HEADER VIRAL PROTEIN/IMMUNE SYSTEM 26-AUG-16 5T3X TITLE 3.9 ANGSTROM CRYSTAL STRUCTURE OF A FULLY AND NATIVELY GLYCOSYLATED TITLE 2 BG505 SOSIP.664 HIV-1 ENV TRIMER IN COMPLEX WITH THE BROADLY TITLE 3 NEUTRALIZING ANTIBODIES IOMA AND 10-1074. COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPE GLYCOPROTEIN GP160; COMPND 3 CHAIN: B; COMPND 4 FRAGMENT: UNP RESIDUES 509-611; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: ENVELOPE GLYCOPROTEIN GP160; COMPND 8 CHAIN: G; COMPND 9 FRAGMENT: UNP RESIDUES 30-508; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: 10-1074 HEAVY CHAIN; COMPND 13 CHAIN: H; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: 10-1074 LIGHT CHAIN; COMPND 17 CHAIN: L; COMPND 18 ENGINEERED: YES; COMPND 19 MOL_ID: 5; COMPND 20 MOLECULE: IOMA HEAVY CHAIN; COMPND 21 CHAIN: D; COMPND 22 ENGINEERED: YES; COMPND 23 MOL_ID: 6; COMPND 24 MOLECULE: IOMA LIGHT CHAIN; COMPND 25 CHAIN: E; COMPND 26 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_TAXID: 11676; SOURCE 4 GENE: ENV; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 9 ORGANISM_TAXID: 11676; SOURCE 10 GENE: ENV; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 MOL_ID: 4; SOURCE 19 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 23 MOL_ID: 5; SOURCE 24 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 28 MOL_ID: 6; SOURCE 29 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 30 ORGANISM_TAXID: 9606; SOURCE 31 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 32 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HIV, N-LINKED GLYCOSYLATION, BROADLY NEUTRALIZING ANTIBODIES, VIRAL KEYWDS 2 PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR H.B.GRISTICK,P.J.BJORKMAN REVDAT 2 19-OCT-16 5T3X 1 JRNL REVDAT 1 05-OCT-16 5T3X 0 JRNL AUTH H.B.GRISTICK,L.VON BOEHMER,A.P.WEST,M.SCHAMBER,A.GAZUMYAN, JRNL AUTH 2 J.GOLIJANIN,M.S.SEAMAN,G.FATKENHEUER,F.KLEIN, JRNL AUTH 3 M.C.NUSSENZWEIG,P.J.BJORKMAN JRNL TITL NATIVELY GLYCOSYLATED HIV-1 ENV STRUCTURE REVEALS NEW MODE JRNL TITL 2 FOR ANTIBODY RECOGNITION OF THE CD4-BINDING SITE. JRNL REF NAT.STRUCT.MOL.BIOL. V. 23 906 2016 JRNL REFN ESSN 1545-9985 JRNL PMID 27617431 JRNL DOI 10.1038/NSMB.3291 REMARK 2 REMARK 2 RESOLUTION. 3.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.10.1_2155 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 : TWIN_LSQ_F REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 80.63 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 25058 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.300 REMARK 3 R VALUE (WORKING SET) : 0.296 REMARK 3 FREE R VALUE : 0.331 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090 REMARK 3 FREE R VALUE TEST SET COUNT : 1276 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 43.4103 - 8.0982 0.95 2645 135 0.2439 0.3115 REMARK 3 2 8.0982 - 6.4345 0.95 2653 139 0.3091 0.3336 REMARK 3 3 6.4345 - 5.6231 0.95 2629 149 0.3252 0.3634 REMARK 3 4 5.6231 - 5.1098 0.95 2664 138 0.2976 0.3130 REMARK 3 5 5.1098 - 4.7441 0.95 2650 127 0.3078 0.3057 REMARK 3 6 4.7441 - 4.4647 0.95 2657 137 0.3184 0.3013 REMARK 3 7 4.4647 - 4.2413 0.94 2593 159 0.3255 0.3706 REMARK 3 8 4.2413 - 4.0568 0.95 2654 142 0.3419 0.3839 REMARK 3 9 4.0568 - 3.9007 0.94 2615 149 0.3623 0.3818 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) : NULL REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 44.460 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: 0.1600 REMARK 3 OPERATOR: K,H,-L REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.003 13016 REMARK 3 ANGLE : 1.108 17908 REMARK 3 CHIRALITY : 0.051 1956 REMARK 3 PLANARITY : 0.005 2071 REMARK 3 DIHEDRAL : 13.862 7559 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 28 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 518 THROUGH 571 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.1248 -11.4239 126.6706 REMARK 3 T TENSOR REMARK 3 T11: 2.9422 T22: 2.6859 REMARK 3 T33: 1.9188 T12: -1.0281 REMARK 3 T13: -0.0804 T23: 0.1594 REMARK 3 L TENSOR REMARK 3 L11: 0.1151 L22: 0.1534 REMARK 3 L33: 0.0244 L12: -0.1957 REMARK 3 L13: -0.1524 L23: 0.0975 REMARK 3 S TENSOR REMARK 3 S11: 1.6387 S12: -0.2813 S13: -0.8531 REMARK 3 S21: 1.0101 S22: -0.0481 S23: -0.5653 REMARK 3 S31: 0.3614 S32: -0.4334 S33: 0.0013 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 572 THROUGH 610 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.2277 1.2999 126.7059 REMARK 3 T TENSOR REMARK 3 T11: 1.1555 T22: 2.5437 REMARK 3 T33: 1.6272 T12: -1.0067 REMARK 3 T13: 0.3581 T23: 0.8508 REMARK 3 L TENSOR REMARK 3 L11: 1.6607 L22: 3.9026 REMARK 3 L33: 1.0297 L12: -2.1362 REMARK 3 L13: 0.9142 L23: -1.3198 REMARK 3 S TENSOR REMARK 3 S11: -1.3794 S12: -0.5029 S13: -0.9407 REMARK 3 S21: 2.5331 S22: 0.9828 S23: 0.1256 REMARK 3 S31: -1.4641 S32: -0.4101 S33: 0.0565 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 611 THROUGH 650 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.3950 5.3223 135.9566 REMARK 3 T TENSOR REMARK 3 T11: 3.0546 T22: 2.4073 REMARK 3 T33: 1.4154 T12: 0.2274 REMARK 3 T13: 0.2320 T23: -0.0621 REMARK 3 L TENSOR REMARK 3 L11: 0.0722 L22: 0.1111 REMARK 3 L33: 0.0141 L12: -0.1273 REMARK 3 L13: -0.0029 L23: -0.0311 REMARK 3 S TENSOR REMARK 3 S11: 0.4630 S12: 0.1410 S13: 0.2891 REMARK 3 S21: -0.0033 S22: -0.7393 S23: 0.1157 REMARK 3 S31: -0.0721 S32: -1.1742 S33: -0.0000 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 651 THROUGH 664 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.0337 14.7132 145.6516 REMARK 3 T TENSOR REMARK 3 T11: 5.3583 T22: 2.4663 REMARK 3 T33: 1.5526 T12: 0.7078 REMARK 3 T13: 0.0692 T23: -0.0452 REMARK 3 L TENSOR REMARK 3 L11: 0.0015 L22: 0.0246 REMARK 3 L33: 0.0207 L12: -0.0099 REMARK 3 L13: -0.0017 L23: -0.0002 REMARK 3 S TENSOR REMARK 3 S11: 0.0580 S12: -0.7261 S13: 0.0209 REMARK 3 S21: -0.3469 S22: 0.0162 S23: 0.2245 REMARK 3 S31: 0.0130 S32: 0.2066 S33: -0.0000 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 33 THROUGH 98 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.1030 -11.6983 113.6082 REMARK 3 T TENSOR REMARK 3 T11: 2.1038 T22: 2.3939 REMARK 3 T33: 2.2900 T12: 0.0668 REMARK 3 T13: 0.1556 T23: 0.2992 REMARK 3 L TENSOR REMARK 3 L11: 0.6054 L22: -0.1913 REMARK 3 L33: 0.4448 L12: -0.2467 REMARK 3 L13: 0.6063 L23: 0.0384 REMARK 3 S TENSOR REMARK 3 S11: 0.5865 S12: -0.1480 S13: -0.7689 REMARK 3 S21: 0.5190 S22: -0.0589 S23: 0.5123 REMARK 3 S31: -0.3651 S32: 0.4267 S33: 0.0001 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 99 THROUGH 190 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.4988 -11.7512 71.6600 REMARK 3 T TENSOR REMARK 3 T11: 0.6966 T22: 0.9449 REMARK 3 T33: 1.0657 T12: -0.1069 REMARK 3 