HEADER IMMUNE SYSTEM 05-JUN-17 5W24 TITLE CRYSTAL STRUCTURE OF 5C4 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: 5C4 FAB LIGHT CHAIN; COMPND 3 CHAIN: L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 5C4 FAB HEAVY CHAIN; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 STRAIN: BALB/C; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: EXPI293; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PVRC8400; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 12 ORGANISM_TAXID: 10090; SOURCE 13 STRAIN: BALB/C; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: EXPI293; SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PVRC8400 KEYWDS FAB, ANTIBODY, NEUTRALIZING ANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR M.B.BATTLES,J.S.MCLELLAN,N.M.TAHER REVDAT 2 13-DEC-17 5W24 1 JRNL REVDAT 1 06-DEC-17 5W24 0 JRNL AUTH D.TIAN,M.B.BATTLES,S.M.MOIN,M.CHEN,K.MODJARRAD,A.KUMAR, JRNL AUTH 2 M.KANEKIYO,K.W.GRAEPEL,N.M.TAHER,A.L.HOTARD,M.L.MOORE, JRNL AUTH 3 M.ZHAO,Z.Z.ZHENG,N.S.XIA,J.S.MCLELLAN,B.S.GRAHAM JRNL TITL STRUCTURAL BASIS OF RESPIRATORY SYNCYTIAL VIRUS JRNL TITL 2 SUBTYPE-DEPENDENT NEUTRALIZATION BY AN ANTIBODY TARGETING JRNL TITL 3 THE FUSION GLYCOPROTEIN. JRNL REF NAT COMMUN V. 8 1877 2017 JRNL REFN ESSN 2041-1723 JRNL PMID 29187732 JRNL DOI 10.1038/S41467-017-01858-W REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.B.BATTLES,J.S.MCLELLAN,N.M.TAHER REMARK 1 TITL STRUCTURE OF 5C4 FAB REMARK 1 REF TO BE PUBLISHED REMARK 1 REFN REMARK 2 REMARK 2 RESOLUTION. 1.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.11.1_2575 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.88 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.4 REMARK 3 NUMBER OF REFLECTIONS : 60747 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.171 REMARK 3 R VALUE (WORKING SET) : 0.170 REMARK 3 FREE R VALUE : 0.203 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040 REMARK 3 FREE R VALUE TEST SET COUNT : 3064 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 32.8907 - 4.2003 0.92 2686 131 0.1532 0.1702 REMARK 3 2 4.2003 - 3.3349 0.97 2762 140 0.1463 0.1729 REMARK 3 3 3.3349 - 2.9137 0.97 2735 144 0.1569 0.1982 REMARK 3 4 2.9137 - 2.6474 0.97 2701 169 0.1697 0.1979 REMARK 3 5 2.6474 - 2.4577 0.97 2709 147 0.1731 0.1914 REMARK 3 6 2.4577 - 2.3128 0.96 2743 132 0.1736 0.2227 REMARK 3 7 2.3128 - 2.1970 0.96 2667 162 0.1653 0.2391 REMARK 3 8 2.1970 - 2.1014 0.96 2689 144 0.1692 0.1930 REMARK 3 9 2.1014 - 2.0205 0.96 2660 149 0.1724 0.2259 REMARK 3 10 2.0205 - 1.9508 0.96 2708 140 0.1723 0.1820 REMARK 3 11 1.9508 - 1.8898 0.95 2650 155 0.1805 0.1793 REMARK 3 12 1.8898 - 1.8358 0.95 2667 163 0.1858 0.2366 REMARK 3 13 1.8358 - 1.7875 0.95 2638 151 0.1847 0.2285 REMARK 3 14 1.7875 - 1.7439 0.95 2657 135 0.1888 0.2350 REMARK 3 15 1.7439 - 1.7042 0.95 2661 117 0.1927 0.2038 REMARK 3 16 1.7042 - 1.6680 0.95 2651 147 0.1919 0.2157 REMARK 3 17 1.6680 - 1.6346 0.94 2641 128 0.1973 0.2564 REMARK 3 18 1.6346 - 1.6038 0.94 2657 136 0.1995 0.2571 REMARK 3 19 1.6038 - 1.5751 0.94 2621 129 