9 AA9 LYS E 183 GLU E 187 1 5 HELIX 10 AB1 GLN I 79 PHE I 83 5 5 HELIX 11 AB2 SER I 121 LYS I 126 1 6 HELIX 12 AB3 LYS I 183 GLU I 187 1 5 HELIX 13 AB4 GLN K 79 PHE K 83 5 5 HELIX 14 AB5 SER K 121 LYS K 126 1 6 HELIX 15 AB6 LYS K 183 GLU K 187 1 5 HELIX 16 AB7 ARG B 83 THR B 87 5 5 HELIX 17 AB8 CYS B 97 GLY B 99 5 3 HELIX 18 AB9 PRO B 185 LEU B 189 5 5 HELIX 19 AC1 ARG D 83 THR D 87 5 5 HELIX 20 AC2 CYS D 97 GLY D 99 5 3 HELIX 21 AC3 SER D 187 LEU D 189 5 3 HELIX 22 AC4 ARG F 83 THR F 87 5 5 HELIX 23 AC5 ARG J 83 THR J 87 5 5 HELIX 24 AC6 SER J 156 ALA J 158 5 3 HELIX 25 AC7 SER J 187 LEU J 189 5 3 HELIX 26 AC8 ARG L 83 THR L 87 5 5 HELIX 27 AC9 CYS L 97 GLY L 99 5 3 HELIX 28 AD1 SER L 187 LEU L 189 5 3 HELIX 29 AD2 GLN G 79 PHE G 83 5 5 HELIX 30 AD3 SER G 121 LYS G 126 1 6 HELIX 31 AD4 LYS G 183 GLU G 187 1 5 HELIX 32 AD5 ARG H 83 THR H 87 5 5 HELIX 33 AD6 CYS H 97 GLY H 99 5 3 SHEET 1 AA1 4 MET A 4 SER A 7 0 SHEET 2 AA1 4 VAL A 19 ALA A 25 -1 O ARG A 24 N THR A 5 SHEET 3 AA1 4 ASP A 70 ILE A 75 -1 O PHE A 71 N CYS A 23 SHEET 4 AA1 4 PHE A 62 SER A 67 -1 N SER A 63 O THR A 74 SHEET 1 AA2 2 SER A 10 ALA A 13 0 SHEET 2 AA2 2 ARG A 103 ILE A 106 1 O GLU A 105 N ALA A 13 SHEET 1 AA3 4 THR A 53 LEU A 54 0 SHEET 2 AA3 4 LYS A 45 LYS A 49 -1 N LYS A 49 O THR A 53 SHEET 3 AA3 4 LEU A 33 HIS A 38 -1 N GLN A 37 O LYS A 45 SHEET 4 AA3 4 THR A 85 GLN A 90 -1 O TYR A 87 N TYR A 36 SHEET 1 AA4 4 SER A 114 PHE A 118 0 SHEET 2 AA4 4 THR A 129 PHE A 139 -1 O LEU A 135 N PHE A 116 SHEET 3 AA4 4 TYR A 173 SER A 182 -1 O LEU A 175 N LEU A 136 SHEET 4 AA4 4 SER A 159 VAL A 163 -1 N GLN A 160 O THR A 178 SHEET 1 AA5 4 ALA A 153 LEU A 154 0 SHEET 2 AA5 4 ALA A 144 VAL A 150 -1 N VAL A 150 O ALA A 153 SHEET 3 AA5 4 TYR A 192 HIS A 198 -1 O GLU A 195 N GLN A 147 SHEET 4 AA5 4 VAL A 205 PHE A 209 -1 O LYS A 207 N CYS A 194 SHEET 1 AA6 3 MET C 4 SER C 7 0 SHEET 2 AA6 3 VAL C 19 ILE C 29 -1 O ARG C 24 N THR C 5 SHEET 3 AA6 3 PHE C 62 ILE C 75 -1 O THR C 69 N ALA C 25 SHEET 1 AA7 6 SER C 10 ALA C 13 0 SHEET 2 AA7 6 THR C 102 ILE C 106 1 O GLU C 105 N LEU C 11 SHEET 3 AA7 6 THR C 85 GLN C 90 -1 N PHE C 86 O THR C 102 SHEET 