HEADER STRUCTURAL PROTEIN 25-APR-24 9BJG TITLE CRYSTAL STRUCTURE OF BROADLY NEUTRALIZING HUMAN MONOCLONAL ANTIBODY TITLE 2 75B10 IN COMPLEX WITH AMA1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: APICAL MEMBRANE ANTIGEN 1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: MEROZOITE SURFACE ANTIGEN; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: 75B10 FAB HEAVY CHAIN; COMPND 9 CHAIN: H; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: 75B10 FAB LIGHT CHAIN; COMPND 13 CHAIN: L; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM 3D7; SOURCE 3 ORGANISM_TAXID: 36329; SOURCE 4 GENE: PF3D7_1133400; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; SOURCE 9 EXPRESSION_SYSTEM_CELL: KIDNEY (EMBRYONIC); SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PHL-SEC; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_COMMON: HUMAN; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; SOURCE 19 EXPRESSION_SYSTEM_CELL: KIDNEY (EMBRYONIC); SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PHL-SEC; SOURCE 21 MOL_ID: 3; SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 23 ORGANISM_COMMON: HUMAN; SOURCE 24 ORGANISM_TAXID: 9606; SOURCE 25 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 26 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 27 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 28 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; SOURCE 29 EXPRESSION_SYSTEM_CELL: KIDNEY (EMBRYONIC); SOURCE 30 EXPRESSION_SYSTEM_PLASMID: PHL-SEC KEYWDS APICAL MEMBRANE ANTIGEN 1, PLASMODIUM, MALARIA, ANTIGEN-ANTIBODY KEYWDS 2 COMPLEX, STRUCTURAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR P.N.PATEL,W.K.TANG,N.H.TOLIA REVDAT 1 12-MAR-25 9BJG 0 JRNL AUTH P.N.PATEL,A.DIOUF,T.H.DICKEY,W.K.TANG,C.S.HOPP,B.TRAORE, JRNL AUTH 2 C.A.LONG,K.MIURA,P.D.CROMPTON,N.H.TOLIA JRNL TITL A STRAIN-TRANSCENDING ANTI-AMA1 HUMAN MONOCLONAL ANTIBODY JRNL TITL 2 NEUTRALIZES MALARIA PARASITES INDEPENDENT OF DIRECT RON2L JRNL TITL 3 RECEPTOR BLOCKADE JRNL REF CELL REP MED 2025 JRNL REFN ESSN 2666-3791 JRNL DOI 10.1016/J.XCRM.2025.101985 REMARK 2 REMARK 2 RESOLUTION. 2.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21_5207 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.88 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.020 REMARK 3 COMPLETENESS FOR RANGE (%) : 92.3 REMARK 3 NUMBER OF REFLECTIONS : 24131 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.201 REMARK 3 R VALUE (WORKING SET) : 0.199 REMARK 3 FREE R VALUE : 0.232 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.640 REMARK 3 FREE R VALUE TEST SET COUNT : 1843 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 19.8800 - 6.7400 0.98 1954 158 0.1888 0.2094 REMARK 3 2 6.7300 - 5.3800 0.97 1858 152 0.1865 0.1940 REMARK 3 3 5.3800 - 4.7100 0.98 1857 154 0.1521 0.1679 REMARK 3 4 4.7100 - 4.2900 0.97 1805 154 0.1459 0.1805 REMARK 3 5 4.2900 - 3.9800 0.97 1802 144 0.1679 0.2140 REMARK 3 6 3.9800 - 3.7500 0.97 1784 148 0.1931 0.2474 REMARK 3 7 3.7500 - 3.5600 0.94 1734 141 0.2007 0.2518 REMARK 3 8 3.5600 - 3.4100 0.94 1740 140 0.2265 0.2569 REMARK 3 9 3.4100 - 3.2800 0.93 1695 138 0.2529 0.2933 REMARK 3 10 3.2800 - 3.1600 0.89 1599 144 0.2597 0.3100 REMARK 3 11 3.1600 - 3.0700 0.85 1570 132 0.2819 0.3220 REMARK 3 12 3.0700 - 2.9800 0.82 1490 120 