0.1994 0.2446 REMARK 3 20 1.5751 - 1.5484 0.93 2592 147 0.2015 0.2291 REMARK 3 21 1.5484 - 1.5234 0.80 2255 107 0.2100 0.2367 REMARK 3 22 1.5234 - 1.5000 0.69 1933 91 0.2127 0.2519 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL 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) : 0.150 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.840 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 14.02 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.89 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 : 0.006 3407 REMARK 3 ANGLE : 0.846 4659 REMARK 3 CHIRALITY : 0.053 538 REMARK 3 PLANARITY : 0.005 595 REMARK 3 DIHEDRAL : 11.146 2046 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 19 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 88 THROUGH 111 ) REMARK 3 ORIGIN FOR THE GROUP (A): -4.0891 -85.7201 135.3894 REMARK 3 T TENSOR REMARK 3 T11: 0.0848 T22: 0.0591 REMARK 3 T33: 0.0697 T12: -0.0073 REMARK 3 T13: -0.0128 T23: -0.0126 REMARK 3 L TENSOR REMARK 3 L11: 3.2270 L22: 2.5832 REMARK 3 L33: 2.5377 L12: -0.1594 REMARK 3 L13: 1.3773 L23: -0.9252 REMARK 3 S TENSOR REMARK 3 S11: -0.1376 S12: -0.0825 S13: 0.2584 REMARK 3 S21: -0.0763 S22: -0.0267 S23: 0.1038 REMARK 3 S31: -0.0597 S32: -0.0766 S33: 0.1669 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 112 THROUGH 134 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.2667 -88.9721 132.1323 REMARK 3 T TENSOR REMARK 3 T11: 0.0806 T22: 0.1256 REMARK 3 T33: 0.1449 T12: 0.0204 REMARK 3 T13: -0.0210 T23: 0.0330 REMARK 3 L TENSOR REMARK 3 L11: 2.8230 L22: 2.7014 REMARK 3 L33: 1.4220 L12: 1.2812 REMARK 3 L13: -0.5090 L23: -0.1774 REMARK 3 S TENSOR REMARK 3 S11: 0.1659 S12: -0.1224 S13: -0.0481 REMARK 3 S21: 0.1416 S22: -0.2610 S23: -0.3192 REMARK 3 S31: -0.2460 S32: 0.5866 S33: 0.0643 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 135 THROUGH 184 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.3646 -85.7077 127.2517 REMARK 3 T TENSOR REMARK 3 T11: 0.0704 T22: 0.0617 REMARK 3 T33: 0.0712 T12: 0.0019 REMARK 3 T13: -0.0080 T23: 0.0013 REMARK 3 L TENSOR REMARK 3 L11: 2.4458 L22: 3.8790 REMARK 3 L33: 3.5638 L12: 0.9745 REMARK 3 L13: 0.0103 L23: -1.2444 REMARK 3 S TENSOR REMARK 3 S11: 0.0069 S12: 0.0444 S13: 0.0395 REMARK 3 S21: -0.0594 S22: -0.0481 S23: -0.0122 REMARK 3 S31: -0.0206 S32: 0.0110 S33: 0.0386 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 185 THROUGH 214 ) REMARK 3 ORIGIN FOR THE GROUP (A): 28.5167 -78.1099 129.9080 REMARK 3 T TENSOR REMARK 3 T11: 0.1606 T22: 0.1279 REMARK 3 T33: 0.1712 T12: -0.0601 REMARK 3 T13: -0.0315 T23: 0.0270 REMARK 3 L TENSOR REMARK 3 L11: 4.2089 L22: 3.6084 REMARK 3 L33: 2.5905 L12: 1.7506 REMARK 3 L13: -0.4829 L23: -0.8928 REMARK 3 S TENSOR REMARK 3 S11: 0.0205 S12: -0.0593 S13: 0.3636 REMARK 3 S21: 0.2315 S22: -0.1402 S23: -0.1152 REMARK 3 S31: -0.3877 S32: 0.4045 S33: 0.1182 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 25 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.5133 -93.2900 114.5069 REMARK 3 T TENSOR REMARK 3 T11: 0.1549 T22: 0.2936 