4 AA7 6 LEU C 33 HIS C 38 -1 N TYR C 36 O TYR C 87 SHEET 5 AA7 6 PRO C 44 LYS C 49 -1 O LYS C 45 N GLN C 37 SHEET 6 AA7 6 THR C 53 LEU C 54 -1 O THR C 53 N LYS C 49 SHEET 1 AA8 4 SER C 114 PHE C 118 0 SHEET 2 AA8 4 THR C 129 PHE C 139 -1 O LEU C 135 N PHE C 116 SHEET 3 AA8 4 TYR C 173 SER C 182 -1 O LEU C 175 N LEU C 136 SHEET 4 AA8 4 SER C 159 VAL C 163 -1 N GLN C 160 O THR C 178 SHEET 1 AA9 4 ALA C 153 LEU C 154 0 SHEET 2 AA9 4 ALA C 144 VAL C 150 -1 N VAL C 150 O ALA C 153 SHEET 3 AA9 4 VAL C 191 HIS C 198 -1 O GLU C 195 N GLN C 147 SHEET 4 AA9 4 VAL C 205 ASN C 210 -1 O VAL C 205 N VAL C 196 SHEET 1 AB1 3 MET E 4 SER E 7 0 SHEET 2 AB1 3 VAL E 19 ILE E 29 -1 O ARG E 24 N THR E 5 SHEET 3 AB1 3 PHE E 62 ILE E 75 -1 O GLY E 68 N ILE E 29 SHEET 1 AB2 2 SER E 10 ALA E 13 0 SHEET 2 AB2 2 ARG E 103 ILE E 106 1 O GLU E 105 N ALA E 13 SHEET 1 AB3 4 THR E 53 LEU E 54 0 SHEET 2 AB3 4 PRO E 44 LYS E 49 -1 N LYS E 49 O THR E 53 SHEET 3 AB3 4 LEU E 33 HIS E 38 -1 N GLN E 37 O LYS E 45 SHEET 4 AB3 4 THR E 85 GLN E 90 -1 O TYR E 87 N TYR E 36 SHEET 1 AB4 4 SER E 114 PHE E 118 0 SHEET 2 AB4 4 THR E 129 PHE E 139 -1 O LEU E 135 N PHE E 116 SHEET 3 AB4 4 TYR E 173 SER E 182 -1 O LEU E 175 N LEU E 136 SHEET 4 AB4 4 SER E 159 VAL E 163 -1 N GLN E 160 O THR E 178 SHEET 1 AB5 4 ALA E 153 LEU E 154 0 SHEET 2 AB5 4 LYS E 145 VAL E 150 -1 N VAL E 150 O ALA E 153 SHEET 3 AB5 4 VAL E 191 THR E 197 -1 O ALA E 193 N LYS E 149 SHEET 4 AB5 4 VAL E 205 ASN E 210 -1 O LYS E 207 N CYS E 194 SHEET 1 AB6 3 MET I 4 SER I 7 0 SHEET 2 AB6 3 VAL I 19 ILE I 29 -1 O ARG I 24 N THR I 5 SHEET 3 AB6 3 PHE I 62 ILE I 75 -1 O THR I 69 N ALA I 25 SHEET 1 AB7 2 SER I 10 ALA I 13 0 SHEET 2 AB7 2 ARG I 103 ILE I 106 1 O GLU I 105 N LEU I 11 SHEET 1 AB8 4 THR I 53 LEU I 54 0 SHEET 2 AB8 4 LYS I 45 LYS I 49 -1 N LYS I 49 O THR I 53 SHEET 3 AB8 4 LEU I 33 HIS I 38 -1 N GLN I 37 O LYS I 45 SHEET 4 AB8 4 THR I 85 GLN I 90 -1 O TYR I 87 N TYR I 36 SHEET 1 AB9 4 SER I 114 PHE I 118 0 SHEET 2 AB9 4 THR I 129 PHE I 139 -1 O LEU I 135 N PHE I 116 SHEET 3 AB9 4 TYR I 173 SER I 182 -1 O LEU I 175 N LEU I 136 SHEET 4 AB9 4 SER I 159 VAL I 163 -1 N GLN I 160 