T13: -0.0272 T23: 0.0299 REMARK 3 L TENSOR REMARK 3 L11: 0.8885 L22: 0.4827 REMARK 3 L33: 0.5863 L12: -0.5176 REMARK 3 L13: -0.7192 L23: -0.1202 REMARK 3 S TENSOR REMARK 3 S11: 0.3976 S12: 0.0333 S13: -0.0927 REMARK 3 S21: 0.0211 S22: -0.2394 S23: -0.6768 REMARK 3 S31: -0.1386 S32: 0.0769 S33: -0.0003 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 191 THROUGH 505 ) REMARK 3 ORIGIN FOR THE GROUP (A): -28.1857 -15.8999 93.5666 REMARK 3 T TENSOR REMARK 3 T11: 0.7338 T22: 0.8126 REMARK 3 T33: 0.3792 T12: -0.2271 REMARK 3 T13: 0.1046 T23: 0.2979 REMARK 3 L TENSOR REMARK 3 L11: 0.0939 L22: 0.4115 REMARK 3 L33: 1.3316 L12: -1.0154 REMARK 3 L13: -0.0703 L23: 0.7230 REMARK 3 S TENSOR REMARK 3 S11: 0.3992 S12: -0.3156 S13: -0.6529 REMARK 3 S21: 0.0131 S22: -0.0841 S23: 0.2751 REMARK 3 S31: -0.1755 S32: -0.2177 S33: 0.1808 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 23 ) REMARK 3 ORIGIN FOR THE GROUP (A): -41.6690 -46.7461 32.9480 REMARK 3 T TENSOR REMARK 3 T11: 3.7571 T22: 1.9962 REMARK 3 T33: 2.9040 T12: -0.5137 REMARK 3 T13: -0.6725 T23: 0.0558 REMARK 3 L TENSOR REMARK 3 L11: 0.0828 L22: 0.1232 REMARK 3 L33: 0.0668 L12: -0.0918 REMARK 3 L13: -0.0436 L23: 0.0956 REMARK 3 S TENSOR REMARK 3 S11: -0.1935 S12: 0.3795 S13: -0.5599 REMARK 3 S21: -0.3774 S22: 0.0256 S23: 0.2924 REMARK 3 S31: -0.5832 S32: 0.5171 S33: -0.0000 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 24 THROUGH 63 ) REMARK 3 ORIGIN FOR THE GROUP (A): -38.8843 -41.7548 45.5746 REMARK 3 T TENSOR REMARK 3 T11: 2.5180 T22: 1.8895 REMARK 3 T33: 3.8035 T12: -0.3790 REMARK 3 T13: -0.5021 T23: -0.2057 REMARK 3 L TENSOR REMARK 3 L11: 0.1506 L22: 0.2695 REMARK 3 L33: 0.2602 L12: -0.1037 REMARK 3 L13: 0.2058 L23: -0.0124 REMARK 3 S TENSOR REMARK 3 S11: -1.1636 S12: -0.5039 S13: -0.8228 REMARK 3 S21: -1.0062 S22: -0.6038 S23: 0.0883 REMARK 3 S31: -0.7741 S32: -0.6520 S33: 0.0001 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 64 THROUGH 90 ) REMARK 3 ORIGIN FOR THE GROUP (A): -40.9838 -39.9127 35.9926 REMARK 3 T TENSOR REMARK 3 T11: 2.9107 T22: 2.9334 REMARK 3 T33: 3.4174 T12: -0.0481 REMARK 3 T13: -0.4883 T23: 0.0276 REMARK 3 L TENSOR REMARK 3 L11: 0.0898 L22: 0.0570 REMARK 3 L33: 0.0721 L12: -0.0576 REMARK 3 L13: 0.1066 L23: -0.0728 REMARK 3 S TENSOR REMARK 3 S11: 0.4394 S12: -0.1896 S13: -0.0361 REMARK 3 S21: -1.0120 S22: 0.8720 S23: 0.0586 REMARK 3 S31: 0.3792 S32: -0.3702 S33: -0.0001 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 91 THROUGH 124 ) REMARK 3 ORIGIN FOR THE GROUP (A): -34.6996 -45.9601 45.2163 REMARK 3 T TENSOR REMARK 3 T11: 2.2549 T22: 0.7561 REMARK 3 T33: 1.9455 T12: -0.6698 REMARK 3 T13: -0.6845 T23: -0.0789 REMARK 3 L TENSOR REMARK 3 L11: 0.8924 L22: 0.3677 REMARK 3 L33: -0.0005 L12: -0.7699 REMARK 3 L13: 0.2410 L23: -0.0257 REMARK 3 S TENSOR REMARK 3 S11: 0.5937 S12: -0.5431 S13: -0.3676 REMARK 3 S21: -0.4536 S22: 0.5043 S23: 0.5970 REMARK 3 S31: 0.1114 S32: 0.2757 S33: 0.2390 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 125 THROUGH 184 ) REMARK 3 ORIGIN FOR THE GROUP (A): -31.4631 -65.5237 21.4430 REMARK 3 T TENSOR REMARK 3 T11: 4.6772 T22: 2.0124 REMARK 3 T33: 2.3836 T12: -0.0318 REMARK 3 T13: 0.0624 T23: -0.9011 REMARK 3 L TENSOR REMARK 3 L11: 0.1237 L22: 0.0838 REMARK 3 L33: 0.1116 L12: -0.0607 REMARK 3 L13: 0.0081 L23: -0.0456 REMARK 3 S TENSOR REMARK 3 S11: -0.3955 S12: 1.3431 S13: -0.8810 REMARK 3 S21: -0.2174 S22: -1.3157 S23: 0.5729 REMARK 3 S31: -0.1683 S32: -1.1422 S33: -0.0418 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 185 THROUGH 216 ) REMARK 3 ORIGIN FOR THE GROUP (A): -40.0014 -70.8204 18.8579 REMARK 3 T TENSOR REMARK 3 T11: 3.9043 T22: 2.6823 REMARK 3 T33: 3.2336 T12: -0.9868 REMARK 3 T13: -0.8139 T23: -0.4336 REMARK 3 L TENSOR REMARK 3 L11: 0.0566 L22: 0.0114 REMARK 3 L33: 0.1099 L12: -0.0389 REMARK 3 L13: 0.0726 L23: -0.0372 REMARK 3 S TENSOR REMARK 3 S11: -0.8919 S12: 0.2180 S13: -0.5282 REMARK 3 S21: 0.0760 S22: -0.7309 S23: -0.2849 REMARK 3 S31: -0.9291 S32: -0.1218 S33: -0.0002 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 8 THROUGH 22 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.9163 -56.7064 51.3184 REMARK 3 T TENSOR REMARK 3 T11: 2.5783 T22: 3.0267 REMARK 3 T33: 2.9645 T12: 0.0438 REMARK 3 T13: -0.5490 T23: -0.9193 REMARK 3 L TENSOR REMARK 3 L11: 0.0297 L22: 0.0517 REMARK 3 L33: 0.0065 L12: -0.0656 REMARK 3 L13: -0.0237 L23: 0.0368 REMARK 3 S TENSOR REMARK 3 S11: -0.5229 S12: -0.1578 S13: -0.5553 REMARK 3 S21: -0.1991 S22: -0.8425 S23: -0.6098 REMARK 3 S31: -0.0358 S32: 0.1845 S33: 0.0000 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 23 THROUGH 44 ) REMARK 3 ORIGIN FOR THE GROUP (A): -23.4791 -47.7194 52.0046 REMARK 3 T TENSOR REMARK 3 T11: 1.8836 T22: 0.6834 REMARK 3 T33: 2.1871 T12: -0.5157 REMARK 3 T13: -0.7422 T23: -0.8708 REMARK 3 L TENSOR REMARK 3 L11: 0.8454 L22: 0.7163 REMARK 3 L33: 0.3612 L12: -0.3712 REMARK 3 L13: 0.0851 L23: 0.4005 REMARK 3 S TENSOR REMARK 3 S11: 0.1254 S12: -0.3860 S13: 0.0017 REMARK 3 S21: -1.5535 S22: 1.2094 S23: -0.5249 REMARK 3 S31: 1.1082 S32: 0.1387 S33: 0.5651 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 45 THROUGH 84 ) REMARK 3 ORIGIN FOR THE GROUP (A): -22.3460 -54.4612 58.6412 REMARK 3 T TENSOR REMARK 3 T11: 1.6903 T22: 1.8730 REMARK 3 T33: 2.7695 T12: -0.2420 REMARK 3 T13: -0.3337 T23: -0.3186 REMARK 3 L TENSOR REMARK 3 L11: 0.0343 L22: 0.0112 REMARK 3 L33: 0.0048 L12: 0.0538 REMARK 3 L13: -0.0312 L23: -0.0075 REMARK 3 S TENSOR REMARK 3 S11: -0.0890 S12: 0.1779 S13: -0.5943 REMARK 3 S21: 0.3471 S22: 0.2148 S23: -0.9821 REMARK 3 S31: -0.4326 S32: 0.3825 S33: -0.0002 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 85 THROUGH 101 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.4812 -41.1989 52.2333 REMARK 3 T TENSOR REMARK 3 T11: 1.3160 T22: 1.1507 REMARK 3 T33: 2.3862 T12: -0.3417 REMARK 3 T13: -0.3607 T23: -0.7234 REMARK 3 L TENSOR REMARK 3 L11: 0.1317 L22: 0.3335 REMARK 3 L33: 0.8755 L12: 0.0077 REMARK 3 L13: -0.1065 L23: -0.5046 REMARK 3 S TENSOR REMARK 3 S11: 0.7128 S12: -0.9006 S13: -0.1890 REMARK 3 S21: 0.2590 S22: 1.0995 S23: 0.0341 REMARK 3 S31: 0.1384 S32: -0.2951 S33: 0.4630 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 102 THROUGH 130 ) REMARK 3 ORIGIN FOR THE GROUP (A): -21.7288 -67.8506 23.9647 REMARK 3 T TENSOR REMARK 3 T11: 3.9688 T22: 2.9780 REMARK 3 T33: 3.0282 T12: 0.8013 REMARK 3 T13: -0.2117 T23: -0.5974 REMARK 3 L TENSOR REMARK 3 L11: 0.1837 L22: 0.1019 REMARK 3 L33: 0.0900 L12: -0.1658 REMARK 3 L13: 0.0311 L23: -0.0879 REMARK 3 S TENSOR REMARK 3 S11: -0.0972 S12: 0.4265 S13: 0.2494 REMARK 3 S21: -0.6235 S22: -0.5646 S23: -1.3748 REMARK 3 S31: -0.2823 