0.2945 0.3228 REMARK 3 13 2.9800 - 2.9000 0.77 1400 118 0.3174 0.3651 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) : 0.364 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.858 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 52.80 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.00 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 5714 REMARK 3 ANGLE : 0.587 7757 REMARK 3 CHIRALITY : 0.045 841 REMARK 3 PLANARITY : 0.005 1011 REMARK 3 DIHEDRAL : 5.152 768 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 15 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ( CHAIN A AND RESID 108:144 ) REMARK 3 ORIGIN FOR THE GROUP (A): -39.294 34.412 35.296 REMARK 3 T TENSOR REMARK 3 T11: 0.3899 T22: 0.6711 REMARK 3 T33: 0.3362 T12: 0.0386 REMARK 3 T13: -0.0582 T23: -0.0646 REMARK 3 L TENSOR REMARK 3 L11: 3.1174 L22: 5.9550 REMARK 3 L33: 4.8721 L12: 1.1735 REMARK 3 L13: -1.6302 L23: -1.8648 REMARK 3 S TENSOR REMARK 3 S11: 0.0243 S12: -0.4510 S13: -0.0258 REMARK 3 S21: 0.5316 S22: -0.2276 S23: -0.3447 REMARK 3 S31: -0.0199 S32: 1.0037 S33: 0.1716 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: ( CHAIN A AND RESID 145:201 ) REMARK 3 ORIGIN FOR THE GROUP (A): -43.313 38.582 14.674 REMARK 3 T TENSOR REMARK 3 T11: 0.3020 T22: 0.4713 REMARK 3 T33: 0.3272 T12: -0.0402 REMARK 3 T13: -0.0995 T23: -0.0217 REMARK 3 L TENSOR REMARK 3 L11: 4.2187 L22: 6.2250 REMARK 3 L33: 6.4859 L12: -0.2544 REMARK 3 L13: 0.2408 L23: 1.3723 REMARK 3 S TENSOR REMARK 3 S11: -0.0761 S12: 0.0516 S13: 0.7086 REMARK 3 S21: -0.3659 S22: 0.0182 S23: -0.1412 REMARK 3 S31: -0.8409 S32: 0.0107 S33: 0.0295 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: ( CHAIN A AND RESID 202:297 ) REMARK 3 ORIGIN FOR THE GROUP (A): -39.843 34.516 19.808 REMARK 3 T TENSOR REMARK 3 T11: 0.2648 T22: 0.5043 REMARK 3 T33: 0.2800 T12: -0.0059 REMARK 3 T13: 0.0134 T23: -0.0581 REMARK 3 L TENSOR REMARK 3 L11: 2.9956 L22: 5.2228 REMARK 3 L33: 3.0882 L12: 0.0866 REMARK 3 L13: 0.6926 L23: -0.3245 REMARK 3 S TENSOR REMARK 3 S11: -0.1587 S12: 0.1848 S13: -0.1995 REMARK 3 S21: -0.0661 S22: 0.1001 S23: -0.2368 REMARK 3 S31: -0.1510 S32: 0.2423 S33: 0.0228 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: ( CHAIN A AND RESID 298:438 ) REMARK 3 ORIGIN FOR THE GROUP (A): -54.063 31.934 39.731 REMARK 3 T TENSOR REMARK 3 T11: 0.4023 T22: 0.5764 REMARK 3 T33: 0.2742 T12: 0.0020 REMARK 3 T13: -0.0239 T23: -0.0640 REMARK 3 L TENSOR REMARK 3 L11: 2.9918 L22: 4.5423 REMARK 3 L33: 4.2188 L12: 0.0567 REMARK 3 L13: -1.1925 L23: 0.0828 REMARK 3 S TENSOR REMARK 3 S11: 0.0600 S12: -0.4999 S13: 0.0464 REMARK 3 S21: 0.6713 S22: -0.1036 S23: 0.1029 REMARK 3 S31: 0.1942 S32: 0.0108 S33: 0.0727 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: ( CHAIN H AND RESID 1:33 ) REMARK 3 ORIGIN FOR THE GROUP (A): -52.482 6.841 6.682 REMARK 3 T TENSOR REMARK 3 T11: 0.4442 T22: 0.4109 REMARK 3 T33: 0.3039 T12: 0.0441 REMARK 3 T13: 0.0248 T23: 0.0551 REMARK 3 L TENSOR REMARK 3 L11: 5.7051 L22: 6.3422 REMARK 3 L33: 1.8191 L12: 4.8765 REMARK 3 L13: 1.4931 L23: 2.0862 REMARK 3 S TENSOR REMARK 3 S11: -0.0054 S12: 0.0854 S13: -0.3634 REMARK 3 S21: 0.1463 S22: -0.0811 S23: -0.3547 REMARK 3 S31: 0.0977 S32: -0.0540 S33: 0.0536 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: ( CHAIN H AND RESID 34:60 ) REMARK 3 ORIGIN FOR THE GROUP (A): -61.356 11.993 11.054 REMARK 3 T TENSOR REMARK 3 T11: 0.3817 T22: 0.3211 REMARK 3 T33: 0.3070 T12: 0.0004 REMARK 3 T13: 0.0847 T23: 0.0188 REMARK 3 L TENSOR REMARK 3 L11: 8.2217 L22: 7.4038 REMARK 3 L33: 5.5926 L12: -0.3015 REMARK 3 L13: 1.9269 L23: 0.0561 REMARK 3 S TENSOR REMARK 3 S11: 0.4529 S12: -0.4350 S13: 0.0296 REMARK 3 S21: 0.1190 S22: -0.2615 S23: 0.4232 REMARK 3 S31: 0.8662 S32: -0.1849 S33: -0.2257 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: ( CHAIN H AND RESID 61:178 ) REMARK 3 ORIGIN FOR THE GROUP (A): -61.443 6.170 -2.098 REMARK 3 T TENSOR REMARK 3 T11: 0.2809 T22: 0.2921 REMARK 3 T33: 0.3586 T12: 0.0217 REMARK 3 T13: 0.0374 T23: 0.0759 REMARK 3 L TENSOR REMARK 3 L11: 1.0619 L22: 2.1830 REMARK 3 L33: 3.0484 L12: 0.3043 REMARK 3 L13: 0.4683 L23: 2.3238 REMARK 3 S TENSOR REMARK 3 S11: 0.1118 S12: -0.0627 S13: -0.1027 REMARK 3 S21: 0.1158 S22: -0.1141 S23: 0.1007 REMARK 3 S31: 0.2390 S32: -0.1340 S33: 0.0275 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: ( CHAIN H AND RESID 179:229 ) REMARK 3 ORIGIN FOR THE GROUP (A): -62.265 -0.807 -23.389 REMARK 3 T TENSOR REMARK 3 T11: 0.4833 T22: 0.3804 REMARK 3 T33: 0.4353 T12: 0.0837 REMARK 3 T13: -0.0041 T23: -0.0145 REMARK 3 L TENSOR REMARK 3 L11: 2.3904 L22: 3.8566 REMARK 3 L33: 4.9409 L12: 1.1604 REMARK 3 L13: -0.4360 L23: -1.1625 REMARK 3 S TENSOR REMARK 3 S11: -0.0703 S12: 0.3195 S13: -0.3473 REMARK 3 S21: -0.4553 S22: -0.0938 S23: -0.3099 REMARK 3 S31: 0.4520 S32: 0.3445 S33: 0.0799 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: ( CHAIN L AND RESID 1:38 ) REMARK 3 ORIGIN FOR THE GROUP (A): -67.915 28.455 0.725 REMARK 3 T TENSOR REMARK 3 T11: 0.2921 T22: 0.2684 REMARK 3 T33: 0.3874 T12: -0.0421 REMARK 3 T13: -0.0359 T23: -0.0513 REMARK 3 L TENSOR REMARK 3 L11: 4.8541 L22: 2.3881 REMARK 3 L33: 5.9546 L12: -2.7816 REMARK 3 L13: 1.2535 L23: 1.4889 REMARK 3 S TENSOR REMARK 3 S11: -0.2532 S12: -0.1736 S13: -0.0466 REMARK 3 S21: -0.0719 S22: -0.2530 S23: 0.3450 REMARK 3 S31: -0.2532 S32: -0.5022 S33: 0.5418 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: ( CHAIN L AND RESID 39:61 ) REMARK 3 ORIGIN FOR THE GROUP (A): -55.424 26.553 -1.737 REMARK 3 T TENSOR REMARK 3 T11: 0.3510 T22: 0.4484 REMARK 3 T33: 0.3590 T12: 0.0031 REMARK 3 T13: 0.0328 T23: 0.0523 REMARK 3 L TENSOR REMARK 3 L11: 3.2881 L22: 3.8600 REMARK 3 L33: 4.2300 L12: 1.1045 REMARK 3 L13: 1.6388 L23: -0.8590 REMARK 3 S TENSOR REMARK 3 S11: -0.0830 S12: 0.4317 S13: 0.3194 REMARK 3 S21: -0.7337 S22: -0.0307 S23: -0.4284 REMARK 3 S31: -0.2686 S32: 0.8447 S33: 0.1391 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: ( CHAIN L AND RESID 62:90 ) REMARK 3 ORIGIN FOR THE GROUP (A): -62.972 30.021 -3.101 REMARK 3 T TENSOR REMARK 3 T11: 0.3609 T22: 0.3060 REMARK 3 T33: 0.3916 T12: 0.0171 REMARK 3 T13: -0.0323 T23: -0.0180 REMARK 3 L TENSOR REMARK 3 L11: 2.3740 L22: 3.6745 REMARK 3 L33: 5.4231 L12: -0.2910 REMARK 3 L13: 0.2080 L23: 1.3393 REMARK 3 S TENSOR REMARK 3 S11: -0.0407 S12: 0.0489 S13: 0.3955 REMARK 3 S21: -0.2072 S22: -0.3327 S23: 0.0977 REMARK 3 S31: -0.7894 S32: -0.0369 S33: 0.3971 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: ( CHAIN L AND RESID 91:102 ) REMARK 3 ORIGIN FOR THE GROUP (A): -67.069 21.513 8.915 REMARK 3 T TENSOR REMARK 3 T11: 0.2533 