HEADER IMMUNE SYSTEM 15-NOV-24 9ECX TITLE CRYSTAL STRUCTURE OF THE SARS-COV-2 NTD-TARGETED NEUTRALIZING ANTIBODY TITLE 2 WRAIR-2008 COMPND MOL_ID: 1; COMPND 2 MOLECULE: WRAIR-2008 FAB HEAVY CHAIN; COMPND 3 CHAIN: H, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: WRAIR-2008 FAB LIGHT CHAIN; COMPND 7 CHAIN: L, D; 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 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS ANTIBODY, NEUTRALIZING ANTIBODY, HUMAN ANTIBODY, SARS-COV-2, IMMUNE KEYWDS 2 SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR J.L.JENSEN,M.G.JOYCE REVDAT 1 20-AUG-25 9ECX 0 JRNL AUTH J.L.JENSEN,M.G.JOYCE JRNL TITL CRYSTAL STRUCTURE OF THE SARS-COV-2 NTD-TARGETED JRNL TITL 2 NEUTRALIZING ANTIBODY WRAIR-2008 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.67 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) : 2.67 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.17 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 76.3 REMARK 3 NUMBER OF REFLECTIONS : 20933 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.226 REMARK 3 R VALUE (WORKING SET) : 0.223 REMARK 3 FREE R VALUE : 0.289 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950 REMARK 3 FREE R VALUE TEST SET COUNT : 1037 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 34.1700 - 5.1000 0.99 3801 204 0.2273 0.2701 REMARK 3 2 5.1000 - 4.0500 0.99 3709 199 0.1874 0.2579 REMARK 3 3 4.0500 - 3.5400 0.99 3692 194 0.2175 0.2716 REMARK 3 4 3.5400 - 3.2100 1.00 3721 190 0.2283 0.3363 REMARK 3 5 3.2100 - 2.9800 0.85 3153 163 0.2682 0.3404 REMARK 3 6 2.9800 - 2.8100 0.38 1416 64 0.2793 0.3699 REMARK 3 7 2.8100 - 2.6700 0.11 404 23 0.2910 0.3727 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) : 0.370 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.460 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.009 7008 REMARK 3 ANGLE : 1.430 9528 REMARK 3 CHIRALITY : 0.067 1077 REMARK 3 PLANARITY : 0.010 2108 REMARK 3 DIHEDRAL : 18.491 2516 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 22 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 95 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.7389 -3.9342 -29.3353 REMARK 3 T TENSOR REMARK 3 T11: 0.3040 T22: 0.5202 REMARK 3 T33: 0.4366 T12: 0.0671 REMARK 3 T13: -0.1265 T23: -0.0888 REMARK 3 L TENSOR REMARK 3 L11: 3.1184 L22: 2.6129 REMARK 3 L33: 2.5181 L12: 0.2659 REMARK 3 L13: -0.3352 L23: -0.7744 REMARK 3 S TENSOR REMARK 3 S11: 0.0151 S12: 0.0750 S13: -0.1100 REMARK 3 S21: 0.2956 S22: -0.0506 S23: -0.3829 REMARK 3 S31: -0.1643 S32: 0.6623 S33: 0.2019 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 96 THROUGH 106 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.4444 -18.4230 -40.0020 REMARK 3 T TENSOR REMARK 3 T11: 1.1687 T22: 1.3417 REMARK 3 T33: 1.2715 T12: 0.1606 REMARK 3 T13: 0.0101 T23: -0.3935 REMARK 3 L TENSOR REMARK 3 L11: 1.9998 L22: 8.2490 REMARK 3 L33: 7.6068 L12: 2.9993 REMARK 3 L13: -1.3305 L23: -5.9321 REMARK 3 S TENSOR REMARK 3 S11: -0.3708 S12: 1.6468 S13: -1.6871 REMARK 3 S21: -1.4037 S22: -0.3072 S23: -1.8430 REMARK 3 S31: 2.3687 S32: 1.5622 S33: -1.1595 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 107 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): -38.0218 -11.5491 -38.3180 REMARK 3 T TENSOR REMARK 3 T11: 0.3254 T22: 0.1278 REMARK 3 T33: 0.2409 T12: -0.0492 REMARK 3 T13: -0.0357 T23: 0.0362 REMARK 3 L