REMARK 3 T33: 0.1226 T12: -0.0212 REMARK 3 T13: -0.0195 T23: -0.0277 REMARK 3 L TENSOR REMARK 3 L11: 3.1948 L22: 1.1160 REMARK 3 L33: 5.1088 L12: 0.7457 REMARK 3 L13: -1.8139 L23: -1.5406 REMARK 3 S TENSOR REMARK 3 S11: -0.1632 S12: 0.7827 S13: -0.0285 REMARK 3 S21: -0.1812 S22: 0.1156 S23: 0.0090 REMARK 3 S31: 0.1874 S32: -0.0774 S33: 0.0380 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 26 THROUGH 61 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.7704 -84.7555 123.3743 REMARK 3 T TENSOR REMARK 3 T11: 0.1092 T22: 0.1298 REMARK 3 T33: 0.1113 T12: -0.0010 REMARK 3 T13: -0.0264 T23: 0.0499 REMARK 3 L TENSOR REMARK 3 L11: 3.5205 L22: 0.7986 REMARK 3 L33: 1.8396 L12: -0.9194 REMARK 3 L13: -0.0882 L23: 0.1321 REMARK 3 S TENSOR REMARK 3 S11: -0.0247 S12: 0.4776 S13: 0.4844 REMARK 3 S21: -0.0917 S22: -0.0172 S23: 0.0315 REMARK 3 S31: -0.0983 S32: 0.1062 S33: 0.0379 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 62 THROUGH 90 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.9816 -87.2343 116.7836 REMARK 3 T TENSOR REMARK 3 T11: 0.1246 T22: 0.2859 REMARK 3 T33: 0.1210 T12: -0.0200 REMARK 3 T13: -0.0368 T23: 0.0635 REMARK 3 L TENSOR REMARK 3 L11: 2.3550 L22: 0.7995 REMARK 3 L33: 3.1573 L12: -0.8994 REMARK 3 L13: -0.9529 L23: -0.6570 REMARK 3 S TENSOR REMARK 3 S11: 0.0120 S12: 0.7276 S13: 0.3200 REMARK 3 S21: -0.1123 S22: -0.0269 S23: 0.0263 REMARK 3 S31: -0.0583 S32: -0.0040 S33: 0.0107 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 91 THROUGH 101 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.5633 -94.4923 130.3399 REMARK 3 T TENSOR REMARK 3 T11: 0.0599 T22: 0.0517 REMARK 3 T33: 0.0702 T12: -0.0124 REMARK 3 T13: -0.0170 T23: -0.0157 REMARK 3 L TENSOR REMARK 3 L11: 6.2820 L22: 3.9582 REMARK 3 L33: 9.3601 L12: -0.3869 REMARK 3 L13: -2.7733 L23: -1.1554 REMARK 3 S TENSOR REMARK 3 S11: -0.1331 S12: 0.2116 S13: -0.0555 REMARK 3 S21: 0.0708 S22: 0.0359 S23: 0.0467 REMARK 3 S31: 0.2034 S32: -0.1748 S33: 0.0997 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 102 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.7265 -89.1798 108.7750 REMARK 3 T TENSOR REMARK 3 T11: 0.2160 T22: 0.5625 REMARK 3 T33: 0.1266 T12: -0.0598 REMARK 3 T13: -0.0089 T23: 0.0150 REMARK 3 L TENSOR REMARK 3 L11: 0.7248 L22: 0.0915 REMARK 3 L33: 0.5797 L12: 0.3108 REMARK 3 L13: -0.6708 L23: -0.2337 REMARK 3 S TENSOR REMARK 3 S11: -0.2980 S12: 1.0779 S13: -0.0878 REMARK 3 S21: -0.3029 S22: 0.2212 S23: 0.0216 REMARK 3 S31: 0.1301 S32: -0.1549 S33: 0.0852 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 114 THROUGH 144 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.8884 -90.3634 119.7435 REMARK 3 T TENSOR REMARK 3 T11: 0.1409 T22: 0.1162 REMARK 3 T33: 0.1161 T12: 0.0266 REMARK 3 T13: 0.0453 T23: 0.0181 REMARK 3 L TENSOR REMARK 3 L11: 7.0764 L22: 2.7696 REMARK 3 L33: 5.6626 L12: -0.4364 REMARK 3 L13: 2.5215 L23: -0.6901 REMARK 3 S TENSOR REMARK 3 S11: -0.2127 S12: -0.0266 S13: -0.3368 REMARK 3 S21: -0.0701 S22: 0.1050 S23: -0.1633 REMARK 3 S31: 0.2865 S32: 0.1710 S33: 0.0991 