HEADER VIRAL PROTEIN 08-MAR-16 5FYL TITLE CRYSTAL STRUCTURE AT 3.7 A RESOLUTION OF FULLY GLYCOSYLATED HIV-1 TITLE 2 CLADE A BG505 SOSIP.664 PREFUSION ENV TRIMER IN COMPLEX WITH BROADLY TITLE 3 NEUTRALIZING ANTIBODIES PGT122 AND 35O22 COMPND MOL_ID: 1; COMPND 2 MOLECULE: BG505 GP120 ENV ECTODOMAIN; COMPND 3 CHAIN: B; COMPND 4 FRAGMENT: GP120 ENV ECTODOMAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: 35O22 ANTIBODY FAB HEAVY CHAIN; COMPND 9 CHAIN: D; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: 35O22 ANTIBODY FAB LIGHT CHAIN; COMPND 13 CHAIN: E; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: BG505 GP120 ENV ECTODOMAIN; COMPND 17 CHAIN: G; COMPND 18 FRAGMENT: GP120 ENV ECTODOMAIN; COMPND 19 ENGINEERED: YES; COMPND 20 MUTATION: YES; COMPND 21 MOL_ID: 5; COMPND 22 MOLECULE: PGT122 ANTIBODY FAB HEAVY CHAIN; COMPND 23 CHAIN: H; COMPND 24 ENGINEERED: YES; COMPND 25 MOL_ID: 6; COMPND 26 MOLECULE: PGT122 ANTIBODY FAB LIGHT CHAIN; COMPND 27 CHAIN: L; COMPND 28 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_TAXID: 11676; SOURCE 4 CELL: T-CELL; SOURCE 5 GENE: ENV; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK-293T GNTI-; SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PVRC8400; SOURCE 12 MOL_ID: 2; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_COMMON: HUMAN; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 CELL: B-CELL; SOURCE 17 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 18 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 20 EXPRESSION_SYSTEM_CELL_LINE: HEK-293T; SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PVRC8400; SOURCE 23 MOL_ID: 3; SOURCE 24 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 25 ORGANISM_COMMON: HUMAN; SOURCE 26 ORGANISM_TAXID: 9606; SOURCE 27 CELL: B-CELL; SOURCE 28 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 29 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 30 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 31 EXPRESSION_SYSTEM_CELL_LINE: HEK-293T; SOURCE 32 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 33 EXPRESSION_SYSTEM_PLASMID: PVRC8400; SOURCE 34 MOL_ID: 4; SOURCE 35 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 36 ORGANISM_TAXID: 11676; SOURCE 37 CELL: T-CELL; SOURCE 38 GENE: ENV; SOURCE 39 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 40 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 41 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 42 EXPRESSION_SYSTEM_CELL_LINE: HEK-293T GNTI-; SOURCE 43 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 44 EXPRESSION_SYSTEM_PLASMID: PVRC8400; SOURCE 45 MOL_ID: 5; SOURCE 46 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 47 ORGANISM_COMMON: HUMAN; SOURCE 48 ORGANISM_TAXID: 9606; SOURCE 49 CELL: B-CELL; SOURCE 50 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 51 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 52 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 53 EXPRESSION_SYSTEM_CELL_LINE: HEK-293T GNTI-; SOURCE 54 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 55 EXPRESSION_SYSTEM_PLASMID: PVRC8400; SOURCE 56 MOL_ID: 6; SOURCE 57 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 58 ORGANISM_COMMON: HUMAN; SOURCE 59 ORGANISM_TAXID: 9606; SOURCE 60 CELL: B-CELL; SOURCE 61 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 62 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 63 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 64 EXPRESSION_SYSTEM_CELL_LINE: HEK-293T GNTI-; SOURCE 65 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 66 EXPRESSION_SYSTEM_PLASMID: PVRC8400 KEYWDS VIRAL PROTEIN, HIV, ENVELOPE, GLYCAN, TRIMER EXPDTA X-RAY DIFFRACTION AUTHOR G.B.E.STEWART-JONES,T.ZHOU,P.D.KWONG REVDAT 4 18-MAY-16 5FYL 1 JRNL REVDAT 3 11-MAY-16 5FYL 1 JRNL REMARK MASTER REVDAT 2 04-MAY-16 5FYL 1 JRNL REVDAT 1 27-APR-16 5FYL 0 JRNL AUTH G.B.E.STEWART-JONES,C.SOTO,T.LEMMIN,G.Y.CHUANG,A.DRUZ, JRNL AUTH 2 R.KONG,P.V.THOMAS,K.WAGH,T.ZHOU,A.J.BEHRENS,T.BYLUND, JRNL AUTH 3 C.W.CHOI,J.R.DAVISON,I.S.GEORGIEV,M.G.JOYCE,Y.D.KWON, JRNL AUTH 4 M.PANCERA,J.TAFT,Y.YANG,B.ZHANG,S.S.SHIVATARE,V.S.SHIVATARE, JRNL AUTH 5 C.C.D.LEE,C.Y.WU,C.A.BEWLEY,D.R.BURTON,W.C.KOFF,M.CONNORS, JRNL AUTH 6 M.CRISPIN,B.T.KORBER,C.H.WONG,J.R.MASCOLA,P.D.KWONG JRNL TITL TRIMERIC HIV-1-ENV STRUCTURES DEFINE GLYCAN SHIELDS FROM JRNL TITL 2 CLADES A, B AND G JRNL REF CELL(CAMBRIDGE,MASS.) V. 165 813 2016 JRNL REFN ISSN 0092-8674 JRNL PMID 27114034 JRNL DOI 10.1016/J.CELL.2016.04.010 REMARK 2 REMARK 2 RESOLUTION. 3.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692) REMARK 3 AUTHORS : ADAMS,AFONINE,BURNLEY,CHEN,DAVIS,ECHOLS,GILDEA, REMARK 3 : GOPAL,GROS,GROSSE-KUNSTLEVE,HEADD,HUNG,IMMORMINO, REMARK 3 : IOERGER,MCCOY,MCKEE,MORIARTY,PAI,READ,RICHARDSON, REMARK 3 : RICHARDSON,ROMO,SACCHETTINI,SAUTER,SMITH,STORONI, REMARK 3 : TERWILLIGER,ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : TWIN_LSQ_F REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.100 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.998 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.36 REMARK 3 COMPLETENESS FOR RANGE (%) : 58.47 REMARK 3 NUMBER OF REFLECTIONS : 31517 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.2537 REMARK 3 R VALUE (WORKING SET) : 0.2503 REMARK 3 FREE R VALUE : 0.3072 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.4 REMARK 3 FREE R VALUE TEST SET COUNT : 1710 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 32.9447 - 6.8759 0.95 4673 253 0.2388 0.2917 REMARK 3 2 6.8759 - 5.4657 0.95 4649 246 0.2608 0.3341 REMARK 3 3 5.4657 - 4.7772 0.94 4627 241 0.2295 0.2763 REMARK 3 4 4.7772 - 4.3414 0.82 4000 203 0.2264 0.2676 REMARK 3 5 4.3414 - 4.0309 0.69 3381 186 0.2485 0.3197 REMARK 3 6 4.0309 - 3.7936 0.57 2775 152 0.2733 0.3313 REMARK 3 7 3.7936 - 3.6038 0.41 