HEADER IMMUNE SYSTEM 06-FEB-25 9N7K TITLE CRYSTAL STRUCTURE OF HUMAN ANTI-PFS48/45 TRANSMISSION-BLOCKING TITLE 2 ANTIBODY RUPA-71 COMPND MOL_ID: 1; COMPND 2 MOLECULE: RUPA-71 FAB HEAVY CHAIN; COMPND 3 CHAIN: A, H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: RUPA-71 FAB KAPPA CHAIN; COMPND 7 CHAIN: B, L; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: HEK293 F; SOURCE 7 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1573; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM_CELL_LINE: HEK293 F; SOURCE 14 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1573 KEYWDS PFS48/45, HUMAN TRANSMISSION-BLOCKING ANTIBODIES, MALARIA, IMMUNE KEYWDS 2 SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR S.HAILEMARIAM,D.IVANOCHKO,X.LIU,J.P.JULIEN REVDAT 1 15-OCT-25 9N7K 0 JRNL AUTH E.BEKKERING,R.YOO,S.HAILEMARIAM,F.HEIDE,D.IVANOCHKO, JRNL AUTH 2 M.JACKMAN,N.I.PROELLOCHS,R.STOTER,G.VAN GEMERT,A.MAEDA, JRNL AUTH 3 T.YUGUCHI,O.T.WANDERS,R.C.VAN DAALEN,M.R.INKLAAR, JRNL AUTH 4 C.M.ANDRADE,P.W.T.C.JANSEN,M.VERMEULEN,T.BOUSEMA, JRNL AUTH 5 E.TAKASHIMA,J.L.RUBINSTEIN,T.W.A.KOOIJ,M.M.JORE,J.P.JULIEN JRNL TITL CRYO-EM STRUCTURE OF ENDOGENOUS PFS230:PFS48/45 COMPLEX WITH JRNL TITL 2 SIX ANTIBODIES REVEALS MECHANISMS OF MALARIA JRNL TITL 3 TRANSMISSION-BLOCKING ACTIVITY JRNL REF IMMUNITY 2025 JRNL REFN ISSN 1074-7613 REMARK 2 REMARK 2 RESOLUTION. 2.28 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.21.1_5286: ???) 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) : 2.28 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.85 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 46103 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.193 REMARK 3 R VALUE (WORKING SET) : 0.191 REMARK 3 FREE R VALUE : 0.241 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.340 REMARK 3 FREE R VALUE TEST SET COUNT : 2000 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 48.8500 - 5.4900 1.00 3373 153 0.1700 0.2194 REMARK 3 2 5.4900 - 4.3600 1.00 3214 146 0.1468 0.1711 REMARK 3 3 4.3600 - 3.8100 1.00 3196 145 0.1590 0.2053 REMARK 3 4 3.8100 - 3.4600 1.00 3158 143 0.1779 0.2131 REMARK 3 5 3.4600 - 3.2100 1.00 3148 143 0.1893 0.2559 REMARK 3 6 3.2100 - 3.0200 1.00 3139 142 0.1986 0.2708 REMARK 3 7 3.0200 - 2.8700 1.00 3111 141 0.2103 0.2909 REMARK 3 8 2.8700 - 2.7500 1.00 3126 142 0.2260 0.2729 REMARK 3 9 2.7500 - 2.6400 1.00 3131 141 0.2357 0.2867 REMARK 3 10 2.6400 - 2.5500 1.00 3117 142 0.2420 0.3064 REMARK 3 11 2.5500 - 2.4700 1.00 3070 139 0.2441 0.3076 REMARK 3 12 2.4700 - 2.4000 1.00 3096 140 0.2530 0.3115 REMARK 3 13 2.4000 - 2.3400 1.00 3121 143 0.2628 0.3556 REMARK 3 14 2.3400 - 2.2800 1.00 3103 140 0.2738 0.3227 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.290 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.450 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.37 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 : 0.009 NULL REMARK 3 ANGLE : 0.991 NULL REMARK 3 CHIRALITY : 0.058 1055 REMARK 3 PLANARITY : 0.007 