S32: -0.7221 S33: -0.0002 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 131 THROUGH 151 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.3847 -68.3326 22.0349 REMARK 3 T TENSOR REMARK 3 T11: 3.8296 T22: 4.5596 REMARK 3 T33: 5.2031 T12: -1.0903 REMARK 3 T13: 0.8176 T23: -0.8120 REMARK 3 L TENSOR REMARK 3 L11: 0.0509 L22: 0.0241 REMARK 3 L33: 0.0213 L12: 0.0122 REMARK 3 L13: -0.0344 L23: -0.0039 REMARK 3 S TENSOR REMARK 3 S11: -0.0634 S12: 0.1121 S13: -0.0684 REMARK 3 S21: -0.1334 S22: 0.0850 S23: 0.2013 REMARK 3 S31: -0.0352 S32: -0.1360 S33: 0.0000 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 152 THROUGH 172 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.4295 -64.8449 22.0823 REMARK 3 T TENSOR REMARK 3 T11: 4.4688 T22: 3.1022 REMARK 3 T33: 3.9708 T12: -0.5084 REMARK 3 T13: 0.7138 T23: -0.5579 REMARK 3 L TENSOR REMARK 3 L11: -0.0004 L22: -0.0082 REMARK 3 L33: 0.0164 L12: -0.0068 REMARK 3 L13: 0.0194 L23: -0.0067 REMARK 3 S TENSOR REMARK 3 S11: 0.1621 S12: 0.8494 S13: -0.8566 REMARK 3 S21: -0.4153 S22: -0.1903 S23: 0.5807 REMARK 3 S31: -0.1896 S32: 0.4392 S33: 0.0001 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 173 THROUGH 188 ) REMARK 3 ORIGIN FOR THE GROUP (A): -21.0850 -66.2224 11.5453 REMARK 3 T TENSOR REMARK 3 T11: 5.4368 T22: 4.7236 REMARK 3 T33: 2.3383 T12: -2.0430 REMARK 3 T13: 0.1361 T23: -0.6634 REMARK 3 L TENSOR REMARK 3 L11: -0.0304 L22: 0.0640 REMARK 3 L33: 0.0162 L12: -0.0221 REMARK 3 L13: 0.0169 L23: -0.0183 REMARK 3 S TENSOR REMARK 3 S11: 0.1722 S12: 0.9589 S13: 0.1945 REMARK 3 S21: -0.0132 S22: -0.0269 S23: -0.0373 REMARK 3 S31: 0.0941 S32: 0.0160 S33: -0.0001 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 189 THROUGH 198 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.4330 -72.9514 13.7661 REMARK 3 T TENSOR REMARK 3 T11: 3.9886 T22: 4.7940 REMARK 3 T33: 3.5306 T12: -0.6096 REMARK 3 T13: 0.6624 T23: -0.1493 REMARK 3 L TENSOR REMARK 3 L11: 0.0136 L22: 0.0167 REMARK 3 L33: 0.0273 L12: -0.0247 REMARK 3 L13: 0.0271 L23: -0.0108 REMARK 3 S TENSOR REMARK 3 S11: 0.5035 S12: 0.2380 S13: 0.6448 REMARK 3 S21: -0.2366 S22: -0.3481 S23: 0.0502 REMARK 3 S31: 0.0720 S32: 0.2486 S33: 0.0001 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 199 THROUGH 212 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.0113 -77.3419 16.1783 REMARK 3 T TENSOR REMARK 3 T11: 4.5972 T22: 4.7954 REMARK 3 T33: 2.4105 T12: -0.2437 REMARK 3 T13: -0.3735 T23: -0.1776 REMARK 3 L TENSOR REMARK 3 L11: 0.0113 L22: 0.0407 REMARK 3 L33: 0.0332 L12: 0.0341 REMARK 3 L13: 0.0095 L23: -0.0495 REMARK 3 S TENSOR REMARK 3 S11: -0.0929 S12: 0.3232 S13: 0.2157 REMARK 3 S21: -0.1056 S22: 0.7889 S23: -0.0167 REMARK 3 S31: 0.3547 S32: -0.2952 S33: -0.0001 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 125 ) REMARK 3 ORIGIN FOR THE GROUP (A): -42.7550 7.9885 77.9873 REMARK 3 T TENSOR REMARK 3 T11: 0.9644 T22: 1.5090 REMARK 3 T33: 1.4040 T12: 0.0313 REMARK 3 T13: 0.0914 T23: -0.0653 REMARK 3 L TENSOR REMARK 3 L11: 0.0748 L22: 0.4641 REMARK 3 L33: -0.0398 L12: -0.3314 REMARK 3 L13: 0.1718 L23: -0.2684 REMARK 3 S TENSOR REMARK 3 S11: -0.1091 S12: -0.0955 S13: 0.3751 REMARK 3 S21: -0.0745 S22: -0.2958 S23: 0.3375 REMARK 3 S31: 0.3113 S32: -0.1729 S33: 0.0000 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 126 THROUGH 211 ) REMARK 3 ORIGIN FOR THE GROUP (A): -65.6262 30.4339 60.4412 REMARK 3 T TENSOR REMARK 3 T11: 2.9740 T22: 3.9311 REMARK 3 T33: 4.0331 T12: 0.0573 REMARK 3 T13: 0.0473 T23: 0.4029 REMARK 3 L TENSOR REMARK 3 L11: 0.0683 L22: 0.0677 REMARK 3 L33: 0.0346 L12: -0.1330 REMARK 3 L13: 0.0859 L23: -0.1049 REMARK 3 S TENSOR REMARK 3 S11: -0.1734 S12: 0.0561 S13: 0.4314 REMARK 3 S21: -0.4652 S22: -1.1957 S23: -0.2068 REMARK 3 S31: 0.0275 S32: -0.6008 S33: -0.0002 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 212 THROUGH 216 ) REMARK 3 ORIGIN FOR THE GROUP (A): -80.3808 35.3572 53.8697 REMARK 3 T TENSOR REMARK 3 T11: 5.5284 T22: 6.8260 REMARK 3 T33: 3.0133 T12: -1.0697 REMARK 3 T13: 1.0178 T23: -0.5449 REMARK 3 L TENSOR REMARK 3 L11: 0.2187 L22: 0.0516 REMARK 3 L33: 0.0146 L12: 0.1099 REMARK 3 L13: 0.0044 L23: 0.0059 REMARK 3 S TENSOR REMARK 3 S11: 0.0535 S12: 0.0260 S13: -0.0448 REMARK 3 S21: 0.0834 S22: 0.0580 S23: 0.1295 REMARK 3 S31: -0.1388 S32: -0.0656 S33: 0.0012 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 2 THROUGH 114 ) REMARK 3 ORIGIN FOR THE GROUP (A): -52.8077 20.3767 94.4008 REMARK 3 T TENSOR REMARK 3 T11: 1.2465 T22: 1.9217 REMARK 3 T33: 2.0348 T12: 0.2963 REMARK 3 T13: 0.2411 T23: -0.6843 REMARK 3 L TENSOR REMARK 3 L11: 0.3963 L22: 0.5687 REMARK 3 L33: 0.3627 L12: 0.0804 REMARK 3 L13: 0.2276 L23: 0.6005 REMARK 3 S TENSOR REMARK 3 S11: -0.2849 S12: -0.0907 S13: 0.1261 REMARK 3 S21: 0.3600 S22: -0.3649 S23: 0.5738 REMARK 3 S31: -0.5271 S32: -0.5606 S33: -0.0060 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 115 THROUGH 210 ) REMARK 3 ORIGIN FOR THE GROUP (A): -75.4569 22.2991 68.3839 REMARK 3 T TENSOR REMARK 3 T11: 3.0841 T22: 3.6607 REMARK 3 T33: 6.6124 T12: 0.3996 REMARK 3 T13: -2.6794 T23: 0.1963 REMARK 3 L TENSOR REMARK 3 L11: 0.2910 L22: 1.6986 REMARK 3 L33: 1.2806 L12: 0.0852 REMARK 3 L13: -0.2338 L23: 1.2788 REMARK 3 S TENSOR REMARK 3 S11: 1.0668 S12: 1.0176 S13: 0.9375 REMARK 3 S21: -2.1832 S22: 1.1601 S23: 0.4786 REMARK 3 S31: -0.1575 S32: -1.0953 S33: 0.3550 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 5T3X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-SEP-16. REMARK 100 THE DEPOSITION ID IS D_1000223652. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-DEC-15 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 : SSRL REMARK 200 BEAMLINE : BL12-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.00 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25079 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.900 REMARK 200 RESOLUTION RANGE LOW (A) : 80.630 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 18.20 REMARK 200 R MERGE (I) : 0.35000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.17 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 18.30 REMARK 200 R MERGE FOR SHELL (I) : 2.85000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.500 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: PHASER 1.10.1-2155 REMARK 200 STARTING MODEL: 4TVP, 4FQ2, 4TNN, 4XVS REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 70.94 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.23 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM AMMONIUM CITRATE TRIBASIC PH REMARK 280 7.0 100 MM IMIDAZOLE PH 7.0 20% PEG MME 2,000, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 X+2/3,Y+1/3,Z+1/3 REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3 REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3 REMARK 290 7555 X+1/3,Y+2/3,Z+2/3 REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3 REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 108.75450 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 62.78944 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 52.00300 REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 108.75450 REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 62.78944 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 52.00300 REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 108.75450 REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 62.78944 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 52.00300 REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 125.57888 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 104.00600 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 125.57888 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 104.00600 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 125.57888 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 104.00600 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: OCTADECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G, H, L, D, E 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 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 350 BIOMT3 3 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 ALA B 512 REMARK 465 VAL B 513 REMARK 465 GLY B 514 REMARK 465 ILE B 515 REMARK 465 GLY B 516 REMARK 465 ALA B 517 REMARK 465 ILE B 548 REMARK 465 VAL B 549 REMARK 465 GLN B 550 REMARK 465 GLN B 551 REMARK 465 GLN B 552 REMARK 465 SER B 553 REMARK 465 ASN B 554 REMARK 465 LEU B 555 REMARK 465 LEU B 556 REMARK 465 ARG B 557 REMARK 465 ALA B 558 REMARK 465 PRO B 559 REMARK 465 GLU B 560 REMARK 465 ALA B 561 REMARK 465 GLN B 562 REMARK 465 GLN B 563 REMARK 465 HIS B 564 REMARK 465 LEU B 565 REMARK 465 LEU B 566 REMARK 465 LYS B 567 REMARK 465 LEU B 568 REMARK 465 ALA G 31 REMARK 465 GLU G 32 REMARK 465 MET G 150 REMARK 465 ARG G 151 REMARK 465 GLU G 185A REMARK 465 ASN G 185B REMARK 465 GLN G 185C REMARK 465 GLY G 185D REMARK 465 ASN G 185E REMARK 465 ARG G 185F REMARK 465 SER G 185G REMARK 465 ASN G 185H REMARK 465 ASN G 185I REMARK 465 THR G 400 REMARK 465 SER G 401 REMARK 465 VAL G 402 REMARK 465 GLN G 403 REMARK 465 GLY G 404 REMARK 465 SER G 405 REMARK 465 ASN G 406 REMARK 465 SER G 407 REMARK 465 THR G 408 REMARK 465 GLY G 409 REMARK 465 SER G 410 REMARK 465 VAL G 506 REMARK 465 GLY G 507 REMARK 465 ARG G 508 REMARK 465 ARG G 509 REMARK 465 ARG G 510 REMARK 465 ARG G 511 REMARK 465 ARG G 512 REMARK 465 ARG G 513 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 ASP H 217 REMARK 465 LYS H 218 REMARK 465 THR H 219 REMARK 465 SER L 6 REMARK 465 TYR L 7 REMARK 465 SER L 213 REMARK 465 ASP D 217 REMARK 465 LYS D 218 REMARK 465 THR D 219 REMARK 465 GLN E 1 REMARK 465 GLU E 211 REMARK 465 CYS E 212 REMARK 465 SER E 213 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 O6 GAL G 2771 C1 SIA G 2772 2.03 REMARK 500 O6 GAL G 2766 C1 SIA G 2767 2.05 REMARK 500 O6 GAL G 1975 O6 SIA G 1976 2.05 REMARK 500 O LEU G 175 OG1 THR G 320 2.06 REMARK 500 OG1 THR B 606 O VAL G 36 2.11 REMARK 500 OD1 ASN D 199 NZ LYS D 206 2.13 REMARK 500 O6 GAL G 1975 C3 SIA G 1976 2.19 REMARK 500 O3 NAG G 3011 O2 BMA G 3012 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES 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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) 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 ATM2 ATM3 REMARK 500 GLY G 458 O - C - N ANGL. DEV. = -13.6 DEGREES REMARK 500 PRO D 100E C - N - CA ANGL. DEV. = 21.5 DEGREES REMARK 500 PRO D 100E C - N - CD ANGL. DEV. = -17.7 DEGREES 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 TRP B 571 -14.16 70.10 REMARK 500 CYS B 598 -84.62 -110.43 REMARK 500 SER B 599 -15.59 58.92 REMARK 500 LEU B 602 -22.13 78.18 REMARK 500 SER B 615 70.79 39.12 REMARK 500 GLU B 648 -62.57 -104.66 REMARK 500 GLN B 650 -78.81 -103.86 REMARK 500 GLN B 653 -62.77 -99.48 REMARK 500 PRO G 43 49.84 -74.23 REMARK 500 ASP G 57 -153.47 56.98 REMARK 500 GLU G 64 -113.93 48.12 REMARK 500 HIS G 66 72.47 58.67 REMARK 500 ASN G 67 73.44 62.79 REMARK 500 TRP G 69 -119.37 42.91 REMARK 500 HIS G 72 -69.03 -137.47 REMARK 500 PRO G 81 78.06 -65.79 REMARK 500 ILE G 138 -136.45 40.12 REMARK 500 ASP G 140 -74.29 -105.09 REMARK 500 GLU G 153 -14.31 68.92 REMARK 500 THR G 198 -73.69 -117.18 REMARK 500 PRO G 253 71.09 -68.10 REMARK 500 GLN G 258 -17.70 74.39 REMARK 500 ASN G 262 -1.29 71.06 REMARK 500 GLU G 268 -125.67 58.68 REMARK 500 SER G 365 -73.45 -101.56 REMARK 500 VAL G 371 -60.27 -103.01 REMARK 500 PHE G 376 160.84 178.88 REMARK 500 SER G 388 -64.45 -133.39 REMARK 500 ILE G 396 -89.04 -116.14 REMARK 500 SER G 397 -72.45 -136.54 REMARK 500 GLN G 422 -61.36 -91.58 REMARK 500 GLN G 428 -7.41 62.14 REMARK 500 ASP G 457 -126.31 -84.27 REMARK 500 SER G 460 -113.46 55.44 REMARK 500 THR G 464 -76.45 -108.88 REMARK 500 GLU G 492 77.92 -117.22 REMARK 500 ILE H 48 -74.09 -120.45 REMARK 500 GLU H 55 -3.21 78.46 REMARK 500 SER H 82B 70.66 50.83 REMARK 500 LYS H 105 -72.45 -86.07 REMARK 500 THR H 160 -72.83 -122.75 REMARK 500 LEU L 47 -63.84 -108.13 REMARK 500 ASN L 51 -36.62 76.29 REMARK 500 PRO L 66 -178.76 -68.51 REMARK 500 ASN L 66C 77.78 70.44 REMARK 500 PHE L 67 -134.78 65.93 REMARK 500 ASP L 152 -117.57 52.77 REMARK 500 ARG D 54 -2.09 59.60 REMARK 500 SER D 99 -179.24 -171.42 REMARK 500 ALA D 100A -78.63 -122.87 REMARK 500 REMARK 500 THIS ENTRY HAS 64 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC B REMARK 800 6110 through NAG B 6111 bound to ASN B 611 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC B REMARK 800 6370 through BMA B 6373 bound to ASN B 637 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC G REMARK 800 880 through NAG G 882 bound to ASN G 88 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 1330 through BMA G 1332 bound to ASN G 133 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC G REMARK 800 1560 through GAL G 1572 bound to ASN G 156 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC G REMARK 800 1600 through GAL G 1609 bound to ASN G 160 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 1970 through NAG G 1978 bound to ASN G 197 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 2340 through NAG G 2341 bound to ASN G 234 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 2620 through MAN G 2626 bound to ASN G 262 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC G REMARK 800 2760 through