O THR I 178 SHEET 1 AC1 3 ALA I 144 VAL I 150 0 SHEET 2 AC1 3 VAL I 191 HIS I 198 -1 O ALA I 193 N LYS I 149 SHEET 3 AC1 3 VAL I 205 ASN I 210 -1 O LYS I 207 N CYS I 194 SHEET 1 AC2 4 MET K 4 SER K 7 0 SHEET 2 AC2 4 VAL K 19 ALA K 25 -1 O ARG K 24 N THR K 5 SHEET 3 AC2 4 ASP K 70 ILE K 75 -1 O ILE K 75 N VAL K 19 SHEET 4 AC2 4 PHE K 62 SER K 67 -1 N SER K 63 O THR K 74 SHEET 1 AC3 2 SER K 10 SER K 14 0 SHEET 2 AC3 2 ARG K 103 LYS K 107 1 O LYS K 107 N ALA K 13 SHEET 1 AC4 4 THR K 53 LEU K 54 0 SHEET 2 AC4 4 LYS K 45 LYS K 49 -1 N LYS K 49 O THR K 53 SHEET 3 AC4 4 LEU K 33 HIS K 38 -1 N GLN K 37 O LYS K 45 SHEET 4 AC4 4 THR K 85 GLN K 90 -1 O TYR K 87 N TYR K 36 SHEET 1 AC5 4 SER K 114 PHE K 118 0 SHEET 2 AC5 4 THR K 129 PHE K 139 -1 O LEU K 135 N PHE K 116 SHEET 3 AC5 4 TYR K 173 SER K 182 -1 O TYR K 173 N PHE K 139 SHEET 4 AC5 4 SER K 159 VAL K 163 -1 N GLN K 160 O THR K 178 SHEET 1 AC6 4 ALA K 153 LEU K 154 0 SHEET 2 AC6 4 ALA K 144 VAL K 150 -1 N VAL K 150 O ALA K 153 SHEET 3 AC6 4 VAL K 191 HIS K 198 -1 O ALA K 193 N LYS K 149 SHEET 4 AC6 4 VAL K 205 ASN K 210 -1 O LYS K 207 N CYS K 194 SHEET 1 AC7 4 GLN B 3 GLN B 6 0 SHEET 2 AC7 4 VAL B 18 SER B 25 -1 O GLN B 23 N VAL B 5 SHEET 3 AC7 4 THR B 77 LEU B 82 -1 O ALA B 78 N CYS B 22 SHEET 4 AC7 4 VAL B 67 ASP B 72 -1 N THR B 68 O GLU B 81 SHEET 1 AC8 6 GLU B 10 LYS B 12 0 SHEET 2 AC8 6 THR B 107 VAL B 111 1 O THR B 110 N GLU B 10 SHEET 3 AC8 6 ALA B 88 ASP B 95 -1 N ALA B 88 O VAL B 109 SHEET 4 AC8 6 TYR B 33 GLN B 39 -1 N LEU B 37 O TYR B 91 SHEET 5 AC8 6 LEU B 45 MET B 51 -1 O GLU B 46 N ARG B 38 SHEET 6 AC8 6 THR B 57 TYR B 59 -1 O LYS B 58 N TRP B 50 SHEET 1 AC9 4 GLU B 10 LYS B 12 0 SHEET 2 AC9 4 THR B 107 VAL B 111 1 O THR B 110 N GLU B 10 SHEET 3 AC9 4 ALA B 88 ASP B 95 -1 N ALA B 88 O VAL B 109 SHEET 4 AC9 4 TYR B 100G TRP B 103 -1 O TYR B 102 N ARG B 94 SHEET 1 AD1 4 SER B 120 LEU B 124 0 SHEET 2 AD1 4 ALA B 136 TYR B 145 -1 O LEU B 141 N PHE B 122 SHEET 3 AD1 4 TYR B 176 VAL B 184 -1 O TYR B 176 N TYR B 145 SHEET 4 AD1 4 VAL B 163 THR B 165 -1 N HIS B 164 O VAL B 181 SHEET 1 AD2 4 SER B 120 LEU B 124 0 SHEET 2 AD2 4 ALA B 136 TYR B 145 -1 O LEU B 141 N PHE B 122 SHEET 3 AD2 4 TYR B 176 VAL B 184 -1 O TYR B 176 N TYR B 145 SHEET 4 AD2 4 VAL B 169 LEU B 170 -1 N VAL B 169 O SER B 177 SHEET 1 AD3 3 THR B 151 TRP B 154 0 SHEET 2 AD3 3 TYR B 194 HIS B 200 -1 O ASN B 197 N SER B 153 SHEET 3 AD3 3 THR B 205 VAL B 211 -1 O THR B 205 N HIS B 200 SHEET 1 AD4 4 GLN D 3 GLN D 6 0 SHEET 2 AD4 4 VAL D 18 SER D 25 -1 O GLN D 23 N VAL D 5 SHEET 3 AD4 4 THR D 77 LEU D 82 -1 O ALA D 78 N CYS D 22 SHEET 4 AD4 4 VAL D 67 ASP D 72 -1 N THR D 70 O HIS D 79 SHEET 1 AD5 6 GLU D 10 LYS D 12 0 SHEET 2 AD5 6 THR D 107 VAL D 111 1 O THR D 110 N GLU D 10 SHEET 3 AD5 6 ALA D 88 ASP D 95 -1 N TYR D 90 O THR D 107 SHEET 4 AD5 6 TYR D 33 ALA D 40 -1 N LEU D 37 O TYR D 91 SHEET 5 AD5 6 GLY D 44 MET D 51 -1 O GLY D 49 N TRP D 36 SHEET 6 AD5 6 THR D 57 TYR D 59 -1 O LYS D 58 N TRP D 50 SHEET 1 AD6 4 GLU D 10 LYS D 12 0 SHEET 2 AD6 4 THR D 107 VAL D 111 1 O THR D 110 N GLU D 10 SHEET 3 AD6 4 ALA D 88 ASP D 95 -1 N TYR D 90 O THR D 107 SHEET 4 AD6 4 TYR D 100G TRP D 103 -1 O TYR D 102 N ARG D 94 SHEET 1 AD7 4 SER D 120 LEU D 124 0 SHEET 2 AD7 4 THR D 135 TYR D 145 -1 O LEU D 141 N PHE D 122 SHEET 3 AD7 4 TYR D 176 PRO D 185 -1 O VAL D 184 N ALA D 136 SHEET 4 AD7 4 VAL D 163 THR D 165 -1 N HIS D 164 O VAL D 181 SHEET 1 AD8 4 SER D 120 LEU D 124 0 SHEET 2 AD8 4 THR D 135 TYR D 145 -1 O LEU D 141 N PHE D 122 SHEET 3 AD8 4 TYR D 176 PRO D 185 -1 O VAL D 184 N ALA D 136 SHEET 4 AD8 4 VAL D 169 LEU D 170 -1 N VAL D 169 O SER D 177 SHEET 1 AD9 3 THR D 151 TRP D 154 0 SHEET 2 AD9 3 TYR D 194 HIS D 200 -1 O ASN D 197 N SER D 153 SHEET 3 AD9 3 THR D 205 VAL D 211 -1 O THR D 205 N HIS D 200 SHEET 1 AE1 4 GLN F 3 GLN F 6 0 SHEET 2 AE1 4 VAL F 18 SER F 25 -1 O GLN F 23 N VAL F 5 SHEET 3 AE1 4 THR F 77 LEU F 82 -1 O ALA F 78 N CYS F 22 SHEET 4 AE1 4 VAL F 67 ASP F 72 -1 N THR F 70 O HIS F 79 SHEET 1 AE2 6 GLU F 10 LYS F 12 0 SHEET 2 AE2 6 THR F 107 VAL F 111 1 O LEU F 108 N GLU F 10 SHEET 3 AE2 6 ALA F 88 ASP F 95 -1 N TYR F 90 O THR F 107 SHEET 4 AE2 6 TYR F 33 GLN F 39 -1 N LEU F 37 O TYR F 91 SHEET 5 AE2 6 LEU F 45 MET F 51 -1 O GLU F 46 N ARG F 38 SHEET 6 AE2 6 THR F 57 