HEADER IMMUNE SYSTEM 14-MAY-24 9BT5 TITLE THE CRYSTAL STRUCTURE OF THE HA1 DOMAIN OF HEMAGGLUTININ FROM TITLE 2 A/SHANGHAI/02/2013 (H7N9) BOUND TO H7-235 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMAGGLUTININ; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: HA1 DOMAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: MONOCLONAL ANTIBODY H7-235 HEAVY CHAIN; COMPND 8 CHAIN: C, E; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: MONOCLONAL ANTIBODY H7-235 LIGHT CHAIN; COMPND 12 CHAIN: D, F; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS (A/SHANGHAI/02/2013(H7N9)); SOURCE 3 ORGANISM_TAXID: 1332244; SOURCE 4 GENE: HA; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_COMMON: HUMAN; SOURCE 17 ORGANISM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS ANTIBODY, INFLUENZA, HEMAGGLUTININ, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR C.D.BUCHMAN,J.DONG,J.E.CROWE REVDAT 1 25-JUN-25 9BT5 0 JRNL AUTH I.M.GILCHUK,J.DONG,R.P.IRVING,C.D.BUCHMAN,E.ARMSTRONG, JRNL AUTH 2 H.L.TURNER,S.LI,A.B.WARD,R.H.CARNAHAN,J.E.CROWE JR. JRNL TITL PAN-H7 INFLUENZA HUMAN ANTIBODY VIRUS NEUTRALIZATION DEPENDS JRNL TITL 2 ON AVIDITY AND STERIC HINDRANCE. JRNL REF JCI INSIGHT 2025 JRNL REFN ISSN 2379-3708 JRNL PMID 40471690 JRNL DOI 10.1172/JCI.INSIGHT.186182 REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 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) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.37 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 3 NUMBER OF REFLECTIONS : 76698 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.198 REMARK 3 R VALUE (WORKING SET) : 0.195 REMARK 3 FREE R VALUE : 0.251 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.160 REMARK 3 FREE R VALUE TEST SET COUNT : 3959 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 49.3700 - 7.5800 1.00 2705 147 0.1783 0.2127 REMARK 3 2 7.5800 - 6.0200 1.00 2642 160 0.1715 0.2267 REMARK 3 3 6.0200 - 5.2600 1.00 2630 139 0.1496 0.1752 REMARK 3 4 5.2600 - 4.7800 1.00 2603 171 0.1361 0.1767 REMARK 3 5 4.7800 - 4.4400 1.00 2620 134 0.1312 0.1832 REMARK 3 6 4.4400 - 4.1800 1.00 2612 147 0.1358 0.1961 REMARK 3 7 4.1800 - 3.9700 1.00 2618 127 0.1544 0.2250 REMARK 3 8 3.9700 - 3.8000 1.00 2605 132 0.1624 0.2216 REMARK 3 9 3.8000 - 3.6500 1.00 2653 117 0.1779 0.2111 REMARK 3 10 3.6500 - 3.5200 1.00 2600 134 0.1903 0.2376 REMARK 3 11 3.5200 - 3.4100 0.99 2632 135 0.2019 0.2588 REMARK 3 12 3.4100 - 3.3200 1.00 2586 146 0.2020 0.2635 REMARK 3 13 3.3200 - 3.2300 1.00 2592 138 0.2121 0.2660 REMARK 3 14 3.2300 - 3.1500 1.00 2597 147 0.2213 0.2920 REMARK 3 15 3.1500 - 3.0800 1.00 2595 137 0.2355 0.3356 REMARK 3 16 3.0800 - 3.0100 0.99 2572 143 0.2534 0.3116 REMARK 3 17 3.0100 - 2.9500 0.99 2636 129 0.2538 0.3844 REMARK 3 18 2.9500 - 2.9000 0.99 2544 151 0.2761 0.3338 REMARK 3 19 2.9000 - 2.8400 0.99 2596 151 0.2697 0.3376 REMARK 3 20 2.8400 - 2.8000 0.99 2547 145 0.2641 0.3070 REMARK 3 21 2.8000 - 2.7500 0.99 2569 127 0.2691 0.3174 REMARK 3 22 2.7500 - 2.7100 0.99 2611 136 0.2725 0.3756 REMARK 3 23 2.7100 - 2.6700 0.99 2574 139 0.2817 0.3159 REMARK 3 24 2.6700 - 2.6300 0.99 2567 142 0.2971 0.3573 REMARK 3 25 2.6300 - 2.6000 0.99 2568 144 0.2954 0.3656 REMARK 3 26 2.6000 - 2.5600 0.99 2606 136 0.3181 0.3827 REMARK 3 27 2.5600 - 2.5300 0.99 2527 155 0.3558 0.4285 REMARK 3 28 2.5300 - 2.5000 0.99 2532 150 0.3847 0.4740 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) : 0.375 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.331 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 46.63 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.58 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 : 0.010 10152 REMARK 3 ANGLE : 1.113 13817 REMARK 3 CHIRALITY : 0.059 1537 REMARK 3 PLANARITY : 0.009 1795 REMARK 3 DIHEDRAL : 6.623 1421 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 24 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 46 THROUGH 66 ) REMARK 3 ORIGIN FOR THE GROUP (A): 5.1892 29.8614 34.4509 REMARK 3 T TENSOR REMARK 3 T11: 0.5411 T22: 0.8347 REMARK 3 T33: 0.3399 T12: 0.1004 REMARK 3 T13: -0.0295 T23: 0.1253 REMARK 3 L TENSOR REMARK 3 L11: 0.8139 L22: 0.0176 REMARK 3 L33: -0.0049 L12: -0.1078 REMARK 3 L13: 0.0164 L23: 0.0001 REMARK 3 S TENSOR REMARK 3 S11: -0.1177 S12: -0.6869 S13: 0.1507 REMARK 3 S21: 0.0127 S22: 0.0860 S23: -0.0122 REMARK 3 S31: 0.3771 S32: 0.5895 S33: -0.0098 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 67 THROUGH 94 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.4149 31.5407 34.6878 REMARK 3 T TENSOR REMARK 3 T11: 0.4229 T22: 0.6810 REMARK 3 T33: 0.3087 T12: 0.0402 REMARK 3 T13: 0.0126 T23: 0.1035 REMARK 3 L TENSOR REMARK 3 L11: 0.0729 L22: 0.1260 REMARK 3 L33: 0.6421 