TENSOR REMARK 3 L11: 0.7986 L22: 2.2688 REMARK 3 L33: 0.9845 L12: 0.9381 REMARK 3 L13: 0.1629 L23: 1.0914 REMARK 3 S TENSOR REMARK 3 S11: 0.0213 S12: -0.2212 S13: 0.0090 REMARK 3 S21: 0.2085 S22: -0.1904 S23: 0.0769 REMARK 3 S31: -0.0285 S32: -0.2703 S33: 0.0225 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 215 THROUGH 216 ) REMARK 3 ORIGIN FOR THE GROUP (A): -56.2835 -14.6781 -44.3551 REMARK 3 T TENSOR REMARK 3 T11: 0.8235 T22: 1.1730 REMARK 3 T33: 1.8876 T12: 0.0602 REMARK 3 T13: -0.1895 T23: 0.2768 REMARK 3 L TENSOR REMARK 3 L11: 0.6304 L22: 0.4663 REMARK 3 L33: 0.8877 L12: -0.1075 REMARK 3 L13: 0.7478 L23: -0.1103 REMARK 3 S TENSOR REMARK 3 S11: 0.0744 S12: -0.1391 S13: 0.0290 REMARK 3 S21: 0.0923 S22: 0.0416 S23: -0.0121 REMARK 3 S31: 0.0263 S32: 0.0088 S33: 0.0008 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 14 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.7541 1.6544 -55.3073 REMARK 3 T TENSOR REMARK 3 T11: 0.9669 T22: 0.5705 REMARK 3 T33: 0.5508 T12: -0.2693 REMARK 3 T13: -0.0751 T23: -0.0367 REMARK 3 L TENSOR REMARK 3 L11: 3.0237 L22: 3.3408 REMARK 3 L33: 4.9511 L12: -1.4767 REMARK 3 L13: 0.9836 L23: 3.0101 REMARK 3 S TENSOR REMARK 3 S11: -0.2096 S12: -0.3294 S13: 0.7493 REMARK 3 S21: -1.0269 S22: 0.3384 S23: -0.6298 REMARK 3 S31: -0.8397 S32: 0.7336 S33: -0.0626 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 15 THROUGH 48 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.4982 -5.6149 -50.6199 REMARK 3 T TENSOR REMARK 3 T11: 0.4508 T22: 0.8995 REMARK 3 T33: 0.6067 T12: -0.1361 REMARK 3 T13: 0.1246 T23: -0.1309 REMARK 3 L TENSOR REMARK 3 L11: 2.2296 L22: 2.6708 REMARK 3 L33: 1.4353 L12: 0.0915 REMARK 3 L13: 1.1745 L23: 0.4443 REMARK 3 S TENSOR REMARK 3 S11: 0.0108 S12: -0.0554 S13: 0.1730 REMARK 3 S21: -0.1062 S22: 0.0024 S23: -0.7443 REMARK 3 S31: -0.5793 S32: 1.0754 S33: 0.1591 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 49 THROUGH 61 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.4053 -15.3253 -51.7767 REMARK 3 T TENSOR REMARK 3 T11: 0.6513 T22: 1.1343 REMARK 3 T33: 0.7694 T12: 0.5135 REMARK 3 T13: -0.2167 T23: -0.1482 REMARK 3 L TENSOR REMARK 3 L11: 0.4794 L22: 0.3396 REMARK 3 L33: 0.1591 L12: 0.4078 REMARK 3 L13: 0.2790 L23: 0.2337 REMARK 3 S TENSOR REMARK 3 S11: -0.0155 S12: -0.7590 S13: -0.5850 REMARK 3 S21: 0.3148 S22: 0.3515 S23: -0.2884 REMARK 3 S31: 0.1867 S32: 0.4865 S33: -0.5214 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 62 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.3999 -5.8388 -53.9961 REMARK 3 T TENSOR REMARK 3 T11: 0.4009 T22: 0.5476 REMARK 3 T33: 0.3004 T12: -0.1119 REMARK 3 T13: 0.0624 T23: -0.1267 REMARK 3 L TENSOR REMARK 3 L11: 0.1690 L22: 1.6056 REMARK 3 L33: 2.4995 L12: -0.3412 REMARK 3 L13: 0.3881 L23: 0.6190 REMARK 3 S TENSOR REMARK 3 S11: 0.0935 S12: -0.1703 S13: 0.1860 REMARK 3 S21: -0.2073 S22: -0.0056 S23: -0.5174 REMARK 3 S31: -0.1473 S32: 0.9551 S33: -0.2445 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 114 THROUGH 188 ) REMARK 3 ORIGIN FOR THE GROUP (A): -44.6042 -4.6424 -48.7389 REMARK 3 T TENSOR REMARK 3 T11: 0.2784 T22: 0.1139 REMARK 3 T33: 0.2568 T12: 0.0066 REMARK 3 T13: -0.0163 T23: 0.0048 REMARK 3 L TENSOR REMARK 3 L11: 0.8723 L22: 0.7830 REMARK 3 L33: 2.5939 L12: 0.1552 REMARK 3 L13: -0.6738 L23: 0.1790 REMARK 3 S TENSOR REMARK 3 S11: 0.1024 S12: 0.0354 S13: -0.0074 REMARK 3 S21: -0.2388 