1207 REMARK 3 DIHEDRAL : 15.997 2507 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 14 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -36.5003 -45.6339 -29.3447 REMARK 3 T TENSOR REMARK 3 T11: 0.3844 T22: 0.3242 REMARK 3 T33: 0.3538 T12: 0.0485 REMARK 3 T13: -0.0463 T23: 0.0723 REMARK 3 L TENSOR REMARK 3 L11: 6.8922 L22: 7.3686 REMARK 3 L33: 4.8145 L12: -2.8183 REMARK 3 L13: -2.8228 L23: 5.9721 REMARK 3 S TENSOR REMARK 3 S11: -0.2651 S12: -0.1570 S13: -0.2088 REMARK 3 S21: 0.6976 S22: 0.4082 S23: -0.4146 REMARK 3 S31: 0.3180 S32: 0.2880 S33: -0.1712 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 18 THROUGH 216 ) REMARK 3 ORIGIN FOR THE GROUP (A): -30.3016 -40.6686 -32.4147 REMARK 3 T TENSOR REMARK 3 T11: 0.2277 T22: 0.1681 REMARK 3 T33: 0.1988 T12: 0.0047 REMARK 3 T13: 0.0191 T23: 0.0172 REMARK 3 L TENSOR REMARK 3 L11: 3.7620 L22: 0.6449 REMARK 3 L33: 0.5135 L12: -0.6376 REMARK 3 L13: -0.3450 L23: 0.0528 REMARK 3 S TENSOR REMARK 3 S11: -0.0782 S12: 0.0557 S13: -0.1820 REMARK 3 S21: 0.0009 S22: 0.0238 S23: 0.0670 REMARK 3 S31: -0.0297 S32: -0.0014 S33: 0.0613 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 25 ) REMARK 3 ORIGIN FOR THE GROUP (A): -38.3561 -18.1639 -44.7229 REMARK 3 T TENSOR REMARK 3 T11: 0.4183 T22: 0.4736 REMARK 3 T33: 0.5257 T12: 0.0216 REMARK 3 T13: 0.0596 T23: 0.1835 REMARK 3 L TENSOR REMARK 3 L11: 6.2485 L22: 2.8688 REMARK 3 L33: 3.6054 L12: -0.2421 REMARK 3 L13: 0.8351 L23: 0.4990 REMARK 3 S TENSOR REMARK 3 S11: -0.6387 S12: 0.9752 S13: 0.5275 REMARK 3 S21: -0.5733 S22: 0.2944 S23: -0.0635 REMARK 3 S31: -0.3188 S32: -0.1607 S33: 0.3179 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 26 THROUGH 101 ) REMARK 3 ORIGIN FOR THE GROUP (A): -40.5929 -20.7075 -35.3295 REMARK 3 T TENSOR REMARK 3 T11: 0.2609 T22: 0.2196 REMARK 3 T33: 0.3447 T12: 0.0294 REMARK 3 T13: 0.0095 T23: 0.0453 REMARK 3 L TENSOR REMARK 3 L11: 5.2142 L22: 4.4449 REMARK 3 L33: 2.0053 L12: 0.8681 REMARK 3 L13: -1.6049 L23: -0.7999 REMARK 3 S TENSOR REMARK 3 S11: 0.0667 S12: 0.2047 S13: 0.6990 REMARK 3 S21: 0.0270 S22: 0.0690 S23: -0.0828 REMARK 3 S31: -0.3533 S32: -0.0135 S33: -0.1022 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 102 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.8088 -20.1605 -45.7542 REMARK 3 T TENSOR REMARK 3 T11: 0.3432 T22: 0.3534 REMARK 3 T33: 0.5810 T12: 0.0002 REMARK 3 T13: 0.1038 T23: 0.1376 REMARK 3 L TENSOR REMARK 3 L11: 7.3774 L22: 0.1132 REMARK 3 L33: 1.3073 L12: 0.9012 REMARK 3 L13: -3.0221 L23: -0.3243 REMARK 3 S TENSOR REMARK 3 S11: 0.0771 S12: 0.6505 S13: 0.2076 REMARK 3 S21: 0.5441 S22: 0.2630 S23: 0.1959 REMARK 3 S31: 0.1017 S32: -0.4924 S33: -0.2877 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 114 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.6206 -38.2187 -50.2555 REMARK 3 T TENSOR REMARK 3 T11: 0.2552 T22: 0.2992 REMARK 3 T33: 0.2723 T12: -0.0212 REMARK 3 T13: 0.0105 T23: 0.0336 REMARK 3 L TENSOR REMARK 3 L11: 3.0666 L22: 6.6089 REMARK 3 L33: 1.6664 L12: -1.2519 REMARK 