HEADER IMMUNE SYSTEM 28-FEB-23 8GBV TITLE CRYSTAL STRUCTURE OF PC39-17A, AN ANTI-HIV BROADLY NEUTRALIZING TITLE 2 ANTIBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: PC39-17A FAB HEAVY CHAIN; COMPND 3 CHAIN: H, A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: PC39-17A FAB LIGHT CHAIN; COMPND 7 CHAIN: L, B; COMPND 8 ENGINEERED: YES; COMPND 9 OTHER_DETAILS: THE N-TERMINAL RESIDUE (H) ORIGINATES FROM THE SIGNAL COMPND 10 PEPTIDE 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, BROADLY NEUTRALIZING, HIV-1, V3 GLYCAN, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR S.MURRELL,O.OMORODION,I.A.WILSON REVDAT 1 07-JUN-23 8GBV 0 JRNL AUTH C.JOYCE,S.MURRELL,B.MURRELL,O.OMORODION,L.S.VER,N.CARRICO, JRNL AUTH 2 R.ROUZEAU,R.BASTIDAS,R.NEDELLEC,M.BICK,J.WOEHL,F.ZHAO, JRNL AUTH 3 A.BURNS,S.BARMAN,M.APPEL,A.RAMOS,L.WICKRAMASINGHE,K.EREN, JRNL AUTH 4 T.VOLLBRECHT,D.M.SMITH,S.L.KOSAKOVSKY POND,R.MCBRIDE, JRNL AUTH 5 C.WORTH,J.C.PAULSON,F.BATISTA,D.SOK,P.POIGNARD,B.BRINEY, JRNL AUTH 6 I.A.WILSON,E.LANDAIS,D.R.BURTON JRNL TITL ANTIGEN PRESSURE FROM TWO FOUNDER VIRUSES INDUCES MULTIPLE JRNL TITL 2 INSERTIONS AT A SINGLE POSITION TO GENERATE BROADLY JRNL TITL 3 NEUTRALIZING HIV ANTIBODIES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.08 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) : 2.08 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.63 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6 REMARK 3 NUMBER OF REFLECTIONS : 53260 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.195 REMARK 3 R VALUE (WORKING SET) : 0.193 REMARK 3 FREE R VALUE : 0.230 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.840 REMARK 3 FREE R VALUE TEST SET COUNT : 2580 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 47.6300 - 5.4400 0.99 2864 139 0.1591 0.1833 REMARK 3 2 5.4400 - 4.3200 0.99 2891 136 0.1275 0.1285 REMARK 3 3 4.3200 - 3.7700 0.99 2866 135 0.1398 0.1683 REMARK 3 4 3.7700 - 3.4300 0.99 2849 158 0.1522 0.1866 REMARK 3 5 3.4300 - 3.1800 0.99 2882 137 0.1806 0.2057 REMARK 3 6 3.1800 - 3.0000 0.99 2808 160 0.1909 0.2399 REMARK 3 7 3.0000 - 2.8500 0.98 2839 145 0.2050 0.2607 REMARK 3 8 2.8500 - 2.7200 0.98 2785 155 0.2169 0.2359 REMARK 3 9 2.7200 - 2.6200 0.98 2868 157 0.2174 0.3005 REMARK 3 10 2.6200 - 2.5300 0.98 2779 164 0.2271 0.2663 REMARK 3 11 2.5300 - 2.4500 0.98 2844 124 0.2315 0.2748 REMARK 3 12 2.4500 - 2.3800 0.98 2848 135 0.2342 0.2969 REMARK 3 13 2.3800 - 2.3200 0.98 2800 132 0.2494 0.2910 REMARK 3 14 2.3100 - 2.2600 0.97 2834 143 0.2568 0.3096 REMARK 3 15 2.2600 - 2.2100 0.97 2818 134 0.2600 0.3260 REMARK 3 16 2.2100 - 2.1600 0.97 2797 142 0.2736 0.3589 REMARK 3 17 2.1600 - 2.1200 0.97 2792 138 0.2922 0.3400 REMARK 3 18 2.1200 - 2.0800 0.88 2516 146 0.2928 0.3568 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.288 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.274 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 21.88 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.48 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 : 0.003 7317 REMARK 3 ANGLE : 0.653 9949 REMARK 3 CHIRALITY : 0.046 1092 REMARK 3 PLANARITY : 0.005 1277 REMARK 3 DIHEDRAL : 11.791 2659 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 25 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): 31.8182 -3.4615 -45.4816 REMARK 3 T TENSOR REMARK 3 T11: 0.2564 T22: 0.1383 REMARK 3 T33: 0.3193 T12: -0.0089 REMARK 3 T13: 0.0583 T23: -0.0933 REMARK 3 L TENSOR REMARK 3 L11: 2.0176 L22: 2.2929 REMARK 3 L33: 1.8720 L12: -0.5553 REMARK 3 L13: -0.2351 L23: 0.2401 REMARK 3 S TENSOR REMARK 3 S11: 0.0559 S12: -0.3761 S13: 0.3447 REMARK 3 S21: 0.5989 S22: -0.0652 S23: 0.2532 REMARK 3 S31: 0.1761 S32: 0.1908 S33: 0.0063 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 18 THROUGH 109 ) REMARK 3 ORIGIN FOR THE GROUP (A): 36.0208 -4.0787 -58.2985 REMARK 3 T TENSOR REMARK 3 T11: 0.1559 T22: 0.0505 REMARK 3 T33: 