1967 107 0.2963 0.3538 REMARK 3 8 3.6038 - 3.4471 0.29 1425 76 0.2996 0.3600 REMARK 3 9 3.4471 - 3.3145 0.22 1071 61 0.3167 0.3733 REMARK 3 10 3.3145 - 3.2003 0.16 773 38 0.3151 0.3897 REMARK 3 11 3.2003 - 3.1003 0.12 566 31 0.3202 0.3631 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) : 33.29 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.005 13142 REMARK 3 ANGLE : 0.961 18065 REMARK 3 CHIRALITY : 0.036 2366 REMARK 3 PLANARITY : 0.004 2081 REMARK 3 DIHEDRAL : 14.970 5069 REMARK 3 REMARK 3 TLS DETAILS. REMARK 3 NUMBER OF TLS GROUPS: 18 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 518 THROUGH 616 ) REMARK 3 ORIGIN FOR THE GROUP (A): 268.7513 140.3239 19.6222 REMARK 3 T TENSOR REMARK 3 T11: 0.1860 T22: 0.0373 REMARK 3 T33: 0.6790 T12: -0.2009 REMARK 3 T13: 0.0974 T23: -0.0696 REMARK 3 L TENSOR REMARK 3 L11: 1.8427 L22: 2.3358 REMARK 3 L33: 2.8522 L12: -0.7637 REMARK 3 L13: 0.5641 L23: 0.4143 REMARK 3 S TENSOR REMARK 3 S11: 0.0691 S12: -0.3634 S13: -0.1446 REMARK 3 S21: 0.0686 S22: -0.1273 S23: 0.0831 REMARK 3 S31: 0.2309 S32: -0.1633 S33: 0.0751 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 617 THROUGH 664 ) REMARK 3 ORIGIN FOR THE GROUP (A): 262.1578 131.6601 30.7064 REMARK 3 T TENSOR REMARK 3 T11: 1.1710 T22: 0.7711 REMARK 3 T33: 0.7863 T12: -0.0202 REMARK 3 T13: 0.1299 T23: 0.2854 REMARK 3 L TENSOR REMARK 3 L11: 2.4606 L22: 3.4640 REMARK 3 L33: 3.1189 L12: -2.7575 REMARK 3 L13: -1.6624 L23: 1.4415 REMARK 3 S TENSOR REMARK 3 S11: -0.5786 S12: -0.1642 S13: -0.3818 REMARK 3 S21: 0.2170 S22: -0.1219 S23: 0.0150 REMARK 3 S31: 1.1112 S32: -0.3918 S33: 0.4962 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 147 ) REMARK 3 ORIGIN FOR THE GROUP (A): 299.0045 108.0312 30.4378 REMARK 3 T TENSOR REMARK 3 T11: 1.5013 T22: 1.6107 REMARK 3 T33: 1.2886 T12: 0.6401 REMARK 3 T13: 0.2737 T23: 0.5048 REMARK 3 L TENSOR REMARK 3 L11: 0.6880 L22: 3.3048 REMARK 3 L33: 0.4319 L12: 0.5226 REMARK 3 L13: -0.2917 L23: -1.1552 REMARK 3 S TENSOR REMARK 3 S11: -0.1796 S12: 0.0515 S13: -0.5283 REMARK 3 S21: 0.3295 S22: 0.2751 S23: -0.4344 REMARK 3 S31: 0.2262 S32: -0.0532 S33: 0.0210 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 148 THROUGH 224 ) REMARK 3 ORIGIN FOR THE GROUP (A): 293.6429 81.2814 26.7872 REMARK 3 T TENSOR REMARK 3 T11: 2.5874 T22: 1.9616 REMARK 3 T33: 2.2153 T12: 0.0636 REMARK 3 T13: 0.2048 T23: -0.1316 REMARK 3 L TENSOR REMARK 3 L11: 0.1173 L22: 1.0233 REMARK 3 L33: 1.5432 L12: -0.3450 REMARK 3 L13: 0.4248 L23: -1.2562 REMARK 3 S TENSOR REMARK 3 S11: 0.0927 S12: 0.2029 S13: -0.0290 REMARK 3 S21: 0.0415 S22: -0.2183 S23: 0.2440 REMARK 3 S31: 0.0507 S32: -0.2035 S33: 0.0875 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 2 THROUGH 102 ) REMARK 3 ORIGIN FOR THE GROUP (A): 286.6452 112.8594 48.9389 REMARK 3 T TENSOR REMARK 3 T11: 1.9951 T22: 1.6239 REMARK 3 T33: 1.2836 T12: 0.4449 REMARK 3 T13: 0.1565 T23: 0.6540 REMARK 3 L TENSOR REMARK 3 L11: 3.1343 L22: 3.7169 REMARK 3 L33: 1.5156 L12: 2.0138 REMARK 3 L13: -1.3553 L23: -2.3729 REMARK 3 S TENSOR REMARK 3 S11: -0.0850 S12: -0.0428 S13: -0.4440 REMARK 3 S21: 0.6414 S22: 0.1994 S23: 0.0963 REMARK 3 S31: 0.0629 S32: 0.1995 S33: -0.1636 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 103 THROUGH 148 ) REMARK 3 ORIGIN FOR THE GROUP (A): 293.1762 80.2328 41.7749 REMARK 3 T TENSOR REMARK 3 T11: 2.1965 T22: 1.5917 REMARK 3 T33: 1.7382 T12: 0.1959 REMARK 3 T13: 0.2787 T23: 0.2228 REMARK 3 L TENSOR REMARK 3 L11: 0.8715 L22: 0.5883 REMARK 3 L33: 3.4982 L12: 0.7157 REMARK 3 L13: -1.7464 L23: -1.4350 REMARK 3 S TENSOR REMARK 3 S11: -0.1007 S12: 0.0455 S13: -0.0896 REMARK 3 S21: 0.3182 S22: 0.0082 S23: 0.1847 REMARK 3 S31: -0.0422 S32: 0.2638 S33: 0.0781 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 149 THROUGH 210 ) REMARK 3 ORIGIN FOR THE GROUP (A): 298.2068 74.5971 44.7465 REMARK 3 T TENSOR REMARK 3 T11: 2.3058 T22: 1.8803 REMARK 3 T33: 2.2349 T12: 0.3241 REMARK 3 T13: 0.2027 T23: 0.1853 REMARK 3 L TENSOR REMARK 3 L11: 0.3442 L22: 1.8500 REMARK 3 L33: 0.3048 L12: 0.7950 REMARK 3 L13: -0.3173 L23: -0.7471 REMARK 3 S TENSOR REMARK 3 S11: 0.0345 S12: 0.1268 S13: -0.4733 REMARK 3 S21: 0.1844 S22: -0.0930 S23: 0.2032 REMARK 3 S31: -0.1442 S32: -0.2796 S33: 0.0393 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 31 THROUGH 77 ) REMARK 3 ORIGIN FOR THE GROUP (A): 274.9867 144.3145 6.3142 REMARK 3 T TENSOR REMARK 3 T11: 0.5007 T22: 0.3977 REMARK 3 T33: 0.9992 T12: -0.0420 REMARK 3 T13: 0.1756 T23: 0.2881 REMARK 3 L TENSOR REMARK 3 L11: 4.4049 L22: 1.6859 REMARK 3 L33: 1.6524 L12: -0.2434 REMARK 3 L13: -1.2723 L23: 1.5386 REMARK 3 S TENSOR REMARK 3 S11: 0.2631 S12: 0.4305 S13: 0.6285 REMARK 3 S21: -0.5549 S22: -0.3594 S23: 0.0097 REMARK 3 S31: -0.5418 S32: 0.5461 S33: -0.0195 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 78 THROUGH 255 ) REMARK 3 ORIGIN FOR THE GROUP (A): 279.8319 140.9089 -20.4745 REMARK 3 T TENSOR REMARK 3 T11: 0.1942 T22: 0.0908 REMARK 3 T33: 0.7751 T12: 0.4927 REMARK 3 T13: 0.2535 T23: 0.2048 REMARK 3 L TENSOR REMARK 3 L11: 1.1232 L22: 0.9489 REMARK 3 L33: 0.4396 L12: -0.3880 REMARK 3 L13: 0.3023 L23: -0.6629 REMARK 3 S TENSOR REMARK 3 S11: -0.0115 S12: 0.4161 S13: -0.0559 REMARK 3 S21: -0.3287 S22: -0.0471 S23: -0.2385 REMARK 3 S31: 0.4520 S32: 0.3177 S33: 0.1730 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 256 THROUGH 505 ) REMARK 3 ORIGIN FOR THE GROUP (A): 289.5202 132.7474 -16.1030 REMARK 3 T TENSOR REMARK 3 T11: 0.0620 T22: 0.3225 REMARK 3 T33: 1.0302 T12: 0.5295 REMARK 3 T13: 0.4843 T23: 0.3361 REMARK 3 L TENSOR REMARK 3 L11: 0.6822 L22: 0.0017 REMARK 3 L33: 1.9338 L12: 0.0742 REMARK 3 L13: -0.6962 L23: -0.1831 REMARK 3 S TENSOR REMARK 3 S11: -0.1220 S12: 0.0497 S13: -0.3365 REMARK 3 S21: -0.0632 S22: -0.0444 S23: -0.2483 REMARK 3 S31: 0.6655 S32: 0.7010 