3 L13: 0.2622 L23: 0.8360 REMARK 3 S TENSOR REMARK 3 S11: 0.1750 S12: 0.2651 S13: 0.1038 REMARK 3 S21: -0.7967 S22: -0.0663 S23: 0.0051 REMARK 3 S31: -0.1279 S32: 0.1219 S33: -0.1092 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.2256 -14.1052 -4.5487 REMARK 3 T TENSOR REMARK 3 T11: 0.2845 T22: 0.2662 REMARK 3 T33: 0.3412 T12: -0.0403 REMARK 3 T13: 0.0594 T23: 0.1146 REMARK 3 L TENSOR REMARK 3 L11: 7.2425 L22: 8.6917 REMARK 3 L33: 5.1444 L12: -3.6741 REMARK 3 L13: -4.5038 L23: 6.4189 REMARK 3 S TENSOR REMARK 3 S11: -0.3380 S12: 0.2976 S13: -0.5888 REMARK 3 S21: 0.0576 S22: -0.4583 S23: 0.5494 REMARK 3 S31: 0.2217 S32: -1.2487 S33: 0.7423 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 18 THROUGH 59 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.9815 -17.6078 -9.0756 REMARK 3 T TENSOR REMARK 3 T11: 0.2185 T22: 0.2575 REMARK 3 T33: 0.3247 T12: 0.0505 REMARK 3 T13: 0.0459 T23: 0.0161 REMARK 3 L TENSOR REMARK 3 L11: 3.1133 L22: 5.0437 REMARK 3 L33: 5.9714 L12: 0.7660 REMARK 3 L13: -0.1764 L23: 1.5143 REMARK 3 S TENSOR REMARK 3 S11: -0.1097 S12: -0.0645 S13: -0.3768 REMARK 3 S21: 0.3574 S22: -0.0579 S23: 0.0430 REMARK 3 S31: 0.5411 S32: 0.0539 S33: 0.1795 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 60 THROUGH 124 ) REMARK 3 ORIGIN FOR THE GROUP (A): -4.4648 -12.3575 -6.2947 REMARK 3 T TENSOR REMARK 3 T11: 0.2600 T22: 0.2427 REMARK 3 T33: 0.2578 T12: 0.0096 REMARK 3 T13: 0.0170 T23: 0.0140 REMARK 3 L TENSOR REMARK 3 L11: 1.8373 L22: 2.2089 REMARK 3 L33: 1.1968 L12: -1.7746 REMARK 3 L13: -1.0193 L23: 1.3043 REMARK 3 S TENSOR REMARK 3 S11: -0.1722 S12: -0.1305 S13: -0.1858 REMARK 3 S21: 0.3045 S22: 0.1720 S23: 0.0821 REMARK 3 S31: 0.2457 S32: 0.1271 S33: 0.0137 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 125 THROUGH 145 ) REMARK 3 ORIGIN FOR THE GROUP (A): -26.2875 22.1441 -8.9763 REMARK 3 T TENSOR REMARK 3 T11: 0.2605 T22: 0.3425 REMARK 3 T33: 0.3157 T12: 0.0332 REMARK 3 T13: 0.0324 T23: -0.0029 REMARK 3 L TENSOR REMARK 3 L11: 4.8709 L22: 5.2466 REMARK 3 L33: 4.7524 L12: -1.4573 REMARK 3 L13: -0.6438 L23: 1.8893 REMARK 3 S TENSOR REMARK 3 S11: 0.2241 S12: 0.3434 S13: 0.3642 REMARK 3 S21: -0.1638 S22: -0.1735 S23: 0.4736 REMARK 3 S31: -0.8679 S32: -0.2552 S33: -0.0558 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 146 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): -27.9720 11.8574 -7.8951 REMARK 3 T TENSOR REMARK 3 T11: 0.2245 T22: 0.2235 REMARK 3 T33: 0.2651 T12: 0.0194 REMARK 3 T13: 0.0215 T23: -0.0021 REMARK 3 L TENSOR REMARK 3 L11: 2.7110 L22: 2.3622 REMARK 3 L33: 4.1045 L12: -1.1131 REMARK 3 L13: 0.4156 L23: -0.9742 REMARK 3 S TENSOR REMARK 3 S11: 0.0202 S12: 0.0175 S13: -0.0162 REMARK 3 S21: 0.0190 S22: 0.1236 S23: 0.2797 REMARK 3 S31: 0.0890 S32: -0.2880 S33: -0.1405 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.8759 -3.0362 -26.2191 REMARK 3 T TENSOR REMARK 3 T11: 0.4032 T22: 0.2714 REMARK 3 T33: 0.3280 T12: 0.0126 REMARK 3 T13: 0.1284 T23: -0.0240 REMARK 3 L TENSOR REMARK 3 L11: 