NAG G 2775 bound to ASN G 276 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 2950 through NAG G 2951 bound to ASN G 295 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 3010 through NAG G 3016 bound to ASN G 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 3320 through MAN G 3329 bound to ASN G 332 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 3390 REMARK 800 bound to ASN G 339 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 3550 through NAG G 3551 bound to ASN G 355 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 3630 through MAN G 3636 bound to ASN G 363 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 3860 through MAN G 3864 bound to ASN G 386 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC G REMARK 800 3920 through MAN G 3925 bound to ASN G 392 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 4480 through MAN G 4484 bound to ASN G 448 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5T3Z RELATED DB: PDB DBREF 5T3X B 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 5T3X G 31 511 UNP Q2N0S6 Q2N0S6_9HIV1 30 508 DBREF 5T3X H 1 219 PDB 5T3X 5T3X 1 219 DBREF 5T3X L 6 213 PDB 5T3X 5T3X 6 213 DBREF 5T3X D 1 219 PDB 5T3X 5T3X 1 219 DBREF 5T3X E 1 213 PDB 5T3X 5T3X 1 213 SEQADV 5T3X PRO B 559 UNP Q2N0S6 ILE 556 ENGINEERED MUTATION SEQADV 5T3X CYS B 605 UNP Q2N0S6 THR 602 ENGINEERED MUTATION SEQADV 5T3X ASN G 332 UNP Q2N0S6 THR 330 ENGINEERED MUTATION SEQADV 5T3X CYS G 501 UNP Q2N0S6 ALA 498 ENGINEERED MUTATION SEQADV 5T3X ARG G 509 UNP Q2N0S6 EXPRESSION TAG SEQADV 5T3X ARG G 510 UNP Q2N0S6 EXPRESSION TAG SEQADV 5T3X ARG G 512 UNP Q2N0S6 EXPRESSION TAG SEQADV 5T3X ARG G 513 UNP Q2N0S6 EXPRESSION TAG SEQRES 1 B 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 B 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 B 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 B 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 B 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 B 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 B 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 B 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 B 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 B 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 B 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 B 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 G 481 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 G 481 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 G 481 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 G 481 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 G 481 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 G 481 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 G 481 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 G 481 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 G 481 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 G 481 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 G 481 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 G 481 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 G 481 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 G 481 ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 G 481 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 G 481 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 G 481 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 G 481 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 G 481 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 G 481 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 G 481 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 G 481 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 G 481 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 G 481 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 G 481 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 G 481 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 G 481 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 G 481 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 G 481 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 G 481 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 G 481 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR SEQRES 32 G 481 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 G 481 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 G 481 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 G 481 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 G 481 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 G 481 CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 H 238 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 238 PRO SER GLU THR LEU SER VAL THR CYS SER VAL SER GLY SEQRES 3 H 238 ASP SER MET ASN ASN TYR TYR TRP THR TRP ILE ARG GLN SEQRES 4 H 238 SER PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE SER SEQRES 5 H 238 ASP ARG GLU SER ALA THR TYR ASN PRO SER LEU ASN SER SEQRES 6 H 238 ARG VAL VAL ILE SER ARG ASP THR SER LYS ASN GLN LEU SEQRES 7 H 238 SER LEU LYS LEU ASN SER VAL THR PRO ALA ASP THR ALA SEQRES 8 H 238 VAL TYR TYR CYS ALA THR ALA ARG ARG GLY GLN ARG ILE SEQRES 9 H 238 TYR GLY VAL VAL SER PHE GLY GLU PHE PHE TYR TYR TYR SEQRES 10 H 238 SER MET ASP VAL TRP GLY LYS GLY THR THR VAL THR VAL SEQRES 11 H 238 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 12 H 238 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 13 H 238 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 14 H 238 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 15 H 238 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 16 H 238 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 17 H 238 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 18 H 238 SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER SEQRES 19 H 238 CYS ASP LYS THR SEQRES 1 L 214 SER TYR VAL ARG PRO LEU SER VAL ALA LEU GLY GLU THR SEQRES 2 L 214 ALA ARG ILE SER CYS GLY ARG GLN ALA LEU GLY SER ARG SEQRES 3 L 214 ALA VAL GLN TRP TYR GLN HIS ARG PRO GLY GLN ALA PRO SEQRES 4 L 214 ILE LEU LEU ILE TYR ASN ASN GLN ASP ARG PRO SER GLY SEQRES 5 L 214 ILE PRO GLU ARG PHE SER GLY THR PRO ASP ILE ASN PHE SEQRES 6 L 214 GLY THR ARG ALA THR LEU THR ILE SER GLY VAL GLU ALA SEQRES 7 L 214 GLY ASP GLU ALA ASP TYR TYR CYS HIS MET TRP ASP SER SEQRES 8 L 214 ARG SER GLY PHE SER TRP SER PHE GLY GLY ALA THR ARG SEQRES 9 L 214 LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL SEQRES 10 L 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN SEQRES 11 L 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO SEQRES 12 L 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO SEQRES 13 L 