HEADER STRUCTURAL PROTEIN 25-APR-24 9BJH TITLE CRYSTAL STRUCTURE OF NEUTRALIZING HUMAN MONOCLONAL ANTIBODY 75C8 IN TITLE 2 COMPLEX WITH AMA1 DI-DII COMPND MOL_ID: 1; COMPND 2 MOLECULE: APICAL MEMBRANE ANTIGEN 1; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: MEROZOITE SURFACE ANTIGEN; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: 75C8 FAB HEAVY CHAIN; COMPND 9 CHAIN: H, I; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: 75C8 FAB LIGHT CHAIN; COMPND 13 CHAIN: L, M; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM 3D7; SOURCE 3 ORGANISM_TAXID: 36329; SOURCE 4 STRAIN: ISOLATE 3D7; SOURCE 5 GENE: PF3D7_1133400; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; SOURCE 10 EXPRESSION_SYSTEM_CELL: KIDNEY (EMBRYONIC); SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PHL-SEC; 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: EXPI293F; SOURCE 20 EXPRESSION_SYSTEM_CELL: KIDNEY (EMBRYONIC); SOURCE 21 EXPRESSION_SYSTEM_PLASMID: PHL-SEC; SOURCE 22 MOL_ID: 3; SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 24 ORGANISM_COMMON: HUMAN; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 29 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; SOURCE 30 EXPRESSION_SYSTEM_CELL: KIDNEY (EMBRYONIC); SOURCE 31 EXPRESSION_SYSTEM_PLASMID: PHL-SEC KEYWDS APICAL MEMBRANE ANTIGEN 1, AMA1, PLASMODIUM, MALARIA, ANTIGEN- KEYWDS 2 ANTIBODY COMPLEX, STRUCTURAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR P.N.PATEL,W.K.TANG,N.H.TOLIA REVDAT 1 12-MAR-25 9BJH 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. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.2_4158 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) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.87 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.010 REMARK 3 COMPLETENESS FOR RANGE (%) : 86.6 REMARK 3 NUMBER OF REFLECTIONS : 38941 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.213 REMARK 3 R VALUE (WORKING SET) : 0.211 REMARK 3 FREE R VALUE : 0.253 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.780 REMARK 3 FREE R VALUE TEST SET COUNT : 1860 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 19.8700 - 6.5100 0.93 3038 154 0.1914 0.1910 REMARK 3 2 6.5100 - 5.2000 0.95 3147 162 0.1961 0.2167 REMARK 3 3 5.2000 - 4.5500 0.92 3025 156 0.1634 0.2135 REMARK 3 4 4.5500 - 4.1400 0.89 2969 141 0.1746 0.2351 REMARK 3 5 4.1400 - 3.8400 0.91 2995 150 0.1952 0.2226 REMARK 3 6 3.8400 - 3.6200 0.92 2969 157 0.2100 0.2603 REMARK 3 7 3.6200 - 3.4400 0.91 2973 150 0.2128 0.3035 REMARK 3 8 3.4400 - 3.2900 0.89 2962 152 0.2413 0.2700 REMARK 3 9 3.2900 - 3.1600 0.87 2902 141 0.2545 0.3342 REMARK 3 10 3.1600 - 3.0500 0.76 2507 120 0.2730 0.3170 REMARK 3 11 3.0500 - 2.9600 0.79 2598 127 0.2752 0.3507 REMARK 3 12 2.9600 - 2.8700 0.77 2453 130 0.2915 0.3240 REMARK 3 13 2.8700 - 2.8000 0.74 2537 120 0.3105 0.3832 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) : 0.395 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.152 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 43.06 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.17 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 : 0.002 11494 REMARK 3 ANGLE : 0.473 15645 REMARK 3 CHIRALITY : 0.043 1725 REMARK 3 PLANARITY : 0.004 2023 REMARK 3 DIHEDRAL : 10.772 4175 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 32 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 108 THROUGH 144 ) REMARK 3 ORIGIN FOR THE GROUP (A): -30.0715 12.3725 -2.6501 REMARK 3 T TENSOR REMARK 3 T11: 0.2982 T22: 0.4172 REMARK 3 T33: 0.3470 T12: 0.1113 REMARK 3 T13: 0.0117 T23: -0.0392 REMARK 3 L TENSOR REMARK 3 L11: 2.8105 L22: 4.2465 REMARK 3 L33: 3.8925 L12: 0.2220 REMARK 3 L13: 0.1462 L23: -1.2076 REMARK 3 S TENSOR REMARK 3 S11: -0.2056 S12: -0.3551 S13: 0.2850 REMARK 3 S21: 1.0691 S22: -0.1283 S23: -0.2601 REMARK 3 S31: -1.3544 S32: -0.5453 S33: -0.2682 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 145 THROUGH 201 ) REMARK 3 ORIGIN FOR THE GROUP (A): -32.7994 -8.7238 -4.5144 REMARK 3 T TENSOR REMARK 3 T11: 0.3209 T22: 0.3606 REMARK 3 T33: 0.3508 T12: 0.0548 REMARK 3 T13: 0.0101 T23: 0.0677 REMARK 3 L TENSOR REMARK 3 L11: 3.7113 L22: 4.0493 REMARK 3 L33: 3.3657 L12: 0.8340 REMARK 3 L13: -0.7531 L23: -0.3400 REMARK 3 S TENSOR REMARK 3 S11: -0.1465 S12: -0.2781 S13: -0.5539 REMARK 3 S21: 0.3248 S22: 0.1252 S23: 0.1276 REMARK 3 S31: 0.2848 S32: -0.1417 S33: 0.0058 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 202 THROUGH 264 ) REMARK 3 ORIGIN FOR THE GROUP (A): -36.2205 -2.9980 -1.7117 REMARK 3 T TENSOR REMARK 3 T11: 0.3849 T22: 0.2927 REMARK 3 T33: 0.3822 T12: 0.0078 REMARK 3 T13: 0.0395 T23: 0.0650 REMARK 3 L TENSOR REMARK 3 L11: 5.5414 L22: 3.9974 REMARK 3 L33: 4.5899 L12: 0.1278 REMARK 3 L13: -0.5929 L23: -0.0589 REMARK 3 S TENSOR REMARK 3 S11: -0.0343 S12: -0.3723 S13: 0.0737 REMARK 3 S21: 0.5074 S22: 0.0678 S23: 0.2229 REMARK 3 S31: 0.1485 S32: -0.4173 S33: -0.0051 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 265 THROUGH 290 ) REMARK 3 ORIGIN FOR THE GROUP (A): -22.3913 -4.2805 -8.9577 REMARK 3 T TENSOR REMARK 3 T11: 0.3693 T22: 0.2590 REMARK 3 T33: 0.2829 T12: 0.0249 REMARK 3 T13: 0.0080 T23: 0.1122 REMARK 3 L TENSOR REMARK 3 L11: 5.7683 L22: 3.9411 REMARK 3 L33: 5.2425 L12: 0.9729 REMARK 3 L13: 0.1413 L23: 1.1230 REMARK 3 S TENSOR REMARK 3 S11: 0.1440 S12: -0.2165 S13: 0.2038 