TYR F 59 -1 O LYS F 58 N TRP F 50 SHEET 1 AE3 4 GLU F 10 LYS F 12 0 SHEET 2 AE3 4 THR F 107 VAL F 111 1 O LEU F 108 N GLU F 10 SHEET 3 AE3 4 ALA F 88 ASP F 95 -1 N TYR F 90 O THR F 107 SHEET 4 AE3 4 TYR F 100G TRP F 103 -1 O TYR F 102 N ARG F 94 SHEET 1 AE4 4 SER F 120 LEU F 124 0 SHEET 2 AE4 4 THR F 135 TYR F 145 -1 O LEU F 141 N PHE F 122 SHEET 3 AE4 4 TYR F 176 PRO F 185 -1 O VAL F 184 N ALA F 136 SHEET 4 AE4 4 VAL F 163 THR F 165 -1 N HIS F 164 O VAL F 181 SHEET 1 AE5 4 SER F 120 LEU F 124 0 SHEET 2 AE5 4 THR F 135 TYR F 145 -1 O LEU F 141 N PHE F 122 SHEET 3 AE5 4 TYR F 176 PRO F 185 -1 O VAL F 184 N ALA F 136 SHEET 4 AE5 4 VAL F 169 LEU F 170 -1 N VAL F 169 O SER F 177 SHEET 1 AE6 3 THR F 151 TRP F 154 0 SHEET 2 AE6 3 ILE F 195 HIS F 200 -1 O ASN F 197 N SER F 153 SHEET 3 AE6 3 THR F 205 LYS F 210 -1 O THR F 205 N HIS F 200 SHEET 1 AE7 4 GLN J 3 GLN J 6 0 SHEET 2 AE7 4 VAL J 18 SER J 25 -1 O GLN J 23 N VAL J 5 SHEET 3 AE7 4 THR J 77 LEU J 82 -1 O ALA J 78 N CYS J 22 SHEET 4 AE7 4 VAL J 67 ASP J 72 -1 N THR J 70 O HIS J 79 SHEET 1 AE8 6 GLU J 10 LYS J 12 0 SHEET 2 AE8 6 THR J 107 VAL J 111 1 O THR J 110 N LYS J 12 SHEET 3 AE8 6 ALA J 88 ASP J 95 -1 N TYR J 90 O THR J 107 SHEET 4 AE8 6 TYR J 33 GLN J 39 -1 N LEU J 37 O TYR J 91 SHEET 5 AE8 6 LEU J 45 MET J 51 -1 O GLU J 46 N ARG J 38 SHEET 6 AE8 6 THR J 57 TYR J 59 -1 O LYS J 58 N TRP J 50 SHEET 1 AE9 4 GLU J 10 LYS J 12 0 SHEET 2 AE9 4 THR J 107 VAL J 111 1 O THR J 110 N LYS J 12 SHEET 3 AE9 4 ALA J 88 ASP J 95 -1 N TYR J 90 O THR J 107 SHEET 4 AE9 4 TYR J 100G TRP J 103 -1 O TYR J 102 N ARG J 94 SHEET 1 AF1 4 SER J 120 LEU J 124 0 SHEET 2 AF1 4 THR J 135 TYR J 145 -1 O LEU J 141 N PHE J 122 SHEET 3 AF1 4 TYR J 176 PRO J 185 -1 O TYR J 176 N TYR J 145 SHEET 4 AF1 4 VAL J 163 THR J 165 -1 N HIS J 164 O VAL J 181 SHEET 1 AF2 4 SER J 120 LEU J 124 0 SHEET 2 AF2 4 THR J 135 TYR J 145 -1 O LEU J 141 N PHE J 122 SHEET 3 AF2 4 TYR J 176 PRO J 185 -1 O TYR J 176 N TYR J 145 SHEET 4 AF2 4 VAL J 169 LEU J 170 -1 N VAL J 169 O SER J 177 SHEET 1 AF3 3 THR J 151 TRP J 154 0 SHEET 2 AF3 3 TYR J 194 HIS J 200 -1 O ASN J 197 N SER J 153 SHEET 3 AF3 3 THR J 