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 145 THROUGH 155 ) REMARK 3 ORIGIN FOR THE GROUP (A): 32.3229-101.6731 114.7386 REMARK 3 T TENSOR REMARK 3 T11: 0.4573 T22: 0.4165 REMARK 3 T33: 0.5239 T12: 0.0363 REMARK 3 T13: 0.2170 T23: -0.1239 REMARK 3 L TENSOR REMARK 3 L11: 2.0162 L22: 5.2965 REMARK 3 L33: 0.9058 L12: -5.4593 REMARK 3 L13: -2.6905 L23: 0.4060 REMARK 3 S TENSOR REMARK 3 S11: -0.1900 S12: 0.9127 S13: -1.3739 REMARK 3 S21: -0.6139 S22: -0.1018 S23: 0.0036 REMARK 3 S31: 0.8075 S32: 0.4021 S33: 0.2299 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 156 THROUGH 174 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.6464 -91.3242 117.1913 REMARK 3 T TENSOR REMARK 3 T11: 0.1529 T22: 0.1909 REMARK 3 T33: 0.0891 T12: -0.0522 REMARK 3 T13: 0.0080 T23: -0.0530 REMARK 3 L TENSOR REMARK 3 L11: 9.1363 L22: 4.6754 REMARK 3 L33: 5.7201 L12: -4.3847 REMARK 3 L13: 3.6709 L23: -4.9785 REMARK 3 S TENSOR REMARK 3 S11: 0.0518 S12: 0.5385 S13: -0.2745 REMARK 3 S21: -0.3468 S22: -0.0035 S23: 0.1085 REMARK 3 S31: 0.3065 S32: -0.0996 S33: -0.0902 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 175 THROUGH 188 ) REMARK 3 ORIGIN FOR THE GROUP (A): 35.2925 -97.9668 125.1023 REMARK 3 T TENSOR REMARK 3 T11: 0.2719 T22: 0.4480 REMARK 3 T33: 0.3698 T12: 0.2735 REMARK 3 T13: 0.1494 T23: 0.1591 REMARK 3 L TENSOR REMARK 3 L11: 5.6257 L22: 4.5174 REMARK 3 L33: 0.7609 L12: -3.6544 REMARK 3 L13: 0.0699 L23: -1.3671 REMARK 3 S TENSOR REMARK 3 S11: -0.2945 S12: -0.3962 S13: -0.6059 REMARK 3 S21: -0.2880 S22: -0.1117 S23: -0.4766 REMARK 3 S31: 0.9053 S32: 0.7613 S33: 0.2643 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 189 THROUGH 211 ) REMARK 3 ORIGIN FOR THE GROUP (A): 32.3289 -94.9708 111.0062 REMARK 3 T TENSOR REMARK 3 T11: 0.3019 T22: 0.3945 REMARK 3 T33: 0.3112 T12: 0.0157 REMARK 3 T13: 0.1262 T23: -0.0889 REMARK 3 L TENSOR REMARK 3 L11: 5.6946 L22: 4.0033 REMARK 3 L33: 6.0405 L12: 0.0510 REMARK 3 L13: 1.8484 L23: 0.0641 REMARK 3 S TENSOR REMARK 3 S11: -0.1687 S12: 1.4481 S13: -0.8475 REMARK 3 S21: -0.4802 S22: -0.0954 S23: -0.0779 REMARK 3 S31: 0.4459 S32: 0.7913 S33: 0.1988 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 32 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.0388 -83.2184 143.1585 REMARK 3 T TENSOR REMARK 3 T11: 0.0829 T22: 0.0665 REMARK 3 T33: 0.0577 T12: -0.0132 REMARK 3 T13: -0.0102 T23: -0.0091 REMARK 3 L TENSOR REMARK 3 L11: 3.9690 L22: 5.0026 REMARK 3 L33: 1.1602 L12: -3.5173 REMARK 3 L13: 0.8735 L23: -0.8494 REMARK 3 S TENSOR REMARK 3 S11: -0.0825 S12: -0.1057 S13: 0.0930 REMARK 3 S21: 0.0403 S22: 0.0182 S23: -0.0611 REMARK 3 S31: -0.0455 S32: 0.0288 S33: 0.0871 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 33 THROUGH 44 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.5361 -91.8830 134.8311 REMARK 3 T TENSOR REMARK 3 T11: 0.1029 T22: 0.0803 REMARK 3 T33: 0.0832 T12: -0.0050 REMARK 3 T13: -0.0468 T23: 0.0032 REMARK 3 L TENSOR REMARK 3 L11: 8.1417 L22: 8.0162 REMARK 3 L33: 6.3703 L12: -3.7054 REMARK 3 L13: -2.0402 L23: 2.2154 REMARK 3 S TENSOR