S33: 0.4563 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 32 ) REMARK 3 ORIGIN FOR THE GROUP (A): 323.8429 139.3396 -69.4449 REMARK 3 T TENSOR REMARK 3 T11: 1.5920 T22: 1.6688 REMARK 3 T33: 1.3403 T12: 0.3743 REMARK 3 T13: 0.7827 T23: -0.0883 REMARK 3 L TENSOR REMARK 3 L11: 2.0126 L22: 1.6519 REMARK 3 L33: 5.7893 L12: 0.2474 REMARK 3 L13: -1.2066 L23: 0.0637 REMARK 3 S TENSOR REMARK 3 S11: 0.0371 S12: 0.1440 S13: -0.5431 REMARK 3 S21: -0.5547 S22: 0.1024 S23: -0.6065 REMARK 3 S31: 0.0557 S32: 0.9105 S33: -0.1403 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 33 THROUGH 72 ) REMARK 3 ORIGIN FOR THE GROUP (A): 313.3121 139.4851 -64.2419 REMARK 3 T TENSOR REMARK 3 T11: 1.5282 T22: 1.0095 REMARK 3 T33: 1.0525 T12: 0.3052 REMARK 3 T13: 0.7320 T23: 0.2231 REMARK 3 L TENSOR REMARK 3 L11: 5.9816 L22: 6.8609 REMARK 3 L33: 9.4853 L12: 1.9618 REMARK 3 L13: -3.5420 L23: -0.5093 REMARK 3 S TENSOR REMARK 3 S11: -0.1926 S12: 0.0214 S13: -0.6117 REMARK 3 S21: 0.3087 S22: -0.0310 S23: 0.0998 REMARK 3 S31: 0.8860 S32: 0.8314 S33: 0.2009 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 73 THROUGH 101 ) REMARK 3 ORIGIN FOR THE GROUP (A): 315.0595 141.0194 -57.4113 REMARK 3 T TENSOR REMARK 3 T11: 1.2058 T22: 1.3476 REMARK 3 T33: 1.1708 T12: 0.5889 REMARK 3 T13: 0.6149 T23: 0.3355 REMARK 3 L TENSOR REMARK 3 L11: 0.8126 L22: 1.7013 REMARK 3 L33: 5.8873 L12: 0.0335 REMARK 3 L13: -0.5284 L23: 1.7093 REMARK 3 S TENSOR REMARK 3 S11: -0.1099 S12: -0.0435 S13: -0.6933 REMARK 3 S21: -0.6664 S22: 0.3597 S23: -0.6397 REMARK 3 S31: 0.1273 S32: 0.9050 S33: -0.1960 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 102 THROUGH 140 ) REMARK 3 ORIGIN FOR THE GROUP (A): 328.9360 157.2094 -86.5659 REMARK 3 T TENSOR REMARK 3 T11: 1.7264 T22: 1.0165 REMARK 3 T33: 1.4376 T12: 0.4588 REMARK 3 T13: 0.6553 T23: 0.0735 REMARK 3 L TENSOR REMARK 3 L11: 5.5354 L22: 0.4744 REMARK 3 L33: 4.1340 L12: 1.1491 REMARK 3 L13: -0.0023 L23: -0.9894 REMARK 3 S TENSOR REMARK 3 S11: -0.4809 S12: 0.4262 S13: -0.0409 REMARK 3 S21: -0.0659 S22: -0.0422 S23: -0.1874 REMARK 3 S31: 0.6742 S32: 0.3211 S33: 0.5001 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 141 THROUGH 155 ) REMARK 3 ORIGIN FOR THE GROUP (A): 329.7512 154.0587 -84.5107 REMARK 3 T TENSOR REMARK 3 T11: 1.8081 T22: 1.3528 REMARK 3 T33: 1.3839 T12: 0.2525 REMARK 3 T13: 0.4387 T23: 0.4941 REMARK 3 L TENSOR REMARK 3 L11: 7.1636 L22: 2.2846 REMARK 3 L33: 5.0491 L12: -1.1862 REMARK 3 L13: -3.2447 L23: 3.2212 REMARK 3 S TENSOR REMARK 3 S11: -0.1249 S12: 0.3717 S13: -0.8594 REMARK 3 S21: 1.0216 S22: -0.8201 S23: -0.6512 REMARK 3 S31: 0.1103 S32: 0.0760 S33: 0.9420 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 156 THROUGH 211 ) REMARK 3 ORIGIN FOR THE GROUP (A): 335.1499 158.6013 -85.7288 REMARK 3 T TENSOR REMARK 3 T11: 1.2578 T22: 1.4558 REMARK 3 T33: 1.5016 T12: 0.4071 REMARK 3 T13: 0.4307 T23: 0.2299 REMARK 3 L TENSOR REMARK 3 L11: 0.6441 L22: 4.6157 REMARK 3 L33: 0.0468 L12: 0.8172 REMARK 3 L13: -0.0356 L23: 0.3604 REMARK 3 S TENSOR REMARK 3 S11: 0.3011 S12: 0.5472 S13: -0.6619 REMARK 3 S21: 0.6443 S22: -0.4056 S23: -0.9185 REMARK 3 S31: -0.4033 S32: 0.0710 S33: 0.0662 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 6 THROUGH 101 ) REMARK 3 ORIGIN FOR THE GROUP (A): 313.7426 158.5095 -53.4150 REMARK 3 T TENSOR REMARK 3 T11: 0.6893 T22: 1.2325 REMARK 3 T33: 1.0307 T12: 0.0258 REMARK 3 T13: 0.5907 T23: 0.1058 REMARK 3 L TENSOR REMARK 3 L11: 2.0698 L22: 2.1190 REMARK 3 L33: 2.5086 L12: 0.4612 REMARK 3 L13: -1.4911 L23: -0.7558 REMARK 3 S TENSOR REMARK 3 S11: 0.1048 S12: 0.1964 S13: 0.1789 REMARK 3 S21: -0.3379 S22: -0.2081 S23: -0.5703 REMARK 3 S31: -0.2377 S32: 0.5075 S33: 0.0391 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 102 THROUGH 210 ) REMARK 3 ORIGIN FOR THE GROUP (A): 324.8565 172.6044 -87.3391 REMARK 3 T TENSOR REMARK 3 T11: 1.0886 T22: 0.9115 REMARK 3 T33: 1.0801 T12: 0.6413 REMARK 3 T13: 0.3171 T23: 0.2554 REMARK 3 L TENSOR REMARK 3 L11: 2.6294 L22: 5.5886 REMARK 3 L33: 5.9556 L12: 3.2620 REMARK 3 L13: -2.2379 L23: -3.2994 REMARK 3 S TENSOR REMARK 3 S11: -0.2172 S12: -0.0553 S13: -0.0743 REMARK 3 S21: -0.0042 S22: -0.3073 S23: 0.1793 REMARK 3 S31: 0.6471 S32: 0.5281 S33: 0.5190 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 5FYL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-APR-16. REMARK 100 THE PDBE ID CODE IS EBI-66190. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 23-AUG-14 REMARK 200 TEMPERATURE (KELVIN) : 77 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 22-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53617 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.10 REMARK 200 RESOLUTION RANGE LOW (A) : 50.00 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 85.1 REMARK 200 DATA REDUNDANCY : 5.0 REMARK 200 R MERGE (I) : 0.06 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.82 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NONE REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 72.52 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.48 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.18 M LI2SO4, 4.79% PEG 1500, REMARK 280 14.4% ISOPROPANOL, 10 MM YTTRIUM CHLORIDE, 0.09 M SODIUM REMARK 280 ACETATE PH 5.5 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 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,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+1/2 REMARK 290 6555 X-Y,X,Z+1/2 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 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 156.53000 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 156.53000 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 156.53000 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: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PQS REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, B, D, E, H, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 GLN D 225 REMARK 465 GLN E 1 REMARK 465 CYS E 211 REMARK 465 SER E 212 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 186 REMARK 465 THR G 399 REMARK 465 SER G 400 REMARK 465 VAL G 401 REMARK 465 GLN G 402 REMARK 465 GLY G 403 REMARK 465 SER G 404 REMARK 465 ASN G 405 REMARK 465 SER G 406 REMARK 465 THR G 407 REMARK 465 GLY G 408 REMARK 465 SER G 409 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 LYS H 127 REMARK 465 SER H 128 REMARK 465 THR H 129 REMARK 465 SER H 130 REMARK 465 LYS H 212 REMARK 465 SER H 213 REMARK 465 CYS H 214 REMARK 465 ASP H 215 REMARK 465 LYS H 216 REMARK 465 GLY H 217 REMARK 465 LEU H 218 REMARK 465 GLU H 219 REMARK 465 VAL H 220 REMARK 465 LEU H 221 REMARK 465 PHE H 222 REMARK 465 GLN H 223 REMARK 465 GLU L 211 REMARK 465 CYS L 212 REMARK 465 SER L 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 O LYS D 143 OG SER D 177 2.17 REMARK 500 ND2 ASN G 339 O5 NAG G 3391 2.16 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ALA B 525 41.39 -88.70 REMARK 500 LEU B 545 -80.08 -133.66 REMARK 500 TRP B 596 -163.84 -102.41 REMARK 500 CYS B 598 49.55 -101.71 REMARK 500 LYS B 601 -95.90 -134.85 REMARK 500 LEU B 602 -107.76 58.11 REMARK 500 SER B 615 -65.08 -132.76 REMARK 500 ASN B 616 -0.63 78.50 REMARK 500 ASN B 625 -74.21 -135.47 REMARK 500 ALA D 16 -149.86 -121.93 REMARK 500 CYS D 22 109.51 -161.51 REMARK 500 GLN D 39 55.81 -103.62 REMARK 500 MET D 80 99.99 -161.52 REMARK 500 LEU D 96 -72.10 -74.14 REMARK 500 PRO D 100F 103.38 -59.55 REMARK 500 TYR D 101 -61.62 -93.23 REMARK 500 PHE D 146 129.20 -172.13 REMARK 500 VAL D 152 48.27 -145.58 REMARK 500 ALA D 158 -65.22 -99.99 REMARK 500 SER D 177 117.17 -167.35 REMARK 500 LEU D 189 -59.90 -128.83 REMARK 500 ASN D 197 84.17 -64.34 REMARK 500 CYS D 216 -58.59 -133.13 REMARK 500 GLN E 17 -169.30 -119.77 REMARK 500 CYS E 23 63.90 -150.06 REMARK 500 ASP E 51 -49.89 71.48 REMARK 500 SER E 95 -157.83 -77.83 REMARK 500 ALA E 127 -53.04 -132.37 REMARK 500 ALA E 150 97.14 -162.31 REMARK 500 TRP E 185 -67.71 -98.66 REMARK 500 ARG E 189 -73.05 -76.13 REMARK 500 THR E 209 34.91 -152.03 REMARK 500 GLU G 64 -135.83 36.72 REMARK 500 LYS G 65 13.70 55.39 REMARK 500 LEU G 122 38.09 -97.78 REMARK 500 THR G 132 -161.57 -127.52 REMARK 500 THR G 135 110.00 -55.99 REMARK 500 PRO G 220 -176.85 -69.50 REMARK 500 LYS G 232 36.71 -148.43 REMARK 500 THR G 248 -173.94 -69.29 REMARK 500 GLN G 258 -105.56 55.39 REMARK 500 ASN G 262 11.43 51.87 REMARK 500 GLU G 268 -71.88 -122.58 REMARK 500 ARG G 327 -169.70 -112.87 REMARK 500 ASN G 356 60.46 -102.31 REMARK 500 HIS G 374 102.48 -59.77 REMARK 500 ASN G 392 78.09 -166.56 REMARK 500 THR G 394 141.66 -174.33 REMARK 500 ASP G 412 -159.84 -91.14 REMARK 500 ILE G 430 -49.42 -133.61 REMARK 500 REMARK 500 THIS ENTRY HAS 73 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 MONO-SACCHARIDE REMARK 800 NAG B6111 BOUND TO ASN B 611 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE REMARK 800 NAG B6181 BOUND TO ASN B 618 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE REMARK 800 RESIDUES NAG B6371 THROUGH BMA B6373 BOUND TO ASN B 637 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE REMARK 800 RESIDUES NAG G 881 THROUGH MAN G 888 BOUND TO ASN G 88 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE REMARK 800 RESIDUES NAG G1331 THROUGH NAG G1332 BOUND TO ASN G 133 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE REMARK 800 RESIDUES NAG G1371 THROUGH MAN G1378 BOUND TO ASN G 137 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE REMARK 800 RESIDUES NAG G1561 THROUGH MAN G1569B BOUND TO ASN G 156 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE REMARK 800 RESIDUES NAG G1601 THROUGH MAN G1609 BOUND TO ASN G 160 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE REMARK 800 RESIDUES NAG G1971 THROUGH MAN G1977 BOUND TO ASN G 197 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE REMARK 800 RESIDUES NAG G2341 THROUGH MAN G2345 BOUND TO ASN G 234 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE REMARK 800 RESIDUES NAG G2621 THROUGH MAN G2629A BOUND TO ASN G 262 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE REMARK 800 RESIDUES NAG G2761 THROUGH MAN G2765 BOUND TO ASN G 276 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE REMARK 800 RESIDUES NAG G2951 THROUGH MAN G2957 BOUND TO ASN G 295 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE REMARK 800 RESIDUES NAG G3011 THROUGH MAN G3018 BOUND TO ASN G 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE REMARK 800 RESIDUES NAG G3321 THROUGH MAN G3329 BOUND TO ASN G 332 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE REMARK 800 NAG G3391 BOUND TO ASN G 339 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE REMARK 800 NAG G3551 BOUND TO ASN G 355 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE REMARK 800 RESIDUES NAG G3631 THROUGH BMA G3633 BOUND TO ASN G 363 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE REMARK 800 RESIDUES NAG G3861 THROUGH MAN G3866 BOUND TO ASN G 386 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE REMARK 800 RESIDUES NAG G3921 THROUGH MAN G3926 BOUND TO ASN G 392 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE REMARK 800 RESIDUES NAG G4481 THROUGH MAN G4489B BOUND TO ASN G 448 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE REMARK 800 RESIDUES NAG H 231 THROUGH MAN H 234 BOUND TO ASN H 23 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5FYJ RELATED DB: PDB REMARK 900 STRUCTURES OF FULLY GLYCOSYLATED HIV-1-ENV TRIMER FROM REMARK 900 CLADE G REMARK 900 RELATED ID: 5FYK RELATED DB: PDB REMARK 900 STRUCTURES OF FULLY GLYCOSYLATED HIV-1-ENV TRIMER FROM REMARK 900 CLADE B DBREF 5FYL B 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 