205 VAL J 211 -1 O THR J 205 N HIS J 200 SHEET 1 AF4 4 GLN L 3 GLN L 6 0 SHEET 2 AF4 4 VAL L 18 SER L 25 -1 O GLN L 23 N VAL L 5 SHEET 3 AF4 4 THR L 77 LEU L 82 -1 O ALA L 78 N CYS L 22 SHEET 4 AF4 4 VAL L 67 ASP L 72 -1 N THR L 68 O GLU L 81 SHEET 1 AF5 6 GLU L 10 LYS L 12 0 SHEET 2 AF5 6 THR L 107 VAL L 111 1 O THR L 110 N LYS L 12 SHEET 3 AF5 6 ALA L 88 ASP L 95 -1 N TYR L 90 O THR L 107 SHEET 4 AF5 6 TYR L 33 GLN L 39 -1 N LEU L 37 O TYR L 91 SHEET 5 AF5 6 LEU L 45 MET L 51 -1 O GLU L 46 N ARG L 38 SHEET 6 AF5 6 THR L 57 TYR L 59 -1 O LYS L 58 N TRP L 50 SHEET 1 AF6 4 GLU L 10 LYS L 12 0 SHEET 2 AF6 4 THR L 107 VAL L 111 1 O THR L 110 N LYS L 12 SHEET 3 AF6 4 ALA L 88 ASP L 95 -1 N TYR L 90 O THR L 107 SHEET 4 AF6 4 TYR L 100G TRP L 103 -1 O TYR L 102 N ARG L 94 SHEET 1 AF7 4 SER L 120 LEU L 124 0 SHEET 2 AF7 4 THR L 135 TYR L 145 -1 O LEU L 141 N PHE L 122 SHEET 3 AF7 4 TYR L 176 PRO L 185 -1 O TYR L 176 N TYR L 145 SHEET 4 AF7 4 VAL L 163 THR L 165 -1 N HIS L 164 O VAL L 181 SHEET 1 AF8 4 SER L 120 LEU L 124 0 SHEET 2 AF8 4 THR L 135 TYR L 145 -1 O LEU L 141 N PHE L 122 SHEET 3 AF8 4 TYR L 176 PRO L 185 -1 O TYR L 176 N TYR L 145 SHEET 4 AF8 4 VAL L 169 LEU L 170 -1 N VAL L 169 O SER L 177 SHEET 1 AF9 3 THR L 151 TRP L 154 0 SHEET 2 AF9 3 TYR L 194 HIS L 200 -1 O ASN L 197 N SER L 153 SHEET 3 AF9 3 THR L 205 VAL L 211 -1 O THR L 205 N HIS L 200 SHEET 1 AG1 4 MET G 4 SER G 7 0 SHEET 2 AG1 4 VAL G 19 ALA G 25 -1 O ARG G 24 N THR G 5 SHEET 3 AG1 4 ASP G 70 ILE G 75 -1 O LEU G 73 N ILE G 21 SHEET 4 AG1 4 PHE G 62 SER G 67 -1 N SER G 63 O THR G 74 SHEET 1 AG2 2 SER G 10 SER G 12 0 SHEET 2 AG2 2 ARG G 103 GLU G 105 1 O GLU G 105 N LEU G 11 SHEET 1 AG3 5 THR G 53 LEU G 54 0 SHEET 2 AG3 5 PRO G 44 LYS G 49 -1 N LYS G 49 O THR G 53 SHEET 3 AG3 5 LEU G 33 HIS G 38 -1 N GLN G 37 O LYS G 45 SHEET 4 AG3 5 THR G 85 GLN G 90 -1 O TYR G 87 N TYR G 36 SHEET 5 AG3 5 THR G 97 PHE G 98 -1 O THR G 97 N GLN G 90 SHEET 1 AG4 4 SER G 114 PHE G 118 0 SHEET 2 AG4 4 THR G 129 PHE G 139 -1 O ASN G 137 N SER G 114 SHEET 3 AG4 4 TYR G 173 SER G 182 -1 O LEU G 179 N VAL G 132 SHEET 4 AG4 4 SER G 159 VAL G 163 -1 N GLN G 