REMARK 3 S21: -0.2188 S22: -0.2677 S23: -0.2609 REMARK 3 S31: 0.4919 S32: 0.0937 S33: -0.1501 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 291 THROUGH 316 ) REMARK 3 ORIGIN FOR THE GROUP (A): -32.6429 14.5536 -14.8359 REMARK 3 T TENSOR REMARK 3 T11: 0.4639 T22: 0.4003 REMARK 3 T33: 0.6178 T12: 0.0944 REMARK 3 T13: -0.0263 T23: 0.0306 REMARK 3 L TENSOR REMARK 3 L11: 0.0931 L22: 3.5175 REMARK 3 L33: 2.0325 L12: 0.1629 REMARK 3 L13: -0.1192 L23: -2.2333 REMARK 3 S TENSOR REMARK 3 S11: 0.2100 S12: 0.2098 S13: 0.2086 REMARK 3 S21: -0.1071 S22: 0.0015 S23: 0.4786 REMARK 3 S31: -0.5353 S32: -0.9025 S33: -0.4242 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 317 THROUGH 438 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.1040 14.3708 -15.2349 REMARK 3 T TENSOR REMARK 3 T11: 0.3760 T22: 0.2481 REMARK 3 T33: 0.4788 T12: 0.0588 REMARK 3 T13: -0.0307 T23: 0.0840 REMARK 3 L TENSOR REMARK 3 L11: 2.3943 L22: 0.8293 REMARK 3 L33: 2.9840 L12: 0.4007 REMARK 3 L13: -0.2695 L23: 0.3219 REMARK 3 S TENSOR REMARK 3 S11: -0.0032 S12: -0.0883 S13: 0.3808 REMARK 3 S21: -0.0875 S22: -0.0851 S23: -0.0697 REMARK 3 S31: -0.3450 S32: 0.0190 S33: 0.0826 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 108 THROUGH 163 ) REMARK 3 ORIGIN FOR THE GROUP (A): -28.7308 -63.1245 20.9663 REMARK 3 T TENSOR REMARK 3 T11: 0.2726 T22: 0.3881 REMARK 3 T33: 0.5025 T12: 0.0728 REMARK 3 T13: 0.0155 T23: 0.0133 REMARK 3 L TENSOR REMARK 3 L11: 3.4397 L22: 1.9440 REMARK 3 L33: 2.8986 L12: 1.2320 REMARK 3 L13: 0.6602 L23: 0.5396 REMARK 3 S TENSOR REMARK 3 S11: 0.0311 S12: 0.1565 S13: 0.0024 REMARK 3 S21: -0.1678 S22: -0.2516 S23: 0.0290 REMARK 3 S31: 0.2547 S32: -0.1093 S33: 0.1741 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 164 THROUGH 237 ) REMARK 3 ORIGIN FOR THE GROUP (A): -40.6577 -49.0249 18.6463 REMARK 3 T TENSOR REMARK 3 T11: 0.3556 T22: 0.4519 REMARK 3 T33: 0.4469 T12: 0.0765 REMARK 3 T13: -0.0530 T23: 0.0524 REMARK 3 L TENSOR REMARK 3 L11: 1.7490 L22: 3.1439 REMARK 3 L33: 6.1912 L12: -0.7735 REMARK 3 L13: 1.8642 L23: 0.3795 REMARK 3 S TENSOR REMARK 3 S11: -0.0349 S12: 0.2514 S13: 0.1353 REMARK 3 S21: -0.4719 S22: -0.1233 S23: 0.5055 REMARK 3 S31: -0.2045 S32: -0.4432 S33: 0.1429 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 238 THROUGH 290 ) REMARK 3 ORIGIN FOR THE GROUP (A): -25.2782 -50.6839 23.4876 REMARK 3 T TENSOR REMARK 3 T11: 0.3107 T22: 0.2770 REMARK 3 T33: 0.3684 T12: 0.0779 REMARK 3 T13: -0.0258 T23: 0.0792 REMARK 3 L TENSOR REMARK 3 L11: 4.0183 L22: 4.8507 REMARK 3 L33: 6.2877 L12: -0.1585 REMARK 3 L13: -1.4079 L23: 0.0194 REMARK 3 S TENSOR REMARK 3 S11: 0.1427 S12: 0.1625 S13: 0.4928 REMARK 3 S21: -0.2630 S22: -0.0416 S23: -0.4100 REMARK 3 S31: -0.0028 S32: 0.1339 S33: -0.0762 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 291 THROUGH 438 ) REMARK 3 ORIGIN FOR THE GROUP (A): -23.2049 -69.6442 32.0281 REMARK 3 T TENSOR REMARK 3 T11: 0.3262 T22: 0.2878 REMARK 3 T33: 0.5130 T12: -0.0276 REMARK 3 T13: 0.0300 T23: 0.0336 REMARK 3 L TENSOR REMARK 3 L11: 3.0700 L22: 2.4831 REMARK 3 L33: 3.2790 L12: -0.1351 REMARK 3 L13: 0.7247 L23: -0.1961 REMARK 3 S TENSOR REMARK 3 S11: 0.0246 S12: 0.0196 S13: -0.5051 REMARK 3 S21: 0.0928 S22: -0.0895 S23: 0.2598 REMARK 3 S31: 0.3573 S32: -0.1847 S33: 0.1045 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 2 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.7735 -24.5654 -27.5156 REMARK 3 T TENSOR REMARK 3 T11: 0.4940 T22: 0.3557 REMARK 3 T33: 0.6391 T12: 0.0268 REMARK 3 T13: 0.1212 T23: 0.1786 REMARK 3 L TENSOR REMARK 3 L11: 2.5486 L22: 2.9468 REMARK 3 L33: 8.4371 L12: 0.2601 REMARK 3 L13: 3.9408 L23: 3.4430 REMARK 3 S TENSOR REMARK 3 S11: 0.1435 S12: 0.2702 S13: -0.1459 REMARK 3 S21: 0.5869 S22: 0.0493 S23: 0.6191 REMARK 3 S31: 0.9435 S32: 0.6537 S33: -0.3804 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 19 THROUGH 83 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.7507 -14.1985 -24.7687 REMARK 3 T TENSOR REMARK 3 T11: 0.3682 T22: 0.3195 REMARK 3 T33: 0.4893 T12: 0.0618 REMARK 3 T13: -0.0070 T23: 0.1403 REMARK 3 L TENSOR REMARK 3 L11: 1.7138 L22: 2.1696 REMARK 3 L33: 2.1906 L12: 0.6983 REMARK 3 L13: -0.0535 L23: 0.3908 REMARK 3 S TENSOR REMARK 3 S11: 0.0192 S12: 0.2226 S13: -0.1007 REMARK 3 S21: -0.1927 S22: -0.0308 S23: 0.0533 REMARK 3 S31: 0.0940 S32: 0.0714 S33: 0.0811 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 84 THROUGH 118 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.7313 -12.3031 -26.9958 REMARK 3 T TENSOR REMARK 3 T11: 0.2908 T22: 0.2441 REMARK 3 T33: 0.3940 T12: 0.0315 REMARK 3 T13: 0.0372 T23: 0.1143 REMARK 3 L TENSOR REMARK 3 L11: 1.7211 L22: 3.8827 REMARK 3 L33: 2.9590 L12: -0.0227 REMARK 3 L13: 0.2635 L23: 2.3209 REMARK 3 S TENSOR REMARK 3 S11: 0.0284 S12: -0.0521 S13: 0.0865 REMARK 3 S21: 0.5900 S22: 0.2177 S23: -0.3743 REMARK 3 S31: 0.2482 S32: 0.2508 S33: -0.1500 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 119 THROUGH 223 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.3635 -35.3078 -36.6566 REMARK 3 T TENSOR REMARK 3 T11: 0.4201 T22: 0.2661 REMARK 3 T33: 0.4699 T12: 0.0413 REMARK 3 T13: 0.0036 T23: 0.1014 REMARK 3 L TENSOR REMARK 3 L11: 3.7282 L22: 1.4619 REMARK 3 L33: 0.9448 L12: -0.3004 REMARK 3 L13: -0.5788 L23: 0.2499 REMARK 3 S TENSOR REMARK 3 S11: 0.1649 S12: -0.3300 S13: -0.4356 REMARK 3 S21: 0.0674 S22: -0.1338 S23: -0.1175 