0.2505 T12: 0.0314 REMARK 3 T13: -0.0073 T23: -0.0099 REMARK 3 L TENSOR REMARK 3 L11: 1.3194 L22: 1.3368 REMARK 3 L33: 1.4007 L12: 0.2448 REMARK 3 L13: -0.6439 L23: 0.2846 REMARK 3 S TENSOR REMARK 3 S11: 0.0127 S12: 0.0273 S13: 0.3279 REMARK 3 S21: 0.1005 S22: 0.0154 S23: 0.0570 REMARK 3 S31: -0.0378 S32: 0.0876 S33: -0.0248 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 110 THROUGH 175 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.6480 -18.8775 -35.3835 REMARK 3 T TENSOR REMARK 3 T11: 0.1486 T22: 0.2931 REMARK 3 T33: 0.1911 T12: 0.0228 REMARK 3 T13: -0.0253 T23: -0.0127 REMARK 3 L TENSOR REMARK 3 L11: 2.3811 L22: 4.8176 REMARK 3 L33: 2.6531 L12: -0.5788 REMARK 3 L13: -0.0918 L23: -0.4283 REMARK 3 S TENSOR REMARK 3 S11: 0.0262 S12: -0.6000 S13: -0.0871 REMARK 3 S21: 0.1291 S22: 0.1452 S23: -0.2434 REMARK 3 S31: 0.0278 S32: 0.0913 S33: -0.1922 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 176 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.5702 -25.7093 -29.5848 REMARK 3 T TENSOR REMARK 3 T11: 0.2559 T22: 0.4846 REMARK 3 T33: 0.3450 T12: 0.0820 REMARK 3 T13: -0.0515 T23: 0.1140 REMARK 3 L TENSOR REMARK 3 L11: 2.5860 L22: 5.1743 REMARK 3 L33: 3.5442 L12: 0.9070 REMARK 3 L13: -0.2564 L23: 0.4148 REMARK 3 S TENSOR REMARK 3 S11: 0.1029 S12: -1.1537 S13: -0.5932 REMARK 3 S21: 0.6813 S22: 0.1093 S23: -0.2252 REMARK 3 S31: 0.2584 S32: 0.0607 S33: -0.2101 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 0 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.5517 -20.8470 -68.6290 REMARK 3 T TENSOR REMARK 3 T11: 0.1248 T22: 0.1409 REMARK 3 T33: 0.1899 T12: 0.0077 REMARK 3 T13: -0.0021 T23: -0.0949 REMARK 3 L TENSOR REMARK 3 L11: 3.7361 L22: 7.5442 REMARK 3 L33: 3.3098 L12: 1.1627 REMARK 3 L13: -0.5856 L23: -0.7686 REMARK 3 S TENSOR REMARK 3 S11: 0.0732 S12: 0.3165 S13: -0.0571 REMARK 3 S21: -0.4556 S22: -0.1110 S23: 0.5071 REMARK 3 S31: 0.1946 S32: -0.2249 S33: 0.0366 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 19 THROUGH 48 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.7114 -16.8604 -67.4178 REMARK 3 T TENSOR REMARK 3 T11: 0.1665 T22: 0.0834 REMARK 3 T33: 0.2077 T12: 0.0122 REMARK 3 T13: 0.0171 T23: -0.0450 REMARK 3 L TENSOR REMARK 3 L11: 1.3461 L22: 0.2618 REMARK 3 L33: 1.0501 L12: 0.5467 REMARK 3 L13: -0.1429 L23: 0.0003 REMARK 3 S TENSOR REMARK 3 S11: -0.1029 S12: 0.2074 S13: -0.1745 REMARK 3 S21: 0.0459 S22: -0.0078 S23: -0.0237 REMARK 3 S31: 0.2627 S32: 0.0306 S33: 0.0705 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 49 THROUGH 90 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.9871 -23.8233 -67.6757 REMARK 3 T TENSOR REMARK 3 T11: 0.2222 T22: 0.1331 REMARK 3 T33: 0.3442 T12: -0.0045 REMARK 3 T13: 0.0175 T23: -0.1088 REMARK 3 L TENSOR REMARK 3 L11: 1.3758 L22: 0.9879 REMARK 3 L33: 0.3767 L12: 0.7094 REMARK 3 L13: -0.3414 L23: 0.2105 REMARK 3 S TENSOR REMARK 3 S11: -0.1792 S12: 0.4444 S13: -0.5565 REMARK 3 S21: -0.1125 S22: 0.0935 S23: -0.2149 REMARK 3 S31: 0.2166 S32: 0.0700 S33: 0.0334 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 91 THROUGH 128 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.5412 -20.4550 -49.7362 REMARK 3 T TENSOR REMARK 3 T11: 0.1883 T22: 0.1329 REMARK 3 T33: 0.1963 T12: 0.0271 REMARK 3 T13: -0.0282 T23: 0.0016 REMARK 3 L TENSOR REMARK 3 L11: 1.7579 L22: 0.4842 REMARK 3 L33: 0.5691 L12: 0.4161 REMARK 3 L13: -0.5319 L23: -0.5753 REMARK 3 S TENSOR REMARK 3 S11: -0.0452 S12: -0.2656 S13: -0.1289 REMARK 3 S21: 0.0420 S22: -0.0303 S23: -0.0564 REMARK 3 S31: -0.0965 S32: -0.0421 S33: 0.0920 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 129 THROUGH 174 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.9335 -24.3848 -46.3854 REMARK 3 T TENSOR REMARK 3 T11: 0.1932 T22: 0.0789 REMARK 3 T33: 0.2172 T12: 0.0150 REMARK 3 T13: -0.0126 T23: 0.0143 REMARK 3 L TENSOR REMARK 3 L11: 3.4104 L22: 3.0054 REMARK 3 L33: 1.8748 L12: -2.2209 REMARK 