S22: 0.0361 S23: 0.1801 REMARK 3 S31: -0.0677 S32: -0.1776 S33: -0.0439 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 189 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): -52.0736 -6.3048 -54.5538 REMARK 3 T TENSOR REMARK 3 T11: 0.4049 T22: 0.2868 REMARK 3 T33: 0.4586 T12: -0.0038 REMARK 3 T13: -0.0750 T23: -0.0397 REMARK 3 L TENSOR REMARK 3 L11: 2.0250 L22: 2.6053 REMARK 3 L33: 2.6350 L12: 0.5274 REMARK 3 L13: -0.2283 L23: -1.2824 REMARK 3 S TENSOR REMARK 3 S11: 0.0399 S12: 0.5137 S13: -0.2944 REMARK 3 S21: -0.3028 S22: 0.0893 S23: 0.8073 REMARK 3 S31: -0.2608 S32: -0.7569 S33: -0.3234 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 95 ) REMARK 3 ORIGIN FOR THE GROUP (A): -73.2790 -8.8275 6.7005 REMARK 3 T TENSOR REMARK 3 T11: 0.4461 T22: 0.8160 REMARK 3 T33: 1.0155 T12: 0.2546 REMARK 3 T13: 0.1559 T23: 0.2588 REMARK 3 L TENSOR REMARK 3 L11: 0.4535 L22: 0.1142 REMARK 3 L33: 0.9383 L12: 0.1568 REMARK 3 L13: 0.7047 L23: 0.2062 REMARK 3 S TENSOR REMARK 3 S11: 0.0379 S12: 0.3840 S13: 0.5139 REMARK 3 S21: 0.4459 S22: 0.1474 S23: 0.9663 REMARK 3 S31: -0.5477 S32: -1.2131 S33: 0.3727 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 96 THROUGH 106 ) REMARK 3 ORIGIN FOR THE GROUP (A): -72.0857 5.0671 -5.0223 REMARK 3 T TENSOR REMARK 3 T11: 0.7492 T22: 1.6380 REMARK 3 T33: 1.7105 T12: 0.2461 REMARK 3 T13: 0.2755 T23: 0.5031 REMARK 3 L TENSOR REMARK 3 L11: 0.6743 L22: 2.6938 REMARK 3 L33: 0.1248 L12: -0.6550 REMARK 3 L13: 0.2010 L23: 0.1900 REMARK 3 S TENSOR REMARK 3 S11: 0.3345 S12: 2.1393 S13: 1.0324 REMARK 3 S21: -0.4665 S22: 0.1795 S23: 1.9209 REMARK 3 S31: -0.4819 S32: -1.2028 S33: -0.1685 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 107 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): -44.1730 -0.6438 7.6841 REMARK 3 T TENSOR REMARK 3 T11: 0.2203 T22: -0.2233 REMARK 3 T33: 0.1865 T12: 0.2347 REMARK 3 T13: 0.0195 T23: -0.0559 REMARK 3 L TENSOR REMARK 3 L11: 1.2261 L22: 0.2867 REMARK 3 L33: 0.6541 L12: 0.2152 REMARK 3 L13: 0.0226 L23: 0.1685 REMARK 3 S TENSOR REMARK 3 S11: 0.0781 S12: -0.6379 S13: -0.3762 REMARK 3 S21: 0.2724 S22: -0.0610 S23: -0.2479 REMARK 3 S31: 0.5361 S32: 0.0381 S33: 0.4661 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 14 ) REMARK 3 ORIGIN FOR THE GROUP (A): -63.8127 -14.5336 -17.1532 REMARK 3 T TENSOR REMARK 3 T11: 0.4308 T22: 0.5781 REMARK 3 T33: 0.8314 T12: 0.1810 REMARK 3 T13: 0.0354 T23: 0.0071 REMARK 3 L TENSOR REMARK 3 L11: 3.8313 L22: 2.1959 REMARK 3 L33: 2.0466 L12: 2.8515 REMARK 3 L13: -0.9215 L23: -1.0861 REMARK 3 S TENSOR REMARK 3 S11: 0.1487 S12: -0.5607 S13: -0.7583 REMARK 3 S21: -0.8312 S22: -0.2387 S23: 0.1061 REMARK 3 S31: 0.4725 S32: 0.0224 S33: -0.3731 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 15 THROUGH 32 ) REMARK 3 ORIGIN FOR THE GROUP (A): -74.2728 -10.8472 -19.3076 REMARK 3 T TENSOR REMARK 3 T11: 0.6171 T22: 0.6456 REMARK 3 T33: 0.9758 T12: -0.0554 REMARK 3 T13: -0.2074 T23: 0.3074 REMARK 3 L TENSOR REMARK 3 L11: 1.3562 L22: 1.3794 REMARK 3 L33: 0.9966 L12: 0.7135 REMARK 3 L13: -1.0320 L23: -0.2172 REMARK 3 S TENSOR REMARK 3 S11: 0.2674 S12: 0.0685 S13: -0.7947 REMARK 3 S21: -0.2101 S22: 0.2455 S23: 0.6989 REMARK 3 S31: -0.0321 S32: -0.6851 S33: -0.4750 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 33 THROUGH 48 ) REMARK 3 ORIGIN FOR THE GROUP (A): -65.9619 -3.3025 -9.7090 REMARK 3 T TENSOR REMARK 3 T11: 0.2972 