5FYL D 1 225 PDB 5FYL 5FYL 1 225 DBREF 5FYL E 1 212 PDB 5FYL 5FYL 1 212 DBREF 5FYL G 31 508 UNP Q2N0S6 Q2N0S6_9HIV1 30 505 DBREF 5FYL H 1 223 PDB 5FYL 5FYL 1 223 DBREF 5FYL L 6 213 PDB 5FYL 5FYL 6 213 SEQADV 5FYL PRO B 559 UNP Q2N0S6 ILE 556 ENGINEERED MUTATION SEQADV 5FYL CYS B 605 UNP Q2N0S6 THR 602 ENGINEERED MUTATION SEQADV 5FYL ASN G 332 UNP Q2N0S6 THR 330 ENGINEERED MUTATION SEQADV 5FYL CYS G 501 UNP Q2N0S6 ALA 498 ENGINEERED MUTATION SEQADV 5FYL ARG G 509 UNP Q2N0S6 EXPRESSION TAG SEQADV 5FYL ARG G 510 UNP Q2N0S6 EXPRESSION TAG SEQADV 5FYL ARG G 511 UNP Q2N0S6 EXPRESSION TAG SEQADV 5FYL ARG G 512 UNP Q2N0S6 EXPRESSION TAG SEQADV 5FYL ARG G 513 UNP Q2N0S6 EXPRESSION TAG 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 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 H 244 GLN VAL HIS LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 244 PRO SER GLU THR LEU SER LEU THR CYS ASN VAL SER GLY SEQRES 3 H 244 THR LEU VAL ARG ASP ASN TYR TRP SER TRP ILE ARG GLN SEQRES 4 H 244 PRO LEU GLY LYS GLN PRO GLU TRP ILE GLY TYR VAL HIS SEQRES 5 H 244 ASP SER GLY ASP THR ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 H 244 ARG VAL HIS LEU SER LEU ASP LYS SER LYS ASN LEU VAL SEQRES 7 H 244 SER LEU ARG LEU THR GLY VAL THR ALA ALA ASP SER ALA SEQRES 8 H 244 ILE TYR TYR CYS ALA THR THR LYS HIS GLY ARG ARG ILE SEQRES 9 H 244 TYR GLY VAL VAL ALA PHE LYS GLU TRP PHE THR TYR PHE SEQRES 10 H 244 TYR MET ASP VAL TRP GLY LYS GLY THR SER VAL THR VAL SEQRES 11 H 244 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 12 H 244 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 13 H 244 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 14 H 244 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 15 H 244 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 16 H 244 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 17 H 244 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 18 H 244 SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER SEQRES 19 H 244 CYS ASP LYS GLY LEU GLU VAL LEU PHE GLN SEQRES 1 L 213 ALA PRO THR PHE VAL SER VAL ALA PRO GLY GLN THR ALA SEQRES 2 L 213 ARG ILE THR CYS GLY GLU GLU SER LEU GLY SER ARG SER SEQRES 3 L 213 VAL ILE TRP TYR GLN GLN ARG PRO GLY GLN ALA PRO SER SEQRES 4 L 213 LEU ILE ILE TYR ASN ASN ASN ASP ARG PRO SER GLY ILE SEQRES 5 L 213 PRO ASP ARG PHE SER GLY SER PRO GLY SER THR PHE GLY SEQRES 6 L 213 THR THR ALA THR LEU THR ILE THR SER VAL GLU ALA GLY SEQRES 7 L 213 ASP GLU ALA ASP TYR TYR CYS HIS ILE TRP ASP SER ARG SEQRES 8 L 213 ARG PRO THR ASN TRP VAL PHE GLY GLU GLY THR THR LEU SEQRES 9 L 213 ILE VAL LEU SER GLN PRO LYS ALA ALA PRO SER VAL THR SEQRES 10 L 213 LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN LYS SEQRES 11 L 213 ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY SEQRES 12 L 213 ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO VAL SEQRES 13 L 213 LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SER SEQRES 14 L 213 ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU THR SEQRES 15 L 213 PRO GLU GLN TRP LYS SER HIS LYS SER TYR SER CYS GLN SEQRES 16 L 213 VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL ALA SEQRES 17 L 213 PRO THR GLU CYS SER SEQRES 1 D 243 GLN GLY GLN LEU VAL GLN SER GLY ALA GLU LEU LYS LYS SEQRES 2 D 243 PRO GLY ALA SER VAL LYS ILE SER CYS LYS THR SER GLY SEQRES 3 D 243 TYR ARG PHE ASN PHE TYR HIS ILE ASN TRP ILE ARG GLN SEQRES 4 D 243 THR ALA GLY ARG GLY PRO GLU TRP MET GLY TRP ILE SER SEQRES 5 D 243 PRO TYR SER GLY ASP LYS ASN LEU ALA PRO ALA PHE GLN SEQRES 6 D 243 ASP ARG VAL ILE MET THR THR ASP THR GLU VAL PRO VAL SEQRES 7 D 243 THR SER PHE THR SER THR GLY ALA ALA TYR MET GLU ILE SEQRES 8 D 243 ARG ASN LEU LYS PHE ASP ASP THR GLY THR TYR PHE CYS SEQRES 9 D 243 ALA LYS GLY LEU LEU ARG ASP GLY SER SER THR TRP LEU SEQRES 10 D 243 PRO TYR LEU TRP GLY GLN GLY THR LEU LEU THR VAL SER SEQRES 11 D 243 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 12 D 243 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 13 D 243 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 14 D 243 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 15 D 243 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 16 D 243 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 17 D 243 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 18 D 243 ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS SEQRES 19 D 243 ASP LYS GLY LEU GLU VAL LEU PHE GLN SEQRES 1 E 216 GLN SER VAL LEU THR GLN SER ALA SER VAL SER GLY SER SEQRES 2 E 216 LEU GLY GLN SER VAL THR ILE SER CYS THR GLY PRO ASN SEQRES 3 E 216 SER VAL CYS CYS SER HIS LYS SER ILE SER TRP TYR GLN SEQRES 4 E 216 TRP PRO PRO GLY ARG ALA PRO THR LEU ILE ILE TYR GLU SEQRES 5 E 216 ASP ASN GLU ARG ALA PRO GLY ILE SER PRO ARG PHE SER SEQRES 6 E 216 GLY TYR LYS SER TYR TRP SER ALA TYR LEU THR ILE SER SEQRES 7 E 216 ASP LEU ARG PRO GLU ASP GLU THR THR TYR TYR CYS CYS SEQRES 8 E 216 SER TYR THR HIS ASN SER GLY CYS VAL PHE GLY THR GLY SEQRES 9 E 216 THR LYS VAL SER VAL LEU GLY GLN SER LYS ALA ASN PRO SEQRES 10 E 216 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 E 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 E 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SEQRES 13 E 216 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER SEQRES 14 E 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 E 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SEQRES 16 E 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 E 216 THR VAL ALA PRO THR GLU CYS SER HET NAG B6111 14 HET NAG B6181 14 HET NAG B6371 14 HET NAG B6372 14 HET BMA B6373 11 HET NAG G 881 14 HET NAG G 882 14 HET BMA G 883 11 HET MAN G 884 11 HET MAN G 885 11 HET MAN G 887 11 HET MAN G 888 11 HET NAG G1331 14 HET NAG G1332 14 HET NAG G1371 