REMARK 3 S31: 0.1282 S32: 0.2213 S33: -0.0558 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 2 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.8439 -30.6273 44.5747 REMARK 3 T TENSOR REMARK 3 T11: 0.5067 T22: 0.1626 REMARK 3 T33: 0.9668 T12: 0.1931 REMARK 3 T13: -0.2632 T23: 0.1989 REMARK 3 L TENSOR REMARK 3 L11: 2.4719 L22: 2.7676 REMARK 3 L33: 0.8940 L12: -1.7176 REMARK 3 L13: -0.7248 L23: 1.4557 REMARK 3 S TENSOR REMARK 3 S11: 0.0686 S12: 0.7512 S13: 0.6372 REMARK 3 S21: -0.6586 S22: 0.2132 S23: 0.1124 REMARK 3 S31: -0.3350 S32: 0.0498 S33: -0.2595 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 19 THROUGH 60 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.9467 -42.5222 41.4246 REMARK 3 T TENSOR REMARK 3 T11: 0.2922 T22: 0.2827 REMARK 3 T33: 0.3797 T12: 0.0079 REMARK 3 T13: -0.0303 T23: 0.0976 REMARK 3 L TENSOR REMARK 3 L11: 4.4904 L22: 4.2378 REMARK 3 L33: 3.1592 L12: -0.2174 REMARK 3 L13: -0.0753 L23: 0.8645 REMARK 3 S TENSOR REMARK 3 S11: -0.0906 S12: -0.0532 S13: 0.2632 REMARK 3 S21: 0.1140 S22: -0.0908 S23: 0.2649 REMARK 3 S31: 0.0194 S32: -0.1099 S33: 0.2277 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 61 THROUGH 108 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.5333 -41.4698 43.4521 REMARK 3 T TENSOR REMARK 3 T11: 0.2442 T22: 0.3417 REMARK 3 T33: 0.5273 T12: 0.0122 REMARK 3 T13: 0.0332 T23: 0.0646 REMARK 3 L TENSOR REMARK 3 L11: 2.0236 L22: 2.7789 REMARK 3 L33: 0.8260 L12: -0.9676 REMARK 3 L13: 0.8595 L23: 0.1147 REMARK 3 S TENSOR REMARK 3 S11: -0.1506 S12: 0.0142 S13: 0.1389 REMARK 3 S21: -0.0249 S22: -0.0056 S23: 0.2604 REMARK 3 S31: 0.0747 S32: -0.0007 S33: 0.2077 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 109 THROUGH 197 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.9029 -24.1594 53.8017 REMARK 3 T TENSOR REMARK 3 T11: 0.4419 T22: 0.4316 REMARK 3 T33: 0.9516 T12: 0.1234 REMARK 3 T13: -0.0893 T23: -0.0727 REMARK 3 L TENSOR REMARK 3 L11: 1.2838 L22: 1.7591 REMARK 3 L33: 1.0609 L12: 1.3145 REMARK 3 L13: 0.1764 L23: 0.5786 REMARK 3 S TENSOR REMARK 3 S11: 0.0736 S12: -0.0868 S13: 0.2296 REMARK 3 S21: 0.1348 S22: 0.0711 S23: -0.3359 REMARK 3 S31: -0.1275 S32: 0.1187 S33: -0.0767 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 198 THROUGH 222 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.1208 -15.9399 48.3673 REMARK 3 T TENSOR REMARK 3 T11: 0.5181 T22: 0.5683 REMARK 3 T33: 1.1212 T12: 0.0003 REMARK 3 T13: 0.0017 T23: 0.2051 REMARK 3 L TENSOR REMARK 3 L11: 5.2748 L22: 0.5630 REMARK 3 L33: 2.0379 L12: -0.5345 REMARK 3 L13: -0.4704 L23: 1.2429 REMARK 3 S TENSOR REMARK 3 S11: -0.0700 S12: 0.7951 S13: 1.3059 REMARK 3 S21: -0.3738 S22: 0.1165 S23: -0.3843 REMARK 3 S31: -0.3895 S32: 0.5449 S33: -0.0436 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.2889 -1.4393 -40.6070 REMARK 3 T TENSOR REMARK 3 T11: 0.7066 T22: 0.3654 REMARK 3 T33: 0.5563 T12: -0.0340 REMARK 3 T13: 0.0760 T23: 0.1550 REMARK 3 L TENSOR REMARK 3 L11: 1.6122 L22: 0.5458 REMARK 3 L33: 2.5492 L12: -0.8690 REMARK 3 L13: -0.1439 L23: -0.6978 REMARK 3 S TENSOR REMARK 3 S11: 0.0145 S12: 0.1075 S13: 0.1000 REMARK 3 S21: -0.5759 S22: -0.0145 S23: 0.0459 REMARK 3 S31: -0.4786 S32: 0.0849 S33: -0.1089 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 19 THROUGH 30 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.7802 5.2813 -38.1981 REMARK 3 T TENSOR REMARK 3 T11: 0.6146 T22: 0.3276 REMARK 3 T33: 0.5328 T12: 0.0101 REMARK 3 T13: 0.0367 T23: 0.2059 REMARK 3 L TENSOR REMARK 3 L11: 5.8063 L22: 3.2132 REMARK 3 L33: 3.9267 L12: -2.2384 REMARK 3 L13: 3.7563 L23: -0.1927 REMARK 3 S TENSOR REMARK 3 S11: 0.0112 S12: 0.7452 S13: 0.3466 REMARK 3 S21: -0.7638 S22: 0.0847 S23: 0.1053 REMARK 3 S31: -0.3749 S32: -0.0222 S33: -0.1117 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 31 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.9690 -0.7931 -29.9061 REMARK 3 T TENSOR REMARK 3 T11: 0.3437 T22: 0.2518 REMARK 3 T33: 0.4539 T12: -0.0015 REMARK 3 T13: 0.0413 T23: 0.0728 REMARK 3 L TENSOR REMARK 3 L11: 3.9103 L22: 1.5539 REMARK 3 L33: 3.5486 L12: -1.9352 REMARK 3 L13: -0.6396 L23: 1.6278 REMARK 3 S TENSOR REMARK 3 S11: 0.0743 S12: -0.0617 S13: 0.1915 REMARK 3 S21: -0.1683 S22: 0.1425 S23: -0.3307 REMARK 3 S31: -0.2203 S32: 0.3142 S33: -0.1950 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 92 THROUGH 114 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.9394 -6.5087 -38.0243 REMARK 3 T TENSOR REMARK 3 T11: 0.4067 T22: 0.3236 REMARK 3 T33: 0.4312 T12: -0.0206 REMARK 3 T13: 0.0123 T23: 0.0994 REMARK 3 L TENSOR REMARK 3 L11: 3.2785 L22: 1.0399 REMARK 3 L33: 1.3457 L12: 0.8230 REMARK 3 L13: -1.0255 L23: -0.4236 REMARK 3 S TENSOR REMARK 3 S11: -0.0696 S12: 0.6918 S13: 0.3478 REMARK 3 S21: -0.2482 S22: 0.0576 S23: -0.1512 REMARK 3 S31: -0.0373 S32: -0.3003 S33: -0.0819 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 115 THROUGH 151 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.4308 -32.1495 -48.4891 REMARK 3 T TENSOR REMARK 3 T11: 0.2351 T22: 0.2771 REMARK 3 T33: 0.4615 T12: 0.0307 REMARK 3 T13: -0.0083 T23: 0.0649 REMARK 3 L TENSOR REMARK 3 L11: 3.1695 L22: 4.4289 REMARK 3 L33: 2.9040 L12: -0.0741 REMARK 3 L13: 0.9332 L23: 3.3033 REMARK 3 S TENSOR REMARK 3 S11: 0.1472 S12: 0.1400 S13: -0.3150 REMARK 3 S21: -0.1405 S22: -0.1822 S23: 0.0101 REMARK 3 S31: -0.0795 S32: 0.2279 S33: 0.0128 