T22: 0.3759 REMARK 3 T33: 0.5758 T12: 0.0300 REMARK 3 T13: -0.0473 T23: 0.1773 REMARK 3 L TENSOR REMARK 3 L11: 6.3166 L22: 2.5510 REMARK 3 L33: 4.7411 L12: -0.4827 REMARK 3 L13: -1.4546 L23: -0.6352 REMARK 3 S TENSOR REMARK 3 S11: 0.3337 S12: -0.4213 S13: 0.6566 REMARK 3 S21: 0.4290 S22: 0.2978 S23: 0.0012 REMARK 3 S31: -0.2015 S32: 0.2635 S33: 1.5728 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 49 THROUGH 61 ) REMARK 3 ORIGIN FOR THE GROUP (A): -73.0166 1.9471 -16.9173 REMARK 3 T TENSOR REMARK 3 T11: 0.7335 T22: 0.6001 REMARK 3 T33: 0.7843 T12: 0.3036 REMARK 3 T13: -0.0557 T23: 0.4821 REMARK 3 L TENSOR REMARK 3 L11: 0.3669 L22: 0.2256 REMARK 3 L33: 0.7331 L12: 0.1565 REMARK 3 L13: 0.0793 L23: 0.0397 REMARK 3 S TENSOR REMARK 3 S11: 0.0455 S12: -0.0938 S13: -0.1645 REMARK 3 S21: -0.3938 S22: -0.0059 S23: 0.4986 REMARK 3 S31: -0.2212 S32: -0.1702 S33: 0.4613 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 62 THROUGH 90 ) REMARK 3 ORIGIN FOR THE GROUP (A): -66.0409 -5.0703 -18.4670 REMARK 3 T TENSOR REMARK 3 T11: 0.4671 T22: 0.5698 REMARK 3 T33: 0.4559 T12: 0.0360 REMARK 3 T13: -0.1570 T23: 0.2774 REMARK 3 L TENSOR REMARK 3 L11: 1.4862 L22: 0.9151 REMARK 3 L33: 2.0061 L12: -1.1223 REMARK 3 L13: 0.4544 L23: 0.0421 REMARK 3 S TENSOR REMARK 3 S11: 0.1897 S12: 0.4209 S13: -0.2472 REMARK 3 S21: -0.6508 S22: 0.3653 S23: 0.9461 REMARK 3 S31: -0.0829 S32: -0.5253 S33: 0.9416 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 91 THROUGH 128 ) REMARK 3 ORIGIN FOR THE GROUP (A): -49.5561 -6.7633 -4.4386 REMARK 3 T TENSOR REMARK 3 T11: 0.2543 T22: 0.2785 REMARK 3 T33: 0.3745 T12: 0.0162 REMARK 3 T13: -0.0582 T23: 0.2220 REMARK 3 L TENSOR REMARK 3 L11: 1.1880 L22: 0.7943 REMARK 3 L33: 0.6208 L12: 0.0857 REMARK 3 L13: 0.0369 L23: 0.3635 REMARK 3 S TENSOR REMARK 3 S11: 0.1414 S12: -0.0196 S13: -0.4164 REMARK 3 S21: 0.0328 S22: 0.2518 S23: 0.3038 REMARK 3 S31: -0.3225 S32: -0.3453 S33: 0.1656 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 129 THROUGH 150 ) REMARK 3 ORIGIN FOR THE GROUP (A): -35.0254 -7.8207 -5.2609 REMARK 3 T TENSOR REMARK 3 T11: 0.4368 T22: -0.0286 REMARK 3 T33: 0.0916 T12: 0.0225 REMARK 3 T13: 0.0708 T23: 0.1667 REMARK 3 L TENSOR REMARK 3 L11: 0.4791 L22: 0.7061 REMARK 3 L33: 0.5686 L12: -0.2328 REMARK 3 L13: 0.2086 L23: -0.3432 REMARK 3 S TENSOR REMARK 3 S11: 0.1178 S12: -0.0519 S13: -0.2857 REMARK 3 S21: -0.4408 S22: -0.1789 S23: -0.0845 REMARK 3 S31: 0.1027 S32: 0.0229 S33: -0.0474 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 151 THROUGH 211 ) REMARK 3 ORIGIN FOR THE GROUP (A): -31.6937 -8.1156 -1.9152 REMARK 3 T TENSOR REMARK 3 T11: 0.2346 T22: 0.1489 REMARK 3 T33: 0.5432 T12: 0.0594 REMARK 3 T13: -0.0448 T23: -0.0786 REMARK 3 L TENSOR REMARK 3 L11: 0.8940 L22: 0.7141 REMARK 3 L33: 2.0203 L12: -0.4397 REMARK 3 L13: 1.1195 L23: -0.8875 REMARK 3 S TENSOR REMARK 3 S11: -0.1439 S12: 0.2855 S13: 0.2232 REMARK 3 S21: 0.2186 S22: -0.0900 S23: -0.2853 REMARK 3 S31: -0.0322 S32: 0.5401 S33: -0.1388 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 212 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): -22.6605 0.9542 8.3307 REMARK 3 T TENSOR REMARK 3 T11: 0.4460 T22: 0.9676 REMARK 3 T33: 1.0597 T12: 0.1874 REMARK 3 T13: -0.3676 T23: -0.4284 REMARK 3 L TENSOR REMARK 3 L11: 7.5731 L22: 7.1751 REMARK 3 L33: 7.9847 L12: -6.4646 REMARK 3 L13: 7.7134 L23: -7.0454 REMARK 3 S TENSOR REMARK 3 S11: 0.0404 S12: -0.0693 S13: -0.0047 REMARK 3 S21: 0.1221 S22: 0.0400 S23: -0.0977 REMARK 3 S31: 0.1604 S32: 0.2034 S33: -0.1627 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 9ECX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-NOV-24. REMARK 100 THE DEPOSITION ID IS D_1000289341. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 13-MAR-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS-II REMARK 200 BEAMLINE : 17-ID-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.920105 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 : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27956 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.647 REMARK 200 RESOLUTION RANGE LOW (A) : 34.175 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 3.900 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL 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 (%): 50.28 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.17 M AMMONIUM SULFATE, 25.5% W/V PEG REMARK 280 4000, 15% V/V GLYCEROL, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 30.20000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: 5290 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19620 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 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 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: 4680 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19780 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 C 215 REMARK 465 CYS C 216 REMARK 465 CYS D 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 LEU H 29 49.57 -78.80 REMARK 500 GLU H 31 16.77 59.33 REMARK 500 ALA H 95 62.77 -105.63 REMARK 500 ALA H 97 -136.18 53.56 REMARK 500 ASN H 100D -116.55 66.22 REMARK 500 TYR H 100H -130.01 50.62 REMARK 500 SER H 215 -131.92 56.93 REMARK 500 LYS L 50 -126.23 60.82 REMARK 500 ASN L 152 -6.07 66.86 REMARK 500 LYS L 188 3.12 -66.08 REMARK 500 GLU L 213 46.71 70.30 REMARK 500 ASP C 54 -42.93 80.40 REMARK 500 THR C 87 107.45 -59.58 REMARK 500 ALA C 95 54.95 -103.45 REMARK 500 ALA C 97 -134.51 58.35 REMARK 500 ARG C 100C 108.64 -163.05 REMARK 500 ASN C 100D -123.71 64.67 REMARK 500 TYR C 100H -119.90 54.59 REMARK 500 ASP C 144 70.41 50.30 REMARK 500 SER C 173 -9.23 -59.08 REMARK 500 LEU D 9 -14.42 76.04 REMARK 500 SER D 10 137.82 -177.50 REMARK 500 TYR D 49 -62.65 -99.45 REMARK 500 ASN D 152 -7.03 71.91 REMARK 500 GLN D 166 128.39 -36.60 REMARK 500 SER D 168 -9.84 75.84 REMARK 500 LYS D 169 -52.46 -122.26 REMARK 500 REMARK 500 REMARK: NULL DBREF 9ECX H 1 216 PDB 9ECX 9ECX 1 216 DBREF 9ECX L 1 214 PDB 9ECX 9ECX 1 214 DBREF 9ECX C 1 216 PDB 9ECX 9ECX 1 216 DBREF 9ECX D 1 214 PDB 9ECX 9ECX 1 214 SEQRES 1 H 231 GLN VAL ARG VAL VAL GLN SER GLY ALA GLU VAL LYS ASN SEQRES 2 H 231 PRO GLY ALA SER VAL LYS VAL SER CYS LYS VAL SER GLY SEQRES 3 H 231 TYR THR LEU THR GLU LEU SER ILE HIS TRP VAL ARG GLN SEQRES 4 H 231 ALA PRO GLY ASN GLY LEU GLU TRP MET GLY GLY PHE ASP SEQRES 5 H 231 PRO GLU ASP GLY GLU THR ILE TYR ALA GLN LYS PHE GLN SEQRES 6 H 231 GLY ARG VAL THR MET THR GLU ASP THR SER THR ASP THR SEQRES 7 H 231 ALA TYR MET GLU LEU SER SER LEU ARG SER ASP ASP THR SEQRES 8 H 231 ALA VAL TYR TYR CYS ALA THR ALA GLY ALA ILE THR GLY SEQRES 9 H 231 THR PRO ARG ASN PHE TYR TYR TYR TYR GLY MET ASP VAL SEQRES 10 H 231 TRP GLY GLN GLY THR THR VAL THR VAL SER SER ALA SER SEQRES 11 H 