3 L13: -1.6832 L23: 1.8165 REMARK 3 S TENSOR REMARK 3 S11: -0.0253 S12: -0.1840 S13: -0.2456 REMARK 3 S21: 0.0200 S22: 0.0857 S23: -0.0679 REMARK 3 S31: 0.0394 S32: 0.1045 S33: -0.0523 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 175 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.2099 -23.5530 -39.2160 REMARK 3 T TENSOR REMARK 3 T11: 0.1522 T22: 0.2089 REMARK 3 T33: 0.2478 T12: 0.0299 REMARK 3 T13: -0.0159 T23: 0.0978 REMARK 3 L TENSOR REMARK 3 L11: 3.8558 L22: 5.2908 REMARK 3 L33: 3.3648 L12: -1.0945 REMARK 3 L13: -0.3514 L23: 2.4542 REMARK 3 S TENSOR REMARK 3 S11: -0.0202 S12: -0.5832 S13: -0.5098 REMARK 3 S21: 0.2590 S22: -0.1868 S23: 0.2094 REMARK 3 S31: 0.0948 S32: -0.3650 S33: 0.1912 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.2951 16.0097 -98.1528 REMARK 3 T TENSOR REMARK 3 T11: 0.3285 T22: 0.4308 REMARK 3 T33: 0.2772 T12: -0.0568 REMARK 3 T13: -0.1133 T23: 0.1405 REMARK 3 L TENSOR REMARK 3 L11: 5.4697 L22: 2.0036 REMARK 3 L33: 3.7069 L12: 1.5408 REMARK 3 L13: 1.9047 L23: 1.9455 REMARK 3 S TENSOR REMARK 3 S11: 0.1367 S12: 0.7527 S13: 0.7159 REMARK 3 S21: -0.3584 S22: 0.1361 S23: 0.4425 REMARK 3 S31: -0.2616 S32: 0.1885 S33: -0.0855 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 18 THROUGH 51 ) REMARK 3 ORIGIN FOR THE GROUP (A): -4.3337 6.8261 -89.7782 REMARK 3 T TENSOR REMARK 3 T11: 0.1676 T22: 0.2598 REMARK 3 T33: 0.1528 T12: -0.0238 REMARK 3 T13: -0.0264 T23: 0.0525 REMARK 3 L TENSOR REMARK 3 L11: 2.1220 L22: 2.4435 REMARK 3 L33: 2.7355 L12: 1.6094 REMARK 3 L13: -1.5586 L23: -1.1247 REMARK 3 S TENSOR REMARK 3 S11: -0.0256 S12: 0.2395 S13: 0.1691 REMARK 3 S21: -0.0816 S22: 0.1059 S23: 0.1689 REMARK 3 S31: -0.1188 S32: -0.1057 S33: -0.0545 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 52 THROUGH 66 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.1392 11.2005 -81.1547 REMARK 3 T TENSOR REMARK 3 T11: 0.2933 T22: 0.3443 REMARK 3 T33: 0.1897 T12: -0.0739 REMARK 3 T13: -0.0156 T23: 0.0343 REMARK 3 L TENSOR REMARK 3 L11: 2.9769 L22: 2.7849 REMARK 3 L33: 3.1061 L12: 1.3242 REMARK 3 L13: -2.2728 L23: -1.4509 REMARK 3 S TENSOR REMARK 3 S11: 0.3391 S12: -0.5003 S13: 0.0602 REMARK 3 S21: 0.4061 S22: -0.2418 S23: -0.1177 REMARK 3 S31: -0.3062 S32: 0.5507 S33: -0.0063 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 67 THROUGH 87 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.2681 16.9018 -89.7080 REMARK 3 T TENSOR REMARK 3 T11: 0.2218 T22: 0.2965 REMARK 3 T33: 0.2063 T12: -0.0585 REMARK 3 T13: 0.0039 T23: 0.0448 REMARK 3 L TENSOR REMARK 3 L11: 3.4444 L22: 2.6203 REMARK 3 L33: 3.0762 L12: 1.9400 REMARK 3 L13: -2.0637 L23: -0.9680 REMARK 3 S TENSOR REMARK 3 S11: 0.1521 S12: -0.0608 S13: 0.6018 REMARK 3 S21: 0.2634 S22: -0.0406 S23: 0.1403 REMARK 3 S31: -0.4712 S32: 0.2406 S33: -0.1657 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 88 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.1304 4.6014 -93.9787 REMARK 3 T TENSOR REMARK 3 T11: 0.1446 T22: 0.3965 REMARK 3 T33: 0.2133 T12: -0.0229 REMARK 3 T13: -0.0336 T23: 0.0712 REMARK 3 L TENSOR REMARK 3 L11: 1.0816 L22: 0.8427 REMARK 3 L33: 2.4540 L12: 0.3867 REMARK 3 L13: -0.9934 L23: -0.9813 REMARK 3 S TENSOR REMARK 3 S11: -0.0973 S12: 0.5660 S13: 0.2673 REMARK 3 S21: -0.1158 S22: 0.1533 S23: 0.1141 REMARK 3 S31: -0.0514 S32: -0.1149 S33: -0.1477 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 120 THROUGH 134 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.0240 6.0090-126.6027 REMARK 3 T TENSOR REMARK 3 T11: 0.3013 T22: 1.3728 REMARK 3 T33: 0.2649 T12: -0.0391 REMARK 3 T13: -0.1032 T23: 0.1077 REMARK 3 L TENSOR REMARK 3 L11: 0.3105 L22: 2.1063 REMARK 3 L33: 2.3328 L12: 0.0622 REMARK 3 L13: -0.4766 L23: 0.4424 REMARK 3 S TENSOR REMARK 3 S11: -0.0851 S12: 0.4305 S13: 0.1550 REMARK 3 S21: -0.2861 S22: 0.0457 S23: -0.2797 REMARK 3 S31: 0.3003 S32: 0.4196 S33: -0.0297 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 