HEADER IMMUNE SYSTEM 02-JUN-25 9OWF TITLE X-RAY CRYSTAL STRUCTURE OF ZIKA VIRUS ENVELOPE GLYCOPROTEIN IN COMPLEX TITLE 2 WITH FAB OF F25.S02 COMPND MOL_ID: 1; COMPND 2 MOLECULE: GENOME POLYPROTEIN; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: F25.S02 HEAVY CHAIN; COMPND 7 CHAIN: C, H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: F25.S02 LIGHT CHAIN; COMPND 11 CHAIN: D, L; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ZIKA VIRUS; SOURCE 3 ORGANISM_TAXID: 64320; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 EXPRESSION_SYSTEM_CELL: HEK EXPI293; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM_CELL: HEK EXPI293; 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 EXPRESSION_SYSTEM_CELL: HEK EXPI293 KEYWDS ORTHOFLAVIVIRUS, ZIKA, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR N.K.HURLBURT,M.PANCERA REVDAT 1 04-MAR-26 9OWF 0 JRNL AUTH N.K.HURLBURT,M.PANCERA JRNL TITL STRUCTURAL BASIS FOR ANTIBODY CROSS-NEUTRALIZATION OF DENGUE JRNL TITL 2 AND ZIKA VIRUSES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH D.LIEBSCHNER,P.V.AFONINE,M.L.BAKER,G.BUNKOCZI,V.B.CHEN, REMARK 1 AUTH 2 T.I.CROLL,B.HINTZE,L.W.HUNG,S.JAIN,A.J.MCCOY,N.W.MORIARTY, REMARK 1 AUTH 3 R.D.OEFFNER,B.K.POON,M.G.PRISANT,R.J.READ,J.S.RICHARDSON, REMARK 1 AUTH 4 D.C.RICHARDSON,M.D.SAMMITO,O.V.SOBOLEV,D.H.STOCKWELL, REMARK 1 AUTH 5 T.C.TERWILLIGER,A.G.URZHUMTSEV,L.L.VIDEAU,C.J.WILLIAMS, REMARK 1 AUTH 6 P.D.ADAMS REMARK 1 TITL MACROMOLECULAR STRUCTURE DETERMINATION USING X-RAYS, REMARK 1 TITL 2 NEUTRONS AND ELECTRONS: RECENT DEVELOPMENTS IN PHENIX. REMARK 1 REF ACTA CRYSTALLOGR D STRUCT V. 75 861 2019 REMARK 1 REF 2 BIOL REMARK 1 REFN ISSN 2059-7983 REMARK 1 PMID 31588918 REMARK 1 DOI 10.1107/S2059798319011471 REMARK 2 REMARK 2 RESOLUTION. 2.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.70 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 3 NUMBER OF REFLECTIONS : 206051 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.228 REMARK 3 R VALUE (WORKING SET) : 0.225 REMARK 3 FREE R VALUE : 0.274 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960 REMARK 3 FREE R VALUE TEST SET COUNT : 10226 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 48.7000 - 7.1400 1.00 6556 360 0.1900 0.2313 REMARK 3 2 7.1300 - 5.6700 0.99 6461 379 0.2081 0.2515 REMARK 3 3 5.6600 - 4.9500 1.00 6516 367 0.1690 0.2212 REMARK 3 4 4.9500 - 4.5000 1.00 6514 370 0.1534 0.1940 REMARK 3 5 4.5000 - 4.1800 1.00 6606 307 0.1548 0.2153 REMARK 3 6 4.1700 - 3.9300 1.00 6553 315 0.1759 0.1888 REMARK 3 7 3.9300 - 3.7300 0.99 6540 350 0.1985 0.2436 REMARK 3 8 3.7300 - 3.5700 0.99 6558 308 0.2214 0.2978 REMARK 3 9 3.5700 - 3.4300 0.98 6440 328 0.2280 0.2808 REMARK 3 10 3.4300 - 3.3100 0.98 6413 378 0.2432 0.2676 REMARK 3 11 3.3100 - 3.2100 0.99 6450 351 0.2675 0.3570 REMARK 3 12 3.2100 - 3.1200 1.00 6621 292 0.2866 0.3762 REMARK 3 13 3.1200 - 3.0400 1.00 6517 310 0.2945 0.3572 REMARK 3 14 3.0400 - 2.9600 0.99 6519 344 0.2828 0.3489 REMARK 3 15 2.9600 - 2.9000 0.99 6544 338 0.2712 0.3096 REMARK 3 16 2.9000 - 2.8300 0.99 6565 335 0.2596 0.3096 REMARK 3 17 2.8300 - 2.7800 1.00 6522 324 0.2584 0.3161 REMARK 3 18 2.7800 - 2.7200 1.00 6571 346 0.2674 0.3108 REMARK 3 19 2.7200 - 2.6800 0.99 6445 402 0.3078 0.3479 REMARK 3 20 2.6800 - 2.6300 0.98 6456 335 0.3152 0.3947 REMARK 3 21 2.6300 - 2.5900 1.00 6555 353 0.2841 0.3468 REMARK 3 22 2.5900 - 2.5500 1.00 6546 364 0.2967 0.3270 REMARK 3 23 2.5500 - 2.5100 1.00 6460 366 0.3151 0.3808 REMARK 3 24 2.5100 - 2.4800 1.00 6618 349 0.2861 0.3348 REMARK 3 25 2.4800 - 2.4400 1.00 6496 325 0.2880 0.3199 REMARK 3 26 2.4400 - 2.4100 1.00 6612 321 0.2905 0.3203 REMARK 3 27 2.4100 - 2.3800 1.00 6587 312 0.2948 0.3257 REMARK 3 28 2.3800 - 2.3500 0.99 6438 341 0.2906 0.3240 REMARK 3 29 2.3500 - 2.3200 1.00 6636 330 0.2959 0.3263 REMARK 3 30 2.3200 - 2.3000 0.99 6510 326 0.3069 0.3359 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.328 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.081 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 43.71 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 68.64 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 : 0.004 13005 REMARK 3 ANGLE : 0.746 17672 REMARK 3 CHIRALITY : 0.048 2019 REMARK 3 PLANARITY : 0.009 2241 REMARK 3 DIHEDRAL : 6.377 1874 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 6 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN 'A' AND RESID 1 THROUGH 404) REMARK 3 ORIGIN FOR THE GROUP (A): 7.1542 39.8334 -48.6919 REMARK 3 T TENSOR REMARK 3 T11: 0.5030 T22: 0.4192 REMARK 3 T33: 0.5530 T12: 0.1029 REMARK 3 T13: 0.1467 T23: 0.1628 REMARK 3 L TENSOR REMARK 3 L11: 0.1050 L22: 2.3934 REMARK 3 L33: 0.6538 L12: 0.8401 REMARK 3 L13: -0.4019 L23: -1.2636 REMARK 3 S TENSOR REMARK 3 S11: 0.0481 S12: 0.0622 S13: 0.1084 REMARK 3 S21: 0.3265 S22: 0.2331 S23: 0.4400 REMARK 3 S31: -0.2033 S32: -0.1931 S33: -0.2702 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN 'B' AND RESID 1 THROUGH 404) REMARK 3 ORIGIN FOR THE GROUP (A): 15.3753 -12.7755 -37.5810 REMARK 3 T TENSOR REMARK 3 T11: 0.5275 T22: 0.2936 REMARK 3 T33: 0.4181 T12: 0.0112 REMARK 3 T13: 0.1235 T23: 0.0187 REMARK 3 L TENSOR REMARK 3 L11: 0.0623 L22: 2.5742 REMARK 3 L33: 0.8735 L12: 0.4347 REMARK 3 L13: -0.0431 L23: -1.3380 REMARK 3 S TENSOR REMARK 3 S11: -0.0626 S12: 0.0678 S13: -0.0421 REMARK 3 S21: -0.3807 S22: 0.0414 S23: -0.2325 REMARK 3 S31: 0.3267 S32: -0.0294 S33: 0.0160 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN 'C' AND RESID 1 THROUGH 226) REMARK 3 ORIGIN FOR THE GROUP (A): 34.9851 53.1011 -27.6360 REMARK 3 T TENSOR REMARK 3 T11: 0.7237 T22: 0.5857 REMARK 3 T33: 0.4236 T12: -0.0082 REMARK 3 T13: -0.0062 T23: 0.0926 REMARK 3 L TENSOR REMARK 3 L11: 1.5719 L22: 1.1404 REMARK 3 L33: 1.7004 L12: 0.1984 REMARK 3 L13: 0.8029 L23: 0.9655 REMARK 3 S TENSOR REMARK 3 S11: -0.0416 S12: -0.6444 S13: 0.1571 REMARK 3 S21: 0.5286 S22: -0.0860 S23: -0.0110 REMARK 3 S31: 0.0829 S32: -0.4386 S33: 0.1048 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN 'D' AND RESID 3 THROUGH 213) REMARK 3 ORIGIN FOR THE GROUP (A): 47.4292 66.3526 -28.6780 REMARK 3 T TENSOR REMARK 3 T11: 0.8635 T22: 0.5418 REMARK 3 T33: 0.4427 T12: -0.0525 REMARK 3 T13: -0.0878 T23: 0.0108 REMARK 3 L TENSOR REMARK 3 L11: 0.5509 L22: 0.0229 REMARK 3 L33: 3.0217 L12: -0.2030 REMARK 3 L13: 0.8562 L23: 0.0283 REMARK 3 S TENSOR REMARK 3 S11: -0.2047 S12: -0.4100 S13: 0.1679 REMARK 3 S21: 0.3709 S22: 0.0451 S23: -0.1452 REMARK 3 S31: -0.5315 S32: 0.1008 S33: 0.1559 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (CHAIN 'H' AND RESID 1 THROUGH 226) REMARK 3 ORIGIN FOR THE GROUP (A): 29.6841 -9.9765 -3.7909 REMARK 3 T TENSOR REMARK 3 T11: 0.4208 T22: 0.4551 REMARK 3 T33: 0.5708 T12: -0.1015 REMARK 3 T13: 0.0365 T23: 0.1543 REMARK 3 L TENSOR REMARK 3 L11: 2.4109 L22: 0.8302 REMARK 3 L33: 2.2103 L12: -0.1990 REMARK 3 L13: 0.9264 L23: -1.0207 REMARK 3 S TENSOR REMARK 3 S11: -0.1267 S12: 0.1831 S13: 0.2391 REMARK 3 S21: -0.0063 S22: -0.2718 S23: -0.4773 REMARK 3 S31: -0.3719 S32: 0.7040 S33: 0.2609 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (CHAIN 'L' AND RESID 2 THROUGH 213) REMARK 3 ORIGIN FOR THE GROUP (A): 29.4975 -20.4377 11.9616 REMARK 3 T TENSOR REMARK 3 T11: 0.2789 T22: 0.4328 REMARK 3 T33: 0.4571 T12: -0.0810 REMARK 3 T13: -0.0590 T23: 0.1370 REMARK 3 L TENSOR REMARK 3 L11: 1.0636 L22: 1.8100 REMARK 3 L33: 1.7222 L12: -0.3469 REMARK 3 L13: -0.0688 L23: -1.0856 REMARK 3 S TENSOR REMARK 3 S11: 0.0397 S12: -0.1052 S13: 0.1848 REMARK 3 S21: 0.2100 S22: -0.3733 S23: -0.6344 REMARK 3 S31: -0.2362 S32: 0.6079 S33: 0.0288 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 9OWF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUN-25. REMARK 100 THE DEPOSITION ID IS D_1000296410. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-OCT-24 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 : ALS REMARK 200 BEAMLINE : 5.0.3 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.976 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 206051 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 REMARK 200 RESOLUTION RANGE LOW (A) : 48.700 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 16.30 REMARK 200 R MERGE (I) : 0.16400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 20.