L12: -0.0947 REMARK 3 L13: -0.2716 L23: 0.2469 REMARK 3 S TENSOR REMARK 3 S11: -0.0190 S12: -0.3989 S13: -0.0881 REMARK 3 S21: 0.0341 S22: -0.0695 S23: 0.1067 REMARK 3 S31: 0.0376 S32: 0.2020 S33: -0.0002 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 95 THROUGH 112 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.5012 26.9157 29.4489 REMARK 3 T TENSOR REMARK 3 T11: 0.6748 T22: 0.6684 REMARK 3 T33: 0.5221 T12: -0.0011 REMARK 3 T13: 0.0547 T23: 0.1010 REMARK 3 L TENSOR REMARK 3 L11: 0.1893 L22: 0.2218 REMARK 3 L33: 0.0331 L12: 0.0915 REMARK 3 L13: 0.0745 L23: 0.0055 REMARK 3 S TENSOR REMARK 3 S11: 0.0562 S12: -0.3903 S13: -0.2712 REMARK 3 S21: 0.0628 S22: 0.1732 S23: -0.0440 REMARK 3 S31: 0.2984 S32: 0.0593 S33: 0.0001 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 113 THROUGH 132 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.4716 45.4015 21.2767 REMARK 3 T TENSOR REMARK 3 T11: 0.3194 T22: 0.5109 REMARK 3 T33: 0.3397 T12: -0.0455 REMARK 3 T13: -0.0017 T23: -0.0223 REMARK 3 L TENSOR REMARK 3 L11: 0.2976 L22: -0.0049 REMARK 3 L33: 0.0402 L12: 0.0188 REMARK 3 L13: -0.0871 L23: -0.0330 REMARK 3 S TENSOR REMARK 3 S11: 0.1064 S12: -0.4432 S13: 0.0015 REMARK 3 S21: -0.0763 S22: -0.1870 S23: 0.0883 REMARK 3 S31: -0.0774 S32: -0.0564 S33: 0.0001 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 133 THROUGH 142 ) REMARK 3 ORIGIN FOR THE GROUP (A): 6.4914 42.8090 25.5231 REMARK 3 T TENSOR REMARK 3 T11: 0.4340 T22: 0.7495 REMARK 3 T33: 0.3503 T12: -0.0322 REMARK 3 T13: -0.0490 T23: 0.0016 REMARK 3 L TENSOR REMARK 3 L11: 0.0734 L22: 0.0184 REMARK 3 L33: 0.0360 L12: -0.0370 REMARK 3 L13: 0.0007 L23: 0.0059 REMARK 3 S TENSOR REMARK 3 S11: -0.1379 S12: -0.7133 S13: -0.1734 REMARK 3 S21: -0.0263 S22: 0.1473 S23: -0.1886 REMARK 3 S31: -0.0180 S32: 0.7397 S33: 0.0010 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 143 THROUGH 186 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.2646 46.8282 19.4606 REMARK 3 T TENSOR REMARK 3 T11: 0.3785 T22: 0.3142 REMARK 3 T33: 0.3541 T12: 0.0214 REMARK 3 T13: 0.0235 T23: -0.0291 REMARK 3 L TENSOR REMARK 3 L11: 0.3332 L22: 0.3437 REMARK 3 L33: 0.4377 L12: 0.1914 REMARK 3 L13: -0.3774 L23: -0.2882 REMARK 3 S TENSOR REMARK 3 S11: 0.0085 S12: -0.2148 S13: 0.0653 REMARK 3 S21: 0.1420 S22: 0.0434 S23: 0.1472 REMARK 3 S31: -0.0688 S32: 0.0648 S33: -0.0001 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 187 THROUGH 204 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.8302 45.4084 19.2221 REMARK 3 T TENSOR REMARK 3 T11: 0.3867 T22: 0.3967 REMARK 3 T33: 0.4644 T12: 0.0543 REMARK 3 T13: -0.0003 T23: -0.0333 REMARK 3 L TENSOR REMARK 3 L11: 0.4587 L22: 0.1215 REMARK 3 L33: 0.1493 L12: -0.2345 REMARK 3 L13: -0.1543 L23: 0.1145 REMARK 3 S TENSOR REMARK 3 S11: 0.2334 S12: -0.2613 S13: -0.1179 REMARK 3 S21: -0.2673 S22: -0.2559 S23: -0.3451 REMARK 3 S31: -0.0856 S32: -0.2792 S33: 0.0005 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 205 THROUGH 228 ) REMARK 3 ORIGIN FOR THE GROUP (A): -4.6252 46.3361 31.5757 REMARK 3 T TENSOR REMARK 3 T11: 0.5070 T22: 0.5587 REMARK 3 T33: 0.3908 T12: -0.0495 REMARK 3 T13: 0.0002 T23: -0.0499 REMARK 3 L TENSOR REMARK 3 L11: 0.0972 L22: 0.0191 REMARK 3 L33: 0.1424 L12: 0.0669 REMARK 3 L13: -0.1195 L23: 0.0110 REMARK 3 S TENSOR REMARK 3 S11: 0.0742 S12: -0.4150 S13: 0.0441 REMARK 3 S21: 0.5546 S22: -0.2957 S23: 0.1668 REMARK 3 S31: 0.3279 S32: -0.0576 S33: 0.0000 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 229 THROUGH 246 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.1652 39.4963 16.2814 REMARK 3 T TENSOR REMARK 3 T11: 0.4104 T22: 0.5087 REMARK 3 T33: 0.4162 T12: 0.0711 REMARK 3 T13: -0.0074 T23: -0.0919 REMARK 3 L TENSOR REMARK 3 L11: 0.2208 L22: 0.0569 REMARK 3 L33: 0.2417 L12: 0.0225 REMARK 3 L13: -0.0973 L23: 0.1198 REMARK 3 S TENSOR REMARK 3 S11: -0.1016 S12: 0.1040 S13: -0.1639 REMARK 3 S21: 0.1337 S22: 0.0493 S23: -0.2795 REMARK 3 S31: 0.0732 S32: -0.3852 S33: 0.0001 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 247 THROUGH 262 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.2482 23.6315 30.7156 REMARK 3 T TENSOR REMARK 3 T11: 0.7113 T22: 0.7545 REMARK 3 T33: 0.5346 T12: 0.0581 REMARK 3 T13: 0.0252 T23: 0.0380 REMARK 3 L TENSOR REMARK 3 L11: 0.0097 L22: 0.1457 REMARK 3 L33: 0.0402 L12: -0.0320 REMARK 3 L13: -0.0306 L23: 0.0453 REMARK 3 S TENSOR REMARK 3 S11: -0.3431 S12: -0.8199 S13: -0.0963 REMARK 3 S21: 0.5443 S22: 0.1303 S23: -0.1165 REMARK 3 S31: -0.0217 S32: -0.1459 S33: 0.0002 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 123 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.0825 36.0294 15.1226 REMARK 3 T TENSOR REMARK 3 T11: 0.3235 T22: 0.4975 REMARK 3 T33: 0.3823 T12: 0.0696 