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SEQRES 14 L 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU SEQRES 15 L 214 THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS SEQRES 16 L 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL SEQRES 17 L 214 ALA PRO THR GLU CYS SER SEQRES 1 D 232 GLU VAL GLN LEU VAL GLU SER GLY ALA GLN VAL LYS LYS SEQRES 2 D 232 PRO GLY ALA SER VAL THR VAL SER CYS THR ALA SER GLY SEQRES 3 D 232 TYR LYS PHE THR GLY TYR HIS MET HIS TRP VAL ARG GLN SEQRES 4 D 232 ALA PRO GLY ARG GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 D 232 PRO PHE ARG GLY ALA VAL LYS TYR PRO GLN ASN PHE ARG SEQRES 6 D 232 GLY ARG VAL SER MET THR ARG ASP THR SER MET GLU ILE SEQRES 7 D 232 PHE TYR MET GLU LEU SER ARG LEU THR SER ASP ASP THR SEQRES 8 D 232 ALA VAL TYR TYR CYS ALA ARG GLU MET PHE ASP SER SER SEQRES 9 D 232 ALA ASP TRP SER PRO TRP ARG GLY MET VAL ALA TRP GLY SEQRES 10 D 232 GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS SEQRES 11 D 232 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 12 D 232 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 13 D 232 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 D 232 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 15 D 232 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 16 D 232 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 17 D 232 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 18 D 232 LYS ARG VAL GLU PRO LYS SER CYS ASP LYS THR SEQRES 1 E 214 GLN SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SER SEQRES 2 E 214 PRO GLY GLN SER ILE THR ILE SER CYS ALA GLY SER SER SEQRES 3 E 214 ARG ASP VAL GLY GLY PHE ASP LEU VAL SER TRP TYR GLN SEQRES 4 E 214 GLN HIS PRO GLY LYS ALA PRO LYS LEU ILE ILE TYR GLU SEQRES 5 E 214 VAL ASN LYS ARG PRO SER GLY ILE SER SER ARG PHE SER SEQRES 6 E 214 ALA SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER SEQRES 7 E 214 GLY LEU GLN GLU GLU ASP GLU ALA HIS TYR TYR CYS TYR SEQRES 8 E 214 SER TYR ALA ASP GLY VAL ALA PHE GLY GLY GLY THR LYS SEQRES 9 E 214 LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL SEQRES 10 E 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN SEQRES 11 E 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO SEQRES 12 E 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO SEQRES 13 E 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SEQRES 14 E 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU SEQRES 15 E 214 THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS SEQRES 16 E 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL SEQRES 17 E 214 ALA PRO THR GLU CYS SER HET FUC B6110 10 HET NAG B6111 14 HET FUC B6370 10 HET NAG B6371 14 HET NAG B6372 14 HET BMA B6373 11 HET FUC G 880 10 HET NAG G 881 14 HET NAG G 882 14 HET NAG G1330 14 HET NAG G1331 14 HET BMA G1332 11 HET FUC G1560 10 HET NAG G1561 14 HET NAG G1562 14 HET BMA G1563 11 HET MAN G1564 11 HET NAG G1565 14 HET NAG G1566 14 HET GAL G1567 11 HET MAN G1568 11 HET NAG G1569 14 HET GAL G1570 11 HET NAG G1571 14 HET GAL G1572 11 HET FUC G1600 10 HET NAG G1601 14 HET NAG G1602 14 HET BMA G1603 11 HET MAN G1604 11 HET NAG G1605 14 HET GAL G1606 11 HET MAN G1607 11 HET NAG G1608 14 HET GAL G1609 11 HET NAG G1970 14 HET NAG G1971 14 HET BMA G1972 11 HET MAN G1973 11 HET NAG G1974 14 HET GAL G1975 11 HET SIA G1976 20 HET MAN G1977 11 HET NAG G1978 14 HET NAG G2340 14 HET NAG G2341 14 HET NAG G2620 14 HET NAG G2621 14 HET BMA G2622 11 HET MAN G2623 11 HET MAN G2624 11 HET MAN G2625 11 HET MAN G2626 11 HET FUC G2760 10 HET NAG G2761 14 HET NAG G2762 14 HET BMA G2763 11 HET MAN G2764 11 HET NAG G2765 14 HET GAL G2766 11 HET SIA G2767 20 HET NAG G2768 14 HET MAN G2769 11 HET NAG G2770 14 HET GAL G2771 11 HET SIA G2772 20 HET NAG G2773 14 HET GAL G2774 11 HET NAG G2775 14 HET NAG G2950 14 HET NAG G2951 14 HET NAG G3010 14 HET NAG G3011 14 HET BMA G3012 11 HET MAN G3013 11 HET NAG G3014 14 HET MAN G3015 11 HET NAG G3016 14 HET NAG G3320 14 HET NAG G3321 14 HET BMA G3322 11 HET MAN G3323 11 HET MAN G3324 11 HET MAN G3325 11 HET MAN G3326 11 HET MAN G3327 11 HET MAN G3328 11 HET MAN G3329 11 HET NAG G3390 14 HET NAG G3550 14 HET NAG G3551 14 HET NAG G3630 14 HET NAG G3631 14 HET BMA G3632 11 HET MAN G3633 11 HET MAN G3634 11 HET MAN G3635 11 HET MAN G3636 11 HET NAG G3860 14 HET NAG G3861 14 HET BMA G3862 11 HET MAN G3863 11 HET MAN G3864 11 HET FUC G3920 10 HET NAG G3921 14 HET NAG G3922 14 HET BMA G3923 11 HET MAN G3924 11 HET MAN G3925 11 HET NAG G4480 14 HET NAG G4481 14 HET BMA G4482 11 HET MAN G4483 11 HET MAN G4484 11 HETNAM FUC ALPHA-L-FUCOSE HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE HETNAM GAL BETA-D-GALACTOSE HETNAM SIA O-SIALIC ACID FORMUL 7 FUC 7(C6 H12 O5) FORMUL 7 NAG 51(C8 H15 N O6) FORMUL 8 BMA 13(C6 H12 O6) FORMUL 11 MAN 31(C6 H12 O6) FORMUL 11 GAL 9(C6 H12 O6) FORMUL 13 SIA 3(C11 H19 N O9) HELIX 1 AA1 THR B 529 SER B 534 1 6 HELIX 2 AA2 THR B 536 ALA B 541 1 6 HELIX 3 AA3 GLY B 572 GLN B 577 1 6 HELIX 4 AA4 ARG B 579 TRP B 596 1 18 HELIX 5 AA5 THR B 627 SER B 636 1 10 HELIX 6 AA6 TYR B 638 GLU B 648 1 11 HELIX 7 AA7 GLN B 653 LEU B 663 1 11 HELIX 8 AA8 ASN G 99 LYS G 117 1 19 HELIX 9 AA9 THR G 123 CYS G 126 5 4 HELIX 10 AB1 LYS G 335 PHE G 353 1 19 HELIX 11 AB2 ASP G 368 THR G 373 1 6 HELIX 12 AB3 SER G 388 ASN G 392 5 5 HELIX 13 AB4 MET G 475 TYR G 484 1 10 HELIX 14 AB5 PRO H 61 ASN H 64 5 4 HELIX 15 AB6 THR H 83 THR H 87 5 5 HELIX 16 AB7 VAL H 100D GLY H 100H 5 5 HELIX 17 AB8 PRO H 185 LEU H 189 5 5 HELIX 18 AB9 GLU L 79 GLU L 83 5 5 HELIX 19 AC1 GLU L 125 ASN L 129 5 5 HELIX 20 AC2 THR L 182 SER L 188 1 7 HELIX 21 AC3 THR D 83 THR D 87 5 5 HELIX 22 AC4 SER D 156 ALA D 158 5 3 HELIX 23 AC5 GLN E 79 GLU E 83 5 5 HELIX 24 AC6 SER E 122 GLN E 127 1 6 HELIX 25 AC7 THR E 182 HIS E 189 1 8 SHEET 1 AA1 2 THR G 37 TYR G 39 0 SHEET 2 AA1 2 GLY G 495 ALA G 497 -1 O GLY G 495 N TYR G 39 SHEET 1 AA2 5 TRP G 45 LYS G 46 0 SHEET 2 AA2 5 VAL G 488 ILE G 491 -1 O LYS G 490 N LYS G 46 SHEET 3 AA2 5 PHE G 223 CYS G 228 -1 N ALA G 224 O VAL G 489 SHEET 4 AA2 5 VAL G 242 VAL G 245 -1 O SER G 243 N LYS G 227 SHEET 5 AA2 5 GLU G 83 HIS G 85 -1 N ILE G 84 O THR G 244 SHEET 1 AA3 2 GLU G 91 GLU G 92 0 SHEET 2 AA3 2 PRO G 238 CYS G 239 -1 O CYS G 239 N GLU G 91 SHEET 1 AA4 4 VAL G 120 LYS G 121 0 SHEET 2 AA4 4 ALA G 200 GLN G 203 -1 O GLN G 203 N VAL G 120 SHEET 3 AA4 4 GLN G 432 TYR G 435 1 O ALA G 433 N ALA G 200 SHEET 4 AA4 4 ILE G 423 ILE G 424 -1 N ILE G 424 O MET G 434 SHEET 1 AA5 3 LEU G 129 GLN G 130 0 SHEET 2 AA5 3 GLU G 190 LEU G 193 -1 O TYR G 191 N LEU G 129 SHEET 3 AA5 3 VAL G 181 ILE G 184 -1 N VAL G 182 O ARG G 192 SHEET 1 AA6 2 LEU G 154 THR