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 1.87800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.700 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 62.03 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.24 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, PH 8.0, 0.1 M NACL, 5% W/V REMARK 280 PEG 20K, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -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 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 173.04800 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 58.92750 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 58.92750 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 86.52400 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 58.92750 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 58.92750 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 259.57200 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 58.92750 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 58.92750 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 86.52400 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 58.92750 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 58.92750 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 259.57200 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 173.04800 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: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 17780 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 70440 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, H, L, E, F REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 SER C 127 REMARK 465 SER C 128 REMARK 465 LYS C 129 REMARK 465 SER C 130 REMARK 465 THR C 131 REMARK 465 SER C 132 REMARK 465 LYS C 214 REMARK 465 SER C 215 REMARK 465 CYS C 216 REMARK 465 ASP C 217 REMARK 465 LYS C 218 REMARK 465 THR C 219 REMARK 465 HIS C 220 REMARK 465 HIS C 221 REMARK 465 HIS C 222 REMARK 465 HIS C 223 REMARK 465 HIS C 224 REMARK 465 HIS C 225 REMARK 465 GLN D 1 REMARK 465 SER D 2 REMARK 465 THR D 209 REMARK 465 GLU D 210 REMARK 465 CYS D 211 REMARK 465 SER D 212 REMARK 465 SER H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 REMARK 465 GLY H 134 REMARK 465 VAL H 184 REMARK 465 PRO H 185 REMARK 465 SER H 186 REMARK 465 SER H 187 REMARK 465 SER H 188 REMARK 465 LEU H 189 REMARK 465 GLY H 190 REMARK 465 LYS H 214 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 THR H 219 REMARK 465 HIS H 220 REMARK 465 HIS H 221 REMARK 465 HIS H 222 REMARK 465 HIS H 223 REMARK 465 HIS H 224 REMARK 465 HIS H 225 REMARK 465 GLN L 1 REMARK 465 THR L 209 REMARK 465 GLU L 210 REMARK 465 CYS L 211 REMARK 465 SER L 212 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 OG SER C 188 OH TYR C 194 2.16 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 PCA H 1 O - C - N ANGL. DEV. = -9.9 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 ASN A 52 60.30 6.97 REMARK 500 THR A 76 -1.44 71.15 REMARK 500 VAL A 153 78.92 -109.36 REMARK 500 ASN A 154 101.11 -164.06 REMARK 500 ASP A 247 -147.36 -116.11 REMARK 500 ALA A 248 -140.70 -124.43 REMARK 500 ALA A 250 45.08 148.25 REMARK 500 GLN A 253 94.01 -161.00 REMARK 500 ALA A 280 -51.21 77.79 REMARK 500 SER A 285 54.49 -91.85 REMARK 500 MET A 349 0.38 -69.63 REMARK 500 THR B 76 -5.82 75.35 REMARK 500 VAL B 153 74.83 -116.22 REMARK 500 GLU B 159 -45.45 93.68 REMARK 500 THR B 194 10.02 -64.52 REMARK 500 THR B 231 139.91 -175.92 REMARK 500 HIS B 249 -109.18 52.64 REMARK 500 MET B 277 -74.96 -107.67 REMARK 500 THR C 28 -169.80 -70.41 REMARK 500 SER C 30 -149.17 46.21 REMARK 500 ALA C 100C 71.41 -175.30 REMARK 500 ASP C 144 87.77 40.00 REMARK 500 THR C 191 -46.98 -139.01 REMARK 500 ASP D 27B -88.77 -126.08 REMARK 500 LYS D 31 50.36 -104.37 REMARK 500 VAL D 51 -47.74 78.16 REMARK 500 ALA D 84 171.70 176.84 REMARK 500 SER H 30 -134.60 69.05 REMARK 500 ALA H 100C 74.71 -175.84 REMARK 500 ALA H 136 66.82 -154.77 REMARK 500 ASP H 144 88.89 46.23 REMARK 500 ASP L 27B -96.01 -129.83 REMARK 500 LYS L 31 46.76 -103.84 REMARK 500 VAL L 51 -50.45 72.92 REMARK 500 ASN L 128 -2.70 73.28 REMARK 500 ASN L 170 -2.98 78.57 REMARK 500 SER L 190 155.19 69.94 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 252 0.12 SIDE CHAIN REMARK 500 ARG B 252 0.15 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 PCA H 1 -19.00 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9OWE RELATED DB: PDB DBREF1 9OWF A 1 404 UNP A0A0U3FSM8_ZIKV DBREF2 9OWF A A0A0U3FSM8 291 694 DBREF1 9OWF B 1 404 UNP A0A0U3FSM8_ZIKV DBREF2 9OWF B A0A0U3FSM8 291 694 DBREF 9OWF C 1 225 PDB 9OWF 9OWF 1 225 DBREF 9OWF D 1 212 PDB 9OWF 9OWF 1 212 DBREF 9OWF H 1 225 PDB 9OWF 9OWF 1 225 DBREF 9OWF L 1 212 PDB 9OWF 9OWF 1 212 SEQRES 1 A 404 ILE ARG CYS ILE GLY VAL SER ASN ARG ASP PHE VAL GLU SEQRES 2 A 404 GLY MET SER GLY GLY THR TRP VAL ASP ILE VAL LEU GLU SEQRES 3 A 404 HIS GLY GLY CYS VAL THR VAL MET ALA GLN ASP LYS PRO