135 THROUGH 203 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.5007 8.5169-119.6255 REMARK 3 T TENSOR REMARK 3 T11: 0.1627 T22: 1.1889 REMARK 3 T33: 0.1537 T12: -0.0827 REMARK 3 T13: -0.1629 T23: 0.0894 REMARK 3 L TENSOR REMARK 3 L11: 1.1251 L22: 1.1531 REMARK 3 L33: 1.9579 L12: 0.4918 REMARK 3 L13: 0.0487 L23: 0.6097 REMARK 3 S TENSOR REMARK 3 S11: 0.1831 S12: 0.6886 S13: 0.5045 REMARK 3 S21: 0.0745 S22: -0.0576 S23: 0.4961 REMARK 3 S31: -0.3456 S32: 0.2369 S33: 0.0085 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 204 THROUGH 215 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.1832 14.2334-127.6358 REMARK 3 T TENSOR REMARK 3 T11: 0.4193 T22: 1.1750 REMARK 3 T33: 0.4258 T12: -0.1588 REMARK 3 T13: 0.0018 T23: 0.1593 REMARK 3 L TENSOR REMARK 3 L11: 2.4229 L22: 1.3501 REMARK 3 L33: 2.4922 L12: -0.0511 REMARK 3 L13: -0.7580 L23: 0.7433 REMARK 3 S TENSOR REMARK 3 S11: -0.0036 S12: 0.5402 S13: 0.2112 REMARK 3 S21: -0.3816 S22: 0.0960 S23: 0.0667 REMARK 3 S31: -0.4166 S32: 0.1651 S33: -0.1212 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 0 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.3058 -12.7018 -92.6229 REMARK 3 T TENSOR REMARK 3 T11: 0.1573 T22: 0.4524 REMARK 3 T33: 0.2035 T12: 0.0134 REMARK 3 T13: 0.0179 T23: 0.0275 REMARK 3 L TENSOR REMARK 3 L11: 4.0437 L22: 3.7436 REMARK 3 L33: 4.2334 L12: -2.1116 REMARK 3 L13: -3.0017 L23: 2.4604 REMARK 3 S TENSOR REMARK 3 S11: -0.1477 S12: 0.3167 S13: -0.2309 REMARK 3 S21: -0.2253 S22: 0.1871 S23: -0.1833 REMARK 3 S31: -0.0451 S32: 0.7039 S33: -0.0918 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 19 THROUGH 48 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.3820 -8.1272 -90.8850 REMARK 3 T TENSOR REMARK 3 T11: 0.1403 T22: 0.3790 REMARK 3 T33: 0.1967 T12: -0.0533 REMARK 3 T13: -0.0034 T23: -0.0277 REMARK 3 L TENSOR REMARK 3 L11: 0.5526 L22: 1.2831 REMARK 3 L33: 2.5862 L12: -0.1963 REMARK 3 L13: -1.0087 L23: -0.4213 REMARK 3 S TENSOR REMARK 3 S11: -0.1391 S12: 0.5224 S13: -0.0820 REMARK 3 S21: -0.1564 S22: 0.0350 S23: -0.1062 REMARK 3 S31: 0.0386 S32: 0.0612 S33: 0.1105 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 49 THROUGH 75 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.5919 -14.8998 -91.5012 REMARK 3 T TENSOR REMARK 3 T11: 0.1597 T22: 0.3816 REMARK 3 T33: 0.1813 T12: -0.0496 REMARK 3 T13: 0.0063 T23: -0.0422 REMARK 3 L TENSOR REMARK 3 L11: 2.3429 L22: 1.6220 REMARK 3 L33: 0.7528 L12: 0.1635 REMARK 3 L13: -0.9819 L23: 0.7048 REMARK 3 S TENSOR REMARK 3 S11: -0.0548 S12: 0.6478 S13: -0.2805 REMARK 3 S21: -0.1422 S22: 0.0692 S23: -0.0233 REMARK 3 S31: 0.1428 S32: -0.2244 S33: -0.0368 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 76 THROUGH 90 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.1401 -11.3259 -99.5763 REMARK 3 T TENSOR REMARK 3 T11: 0.1587 T22: 0.6202 REMARK 3 T33: 0.2063 T12: -0.0577 REMARK 3 T13: 0.0155 T23: -0.0536 REMARK 3 L TENSOR REMARK 3 L11: 0.8863 L22: 1.7447 REMARK 3 L33: 3.0778 L12: -0.1884 REMARK 3 L13: -0.4777 L23: -2.1149 REMARK 3 S TENSOR REMARK 3 S11: -0.0042 S12: 0.6175 S13: -0.3351 REMARK 3 S21: -0.3311 S22: -0.1707 S23: -0.1579 REMARK 3 S31: 0.0850 S32: -0.2747 S33: 0.1845 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 91 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.1722 -7.3745 -95.9381 REMARK 3 T TENSOR REMARK 3 T11: 0.2161 T22: 0.6499 REMARK 3 T33: 0.1935 T12: -0.0543 REMARK 3 T13: -0.0053 T23: -0.0196 REMARK 3 L TENSOR REMARK 3 L11: 1.1025 L22: 0.4216 REMARK 3 L33: 2.7074 L12: -0.3932 REMARK 3 L13: -1.6854 L23: 0.6034 REMARK 3 S TENSOR REMARK 3 S11: -0.2280 S12: 0.3719 S13: 0.0191 REMARK 3 S21: -0.0380 S22: 0.2191 S23: -0.1342 REMARK 3 S31: 0.1471 S32: 0.3338 S33: 0.0114 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 114 THROUGH 163 ) REMARK 3 ORIGIN FOR THE GROUP (A): 33.4144 4.7299-114.2821 REMARK 3 T TENSOR REMARK 3 T11: 0.2720 T22: 0.9476 REMARK 3 T33: 