REMARK 3 S11: 0.0655 S12: 0.3831 S13: -0.6197 REMARK 3 S21: -0.2070 S22: -0.3179 S23: 0.2885 REMARK 3 S31: 0.3943 S32: 0.0827 S33: 0.1397 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 45 THROUGH 59 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.3713 -89.3791 142.1526 REMARK 3 T TENSOR REMARK 3 T11: 0.0653 T22: 0.1290 REMARK 3 T33: 0.1171 T12: -0.0310 REMARK 3 T13: -0.0070 T23: -0.0230 REMARK 3 L TENSOR REMARK 3 L11: 1.9311 L22: 1.3986 REMARK 3 L33: 2.7032 L12: -0.3460 REMARK 3 L13: -0.6385 L23: 0.2157 REMARK 3 S TENSOR REMARK 3 S11: -0.0300 S12: 0.1351 S13: -0.0833 REMARK 3 S21: 0.1236 S22: -0.1836 S23: 0.2008 REMARK 3 S31: 0.2477 S32: -0.4848 S33: 0.1245 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 60 THROUGH 72 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.5897 -94.8230 144.9488 REMARK 3 T TENSOR REMARK 3 T11: 0.1249 T22: 0.0901 REMARK 3 T33: 0.1089 T12: -0.0338 REMARK 3 T13: 0.0026 T23: 0.0339 REMARK 3 L TENSOR REMARK 3 L11: 2.3881 L22: 2.6890 REMARK 3 L33: 2.7155 L12: -0.3818 REMARK 3 L13: -0.0627 L23: 0.1315 REMARK 3 S TENSOR REMARK 3 S11: -0.0572 S12: -0.1534 S13: -0.3609 REMARK 3 S21: 0.1066 S22: 0.0790 S23: 0.1250 REMARK 3 S31: 0.4288 S32: -0.0321 S33: 0.1418 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 73 THROUGH 87 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.5387 -91.0050 146.0192 REMARK 3 T TENSOR REMARK 3 T11: 0.1083 T22: 0.0708 REMARK 3 T33: 0.0791 T12: -0.0068 REMARK 3 T13: -0.0058 T23: 0.0300 REMARK 3 L TENSOR REMARK 3 L11: 2.0522 L22: 2.3933 REMARK 3 L33: 1.5815 L12: -0.5918 REMARK 3 L13: -0.1692 L23: -0.5306 REMARK 3 S TENSOR REMARK 3 S11: -0.1538 S12: -0.1601 S13: -0.2047 REMARK 3 S21: 0.2521 S22: 0.0246 S23: 0.1141 REMARK 3 S31: 0.1973 S32: 0.0875 S33: 0.1121 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 5W24 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUN-17. REMARK 100 THE DEPOSITION ID IS D_1000228271. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 25-MAR-14 REMARK 200 TEMPERATURE (KELVIN) : 293 REMARK 200 PH : 4.6 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS REMARK 200 BEAMLINE : X6A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AIMLESS REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.3.6 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60748 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500 REMARK 200 RESOLUTION RANGE LOW (A) : 32.883 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.7 REMARK 200 DATA REDUNDANCY : 3.700 REMARK 200 R MERGE (I) : 0.04400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53 REMARK 200 COMPLETENESS FOR SHELL (%) : 69.7 REMARK 200 DATA REDUNDANCY IN SHELL : 3.50 REMARK 200 R MERGE FOR SHELL (I) : 0.23400 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: 3T3P, 4GAG REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 36.22 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10.1 M SODIUM ACETATE TRIHYDRATE PH REMARK 280 4.6 AND 20% PEG 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 