T22: 0.6192 REMARK 3 T33: 0.3601 T12: 0.0023 REMARK 3 T13: 0.0591 T23: 0.0016 REMARK 3 L TENSOR REMARK 3 L11: 2.9350 L22: 6.3667 REMARK 3 L33: 2.0373 L12: 0.3391 REMARK 3 L13: -0.9703 L23: 0.2585 REMARK 3 S TENSOR REMARK 3 S11: -0.0859 S12: 0.0969 S13: -0.0010 REMARK 3 S21: 0.1269 S22: -0.2886 S23: 0.8256 REMARK 3 S31: 0.2738 S32: -1.4350 S33: 0.4081 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: ( CHAIN L AND RESID 103:113 ) REMARK 3 ORIGIN FOR THE GROUP (A): -69.101 24.658 -22.003 REMARK 3 T TENSOR REMARK 3 T11: 0.7059 T22: 0.4789 REMARK 3 T33: 0.6319 T12: 0.1659 REMARK 3 T13: -0.1811 T23: -0.0649 REMARK 3 L TENSOR REMARK 3 L11: 5.0350 L22: 4.7063 REMARK 3 L33: 4.6979 L12: 1.7241 REMARK 3 L13: 0.2981 L23: 3.4731 REMARK 3 S TENSOR REMARK 3 S11: -0.3844 S12: -0.5545 S13: 1.1960 REMARK 3 S21: -0.5781 S22: 0.1960 S23: 0.5489 REMARK 3 S31: -0.5136 S32: -0.3703 S33: 0.1525 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: ( CHAIN L AND RESID 114:150 ) REMARK 3 ORIGIN FOR THE GROUP (A): -75.151 4.356 -27.568 REMARK 3 T TENSOR REMARK 3 T11: 0.5223 T22: 0.5706 REMARK 3 T33: 0.4457 T12: 0.0785 REMARK 3 T13: -0.1075 T23: 0.0087 REMARK 3 L TENSOR REMARK 3 L11: 2.8510 L22: 4.0982 REMARK 3 L33: 2.1027 L12: 3.0723 REMARK 3 L13: 0.9521 L23: 1.4394 REMARK 3 S TENSOR REMARK 3 S11: -0.0250 S12: 0.2375 S13: 0.1970 REMARK 3 S21: -0.5339 S22: -0.0195 S23: 0.6472 REMARK 3 S31: -0.0203 S32: -0.0121 S33: 0.0974 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: ( CHAIN L AND RESID 151:212 ) REMARK 3 ORIGIN FOR THE GROUP (A): -78.549 5.986 -28.016 REMARK 3 T TENSOR REMARK 3 T11: 0.5114 T22: 0.6150 REMARK 3 T33: 0.4836 T12: 0.0999 REMARK 3 T13: -0.1013 T23: -0.0341 REMARK 3 L TENSOR REMARK 3 L11: 3.4032 L22: 7.1012 REMARK 3 L33: 3.3390 L12: 2.4509 REMARK 3 L13: 0.5024 L23: 0.1335 REMARK 3 S TENSOR REMARK 3 S11: -0.0437 S12: 0.4940 S13: 0.1577 REMARK 3 S21: -0.9601 S22: 0.0051 S23: 0.9710 REMARK 3 S31: 0.2583 S32: -0.4821 S33: 0.0304 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 9BJG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-APR-24. REMARK 100 THE DEPOSITION ID IS D_1000283439. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-JUN-22 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 22-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26126 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900 REMARK 200 RESOLUTION RANGE LOW (A) : 19.880 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.3 REMARK 200 DATA REDUNDANCY : 10.10 REMARK 200 R MERGE (I) : 0.25850 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.98 REMARK 200 COMPLETENESS FOR SHELL (%) : 77.5 REMARK 200 DATA REDUNDANCY IN SHELL : 10.00 REMARK 200 R MERGE FOR SHELL (I) : 1.59400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.590 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX 1.20.1-4487 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 61.39 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.19 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CALCIUM ACETATE, 0.1 M REMARK 280 IMIDAZOLE, 20% PEG 1000, PH 8.0, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 291.