6.3672 L22: 7.0556 REMARK 3 L33: 3.0697 L12: -2.1476 REMARK 3 L13: -0.8179 L23: 0.4594 REMARK 3 S TENSOR REMARK 3 S11: 0.1530 S12: 0.2197 S13: 0.2721 REMARK 3 S21: -0.7694 S22: -0.0572 S23: -0.7993 REMARK 3 S31: -0.3671 S32: 0.0113 S33: -0.0661 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 76 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.3017 0.5971 -22.4251 REMARK 3 T TENSOR REMARK 3 T11: 0.2992 T22: 0.3027 REMARK 3 T33: 0.2822 T12: 0.0201 REMARK 3 T13: 0.0490 T23: 0.0160 REMARK 3 L TENSOR REMARK 3 L11: 3.3898 L22: 8.4376 REMARK 3 L33: 0.0300 L12: -4.9237 REMARK 3 L13: 0.6761 L23: -1.0297 REMARK 3 S TENSOR REMARK 3 S11: 0.2227 S12: 0.2781 S13: 0.0032 REMARK 3 S21: -0.4489 S22: -0.1868 S23: -0.1370 REMARK 3 S31: -0.0418 S32: 0.0591 S33: -0.0112 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 114 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.7517 23.4717 -6.9663 REMARK 3 T TENSOR REMARK 3 T11: 0.2372 T22: 0.2071 REMARK 3 T33: 0.2751 T12: 0.0442 REMARK 3 T13: -0.0394 T23: 0.0264 REMARK 3 L TENSOR REMARK 3 L11: 1.3883 L22: 2.3354 REMARK 3 L33: 6.9179 L12: 0.0366 REMARK 3 L13: -0.6886 L23: 1.4931 REMARK 3 S TENSOR REMARK 3 S11: -0.0500 S12: -0.0339 S13: 0.0973 REMARK 3 S21: 0.2054 S22: -0.0201 S23: -0.0383 REMARK 3 S31: -0.1499 S32: -0.0332 S33: 0.0604 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 9N7K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-FEB-25. REMARK 100 THE DEPOSITION ID IS D_1000292654. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-NOV-23 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 : CLSI REMARK 200 BEAMLINE : 08ID-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.95357 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AIMLESS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46105 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.280 REMARK 200 RESOLUTION RANGE LOW (A) : 48.850 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 15.40 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.28 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.36 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 15.20 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.700 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.94 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 0.1 M MES, 30 REMARK 280 %W/V PEG MME 5K, PH 6.5, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 100K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 32.33000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 102.45000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.27500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 102.45000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.33000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.27500 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: 4690 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19310 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 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: 5040 