SEQRES 4 A 404 THR VAL ASP ILE GLU LEU VAL THR THR THR VAL SER ASN SEQRES 5 A 404 MET ALA GLU VAL ARG SER TYR CYS TYR GLU ALA SER ILE SEQRES 6 A 404 SER ASP MET ALA SER ASP SER ARG CYS PRO THR GLN GLY SEQRES 7 A 404 GLU ALA TYR LEU ASP LYS GLN SER ASP THR GLN TYR VAL SEQRES 8 A 404 CYS LYS ARG THR LEU VAL ASP ARG GLY TRP GLY ASN GLY SEQRES 9 A 404 CYS GLY LEU PHE GLY LYS GLY SER LEU VAL THR CYS ALA SEQRES 10 A 404 LYS PHE ALA CYS SER LYS LYS MET THR GLY LYS SER ILE SEQRES 11 A 404 GLN PRO GLU ASN LEU GLU TYR ARG ILE MET LEU SER VAL SEQRES 12 A 404 HIS GLY SER GLN HIS SER GLY MET ILE VAL ASN ASP THR SEQRES 13 A 404 GLY HIS GLU THR ASP GLU ASN ARG ALA LYS VAL GLU ILE SEQRES 14 A 404 THR PRO ASN SER PRO ARG ALA GLU ALA THR LEU GLY GLY SEQRES 15 A 404 PHE GLY SER LEU GLY LEU ASP CYS GLU PRO ARG THR GLY SEQRES 16 A 404 LEU ASP PHE SER ASP LEU TYR TYR LEU THR MET ASN ASN SEQRES 17 A 404 LYS HIS TRP LEU VAL HIS LYS GLU TRP PHE HIS ASP ILE SEQRES 18 A 404 PRO LEU PRO TRP HIS ALA GLY ALA ASP THR GLY THR PRO SEQRES 19 A 404 HIS TRP ASN ASN LYS GLU ALA LEU VAL GLU PHE LYS ASP SEQRES 20 A 404 ALA HIS ALA LYS ARG GLN THR VAL VAL VAL LEU GLY SER SEQRES 21 A 404 GLN GLU GLY ALA VAL HIS THR ALA LEU ALA GLY ALA LEU SEQRES 22 A 404 GLU ALA GLU MET ASP GLY ALA LYS GLY ARG LEU SER SER SEQRES 23 A 404 GLY HIS LEU LYS CYS ARG LEU LYS MET ASP LYS LEU ARG SEQRES 24 A 404 LEU LYS GLY VAL SER TYR SER LEU CYS THR ALA ALA PHE SEQRES 25 A 404 THR PHE THR LYS ILE PRO ALA GLU THR LEU HIS GLY THR SEQRES 26 A 404 VAL THR VAL GLU VAL GLN TYR ALA GLY THR ASP GLY PRO SEQRES 27 A 404 CYS LYS VAL PRO ALA GLN MET ALA VAL ASP MET GLN THR SEQRES 28 A 404 LEU THR PRO VAL GLY ARG LEU ILE THR ALA ASN PRO VAL SEQRES 29 A 404 ILE THR GLU SER THR GLU ASN SER LYS MET MET LEU GLU SEQRES 30 A 404 LEU ASP PRO PRO PHE GLY ASP SER TYR ILE VAL ILE GLY SEQRES 31 A 404 VAL GLY GLU LYS LYS ILE THR HIS HIS TRP HIS ARG SER SEQRES 32 A 404 GLY SEQRES 1 B 404 ILE ARG CYS ILE GLY VAL SER ASN ARG ASP PHE VAL GLU SEQRES 2 B 404 GLY MET SER GLY GLY THR TRP VAL ASP ILE VAL LEU GLU SEQRES 3 B 404 HIS GLY GLY CYS VAL THR VAL MET ALA GLN ASP LYS PRO SEQRES 4 B 404 THR VAL ASP ILE GLU LEU VAL THR THR THR VAL SER ASN SEQRES 5 B 404 MET ALA GLU VAL ARG SER TYR CYS TYR GLU ALA SER ILE SEQRES 6 B 404 SER ASP MET ALA SER ASP SER ARG CYS PRO THR GLN GLY SEQRES 7 B 404 GLU ALA TYR LEU ASP LYS GLN SER ASP THR GLN TYR VAL SEQRES 8 B 404 CYS LYS ARG THR LEU VAL ASP ARG GLY TRP GLY ASN GLY SEQRES 9 B 404 CYS GLY LEU PHE GLY LYS GLY SER LEU VAL THR CYS ALA SEQRES 10 B 404 LYS PHE ALA CYS SER LYS LYS MET THR GLY LYS SER ILE SEQRES 11 B 404 GLN PRO GLU ASN LEU GLU TYR ARG ILE MET LEU SER VAL SEQRES 12 B 404 HIS GLY SER GLN HIS SER GLY MET ILE VAL ASN ASP THR SEQRES 13 B 404 GLY HIS GLU THR ASP GLU ASN ARG ALA LYS VAL GLU ILE SEQRES 14 B 404 THR PRO ASN SER PRO ARG ALA GLU ALA THR LEU GLY GLY SEQRES 15 B 404 PHE GLY SER LEU GLY LEU ASP CYS GLU PRO ARG THR GLY SEQRES 16 B 404 LEU ASP PHE SER ASP LEU TYR TYR LEU THR MET ASN ASN SEQRES 17 B 404 LYS HIS TRP LEU VAL HIS LYS GLU TRP PHE HIS ASP ILE SEQRES 18 B 404 PRO LEU PRO TRP HIS ALA GLY ALA ASP THR GLY THR PRO SEQRES 19 B 404 HIS TRP ASN ASN LYS GLU ALA LEU VAL GLU PHE LYS ASP SEQRES 20 B 404 ALA HIS ALA LYS ARG GLN THR VAL VAL VAL LEU GLY SER SEQRES 21 B 404 GLN GLU GLY ALA VAL HIS THR ALA LEU ALA GLY ALA LEU SEQRES 22 B 404 GLU ALA GLU MET ASP GLY ALA LYS GLY ARG LEU SER SER SEQRES 23 B 404 GLY HIS LEU LYS CYS ARG LEU LYS MET ASP LYS LEU ARG SEQRES 24 B 404 LEU LYS GLY VAL SER TYR SER LEU CYS THR ALA ALA PHE SEQRES 25 B 404 THR PHE THR LYS ILE PRO ALA GLU THR LEU HIS GLY THR SEQRES 26 B 404 VAL THR VAL GLU VAL GLN TYR ALA GLY THR ASP GLY PRO SEQRES 27 B 404 CYS LYS VAL PRO ALA GLN MET ALA VAL ASP MET GLN THR SEQRES 28 B 404 LEU THR PRO VAL GLY ARG LEU ILE THR ALA ASN PRO VAL SEQRES 29 B 404 ILE THR GLU SER THR GLU ASN SER LYS MET MET LEU GLU SEQRES 30 B 404 LEU ASP PRO PRO PHE GLY ASP SER TYR ILE VAL ILE GLY SEQRES 31 B 404 VAL GLY GLU LYS LYS ILE THR HIS HIS TRP HIS ARG SER SEQRES 32 B 404 GLY SEQRES 1 C 238 PCA VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 C 238 PRO GLY SER SER ALA LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 C 238 GLY THR PHE SER SER TYR ALA ILE SER TRP VAL ARG GLN SEQRES 4 C 238 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY SER ILE MET SEQRES 5 C 238 PRO ILE PHE GLY THR VAL ASN TYR ALA GLN