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 152 THROUGH 173 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.3579 -25.0099 -48.0651 REMARK 3 T TENSOR REMARK 3 T11: 0.4182 T22: 0.3601 REMARK 3 T33: 0.4026 T12: 0.0370 REMARK 3 T13: 0.0048 T23: 0.1241 REMARK 3 L TENSOR REMARK 3 L11: 2.6965 L22: 1.7351 REMARK 3 L33: 0.5725 L12: 0.7868 REMARK 3 L13: -0.0979 L23: 0.7426 REMARK 3 S TENSOR REMARK 3 S11: 0.3061 S12: 0.0262 S13: -0.1072 REMARK 3 S21: -0.0292 S22: -0.0019 S23: -0.2814 REMARK 3 S31: -0.1073 S32: 0.1343 S33: -0.1779 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 174 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.6861 -34.1448 -54.0467 REMARK 3 T TENSOR REMARK 3 T11: 0.4280 T22: 0.3649 REMARK 3 T33: 0.5058 T12: 0.0621 REMARK 3 T13: 0.0526 T23: 0.0656 REMARK 3 L TENSOR REMARK 3 L11: 4.1877 L22: 3.9618 REMARK 3 L33: 2.1471 L12: 1.9272 REMARK 3 L13: 0.2440 L23: 1.5849 REMARK 3 S TENSOR REMARK 3 S11: -0.2749 S12: 0.3691 S13: -0.6593 REMARK 3 S21: -0.6635 S22: 0.2526 S23: -0.2629 REMARK 3 S31: -0.0041 S32: 0.0730 S33: -0.0077 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'M' AND (RESID -1 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.0804 -53.9886 57.5233 REMARK 3 T TENSOR REMARK 3 T11: 0.6048 T22: 0.3053 REMARK 3 T33: 0.4132 T12: 0.1621 REMARK 3 T13: -0.0940 T23: 0.1217 REMARK 3 L TENSOR REMARK 3 L11: 2.4433 L22: 2.3923 REMARK 3 L33: 3.6357 L12: 1.3725 REMARK 3 L13: -1.1687 L23: -0.9663 REMARK 3 S TENSOR REMARK 3 S11: -0.0574 S12: 0.0960 S13: -0.1539 REMARK 3 S21: 0.6841 S22: 0.0880 S23: 0.0023 REMARK 3 S31: 0.5722 S32: -0.0118 S33: -0.0133 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 19 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.7029 -55.3679 48.1127 REMARK 3 T TENSOR REMARK 3 T11: 0.3842 T22: 0.2948 REMARK 3 T33: 0.4803 T12: 0.1189 REMARK 3 T13: -0.0265 T23: 0.0364 REMARK 3 L TENSOR REMARK 3 L11: 2.4873 L22: 1.2721 REMARK 3 L33: 3.5416 L12: 1.1953 REMARK 3 L13: 1.4007 L23: 0.4427 REMARK 3 S TENSOR REMARK 3 S11: 0.0437 S12: 0.1191 S13: -0.0535 REMARK 3 S21: 0.0586 S22: 0.1255 S23: -0.1924 REMARK 3 S31: 0.2244 S32: 0.3492 S33: -0.2177 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 92 THROUGH 114 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.8705 -48.8957 55.0066 REMARK 3 T TENSOR REMARK 3 T11: 0.5112 T22: 0.3532 REMARK 3 T33: 0.4086 T12: 0.1350 REMARK 3 T13: -0.0688 T23: 0.0672 REMARK 3 L TENSOR REMARK 3 L11: 1.9194 L22: 2.7284 REMARK 3 L33: 1.6814 L12: -0.6403 REMARK 3 L13: -1.2772 L23: -0.1684 REMARK 3 S TENSOR REMARK 3 S11: 0.1439 S12: -0.6432 S13: -0.0852 REMARK 3 S21: 0.5944 S22: 0.2284 S23: -0.4602 REMARK 3 S31: 0.2452 S32: -0.0618 S33: -0.1118 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 115 THROUGH 151 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.1056 -23.3410 65.8571 REMARK 3 T TENSOR REMARK 3 T11: 0.5582 T22: 0.6524 REMARK 3 T33: 0.8226 T12: 0.1396 REMARK 3 T13: -0.2156 T23: -0.1276 REMARK 3 L TENSOR REMARK 3 L11: 2.0983 L22: 4.2460 REMARK 3 L33: 2.2204 L12: 2.6038 REMARK 3 L13: 0.0992 L23: 1.0445 REMARK 3 S TENSOR REMARK 3 S11: 0.1102 S12: -0.1268 S13: 0.3325 REMARK 3 S21: 0.6052 S22: -0.0534 S23: -0.1880 REMARK 3 S31: 0.0067 S32: 0.1833 S33: -0.1183 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 152 THROUGH 175 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.3393 -30.9962 64.9015 REMARK 3 T TENSOR REMARK 3 T11: 0.3920 T22: 0.6066 REMARK 3 T33: 0.6343 T12: 0.0791 REMARK 3 T13: -0.1476 T23: 0.0538 REMARK 3 L TENSOR REMARK 3 L11: 0.5069 L22: 5.3173 REMARK 3 L33: 2.8428 L12: -1.2205 REMARK 3 L13: -0.3071 L23: 1.4731 REMARK 3 S TENSOR REMARK 3 S11: 0.1330 S12: -0.1327 S13: -0.0291 REMARK 3 S21: 0.3361 S22: -0.2159 S23: -0.4667 REMARK 3 S31: 0.0673 S32: -0.3243 S33: 0.0805 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: CHAIN 'M' AND (RESID 176 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.4030 -20.5716 72.3229 REMARK 3 T TENSOR REMARK 3 T11: 0.7762 T22: 0.6556 REMARK 3 T33: 1.0656 T12: 0.0907 REMARK 3 T13: -0.3377 T23: -0.1642 REMARK 3 L TENSOR REMARK 3 L11: 0.1232 L22: 5.2390 REMARK 3 L33: 2.0438 L12: -0.5135 REMARK 3 L13: -0.5502 L23: 2.5847 REMARK 3 S TENSOR REMARK 3 S11: -0.1831 S12: 0.1495 S13: -0.0695 REMARK 3 S21: 1.1506 S22: 0.0974 S23: -0.1822 REMARK 3 S31: 0.1180 S32: 0.3211 S33: 0.0526 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 9BJH 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_1000283440. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 17-SEP-22 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 9.5 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 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 : 41930 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 19.870 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 86.6 REMARK 200 DATA REDUNDANCY : 1.900 REMARK 200 R MERGE (I) : 0.11220 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 3.5200 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.87 REMARK 200 COMPLETENESS FOR SHELL (%) : 74.3 REMARK 200 DATA REDUNDANCY IN SHELL : 1.90 REMARK 200 R MERGE FOR SHELL (I) : 0.48180 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.690 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 (%): 53.40 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 50% (V/V) PEG 400, 0.2M SODIUM REMARK 280 CHLORIDE, 0.1M CHES, PH 9.5, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 291.