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20670 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, 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 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 215 REMARK 465 CYS H 216 REMARK 465 CYS L 214 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP A 100A -168.09 -122.61 REMARK 500 ASP A 144 62.17 64.29 REMARK 500 SER B 30 -125.18 61.14 REMARK 500 ALA B 51 -35.50 74.98 REMARK 500 GLN B 89 117.86 -160.95 REMARK 500 TRP B 96 47.42 -95.75 REMARK 500 ASN B 152 -0.69 72.99 REMARK 500 ASP H 100A -166.49 -122.66 REMARK 500 ASP H 144 60.70 67.41 REMARK 500 SER L 30 -125.76 59.45 REMARK 500 ALA L 51 -39.15 74.34 REMARK 500 ALA L 84 -176.64 -170.88 REMARK 500 TRP L 96 49.68 -93.79 REMARK 500 REMARK 500 REMARK: NULL DBREF 9N7K A 1 216 PDB 9N7K 9N7K 1 216 DBREF 9N7K B 1 214 PDB 9N7K 9N7K 1 214 DBREF 9N7K H 1 216 PDB 9N7K 9N7K 1 216 DBREF 9N7K L 1 214 PDB 9N7K 9N7K 1 214 SEQRES 1 A 232 GLU GLU GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 A 232 PRO GLY ARG SER LEU ARG LEU SER CYS SER ALA SER GLY SEQRES 3 A 232 PHE THR LEU GLY ASP TYR ALA VAL THR TRP PHE ARG GLN SEQRES 4 A 232 ALA SER GLY LYS GLU PRO GLU TRP VAL GLY VAL ILE ARG SEQRES 5 A 232 THR LYS ASP GLU GLY GLY THR THR GLU TYR ALA ALA SER SEQRES 6 A 232 VAL LYS GLY ARG PHE SER ILE LEU ARG ASP ASP SER LYS SEQRES 7 A 232 SER ILE ALA HIS LEU GLN MET ASN SER LEU LYS ILE GLU SEQRES 8 A 232 ASP THR ALA VAL TYR TYR CYS THR ARG ASN GLY LEU ARG SEQRES 9 A 232 TRP TYR ASP SER SER GLY PRO ARG GLY TRP ALA PHE ASP SEQRES 10 A 232 ILE TRP GLY PRO GLY THR LEU VAL VAL VAL SER SER ALA SEQRES 11 A 232 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 12 A 232 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 13 A 232 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 14 A 232 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 15 A 232 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 16 A 232 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 17 A 232 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 18 A 232 LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 B 215 GLU ILE VAL MET THR GLN SER PRO ALA THR VAL SER VAL SEQRES 2 B 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG THR SER SEQRES 3 B 215 GLN SER VAL SER ASN LYS LEU ALA TRP TYR GLN GLN LYS SEQRES 4 B 215 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER SEQRES 5 B 215 THR ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 B 215 GLY SER GLY THR GLN PHE THR LEU THR ILE SER SER LEU SEQRES 7 B 215 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8 B 215 ASN ASN TRP PRO PRO TRP THR PHE GLY ARG GLY THR LYS SEQRES 9 B 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 B 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 B 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 B 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 B 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 B 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 