REMARK 3 T13: -0.0302 T23: 0.0509 REMARK 3 L TENSOR REMARK 3 L11: 1.2333 L22: 1.0138 REMARK 3 L33: 0.3142 L12: 0.2343 REMARK 3 L13: -0.0205 L23: 0.2234 REMARK 3 S TENSOR REMARK 3 S11: -0.1177 S12: -0.3937 S13: -0.1114 REMARK 3 S21: 0.0045 S22: 0.1099 S23: -0.0918 REMARK 3 S31: 0.0812 S32: 0.1259 S33: 0.0000 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 124 THROUGH 223 ) REMARK 3 ORIGIN FOR THE GROUP (A): 50.0973 63.6398 12.3896 REMARK 3 T TENSOR REMARK 3 T11: 0.5305 T22: 0.5369 REMARK 3 T33: 0.4516 T12: -0.2504 REMARK 3 T13: -0.0583 T23: 0.1353 REMARK 3 L TENSOR REMARK 3 L11: 0.9431 L22: 0.6755 REMARK 3 L33: 0.5285 L12: -0.0212 REMARK 3 L13: 0.6280 L23: -0.1238 REMARK 3 S TENSOR REMARK 3 S11: -0.3827 S12: 0.5737 S13: 0.1043 REMARK 3 S21: 0.0774 S22: 0.2252 S23: 0.1319 REMARK 3 S31: -0.2499 S32: 0.8333 S33: 0.0095 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 118 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.3315 49.7112 0.3343 REMARK 3 T TENSOR REMARK 3 T11: 0.3076 T22: 0.4150 REMARK 3 T33: 0.3272 T12: -0.0152 REMARK 3 T13: -0.0216 T23: 0.0274 REMARK 3 L TENSOR REMARK 3 L11: 1.1186 L22: 0.6968 REMARK 3 L33: 1.4013 L12: -0.2577 REMARK 3 L13: -0.1422 L23: -0.9195 REMARK 3 S TENSOR REMARK 3 S11: -0.0359 S12: 0.2910 S13: -0.0243 REMARK 3 S21: -0.0996 S22: -0.0046 S23: -0.0321 REMARK 3 S31: -0.0813 S32: -0.0288 S33: 0.0000 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 119 THROUGH 216 ) REMARK 3 ORIGIN FOR THE GROUP (A): 50.1695 64.7433 -4.0674 REMARK 3 T TENSOR REMARK 3 T11: 0.6756 T22: 1.3834 REMARK 3 T33: 0.7202 T12: -0.3176 REMARK 3 T13: 0.0081 T23: 0.2507 REMARK 3 L TENSOR REMARK 3 L11: 0.3921 L22: 1.1129 REMARK 3 L33: 0.8658 L12: -0.2136 REMARK 3 L13: -0.0284 L23: -0.0892 REMARK 3 S TENSOR REMARK 3 S11: -0.4327 S12: 1.2921 S13: 0.2357 REMARK 3 S21: -0.1309 S22: 0.0285 S23: -0.1680 REMARK 3 S31: -0.3267 S32: 0.9382 S33: -0.0045 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 46 THROUGH 69 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.9737 52.4642 52.6240 REMARK 3 T TENSOR REMARK 3 T11: 0.4606 T22: 0.6523 REMARK 3 T33: 0.4447 T12: -0.0648 REMARK 3 T13: -0.0328 T23: 0.0567 REMARK 3 L TENSOR REMARK 3 L11: 0.0782 L22: 0.0256 REMARK 3 L33: 0.1147 L12: -0.0676 REMARK 3 L13: 0.1087 L23: -0.0694 REMARK 3 S TENSOR REMARK 3 S11: -0.2203 S12: 0.3815 S13: -0.0620 REMARK 3 S21: -0.0795 S22: 0.3228 S23: 0.0162 REMARK 3 S31: -0.0281 S32: 0.1974 S33: -0.0003 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 70 THROUGH 142 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.0497 45.9103 57.8685 REMARK 3 T TENSOR REMARK 3 T11: 0.4196 T22: 0.5918 REMARK 3 T33: 0.3789 T12: -0.0600 REMARK 3 T13: -0.0040 T23: -0.0383 REMARK 3 L TENSOR REMARK 3 L11: 0.5318 L22: 0.5323 REMARK 3 L33: 0.4381 L12: 0.1777 REMARK 3 L13: -0.3423 L23: -0.5939 REMARK 3 S TENSOR REMARK 3 S11: -0.1445 S12: 0.4405 S13: 0.0031 REMARK 3 S21: 0.0030 S22: 0.0905 S23: 0.0604 REMARK 3 S31: 0.1423 S32: -0.4478 S33: 0.0000 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 143 THROUGH 246 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.7438 35.6062 66.9753 REMARK 3 T TENSOR REMARK 3 T11: 0.3881 T22: 0.3161 REMARK 3 T33: 0.3309 T12: -0.0576 REMARK 3 T13: 0.0042 T23: -0.0682 REMARK 3 L TENSOR REMARK 3 L11: 1.3446 L22: 0.6597 REMARK 3 L33: 0.8652 L12: -0.2342 REMARK 3 L13: -0.8605 L23: -0.3810 REMARK 3 S TENSOR REMARK 3 S11: -0.1023 S12: 0.0295 S13: -0.1504 REMARK 3 S21: 0.1119 S22: -0.0130 S23: -0.0415 REMARK 3 S31: 0.2321 S32: -0.4135 S33: -0.0001 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 247 THROUGH 262 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.6725 57.1549 59.3394 REMARK 3 T TENSOR REMARK 3 T11: 0.5453 T22: 0.5607 REMARK 3 T33: 0.4332 T12: 0.0560 REMARK 3 T13: -0.0750 T23: 0.0476 REMARK 3 L TENSOR REMARK 3 L11: 0.0565 L22: 0.0820 REMARK 3 L33: 0.1495 L12: -0.0389 REMARK 3 L13: 0.0869 L23: 0.0521 REMARK 3 S TENSOR REMARK 3 S11: -0.0704 S12: 0.0365 S13: 0.0665 REMARK 3 S21: -0.2295 S22: 0.2088 S23: -0.0801 REMARK 3 S31: -0.0536 S32: -0.4960 S33: -0.0005 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 1 THROUGH 33 ) REMARK 3 ORIGIN FOR THE GROUP (A): 36.6075 50.3372 41.8981 REMARK 3 T TENSOR REMARK 3 T11: 0.3784 T22: 0.3642 REMARK 3 T33: 0.3647 T12: -0.0693 REMARK 3 T13: 0.0027 T23: 0.0258 REMARK 3 L TENSOR REMARK 3 L11: 0.1911 L22: 0.4270 REMARK 3 L33: 0.4822 L12: -0.0835 REMARK 3 L13: -0.2689 L23: 0.4443 REMARK 3 S TENSOR REMARK 3 S11: -0.0178 S12: 0.4094 S13: 0.0651 REMARK 3 S21: -0.0377 S22: 0.0049 S23: 0.1199 REMARK 3 S31: -0.1826 S32: -0.6144 S33: 0.0002 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 34 THROUGH 111 ) REMARK 3 ORIGIN FOR THE GROUP (A): 40.5122 54.9237 49.8620 REMARK 