G 162 0 SHEET 2 AA6 2 LYS G 169 TYR G 177 -1 O GLN G 170 N MET G 161 SHEET 1 AA7 7 LEU G 260 LEU G 261 0 SHEET 2 AA7 7 ILE G 443 ARG G 456 -1 O GLY G 451 N LEU G 260 SHEET 3 AA7 7 ILE G 284 ARG G 298 -1 N ARG G 298 O ILE G 443 SHEET 4 AA7 7 HIS G 330 SER G 334 -1 O HIS G 330 N THR G 297 SHEET 5 AA7 7 SER G 413 ILE G 420 -1 O ILE G 414 N VAL G 333 SHEET 6 AA7 7 GLU G 381 CYS G 385 -1 N TYR G 384 O ARG G 419 SHEET 7 AA7 7 HIS G 374 CYS G 378 -1 N CYS G 378 O GLU G 381 SHEET 1 AA8 6 MET G 271 SER G 274 0 SHEET 2 AA8 6 ILE G 284 ARG G 298 -1 O LEU G 285 N ARG G 273 SHEET 3 AA8 6 ILE G 443 ARG G 456 -1 O ILE G 443 N ARG G 298 SHEET 4 AA8 6 GLU G 466 ARG G 469 -1 O ARG G 469 N THR G 455 SHEET 5 AA8 6 ILE G 359 PHE G 361 1 N ARG G 360 O GLU G 466 SHEET 6 AA8 6 SER G 393 TRP G 395 -1 O TRP G 395 N ILE G 359 SHEET 1 AA9 2 ARG G 304 ILE G 307 0 SHEET 2 AA9 2 PHE G 317 THR G 320 -1 O ALA G 319 N LYS G 305 SHEET 1 AB1 4 GLN H 3 GLN H 5 0 SHEET 2 AB1 4 LEU H 18 SER H 25 -1 O SER H 23 N GLN H 5 SHEET 3 AB1 4 GLN H 77 LEU H 82 -1 O LEU H 82 N LEU H 18 SHEET 4 AB1 4 VAL H 67 ASP H 72 -1 N SER H 70 O SER H 79 SHEET 1 AB2 6 LEU H 11 VAL H 12 0 SHEET 2 AB2 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AB2 6 ALA H 88 TYR H 90 -1 N ALA H 88 O VAL H 109 SHEET 4 AB2 6 TYR H 33 GLN H 39 -1 N GLN H 39 O VAL H 89 SHEET 5 AB2 6 LEU H 45 ILE H 51 -1 O ILE H 51 N TRP H 34 SHEET 6 AB2 6 ALA H 57 TYR H 59 -1 O THR H 58 N TYR H 50 SHEET 1 AB3 6 LEU H 11 VAL H 12 0 SHEET 2 AB3 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AB3 6 ALA H 88 TYR H 90 -1 N ALA H 88 O VAL H 109 SHEET 4 AB3 6 TYR H 33 GLN H 39 -1 N GLN H 39 O VAL H 89 SHEET 5 AB3 6 ALA H 93 ILE H 100A-1 O ALA H 95 N TYR H 33 SHEET 6 AB3 6 PHE H 100J SER H 100O-1 O TYR H 100M N GLY H 98 SHEET 1 AB4 4 SER H 120 PHE H 122 0 SHEET 2 AB4 4 ALA H 137 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AB4 4 TYR H 176 THR H 183 -1 O LEU H 178 N VAL H 142 SHEET 4 AB4 4 HIS H 164 LEU H 170 -1 N HIS H 164 O VAL H 181 SHEET 1 AB5 3 VAL H 150 TRP H 154 0 SHEET 2 AB5 3 TYR H 194 HIS H 200 -1 O ASN H 199 N THR H 151 SHEET 3 AB5 3 THR H 205 VAL H 207 -1 O VAL H 207 N VAL H 198 SHEET 1 AB6 3 VAL H 150 TRP H 154 0 SHEET 2 AB6 3 TYR H 194 HIS H 200 -1 O ASN H 199 N THR H 151 SHEET 3 AB6 3 ARG H 210 VAL H 211 -1 O VAL H 211 N TYR H 194 SHEET 1 AB7 5 ARG L 9 VAL L 13 0 SHEET 2 AB7 5 THR L 102 VAL L 106 1 O THR L 105 N LEU L 11 SHEET 3 AB7 5 ASP L 85 ASP L 92 -1 N TYR L 86 O THR L 102 SHEET 4 AB7 5 ARG L 31 HIS L 38 -1 N ALA L 32 O TRP L 91 SHEET 5 AB7 5 ILE L 45 ILE L 48 -1 O ILE L 48 N TRP L 35 SHEET 1 AB8 3 THR L 18 SER L 22 0 SHEET 2 AB8 3 THR L 72 SER L 76 -1 O ILE L 75 N ALA L 19 SHEET 3 AB8 3 PHE L 62 SER L 63 -1 N SER L 63 O THR L 74 SHEET 1 AB9 4 SER L 115 PHE L 119 0 SHEET 2 AB9 4 ALA L 131 PHE L 140 -1 O SER L 138 N SER L 115 SHEET 3 AB9 4 TYR L 173 LEU L 181 -1 O ALA L 175 N ILE L 137 SHEET 4 AB9 4 VAL L 160 THR L 162 -1 N GLU L 161 O TYR L 178 SHEET 1 AC1 4 SER L 115 PHE L 119 0 SHEET 2 AC1 4 ALA L 131 PHE L 140 -1 O SER L 138 N SER L 115 SHEET 3 AC1 4 TYR L 173 LEU L 181 -1 O ALA L 175 N ILE L 137 SHEET 4 AC1 4 SER L 166 LYS L 167 -1 N SER L 166 O ALA L 174 SHEET 1 AC2 4 SER L 154 VAL L 156 0 SHEET 2 AC2 4 THR L 146 ALA L 151 -1 N ALA L 151 O SER L 154 SHEET 3 AC2 4 TYR L 192 HIS L 198 -1 O GLN L 195 N ALA L 148 SHEET 4 AC2 4 SER L 201 VAL L 207 -1 O SER L 201 N HIS L 198 SHEET 1 AC3 4 GLN D 3 GLU D 6 0 SHEET 2 AC3 4 VAL D 18 SER D 25 -1 O THR D 23 N VAL D 5 SHEET 3 AC3 4 ILE D 77 LEU D 82 -1 O MET D 80 N VAL D 20 SHEET 4 AC3 4 VAL D 67 ASP D 72 -1 N THR D 70 O TYR D 79 SHEET 1 AC4 6 GLN D 10 LYS D 12 0 SHEET 2 AC4 6 THR D 107 VAL D 111 1 O THR D 110 N LYS D 12 SHEET 3 AC4 6 ALA D 88 ARG D 94 -1 N TYR D 90 O THR D 107 SHEET 4 AC4 6 MET D 34 GLN D 39 -1 N HIS D 35 O ALA D 93 SHEET 5 AC4 6 GLU D 46 ILE D 51 -1 O MET D 48 N TRP D 36 SHEET 6 AC4 6 VAL D 57 LYS D 58 -1 O LYS D 58 N TRP D 50 SHEET 1 AC5 4 SER D 120 LEU D 124 0 SHEET 2 AC5 4 THR D 135 TYR D 145 -1 O GLY D 139 N LEU D 124 SHEET 3 AC5 4 TYR D 176 PRO D 185 -1 O VAL D 184 N ALA D 136 SHEET 4 AC5 4 HIS D 164 THR D 165 -1 N HIS D 164 O VAL D 181 SHEET 1 AC6 3 VAL D 152 TRP D 154 0 SHEET 2 AC6 3 TYR D 194 VAL D 198 -1 O ASN D 197 N SER D 153 SHEET 3 AC6 3 LYS D 209 VAL D 211 -1 O VAL D 211 N TYR D 194 SHEET 1 AC7 5 SER E 9 GLY E 13 0 SHEET 2 AC7 5 THR E 102 VAL E 106 1 O LYS E 103 N VAL E 11 SHEET 3 AC7 5 HIS E 85 TYR E 89 -1 N TYR E 86 O THR E 102 SHEET 4 AC7 5 SER E 34 GLN E 38 -1 N SER E 34 O TYR E 89 SHEET 5 AC7 5 PRO E 44 ILE E 48 -1 O LYS E 45 N GLN E 37 SHEET 1 AC8 3 ILE E 19 ALA E 24 0 SHEET 2 AC8 3 THR E 70 ILE E 75 -1 O ALA E 71 N CYS E 23 SHEET 3 AC8 3 PHE E 62 SER E 67 -1 N SER E 67 O THR E 70 SHEET 1 AC9 4 SER E 115 PHE E 119 0 SHEET 2 AC9 4 ALA E 131 SER E 138 -1 O LEU E 136 N THR E 117 SHEET 3 AC9 4 TYR E 173 LEU E 181 -1 O LEU E 181 N ALA E 131 SHEET 4 AC9 4 VAL E 160 THR E 162 -1 N GLU E 161 O TYR E 178 SHEET 1 AD1 4 SER E 115 PHE E 119 0 SHEET 2 AD1 4 ALA E 131 SER E 138 -1 O LEU E 136 N THR E 117 SHEET 3 AD1 4 TYR E 173 LEU E 181 -1 O LEU E 181 N ALA E 131 SHEET 4 AD1 4 SER E 166 LYS E 167 -1 N SER E 166 O ALA E 174 SHEET 1 AD2 3 THR E 146 ALA E 151 0 SHEET 2 AD2 3 TYR E 192 HIS E 198 -1 O SER E 193 N LYS E 150 SHEET 3 AD2 3 SER E 201 VAL E 207 -1 O VAL E 203 N VAL E 196 SSBOND 1 CYS B 598 CYS B 604 1555 1555 2.02 SSBOND 2 CYS B 605 CYS G 501 1555 1555 2.03 SSBOND 3 CYS G 54 CYS G 74 1555 1555 2.03 SSBOND 4 CYS G 119 CYS G 205 1555 1555 2.03 SSBOND 5 CYS G 126 CYS G 196 1555 1555 2.03 SSBOND 6 CYS G 131 CYS G 157 1555 1555 2.03 SSBOND 7 CYS G 218 CYS G 247 1555 1555 2.03 SSBOND 8 CYS G 228 CYS G 239 1555 1555 2.03 SSBOND 9 CYS G 296 CYS G 331 1555 1555 2.03 SSBOND 10 CYS G 378 CYS G 445 1555 1555 2.03 SSBOND 11 CYS G 385 CYS G 418 1555 1555 2.03 SSBOND 12 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 13 CYS H 140 CYS H 196 1555 1555 2.03 SSBOND 14 CYS H 216 CYS L 212 1555 1555 2.03 SSBOND 15 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 16 CYS L 135 CYS L 194 1555 1555 2.03 SSBOND 17 CYS D 22 CYS D 92 1555 1555 2.04 SSBOND 18 CYS E 23 CYS E 88 1555 1555 2.03 SSBOND 19 CYS E 135 CYS E 194 1555 1555 2.04 LINK ND2 ASN B 611 C1 NAG B6111 1555 1555 1.44 LINK ND2 ASN B 637 C1 NAG B6371 1555 1555 1.44 LINK ND2 ASN G 88 C1 NAG G 881 1555 1555 1.44 LINK ND2 ASN G 133 C1 NAG G1330 1555 1555 1.46 LINK ND2 ASN G 156 C1 NAG G1561 1555 1555 1.45 LINK ND2 ASN G 160 C1 NAG G1601 1555 1555 1.45 LINK ND2 ASN G 197 C1 NAG G1970 1555 1555 1.43 LINK ND2 ASN G 234 C1 NAG G2340 1555 1555 1.44 LINK ND2 ASN G 262 C1 NAG G2620 1555 1555 1.44 LINK ND2 ASN G 276 C1 NAG G2761 1555 1555 1.44 LINK ND2 ASN G 295 C1 