B 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 B 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 B 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 H 232 GLU GLU GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 H 232 PRO GLY ARG SER LEU ARG LEU SER CYS SER ALA SER GLY SEQRES 3 H 232 PHE THR LEU GLY ASP TYR ALA VAL THR TRP PHE ARG GLN SEQRES 4 H 232 ALA SER GLY LYS GLU PRO GLU TRP VAL GLY VAL ILE ARG SEQRES 5 H 232 THR LYS ASP GLU GLY GLY THR THR GLU TYR ALA ALA SER SEQRES 6 H 232 VAL LYS GLY ARG PHE SER ILE LEU ARG ASP ASP SER LYS SEQRES 7 H 232 SER ILE ALA HIS LEU GLN MET ASN SER LEU LYS ILE GLU SEQRES 8 H 232 ASP THR ALA VAL TYR TYR CYS THR ARG ASN GLY LEU ARG SEQRES 9 H 232 TRP TYR ASP SER SER GLY PRO ARG GLY TRP ALA PHE ASP SEQRES 10 H 232 ILE TRP GLY PRO GLY THR LEU VAL VAL VAL SER SER ALA SEQRES 11 H 232 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 12 H 232 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 13 H 232 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 14 H 232 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 15 H 232 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 16 H 232 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 17 H 232 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 18 H 232 LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 L 215 GLU ILE VAL MET THR GLN SER PRO ALA THR VAL SER VAL SEQRES 2 L 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG THR SER SEQRES 3 L 215 GLN SER VAL SER ASN LYS LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 215 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER SEQRES 5 L 215 THR ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 L 215 GLY SER GLY THR GLN PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 215 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8 L 215 ASN ASN TRP PRO PRO TRP THR PHE GLY ARG GLY THR LYS SEQRES 9 L 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 L 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 215 SER PHE ASN ARG GLY GLU CYS HET GOL A 301 14 HET EDO A 302 10 HET GOL A 303 14 HET EDO A 304 10 HET EDO A 305 10 HET GOL H 301 14 HET EDO H 302 10 HET EDO H 303 10 HET EDO H 304 10 HET EDO H 305 10 HET GOL L 301 14 HETNAM GOL GLYCEROL HETNAM EDO 1,2-ETHANEDIOL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 5 GOL 4(C3 H8 O3) FORMUL 6 EDO 7(C2 H6 O2) FORMUL 16 HOH *209(H2 O) HELIX 1 AA1 THR A 28 TYR A 32 5 5 HELIX 2 AA2 THR A 52A GLY A 54 5 5 HELIX 3 AA3 ASP A 73 LYS A 75 5 3 HELIX 4 AA4 LYS A 83 THR A 87 5 5 HELIX 5 AA5 SER A 127 LYS A 129 5 3 HELIX 6 AA6 SER A 156 ALA A 158 5 3 HELIX 7 AA7 SER A 187 LEU A 189 5 3 HELIX 8 AA8 LYS A 201 ASN A 204 5 4 HELIX 9 AA9 GLN B 79 PHE B 83 5 5 HELIX 10 AB1 SER B 121 SER B 127 1 7 HELIX 11 AB2 LYS B 183 GLU B 187 1 5 HELIX 12 AB3 THR H 28 TYR H 32 5 5 HELIX 13 AB4 THR H 52A GLY H 54 5 5 HELIX 14 AB5 ASP H 73 LYS H 75 5 3 HELIX 15 AB6 LYS H 83 THR H 87 5 5 HELIX 16 AB7 SER H 156 ALA H 158 5 3 HELIX 17 AB8 SER H 187 