14 HET NAG G1372 14 HET BMA G1373 11 HET MAN G1374 11 HET MAN G1375 11 HET MAN G1377 11 HET MAN G1378 11 HET NAG G1561 14 HET NAG G1562 14 HET BMA G1563 11 HET MAN G1564 11 HET MAN G1565 11 HET MAN G1566 11 HET MAN G1567 11 HET MAN G1568 11 HET MAN G1569B 11 HET NAG G1601 14 HET NAG G1602 14 HET BMA G1603 11 HET MAN G1604 11 HET MAN G1605 11 HET MAN G1606 11 HET MAN G1607 11 HET MAN G1609 11 HET NAG G1971 14 HET NAG G1972 14 HET BMA G1973 11 HET MAN G1974 11 HET MAN G1975 11 HET MAN G1977 11 HET NAG G2341 14 HET NAG G2342 14 HET BMA G2343 11 HET MAN G2344 11 HET MAN G2345 11 HET NAG G2621 14 HET NAG G2622 14 HET BMA G2623 11 HET MAN G2624 11 HET MAN G2625 11 HET MAN G2626 11 HET MAN G2627 11 HET MAN G2629A 11 HET NAG G2761 14 HET NAG G2762 14 HET BMA G2763 11 HET MAN G2764 11 HET MAN G2765 11 HET NAG G2951 14 HET NAG G2952 14 HET BMA G2953 11 HET MAN G2954 11 HET MAN G2955 11 HET MAN G2956 11 HET MAN G2957 11 HET NAG G3011 14 HET NAG G3012 14 HET BMA G3013 11 HET MAN G3014 11 HET MAN G3015 11 HET MAN G3016 11 HET MAN G3017 11 HET MAN G3018 11 HET NAG G3321 14 HET NAG G3322 14 HET BMA 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 MAN G3329A 11 HET NAG G3391 14 HET NAG G3551 14 HET NAG G3631 14 HET NAG G3632 14 HET BMA G3633 11 HET NAG G3861 14 HET NAG G3862 14 HET BMA G3863 11 HET MAN G3864 11 HET MAN G3865 11 HET MAN G3866 11 HET NAG G3921 14 HET NAG G3922 14 HET BMA G3923 11 HET MAN G3924 11 HET MAN G3925 11 HET MAN G3926 11 HET NAG G4481 14 HET NAG G4482 14 HET BMA G4483 11 HET MAN G4485 11 HET MAN G4488 11 HET MAN G4489B 11 HET NAG H 231 14 HET NAG H 232 14 HET BMA H 233 11 HET MAN H 234 11 HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE HETNAM NAG N-ACETYL-D-GLUCOSAMINE FORMUL 7 BMA 17(C6 H12 O6) FORMUL 8 MAN 57(C6 H12 O6) FORMUL 9 NAG 40(C8 H15 N O6) HELIX 1 1 THR B 569 TRP B 596 1 28 HELIX 2 2 LEU B 619 ASP B 624 1 6 HELIX 3 3 THR B 627 SER B 636 1 10 HELIX 4 4 TYR B 638 ASP B 664 1 27 HELIX 5 5 ARG D 28 TYR D 32 5 5 HELIX 6 6 PRO D 61 GLN D 64 5 4 HELIX 7 7 LYS D 83 THR D 87 5 5 HELIX 8 8 LYS D 201 ASN D 204 5 4 HELIX 9 9 ASP D 217 PHE D 224 1 8 HELIX 10 10 ARG E 79 GLU E 83 5 5 HELIX 11 11 ASP G 57 GLU G 62 1 6 HELIX 12 12 TRP G 96 ASN G 98 5 3 HELIX 13 13 ASN G 99 LEU G 116 1 18 HELIX 14 14 LEU G 122 CYS G 126 5 5 HELIX 15 15 ILE G 194 SER G 199 1 6 HELIX 16 16 LYS G 335 GLY G 354 1 20 HELIX 17 17 MET G 475 LEU G 483 1 9 HELIX 18 18 TYR G 484 TYR G 486 5 3 HELIX 19 19 HIS H 52 ASP H 56 5 5 HELIX 20 20 LEU H 63 SER H 65 5 3 HELIX 21 21 THR H 83 SER H 87 5 5 HELIX 22 22 SER H 154 ALA H 156 5 3 HELIX 23 23 LYS H 199 ASN H 202 5 4 HELIX 24 24 GLU L 79 GLU L 83 5 5 HELIX 25 25 SER L 122 ALA L 128 1 7 HELIX 26 26 THR L 182 HIS L 189 1 8 SHEET 1 BA 3 ILE B 603 PRO B 609 0 SHEET 2 BA 3 TRP G 35 TYR G 40 -1 O VAL G 36 N THR B 606 SHEET 3 BA 3 LEU G 494 THR G 499 -1 O GLY G 495 N TYR G 39 SHEET 1 DA 6 GLU D 10 LYS D 12 0 SHEET 2 DA 6 THR D 107 VAL D 111 1 O LEU D 108 N GLU D 10 SHEET 3 DA 6 GLY D 88 LYS D 94 -1 O GLY D 88 N LEU D 109 SHEET 4 DA 6 ILE D 34 GLN D 39 -1 O ASN D 35 N ALA D 93 SHEET 5 DA 6 PRO D 45 ILE D 51 -1 O GLU D 46 N ARG D 38 SHEET 6 DA 6 LYS D 57 LEU D 59 -1 O ASN D 58 N TRP D 50 SHEET 1 DB 2 VAL D 18 LYS D 19 0 SHEET 2 DB 2 ALA D 77 ILE D 82 -1 O ILE D 82 N VAL D 18 SHEET 1 DC 2 CYS D 22 LYS D 23 0 SHEET 2 DC 2 ALA D 77 ILE D 82 -1 O ALA D 78 N CYS D 22 SHEET 1 DD 2 VAL D 67 THR D 71 0 SHEET 2 DD 2 ALA D 77 ILE D 82 -1 O TYR D 79 N THR D 70 SHEET 1 DE 2 VAL D 72C THR D 72F 0 SHEET 2 DE 2 THR D 73 THR D 75 -1 O THR D 73 N VAL D 72E SHEET 1 DF 3 VAL D 121 PRO D 123 0 SHEET 2 DF 3 CYS D 140 TYR D 145 -1 O LEU D 141 N PHE D 122 SHEET 3 DF 3 TYR D 176 SER D 179 -1 O TYR D 176 N TYR D 145 SHEET 1 DG 2 ALA D 136 LEU D 138 0 SHEET 2 DG 2 VAL D 182 VAL D 184 -1 O VAL D 182 N LEU D 138 SHEET 1 DH 2 VAL D 198 HIS D 200 0 SHEET 2 DH 2 THR D 205 VAL D 207 -1 O THR D 205 N HIS D 200 SHEET 1 EA 4 THR E 5 GLN E 6 0 SHEET 2 EA 4 VAL E 19 THR E 24 -1 O THR E 24 N THR E 5 SHEET 3 EA 4 SER E 70 ILE E 75 -1 O ALA E 71 N CYS E 23 SHEET 4 EA 4 SER E 63 LYS E 66 -1 O SER E 63 N THR E 74 SHEET 1 EB 4 SER E 9 GLY E 13 0 SHEET 2 EB 4 THR E 102 VAL E 106 1 O LYS E 103 N VAL E 11 SHEET 3 EB 4 THR E 85 TYR E 91 -1 O TYR E 86 N THR E 102 SHEET 4 EB 4 VAL E 97 PHE E 98 -1 O VAL E 97 N SER E 90 SHEET 1 EC 6 SER E 9 GLY E 13 0 SHEET 2 EC 6 THR E 102 VAL E 106 1 O LYS E 103 N VAL E 11 SHEET 3 EC 6 THR E 85 TYR E 91 -1 O TYR E 86 N THR E 102 SHEET 4 EC 6 SER E 32 GLN E 37 -1 O SER E 32 N TYR E 91 SHEET 5 EC 6 THR E 45 TYR E 49 -1 O THR E 45 N GLN E 37 SHEET 6 EC 6 GLU E 53 ARG E 54 -1 O GLU E 53 N TYR E 49 SHEET 1 ED 2 VAL E 97 PHE E 98 0 SHEET 2 ED 2 THR E 85 TYR E 91 -1 O SER E 90 N VAL E 97 SHEET 1 EE 4 SER E 114 VAL E 115 0 SHEET 2 EE 4 THR E 131 PHE E 139 -1 O SER E 137 N SER E 114 SHEET 3 EE 4 TYR E 172 SER E 179 -1 O TYR E 172 N PHE E 139 SHEET 4 EE 4 VAL E 159 THR E 161 -1 O GLU E 160 N TYR E 177 SHEET 1 EF 3 THR E 145 TRP E 148 0 SHEET 2 EF 3 CYS E 193 THR E 196 -1 O GLN E 194 N ALA E 147 SHEET 3 EF 3 THR E 201 GLU E 203 -1 O VAL E 202 N VAL E 195 SHEET 1 GA 5 TRP G 45 ASP G 47 0 SHEET 2 GA 5 VAL G 488 ILE G 491 -1 O LYS G 490 N LYS G 46 SHEET 3 GA 5 PHE G 223 CYS G 228 -1 O ALA G 224 N VAL G 489 SHEET 4 GA 5 VAL G 242 VAL G 245 -1 O SER G 243 N LYS G 227 SHEET 5 GA 5 HIS G 85 LEU G 86 -1 N LEU G 86 O VAL G 242 SHEET 1 GB 3 VAL G 75 PRO G 76 0 SHEET 2 GB 3 PHE G 53 SER G 56 1 O CYS G 54 N VAL G 75 SHEET 3 GB 3 HIS G 216 CYS G 218 -1 O HIS G 216 N ALA G 55 SHEET 1 GC 2 GLU G 91 ASN G 94 0 SHEET 2 GC 2 THR G 236 CYS G 239 -1 O GLY G 237 N PHE G 93 SHEET 1 GD 5 LYS G 169 TYR G 177 0 SHEET 2 GD 5 LEU G 154 THR G 162 -1 O LYS G 155 N PHE G 176 SHEET 3 GD 5 LEU G 129 ASN G 133 -1 O GLN G 130 N SER G 158 SHEET 4 GD 5 GLU G 190 LEU G 193 -1 O TYR G 191 N LEU G 129 SHEET 5 GD 5 VAL