58.48000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.50500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 58.48000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 31.50500 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3710 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19370 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH L 483 LIES ON A SPECIAL POSITION. REMARK 375 HOH L 548 LIES ON A SPECIAL POSITION. REMARK 375 HOH H 418 LIES ON A SPECIAL POSITION. REMARK 375 HOH H 739 LIES ON A SPECIAL POSITION. 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 MET L -22 REMARK 465 ARG L -21 REMARK 465 PRO L -20 REMARK 465 THR L -19 REMARK 465 TRP L -18 REMARK 465 ALA L -17 REMARK 465 TRP L -16 REMARK 465 TRP L -15 REMARK 465 LEU L -14 REMARK 465 PHE L -13 REMARK 465 LEU L -12 REMARK 465 VAL L -11 REMARK 465 LEU L -10 REMARK 465 LEU L -9 REMARK 465 LEU L -8 REMARK 465 ALA L -7 REMARK 465 LEU L -6 REMARK 465 TRP L -5 REMARK 465 ALA L -4 REMARK 465 PRO L -3 REMARK 465 ALA L -2 REMARK 465 ARG L -1 REMARK 465 GLY L 0 REMARK 465 ASN L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 REMARK 465 MET H -22 REMARK 465 ARG H -21 REMARK 465 PRO H -20 REMARK 465 THR H -19 REMARK 465 TRP H -18 REMARK 465 ALA H -17 REMARK 465 TRP H -16 REMARK 465 TRP H -15 REMARK 465 LEU H -14 REMARK 465 PHE H -13 REMARK 465 LEU H -12 REMARK 465 VAL H -11 REMARK 465 LEU H -10 REMARK 465 LEU H -9 REMARK 465 LEU H -8 REMARK 465 ALA H -7 REMARK 465 LEU H -6 REMARK 465 TRP H -5 REMARK 465 ALA H -4 REMARK 465 PRO H -3 REMARK 465 ALA H -2 REMARK 465 ARG H -1 REMARK 465 GLY H 0 REMARK 465 ALA H 97A REMARK 465 VAL H 97B REMARK 465 VAL H 97C REMARK 465 PRO H 97D REMARK 465 THR H 97E REMARK 465 GLY H 129 REMARK 465 GLY H 130 REMARK 465 THR H 131 REMARK 465 THR H 132 REMARK 465 PRO H 215 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ARG H 213 O REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O HOH H 411 O HOH H 544 2.03 REMARK 500 O PRO H 100C O HOH H 401 2.13 REMARK 500 O HOH H 671 O HOH H 733 2.15 REMARK 500 O ASP L 110 O HOH L 301 2.16 REMARK 500 O HOH L 315 O HOH L 493 2.16 REMARK 500 O HOH H 602 O HOH H 721 2.18 REMARK 500 O HOH H 599 O HOH H 652 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH H 404 O HOH H 496 45510 2.14 REMARK 500 O HOH H 417 O HOH H 654 45410 2.15 REMARK 500 NH2 ARG L 24 OD2 ASP L 70 2559 2.17 REMARK 500 REMARK 500 REMARK: NULL 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 ALA L 51 -40.29 71.79 REMARK 500 ALA L 60 36.65 -72.97 REMARK 500 ARG L 68 -98.32 62.55 REMARK 500 ALA L 84 172.66 178.27 REMARK 500 GLU H 42 19.07 59.86 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH L 566 DISTANCE = 6.10 ANGSTROMS REMARK 525 HOH L 567 DISTANCE = 6.30 ANGSTROMS REMARK 525 HOH H 739 DISTANCE = 6.45 ANGSTROMS REMARK 525 HOH H 740 DISTANCE = 6.45 ANGSTROMS REMARK 525 HOH H 741 DISTANCE = 6.89 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue BU3 H 301 DBREF 5W24 L -22 214 PDB 5W24 5W24 -22 214 DBREF 5W24 H -22 215 PDB 5W24 5W24 -22 215 SEQRES 1 L 241 MET ARG PRO THR TRP ALA TRP TRP