0.2535 T12: -0.1026 REMARK 3 T13: -0.0412 T23: 0.1042 REMARK 3 L TENSOR REMARK 3 L11: 2.1883 L22: 0.7846 REMARK 3 L33: 0.3448 L12: 0.7528 REMARK 3 L13: -0.0995 L23: 0.4495 REMARK 3 S TENSOR REMARK 3 S11: 0.0151 S12: 0.6394 S13: 0.1824 REMARK 3 S21: 0.0497 S22: 0.0460 S23: 0.0379 REMARK 3 S31: -0.1217 S32: 0.0233 S33: -0.0331 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 164 THROUGH 213 ) REMARK 3 ORIGIN FOR THE GROUP (A): 34.4090 2.0809-115.5317 REMARK 3 T TENSOR REMARK 3 T11: 0.2920 T22: 0.9171 REMARK 3 T33: 0.2445 T12: -0.1253 REMARK 3 T13: -0.0157 T23: 0.0344 REMARK 3 L TENSOR REMARK 3 L11: 0.8747 L22: 1.7101 REMARK 3 L33: 1.0829 L12: 0.0706 REMARK 3 L13: 0.0356 L23: 0.0696 REMARK 3 S TENSOR REMARK 3 S11: -0.1438 S12: 0.6059 S13: 0.0675 REMARK 3 S21: -0.0347 S22: 0.0672 S23: -0.1468 REMARK 3 S31: 0.0271 S32: -0.0357 S33: 0.0747 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 2 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "A" and (resid 1 through 2 or REMARK 3 resid 4 or resid 6 through 31I or resid REMARK 3 31K through 131 or resid 136 through 142 REMARK 3 or resid 144 through 195 or resid 197 REMARK 3 through 214)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "H" and (resid 1 through 2 or REMARK 3 resid 4 or resid 6 through 31I or resid REMARK 3 31K through 142 or resid 144 through 195 REMARK 3 or resid 197 through 214)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "B" and (resid 0 through 6 or REMARK 3 resid 8 through 17 or resid 19 through REMARK 3 27A or resid 29 through 52 or resid 54 REMARK 3 through 78 or resid 80 through 113 or REMARK 3 resid 115 through 126 or resid 128 REMARK 3 through 173 or resid 175 through 213)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "L" and (resid 0 through 6 or REMARK 3 resid 8 through 17 or resid 19 through REMARK 3 27A or resid 29 through 52 or resid 54 REMARK 3 through 78 or resid 80 through 113 or REMARK 3 resid 115 through 126 or resid 128 REMARK 3 through 173 or resid 175 through 213)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 8GBV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAR-23. REMARK 100 THE DEPOSITION ID IS D_1000272545. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 25-JUL-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.03320 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53284 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.080 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1 REMARK 200 DATA REDUNDANCY : 4.400 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.24000 REMARK 200 FOR THE DATA SET : 7.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.08 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9 REMARK 200 DATA REDUNDANCY IN SHELL : 4.40 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 1.58000 REMARK 200 FOR SHELL : 1.200 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER 2.8.3 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47.31 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CALCIUM ACETATE, 0.1 M IMIDAZOLE REMARK 280 (PH 8), 10% W/V PEG 8000, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 293.15K 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: DIMERIC 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 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 REMARK 465 GLY H 134 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 CYS L 214 REMARK 465 LYS A 129 REMARK 465 SER A 130 REMARK 465 CYS A 216 REMARK 465 ASP A 217 REMARK 465 CYS B 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 H 15 -6.68 76.19 REMARK 500 SER H 127 -159.57 -94.05 REMARK 500 ASP H 144 69.34 61.19 REMARK 500 ASP L 50 72.68 51.87 REMARK 500 ALA L 84 -171.10 -172.05 REMARK 500 LYS L 190 -63.04 -103.48 REMARK 500 SER A 15 -6.07 77.12 REMARK 500 ASP A 144 70.43 60.95 REMARK 500 ASP A 144 70.43 61.19 REMARK 500 ASP B 50 72.38 52.81 REMARK 500 ALA B 84 -169.42 -172.25 REMARK 500 LYS B 190 -62.81 -103.08 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 8GBW RELATED DB: PDB REMARK 900 RELATED ID: 8GBX RELATED DB: PDB REMARK 900 RELATED ID: 8GBY RELATED DB: PDB REMARK 900 RELATED ID: 8GBZ RELATED DB: PDB REMARK 900 RELATED ID: 8GC0 RELATED DB: PDB REMARK 900 RELATED ID: 8GC1 RELATED DB: PDB DBREF 8GBV H 1 217 PDB 8GBV 8GBV 1 217 DBREF 8GBV L 0 214 PDB 8GBV 8GBV 0 214 DBREF 8GBV A 1 217 PDB 8GBV 8GBV 1 217 DBREF 8GBV B 0 214 PDB 8GBV 8GBV 0 214 SEQRES 1 H 243 GLN VAL GLN LEU LYS GLN TRP GLY ALA GLY LEU LEU LYS SEQRES 2 H 243 PRO SER GLU THR LEU SER LEU THR CYS THR VAL TYR GLY SEQRES 3 H 243 ASP SER LEU SER ASP TYR SER TRP SER TRP GLY VAL SER SEQRES 4 H 243 ARG SER ASP TYR TYR TRP SER TRP ILE ARG GLN PRO PRO SEQRES 5 H 243 GLY LYS GLY LEU GLU TRP ILE GLY GLU ILE ASN ARG SER SEQRES 6 H 243 GLY SER THR LYS TYR ASN PRO SER LEU LYS SER ARG VAL SEQRES 7 H 243 SER ILE LEU ILE GLU ALA SER LYS ASN GLN PHE SER LEU SEQRES 8 H 243 LYS LEU PRO SER VAL THR ALA ALA ASP THR ALA VAL TYR SEQRES 9 H 243 TYR CYS ALA ARG GLY ARG ARG SER ARG GLN TRP ILE GLY SEQRES 10 H 243 GLU LEU PRO PRO GLY ASN TYR GLY LEU ASP VAL TRP GLY SEQRES 11 H 243 GLN GLY THR PRO VAL SER VAL SER SER ALA SER THR LYS SEQRES 12 H 243 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 13 H 243 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 14 H 243 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 15 H 243 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 16 H 243 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 17 H 243 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 18 H 243 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 19 H 243 LYS ARG VAL GLU PRO LYS SER CYS ASP SEQRES 1 L 217 HIS GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER SEQRES 2 L 217 LEU SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SEQRES 3 L 217 SER GLN SER VAL SER SER SER TYR LEU ALA TRP TYR GLN SEQRES 4 L 217 HIS LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE SER ASP SEQRES 5 L 217 VAL TYR ARG ARG ALA THR GLY ILE PRO ASP ARG PHE SER SEQRES 6 L 217 GLY SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER SEQRES 7 L 217 ARG LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN SEQRES 8 L 217 GLN TYR GLY SER SER PRO PRO TYR THR PHE GLY GLN GLY SEQRES 9 L 217 THR LYS LEU GLU ILE 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 SEQRES 1 A 243 GLN VAL GLN LEU LYS GLN TRP GLY ALA GLY LEU LEU LYS SEQRES 2 A 243 PRO SER GLU THR LEU SER LEU THR CYS THR VAL TYR GLY SEQRES 3 A 243 ASP SER LEU SER ASP TYR SER TRP SER TRP GLY VAL SER SEQRES 4 A 243 ARG SER ASP TYR TYR TRP SER TRP ILE ARG GLN PRO PRO SEQRES 5 A 243 GLY LYS GLY LEU GLU TRP ILE GLY GLU ILE ASN ARG SER SEQRES 6 A 243 GLY SER THR LYS TYR ASN PRO SER LEU LYS SER ARG VAL SEQRES 7 A 243 SER ILE LEU ILE GLU ALA SER LYS ASN GLN PHE SER LEU SEQRES 8 A 243 LYS LEU PRO SER VAL THR ALA ALA ASP THR ALA VAL TYR SEQRES 9 A 243 TYR CYS ALA ARG GLY ARG ARG SER ARG GLN TRP ILE GLY SEQRES 10 A 243 GLU LEU PRO PRO GLY ASN TYR GLY LEU ASP VAL TRP GLY SEQRES 11 A 243 GLN GLY THR PRO VAL SER VAL SER SER ALA SER THR LYS SEQRES 12 A 243 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 13 A 243 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 14 A 243 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 15 A 243 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 16 A 243 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 17 A 243 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 18 A 243 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 19 A 243 LYS ARG VAL GLU PRO LYS SER CYS ASP SEQRES 1 B 217 HIS GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER SEQRES 2 B 217 LEU SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SEQRES 3 B 217 SER GLN SER VAL SER SER SER TYR LEU ALA TRP TYR GLN SEQRES 4 B 217 HIS LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE SER ASP SEQRES 5 B 217 VAL TYR ARG ARG ALA THR GLY ILE PRO ASP ARG PHE SER SEQRES 6 B 217 GLY SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER SEQRES 7 B 217 ARG LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN SEQRES 8 B 217 GLN TYR GLY SER SER PRO PRO TYR THR PHE GLY GLN GLY SEQRES 9 B 217 THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER SEQRES 10 B 217 VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER SEQRES 11 B 217 GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR SEQRES 12 B 217 PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA SEQRES 13 B 217 LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN SEQRES 14 B 217 ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU SEQRES 15 B 217 THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR SEQRES 16 B 217 ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL SEQRES 17 B 217 THR LYS SER PHE ASN ARG GLY GLU CYS HET EDO H 301 4 HET EDO H 302 4 HET ACT H 303 4 HET EDO L 301 4 HET EDO L 302 4 HET EDO L 303 4 HET EDO L 304 4 HET EDO L 305 4 HET EDO L 306 4 HET EDO L 307 4 HET EDO A 301 4 HET EDO A 302 4 HET EDO A 303 4 HET EDO B 301 4 HET EDO B 302 4 HET EDO B 303 4 HET EDO B 304 4 HET EDO B 305 4 HETNAM EDO 1,2-ETHANEDIOL HETNAM ACT ACETATE ION HETSYN EDO ETHYLENE GLYCOL FORMUL 5 EDO 17(C2 H6 O2) FORMUL 7 ACT C2 H3 O2 1- FORMUL 23 HOH *565(H2 O) HELIX 1 AA1 SER H 31H SER H 31J 5 3 HELIX 2 AA2 ALA H 73 LYS H 75 5 3 HELIX 3 AA3 THR H 83 THR H 87 5 5 HELIX 4 AA4 SER H 156 ALA H 158 5 3 HELIX 5 AA5 PRO H 185 GLY H 190 5 6 HELIX 6 AA6 LYS H 201 ASN H 204 5 4 HELIX 7 AA7 SER L 29 SER L 31 5 3 HELIX 8 AA8 GLU L 79 PHE L 83 5 5 HELIX 9 AA9 SER L 121 SER L 127 1 7 HELIX 10 AB1 LYS L 183 GLU L 187 1 5 HELIX 11 AB2 SER A 31H SER A 31J 5 3 HELIX 12 AB3 ALA A 73 LYS A 75 5 3 HELIX 13 AB4 THR A 83 THR A 87 5 5 HELIX 14 AB5 SER A 156 ALA A 158 5 3 HELIX 15 AB6 SER A 187 GLY A 190 5 4 HELIX 16 AB7 LYS A 201 ASN A 204 5 4 HELIX 17 AB8 SER B 29 SER B 31 5 3 HELIX 18 AB9 GLU B 79 PHE B 83 5 5 HELIX 19 AC1 SER B 121 LYS B 126 1 6 HELIX 20 AC2 LYS B 183 GLU B 187 1 5 SHEET 1 AA1 4 GLN H 3 GLY H 8 0 SHEET 2 AA1 4 LEU H 18 TYR H 25 -1 O THR H 23 N LYS H 5 SHEET 3 AA1 4 GLN H 77 LEU H 82 -1 O LEU H 82 N LEU H 18 SHEET 4 AA1 4 SER H 68 GLU H 72 -1 N GLU H 72 O GLN H 77 SHEET 1 AA2 6 LEU H 11 LEU H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O SER H 110 N LEU H 12 SHEET 3 AA2 6 ALA H 88 ARG H 96 -1 N ALA H 88 O VAL H 109 SHEET 4 AA2 6 TYR H 32 GLN H 39 -1 N ILE H 37 O TYR H 91 SHEET 5 AA2 6 GLU H 46 ILE H 51 -1 O ILE H 48 N TRP H 36 SHEET 6 AA2 6 THR H 57 TYR H 59 -1 O LYS H 58 N GLU H 50 SHEET 1 AA3 4 LEU H 11 LEU H 12 0 SHEET 2 AA3 4 THR H 107 VAL H 111 1 O SER H 110 N LEU H 12 SHEET 3 AA3 4 ALA H 88 ARG H 96 -1 N ALA H 88 O VAL H 109 SHEET 4 AA3 4 GLY H 100K TRP H 103 -1 O VAL H 102 N ARG H 94 SHEET 1 AA4 4 SER H 120 LEU H 124 0 SHEET 2 AA4 4 ALA H 136 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AA4 4 TYR H 176 VAL H 184 -1 O VAL H 184 N ALA H 136 SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA5 4 SER H 120 LEU H 124 0 SHEET 2 AA5 4 ALA H 136 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AA5 4 TYR H 176 VAL H 184 -1 O VAL H 184 N ALA H 136 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 197 N SER H 153 SHEET 3 AA6 3 THR H 205 ARG H 210 -1 O THR H 205 N HIS H 200 SHEET 1 AA7 3 LEU L 4 SER L 7 0 SHEET 2 AA7 3 ALA L 19 VAL L 28 -1 O ARG L 24 N THR L 5 SHEET 3 AA7 3 PHE L 62 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 1 AA8 6 THR L 10 LEU L 13 0 SHEET 2 AA8 6 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AA8 6 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AA8 6 LEU L 33 HIS L 38 -1 N ALA L 34 O GLN L 89 SHEET 5 AA8 6 ARG L 45 SER L 49 -1 O ARG L 45 N GLN L 37 SHEET 6 AA8 6 ARG L 53 ARG L 54 -1 O ARG L 53 N SER L 49 SHEET 1 AA9 4 SER L 114 PHE L 118 0 SHEET 2 AA9 