G 181 GLN G 183 -1 O VAL G 182 N ARG G 192 SHEET 1 GE 3 ALA G 200 GLN G 203 0 SHEET 2 GE 3 GLN G 432 TYR G 435 1 O ALA G 433 N THR G 202 SHEET 3 GE 3 ILE G 423 ILE G 424 -1 O ILE G 424 N MET G 434 SHEET 1 GF 2 LEU G 259 LEU G 261 0 SHEET 2 GF 2 GLY G 441 ARG G 456 1 N THR G 450 O LEU G 260 SHEET 1 GG 2 MET G 271 ARG G 273 0 SHEET 2 GG 2 ILE G 284 ARG G 308 -1 O LEU G 285 N ARG G 273 SHEET 1 GH 2 ALA G 316 ILE G 323 0 SHEET 2 GH 2 ILE G 284 ARG G 308 -1 O ASN G 301 N ILE G 323 SHEET 1 GI 6 HIS G 374 ASN G 377 0 SHEET 2 GI 6 PHE G 382 CYS G 385 -1 O PHE G 383 N PHE G 376 SHEET 3 GI 6 SER G 413 LYS G 421 -1 O ARG G 419 N TYR G 384 SHEET 4 GI 6 HIS G 330 SER G 334 -1 O CYS G 331 N LEU G 416 SHEET 5 GI 6 ILE G 284 ARG G 308 -1 O GLN G 293 N SER G 334 SHEET 6 GI 6 ALA G 316 ILE G 323 -1 O PHE G 317 N ILE G 307 SHEET 1 GJ 7 HIS G 374 ASN G 377 0 SHEET 2 GJ 7 PHE G 382 CYS G 385 -1 O PHE G 383 N PHE G 376 SHEET 3 GJ 7 SER G 413 LYS G 421 -1 O ARG G 419 N TYR G 384 SHEET 4 GJ 7 HIS G 330 SER G 334 -1 O CYS G 331 N LEU G 416 SHEET 5 GJ 7 ILE G 284 ARG G 308 -1 O GLN G 293 N SER G 334 SHEET 6 GJ 7 GLY G 441 ARG G 456 1 O GLY G 441 N ASN G 302 SHEET 7 GJ 7 PHE G 468 PRO G 470 1 O ARG G 469 N THR G 455 SHEET 1 HA 4 GLN H 5 SER H 7 0 SHEET 2 HA 4 LEU H 18 ASN H 23 -1 O THR H 21 N SER H 7 SHEET 3 HA 4 LEU H 77 LEU H 82 -1 O VAL H 78 N CYS H 22 SHEET 4 HA 4 VAL H 67 SER H 70 -1 O HIS H 68 N ARG H 81 SHEET 1 HB 4 LEU H 11 VAL H 12 0 SHEET 2 HB 4 THR H 105 VAL H 109 1 O THR H 108 N VAL H 12 SHEET 3 HB 4 ALA H 88 LYS H 96 -1 O ALA H 88 N VAL H 107 SHEET 4 HB 4 TYR H 100O VAL H 100R 1 O TYR H 100O N LYS H 96 SHEET 1 HC 5 LEU H 11 VAL H 12 0 SHEET 2 HC 5 THR H 105 VAL H 109 1 O THR H 108 N VAL H 12 SHEET 3 HC 5 ALA H 88 LYS H 96 -1 O ALA H 88 N VAL H 107 SHEET 4 HC 5 TYR H 33 GLN H 39 -1 O TYR H 33 N THR H 95 SHEET 5 HC 5 GLU H 46 VAL H 51 -1 O GLU H 46 N ARG H 38 SHEET 1 HD 2 TYR H 100O VAL H 100R 0 SHEET 2 HD 2 ALA H 88 LYS H 96 1 O THR H 94 N ASP H 100Q SHEET 1 HE 2 ARG H 99 ILE H 100A 0 SHEET 2 HE 2 TRP H 100J THR H 100L-1 O PHE H 100K N ARG H 100 SHEET 1 HF 2 THR H 133 TYR H 143 0 SHEET 2 HF 2 TYR H 174 PRO H 183 -1 O TYR H 174 N TYR H 143 SHEET 1 HG 2 THR H 149 TRP H 152 0 SHEET 2 HG 2 CYS H 194 ASN H 197 -1 O ASN H 195 N SER H 151 SHEET 1 LA 2 THR L 8 VAL L 11 0 SHEET 2 LA 2 THR L 102 LEU L 104 1 O THR L 103 N VAL L 11 SHEET 1 LB 3 THR L 18 CYS L 23 0 SHEET 2 LB 3 ALA L 71 THR L 76 -1 O ALA L 71 N CYS L 23 SHEET 3 LB 3 PHE L 62 GLY L 64 -1 O SER L 63 N THR L 74 SHEET 1 LC 3 PRO L 44 ILE L 48 0 SHEET 2 LC 3 ARG L 31 GLN L 38 -1 O TRP L 35 N ILE L 47 SHEET 3 LC 3 ASP L 85 ASP L 92 -1 O ASP L 85 N GLN L 38 SHEET 1 LD 4 THR L 117 PHE L 119 0 SHEET 2 LD 4 VAL L 134 SER L 138 -1 O VAL L 134 N PHE L 119 SHEET 3 LD 4 LYS L 172 SER L 177 -1 O ALA L 175 N ILE L 137 SHEET 4 LD 4 SER L 166 GLN L 168 -1 O SER L 166 N ALA L 174 SHEET 1 LE 2 ALA L 131 THR L 132 0 SHEET 2 LE 2 SER L 180 LEU L 181 -1 O LEU L 181 N ALA L 131 SHEET 1 LF 4 SER L 154 VAL L 156 0 SHEET 2 LF 4 THR L 146 ALA L 151 -1 O TRP L 149 N VAL L 156 SHEET 3 LF 4 TYR L 192 THR L 197 -1 O SER L 193 N LYS L 150 SHEET 4 LF 4 THR L 202 VAL L 207 -1 O VAL L 203 N VAL L 196 SSBOND 1 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 2 CYS B 605 CYS G 501 1555 1555 2.03 SSBOND 3 CYS D 22 CYS D 92 1555 1555 2.03 SSBOND 4 CYS D 140 CYS D 196 1555 1555 2.04 SSBOND 5 CYS E 23 CYS E 88 1555 1555 2.03 SSBOND 6 CYS E 27C CYS E 28 1555 1555 2.03 SSBOND 7 CYS E 89 CYS E 96 1555 1555 2.03 SSBOND 8 CYS E 134 CYS E 193 1555 1555 2.03 SSBOND 9 CYS G 54 CYS G 74 1555 1555 2.03 SSBOND 10 CYS G 119 CYS G 205 1555 1555 2.04 SSBOND 11 CYS G 126 CYS G 196 1555 1555 2.04 SSBOND 12 CYS G 131 CYS G 157 1555 1555 2.03 SSBOND 13 CYS G 218 CYS G 247 1555 1555 2.03 SSBOND 14 CYS G 228 CYS G 239 1555 1555 2.03 SSBOND 15 CYS G 296 CYS G 331 1555 1555 2.03 SSBOND 16 CYS G 378 CYS G 445 1555 1555 2.03 SSBOND 17 CYS G 385 CYS G 418 1555 1555 2.03 SSBOND 18 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 19 CYS H 138 CYS H 194 1555 1555 2.03 SSBOND 20 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 21 CYS L 135 CYS L 194 1555 1555 2.04 LINK ND2 ASN B 611 C1 NAG B6111 1555 1555 1.44 LINK ND2 ASN B 618 C1 NAG B6181 1555 1555 1.44 LINK ND2 ASN B 637 C1 NAG B6371 1555 1555 1.45 LINK O4 NAG B6371 C1 NAG B6372 1555 1555 1.45 LINK O4 NAG B6372 C1 BMA B6373 1555 1555 1.45 LINK ND2 ASN G 88 C1 NAG G 881 1555 1555 1.44 LINK ND2 ASN G 133 C1 NAG G1331 1555 1555 1.44 LINK ND2 ASN G 137 C1 NAG G1371 1555 1555 1.45 LINK ND2 ASN G 156 C1 NAG G1561 1555 1555 1.45 LINK ND2 ASN G 160 C1 NAG G1601 1555 1555 1.44 LINK ND2 ASN G 197 C1 NAG G1971 1555 1555 1.44 LINK ND2 ASN G 234 C1 NAG G2341 1555 1555 1.44 LINK ND2 ASN G 262 C1 NAG G2621 1555 1555 1.44 LINK ND2 ASN G 276 C1 NAG G2761 1555 1555 1.44 LINK ND2 ASN G 295 C1 NAG G2951 1555 1555 1.45 LINK ND2 ASN G 301 C1 NAG G3011 1555 1555 1.45 LINK ND2 ASN G 332 C1 NAG G3321 1555 1555 1.44 LINK ND2 ASN G 339 C1 NAG G3391 1555 1555 1.43 LINK ND2 ASN G 355 C1 NAG G3551 1555 1555 1.44 LINK ND2 ASN G 363 C1 NAG G3631 1555 1555 1.45 LINK ND2 ASN G 386 C1 NAG G3861 1555 1555 1.44 LINK ND2 ASN G 392 C1 NAG G3921 1555 1555 1.44 LINK ND2 ASN G 448 C1 NAG G4481 1555 1555 1.44 LINK O4 NAG G 881 C1 NAG G 882 1555 1555 1.44 LINK O4 NAG G 882 C1 BMA G 883 1555 1555 1.45 LINK O3 BMA G 883 C1 MAN G 884 1555 1555 1.44 LINK O6 BMA G 883 C1 MAN G 885 1555 1555 1.48 LINK O3 MAN G 885 C1 MAN G 887 1555 1555 1.44 LINK O6 MAN G 885 C1 MAN G 888 1555 1555 1.45 LINK O4 NAG G1331 C1 NAG G1332 1555 1555 1.46 LINK O4 NAG G1371 C1 NAG G1372 1555 1555 1.45 LINK O4 NAG G1372 C1 BMA G1373 1555 1555 1.47 LINK O3 BMA G1373 C1 MAN G1374 1555 1555 1.45 LINK O6 BMA G1373 C1 MAN G1375 1555 1555 1.45 LINK O3 MAN G1375 C1 MAN G1377 1555 1555 1.45 LINK O6 MAN G1375 C1 MAN G1378 