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1 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 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+1/3 REMARK 290 6555 -X,-X+Y,-Z+2/3 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 152.01000 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 76.00500 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 76.00500 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 152.01000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5450 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 31550 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 GLU A 101 REMARK 465 THR A 102 REMARK 465 GLY A 103 REMARK 465 ASN A 104 REMARK 465 TYR A 105 REMARK 465 MET A 106 REMARK 465 GLY A 107 REMARK 465 ASN A 173 REMARK 465 GLN A 174 REMARK 465 TYR A 175 REMARK 465 PRO A 260 REMARK 465 ARG A 261 REMARK 465 TYR A 262 REMARK 465 CYS A 263 REMARK 465 ASN A 264 REMARK 465 LYS A 265 REMARK 465 ASP A 266 REMARK 465 GLU A 267 REMARK 465 SER A 268 REMARK 465 LYS A 269 REMARK 465 ARG A 270 REMARK 465 ASN A 271 REMARK 465 SER A 272 REMARK 465 MET A 273 REMARK 465 GLN A 352 REMARK 465 TYR A 353 REMARK 465 GLU A 354 REMARK 465 GLN A 355 REMARK 465 HIS A 356 REMARK 465 LEU A 357 REMARK 465 THR A 358 REMARK 465 ASP A 359 REMARK 465 TYR A 360 REMARK 465 GLU A 361 REMARK 465 LYS A 362 REMARK 465 ILE A 363 REMARK 465 LYS A 364 REMARK 465 GLU A 365 REMARK 465 GLY A 366 REMARK 465 PHE A 367 REMARK 465 LYS A 368 REMARK 465 ASN A 369 REMARK 465 LYS A 370 REMARK 465 ASN A 371 REMARK 465 ALA A 372 REMARK 465 ALA A 373 REMARK 465 MET A 374 REMARK 465 ILE A 375 REMARK 465 LYS A 376 REMARK 465 SER A 377 REMARK 465 ALA A 378 REMARK 465 PHE A 379 REMARK 465 LEU A 380 REMARK 465 PRO A 381 REMARK 465 THR A 382 REMARK 465 GLY A 383 REMARK 465 ALA A 384 REMARK 465 PHE A 385 REMARK 465 LYS A 386 REMARK 465 ALA A 387 REMARK 465 GLY A 439 REMARK 465 THR A 440 REMARK 465 LYS A 441 REMARK 465 HIS A 442 REMARK 465 HIS A 443 REMARK 465 HIS A 444 REMARK 465 HIS A 445 REMARK 465 HIS A 446 REMARK 465 HIS A 447 REMARK 465 MET H -2 REMARK 465 GLY H -1 REMARK 465 ILE H 0 REMARK 465 LYS H 230 REMARK 465 SER H 231 REMARK 465 CYS H 232 REMARK 465 ASP H 233 REMARK 465 LYS H 234 REMARK 465 THR H 235 REMARK 465 GLY H 236 REMARK 465 GLY H 237 REMARK 465 SER H 238 REMARK 465 HIS H 239 REMARK 465 HIS H 240 REMARK 465 HIS H 241 REMARK 465 HIS H 242 REMARK 465 HIS H 243 REMARK 465 HIS H 244 REMARK 465 MET L -2 REMARK 465 GLY L -1 REMARK 465 ILE L 0 REMARK 465 GLU L 213 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 SER A 146 10.86 -142.42 REMARK 500 ASN L 30 -116.47 52.34 REMARK 500 ALA L 50 19.81 56.84 REMARK 500 ALA L 51 -12.03 73.99 REMARK 500 SER L 52 -3.72 -141.49 REMARK 500 SER L 67 143.14 -172.06 REMARK 500 ALA L 84 -167.71 -168.03 REMARK 500 REMARK 500 REMARK: NULL REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE AUTHOR STATES THAT ALL N-LINKED GLYCOSYLATION SITES (NXS/T) REMARK 999 WERE MODIFIED BY SUBSTITUTING THE SERINE OR THREONINE RESIDUE WITH REMARK 999 AN ALANINE RESIDUE TO PREVENT N-LINKED GLYCOSYLATION. DBREF 9BJG A 104 438 UNP Q7KQK5 Q7KQK5_PLAF7 104 438 DBREF 9BJG H -2 244 PDB 9BJG 9BJG -2 244 DBREF 9BJG L -2 214 PDB 9BJG 9BJG -2 214 SEQADV 9BJG GLU A 101 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJG THR A 102 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJG GLY A 103 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJG ALA A 164 UNP Q7KQK5 THR 