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,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 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: TRIMERIC 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, I, M 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 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 GLU B 101 REMARK 465 THR B 102 REMARK 465 GLY B 103 REMARK 465 ASN B 104 REMARK 465 TYR B 105 REMARK 465 MET B 106 REMARK 465 GLY B 107 REMARK 465 GLY B 172 REMARK 465 ASN B 173 REMARK 465 GLN B 174 REMARK 465 TYR B 175 REMARK 465 LYS B 265 REMARK 465 ASP B 266 REMARK 465 GLU B 267 REMARK 465 SER B 268 REMARK 465 LYS B 269 REMARK 465 ARG B 270 REMARK 465 ASN B 271 REMARK 465 SER B 272 REMARK 465 MET B 273 REMARK 465 GLN B 352 REMARK 465 TYR B 353 REMARK 465 GLU B 354 REMARK 465 GLN B 355 REMARK 465 HIS B 356 REMARK 465 LEU B 357 REMARK 465 THR B 358 REMARK 465 ASP B 359 REMARK 465 TYR B 360 REMARK 465 GLU B 361 REMARK 465 LYS B 362 REMARK 465 ILE B 363 REMARK 465 LYS B 364 REMARK 465 GLU B 365 REMARK 465 GLY B 366 REMARK 465 PHE B 367 REMARK 465 LYS B 368 REMARK 465 ASN B 369 REMARK 465 LYS B 370 REMARK 465 ASN B 371 REMARK 465 ALA B 372 REMARK 465 ALA B 373 REMARK 465 MET B 374 REMARK 465 ILE B 375 REMARK 465 LYS B 376 REMARK 465 SER B 377 REMARK 465 ALA B 378 REMARK 465 PHE B 379 REMARK 465 LEU B 380 REMARK 465 PRO B 381 REMARK 465 THR B 382 REMARK 465 GLY B 383 REMARK 465 ALA B 384 REMARK 465 PHE B 385 REMARK 465 LYS B 386 REMARK 465 GLY B 439 REMARK 465 THR B 440 REMARK 465 LYS B 441 REMARK 465 HIS B 442 REMARK 465 HIS B 443 REMARK 465 HIS B 444 REMARK 465 HIS B 445 REMARK 465 HIS B 446 REMARK 465 HIS B 447 REMARK 465 MET H -2 REMARK 465 GLY H -1 REMARK 465 ILE H 0 REMARK 465 SER H 223 REMARK 465 CYS H 224 REMARK 465 ASP H 225 REMARK 465 LYS H 226 REMARK 465 THR H 227 REMARK 465 GLY H 228 REMARK 465 GLY H 229 REMARK 465 SER H 230 REMARK 465 HIS H 231 REMARK 465 HIS H 232 REMARK 465 HIS H 233 REMARK 465 HIS H 234 REMARK 465 HIS H 235 REMARK 465 HIS H 236 REMARK 465 MET I -2 REMARK 465 GLY I -1 REMARK 465 ILE I 0 REMARK 465 LYS I 137 REMARK 465 SER I 138 REMARK 465 THR I 139 REMARK 465 SER I 140 REMARK 465 LYS I 222 REMARK 465 SER I 223 REMARK 465 CYS I 224 REMARK 465 ASP I 225 REMARK 465 LYS I 226 REMARK 465 THR I 227 REMARK 465 GLY I 228 REMARK 465 GLY I 229 REMARK 465 SER I 230 REMARK 465 HIS I 231 REMARK 465 HIS I 232 REMARK 465 HIS I 233 REMARK 465 HIS I 234 REMARK 465 HIS I 235 REMARK 465 HIS I 236 REMARK 465 MET L -2 REMARK 465 GLY L -1 REMARK 465 ILE L 0 REMARK 465 CYS L 215 REMARK 465 MET M -2 REMARK 465 CYS M 215 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 TYR A 262 17.05 -142.60 REMARK 500 SER H 15 -1.93 72.67 REMARK 500 SER I 15 -3.07 73.60 REMARK 500 ILE I 48 -61.21 -95.13 REMARK 500 THR L 52 -16.67 74.70 REMARK 500 SER L 53 -15.77 -143.03 REMARK 500 ASP L 61 1.40 -69.23 REMARK 500 ALA L 85 -169.89 -167.76 REMARK 500 THR M 52 -14.63 75.41 REMARK 500 SER M 53 -4.39 -144.22 REMARK 500 ALA M 85 -172.69 -170.81 REMARK 500 ASP M 152 51.12 39.89 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 9BJH A 104 438 UNP Q7KQK5 Q7KQK5_PLAF7 104 438 DBREF 9BJH B 104 438 UNP Q7KQK5 Q7KQK5_PLAF7 104 438 DBREF 9BJH H -2 236 PDB 9BJH 9BJH -2 236 DBREF 9BJH I -2 236 PDB 9BJH 9BJH -2 236 DBREF 9BJH L -2 215 PDB 9BJH 9BJH -2 215 DBREF 9BJH M -2 215 PDB 9BJH 9BJH -2 215 SEQADV 9BJH GLU A 101 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJH THR A 102 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJH GLY A 103 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJH ALA A 164 UNP Q7KQK5 THR 164 ENGINEERED MUTATION SEQADV 9BJH ALA A 288 UNP Q7KQK5 THR 288 ENGINEERED MUTATION SEQADV 9BJH ALA A 373 UNP Q7KQK5 SER 373 ENGINEERED MUTATION SEQADV 9BJH ALA A 423 UNP Q7KQK5 SER 423 ENGINEERED MUTATION SEQADV 9BJH ALA A 424 UNP Q7KQK5 SER 424 ENGINEERED MUTATION SEQADV 9BJH GLY A 439 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJH THR A 440 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJH LYS A 441 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJH HIS A 442 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJH HIS A 443 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJH HIS A 444 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJH HIS A 445 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJH HIS A 446 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJH HIS A 447 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJH GLU B 101 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJH THR B 102 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJH GLY B 103 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJH ALA B 164 UNP Q7KQK5 THR 164 ENGINEERED MUTATION SEQADV 9BJH ALA B 288 UNP Q7KQK5 THR 288 ENGINEERED MUTATION SEQADV 9BJH ALA B 373 UNP Q7KQK5 SER 373 ENGINEERED MUTATION SEQADV 9BJH ALA B 423 UNP Q7KQK5 SER 423 ENGINEERED MUTATION SEQADV 9BJH ALA B 424 UNP Q7KQK5 SER 424 ENGINEERED MUTATION SEQADV 9BJH GLY B 439 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJH THR B 440 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJH LYS B 441 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJH HIS B 442 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJH HIS B 443 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJH HIS B 444 