3 T TENSOR REMARK 3 T11: 0.3564 T22: 0.2444 REMARK 3 T33: 0.3896 T12: -0.0122 REMARK 3 T13: 0.0045 T23: -0.0012 REMARK 3 L TENSOR REMARK 3 L11: 0.2342 L22: 0.7183 REMARK 3 L33: 1.3300 L12: 0.3013 REMARK 3 L13: -0.5637 L23: -0.1942 REMARK 3 S TENSOR REMARK 3 S11: -0.0794 S12: -0.1685 S13: 0.0216 REMARK 3 S21: -0.0821 S22: 0.0875 S23: -0.0180 REMARK 3 S31: 0.0211 S32: -0.1174 S33: 0.0000 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 112 THROUGH 157 ) REMARK 3 ORIGIN FOR THE GROUP (A): 61.1132 37.8711 32.6937 REMARK 3 T TENSOR REMARK 3 T11: 0.3941 T22: 0.5155 REMARK 3 T33: 0.3587 T12: -0.0049 REMARK 3 T13: -0.0408 T23: -0.0428 REMARK 3 L TENSOR REMARK 3 L11: 0.6933 L22: 0.2575 REMARK 3 L33: 0.8327 L12: -0.2082 REMARK 3 L13: 0.2423 L23: -0.6627 REMARK 3 S TENSOR REMARK 3 S11: 0.2051 S12: 0.4889 S13: -0.0343 REMARK 3 S21: 0.0621 S22: -0.3012 S23: 0.0116 REMARK 3 S31: 0.0724 S32: 0.3546 S33: 0.0000 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 158 THROUGH 223 ) REMARK 3 ORIGIN FOR THE GROUP (A): 61.6603 32.0430 27.7909 REMARK 3 T TENSOR REMARK 3 T11: 0.3825 T22: 0.4602 REMARK 3 T33: 0.4940 T12: 0.1052 REMARK 3 T13: -0.0665 T23: -0.1184 REMARK 3 L TENSOR REMARK 3 L11: 0.3966 L22: 0.7452 REMARK 3 L33: 0.5096 L12: -0.5973 REMARK 3 L13: 0.2472 L23: -0.6394 REMARK 3 S TENSOR REMARK 3 S11: 0.2603 S12: 0.3864 S13: -0.1066 REMARK 3 S21: 0.0336 S22: -0.0312 S23: 0.2769 REMARK 3 S31: 0.0722 S32: 0.4352 S33: 0.0005 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 1 THROUGH 66 ) REMARK 3 ORIGIN FOR THE GROUP (A): 47.4188 40.4608 62.6695 REMARK 3 T TENSOR REMARK 3 T11: 0.3665 T22: 0.2723 REMARK 3 T33: 0.3980 T12: 0.0168 REMARK 3 T13: 0.0348 T23: 0.0009 REMARK 3 L TENSOR REMARK 3 L11: 1.3355 L22: 1.0281 REMARK 3 L33: 0.7139 L12: -0.1138 REMARK 3 L13: 0.4305 L23: -0.2556 REMARK 3 S TENSOR REMARK 3 S11: -0.0746 S12: -0.1488 S13: 0.0184 REMARK 3 S21: 0.0402 S22: 0.0261 S23: -0.1180 REMARK 3 S31: 0.0560 S32: 0.1726 S33: -0.0001 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 67 THROUGH 216 ) REMARK 3 ORIGIN FOR THE GROUP (A): 67.5181 36.2159 45.5098 REMARK 3 T TENSOR REMARK 3 T11: 0.2683 T22: 0.3415 REMARK 3 T33: 0.3850 T12: -0.0379 REMARK 3 T13: -0.0060 T23: 0.0307 REMARK 3 L TENSOR REMARK 3 L11: 1.3313 L22: 0.4644 REMARK 3 L33: 1.0535 L12: -0.7523 REMARK 3 L13: 0.4202 L23: -0.0234 REMARK 3 S TENSOR REMARK 3 S11: -0.0369 S12: 0.2507 S13: 0.0393 REMARK 3 S21: 0.1073 S22: -0.1364 S23: -0.0380 REMARK 3 S31: -0.0139 S32: 0.6896 S33: 0.0013 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 9BT5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAY-24. REMARK 100 THE DEPOSITION ID IS D_1000282804. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 29-OCT-18 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 : APS REMARK 200 BEAMLINE : 21-ID-F REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872 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 : NULL REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76766 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 49.370 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : 3.900 REMARK 200 R MERGE (I) : 0.09600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2 REMARK 200 DATA REDUNDANCY IN SHELL : 3.90 REMARK 200 R MERGE FOR SHELL (I) : 0.86200 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.700 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 68.46 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.90 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M SODIUM CHLORIDE, 8-10% PEG 6000, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 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 120.30150 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.52650 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 120.30150 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 47.52650 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E, F 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 B1122 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 SER C 140 REMARK 465 LYS C 141 REMARK 465 SER C 142 REMARK 465 THR C 143 REMARK 465 SER C 144 REMARK 465 GLY C 145 REMARK 465 GLU C 224 REMARK 465 PRO C 225 REMARK 465 LYS C 226 REMARK 465 SER C 227 REMARK 465 CYS C 228 REMARK 465 GLY D 217 REMARK 465 GLU D 218 REMARK 465 CYS D 219 REMARK 465 GLU E 224 REMARK 465 PRO E 225 REMARK 465 LYS E 226 REMARK 465 SER E 227 REMARK 465 CYS E 228 REMARK 465 GLY F 217 REMARK 465 GLU F 218 REMARK 465 CYS F 219 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 LYS A 46 CG CD CE NZ REMARK 470 ARG A 47 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 81 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 164 CG CD CE NZ REMARK 470 LYS A 254 CG