NAG G2950 1555 1555 1.44 LINK ND2 ASN G 301 C1 NAG G3010 1555 1555 1.45 LINK ND2 ASN G 332 C1 NAG G3320 1555 1555 1.44 LINK ND2 ASN G 339 C1 NAG G3390 1555 1555 1.45 LINK ND2 ASN G 355 C1 NAG G3550 1555 1555 1.45 LINK ND2 ASN G 363 C1 NAG G3630 1555 1555 1.45 LINK ND2 ASN G 386 C1 NAG G3860 1555 1555 1.44 LINK ND2 ASN G 392 C1 NAG G3921 1555 1555 1.45 LINK ND2 ASN G 448 C1 NAG G4480 1555 1555 1.44 LINK C1 FUC B6110 O6 NAG B6111 1555 1555 1.45 LINK C1 FUC B6370 O6 NAG B6371 1555 1555 1.44 LINK O4 NAG B6371 C1 NAG B6372 1555 1555 1.44 LINK O4 NAG B6372 C1 BMA B6373 1555 1555 1.44 LINK C1 FUC G 880 O6 NAG G 881 1555 1555 1.45 LINK O4 NAG G 881 C1 NAG G 882 1555 1555 1.44 LINK O4 NAG G1330 C1 NAG G1331 1555 1555 1.45 LINK O4 NAG G1331 C1 BMA G1332 1555 1555 1.45 LINK C1 FUC G1560 O6 NAG G1561 1555 1555 1.45 LINK O4 NAG G1561 C1 NAG G1562 1555 1555 1.45 LINK O4 NAG G1562 C1 BMA G1563 1555 1555 1.44 LINK O3 BMA G1563 C1 MAN G1564 1555 1555 1.44 LINK O6 BMA G1563 C1 MAN G1568 1555 1555 1.44 LINK O2 MAN G1564 C1 NAG G1565 1555 1555 1.46 LINK O4 MAN G1564 C1 NAG G1566 1555 1555 1.44 LINK O4 NAG G1566 C1 GAL G1567 1555 1555 1.44 LINK O2 MAN G1568 C1 NAG G1571 1555 1555 1.44 LINK O4 MAN G1568 C1 NAG G1569 1555 1555 1.45 LINK O4 NAG G1569 C1 GAL G1570 1555 1555 1.44 LINK O4 NAG G1571 C1 GAL G1572 1555 1555 1.44 LINK C1 FUC G1600 O6 NAG G1601 1555 1555 1.45 LINK O4 NAG G1601 C1 NAG G1602 1555 1555 1.46 LINK O4 NAG G1602 C1 BMA G1603 1555 1555 1.45 LINK O3 BMA G1603 C1 MAN G1604 1555 1555 1.44 LINK O6 BMA G1603 C1 MAN G1607 1555 1555 1.44 LINK O2 MAN G1604 C1 NAG G1605 1555 1555 1.45 LINK O4 NAG G1605 C1 GAL G1606 1555 1555 1.44 LINK O2 MAN G1607 C1 NAG G1608 1555 1555 1.44 LINK O4 NAG G1608 C1 GAL G1609 1555 1555 1.44 LINK O4 NAG G1970 C1 NAG G1971 1555 1555 1.48 LINK O4 NAG G1971 C1 BMA G1972 1555 1555 1.48 LINK O3 BMA G1972 C1 MAN G1973 1555 1555 1.44 LINK O6 BMA G1972 C1 MAN G1977 1555 1555 1.44 LINK O2 MAN G1973 C1 NAG G1974 1555 1555 1.45 LINK O4 NAG G1974 C1 GAL G1975 1555 1555 1.44 LINK O6 GAL G1975 C2 SIA G1976 1555 1555 1.38 LINK O2 MAN G1977 C1 NAG G1978 1555 1555 1.44 LINK O4 NAG G2340 C1 NAG G2341 1555 1555 1.44 LINK O4 NAG G2620 C1 NAG G2621 1555 1555 1.44 LINK O4 NAG G2621 C1 BMA G2622 1555 1555 1.44 LINK O3 BMA G2622 C1 MAN G2625 1555 1555 1.44 LINK O6 BMA G2622 C1 MAN G2623 1555 1555 1.44 LINK O6 MAN G2623 C1 MAN G2624 1555 1555 1.43 LINK O2 MAN G2625 C1 MAN G2626 1555 1555 1.45 LINK C1 FUC G2760 O6 NAG G2761 1555 1555 1.44 LINK O4 NAG G2761 C1 NAG G2762 1555 1555 1.44 LINK O4 NAG G2762 C1 BMA G2763 1555 1555 1.43 LINK O3 BMA G2763 C1 MAN G2764 1555 1555 1.45 LINK O4 BMA G2763 C1 NAG G2775 1555 1555 1.45 LINK O6 BMA G2763 C1 MAN G2769 1555 1555 1.43 LINK O2 MAN G2764 C1 NAG G2765 1555 1555 1.44 LINK O4 MAN G2764 C1 NAG G2768 1555 1555 1.44 LINK O4 NAG G2765 C1 GAL G2766 1555 1555 1.44 LINK O6 GAL G2766 C2 SIA G2767 1555 1555 1.37 LINK O2 MAN G2769 C1 NAG G2770 1555 1555 1.44 LINK O4 MAN G2769 C1 NAG G2773 1555 1555 1.45 LINK O4 NAG G2770 C1 GAL G2771 1555 1555 1.45 LINK O6 GAL G2771 C2 SIA G2772 1555 1555 1.38 LINK O4 NAG G2773 C1 GAL G2774 1555 1555 1.44 LINK O4 NAG G2950 C1 NAG G2951 1555 1555 1.44 LINK O4 NAG G3010 C1 NAG G3011 1555 1555 1.45 LINK O4 NAG G3011 C1 BMA G3012 1555 1555 1.45 LINK O3 BMA G3012 C1 MAN G3013 1555 1555 1.44 LINK O6 BMA G3012 C1 MAN G3015 1555 1555 1.44 LINK O2 MAN G3013 C1 NAG G3014 1555 1555 1.44 LINK O2 MAN G3015 C1 NAG G3016 1555 1555 1.44 LINK O4 NAG G3320 C1 NAG G3321 1555 1555 1.44 LINK O4 NAG G3321 C1 BMA G3322 1555 1555 1.43 LINK O3 BMA G3322 C1 MAN G3327 1555 1555 1.44 LINK O6 BMA G3322 C1 MAN G3323 1555 1555 1.43 LINK O3 MAN G3323 C1 MAN G3326 1555 1555 1.45 LINK O6 MAN G3323 C1 MAN G3324 1555 1555 1.44 LINK O2 MAN G3324 C1 MAN G3325 1555 1555 1.44 LINK O2 MAN G3327 C1 MAN G3328 1555 1555 1.45 LINK O2 MAN G3328 C1 MAN G3329 1555 1555 1.44 LINK O4 NAG G3550 C1 NAG G3551 1555 1555 1.44 LINK O4 NAG G3630 C1 NAG G3631 1555 1555 1.45 LINK O4 NAG G3631 C1 BMA G3632 1555 1555 1.45 LINK O3 BMA G3632 C1 MAN G3636 1555 1555 1.45 LINK O6 BMA G3632 C1 MAN G3633 1555 1555 1.45 LINK O3 MAN G3633 C1 MAN G3635 1555 1555 1.45 LINK O6 MAN G3633 C1 MAN G3634 1555 1555 1.44 LINK O4 NAG G3860 C1 NAG G3861 1555 1555 1.48 LINK O4 NAG G3861 C1 BMA G3862 1555 1555 1.43 LINK O3 BMA G3862 C1 MAN G3864 1555 1555 1.45 LINK O6 BMA G3862 C1 MAN G3863 1555 1555 1.44 LINK C1 FUC G3920 O6 NAG G3921 1555 1555 1.45 LINK O4 NAG G3921 C1 NAG G3922 1555 1555 1.44 LINK O4 NAG G3922 C1 BMA G3923 1555 1555 1.47 LINK O3 BMA G3923 C1 MAN G3924 1555 1555 1.44 LINK O6 BMA G3923 C1 MAN G3925 1555 1555 1.45 LINK O4 NAG G4480 C1 NAG G4481 1555 1555 1.47 LINK O4 NAG G4481 C1 BMA G4482 1555 1555 1.45 LINK O6 BMA G4482 C1 MAN G4483 1555 1555 1.44 LINK O3 MAN G4483 C1 MAN G4484 1555 1555 1.44 CISPEP 1 GLY G 312 PRO G 313 0 12.23 CISPEP 2 PHE H 146 PRO H 147 0 -18.00 CISPEP 3 GLU H 148 PRO H 149 0 -8.84 CISPEP 4 TYR L 141 PRO L 142 0 -2.35 CISPEP 5 SER D 100D PRO D 100E 0 -18.56 CISPEP 6 PHE D 146 PRO D 147 0 -4.50 CISPEP 7 GLU D 148 PRO D 149 0 -13.15 CISPEP 8 TYR E 141 PRO E 142 0 -8.66 SITE 1 AC1 4 ASN B 611 SER B 613 TYR B 638 ILE B 641 SITE 1 AC2 1 ASN B 637 SITE 1 AC3 5 THR B 529 ASP B 624 ASN B 625 GLU G 87 SITE 2 AC3 5 ASN G 88 SITE 1 AC4 5 ASN G 133 ASP G 140 GLY G 152 ARG G 178 SITE 2 AC4 5 LYS G 189 SITE 1 AC5 4 THR G 135 ASN G 156 TYR G 173 ASP G 321A SITE 1 AC6 3 GLN G 130 SER G 158 ASN G 160 SITE 1 AC7 6 ASP D 72 MET D 75 TYR D 79 ARG G 192 SITE 2 AC7 6 ASN G 197 ARG G 308 SITE 1 AC8 4 GLU G 92 ASN G 234 THR G 236 PRO G 238 SITE 1 AC9 9 GLU D 1 GLU G 211 PRO G 212 ASN G 262 SITE 2 AC9 9 GLY G 379 ILE G 439 CYS G 445 VAL G 446 SITE 3 AC9 9 SER G 447 SITE 1 AD1 5 GLY E 29 ASP E 31 ASN G 276 THR G 278 SITE 2 AD1 5 ASN G 279 SITE 1 AD2 2 ASN G 295 ARG G 444 SITE 1 AD3 6 GLN D 105 ASN G 301 GLN G 440 GLY G 441 SITE 2 AD3 6 GLY L 68 THR L 69 SITE 1 AD4 21 THR G 297 ASN G 332 ARG H 96 ARG H 97 SITE 2 AD4 21 GLN H 99 ARG H 100 ILE H 100A TYR H 100B SITE 3 AD4 21 GLY H 100C VAL H 100D TYR H 100M ILE H 195 SITE 4 AD4 21 ASP H 208 ARG H 210 SER L 30 ASN L 50 SITE 5 AD4 21 ASN L 51 GLN L 52 PRO L 66 ASP L 66A SITE 6 AD4 21 ASN L 66C SITE 1 AD5 1 ASN G 339 SITE 1 AD6 1 ASN G 355 SITE 1 AD7 6 ARG D 82B ASN G 363 ASN G 386 SER G 388 SITE 2 AD7 6 NAG G3860 NAG G3861 SITE 1 AD8 4 ASN G 386 SER G 388 NAG G3630 NAG G3631 SITE 1 AD9 1 ASN G 392 SITE 1 AE1 4 PRO G 291 GLN G 293 ASN G 448 ARG L 190 CRYST1 217.509 217.509 156.009 90.00 90.00 120.00 H 3 9 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 0.004598 0.002654 0.000000 0.00000 SCALE2 0.000000 0.005309 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006410 0.00000