LEU H 189 5 3 HELIX 18 AB9 LYS H 201 ASN H 204 5 4 HELIX 19 AC1 GLN L 79 PHE L 83 5 5 HELIX 20 AC2 SER L 121 SER L 127 1 7 HELIX 21 AC3 LYS L 183 GLU L 187 1 5 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O SER A 25 N GLN A 3 SHEET 3 AA1 4 ILE A 77 MET A 82 -1 O ALA A 78 N CYS A 22 SHEET 4 AA1 4 PHE A 67 ASP A 72 -1 N SER A 68 O GLN A 81 SHEET 1 AA2 6 LEU A 11 VAL A 12 0 SHEET 2 AA2 6 THR A 107 VAL A 111 1 O VAL A 110 N VAL A 12 SHEET 3 AA2 6 ALA A 88 ARG A 94 -1 N ALA A 88 O VAL A 109 SHEET 4 AA2 6 VAL A 34 GLN A 39 -1 N PHE A 37 O TYR A 91 SHEET 5 AA2 6 GLU A 46 ILE A 51 -1 O GLY A 49 N TRP A 36 SHEET 6 AA2 6 THR A 57 TYR A 59 -1 O GLU A 58 N VAL A 50 SHEET 1 AA3 4 LEU A 11 VAL A 12 0 SHEET 2 AA3 4 THR A 107 VAL A 111 1 O VAL A 110 N VAL A 12 SHEET 3 AA3 4 ALA A 88 ARG A 94 -1 N ALA A 88 O VAL A 109 SHEET 4 AA3 4 ILE A 102 TRP A 103 -1 O ILE A 102 N ARG A 94 SHEET 1 AA4 2 LEU A 97 ASP A 100A 0 SHEET 2 AA4 2 GLY A 100D ALA A 100I-1 O ARG A 100F N TRP A 99 SHEET 1 AA5 4 SER A 120 LEU A 124 0 SHEET 2 AA5 4 THR A 135 TYR A 145 -1 O GLY A 139 N LEU A 124 SHEET 3 AA5 4 TYR A 176 PRO A 185 -1 O TYR A 176 N TYR A 145 SHEET 4 AA5 4 VAL A 163 THR A 165 -1 N HIS A 164 O VAL A 181 SHEET 1 AA6 4 THR A 131 SER A 132 0 SHEET 2 AA6 4 THR A 135 TYR A 145 -1 O THR A 135 N SER A 132 SHEET 3 AA6 4 TYR A 176 PRO A 185 -1 O TYR A 176 N TYR A 145 SHEET 4 AA6 4 VAL A 169 LEU A 170 -1 N VAL A 169 O SER A 177 SHEET 1 AA7 3 THR A 151 TRP A 154 0 SHEET 2 AA7 3 ILE A 195 HIS A 200 -1 O ASN A 197 N SER A 153 SHEET 3 AA7 3 THR A 205 LYS A 210 -1 O VAL A 207 N VAL A 198 SHEET 1 AA8 4 MET B 4 SER B 7 0 SHEET 2 AA8 4 ALA B 19 THR B 25 -1 O ARG B 24 N THR B 5 SHEET 3 AA8 4 GLN B 70 ILE B 75 -1 O PHE B 71 N CYS B 23 SHEET 4 AA8 4 PHE B 62 SER B 67 -1 N SER B 63 O THR B 74 SHEET 1 AA9 6 THR B 10 VAL B 13 0 SHEET 2 AA9 6 THR B 102 ILE B 106 1 O GLU B 105 N VAL B 11 SHEET 3 AA9 6 ALA B 84 GLN B 90 -1 N ALA B 84 O VAL B 104 SHEET 4 AA9 6 LEU B 33 GLN B 38 -1 N GLN B 38 O VAL B 85 SHEET 5 AA9 6 PRO B 44 TYR B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AA9 6 THR B 53 ARG B 54 -1 O THR B 53 N TYR B 49 SHEET 1 AB1 4 SER B 114 PHE B 118 0 SHEET 2 AB1 4 THR B 129 PHE B 139 -1 O LEU B 135 N PHE B 116 SHEET 3 AB1 4 TYR B 173 SER B 182 -1 O LEU B 179 N VAL B 132 SHEET 4 AB1 4 SER B 159 VAL B 163 -1 N GLN B 160 O THR B 178 SHEET 1 AB2 4 ALA B 153 LEU B 154 0 SHEET 2 AB2 4 LYS B 145 VAL B 150 -1 N VAL B 150 O ALA B 153 SHEET 3 AB2 4 VAL B 191 THR B 197 -1 O ALA B 193 N LYS B 149 SHEET 4 AB2 4 VAL B 205 ASN B 210 -1 O VAL B 205 N VAL B 196 SHEET 1 AB3 4 GLN H 3 SER H 7 0 SHEET 2 AB3 4 LEU H 18 SER H 25 -1 O SER H 23 N VAL H 5 SHEET 3 AB3 4 ILE H 77 MET H 82 -1 O MET H 82 N LEU H 18 SHEET 4 AB3 4 PHE H 67 ASP H 72 -1 N LEU H 70 O HIS H 79 SHEET 1 AB4 6 GLY H 10 VAL H 12 0 SHEET 2 AB4 6 THR H 107 VAL H 111 1 O VAL H 110 N VAL H 12 SHEET 3 AB4 6 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 107 SHEET 4 AB4 6 VAL H 34 GLN H 39 -1 N PHE H 37 O TYR H 91 SHEET 5 AB4 6 GLU H 46 