160 O THR G 178 SHEET 1 AG5 4 ALA G 153 LEU G 154 0 SHEET 2 AG5 4 LYS G 145 VAL G 150 -1 N VAL G 150 O ALA G 153 SHEET 3 AG5 4 TYR G 192 THR G 197 -1 O ALA G 193 N LYS G 149 SHEET 4 AG5 4 VAL G 205 PHE G 209 -1 O LYS G 207 N CYS G 194 SHEET 1 AG6 4 GLN H 3 GLN H 6 0 SHEET 2 AG6 4 VAL H 18 SER H 25 -1 O GLN H 23 N VAL H 5 SHEET 3 AG6 4 THR H 77 LEU H 82 -1 O ALA H 78 N CYS H 22 SHEET 4 AG6 4 VAL H 67 ASP H 72 -1 N THR H 70 O HIS H 79 SHEET 1 AG7 6 GLU H 10 LYS H 12 0 SHEET 2 AG7 6 THR H 107 VAL H 111 1 O LEU H 108 N GLU H 10 SHEET 3 AG7 6 ALA H 88 ASP H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AG7 6 TYR H 33 GLN H 39 -1 N LEU H 37 O TYR H 91 SHEET 5 AG7 6 LEU H 45 MET H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AG7 6 THR H 57 TYR H 59 -1 O LYS H 58 N TRP H 50 SHEET 1 AG8 4 GLU H 10 LYS H 12 0 SHEET 2 AG8 4 THR H 107 VAL H 111 1 O LEU H 108 N GLU H 10 SHEET 3 AG8 4 ALA H 88 ASP H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AG8 4 TYR H 100G TRP H 103 -1 O TYR H 102 N ARG H 94 SHEET 1 AG9 4 SER H 120 LEU H 124 0 SHEET 2 AG9 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AG9 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA H 136 SHEET 4 AG9 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AH1 4 SER H 120 LEU H 124 0 SHEET 2 AH1 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AH1 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA H 136 SHEET 4 AH1 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AH2 3 THR H 151 TRP H 154 0 SHEET 2 AH2 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AH2 3 THR H 205 LYS H 210 -1 O THR H 205 N HIS H 200 SSBOND 1 CYS A 23 CYS A 88 1555 1555 2.03 SSBOND 2 CYS A 134 CYS A 194 1555 1555 2.03 SSBOND 3 CYS C 23 CYS C 88 1555 1555 2.04 SSBOND 4 CYS C 134 CYS C 194 1555 1555 2.03 SSBOND 5 CYS E 23 CYS E 88 1555 1555 2.04 SSBOND 6 CYS E 134 CYS E 194 1555 1555 2.03 SSBOND 7 CYS I 23 CYS I 88 1555 1555 2.04 SSBOND 8 CYS I 134 CYS I 194 1555 1555 2.04 SSBOND 9 CYS K 23 CYS K 88 1555 1555 2.04 SSBOND 10 CYS K 134 CYS K 194 1555 1555 2.04 SSBOND 11 CYS B 22 CYS B 92 1555 1555 2.04 SSBOND 12 CYS B 97 CYS B 100B 1555 1555 