LYS PHE GLN SEQRES 6 C 238 GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER THR SEQRES 7 C 238 ALA TYR MET GLU LEU SER ARG LEU ARG SER GLU ASP THR SEQRES 8 C 238 ALA VAL TYR PHE CYS ALA ARG GLY TRP GLY GLY ASN TYR SEQRES 9 C 238 ARG SER ALA ASP LEU TRP ILE TYR PHE ASP LEU TRP GLY SEQRES 10 C 238 GLN GLY THR LEU VAL THR VAL SER SER ARG SER THR LYS SEQRES 11 C 238 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 12 C 238 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 13 C 238 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 C 238 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 15 C 238 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 16 C 238 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 17 C 238 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 18 C 238 LYS ARG VAL GLU PRO LYS SER CYS ASP LYS THR HIS HIS SEQRES 19 C 238 HIS HIS HIS HIS SEQRES 1 D 217 GLN SER ALA LEU THR GLN PRO ARG SER VAL SER GLY SER SEQRES 2 D 217 PRO GLY GLN SER VAL THR ILE SER CYS THR GLY THR SER SEQRES 3 D 217 SER ASP VAL GLY GLY TYR LYS TYR VAL SER TRP TYR GLN SEQRES 4 D 217 GLN HIS PRO GLY LYS ALA PRO LYS LEU MET ILE TYR ASP SEQRES 5 D 217 VAL THR LYS ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 D 217 GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER SEQRES 7 D 217 GLY LEU GLN ALA ASP ASP GLU ALA ASP TYR TYR CYS CYS SEQRES 8 D 217 SER TYR ALA GLY SER TYR THR HIS VAL VAL PHE GLY GLY SEQRES 9 D 217 GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ASN SEQRES 10 D 217 PRO THR VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11 D 217 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP SEQRES 12 D 217 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SEQRES 13 D 217 SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SEQRES 14 D 217 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR SEQRES 15 D 217 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER SEQRES 16 D 217 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU SEQRES 17 D 217 LYS THR VAL ALA PRO THR GLU CYS SER SEQRES 1 H 238 PCA VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 238 PRO GLY SER SER ALA LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 238 GLY THR PHE SER SER TYR ALA ILE SER TRP VAL ARG GLN SEQRES 4 H 238 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY SER ILE MET SEQRES 5 H 238 PRO ILE PHE GLY THR VAL ASN TYR ALA GLN LYS PHE GLN SEQRES 6 H 238 GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER THR SEQRES 7 H 238 ALA TYR MET GLU LEU SER ARG LEU ARG SER GLU ASP THR SEQRES 8 H 238 ALA VAL TYR PHE CYS ALA ARG GLY TRP GLY GLY ASN TYR SEQRES 9 H 238 ARG SER ALA ASP LEU TRP ILE TYR PHE ASP LEU TRP GLY SEQRES 10 H 238 GLN GLY THR LEU VAL THR VAL SER SER ARG SER THR LYS SEQRES 11 H 238 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 12 H 238 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 13 H 238 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 H 238 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 15 H 238 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 16 H 238 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 17 H 238 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 18 H 238 LYS ARG VAL GLU PRO LYS SER CYS ASP LYS THR HIS HIS SEQRES 19 H 238 HIS HIS HIS HIS SEQRES 1 L 217 GLN SER ALA LEU THR GLN PRO ARG SER VAL SER GLY SER SEQRES 2 L 217 PRO GLY GLN SER VAL THR ILE SER CYS THR GLY THR SER SEQRES 3 L 217 SER ASP VAL GLY GLY TYR LYS TYR VAL SER TRP TYR GLN SEQRES 4 L 217 GLN HIS PRO GLY LYS ALA PRO LYS LEU MET ILE TYR ASP SEQRES 5 L 217 VAL THR LYS ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 L 217 GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER SEQRES 7 L 217 GLY LEU GLN ALA ASP ASP GLU ALA ASP TYR TYR CYS CYS SEQRES 8 L 217 SER TYR ALA GLY SER TYR THR HIS VAL VAL PHE GLY GLY SEQRES 9 L 217 GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ASN SEQRES 10 L 217 PRO THR VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11 L 217 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP SEQRES 12 L 217 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SEQRES 13 L 217 SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SEQRES 14 L 217 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR SEQRES 15 L 217 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER SEQRES 16 L 217 