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJH HIS B 445 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJH HIS B 446 UNP Q7KQK5 EXPRESSION TAG SEQADV 9BJH HIS B 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 B 347 GLU THR GLY ASN TYR MET GLY ASN PRO TRP THR GLU TYR SEQRES 2 B 347 MET ALA LYS TYR ASP ILE GLU GLU VAL HIS GLY SER GLY SEQRES 3 B 347 ILE ARG VAL ASP LEU GLY GLU ASP ALA GLU VAL ALA GLY SEQRES 4 B 347 THR GLN TYR ARG LEU PRO SER GLY LYS CYS PRO VAL PHE SEQRES 5 B 347 GLY LYS GLY ILE ILE ILE GLU ASN SER ASN THR ALA PHE SEQRES 6 B 347 LEU THR PRO VAL ALA THR GLY ASN GLN TYR LEU LYS ASP SEQRES 7 B 347 GLY GLY PHE ALA PHE PRO PRO THR GLU PRO LEU MET SER SEQRES 8 B 347 PRO MET THR LEU ASP GLU MET ARG HIS PHE TYR LYS ASP SEQRES 9 B 347 ASN LYS TYR VAL LYS ASN LEU ASP GLU LEU THR LEU CYS SEQRES 10 B 347 SER ARG HIS ALA GLY ASN MET ILE PRO ASP ASN ASP LYS SEQRES 11 B 347 ASN SER ASN TYR LYS TYR PRO ALA VAL TYR ASP ASP LYS SEQRES 12 B 347 ASP LYS LYS CYS HIS ILE LEU TYR ILE ALA ALA GLN GLU SEQRES 13 B 347 ASN ASN GLY PRO ARG TYR CYS ASN LYS ASP GLU SER LYS SEQRES 14 B 347 ARG ASN SER MET PHE CYS PHE ARG PRO ALA LYS ASP ILE SEQRES 15 B 347 SER PHE GLN ASN TYR ALA TYR LEU SER LYS ASN VAL VAL SEQRES 16 B 347 ASP ASN TRP GLU LYS VAL CYS PRO ARG LYS ASN LEU GLN SEQRES 17 B 347 ASN ALA LYS PHE GLY LEU TRP VAL ASP GLY ASN CYS GLU SEQRES 18 B 347 ASP ILE PRO HIS VAL ASN GLU PHE PRO ALA ILE ASP LEU SEQRES 19 B 347 PHE GLU CYS ASN LYS LEU VAL PHE GLU LEU SER ALA SER SEQRES 20 B 347 ASP GLN PRO LYS GLN TYR GLU GLN HIS LEU THR ASP TYR SEQRES 21 B 347 GLU LYS ILE LYS GLU GLY PHE LYS ASN LYS ASN ALA ALA SEQRES 22 B 347 MET ILE LYS SER ALA PHE LEU PRO THR GLY ALA PHE LYS SEQRES 23 B 347 ALA ASP ARG TYR LYS SER HIS GLY LYS GLY TYR ASN TRP SEQRES 24 B 347 GLY ASN TYR ASN THR GLU THR GLN LYS CYS GLU ILE PHE SEQRES 25 B 347 ASN VAL LYS PRO THR CYS LEU ILE ASN ASN ALA ALA TYR SEQRES 26 B 347 ILE ALA THR THR ALA LEU SER HIS PRO ILE GLU VAL GLU SEQRES 27 B 347 GLY THR LYS HIS HIS HIS HIS HIS HIS SEQRES 1 H 239 MET GLY ILE GLN VAL GLN LEU ARG GLU SER GLY PRO HIS SEQRES 2 H 239 LEU VAL LYS PRO SER GLU THR LEU SER LEU THR CYS ASN SEQRES 3 H 239 VAL SER GLY GLY THR ILE ASN ARG TYR TYR TRP ASN TRP SEQRES 4 H 239 ILE ARG GLN ILE PRO GLY LYS GLY LEU GLU TRP ILE GLY SEQRES 5 H 239 ASN ILE TYR TYR THR GLY THR THR GLU THR ASN PRO SER SEQRES 6 H 239 LEU GLU GLY ARG PRO LEU ILE SER ILE ASP ARG THR THR SEQRES 7 H 239 GLN GLN VAL SER LEU THR LEU THR SER VAL THR PRO ALA SEQRES 8 H 239 ASP THR ALA VAL TYR TYR CYS ALA ARG THR ARG GLY GLU SEQRES 9 H 239 TRP SER PRO ASP TRP CYS LEU ASP ARG TRP GLY ARG GLY SEQRES 10 H 239 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 H 239 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 H 239 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 H 239 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 H 239 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 H 239 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 H 239 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 H 239 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 18 H 239 VAL GLU PRO LYS SER CYS ASP LYS THR GLY GLY SER HIS SEQRES 19 H 239 HIS HIS HIS HIS HIS SEQRES 1 I 239 MET GLY ILE GLN VAL GLN LEU ARG GLU SER GLY PRO HIS SEQRES 2 I 239 LEU VAL LYS PRO SER GLU THR LEU SER LEU THR CYS ASN SEQRES 3 I 239 VAL SER GLY GLY THR ILE ASN ARG TYR TYR TRP ASN TRP SEQRES 4 I 239 ILE ARG GLN ILE PRO GLY LYS GLY LEU GLU TRP ILE GLY SEQRES 5 I 239 ASN ILE TYR TYR THR GLY THR THR GLU THR ASN PRO SER SEQRES 6 I 239 LEU GLU GLY ARG PRO LEU ILE SER ILE ASP ARG THR THR SEQRES 7 I 239 GLN GLN VAL SER LEU THR LEU THR SER VAL THR PRO ALA SEQRES 8 I 239 ASP THR ALA VAL TYR TYR CYS ALA ARG THR ARG GLY GLU SEQRES 9 I 239 TRP SER PRO ASP TRP CYS LEU ASP ARG TRP GLY ARG GLY SEQRES 10 I 239 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 I 239 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 I 239 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 I 239 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 I 239 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 I 239 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 I 239 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 I 239 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 18 I 239 VAL GLU PRO LYS SER CYS ASP LYS THR GLY GLY SER HIS SEQRES 19 I 239 HIS HIS HIS HIS HIS SEQRES 1 L 218 MET GLY ILE GLU ILE VAL LEU THR GLN SER PRO ASP THR SEQRES 2 L 218 LEU SER LEU SER PRO GLY ASP THR ALA THR LEU SER CYS SEQRES 3 L 218 ARG ALA SER GLN THR ILE THR ASN ALA TYR PHE ALA TRP SEQRES 4 L 218 TYR GLN GLN LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE SEQRES 5 L 218 TYR SER THR SER THR ARG ALA SER GLY ILE PRO ASP ARG SEQRES 6 L 218 PHE SER GLY SER GLY SER GLY THR GLU PHE THR LEU THR SEQRES 7 L 218 ILE SER ARG LEU GLU PRO GLU ASP PHE ALA VAL PHE TYR SEQRES 8 L 218 CYS GLN GLN TYR VAL ARG SER PRO TRP THR PHE GLY GLN SEQRES 9 L 218 GLY THR LYS VAL GLU LEU LYS ARG THR VAL ALA ALA PRO SEQRES 10 L 218 SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SEQRES 11 L 218 SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE SEQRES 12 L 218 TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN SEQRES 13 L 218 ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU SEQRES 14 L 218 GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER THR SEQRES 15 L 218 LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL SEQRES 16 L 218 TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO SEQRES 17 L 218 VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 M 218 MET GLY ILE GLU ILE VAL LEU THR GLN SER PRO ASP THR SEQRES 2 M 218 LEU SER LEU SER PRO GLY ASP THR ALA THR LEU SER CYS SEQRES 3 M 218 ARG ALA SER GLN THR ILE THR ASN ALA TYR PHE ALA TRP SEQRES 4 M 218 TYR GLN GLN LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE SEQRES 5 M 218 TYR SER THR SER THR ARG ALA SER GLY ILE PRO ASP ARG SEQRES 6 M 218 PHE SER GLY SER GLY SER GLY THR GLU PHE THR LEU THR SEQRES 7 M 218 ILE SER ARG LEU GLU PRO GLU ASP PHE ALA VAL PHE TYR SEQRES 8 M 218 CYS GLN GLN TYR VAL ARG SER PRO TRP THR PHE GLY GLN SEQRES 9 M 218 GLY THR LYS VAL GLU LEU LYS ARG THR VAL ALA ALA PRO SEQRES 10 M 218 SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SEQRES 11 M 218 SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE SEQRES 12 M 218 TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN SEQRES 13 M 218 ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU SEQRES 14 M 218 GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER THR SEQRES 15 M 218 LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL SEQRES 16 M 218 TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO SEQRES 17 M 218 VAL THR LYS SER PHE ASN ARG GLY GLU CYS FORMUL 7 HOH *21(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 LYS A 206 LEU A 211 1 6 HELIX 5 AA5 ASP A 212 ASN A 223 1 12 HELIX 6 AA6 ILE A 225 ASP A 229 5 5 HELIX 7 AA7 ASN A 297 CYS A 302 1 6 HELIX 8 AA8 ASP A 333 SER A 345 1 13 HELIX 9 AA9 MET B 114 TYR B 117 5 4 HELIX 10 AB1 ASP B 118 HIS B 123 1 6 HELIX 11 AB2 LEU B 195 TYR B 202 1 8 HELIX 12 AB3 LYS B 206 ASN B 210 5 5 HELIX 13 AB4 ASP B 212 ASN B 223 1 12 HELIX 14 AB5 MET B 224 ASP B 229 5 6 HELIX 15 AB6 ILE B 282 GLN B 285 5 4 HELIX 16 AB7 ASN B 297 CYS B 302 1 6 HELIX 17 AB8 TRP B 315 ASN B 319 5 5 HELIX 18 AB9 ASP B 333 SER B 345 1 13 HELIX 19 AC1 ALA B 387 LYS B 391 5 5 HELIX 20 AC2 ASN H 60 GLU H 64 5 5 HELIX 21 AC3 THR H 86 THR H 90 5 5 HELIX 22 AC4 TRP H 102 TRP H 106 5 5 HELIX 23 AC5 SER H 164 ALA H 166 5 3 HELIX 24 AC6 SER H 195 LEU H 197 5 3 HELIX 25 AC7 THR I 86 THR I 90 5 5 HELIX 26 AC8 TRP I 102 TRP I 106 5 5 HELIX 27 AC9 SER I 164 ALA I 166 5 3 HELIX 28 AD1 SER I 195 LEU I 197 5 3 HELIX 29 AD2 LYS I 209 ASN I 212 5 4 HELIX 30 AD3 THR L 30 ALA L 32 5 3 HELIX 31 AD4 GLU L 80 PHE L 84 5 5 HELIX 32 AD5 SER L 122 LYS L 127 1 6 HELIX 33 AD6 LYS L 184 LYS L 189 1 6 HELIX 34 AD7 THR M 30 ALA M 32 5 3 HELIX 35 AD8 GLU M 80 PHE M 84 5 5 HELIX 36 AD9 SER M 122 SER M 128 1 7 HELIX 37 AE1 LYS M 184 GLU M 188 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 158 0 SHEET 2 AA3 2 PHE A 276 LYS A 280 -1 O ARG A 277 N ILE A 157 SHEET 1 AA4 6 ASN A 327 PRO A 330 0 SHEET 2 AA4 6 LYS A 408 PHE A 412 -1 O CYS A 409 N PHE A 329 SHEET 3 AA4 6 TRP A 399 ASN A 403 -1 N ASN A 401 O GLU A 410 SHEET 4 AA4 6 TYR A 425 THR A 429 -1 O THR A 428 N GLY A 400 SHEET 5 AA4 6 ASN A 306 GLN A 308 -1 N LEU A 307 O ALA A 427 SHEET 6 AA4 6 VAL A 437 GLU A 438 1 O GLU A 438 N GLN A 308 SHEET 1 AA5 3 ASN A 319 GLU A 321 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 2 GLU B 133 VAL B 137 0 SHEET 2 AA6 2 THR B 140 LEU B 144 -1 O LEU B 144 N GLU B 133 SHEET 1 AA7 5 VAL B 151 PHE B 152 0 SHEET 2 AA7 5 TYR B 287 LEU B 290 -1 O TYR B 289 N VAL B 151 SHEET 3 AA7 5 ALA B 238 ASP B 241 -1 N ALA B 238 O LEU B 290 SHEET 4 AA7 5 LYS B 246 ILE B 249 -1 O HIS B 248 N VAL B 239 SHEET 5 AA7 5 MET B 193 THR B 194 -1 N MET B 193 O CYS B 247 SHEET 1 AA8 2 LYS B 154 ILE B 158 0 SHEET 2 AA8 2 PHE B 276 LYS B 280 -1 O ARG B 277 N ILE B 157 SHEET 1 AA9 6 ASN B 327 PRO B 330 0 SHEET 2 AA9 6 LYS B 408 PHE B 412 -1 O CYS B 409 N PHE B 329 SHEET 3 AA9 6 TRP B 399 ASN B 403 -1 N ASN B 403 O LYS B 408 SHEET 4 AA9 6 TYR B 425 THR B 429 -1 O THR B 428 N GLY B 400 SHEET 5 AA9 6 ASN B 306 GLN B 308 -1 N LEU B 307 O ALA B 427 SHEET 6 AA9 6 VAL B 437 GLU B 438 1 O GLU B 438 N ASN B 306 SHEET 1 AB1 3 GLU B 321 ASP B 322 0 SHEET 2 AB1 3 LYS B 311 LEU B 314 -1 N LEU B 314 O GLU B 321 SHEET 3 AB1 3 CYS B 418 ILE B 420 -1 O ILE B 420 N LYS B 311 SHEET 1 AB2 4 GLN H 3 SER H 7 0 SHEET 2 AB2 4 LEU H 18 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AB2 4 GLN H 77 LEU H 82 -1 O LEU H 82 N LEU H 18 SHEET 4 AB2 4 PRO H 67 ASP H 72 -1 N LEU H 68 O THR H 81 SHEET 1 AB3 5 LEU H 11 VAL H 12 0 SHEET 2 AB3 5 THR H 115 VAL H 119 1 O THR H 118 N VAL H 12 SHEET 3 AB3 5 ALA H 91 THR H 98 -1 N TYR H 93 O THR H 115 SHEET 4 AB3 5 TYR H 33 GLN H 39 -1 N ILE H 37 O TYR H 94 SHEET 5 AB3 5 LEU H 45 TYR H 52 -1 O GLU H 46 N ARG H 38 SHEET 1 AB4 4 LEU H 11 VAL H 12 0 SHEET 2 AB4 4 THR H 115 VAL H 119 1 O THR H 118 N VAL H 12 SHEET 3 AB4 4 ALA H 91 THR H 98 -1 N TYR H 93 O THR H 115 SHEET 4 AB4 4 LEU H 108 TRP H 111 -1 O ARG H 110 N ARG H 97 SHEET 1 AB5 4 SER H 128 LEU H 132 0 SHEET 2 AB5 4 THR H 143 TYR H 153 -1 O LEU H 149 N PHE H 130 SHEET 3 AB5 4 TYR H 184 PRO H 193 -1 O LEU H 186 N VAL H 150 SHEET 4 AB5 4 VAL H 171 THR H 173 -1 N HIS H 172 O VAL H 189 SHEET 1 AB6 4 THR H 139 SER H 140 0 SHEET 2 AB6 4 THR H 143 TYR H 153 -1 O THR H 143 N SER H 140 SHEET 3 AB6 4 TYR H 184 PRO H 193 -1 O LEU H 186 N VAL H 150 SHEET 4 AB6 4 VAL H 177 LEU H 178 -1 N VAL H 177 O SER H 185 