2.03 SSBOND 13 CYS B 140 CYS B 196 1555 1555 2.03 SSBOND 14 CYS D 22 CYS D 92 1555 1555 2.04 SSBOND 15 CYS D 97 CYS D 100B 1555 1555 2.04 SSBOND 16 CYS D 140 CYS D 196 1555 1555 2.04 SSBOND 17 CYS F 22 CYS F 92 1555 1555 2.04 SSBOND 18 CYS F 97 CYS F 100B 1555 1555 2.03 SSBOND 19 CYS F 140 CYS F 196 1555 1555 2.04 SSBOND 20 CYS J 22 CYS J 92 1555 1555 2.04 SSBOND 21 CYS J 97 CYS J 100B 1555 1555 2.03 SSBOND 22 CYS J 140 CYS J 196 1555 1555 2.04 SSBOND 23 CYS L 22 CYS L 92 1555 1555 2.04 SSBOND 24 CYS L 97 CYS L 100B 1555 1555 2.03 SSBOND 25 CYS L 140 CYS L 196 1555 1555 2.04 SSBOND 26 CYS G 23 CYS G 88 1555 1555 2.04 SSBOND 27 CYS G 134 CYS G 194 1555 1555 2.03 SSBOND 28 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 29 CYS H 97 CYS H 100B 1555 1555 2.03 SSBOND 30 CYS H 140 CYS H 196 1555 1555 2.04 CISPEP 1 SER A 7 PRO A 8 0 -0.70 CISPEP 2 ASP A 94 PRO A 95 0 2.17 CISPEP 3 TYR A 140 PRO A 141 0 2.80 CISPEP 4 SER C 7 PRO C 8 0 0.01 CISPEP 5 ASP C 94 PRO C 95 0 1.58 CISPEP 6 TYR C 140 PRO C 141 0 2.82 CISPEP 7 SER E 7 PRO E 8 0 -0.78 CISPEP 8 ASP E 94 PRO E 95 0 1.74 CISPEP 9 TYR E 140 PRO E 141 0 2.14 CISPEP 10 SER I 7 PRO I 8 0 -0.48 CISPEP 11 ASP I 94 PRO I 95 0 1.93 CISPEP 12 TYR I 140 PRO I 141 0 2.67 CISPEP 13 SER K 7 PRO K 8 0 -0.97 CISPEP 14 ASP K 94 PRO K 95 0 2.04 CISPEP 15 TYR K 140 PRO K 141 0 2.40 CISPEP 16 PHE B 146 PRO B 147 0 -4.93 CISPEP 17 GLU B 148 PRO B 149 0 -1.46 CISPEP 18 PHE D 146 PRO D 147 0 -3.94 CISPEP 19 GLU D 148 PRO D 149 0 -1.55 CISPEP 20 PHE F 146 PRO F 147 0 -5.47 CISPEP 21 GLU F 148 PRO F 149 0 -1.64 CISPEP 22 PHE J 146 PRO J 147 0 -4.38 CISPEP 23 GLU J 148 PRO J 149 0 -2.81 CISPEP 24 PHE L 146 PRO L 147 0 -6.20 CISPEP 25 GLU L 148 PRO L 149 0 -2.04 CISPEP 26 SER G 7 PRO G 8 0 -3.03 CISPEP 27 ASP G 94 PRO G 95 0 1.46 CISPEP 28 TYR G 140 PRO G 141 0 1.30 CISPEP 29 PHE H 146 PRO H 147 0 -3.67 CISPEP 30 GLU H 148 PRO H 149 0 -6.88 CRYST1 164.513 164.513 92.276 90.00 90.00 120.00 P 32 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 0.006079 0.003509 0.000000 0.00000 SCALE2 0.000000 0.007019 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010837 0.00000