164 ENGINEERED MUTATION SEQADV 9BJG ALA A 288 UNP Q7KQK5 THR 288 ENGINEERED MUTATION SEQADV 9BJG ALA A 373 UNP Q7KQK5 SER 373 ENGINEERED MUTATION SEQADV 9BJG ALA A 423 UNP Q7KQK5 SER 423 ENGINEERED MUTATION SEQADV 9BJG ALA A 424 UNP Q7KQK5 SER 424 ENGINEERED MUTATION SEQADV 9BJG GLY A 439 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJG THR A 440 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJG LYS A 441 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJG HIS A 442 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJG HIS A 443 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJG HIS A 444 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJG HIS A 445 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJG HIS A 446 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJG HIS A 447 UNP Q7KQK5 EXPRESSION TAG SEQRES 1 A 347 GLU THR GLY ASN TYR MET GLY ASN PRO TRP THR GLU TYR SEQRES 2 A 347 MET ALA LYS TYR ASP ILE GLU GLU VAL HIS GLY SER GLY SEQRES 3 A 347 ILE ARG VAL ASP LEU GLY GLU ASP ALA GLU VAL ALA GLY SEQRES 4 A 347 THR GLN TYR ARG LEU PRO SER GLY LYS CYS PRO VAL PHE SEQRES 5 A 347 GLY LYS GLY ILE ILE ILE GLU ASN SER ASN THR ALA PHE SEQRES 6 A 347 LEU THR PRO VAL ALA THR GLY ASN GLN TYR LEU LYS ASP SEQRES 7 A 347 GLY GLY PHE ALA PHE PRO PRO THR GLU PRO LEU MET SER SEQRES 8 A 347 PRO MET THR LEU ASP GLU MET ARG HIS PHE TYR LYS ASP SEQRES 9 A 347 ASN LYS TYR VAL LYS ASN LEU ASP GLU LEU THR LEU CYS SEQRES 10 A 347 SER ARG HIS ALA GLY ASN MET ILE PRO ASP ASN ASP LYS SEQRES 11 A 347 ASN SER ASN TYR LYS TYR PRO ALA VAL TYR ASP ASP LYS SEQRES 12 A 347 ASP LYS LYS CYS HIS ILE LEU TYR ILE ALA ALA GLN GLU SEQRES 13 A 347 ASN ASN GLY PRO ARG TYR CYS ASN LYS ASP GLU SER LYS SEQRES 14 A 347 ARG ASN SER MET PHE CYS PHE ARG PRO ALA LYS ASP ILE SEQRES 15 A 347 SER PHE GLN ASN TYR ALA TYR LEU SER LYS ASN VAL VAL SEQRES 16 A 347 ASP ASN TRP GLU LYS VAL CYS PRO ARG LYS ASN LEU GLN SEQRES 17 A 347 ASN ALA LYS PHE GLY LEU TRP VAL ASP GLY ASN CYS GLU SEQRES 18 A 347 ASP ILE PRO HIS VAL ASN GLU PHE PRO ALA ILE ASP LEU SEQRES 19 A 347 PHE GLU CYS ASN LYS LEU VAL PHE GLU LEU SER ALA SER SEQRES 20 A 347 ASP GLN PRO LYS GLN TYR GLU GLN HIS LEU THR ASP TYR SEQRES 21 A 347 GLU LYS ILE LYS GLU GLY PHE LYS ASN LYS ASN ALA ALA SEQRES 22 A 347 MET ILE LYS SER ALA PHE LEU PRO THR GLY ALA PHE LYS SEQRES 23 A 347 ALA ASP ARG TYR LYS SER HIS GLY LYS GLY TYR ASN TRP SEQRES 24 A 347 GLY ASN TYR ASN THR GLU THR GLN LYS CYS GLU ILE PHE SEQRES 25 A 347 ASN VAL LYS PRO THR CYS LEU ILE ASN ASN ALA ALA TYR SEQRES 26 A 347 ILE ALA THR THR ALA LEU SER HIS PRO ILE GLU VAL GLU SEQRES 27 A 347 GLY THR LYS HIS HIS HIS HIS HIS HIS SEQRES 1 H 247 MET GLY ILE GLN VAL GLN LEU VAL GLN SER GLY GLY GLY SEQRES 2 H 247 LEU VAL LYS PRO GLY GLY SER LEU ILE ILE SER CYS GLU SEQRES 3 H 247 GLY SER GLY TYR ARG PHE SER ASP TYR HIS MET SER TRP SEQRES 4 H 247 ILE ARG GLN VAL PRO GLY LYS GLY MET GLU TRP VAL ALA SEQRES 5 H 247 ASP ILE THR THR LYS GLY ASP GLN THR ALA TYR ALA ASP SEQRES 6 H 247 SER VAL ARG GLY ARG PHE THR VAL SER ARG ASP ASN ALA SEQRES 7 H 247 LYS ASN SER MET PHE LEU GLN MET ASN GLY LEU LYS VAL SEQRES 8 H 247 GLU ASP THR ALA VAL TYR PHE CYS GLY ARG ASP ARG PHE SEQRES 9 H 247 ARG GLY GLY TYR ASN TYR PRO SER ASP ILE TYR SER HIS SEQRES 10 H 247 ALA PRO ASP HIS TRP GLY GLN