231 THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER SEQRES 12 H 231 LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU SEQRES 13 H 231 VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP SEQRES 14 H 231 ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO SEQRES 15 H 231 ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER SEQRES 16 H 231 VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR SEQRES 17 H 231 TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS SEQRES 18 H 231 VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 L 219 ASP ILE VAL MET THR GLN THR PRO LEU SER SER PRO VAL SEQRES 2 L 219 THR LEU GLY GLN PRO ALA SER ILE SER CYS ARG SER SER SEQRES 3 L 219 GLN SER LEU VAL HIS SER ASP GLY ASN THR TYR LEU SER SEQRES 4 L 219 TRP LEU GLN GLN ARG PRO GLY GLN PRO PRO ARG LEU LEU SEQRES 5 L 219 ILE TYR LYS ILE SER ASN ARG PHE SER GLY VAL PRO ASP SEQRES 6 L 219 ARG PHE SER GLY SER GLY ALA GLY THR ASP PHE THR LEU SEQRES 7 L 219 LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL TYR SEQRES 8 L 219 TYR CYS MET GLN VAL THR GLN PHE PRO TYR THR PHE GLY SEQRES 9 L 219 GLN GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 L 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 L 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 L 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 L 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 L 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 L 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 L 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 L 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 C 231 GLN VAL ARG VAL VAL GLN SER GLY ALA GLU VAL LYS ASN SEQRES 2 C 231 PRO GLY ALA SER VAL LYS VAL SER CYS LYS VAL SER GLY SEQRES 3 C 231 TYR THR LEU THR GLU LEU SER ILE HIS TRP VAL ARG GLN SEQRES 4 C 231 ALA PRO GLY ASN GLY LEU GLU TRP MET GLY GLY PHE ASP SEQRES 5 C 231 PRO GLU ASP GLY GLU THR ILE TYR ALA GLN LYS PHE GLN SEQRES 6 C 231 GLY ARG VAL THR MET THR GLU ASP THR SER THR ASP THR SEQRES 7 C 231 ALA TYR MET GLU LEU SER SER LEU ARG SER ASP ASP THR SEQRES 8 C 231 ALA VAL TYR TYR CYS ALA THR ALA GLY ALA ILE THR GLY SEQRES 9 C 231 THR PRO ARG ASN PHE TYR TYR TYR TYR GLY MET ASP VAL SEQRES 10 C 231 TRP GLY GLN GLY THR THR VAL THR VAL SER SER ALA SER SEQRES 11 C 231 THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER SEQRES 12 C 231 LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU SEQRES 13 C 231 VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP SEQRES 14 C 231 ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO SEQRES 15 C 231 ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER SEQRES 16 C 231 VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR SEQRES 17 C 231 TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS SEQRES 18 C 231 VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 D 219 ASP ILE VAL MET THR GLN THR PRO LEU SER SER PRO VAL SEQRES 2 D 219 THR LEU GLY GLN PRO ALA SER ILE SER CYS ARG SER SER SEQRES 3 D 219 GLN SER LEU VAL HIS SER ASP GLY ASN THR TYR LEU SER SEQRES 4 D 219 TRP LEU GLN GLN ARG PRO GLY GLN PRO PRO ARG LEU LEU SEQRES 5 D 219 ILE TYR LYS ILE SER ASN ARG PHE SER GLY VAL PRO ASP SEQRES 6 D 219 ARG PHE SER GLY SER GLY ALA GLY THR ASP PHE THR LEU SEQRES 7 D 219 LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL TYR SEQRES 8 D 219 TYR CYS MET GLN VAL THR GLN PHE PRO