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU SEQRES 17 L 217 LYS THR VAL ALA PRO THR GLU CYS SER HET PCA C 1 13 HET PCA H 1 13 HET NAG E 1 26 HET NAG E 2 27 HET BMA E 3 20 HET MAN E 4 22 HET MAN E 5 22 HET FUC E 6 21 HET NAG F 1 26 HET NAG F 2 27 HET BMA F 3 21 HET MAN F 4 22 HET FUC F 5 21 HETNAM PCA PYROGLUTAMIC ACID HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L- HETSYN 2 FUC FUCOSE; FUCOSE FORMUL 3 PCA 2(C5 H7 N O3) FORMUL 7 NAG 4(C8 H15 N O6) FORMUL 7 BMA 2(C6 H12 O6) FORMUL 7 MAN 3(C6 H12 O6) FORMUL 7 FUC 2(C6 H12 O5) FORMUL 9 HOH *438(H2 O) HELIX 1 AA1 LEU A 82 ASP A 87 5 6 HELIX 2 AA2 GLY A 100 GLY A 104 5 5 HELIX 3 AA3 GLN A 131 GLU A 133 5 3 HELIX 4 AA4 HIS A 148 ILE A 152 5 5 HELIX 5 AA5 GLY A 157 ASP A 161 5 5 HELIX 6 AA6 GLY A 181 PHE A 183 5 3 HELIX 7 AA7 ASP A 197 SER A 199 5 3 HELIX 8 AA8 LYS A 215 ASP A 220 1 6 HELIX 9 AA9 ASN A 238 ALA A 241 5 4 HELIX 10 AB1 GLN A 261 LEU A 269 1 9 HELIX 11 AB2 LEU B 82 ASP B 87 5 6 HELIX 12 AB3 GLY B 100 GLY B 104 5 5 HELIX 13 AB4 GLN B 131 GLU B 133 5 3 HELIX 14 AB5 HIS B 148 ILE B 152 5 5 HELIX 15 AB6 GLY B 181 PHE B 183 5 3 HELIX 16 AB7 PRO B 192 GLY B 195 5 4 HELIX 17 AB8 ASP B 197 SER B 199 5 3 HELIX 18 AB9 LYS B 215 ASP B 220 1 6 HELIX 19 AC1 ASN B 238 ALA B 241 5 4 HELIX 20 AC2 GLN B 261 LEU B 269 1 9 HELIX 21 AC3 GLN C 61 GLN C 64 5 4 HELIX 22 AC4 ARG C 83 THR C 87 5 5 HELIX 23 AC5 ASN C 99 ALA C 100C 5 5 HELIX 24 AC6 SER C 156 ALA C 158 5 3 HELIX 25 AC7 LYS C 201 ASN C 204 5 4 HELIX 26 AC8 GLN D 79 GLU D 83 5 5 HELIX 27 AC9 SER D 121 ALA D 127 1 7 HELIX 28 AD1 THR D 181 SER D 187 1 7 HELIX 29 AD2 PRO H 52A GLY H 55 5 4 HELIX 30 AD3 GLN H 61 GLN H 64 5 4 HELIX 31 AD4 ARG H 83 THR H 87 5 5 HELIX 32 AD5 ASN H 99 ALA H 100C 5 5 HELIX 33 AD6 SER H 156 ALA H 158 5 3 HELIX 34 AD7 LYS H 201 ASN H 204 5 4 HELIX 35 AD8 GLN L 79 GLU L 83 5 5 HELIX 36 AD9 SER L 121 ALA L 127 1 7 HELIX 37 AE1 THR L 181 SER L 187 1 7 SHEET 1 AA1 5 ARG A 9 GLU A 13 0 SHEET 2 AA1 5 CYS A 30 MET A 34 1 O THR A 32 N ASP A 10 SHEET 3 AA1 5 VAL A 41 VAL A 50 -1 O VAL A 41 N VAL A 33 SHEET 4 AA1 5 LEU A 135 VAL A 143 -1 O SER A 142 N ASP A 42 SHEET 5 AA1 5 ARG A 164 ILE A 169 -1 O ILE A 169 N TYR A 137 SHEET 1 AA2 4 ARG A 9 GLU A 13 0 SHEET 2 AA2 4 CYS A 30 MET A 34 1 O THR A 32 N ASP A 10 SHEET 3 AA2 4 VAL A 41 VAL A 50 -1 O VAL A 41 N VAL A 33 SHEET 4 AA2 4 GLY A 282 ARG A 283 -1 O GLY A 282 N VAL A 50 SHEET 1 AA3 4 TRP A 20 GLU A 26 0 SHEET 2 AA3 4 HIS A 288 LYS A 294 -1 O LEU A 293 N VAL A 21 SHEET 3 AA3 4 SER A 185 PRO A 192 -1 N GLU A 191 O LYS A 290 SHEET 4 AA3 4 ARG A 175 THR A 179 -1 N ALA A 178 O LEU A 186 SHEET 1 AA4 4 TYR A 90 ARG A 99 0 SHEET 2 AA4 4 GLY A 109 SER A 129 -1 O GLY A 111 N VAL A 97 SHEET 3 AA4 4 ALA A 54 SER A 72 -1 N GLU A 62 O SER A 122 SHEET 4 AA4 4 TRP A 225 ALA A 227 -1 O HIS A 226 N SER A 58 SHEET 1 AA5 5 TYR A 90 ARG A 99 0 SHEET 2 AA5 5 GLY A 109 SER A 129 -1 O GLY A 111 N VAL A 97 SHEET 3 AA5 5 LEU A 201 MET A 206 -1 O TYR A 203 N LYS A 128 SHEET 4 AA5 5 LYS A 209 HIS A 214 -1 O TRP A 211 N LEU A 204 SHEET 5 AA5 5 LEU A 273 ALA A 275 -1 O LEU A 273 N LEU A 212 SHEET 1 AA6 2 VAL A 243 ASP A 247 0 SHEET 2 AA6 2 GLN A 253 VAL A 257 -1 O THR A 254 N LYS A 246 SHEET 1 AA7 3 PHE A 312 PHE A 314 0 SHEET 2 AA7 3 VAL A 326 TYR A 332 -1 O GLN A 331 N THR A 313 SHEET 3 AA7 3 ALA A 319 GLU A 320 -1 N ALA A 319 O THR A 327 SHEET 1 AA8 4 PHE A 312 PHE A 314 0 SHEET 2 AA8 4 VAL A 326 TYR A 332 -1 O GLN A 331 N THR A 313 SHEET 3 AA8 4 SER A 372 ASP A 379 -1 O LEU A 378 N VAL A 326 SHEET 4 AA8 4 ARG A 357 LEU A 358 -1 N ARG A 357 O ASP A 379 SHEET 1 AA9 2 CYS A 339 LYS A 340 0 SHEET 2 AA9 2 VAL A 364 ILE A 365 -1 O ILE A 365 N CYS A 339 SHEET 1 AB1 3 ALA A 343 ALA A 346 0 SHEET 2 AB1 3 GLY A 383 ILE A 389 -1 O VAL A 388 N GLN A 344 SHEET 3 AB1 3 ILE A 396 ARG A 402 -1 O ARG A 402 N GLY A 383 SHEET 1 AB2 9 ARG B 9 GLY B 14 0 SHEET 2 AB2 9 CYS B 30 ALA B 35 1 O THR B 32 N ASP B 10 SHEET 3 AB2 9 VAL B 41 VAL B 50 -1 O ILE B 43 N VAL B 31 SHEET 4 AB2 9 GLY B 282 LEU B 284 -1 O LEU B 284 N THR B 48 SHEET 5 AB2 9 GLU B 274 GLU B 276 -1 N GLU B 276 O ARG B 283 SHEET 6 AB2 9 LYS B 209 HIS B 214 -1 N HIS B 210 O ALA B 275 SHEET 7 AB2 9 LEU B 201 MET B 206 -1 N MET B 206 O LYS B 209 SHEET 8 AB2 9 GLY B 109 SER B 129 -1 N LYS B 128 O TYR B 203 SHEET 9 AB2 9 TYR B 90 ARG B 99 -1 N THR B 95 O LEU B 113 SHEET 1 AB3 9 ALA B 54 SER B 72 0 SHEET 2 AB3 9 GLY B 109 SER B 129 -1 O CYS B 116 