CD CE NZ REMARK 470 MET A 256 CG SD CE REMARK 470 GLN A 259 CG CD OE1 NE2 REMARK 470 VAL A 262 CG1 CG2 REMARK 470 ILE C 207 CG1 CG2 CD1 REMARK 470 LYS C 222 CG CD CE NZ REMARK 470 VAL D 115 CG1 CG2 REMARK 470 SER D 126 OG REMARK 470 ASP D 127 CG OD1 OD2 REMARK 470 LEU D 130 CG CD1 CD2 REMARK 470 LYS D 131 CG CD CE NZ REMARK 470 GLU D 148 CG CD OE1 OE2 REMARK 470 LYS D 150 CG CD CE NZ REMARK 470 LYS D 154 CG CD CE NZ REMARK 470 LEU D 159 CG CD1 CD2 REMARK 470 LYS D 174 CG CD CE NZ REMARK 470 LEU D 186 CG CD1 CD2 REMARK 470 LYS D 188 CG CD CE NZ REMARK 470 LYS D 193 CG CD CE NZ REMARK 470 LYS D 195 CG CD CE NZ REMARK 470 THR D 202 OG1 CG2 REMARK 470 GLN D 204 CG CD OE1 NE2 REMARK 470 SER D 213 OG REMARK 470 ASN D 215 CG OD1 ND2 REMARK 470 ARG D 216 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 46 CG CD CE NZ REMARK 470 ARG B 81 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 164 CG CD CE NZ REMARK 470 LYS B 254 CG CD CE NZ REMARK 470 SER E 142 OG REMARK 470 ILE E 207 CG1 CG2 CD1 REMARK 470 LYS E 222 CG CD CE NZ REMARK 470 ARG F 82 CG CD NE CZ NH1 NH2 REMARK 470 VAL F 115 CG1 CG2 REMARK 470 SER F 126 OG REMARK 470 ASP F 127 CG OD1 OD2 REMARK 470 GLU F 148 CG CD OE1 OE2 REMARK 470 LYS F 150 CG CD CE NZ REMARK 470 LYS F 174 CG CD CE NZ REMARK 470 LYS F 188 CG CD CE NZ REMARK 470 LYS F 195 CG CD CE NZ REMARK 470 SER F 213 OG REMARK 470 ASN F 215 CG OD1 ND2 REMARK 470 ARG F 216 CG CD NE CZ NH1 NH2 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 NH1 ARG A 211 OE1 GLU B 96 2556 2.01 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 CYS C 96 CB CYS C 96 SG -0.100 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 CYS A 87 -54.16 -135.00 REMARK 500 SER A 135 -152.55 -142.62 REMARK 500 PHE A 136 -145.90 -157.39 REMARK 500 ASN A 149 -5.38 80.11 REMARK 500 GLN A 213 111.08 -39.55 REMARK 500 ALA C 28 76.99 -66.92 REMARK 500 ASP C 90 -3.67 -57.42 REMARK 500 ASN C 99 98.68 -65.39 REMARK 500 ASN C 167 71.80 43.17 REMARK 500 SER C 168 -102.65 42.19 REMARK 500 LEU C 171 96.93 -67.19 REMARK 500 LEU C 201 89.36 -62.23 REMARK 500 THR C 203 -71.05 -100.73 REMARK 500 SER D 132 -117.26 -72.67 REMARK 500 ASN D 143 72.90 54.40 REMARK 500 PRO D 146 -165.81 -69.87 REMARK 500 ALA D 189 -70.23 -46.18 REMARK 500 LYS D 193 19.12 -58.43 REMARK 500 LYS D 195 -74.16 -126.00 REMARK 500 CYS B 87 -59.46 -134.03 REMARK 500 SER B 135 -155.40 -152.28 REMARK 500 PHE B 136 -156.64 -161.82 REMARK 500 SER B 188 -177.22 -69.36 REMARK 500 ASN B 231 -8.16 82.33 REMARK 500 SER E 124 145.78 -178.44 REMARK 500 ASP E 156 57.50 71.40 REMARK 500 SER E 168 -158.21 42.28 REMARK 500 THR E 172 -50.45 -120.15 REMARK 500 HIS E 212 75.61 -119.16 REMARK 500 ASN F 143 72.09 43.72 REMARK 500 ASP F 156 25.18 47.14 REMARK 500 ASN F 157 14.03 81.14 REMARK 500 REMARK 500 REMARK: NULL DBREF 9BT5 A 46 262 UNP R4NN21 R4NN21_9INFA 64 280 DBREF 9BT5 C 1 228 PDB 9BT5 9BT5 1 228 DBREF 9BT5 D 1 219 PDB 9BT5 9BT5 1 219 DBREF 9BT5 B 46 262 UNP R4NN21 R4NN21_9INFA 64 280 DBREF 9BT5 E 1 228 PDB 9BT5 9BT5 1 228 DBREF 9BT5 F 1 219 PDB 9BT5 9BT5 1 219 SEQRES 1 A 217 LYS ARG THR VAL ASP LEU GLY GLN CYS GLY LEU LEU GLY SEQRES 2 A 217 THR ILE THR GLY PRO PRO GLN CYS ASP GLN PHE LEU GLU SEQRES 3 A 217 PHE SER ALA ASP LEU ILE ILE GLU ARG ARG GLU GLY SER SEQRES 4 A 217 ASP VAL CYS TYR PRO GLY LYS PHE VAL ASN GLU GLU ALA SEQRES 5 A 217 LEU ARG GLN ILE LEU ARG GLU SER GLY GLY ILE ASP LYS SEQRES 6 A 217 GLU ALA MET GLY PHE THR TYR SER GLY ILE ARG THR ASN SEQRES 7 A 217 GLY ALA THR SER ALA CYS ARG ARG SER GLY SER SER PHE SEQRES 8 A 217 TYR ALA GLU MET LYS TRP LEU LEU SER ASN THR ASP ASN SEQRES 9 A 217 ALA ALA PHE PRO GLN MET THR LYS SER TYR LYS ASN THR SEQRES 10 A 217 ARG LYS SER PRO ALA LEU ILE VAL TRP GLY ILE HIS HIS SEQRES 11 A 217 SER VAL SER THR ALA GLU GLN THR LYS LEU TYR GLY SER SEQRES 12 A 217 GLY ASN LYS LEU VAL THR VAL GLY SER SER ASN TYR GLN SEQRES 13 A 217 GLN SER PHE VAL PRO SER PRO GLY ALA ARG PRO GLN VAL SEQRES 14 A 217 ASN GLY LEU SER GLY ARG ILE ASP PHE HIS TRP LEU MET SEQRES 15 A 217 LEU ASN PRO ASN ASP THR VAL THR PHE SER PHE ASN GLY SEQRES 16 A 217 ALA PHE ILE ALA PRO ASP ARG ALA SER PHE LEU ARG GLY SEQRES 17 A 217 LYS SER MET GLY ILE GLN SER GLY VAL SEQRES 1 C 228 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 C 228 PRO GLY GLU SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 C 228 PHE ALA PHE ARG THR TYR GLY MET HIS TRP VAL ARG GLN SEQRES 4 C 228 ALA PRO GLY LYS GLY LEU GLU TRP VAL GLY VAL ILE TRP SEQRES 5 C 228 TYR ASP GLY SER ASN LYS TYR TYR GLY ASP SER VAL LYS SEQRES 6 C 228 GLY ARG PHE THR ILE SER ARG ASP ASN SER GLN ASN THR SEQRES 7 C 228 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 C 228 ALA VAL TYR TYR CYS ALA ARG ASN GLY GLU ARG TRP ARG