TYR THR PHE GLY SEQRES 9 D 219 GLN GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 D 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 D 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 D 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 D 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 D 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 D 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 D 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 D 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS HET GOL H 301 6 HET GOL H 302 6 HET GOL H 303 6 HET SO4 L 301 5 HET GOL L 302 6 HET GOL L 303 6 HET SO4 C 301 5 HET SO4 D 301 5 HET GOL D 302 6 HETNAM GOL GLYCEROL HETNAM SO4 SULFATE ION HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 5 GOL 6(C3 H8 O3) FORMUL 8 SO4 3(O4 S 2-) FORMUL 14 HOH *102(H2 O) HELIX 1 AA1 ARG H 83 THR H 87 5 5 HELIX 2 AA2 SER H 127 LYS H 129 5 3 HELIX 3 AA3 SER H 156 ALA H 158 5 3 HELIX 4 AA4 SER H 187 THR H 191 5 5 HELIX 5 AA5 GLU L 79 VAL L 83 5 5 HELIX 6 AA6 SER L 121 GLY L 128 1 8 HELIX 7 AA7 LYS L 183 LYS L 188 1 6 HELIX 8 AA8 ARG C 83 THR C 87 5 5 HELIX 9 AA9 SER C 127 LYS C 129 5 3 HELIX 10 AB1 SER C 156 ALA C 158 5 3 HELIX 11 AB2 SER C 187 THR C 191 5 5 HELIX 12 AB3 GLU D 79 VAL D 83 5 5 HELIX 13 AB4 SER D 121 SER D 127 1 7 HELIX 14 AB5 LYS D 183 HIS D 189 1 7 SHEET 1 AA1 4 ARG H 3 GLN H 6 0 SHEET 2 AA1 4 VAL H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AA1 4 THR H 77 LEU H 82 -1 O ALA H 78 N CYS H 22 SHEET 4 AA1 4 VAL H 67 ASP H 72 -1 N THR H 70 O TYR H 79 SHEET 1 AA2 5 GLU H 10 LYS H 12 0 SHEET 2 AA2 5 THR H 107 VAL H 111 1 O THR H 110 N LYS H 12 SHEET 3 AA2 5 ALA H 88 ALA H 95 -1 N ALA H 88 O VAL H 109 SHEET 4 AA2 5 ILE H 34 GLN H 39 -1 N GLN H 39 O VAL H 89 SHEET 5 AA2 5 LEU H 45 PHE H 51 -1 O GLU H 46 N ARG H 38 SHEET 1 AA3 4 GLU H 10 LYS H 12 0 SHEET 2 AA3 4 THR H 107 VAL H 111 1 O THR H 110 N LYS H 12 SHEET 3 AA3 4 ALA H 88 ALA H 95 -1 N ALA H 88 O VAL H 109 SHEET 4 AA3 4 ASP H 101 TRP H 103 -1 O VAL H 102 N THR H 94 SHEET 1 AA4 4 SER H 120 LEU H 124 0 SHEET 2 AA4 4 THR H 135 TYR H 145 -1 O LYS H 143 N SER H 120 SHEET 3 AA4 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145 SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA5 4 THR H 131 SER H 132 0 SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O THR H 135 N SER H 132 SHEET 3 AA5 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145 SHEET 4 AA5 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AA6 3 THR H 151 TRP H 154 0 SHEET 2 AA6 3 ILE H 195 HIS H 200 -1 O ASN H 199 N THR H 151 SHEET 3 AA6 3 THR H 205 LYS H 210 -1 O VAL H 207 N VAL H 198 SHEET 1 AA7 4 MET L 4 GLN L 6 0 SHEET 2 AA7 4 ALA L 19 SER L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA7 4 ASP L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AA7 4 PHE L 62 ALA L 67 -1 N ALA L 67 O ASP L 70 SHEET 1 AA8 6 SER L 10 THR L 14 0 SHEET 2 AA8 6 THR L 102 LYS L 107 1 O LYS L 107 N VAL L 13 SHEET 3 AA8 6 GLY L 84 GLN L 90 -1 N GLY L 84 O LEU L 104 SHEET 4 AA8 6 LEU L 33 GLN L 38 -1 N SER L 34 O MET L 89 SHEET 5 AA8 6 ARG L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA8 6 ASN L 53 ARG L 54 -1 O ASN L 53 N TYR L 49 SHEET 1 AA9 4 SER L 10 THR L 14 0 SHEET 2 AA9 4 THR L 102 LYS L 107 1 O LYS L 107 N VAL L 13 SHEET 3 AA9 4 GLY L 84 GLN L 90 -1 N GLY L 84 O LEU L 104 SHEET 4 AA9 