LEU PHE LEU VAL LEU SEQRES 2 L 241 LEU LEU ALA LEU TRP ALA PRO ALA ARG GLY ASP ILE VAL SEQRES 3 L 241 LEU THR GLN SER PRO ALA SER LEU ALA VAL SER LEU GLY SEQRES 4 L 241 GLN ARG THR THR ILE SER CYS ARG ALA SER GLU SER VAL SEQRES 5 L 241 ASP SER PHE ASP ASN SER PHE ILE HIS TRP TYR GLN GLN SEQRES 6 L 241 LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE PHE LEU ALA SEQRES 7 L 241 SER SER LEU GLU SER GLY VAL PRO ALA ARG PHE SER GLY SEQRES 8 L 241 SER GLY SER ARG THR ASP PHE THR LEU THR ILE ASP PRO SEQRES 9 L 241 VAL GLU ALA ASP ASP ALA ALA THR TYR TYR CYS GLN GLN SEQRES 10 L 241 SER ASN GLU ASP PRO PHE THR PHE GLY SER GLY THR LYS SEQRES 11 L 241 LEU GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER SEQRES 12 L 241 ILE PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY SEQRES 13 L 241 ALA SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS SEQRES 14 L 241 ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG SEQRES 15 L 241 GLN ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER SEQRES 16 L 241 LYS ASP SER THR TYR SER MET SER SER THR LEU THR LEU SEQRES 17 L 241 THR LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS SEQRES 18 L 241 GLU ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SEQRES 19 L 241 SER PHE ASN ARG ASN GLU CYS SEQRES 1 H 249 MET ARG PRO THR TRP ALA TRP TRP LEU PHE LEU VAL LEU SEQRES 2 H 249 LEU LEU ALA LEU TRP ALA PRO ALA ARG GLY GLU VAL GLN SEQRES 3 H 249 LEU GLN GLN SER GLY ALA GLU LEU VAL LYS PRO GLY ALA SEQRES 4 H 249 SER VAL LYS LEU SER CYS THR ALA SER GLY PHE ASN ILE SEQRES 5 H 249 LYS ASP THR PHE PHE HIS TRP VAL LYS GLN ARG PRO GLU SEQRES 6 H 249 GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP PRO ALA ASP SEQRES 7 H 249 GLY HIS THR LYS TYR ASP PRO LYS PHE GLN GLY LYS ALA SEQRES 8 H 249 THR ILE THR ALA ASP THR SER SER ASN THR ALA PHE LEU SEQRES 9 H 249 GLN LEU SER SER LEU THR SER VAL ASP THR ALA VAL TYR SEQRES 10 H 249 TYR CYS ALA THR THR ILE THR ALA VAL VAL PRO THR PRO SEQRES 11 H 249 TYR ASN ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL SEQRES 12 H 249 THR VAL SER SER ALA SER THR THR ALA PRO SER VAL TYR SEQRES 13 H 249 PRO LEU ALA PRO VAL CYS GLY GLY THR THR GLY SER SER SEQRES 14 H 249 VAL THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU SEQRES 15 H 249 PRO VAL THR LEU THR TRP ASN SER GLY SER LEU SER SER SEQRES 16 H 249 GLY VAL HIS THR PHE PRO ALA LEU LEU GLN SER GLY LEU SEQRES 17 H 249 TYR THR LEU SER SER SER VAL THR VAL THR SER ASN THR SEQRES 18 H 249 TRP PRO SER GLN THR ILE THR CYS ASN VAL ALA HIS PRO SEQRES 19 H 249 ALA SER SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG SEQRES 20 H 249 VAL PRO HET BU3 H 301 6 HETNAM BU3 (R,R)-2,3-BUTANEDIOL FORMUL 3 BU3 C4 H10 O2 FORMUL 4 HOH *608(H2 O) HELIX 1 AA1 GLU L 79 ALA L 83 5 5 HELIX 2 AA2 SER L 121 SER L 127 1 7 HELIX 3 AA3 LYS L 183 GLU L 187 1 5 HELIX 4 AA4 ASN H 28 THR H 32 5 5 HELIX 5 AA5 PRO H 61 GLN H 64 5 4 HELIX 6 AA6 THR H 83 THR H 87 5 5 HELIX 7 AA7 SER H 156 SER H 158 5 3 HELIX 8 AA8 PRO H 200 SER H 203 5 4 SHEET 1 AA1 4 LEU L 4 SER L 7 0 SHEET 