SEQRES 9 C 228 VAL GLU ASP TYR TYR TYR GLY MET ASP VAL TRP GLY GLN SEQRES 10 C 228 GLY THR LEU VAL THR VAL SER SER ALA SER PHE LYS GLY SEQRES 11 C 228 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 C 228 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 C 228 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 C 228 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 C 228 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 C 228 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 C 228 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 C 228 LYS VAL GLU PRO LYS SER CYS SEQRES 1 D 219 GLU ILE VAL MET THR GLN SER PRO LEU SER LEU PRO VAL SEQRES 2 D 219 THR PRO GLY GLU PRO ALA SER ILE SER CYS ARG SER SER SEQRES 3 D 219 GLN SER LEU LEU HIS SER ASN ALA HIS ASN TYR LEU ASP SEQRES 4 D 219 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 D 219 ILE TYR LEU GLY SER ASN ARG ALA SER GLY VAL PRO ASP SEQRES 6 D 219 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 D 219 LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY ILE TYR SEQRES 8 D 219 TYR CYS MET GLN ALA LEU GLN THR PRO ILE THR PHE GLY SEQRES 9 D 219 GLN GLY THR ARG 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 SEQRES 1 B 217 LYS ARG THR VAL ASP LEU GLY GLN CYS GLY LEU LEU GLY SEQRES 2 B 217 THR ILE THR GLY PRO PRO GLN CYS ASP GLN PHE LEU GLU SEQRES 3 B 217 PHE SER ALA ASP LEU ILE ILE GLU ARG ARG GLU GLY SER SEQRES 4 B 217 ASP VAL CYS TYR PRO GLY LYS PHE VAL ASN GLU GLU ALA SEQRES 5 B 217 LEU ARG GLN ILE LEU ARG GLU SER GLY GLY ILE ASP LYS SEQRES 6 B 217 GLU ALA MET GLY PHE THR TYR SER GLY ILE ARG THR ASN SEQRES 7 B 217 GLY ALA THR SER ALA CYS ARG ARG SER GLY SER SER PHE SEQRES 8 B 217 TYR ALA GLU MET LYS TRP LEU LEU SER ASN THR ASP ASN SEQRES 9 B 217 ALA ALA PHE PRO GLN MET THR LYS SER TYR LYS ASN THR SEQRES 10 B 217 ARG LYS SER PRO ALA LEU ILE VAL TRP GLY ILE HIS HIS SEQRES 11 B 217 SER VAL SER THR ALA GLU GLN THR LYS LEU TYR GLY SER SEQRES 12 B 217 GLY ASN LYS LEU VAL THR VAL GLY SER SER ASN TYR GLN SEQRES 13 B 217 GLN SER PHE VAL PRO SER PRO GLY ALA ARG PRO GLN VAL SEQRES 14 B 217 ASN GLY LEU SER GLY ARG ILE ASP PHE HIS TRP LEU MET SEQRES 15 B 217 LEU ASN PRO ASN ASP THR VAL THR PHE SER PHE ASN GLY SEQRES 16 B 217 ALA PHE ILE ALA PRO ASP ARG ALA SER PHE LEU ARG GLY SEQRES 17 B 217 LYS SER MET GLY ILE GLN SER GLY VAL SEQRES 1 E 228 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 E 228 PRO GLY GLU SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 E 228 PHE ALA PHE ARG THR TYR GLY MET HIS TRP VAL ARG GLN SEQRES 4 E 228 ALA PRO GLY LYS GLY LEU GLU TRP VAL GLY VAL ILE TRP SEQRES 5 E 228 TYR ASP GLY SER ASN LYS TYR TYR GLY ASP SER VAL LYS SEQRES 6 E 228 GLY ARG PHE THR ILE SER ARG ASP ASN SER GLN ASN THR SEQRES 7 E 228 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 E 228 ALA VAL TYR TYR CYS ALA ARG ASN GLY GLU ARG TRP ARG SEQRES 9 E 228 VAL GLU ASP TYR TYR TYR GLY MET ASP VAL TRP GLY GLN SEQRES 10 E 228 GLY THR LEU VAL THR VAL SER SER ALA SER PHE LYS GLY SEQRES 11 E 228 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 E 228 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 E 228 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 E 228 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 E 228 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 E 228 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 E 228 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 E 228 LYS VAL GLU PRO LYS SER CYS SEQRES 1 F 219 GLU ILE VAL MET THR GLN SER PRO LEU SER LEU PRO VAL SEQRES 2 F 219 THR PRO GLY GLU PRO ALA SER ILE SER CYS ARG SER SER SEQRES 3 F 219 GLN SER LEU LEU HIS SER ASN ALA HIS ASN TYR LEU ASP SEQRES 4 F 219 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 F 219 ILE TYR LEU GLY SER ASN ARG ALA SER GLY VAL PRO ASP SEQRES 6 F 219 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 F 219 LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY ILE TYR SEQRES 8 F 219 TYR CYS MET GLN ALA LEU GLN THR PRO ILE THR PHE GLY SEQRES 9 F 219 GLN GLY THR ARG LEU GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 F 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 F 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 F 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 F 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 F 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 F 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 F 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 F 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS HET NAG A1001 14 HET SIA A1002 39 HET NAG B1001 14 HET SIA B1002 39 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM SIA N-ACETYL-ALPHA-NEURAMINIC ACID HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN SIA N-ACETYLNEURAMINIC ACID; SIALIC ACID; ALPHA-SIALIC HETSYN 2 SIA ACID; O-SIALIC ACID FORMUL 7 NAG 2(C8 H15 N O6) FORMUL 8 SIA 2(C11 H19 N O9) FORMUL 11 HOH *174(H2 O) HELIX 1 AA1 LEU A 57 GLY A 62 1 6 HELIX 2 AA2 PRO A 63 ASP A 67 5 5 HELIX 3 AA3 ASN A 94 GLU A 104 1 11 HELIX 4 AA4 SER A 178 GLY A 187 1 10 HELIX 5 AA5 ALA C 28 TYR C 32 5 5 HELIX 6 AA6 ASN C 74 GLN C 76 5 3 HELIX 7 AA7 ARG C 87 THR C 91 5 5 HELIX 8 AA8 ARG C 104 TYR C 108 5 5 HELIX 9 AA9 LYS C 213 ASN C 216 5 4 HELIX 10 AB1 GLU D 84 VAL D 88 5 5 HELIX 11 AB2 SER D 126 SER D 132 1 7 HELIX 12 AB3 LYS D 188 LYS D 193 1 6 HELIX 13 AB4 LEU B 57 GLY B 62 1 6 HELIX 14 AB5 PRO B 63 LEU B 70 5 8 HELIX 15 AB6 ASN B 94 GLU B 104 1 11 HELIX 16 AB7 SER B 178 GLY B 187 1 10 HELIX 17 AB8 ALA E 28 TYR E 32 5 5 HELIX 18 AB9 ASP E 62 LYS E 65 5 4 HELIX 19 AC1 ASN E 74 GLN E 76 5 3 HELIX 20 AC2 ARG E 87 THR E 91 5 5 HELIX 21 AC3 ARG E 104 TYR E 108 5 5 HELIX 22 AC4 SER E 199 LEU E 201 5 3 HELIX 23 AC5 LYS E 213 ASN E 216 5 4 HELIX 24 AC6 GLU F 84 VAL F 88 5 5 HELIX 25 AC7 SER F 126 SER F 132 1 7 HELIX 26 AC8 LYS F 188 HIS F 194 1 7 SHEET 1 AA1 3 THR A 48 ASP A 50 0 SHEET 2 AA1 3 LEU A 76 GLU A 79 1 O ILE A 78 N VAL A 49 SHEET 3 AA1 3 MET A 256 GLN A 259 1 O ILE A 258 N ILE A 77 SHEET 1 AA2 5 ILE A 108 ALA A 112 0 SHEET 2 AA2 5 ARG A 247 LEU A 251 -1 O ALA A 248 N GLU A 111 SHEET 3 AA2 5 ALA A 167 HIS A 175 -1 N LEU A 168 O SER A 249 SHEET 4 AA2 5 PHE A 242 PRO A 245 -1 O ILE A 243 N GLY A 172 SHEET 5 AA2 5 MET A 140 TRP A 142 -1 N LYS A 141 O ALA A 244 SHEET 1 AA3 4 ILE A 108 ALA A 112 0 SHEET 2 AA3 4 ARG A 247 LEU A 251 -1 O ALA A 248 N GLU A 111 SHEET 3 AA3 4 ALA A 167 HIS A 175 -1 N LEU A 168 O SER A 249 SHEET 4 AA3 4 ARG A 220 LEU A 228 -1 O LEU A 228 N ALA A 167 SHEET 1 AA4 2 ILE A 120 ARG A 121 0 SHEET 2 AA4 2 LEU A 144 SER A 145 -1 O LEU A 144 N ARG A 121 SHEET 1 AA5 2 THR A 126 ARG A 130 0 SHEET 2 AA5 2 SER A 134 SER A 135 -1 O SER A 135 N THR A 126 SHEET 1 AA6 4 MET A 155 LYS A 160 0 SHEET 2 AA6 4 THR A 233 PHE A 238 -1 O PHE A 236 N LYS A 157 SHEET 3 AA6 4 VAL A 193 GLY A 196 -1 N THR A 194 O SER A 237 SHEET 4 AA6 4 GLN A 201 PHE A 204 -1 O PHE A 204 N VAL A 193 SHEET 1 AA7 4 GLN C 3 SER C 7 0 SHEET 2 AA7 4 LEU C 18 SER C 25 -1 O ALA C 23 N VAL C 5 SHEET 3 AA7 4 THR C 78 MET C 83 -1 O MET C 83 N LEU C 18 SHEET 4 AA7 4 PHE C 68 ASP C 73 -1 N THR C 69 O GLN C 82 SHEET 1 AA8 6 GLY C 10 VAL C 12 0 SHEET 2 AA8 6 THR C 119 VAL C 123 1 O THR C 122 N GLY C 10 SHEET 3 AA8 6 ALA C 92 ASN C 99 -1 N TYR C 94 O THR C 119 SHEET 4 AA8 6 MET C 34 GLN C 39 -1 N VAL C 37 O TYR C 95 SHEET 5 AA8 6 LEU C 45 ILE C 51 -1 O GLU C 46 N ARG C 38 SHEET 6 AA8 6 LYS C 58 TYR C 60 -1 O TYR C 59 N VAL C 50 SHEET 1 AA9 4 GLY C 10 VAL C 12 0 SHEET 2 AA9 4 THR C 119 VAL C 123 1 O THR C 122 N GLY C 10 SHEET 3 AA9 4 ALA C 92 ASN C 99 -1 N TYR C 94 O THR C 119 SHEET 4 AA9 4 MET C 112 TRP C 115 -1 O VAL C 114 N ARG C 98 SHEET 1 AB1 4 SER C 132 LEU C 136 0 SHEET 2 AB1 4 THR C 147 TYR C 157 -1 O LYS C 155 N SER C 132 SHEET 3 AB1 4 TYR C 188 PRO C 197 -1 O TYR C 188 N TYR C 157 SHEET 4 AB1 4 VAL C 175 THR C 177 -1 N HIS C 176 O VAL C 193 SHEET 1 AB2 4 SER C 132 LEU C 136 0 SHEET 2 AB2 4 THR C 147 TYR C 157 -1 O LYS C 155 N SER C 132 SHEET 3 AB2 4 TYR C 188 PRO C 197 -1 O TYR C 188 N TYR C 157 SHEET 4 AB2 4 VAL C 181 LEU C 182 -1 N VAL C 181 O SER C 189 SHEET 1 AB3 3 THR C 163 TRP C 166 0 SHEET 2 AB3 3 TYR C 206 HIS C 212 -1 O ASN C 211 N THR C 163 SHEET 3 AB3 3 THR C 217 VAL C 223 -1 O VAL C 219 N VAL C 210 SHEET 1 AB4 4 MET D 4 SER D 7 0 SHEET 2 AB4 4 ALA D 19 SER D 25 -1 O SER D 22 N SER D 7 SHEET 3 AB4 4 ASP D 75 ILE D 80 -1 O ILE D 80 N ALA D 19 SHEET 4 AB4 4 PHE D 67 SER D 72 -1 N SER D 68 O LYS D 79 SHEET 1 AB5 6 SER D 10 VAL D 13 0 SHEET 2 AB5 6 THR D 107 ILE D 111 1 O ARG D 108 N LEU D 11 SHEET 3 AB5 6 GLY D 89 GLN D 95 -1 N GLY D 89 O LEU D 109 SHEET 4 AB5 6 LEU D 38 GLN D 43 -1 N TYR D 41 O TYR D 92 SHEET 5 AB5 6 PRO D 49 TYR D 54 -1 O ILE D 53 N TRP D 40 SHEET 6 AB5 6 ASN D 58 ARG D 59 -1 O ASN D 58 N TYR D 54 SHEET 1 AB6 4 SER D 10 VAL D 13 0 SHEET 2 AB6 4 THR D 107 ILE D 111 1 O ARG D 108 N LEU D 11 SHEET 3 AB6 4 GLY D 89 GLN D 95 -1 N GLY D 89 O LEU D 109 SHEET 4 AB6 4 THR D 102 PHE D 103 -1 O THR D 102 N GLN D 95 SHEET 1 AB7 4 SER D 119 PHE D 123 0 SHEET 2 AB7 4 THR D 134 PHE D 144 -1 O LEU D 140 N PHE D 121 SHEET 3 AB7 4 TYR D 178 SER D 187 -1 O LEU D 186 N ALA D 135 SHEET 4 AB7 4 SER D 164 VAL D 168 -1 N GLN D 165 O THR D 183 SHEET 1 AB8 3 LYS D 150 VAL D 155 0 SHEET 2 AB8 3 VAL D 196 THR D 202 -1 O GLU D 200 N GLN D 152 SHEET 3 AB8 3 VAL D 210 ASN D 215 -1 O VAL D 210 N VAL D 201 SHEET 1 AB9 3 THR B 48 ASP B 50 0 SHEET 2 AB9 3 LEU B 76 