N ALA B 69 SHEET 3 AB3 9 LEU B 201 MET B 206 -1 O TYR B 203 N LYS B 128 SHEET 4 AB3 9 LYS B 209 HIS B 214 -1 O LYS B 209 N MET B 206 SHEET 5 AB3 9 GLU B 274 GLU B 276 -1 O ALA B 275 N HIS B 210 SHEET 6 AB3 9 GLY B 282 LEU B 284 -1 O ARG B 283 N GLU B 276 SHEET 7 AB3 9 VAL B 41 VAL B 50 -1 N THR B 48 O LEU B 284 SHEET 8 AB3 9 LEU B 135 VAL B 143 -1 O SER B 142 N ASP B 42 SHEET 9 AB3 9 ARG B 164 ILE B 169 -1 O ILE B 169 N TYR B 137 SHEET 1 AB4 4 TRP B 20 GLU B 26 0 SHEET 2 AB4 4 HIS B 288 LYS B 294 -1 O LEU B 289 N LEU B 25 SHEET 3 AB4 4 SER B 185 GLU B 191 -1 N ASP B 189 O ARG B 292 SHEET 4 AB4 4 ARG B 175 THR B 179 -1 N ALA B 178 O LEU B 186 SHEET 1 AB5 2 TRP B 225 ALA B 227 0 SHEET 2 AB5 2 HIS B 235 ASN B 237 -1 O ASN B 237 N TRP B 225 SHEET 1 AB6 2 VAL B 243 ALA B 248 0 SHEET 2 AB6 2 ARG B 252 VAL B 257 -1 O VAL B 256 N GLU B 244 SHEET 1 AB7 3 PHE B 312 PHE B 314 0 SHEET 2 AB7 3 VAL B 326 TYR B 332 -1 O GLN B 331 N THR B 313 SHEET 3 AB7 3 ALA B 319 GLU B 320 -1 N ALA B 319 O THR B 327 SHEET 1 AB8 4 PHE B 312 PHE B 314 0 SHEET 2 AB8 4 VAL B 326 TYR B 332 -1 O GLN B 331 N THR B 313 SHEET 3 AB8 4 SER B 372 ASP B 379 -1 O LEU B 378 N VAL B 326 SHEET 4 AB8 4 ARG B 357 LEU B 358 -1 N ARG B 357 O ASP B 379 SHEET 1 AB9 2 CYS B 339 LYS B 340 0 SHEET 2 AB9 2 VAL B 364 ILE B 365 -1 O ILE B 365 N CYS B 339 SHEET 1 AC1 3 ALA B 343 ALA B 346 0 SHEET 2 AC1 3 GLY B 383 ILE B 389 -1 O VAL B 388 N GLN B 344 SHEET 3 AC1 3 ILE B 396 ARG B 402 -1 O ARG B 402 N GLY B 383 SHEET 1 AC2 4 LEU C 4 GLN C 6 0 SHEET 2 AC2 4 ALA C 18 ALA C 24 -1 O LYS C 23 N VAL C 5 SHEET 3 AC2 4 THR C 77 LEU C 82 -1 O ALA C 78 N CYS C 22 SHEET 4 AC2 4 VAL C 67 ASP C 72 -1 N ASP C 72 O THR C 77 SHEET 1 AC3 6 GLU C 10 LYS C 12 0 SHEET 2 AC3 6 THR C 107 VAL C 111 1 O THR C 110 N GLU C 10 SHEET 3 AC3 6 ALA C 88 ARG C 94 -1 N TYR C 90 O THR C 107 SHEET 4 AC3 6 ILE C 34 GLN C 39 -1 N SER C 35 O ALA C 93 SHEET 5 AC3 6 GLU C 46 MET C 52 -1 O ILE C 51 N ILE C 34 SHEET 6 AC3 6 THR C 56 TYR C 59 -1 O ASN C 58 N SER C 50 SHEET 1 AC4 4 GLU C 10 LYS C 12 0 SHEET 2 AC4 4 THR C 107 VAL C 111 1 O THR C 110 N GLU C 10 SHEET 3 AC4 4 ALA C 88 ARG C 94 -1 N TYR C 90 O THR C 107 SHEET 4 AC4 4 LEU C 102 TRP C 103 -1 O LEU C 102 N ARG C 94 SHEET 1 AC5 4 SER C 120 LEU C 124 0 SHEET 2 AC5 4 THR C 135 TYR C 145 -1 O LEU C 141 N PHE C 122 SHEET 3 AC5 4 TYR C 176 PRO C 185 -1 O TYR C 176 N TYR C 145 SHEET 4 AC5 4 VAL C 163 THR C 165 -1 N HIS C 164 O VAL C 181 SHEET 1 AC6 4 SER C 120 LEU C 124 0 SHEET 2 AC6 4 THR C 135 TYR C 145 -1 O LEU C 141 N PHE C 122 SHEET 3 AC6 4 TYR C 176 PRO C 185 -1 O TYR C 176 N TYR C 145 SHEET 4 AC6 4 VAL C 169 LEU C 170 -1 N VAL C 169 O SER C 177 SHEET 1 AC7 3 THR C 151 TRP C 154 0 SHEET 2 AC7 3 TYR C 194 HIS C 200 -1 O ASN C 197 N SER C 153 SHEET 3 AC7 3 THR C 205 VAL C 211 -1 O THR C 205 N HIS C 200 SHEET 1 AC8 5 SER D 9 GLY D 13 0 SHEET 2 AC8 5 THR D 102 VAL D 106 1 O LYS D 103 N VAL D 11 SHEET 3 AC8 5 ALA D 84 ALA D 92 -1 N ALA D 84 O LEU D 104 SHEET 4 AC8 5 VAL D 33 GLN D 38 -1 N GLN D 38 O ASP D 85 SHEET 5 AC8 5 LYS D 45 ILE D 48 -1 O MET D 47 N TRP D 35 SHEET 1 AC9 4 SER D 9 GLY D 13 0 SHEET 2 AC9 4 THR D 102 VAL D 106 1 O LYS D 103 N VAL D 11 SHEET 3 AC9 4 ALA D 84 ALA D 92 -1 N ALA D 84 O LEU D 104 SHEET 4 AC9 4 HIS D 95B PHE D 98 -1 O VAL D 97 N SER D 90 SHEET 1 AD1 3 VAL D 19 THR D 24 0 SHEET 2 AD1 3 THR D 70 ILE D 75 -1 O LEU D 73 N ILE D 21 SHEET 3 AD1 3 PHE D 62 SER D 67 -1 N SER D 63 O THR D 74 SHEET 1 AD2 4 THR D 114 PHE D 118 0 SHEET 2 AD2 4 ALA D 130 PHE D 139 -1 O LEU D 135 N THR D 116 SHEET 3 AD2 4 TYR D 172 LEU D 180 -1 O LEU D 178 N LEU D 132 SHEET 4 AD2 4 VAL D 159 THR D 161 -1 N GLU D 160 O TYR D 177 SHEET 1 AD3 4 THR D 114 PHE D 118 0 SHEET 2 AD3 4 ALA D 130 PHE D 139 -1 O LEU D 135 N THR D 116 SHEET 3 AD3 4 TYR D 172 LEU D 180 -1 O LEU D 178 N LEU D 132 SHEET 4 AD3 4 SER D 165 LYS D 166 -1 N SER D 165 O ALA D 173 SHEET 1 AD4 4 SER D 153 VAL D 155 0 SHEET 2 AD4 4 THR D 145 ALA D 150 -1 N TRP D 148 O VAL D 155 SHEET 3 AD4 4 TYR D 191 HIS D 197 -1 O THR D 196 N THR D 145 SHEET 4 AD4 4 SER D 200 VAL D 206 -1 O SER D 200 N HIS D 197 SHEET 1 AD5 4 LEU H 4 GLN H 6 0 SHEET 2 AD5 4 ALA H 18 ALA H 24 -1 O LYS H 23 N VAL H 5 SHEET 3 AD5 4 THR H 77 LEU H 82 -1 O ALA H 78 N CYS H 22 SHEET 4 AD5 4 VAL H 67 ASP H 72 -1 N THR H 70 O TYR H 79 SHEET 1 AD6 6 GLU H 10 LYS H 12 0 SHEET 2 AD6 6 THR H 107 VAL H 111 1 O THR H 110 N LYS H 12 SHEET 3 