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AA9 4 TYR L 173 SER L 182 -1 O LEU L 181 N ALA L 130 SHEET 4 AA9 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176 SHEET 1 AB1 4 ALA L 153 LEU L 154 0 SHEET 2 AB1 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB1 4 VAL L 191 THR L 197 -1 O ALA L 193 N LYS L 149 SHEET 4 AB1 4 VAL L 205 ASN L 210 -1 O LYS L 207 N CYS L 194 SHEET 1 AB2 4 GLN A 3 GLY A 8 0 SHEET 2 AB2 4 LEU A 18 TYR A 25 -1 O TYR A 25 N GLN A 3 SHEET 3 AB2 4 GLN A 77 LEU A 82 -1 O LEU A 82 N LEU A 18 SHEET 4 AB2 4 SER A 68 GLU A 72 -1 N GLU A 72 O GLN A 77 SHEET 1 AB3 6 LEU A 11 LEU A 12 0 SHEET 2 AB3 6 THR A 107 VAL A 111 1 O SER A 110 N LEU A 12 SHEET 3 AB3 6 ALA A 88 ARG A 96 -1 N ALA A 88 O VAL A 109 SHEET 4 AB3 6 TYR A 32 GLN A 39 -1 N ILE A 37 O TYR A 91 SHEET 5 AB3 6 GLU A 46 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AB3 6 THR A 57 TYR A 59 -1 O LYS A 58 N GLU A 50 SHEET 1 AB4 4 LEU A 11 LEU A 12 0 SHEET 2 AB4 4 THR A 107 VAL A 111 1 O SER A 110 N LEU A 12 SHEET 3 AB4 4 ALA A 88 ARG A 96 -1 N ALA A 88 O VAL A 109 SHEET 4 AB4 4 GLY A 100K TRP A 103 -1 O VAL A 102 N ARG A 94 SHEET 1 AB5 4 SER A 120 LEU A 124 0 SHEET 2 AB5 4 THR A 135 TYR A 145 -1 O GLY A 139 N LEU A 124 SHEET 3 AB5 4 TYR A 176 PRO A 185 -1 O VAL A 184 N ALA A 136 SHEET 4 AB5 4 VAL A 163 THR A 165 -1 N HIS A 164 O VAL A 181 SHEET 1 AB6 4 SER A 120 LEU A 124 0 SHEET 2 AB6 4 THR A 135 TYR A 145 -1 O GLY A 139 N LEU A 124 SHEET 3 AB6 4 TYR A 176 PRO A 185 -1 O VAL A 184 N ALA A 136 SHEET 4 AB6 4 VAL A 169 LEU A 170 -1 N VAL A 169 O SER A 177 SHEET 1 AB7 3 THR A 151 TRP A 154 0 SHEET 2 AB7 3 ILE A 195 HIS A 200 -1 O ASN A 197 N SER A 153 SHEET 3 AB7 3 THR A 205 ARG A 210 -1 O THR A 205 N HIS A 200 SHEET 1 AB8 4 LEU B 4 SER B 7 0 SHEET 2 AB8 4 ALA B 19 ALA B 25 -1 O SER B 22 N SER B 7 SHEET 3 AB8 4 ASP B 70 ILE B 75 -1 O PHE B 71 N CYS B 23 SHEET 4 AB8 4 PHE B 62 SER B 67 -1 N SER B 63 O THR B 74 SHEET 1 AB9 6 THR B 10 LEU B 13 0 SHEET 2 AB9 6 THR B 102 ILE B 106 1 O LYS B 103 N LEU B 11 SHEET 3 AB9 6 VAL B 85 GLN B 90 -1 N TYR B 86 O THR B 102 SHEET 4 AB9 6 LEU B 33 HIS B 38 -1 N ALA B 34 O GLN B 89 SHEET 5 AB9 6 ARG B 45 SER B 49 -1 O ARG B 45 N GLN B 37 SHEET 6 AB9 6 ARG B 53 ARG B 54 -1 O ARG B 53 N SER B 49 SHEET 1 AC1 4 SER B 114 PHE B 118 0 SHEET 2 AC1 4 THR B 129 PHE B 139 -1 O LEU B 135 N PHE B 116 SHEET 3 AC1 4 TYR B 173 SER B 182 -1 O LEU B 181 N ALA B 130 SHEET 4 AC1 4 SER B 159 VAL B 163 -1 N GLN B 160 O THR B 178 SHEET 1 AC2 4 ALA B 153 LEU B 154 0 SHEET 2 AC2 4 LYS B 145 VAL B 150 -1 N VAL B 150 O ALA B 153 SHEET 3 AC2 4 VAL B 191 THR B 197 -1 O ALA B 193 N LYS B 149 SHEET 4 AC2 4 VAL B 205 ASN B 210 -1 O LYS B 207 N CYS B 194 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.02 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.04 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 A 22 CYS A 92 1555 1555 2.03 SSBOND 6 CYS A 140 CYS A 196 1555 1555 2.03 SSBOND 7 CYS B 23 CYS B 88 1555 1555 2.04 SSBOND 8 CYS B 134 CYS B 194 1555 1555 2.04 CISPEP 1 PHE H 146 PRO H 147 0 -5.73 CISPEP 2 GLU H 148 PRO H 149 0 -4.39 CISPEP 3 SER L 7 PRO L 8 0 -4.61 CISPEP 4 PRO L 95 PRO L 95A 0 1.64 CISPEP 5 TYR L 140 PRO L 141 0 2.44 CISPEP 6 PHE A 146 PRO A 147 0 -6.29 CISPEP 7 GLU A 148 PRO A 149 0 -2.76 CISPEP 8 SER B 7 PRO B 8 0 -3.37 CISPEP 9 SER B 7 PRO B 8 0 -4.69 CISPEP 10 PRO B 95 PRO B 95A 0 1.93 CISPEP 11 TYR B 140 PRO B 141 0 1.61 CRYST1 43.519 48.969 113.878 93.07 98.26 102.49 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 0.022978 0.005089 0.003796 0.00000 SCALE2 0.000000 0.020916 0.001840 0.00000 SCALE3 0.000000 0.000000 0.008908 0.00000 MTRIX1 1 -0.999991 -0.003851 -0.002012 33.90634 1 MTRIX2 1 -0.004237 0.761693 0.647924 47.98691 1 MTRIX3 1 -0.000962 0.647926 -0.761702 -131.04101 1 MTRIX1 2 -0.999987 0.004818 0.001544 34.24843 1 MTRIX2 2 0.004659 0.758142 0.652072 48.35170 1 MTRIX3 2 0.001971 0.652071 -0.758155 -130.75364 1