GLY GLN LEU VAL THR VAL SEQRES 11 H 247 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 12 H 247 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 13 H 247 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 14 H 247 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 15 H 247 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 16 H 247 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 17 H 247 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 18 H 247 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 19 H 247 CYS ASP LYS THR GLY GLY SER HIS HIS HIS HIS HIS HIS SEQRES 1 L 217 MET GLY ILE ASP ILE GLN MET THR GLN SER PRO SER THR SEQRES 2 L 217 LEU SER ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS SEQRES 3 L 217 ARG ALA SER GLN THR ILE ASN ASN TRP LEU ALA TRP TYR SEQRES 4 L 217 GLN GLN LYS PRO GLY ARG ALA PRO LYS VAL LEU ILE TYR SEQRES 5 L 217 ALA ALA SER ASP LEU ASP SER GLY VAL PRO SER ARG PHE SEQRES 6 L 217 SER ALA SER GLY SER GLY THR HIS PHE SER LEU THR ILE SEQRES 7 L 217 SER SER LEU GLN PRO ASP ASP PHE ALA THR TYR PHE CYS SEQRES 8 L 217 GLN GLN TYR ASN GLU PHE PRO VAL THR PHE GLY GLN GLY SEQRES 9 L 217 THR LYS LEU GLU LEU LYS ARG THR VAL ALA ALA PRO SER SEQRES 10 L 217 VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER SEQRES 11 L 217 GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR SEQRES 12 L 217 PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA SEQRES 13 L 217 LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN SEQRES 14 L 217 ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU SEQRES 15 L 217 THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR SEQRES 16 L 217 ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL SEQRES 17 L 217 THR LYS SER PHE ASN ARG GLY GLU CYS FORMUL 4 HOH *15(H2 O) HELIX 1 AA1 GLU A 112 TYR A 117 5 6 HELIX 2 AA2 ASP A 118 HIS A 123 1 6 HELIX 3 AA3 LEU A 195 TYR A 202 1 8 HELIX 4 AA4 ASN A 205 LYS A 209 5 5 HELIX 5 AA5 ASP A 212 ASN A 223 1 12 HELIX 6 AA6 ASN A 297 CYS A 302 1 6 HELIX 7 AA7 ASP A 333 SER A 345 1 13 HELIX 8 AA8 ARG H 28 TYR H 32 5 5 HELIX 9 AA9 ASN H 74 LYS H 76 5 3 HELIX 10 AB1 LYS H 87 THR H 91 5 5 HELIX 11 AB2 SER H 172 ALA H 174 5 3 HELIX 12 AB3 SER H 203 LEU H 205 5 3 HELIX 13 AB4 LYS H 217 ASN H 220 5 4 HELIX 14 AB5 GLN L 79 PHE L 83 5 5 HELIX 15 AB6 SER L 121 LYS L 126 1 6 HELIX 16 AB7 LYS L 183 GLU L 187 1 5 SHEET 1 AA1 2 GLU A 133 VAL A 137 0 SHEET 2 AA1 2 THR A 140 LEU A 144 -1 O TYR A 142 N ALA A 135 SHEET 1 AA2 5 VAL A 151 PHE A 152 0 SHEET 2 AA2 5 TYR A 287 LEU A 290 -1 O TYR A 289 N VAL A 151 SHEET 3 AA2 5 ALA A 238 ASP A 241 -1 N ALA A 238 O LEU A 290 SHEET 4 AA2 5 LYS A 246 ILE A 249 -1 O HIS A 248 N VAL A 239 SHEET 5 AA2 5 MET A 193 THR A 194 -1 N MET A 193 O CYS A 247 SHEET 1 AA3 2 LYS A 154 ILE A 157 0 SHEET 2 AA3 2 ARG A 277 LYS A 280 -1 O ARG A 277 N ILE A 157 SHEET 1 AA4 5 LEU A 307 GLN A 308 0 SHEET 2 AA4 5 TYR A 425 THR A 429 -1 O ALA A 427 N LEU A 307 SHEET 3 AA4 5 TRP A 399 ASN A 403 -1 N GLY A 400 O THR A 428 SHEET 4 AA4 5 LYS A 408 PHE A 412 -1 O GLU A 410 N ASN A 401 SHEET 5 AA4 5 ASN A 327 PRO A 330 -1 N PHE A 329 O CYS A 409 SHEET 1 AA5 3 ASN A 319 ASP A 322 0 SHEET 2 AA5 3 LYS A 311 VAL A 316 -1 N LEU A 314 O GLU A 321 SHEET 3 AA5 3 CYS A 418 ILE A 420 -1 O ILE A 420 N LYS A 311 SHEET 1 AA6 4 GLN H 3 