AD6 6 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 107 SHEET 4 AD6 6 ILE H 34 GLN H 39 -1 N SER H 35 O ALA H 93 SHEET 5 AD6 6 GLU H 46 MET H 52 -1 O ILE H 51 N ILE H 34 SHEET 6 AD6 6 THR H 56 TYR H 59 -1 O THR H 56 N MET H 52 SHEET 1 AD7 4 GLU H 10 LYS H 12 0 SHEET 2 AD7 4 THR H 107 VAL H 111 1 O THR H 110 N LYS H 12 SHEET 3 AD7 4 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 107 SHEET 4 AD7 4 LEU H 102 TRP H 103 -1 O LEU H 102 N ARG H 94 SHEET 1 AD8 4 SER H 120 LEU H 124 0 SHEET 2 AD8 4 LEU H 138 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AD8 4 TYR H 176 VAL H 182 -1 O VAL H 182 N LEU H 138 SHEET 4 AD8 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AD9 4 SER H 120 LEU H 124 0 SHEET 2 AD9 4 LEU H 138 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AD9 4 TYR H 176 VAL H 182 -1 O VAL H 182 N LEU H 138 SHEET 4 AD9 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AE1 3 THR H 151 TRP H 154 0 SHEET 2 AE1 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AE1 3 THR H 205 ARG H 210 -1 O VAL H 207 N VAL H 198 SHEET 1 AE2 5 SER L 9 GLY L 13 0 SHEET 2 AE2 5 THR L 102 VAL L 106 1 O LYS L 103 N VAL L 11 SHEET 3 AE2 5 ALA L 84 TYR L 91 -1 N TYR L 86 O THR L 102 SHEET 4 AE2 5 VAL L 33 GLN L 38 -1 N GLN L 38 O ASP L 85 SHEET 5 AE2 5 LYS L 45 ILE L 48 -1 O MET L 47 N TRP L 35 SHEET 1 AE3 4 SER L 9 GLY L 13 0 SHEET 2 AE3 4 THR L 102 VAL L 106 1 O LYS L 103 N VAL L 11 SHEET 3 AE3 4 ALA L 84 TYR L 91 -1 N TYR L 86 O THR L 102 SHEET 4 AE3 4 VAL L 96 PHE L 98 -1 O VAL L 97 N SER L 90 SHEET 1 AE4 3 VAL L 19 THR L 24 0 SHEET 2 AE4 3 THR L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 3 AE4 3 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AE5 4 THR L 114 PHE L 118 0 SHEET 2 AE5 4 THR L 131 PHE L 139 -1 O LEU L 135 N THR L 116 SHEET 3 AE5 4 TYR L 172 SER L 179 -1 O LEU L 178 N LEU L 132 SHEET 4 AE5 4 VAL L 159 THR L 161 -1 N GLU L 160 O TYR L 177 SHEET 1 AE6 4 THR L 114 PHE L 118 0 SHEET 2 AE6 4 THR L 131 PHE L 139 -1 O LEU L 135 N THR L 116 SHEET 3 AE6 4 TYR L 172 SER L 179 -1 O LEU L 178 N LEU L 132 SHEET 4 AE6 4 SER L 165 LYS L 166 -1 N SER L 165 O ALA L 173 SHEET 1 AE7 4 SER L 153 VAL L 155 0 SHEET 2 AE7 4 THR L 145 ALA L 150 -1 N ALA L 150 O SER L 153 SHEET 3 AE7 4 TYR L 191 HIS L 197 -1 O THR L 196 N THR L 145 SHEET 4 AE7 4 SER L 200 VAL L 206 -1 O SER L 200 N HIS L 197 SSBOND 1 CYS A 3 CYS A 30 1555 1555 2.04 SSBOND 2 CYS A 60 CYS A 121 1555 1555 2.07 SSBOND 3 CYS A 74 CYS A 105 1555 1555 2.08 SSBOND 4 CYS A 92 CYS A 116 1555 1555 2.04 SSBOND 5 CYS A 190 CYS A 291 1555 1555 2.04 SSBOND 6 CYS A 308 CYS A 339 1555 1555 2.06 SSBOND 7 CYS B 3 CYS B 30 1555 1555 2.04 SSBOND 8 CYS B 60 CYS B 121 1555 1555 2.07 SSBOND 9 CYS B 74 CYS B 105 1555 1555 2.03 SSBOND 10 CYS B 92 CYS B 116 1555 1555 2.04 SSBOND 11 CYS B 190 CYS B 291 1555 1555 2.05 SSBOND 12 CYS B 308 CYS B 339 1555 1555 2.05 SSBOND 13 CYS C 22 CYS C 92 1555 1555 2.04 SSBOND 14 CYS C 140 CYS C 196 1555 1555 2.03 SSBOND 15 CYS D 23 CYS D 88 1555 1555 2.04 SSBOND 16 CYS D 134 CYS D 193 1555 1555 2.03 SSBOND 17 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 18 CYS H 140 CYS H 196 1555 1555 2.04 SSBOND 19 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 20 CYS L 134 CYS L 193 1555 1555 2.04 LINK ND2 ASN A 154 C1 NAG E 1 1555 1555 1.43 LINK ND2 ASN B 154 C1 NAG F 1 1555 1555 1.44 LINK C PCA C 1 N VAL C 2 1555 1555 1.33 LINK C PCA H 1 N VAL H 2 1555 1555 1.32 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44 LINK O6 NAG E 1 C1 FUC E 6 1555 1555 1.44 LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.45 LINK O3 BMA E 3 C1 MAN E 4 1555 1555 1.45 LINK O6 BMA E 3 C1 MAN E 5 1555 1555 1.45 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44 LINK O6 NAG F 1 C1 FUC F 5 1555 1555 1.44 LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.44 LINK O3 BMA F 3 C1 MAN F 4 1555 1555 1.45 CISPEP 1 GLY A 337 PRO A 338 0 1.47 CISPEP 2 GLY B 337 PRO B 338 0 0.18 CISPEP 3 PHE C 146 PRO C 147 0 -5.88 CISPEP 4 GLU C 148 PRO C 149 0 0.60 CISPEP 5 TYR D 140 PRO D 141 0 1.84 CISPEP 6 PHE H 146 PRO H 147 0 -0.04 CISPEP 7 GLU H 148 PRO H 149 0 0.89 CISPEP 8 TYR L 140 PRO L 141 0 -1.47 CRYST1 117.855 117.855 346.096 90.00 90.00 90.00 P 41 21 2 16 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 0.008485 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008485 0.000000 0.00000 SCALE3 0.000000 0.000000 0.002889 0.00000