GLU B 79 1 O ILE B 78 N VAL B 49 SHEET 3 AB9 3 MET B 256 GLN B 259 1 O ILE B 258 N GLU B 79 SHEET 1 AC1 5 ILE B 108 ALA B 112 0 SHEET 2 AC1 5 ARG B 247 LEU B 251 -1 O ALA B 248 N GLU B 111 SHEET 3 AC1 5 ALA B 167 HIS B 175 -1 N LEU B 168 O SER B 249 SHEET 4 AC1 5 PHE B 242 PRO B 245 -1 O ILE B 243 N GLY B 172 SHEET 5 AC1 5 MET B 140 TRP B 142 -1 N LYS B 141 O ALA B 244 SHEET 1 AC2 4 ILE B 108 ALA B 112 0 SHEET 2 AC2 4 ARG B 247 LEU B 251 -1 O ALA B 248 N GLU B 111 SHEET 3 AC2 4 ALA B 167 HIS B 175 -1 N LEU B 168 O SER B 249 SHEET 4 AC2 4 ARG B 220 LEU B 228 -1 O HIS B 224 N TRP B 171 SHEET 1 AC3 2 ILE B 120 ARG B 121 0 SHEET 2 AC3 2 LEU B 144 SER B 145 -1 O LEU B 144 N ARG B 121 SHEET 1 AC4 2 THR B 126 ARG B 130 0 SHEET 2 AC4 2 SER B 134 SER B 135 -1 O SER B 135 N THR B 126 SHEET 1 AC5 4 MET B 155 LYS B 160 0 SHEET 2 AC5 4 THR B 233 PHE B 238 -1 O PHE B 236 N LYS B 157 SHEET 3 AC5 4 VAL B 193 SER B 197 -1 N THR B 194 O SER B 237 SHEET 4 AC5 4 TYR B 200 PHE B 204 -1 O PHE B 204 N VAL B 193 SHEET 1 AC6 4 GLN E 3 SER E 7 0 SHEET 2 AC6 4 LEU E 18 SER E 25 -1 O SER E 21 N SER E 7 SHEET 3 AC6 4 THR E 78 MET E 83 -1 O MET E 83 N LEU E 18 SHEET 4 AC6 4 THR E 69 ASP E 73 -1 N ASP E 73 O THR E 78 SHEET 1 AC7 6 GLY E 10 VAL E 12 0 SHEET 2 AC7 6 THR E 119 VAL E 123 1 O THR E 122 N VAL E 12 SHEET 3 AC7 6 ALA E 92 ASN E 99 -1 N ALA E 92 O VAL E 121 SHEET 4 AC7 6 MET E 34 GLN E 39 -1 N VAL E 37 O TYR E 95 SHEET 5 AC7 6 GLU E 46 ILE E 51 -1 O GLU E 46 N ARG E 38 SHEET 6 AC7 6 LYS E 58 TYR E 60 -1 O TYR E 59 N VAL E 50 SHEET 1 AC8 4 GLY E 10 VAL E 12 0 SHEET 2 AC8 4 THR E 119 VAL E 123 1 O THR E 122 N VAL E 12 SHEET 3 AC8 4 ALA E 92 ASN E 99 -1 N ALA E 92 O VAL E 121 SHEET 4 AC8 4 MET E 112 TRP E 115 -1 O VAL E 114 N ARG E 98 SHEET 1 AC9 4 SER E 132 LEU E 136 0 SHEET 2 AC9 4 THR E 147 TYR E 157 -1 O GLY E 151 N LEU E 136 SHEET 3 AC9 4 TYR E 188 PRO E 197 -1 O LEU E 190 N VAL E 154 SHEET 4 AC9 4 VAL E 175 THR E 177 -1 N HIS E 176 O VAL E 193 SHEET 1 AD1 4 SER E 132 LEU E 136 0 SHEET 2 AD1 4 THR E 147 TYR E 157 -1 O GLY E 151 N LEU E 136 SHEET 3 AD1 4 TYR E 188 PRO E 197 -1 O LEU E 190 N VAL E 154 SHEET 4 AD1 4 VAL E 181 LEU E 182 -1 N VAL E 181 O SER E 189 SHEET 1 AD2 3 THR E 163 TRP E 166 0 SHEET 2 AD2 3 TYR E 206 HIS E 212 -1 O ASN E 209 N SER E 165 SHEET 3 AD2 3 THR E 217 VAL E 223 -1 O VAL E 219 N VAL E 210 SHEET 1 AD3 4 MET F 4 SER F 7 0 SHEET 2 AD3 4 ALA F 19 SER F 25 -1 O ARG F 24 N THR F 5 SHEET 3 AD3 4 ASP F 75 ILE F 80 -1 O PHE F 76 N CYS F 23 SHEET 4 AD3 4 PHE F 67 SER F 72 -1 N SER F 70 O THR F 77 SHEET 1 AD4 6 SER F 10 VAL F 13 0 SHEET 2 AD4 6 THR F 107 ILE F 111 1 O ARG F 108 N LEU F 11 SHEET 3 AD4 6 GLY F 89 GLN F 95 -1 N GLY F 89 O LEU F 109 SHEET 4 AD4 6 LEU F 38 GLN F 43 -1 N TYR F 41 O TYR F 92 SHEET 5 AD4 6 PRO F 49 TYR F 54 -1 O ILE F 53 N TRP F 40 SHEET 6 AD4 6 ASN F 58 ARG F 59 -1 O ASN F 58 N TYR F 54 SHEET 1 AD5 4 SER F 10 VAL F 13 0 SHEET 2 AD5 4 THR F 107 ILE F 111 1 O ARG F 108 N LEU F 11 SHEET 3 AD5 4 GLY F 89 GLN F 95 -1 N GLY F 89 O LEU F 109 SHEET 4 AD5 4 THR F 102 PHE F 103 -1 O THR F 102 N GLN F 95 SHEET 1 AD6 4 SER F 119 PHE F 123 0 SHEET 2 AD6 4 THR F 134 PHE F 144 -1 O LEU F 140 N PHE F 121 SHEET 3 AD6 4 TYR F 178 SER F 187 -1 O LEU F 180 N LEU F 141 SHEET 4 AD6 4 SER F 164 VAL F 168 -1 N GLN F 165 O THR F 183 SHEET 1 AD7 4 ALA F 158 LEU F 159 0 SHEET 2 AD7 4 ALA F 149 VAL F 155 -1 N VAL F 155 O ALA F 158 SHEET 3 AD7 4 VAL F 196 HIS F 203 -1 O GLU F 200 N GLN F 152 SHEET 4 AD7 4 VAL F 210 ASN F 215 -1 O VAL F 210 N VAL F 201 SSBOND 1 CYS A 54 CYS A 66 1555 1555 2.06 SSBOND 2 CYS A 87 CYS A 129 1555 1555 2.06 SSBOND 3 CYS C 22 CYS C 96 1555 1555 2.03 SSBOND 4 CYS C 152 CYS C 208 1555 1555 2.04 SSBOND 5 CYS D 23 CYS D 93 1555 1555 2.13 SSBOND 6 CYS D 139 CYS D 199 1555 1555 2.06 SSBOND 7 CYS B 54 CYS B 66 1555 1555 2.06 SSBOND 8 CYS B 87 CYS B 129 1555 1555 2.07 SSBOND 9 CYS E 22 CYS E 96 1555 1555 2.08 SSBOND 10 CYS E 152 CYS E 208 1555 1555 2.05 SSBOND 11 CYS F 23 CYS F 93 1555 1555 2.11 SSBOND 12 CYS F 139 CYS F 199 1555 1555 2.02 LINK ND2 ASN A 231 C1 NAG A1001 1555 1555 1.45 LINK ND2 ASN B 231 C1 NAG B1001 1555 1555 1.45 CISPEP 1 PHE C 158 PRO C 159 0 -3.89 CISPEP 2 GLU C 160 PRO C 161 0 4.01 CISPEP 3 SER D 7 PRO D 8 0 -6.19 CISPEP 4 THR D 99 PRO D 100 0 2.53 CISPEP 5 TYR D 145 PRO D 146 0 -0.22 CISPEP 6 PHE E 158 PRO E 159 0 1.93 CISPEP 7 GLU E 160 PRO E 161 0 -4.11 CISPEP 8 SER F 7 PRO F 8 0 -3.87 CISPEP 9 THR F 99 PRO F 100 0 0.61 CISPEP 10 TYR F 145 PRO F 146 0 3.04 CRYST1 240.603 95.053 99.265 90.00 95.85 90.00 C 1 2 1 8 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 0.004156 0.000000 0.000426 0.00000 SCALE2 0.000000 0.010520 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010127 0.00000