SER H 7 0 SHEET 2 AA6 4 LEU H 18 SER H 25 -1 O GLU H 23 N VAL H 5 SHEET 3 AA6 4 SER H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 AA6 4 PHE H 68 ASP H 73 -1 N SER H 71 O PHE H 80 SHEET 1 AA7 6 LEU H 11 VAL H 12 0 SHEET 2 AA7 6 GLN H 123 VAL H 127 1 O THR H 126 N VAL H 12 SHEET 3 AA7 6 ALA H 92 ASP H 99 -1 N TYR H 94 O GLN H 123 SHEET 4 AA7 6 HIS H 33 GLN H 39 -1 N ILE H 37 O PHE H 95 SHEET 5 AA7 6 MET H 45 ILE H 51 -1 O VAL H 48 N TRP H 36 SHEET 6 AA7 6 THR H 58 TYR H 60 -1 O ALA H 59 N ASP H 50 SHEET 1 AA8 2 PHE H 101 ASN H 106 0 SHEET 2 AA8 2 ILE H 111 ALA H 115 -1 O SER H 113 N GLY H 104 SHEET 1 AA9 4 SER H 136 LEU H 140 0 SHEET 2 AA9 4 THR H 151 TYR H 161 -1 O LEU H 157 N PHE H 138 SHEET 3 AA9 4 TYR H 192 PRO H 201 -1 O VAL H 200 N ALA H 152 SHEET 4 AA9 4 HIS H 180 THR H 181 -1 N HIS H 180 O VAL H 197 SHEET 1 AB1 4 THR H 147 SER H 148 0 SHEET 2 AB1 4 THR H 151 TYR H 161 -1 O THR H 151 N SER H 148 SHEET 3 AB1 4 TYR H 192 PRO H 201 -1 O VAL H 200 N ALA H 152 SHEET 4 AB1 4 VAL H 185 LEU H 186 -1 N VAL H 185 O SER H 193 SHEET 1 AB2 3 SER H 169 TRP H 170 0 SHEET 2 AB2 3 TYR H 210 HIS H 216 -1 O ASN H 213 N SER H 169 SHEET 3 AB2 3 THR H 221 VAL H 227 -1 O THR H 221 N HIS H 216 SHEET 1 AB3 4 MET L 4 SER L 7 0 SHEET 2 AB3 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AB3 4 HIS L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AB3 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AB4 6 THR L 10 ALA L 13 0 SHEET 2 AB4 6 THR L 102 LEU L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AB4 6 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB4 6 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AB4 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AB4 6 ASP L 53 LEU L 54 -1 O ASP L 53 N TYR L 49 SHEET 1 AB5 4 THR L 10 ALA L 13 0 SHEET 2 AB5 4 THR L 102 LEU L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AB5 4 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB5 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB6 4 SER L 114 PHE L 118 0 SHEET 2 AB6 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AB6 4 TYR L 173 SER L 182 -1 O LEU L 179 N VAL L 132 SHEET 4 AB6 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176 SHEET 1 AB7 4 ALA L 153 LEU L 154 0 SHEET 2 AB7 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB7 4 VAL L 191 THR L 197 -1 O ALA L 193 N LYS L 149 SHEET 4 AB7 4 VAL L 205 ASN L 210 -1 O LYS L 207 N CYS L 194 SSBOND 1 CYS A 149 CYS A 302 1555 1555 2.03 SSBOND 2 CYS A 217 CYS A 247 1555 1555 2.04 SSBOND 3 CYS A 320 CYS A 418 1555 1555 2.04 SSBOND 4 CYS A 337 CYS A 409 1555 1555 2.04 SSBOND 5 CYS H 22 CYS H 96 1555 1555 2.05 SSBOND 6 CYS H 156 CYS H 212 1555 1555 2.04 SSBOND 7 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 8 CYS L 134 CYS L 194 1555 1555 2.03 CISPEP 1 GLU A 187 PRO A 188 0 1.77 CISPEP 2 SER A 191 PRO A 192 0 -5.02 CISPEP 3 TYR H 107 PRO H 108 0 5.41 CISPEP 4 PHE H 162 PRO H 163 0 -11.03 CISPEP 5 GLU H 164 PRO H 165 0 0.72 CISPEP 6 SER L 7 PRO L 8 0 -5.68 CISPEP 7 PHE L 94 PRO L 95 0 1.30 CISPEP 8 TYR L 140 PRO L 141 0 -0.44 CRYST1 93.236 93.236 228.015 90.00 90.00 120.00 P 32 2 1 6 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 0.010725 0.006192 0.000000 0.00000 SCALE2 0.000000 0.012385 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004386 0.00000