ILE H 51 -1 O GLY H 49 N TRP H 36 SHEET 6 AB4 6 THR H 57 TYR H 59 -1 O GLU H 58 N VAL H 50 SHEET 1 AB5 4 GLY H 10 VAL H 12 0 SHEET 2 AB5 4 THR H 107 VAL H 111 1 O VAL H 110 N VAL H 12 SHEET 3 AB5 4 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 107 SHEET 4 AB5 4 ILE H 102 TRP H 103 -1 O ILE H 102 N ARG H 94 SHEET 1 AB6 2 LEU H 97 ASP H 100A 0 SHEET 2 AB6 2 GLY H 100D ALA H 100I-1 O ARG H 100F N TRP H 99 SHEET 1 AB7 4 SER H 120 LEU H 124 0 SHEET 2 AB7 4 THR H 135 TYR H 145 -1 O LYS H 143 N SER H 120 SHEET 3 AB7 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AB7 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AB8 4 SER H 120 LEU H 124 0 SHEET 2 AB8 4 THR H 135 TYR H 145 -1 O LYS H 143 N SER H 120 SHEET 3 AB8 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AB8 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AB9 3 THR H 151 TRP H 154 0 SHEET 2 AB9 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AB9 3 THR H 205 LYS H 210 -1 O VAL H 207 N VAL H 198 SHEET 1 AC1 4 MET L 4 GLN L 6 0 SHEET 2 AC1 4 ALA L 19 THR L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AC1 4 GLN L 70 ILE L 75 -1 O LEU L 73 N LEU L 21 SHEET 4 AC1 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AC2 6 THR L 10 VAL L 13 0 SHEET 2 AC2 6 THR L 102 ILE L 106 1 O LYS L 103 N VAL L 11 SHEET 3 AC2 6 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AC2 6 LEU L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AC2 6 PRO L 44 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AC2 6 THR L 53 ARG L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AC3 4 SER L 114 PHE L 118 0 SHEET 2 AC3 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AC3 4 TYR L 173 SER L 182 -1 O LEU L 179 N VAL L 132 SHEET 4 AC3 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AC4 4 ALA L 153 GLN L 155 0 SHEET 2 AC4 4 LYS L 145 VAL L 150 -1 N TRP L 148 O GLN L 155 SHEET 3 AC4 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147 SHEET 4 AC4 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SSBOND 1 CYS A 22 CYS A 92 1555 1555 2.06 SSBOND 2 CYS A 140 CYS A 196 1555 1555 2.05 SSBOND 3 CYS A 216 CYS B 214 1555 1555 2.04 SSBOND 4 CYS B 23 CYS B 88 1555 1555 2.07 SSBOND 5 CYS B 134 CYS B 194 1555 1555 2.06 SSBOND 6 CYS H 22 CYS H 92 1555 1555 2.06 SSBOND 7 CYS H 140 CYS H 196 1555 1555 2.05 SSBOND 8 CYS L 23 CYS L 88 1555 1555 2.07 SSBOND 9 CYS L 134 CYS L 194 1555 1555 2.03 CISPEP 1 PHE A 146 PRO A 147 0 -3.60 CISPEP 2 GLU A 148 PRO A 149 0 -0.23 CISPEP 3 SER B 7 PRO B 8 0 -9.51 CISPEP 4 TRP B 94 PRO B 95 0 -0.80 CISPEP 5 TYR B 140 PRO B 141 0 1.15 CISPEP 6 PHE H 146 PRO H 147 0 -1.65 CISPEP 7 GLU H 148 PRO H 149 0 0.78 CISPEP 8 SER L 7 PRO L 8 0 -6.29 CISPEP 9 TRP L 94 PRO L 95 0 -0.92 CISPEP 10 TYR L 140 PRO L 141 0 0.20 CRYST1 64.660 74.550 204.900 90.00 90.00 90.00 P 21 21 21 8 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 0.015466 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013414 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004880 0.00000