1555 1555 1.44 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 1.45 LINK O6 BMA G1563 C1 MAN G1565 1555 1555 1.45 LINK O2 MAN G1564 C1 MAN G1566 1555 1555 1.44 LINK O3 MAN G1565 C1 MAN G1567 1555 1555 1.44 LINK O6 MAN G1565 C1 MAN G1568 1555 1555 1.44 LINK O2 MAN G1568 C1 MAN G1569B 1555 1555 1.45 LINK O4 NAG G1601 C1 NAG G1602 1555 1555 1.44 LINK O4 NAG G1602 C1 BMA G1603 1555 1555 1.45 LINK O6 BMA G1603 C1 MAN G1605 1555 1555 1.44 LINK O3 BMA G1603 C1 MAN G1604 1555 1555 1.45 LINK O2 MAN G1604 C1 MAN G1606 1555 1555 1.45 LINK O3 MAN G1605 C1 MAN G1607 1555 1555 1.45 LINK O2 MAN G1606 C1 MAN G1609 1555 1555 1.45 LINK O4 NAG G1971 C1 NAG G1972 1555 1555 1.44 LINK O4 NAG G1972 C1 BMA G1973 1555 1555 1.45 LINK O3 BMA G1973 C1 MAN G1974 1555 1555 1.45 LINK O6 BMA G1973 C1 MAN G1975 1555 1555 1.45 LINK O3 MAN G1975 C1 MAN G1977 1555 1555 1.44 LINK O4 NAG G2341 C1 NAG G2342 1555 1555 1.46 LINK O4 NAG G2342 C1 BMA G2343 1555 1555 1.45 LINK O6 BMA G2343 C1 MAN G2345 1555 1555 1.45 LINK O3 BMA G2343 C1 MAN G2344 1555 1555 1.44 LINK O4 NAG G2621 C1 NAG G2622 1555 1555 1.45 LINK O4 NAG G2622 C1 BMA G2623 1555 1555 1.45 LINK O6 BMA G2623 C1 MAN G2625 1555 1555 1.45 LINK O3 BMA G2623 C1 MAN G2624 1555 1555 1.45 LINK O2 MAN G2624 C1 MAN G2626 1555 1555 1.46 LINK O3 MAN G2625 C1 MAN G2627 1555 1555 1.45 LINK O2 MAN G2627 C1 MAN G2629A 1555 1555 1.45 LINK O4 NAG G2761 C1 NAG G2762 1555 1555 1.44 LINK O4 NAG G2762 C1 BMA G2763 1555 1555 1.44 LINK O3 BMA G2763 C1 MAN G2764 1555 1555 1.45 LINK O6 BMA G2763 C1 MAN G2765 1555 1555 1.45 LINK O4 NAG G2951 C1 NAG G2952 1555 1555 1.45 LINK O4 NAG G2952 C1 BMA G2953 1555 1555 1.45 LINK O3 BMA G2953 C1 MAN G2954 1555 1555 1.45 LINK O6 BMA G2953 C1 MAN G2955 1555 1555 1.45 LINK O2 MAN G2954 C1 MAN G2956 1555 1555 1.44 LINK O3 MAN G2955 C1 MAN G2957 1555 1555 1.45 LINK O4 NAG G3011 C1 NAG G3012 1555 1555 1.43 LINK O4 NAG G3012 C1 BMA G3013 1555 1555 1.45 LINK O6 BMA G3013 C1 MAN G3015 1555 1555 1.45 LINK O3 BMA G3013 C1 MAN G3014 1555 1555 1.45 LINK O2 MAN G3014 C1 MAN G3016 1555 1555 1.44 LINK O6 MAN G3015 C1 MAN G3018 1555 1555 1.45 LINK O3 MAN G3015 C1 MAN G3017 1555 1555 1.45 LINK O4 NAG G3321 C1 NAG G3322 1555 1555 1.44 LINK O4 NAG G3322 C1 BMA G3323 1555 1555 1.44 LINK O6 BMA G3323 C1 MAN G3325 1555 1555 1.45 LINK O3 BMA G3323 C1 MAN G3324 1555 1555 1.45 LINK O2 MAN G3324 C1 MAN G3326 1555 1555 1.44 LINK O6 MAN G3325 C1 MAN G3328 1555 1555 1.45 LINK O3 MAN G3325 C1 MAN G3327 1555 1555 1.44 LINK O2 MAN G3326 C1 MAN G3329 1555 1555 1.44 LINK O2 MAN G3327 C1 MAN G3329A 1555 1555 1.44 LINK O4 NAG G3631 C1 NAG G3632 1555 1555 1.45 LINK O4 NAG G3632 C1 BMA G3633 1555 1555 1.46 LINK O4 NAG G3861 C1 NAG G3862 1555 1555 1.44 LINK O4 NAG G3862 C1 BMA G3863 1555 1555 1.45 LINK O6 BMA G3863 C1 MAN G3865 1555 1555 1.45 LINK O3 BMA G3863 C1 MAN G3864 1555 1555 1.44 LINK O2 MAN G3864 C1 MAN G3866 1555 1555 1.45 LINK O4 NAG G3921 C1 NAG G3922 1555 1555 1.43 LINK O4 NAG G3922 C1 BMA G3923 1555 1555 1.46 LINK O6 BMA G3923 C1 MAN G3925 1555 1555 1.45 LINK O3 BMA G3923 C1 MAN G3924 1555 1555 1.44 LINK O2 MAN G3924 C1 MAN G3926 1555 1555 1.45 LINK O4 NAG G4481 C1 NAG G4482 1555 1555 1.45 LINK O4 NAG G4482 C1 BMA G4483 1555 1555 1.44 LINK O6 BMA G4483 C1 MAN G4485 1555 1555 1.46 LINK O6 MAN G4485 C1 MAN G4488 1555 1555 1.44 LINK O2 MAN G4488 C1 MAN G4489B 1555 1555 1.45 LINK ND2 ASN H 23 C1 NAG H 231 1555 1555 1.45 LINK O4 NAG H 231 C1 NAG H 232 1555 1555 1.46 LINK O4 NAG H 232 C1 BMA H 233 1555 1555 1.45 LINK O3 BMA H 233 C1 MAN H 234 1555 1555 1.44 CISPEP 1 GLY B 600 LYS B 601 0 4.84 CISPEP 2 PHE D 146 PRO D 147 0 2.45 CISPEP 3 GLU D 148 PRO D 149 0 0.20 CISPEP 4 CYS E 27C CYS E 28 0 3.08 CISPEP 5 ALA E 127 ASN E 128 0 1.13 CISPEP 6 TYR E 140 PRO E 141 0 0.79 CISPEP 7 GLY G 312 PRO G 313 0 -8.78 CISPEP 8 PHE H 144 PRO H 145 0 -4.37 CISPEP 9 GLU H 146 PRO H 147 0 2.64 CISPEP 10 GLY H 188 THR H 189 0 2.37 CISPEP 11 ASP L 60 ARG L 61 0 1.81 CISPEP 12 TYR L 141 PRO L 142 0 -1.37 SITE 1 AC1 2 ASN B 611 SER B 613 SITE 1 AC2 4 ASN B 618 ASN E 52 GLU E 53 ARG E 54 SITE 1 AC3 1 ASN B 637 SITE 1 AC4 19 GLY B 527 SER B 528 ASN D 30 PHE D 31 SITE 2 AC4 19 TYR D 32 HIS D 33 SER D 52 TYR D 53 SITE 3 AC4 19 ASP D 56 LYS D 57 ASN D 58 ARG D 98 SITE 4 AC4 19 ASP D 99 GLY D 100 SER D 100A THR D 100C SITE 5 AC4 19 HIS E 93 ASN E 94 ASN G 88 SITE 1 AC5 4 ASN G 133 ASP G 140 LYS G 155 ARG G 178 SITE 1 AC6 11 ASN G 137 GLY H 55 ASP H 56 ASN H 58 SITE 2 AC6 11 ARG H 99 LYS H 100H TRP H 100J THR H 100L SITE 3 AC6 11 ASP L 92 ARG L 95 THR L 95B SITE 1 AC7 6 VAL G 134 ASN G 156 SER G 158 TYR G 173 SITE 2 AC7 6 GLU L 25 GLU L 26 SITE 1 AC8 2 SER G 158 ASN G 160 SITE 1 AC9 3 ARG G 192 ILE G 194 ASN G 197 SITE 1 BC1 4 ASN G 234 SER G 274 GLU G 275 ILE G 277 SITE 1 BC2 8 LYS G 59 LYS G 65 ASN G 67 ASN G 262 SITE 2 BC2 8 GLY G 379 VAL G 446 SER G 447 NAG G4481 SITE 1 BC3 3 ASN G 276 THR G 278 ASN G 279 SITE 1 BC4 5 GLN G 293 ASN G 295 ASN G 332 ARG G 444 SITE 2 BC4 5 NAG G3321 SITE 1 BC5 3 ASN G 301 ILE G 323 VAL G 442 SITE 1 BC6 15 THR G 297 HIS G 330 ASN G 332 THR G 415 SITE 2 BC6 15 NAG G2951 ARG H 100 ILE H 100A GLY H 100C SITE 3 BC6 15 VAL H 100D SER L 30 ASN L 50 ASN L 51 SITE 4 BC6 15 PRO L 66 GLY L 67 SER L 67A SITE 1 BC7 2 ASN G 339 THR G 394 SITE 1 BC8 2 LYS G 351 ASN G 355 SITE 1 BC9 5 ASN G 363 ASN G 386 SER G 388 NAG G3861 SITE 2 BC9 5 NAG G3862 SITE 1 CC1 6 ASP G 141 ASN G 386 NAG G3631 NAG G3632 SITE 2 CC1 6 BMA G3633 NAG G3922 SITE 1 CC2 2 ASN G 392 MAN G3866 SITE 1 CC3 3 ASN G 262 ASN G 448 NAG G2621 SITE 1 CC4 4 THR H 21 ASN H 23 LYS H 75 LEU H 77 CRYST1 129.780 129.780 313.060 90.00 90.00 120.00 P 63 6 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 0.007705 0.004449 0.000000 0.00000 SCALE2 0.000000 0.008897 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003194 0.00000