2 AA1 4 THR L 19 ALA L 25 -1 O SER L 22 N SER L 7 SHEET 3 AA1 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AA1 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AA2 6 SER L 10 SER L 14 0 SHEET 2 AA2 6 THR L 102 LYS L 107 1 O GLU L 105 N LEU L 11 SHEET 3 AA2 6 ALA L 84 GLN L 90 -1 N ALA L 84 O LEU L 104 SHEET 4 AA2 6 ILE L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AA2 6 LYS L 45 PHE L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA2 6 SER L 53 LEU L 54 -1 O SER L 53 N PHE L 49 SHEET 1 AA3 4 SER L 10 SER L 14 0 SHEET 2 AA3 4 THR L 102 LYS L 107 1 O GLU L 105 N LEU L 11 SHEET 3 AA3 4 ALA L 84 GLN L 90 -1 N ALA L 84 O LEU L 104 SHEET 4 AA3 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AA4 4 THR L 114 PHE L 118 0 SHEET 2 AA4 4 GLY L 129 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 AA4 4 TYR L 173 THR L 182 -1 O LEU L 179 N VAL L 132 SHEET 4 AA4 4 VAL L 159 TRP L 163 -1 N LEU L 160 O THR L 178 SHEET 1 AA5 4 SER L 153 ARG L 155 0 SHEET 2 AA5 4 ASN L 145 ILE L 150 -1 N TRP L 148 O ARG L 155 SHEET 3 AA5 4 SER L 191 HIS L 198 -1 O THR L 197 N ASN L 145 SHEET 4 AA5 4 SER L 201 ASN L 210 -1 O ILE L 205 N ALA L 196 SHEET 1 AA6 4 GLN H 3 GLN H 6 0 SHEET 2 AA6 4 VAL H 18 SER H 25 -1 O THR H 23 N GLN H 5 SHEET 3 AA6 4 THR H 77 LEU H 82 -1 O LEU H 80 N LEU H 20 SHEET 4 AA6 4 ALA H 67 ASP H 72 -1 N THR H 70 O PHE H 79 SHEET 1 AA7 6 GLU H 10 VAL H 12 0 SHEET 2 AA7 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA7 6 ALA H 88 THR H 95 -1 N ALA H 88 O VAL H 109 SHEET 4 AA7 6 PHE H 34 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AA7 6 LEU H 45 ILE H 51 -1 O GLU H 46 N LYS H 38 SHEET 6 AA7 6 THR H 57 TYR H 59 -1 O LYS H 58 N ARG H 50 SHEET 1 AA8 4 GLU H 10 VAL H 12 0 SHEET 2 AA8 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA8 4 ALA H 88 THR H 95 -1 N ALA H 88 O VAL H 109 SHEET 4 AA8 4 MET H 100G TRP H 103 -1 O TYR H 102 N THR H 94 SHEET 1 AA9 4 SER H 120 LEU H 124 0 SHEET 2 AA9 4 SER H 135 TYR H 145 -1 O LYS H 143 N SER H 120 SHEET 3 AA9 4 LEU H 174 THR H 184 -1 O LEU H 177 N VAL H 142 SHEET 4 AA9 4 VAL H 163 GLN H 171 -1 N GLN H 171 O LEU H 174 SHEET 1 AB1 3 THR H 151 TRP H 154 0 SHEET 2 AB1 3 THR H 194 HIS H 199 -1 O ASN H 196 N THR H 153 SHEET 3 AB1 3 THR H 204 LYS H 209 -1 O LYS H 208 N CYS H 195 SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.05 SSBOND 2 CYS L 134 CYS L 194 1555 1555 2.01 SSBOND 3 CYS H 22 CYS H 92 1555 1555 2.05 SSBOND 4 CYS H 140 CYS H 195 1555 1555 2.04 CISPEP 1 SER L 7 PRO L 8 0 -3.47 CISPEP 2 SER L 7 PRO L 8 0 -5.14 CISPEP 3 ASP L 76 PRO L 77 0 -3.76 CISPEP 4 ASP L 94 PRO L 95 0 0.08 CISPEP 5 TYR L 140 PRO L 141 0 0.96 CISPEP 6 PHE H 146 PRO H 147 0 -6.27 CISPEP 7 GLU H 148 PRO H 149 0 1.04 CISPEP 8 TRP H 188 PRO H 189 0 8.95 SITE 1 AC1 5 LYS H 19 THR H 70 ALA H 71 PHE H 79 SITE 2 AC1 5 HOH H 520 CRYST1 116.960 63.010 56.540 90.00 98.60 90.00 C 1 2 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 0.008550 0.000000 0.001293 0.00000 SCALE2 0.000000 0.015870 0.000000 0.00000 SCALE3 0.000000 0.000000 0.017888 0.00000