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB1 4 SER L 114 PHE L 118 0 SHEET 2 AB1 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AB1 4 TYR L 173 SER L 182 -1 O TYR L 173 N PHE L 139 SHEET 4 AB1 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB2 4 ALA L 153 LEU L 154 0 SHEET 2 AB2 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB2 4 VAL L 191 THR L 197 -1 O ALA L 193 N LYS L 149 SHEET 4 AB2 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SHEET 1 AB3 4 ARG C 3 GLN C 6 0 SHEET 2 AB3 4 VAL C 18 SER C 25 -1 O LYS C 23 N VAL C 5 SHEET 3 AB3 4 THR C 77 LEU C 82 -1 O ALA C 78 N CYS C 22 SHEET 4 AB3 4 VAL C 67 ASP C 72 -1 N THR C 70 O TYR C 79 SHEET 1 AB4 6 GLU C 10 LYS C 12 0 SHEET 2 AB4 6 THR C 107 VAL C 111 1 O THR C 108 N GLU C 10 SHEET 3 AB4 6 ALA C 88 ALA C 95 -1 N ALA C 88 O VAL C 109 SHEET 4 AB4 6 ILE C 34 GLN C 39 -1 N GLN C 39 O VAL C 89 SHEET 5 AB4 6 LEU C 45 PHE C 51 -1 O GLU C 46 N ARG C 38 SHEET 6 AB4 6 THR C 57 TYR C 59 -1 O ILE C 58 N GLY C 50 SHEET 1 AB5 4 GLU C 10 LYS C 12 0 SHEET 2 AB5 4 THR C 107 VAL C 111 1 O THR C 108 N GLU C 10 SHEET 3 AB5 4 ALA C 88 ALA C 95 -1 N ALA C 88 O VAL C 109 SHEET 4 AB5 4 ASP C 101 TRP C 103 -1 O VAL C 102 N THR C 94 SHEET 1 AB6 4 SER C 120 LEU C 124 0 SHEET 2 AB6 4 THR C 135 TYR C 145 -1 O LYS C 143 N SER C 120 SHEET 3 AB6 4 TYR C 176 PRO C 185 -1 O VAL C 182 N LEU C 138 SHEET 4 AB6 4 VAL C 163 THR C 165 -1 N HIS C 164 O VAL C 181 SHEET 1 AB7 4 THR C 131 SER C 132 0 SHEET 2 AB7 4 THR C 135 TYR C 145 -1 O THR C 135 N SER C 132 SHEET 3 AB7 4 TYR C 176 PRO C 185 -1 O VAL C 182 N LEU C 138 SHEET 4 AB7 4 VAL C 169 LEU C 170 -1 N VAL C 169 O SER C 177 SHEET 1 AB8 3 THR C 151 TRP C 154 0 SHEET 2 AB8 3 TYR C 194 HIS C 200 -1 O ASN C 197 N SER C 153 SHEET 3 AB8 3 THR C 205 VAL C 211 -1 O VAL C 207 N VAL C 198 SHEET 1 AB9 4 MET D 4 GLN D 6 0 SHEET 2 AB9 4 ALA D 19 SER D 25 -1 O ARG D 24 N THR D 5 SHEET 3 AB9 4 ASP D 70 ILE D 75 -1 O ILE D 75 N ALA D 19 SHEET 4 AB9 4 PHE D 62 ALA D 67 -1 N SER D 63 O LYS D 74 SHEET 1 AC1 5 SER D 10 THR D 14 0 SHEET 2 AC1 5 THR D 102 LYS D 107 1 O LYS D 107 N VAL D 13 SHEET 3 AC1 5 GLY D 84 GLN D 90 -1 N GLY D 84 O LEU D 104 SHEET 4 AC1 5 LEU D 33 GLN D 38 -1 N GLN D 38 O VAL D 85 SHEET 5 AC1 5 PRO D 44 ILE D 48 -1 O LEU D 47 N TRP D 35 SHEET 1 AC2 4 SER D 114 PHE D 118 0 SHEET 2 AC2 4 THR D 129 PHE D 139 -1 O LEU D 135 N PHE D 116 SHEET 3 AC2 4 TYR D 173 SER D 182 -1 O LEU D 175 N LEU D 136 SHEET 4 AC2 4 SER D 159 VAL D 163 -1 N GLN D 160 O THR D 178 SHEET 1 AC3 4 ALA D 153 LEU D 154 0 SHEET 2 AC3 4 LYS D 145 VAL D 150 -1 N VAL D 150 O ALA D 153 SHEET 3 AC3 4 VAL D 191 THR D 197 -1 O GLU D 195 N GLN D 147 SHEET 4 AC3 4 VAL D 205 ASN D 210 -1 O VAL D 205 N VAL D 196 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.02 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.06 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.03 SSBOND 5 CYS C 22 CYS C 92 1555 1555 2.02 SSBOND 6 CYS C 140 CYS C 196 1555 1555 2.06 SSBOND 7 CYS D 23 CYS D 88 1555 1555 2.05 SSBOND 8 CYS D 134 CYS D 194 1555 1555 2.05 CISPEP 1 PHE H 146 PRO H 147 0 -5.90 CISPEP 2 PHE L 94 PRO L 95 0 -0.56 CISPEP 3 PHE D 94 PRO D 95 0 -0.57 CRYST1 87.040 60.400 92.770 90.00 99.20 90.00 P 1 21 1 4 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 0.011489 0.000000 0.001861 0.00000 SCALE2 0.000000 0.016556 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010920 0.00000