SHEET 1 AB7 3 THR H 159 TRP H 162 0 SHEET 2 AB7 3 TYR H 202 HIS H 208 -1 O ASN H 205 N SER H 161 SHEET 3 AB7 3 THR H 213 VAL H 219 -1 O VAL H 215 N VAL H 206 SHEET 1 AB8 4 GLN I 3 SER I 7 0 SHEET 2 AB8 4 LEU I 18 SER I 25 -1 O SER I 25 N GLN I 3 SHEET 3 AB8 4 GLN I 77 LEU I 82 -1 O VAL I 78 N CYS I 22 SHEET 4 AB8 4 ILE I 69 ASP I 72 -1 N SER I 70 O SER I 79 SHEET 1 AB9 6 LEU I 11 VAL I 12 0 SHEET 2 AB9 6 THR I 115 VAL I 119 1 O THR I 118 N VAL I 12 SHEET 3 AB9 6 ALA I 91 THR I 98 -1 N TYR I 93 O THR I 115 SHEET 4 AB9 6 TYR I 33 ILE I 40 -1 N ILE I 37 O TYR I 94 SHEET 5 AB9 6 GLY I 44 TYR I 52 -1 O GLU I 46 N ARG I 38 SHEET 6 AB9 6 THR I 57 THR I 59 -1 O GLU I 58 N ASN I 50 SHEET 1 AC1 4 LEU I 11 VAL I 12 0 SHEET 2 AC1 4 THR I 115 VAL I 119 1 O THR I 118 N VAL I 12 SHEET 3 AC1 4 ALA I 91 THR I 98 -1 N TYR I 93 O THR I 115 SHEET 4 AC1 4 LEU I 108 TRP I 111 -1 O ARG I 110 N ARG I 97 SHEET 1 AC2 4 SER I 128 LEU I 132 0 SHEET 2 AC2 4 THR I 143 TYR I 153 -1 O GLY I 147 N LEU I 132 SHEET 3 AC2 4 TYR I 184 PRO I 193 -1 O VAL I 192 N ALA I 144 SHEET 4 AC2 4 VAL I 171 THR I 173 -1 N HIS I 172 O VAL I 189 SHEET 1 AC3 4 SER I 128 LEU I 132 0 SHEET 2 AC3 4 THR I 143 TYR I 153 -1 O GLY I 147 N LEU I 132 SHEET 3 AC3 4 TYR I 184 PRO I 193 -1 O VAL I 192 N ALA I 144 SHEET 4 AC3 4 VAL I 177 LEU I 178 -1 N VAL I 177 O SER I 185 SHEET 1 AC4 3 THR I 159 TRP I 162 0 SHEET 2 AC4 3 ILE I 203 HIS I 208 -1 O ASN I 205 N SER I 161 SHEET 3 AC4 3 THR I 213 LYS I 218 -1 O THR I 213 N HIS I 208 SHEET 1 AC5 4 LEU L 4 SER L 7 0 SHEET 2 AC5 4 ALA L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AC5 4 GLU L 71 ILE L 76 -1 O LEU L 74 N LEU L 21 SHEET 4 AC5 4 PHE L 63 SER L 68 -1 N SER L 64 O THR L 75 SHEET 1 AC6 6 THR L 10 LEU L 13 0 SHEET 2 AC6 6 THR L 103 LEU L 107 1 O GLU L 106 N LEU L 11 SHEET 3 AC6 6 VAL L 86 GLN L 91 -1 N PHE L 87 O THR L 103 SHEET 4 AC6 6 PHE L 34 GLN L 39 -1 N GLN L 39 O VAL L 86 SHEET 5 AC6 6 ARG L 46 TYR L 50 -1 O ARG L 46 N GLN L 38 SHEET 6 AC6 6 THR L 54 ARG L 55 -1 O THR L 54 N TYR L 50 SHEET 1 AC7 4 THR L 10 LEU L 13 0 SHEET 2 AC7 4 THR L 103 LEU L 107 1 O GLU L 106 N LEU L 11 SHEET 3 AC7 4 VAL L 86 GLN L 91 -1 N PHE L 87 O THR L 103 SHEET 4 AC7 4 THR L 98 PHE L 99 -1 O THR L 98 N GLN L 91 SHEET 1 AC8 4 SER L 115 PHE L 119 0 SHEET 2 AC8 4 THR L 130 PHE L 140 -1 O LEU L 136 N PHE L 117 SHEET 3 AC8 4 TYR L 174 SER L 183 -1 O LEU L 182 N ALA L 131 SHEET 4 AC8 4 SER L 160 VAL L 164 -1 N GLN L 161 O THR L 179 SHEET 1 AC9 4 ALA L 154 LEU L 155 0 SHEET 2 AC9 4 LYS L 146 VAL L 151 -1 N VAL L 151 O ALA L 154 SHEET 3 AC9 4 VAL L 192 THR L 198 -1 O GLU L 196 N GLN L 148 SHEET 4 AC9 4 VAL L 206 ASN L 211 -1 O LYS L 208 N CYS L 195 SHEET 1 AD1 4 GLN M 6 SER M 7 0 SHEET 2 AD1 4 ALA M 19 CYS M 23 -1 O SER M 22 N SER M 7 SHEET 3 AD1 4 GLU M 71 ILE M 76 -1 O LEU M 74 N LEU M 21 SHEET 4 AD1 4 PHE M 63 SER M 68 -1 N SER M 68 O GLU M 71 SHEET 1 AD2 6 THR M 10 LEU M 13 0 SHEET 2 AD2 6 THR M 103 LEU M 107 1 O LYS M 104 N LEU M 11 SHEET 3 AD2 6 VAL M 86 GLN M 91 -1 N PHE M 87 O THR M 103 SHEET 4 AD2 6 PHE M 34 GLN M 39 -1 N GLN M 39 O VAL M 86 SHEET 5 AD2 6 ARG M 46 TYR M 50 -1 O ARG M 46 N GLN M 38 SHEET 6 AD2 6 THR M 54 ARG M 55 -1 O THR M 54 N TYR M 50 SHEET 1 AD3 4 THR M 10 LEU M 13 0 SHEET 2 AD3 4 THR M 103 LEU M 107 1 O LYS M 104 N LEU M 11 SHEET 3 AD3 4 VAL M 86 GLN M 91 -1 N PHE M 87 O THR M 103 SHEET 4 AD3 4 THR M 98 PHE M 99 -1 O THR M 98 N GLN M 91 SHEET 1 AD4 4 SER M 115 PHE M 119 0 SHEET 2 AD4 4 THR M 130 PHE M 140 -1 O LEU M 136 N PHE M 117 SHEET 3 AD4 4 TYR M 174 SER M 183 -1 O LEU M 180 N VAL M 133 SHEET 4 AD4 4 SER M 160 VAL M 164 -1 N SER M 163 O SER M 177 SHEET 1 AD5 4 ALA M 154 LEU M 155 0 SHEET 2 AD5 4 ALA M 145 VAL M 151 -1 N VAL M 151 O ALA M 154 SHEET 3 AD5 4 VAL M 192 HIS M 199 -1 O ALA M 194 N LYS M 150 SHEET 4 AD5 4 VAL M 206 ASN M 211 -1 O VAL M 206 N VAL M 197 SSBOND 1 CYS A 149 CYS A 302 1555 1555 2.03 SSBOND 2 CYS A 217 CYS A 247 1555 1555 2.03 SSBOND 3 CYS A 263 CYS A 275 1555 1555 2.03 SSBOND 4 CYS A 320 CYS A 418 1555 1555 2.03 SSBOND 5 CYS A 337 CYS A 409 1555 1555 2.04 SSBOND 6 CYS B 149 CYS B 302 1555 1555 2.03 SSBOND 7 CYS B 217 CYS B 247 1555 1555 2.03 SSBOND 8 CYS B 263 CYS B 275 1555 1555 2.03 SSBOND 9 CYS B 320 CYS B 418 1555 1555 2.03 SSBOND 10 CYS B 337 CYS B 409 1555 1555 2.04 SSBOND 11 CYS H 22 CYS H 95 1555 1555 2.04 SSBOND 12 CYS H 148 CYS H 204 1555 1555 2.04 SSBOND 13 CYS I 22 CYS I 95 1555 1555 2.03 SSBOND 14 CYS I 148 CYS I 204 1555 1555 2.04 SSBOND 15 CYS L 23 CYS L 89 1555 1555 2.04 SSBOND 16 CYS L 135 CYS L 195 1555 1555 2.03 SSBOND 17 CYS M 23 CYS M 89 1555 1555 2.04 SSBOND 18 CYS M 135 CYS M 195 1555 1555 2.03 CISPEP 1 GLU A 187 PRO A 188 0 2.88 CISPEP 2 SER A 191 PRO A 192 0 -5.05 CISPEP 3 GLU B 187 PRO B 188 0 1.50 CISPEP 4 SER B 191 PRO B 192 0 -2.27 CISPEP 5 PHE H 154 PRO H 155 0 -5.15 CISPEP 6 GLU H 156 PRO H 157 0 3.67 CISPEP 7 PHE I 154 PRO I 155 0 -9.73 CISPEP 8 GLU I 156 PRO I 157 0 5.27 CISPEP 9 SER L 7 PRO L 8 0 -0.06 CISPEP 10 SER L 95 PRO L 96 0 3.48 CISPEP 11 TYR L 141 PRO L 142 0 1.13 CISPEP 12 SER M 7 PRO M 8 0 -3.12 CISPEP 13 SER M 95 PRO M 96 0 0.92 CISPEP 14 TYR M 141 PRO M 142 0 2.18 CRYST1 54.868 71.620 132.927 94.11 99.20 112.39 P 1 2 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 0.018226 0.007509 0.004083 0.00000 SCALE2 0.000000 0.015101 0.002215 0.00000 SCALE3 0.000000 0.000000 0.007702 0.00000