HEADER VIRAL PROTEIN/IMMUNE SYSTEM 17-MAR-24 9B2W TITLE PIV3 HN WITH FAB 13 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMAGGLUTININ-NEURAMINIDASE; COMPND 3 CHAIN: D, A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB 13 HEAVY CHAIN; COMPND 7 CHAIN: B, E; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: FAB 13 LIGHT CHAIN; COMPND 11 CHAIN: C, F; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN RESPIROVIRUS 3; SOURCE 3 ORGANISM_TAXID: 11216; SOURCE 4 GENE: HN; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; 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 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HN, HEMAGGLUTININ NEURAMINIDASE, COMPLEX, ANTIBODY COMPLEX, VIRAL KEYWDS 2 PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR I.A.DURIE,J.J.MOUSA REVDAT 1 04-DEC-24 9B2W 0 JRNL AUTH I.A.DURIE,R.J.MILLER,A.D.GINGERICH,A.G.BRANCH,R.DAVID, JRNL AUTH 2 N.S.ABBADI,M.BRINDLEY,J.J.MOUSA JRNL TITL STRUCTURE AND MECHANISM OF PROTECTIVE AND NONPROTECTIVE JRNL TITL 2 HUMAN MONOCLONAL ANTIBODIES TARGETING THE PARAINFLUENZA JRNL TITL 3 VIRUS TYPE 3 HEMAGGLUTININ-NEURAMINIDASE PROTEIN JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.51 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.51 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.76 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8 REMARK 3 NUMBER OF REFLECTIONS : 61212 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.221 REMARK 3 R VALUE (WORKING SET) : 0.219 REMARK 3 FREE R VALUE : 0.264 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060 REMARK 3 FREE R VALUE TEST SET COUNT : 3099 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 34.7600 - 7.0100 0.94 2653 127 0.1689 0.2033 REMARK 3 2 7.0100 - 5.5700 0.99 2747 123 0.1967 0.2182 REMARK 3 3 5.5700 - 4.8700 0.99 2752 117 0.1691 0.1836 REMARK 3 4 4.8700 - 4.4200 0.94 2611 109 0.1555 0.1783 REMARK 3 5 4.4200 - 4.1100 0.99 2659 175 0.1710 0.2243 REMARK 3 6 4.1100 - 3.8700 0.99 2667 164 0.1985 0.2324 REMARK 3 7 3.8700 - 3.6700 0.99 2722 134 0.2132 0.2590 REMARK 3 8 3.6700 - 3.5100 0.99 2698 157 0.2254 0.2772 REMARK 3 9 3.5100 - 3.3800 0.99 2711 139 0.2312 0.2572 REMARK 3 10 3.3800 - 3.2600 0.99 2654 145 0.2514 0.3160 REMARK 3 11 3.2600 - 3.1600 0.98 2691 141 0.2520 0.3352 REMARK 3 12 3.1600 - 3.0700 0.94 2536 157 0.2690 0.3116 REMARK 3 13 3.0700 - 2.9900 0.98 2692 139 0.2859 0.3388 REMARK 3 14 2.9900 - 2.9200 0.98 2605 169 0.2807 0.3477 REMARK 3 15 2.9200 - 2.8500 0.97 2662 146 0.2755 0.3259 REMARK 3 16 2.8500 - 2.7900 0.97 2639 147 0.2724 0.3469 REMARK 3 17 2.7900 - 2.7300 0.97 2626 144 0.2741 0.3152 REMARK 3 18 2.7300 - 2.6800 0.96 2616 129 0.2817 0.3189 REMARK 3 19 2.6800 - 2.6300 0.97 2633 134 0.2855 0.3263 REMARK 3 20 2.6300 - 2.5900 0.96 2621 144 0.2687 0.3337 REMARK 3 21 2.5900 - 2.5500 0.95 2554 142 0.2943 0.3098 REMARK 3 22 2.5500 - 2.5100 0.85 2364 117 0.3043 0.3728 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) : 0.350 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.120 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 : 0.004 13886 REMARK 3 ANGLE : 0.692 18909 REMARK 3 CHIRALITY : 0.046 2168 REMARK 3 PLANARITY : 0.008 2406 REMARK 3 DIHEDRAL : 5.901 1990 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL 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 9B2W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAR-24. REMARK 100 THE DEPOSITION ID IS D_1000282107. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-FEB-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 14-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61212 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.510 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0 REMARK 200 DATA REDUNDANCY : 1.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 17.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.51 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60 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: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47.58 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M AMMONIUM SULFATE, 0.1M MES PH REMARK 280 6.5, 15% (W/V) PEG 4000, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 300K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 64.67650 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 19200 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 68290 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -93.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, A, B, C, E, F, H, G, I, J, REMARK 350 AND CHAINS: K 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 HIS D 1 REMARK 465 HIS D 2 REMARK 465 HIS D 3 REMARK 465 HIS D 4 REMARK 465 HIS D 5 REMARK 465 HIS D 6 REMARK 465 SER D 7 REMARK 465 LEU D 8 REMARK 465 VAL D 9 REMARK 465 PRO D 10 REMARK 465 ARG D 11 REMARK 465 GLY D 12 REMARK 465 SER D 13 REMARK 465 ILE D 14 REMARK 465 SER D 15 REMARK 465 GLU D 16 REMARK 465 ILE D 17 REMARK 465 THR D 18 REMARK 465 ILE D 19 REMARK 465 ARG D 20 REMARK 465 ASN D 21 REMARK 465 ASP D 22 REMARK 465 ASN D 23 REMARK 465 GLN D 24 REMARK 465 GLU D 25 REMARK 465 VAL D 26 REMARK 465 LEU D 27 REMARK 465 PRO D 28 REMARK 465 GLN D 29 REMARK 465 GLY D 276 REMARK 465 LEU D 277 REMARK 465 HIS A 1 REMARK 465 HIS A 2 REMARK 465 HIS A 3 REMARK 465 HIS A 4 REMARK 465 HIS A 5 REMARK 465 HIS A 6 REMARK 465 SER A 7 REMARK 465 LEU A 8 REMARK 465 VAL A 9 REMARK 465 PRO A 10 REMARK 465 ARG A 11 REMARK 465 GLY A 12 REMARK 465 SER A 13 REMARK 465 ILE A 14 REMARK 465 SER A 15 REMARK 465 GLU A 16 REMARK 465 ILE A 17 REMARK 465 THR A 18 REMARK 465 ILE A 19 REMARK 465 ARG A 20 REMARK 465 ASN A 21 REMARK 465 ASP A 22 REMARK 465 ASN A 23 REMARK 465 GLN A 24 REMARK 465 GLU A 25 REMARK 465 VAL A 26 REMARK 465 LEU A 27 REMARK 465 PRO A 28 REMARK 465 GLN A 29 REMARK 465 GLY A 276 REMARK 465 LEU A 277 REMARK 465 ASN A 278 REMARK 465 ASP C 0 REMARK 465 SER E 136 REMARK 465 LYS E 137 REMARK 465 SER E 138 REMARK 465 THR E 139 REMARK 465 SER E 140 REMARK 465 GLY E 141 REMARK 465 GLY E 142 REMARK 465 ASP F 0 REMARK 465 CYS F 218 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 THR D 32 -169.86 -120.85 REMARK 500 ASN D 88 -160.33 -128.80 REMARK 500 ASN D 151 -108.56 58.23 REMARK 500 VAL D 211 -53.42 73.02 REMARK 500 ASN D 240 -79.57 -129.65 REMARK 500 THR D 241 -6.13 83.17 REMARK 500 TYR D 294 -159.31 -72.28 REMARK 500 SER D 316 -142.21 -112.33 REMARK 500 SER D 345 -142.38 -137.85 REMARK 500 ASN D 349 -164.68 -128.59 REMARK 500 THR D 364 -151.40 -156.19 REMARK 500 LEU D 411 -101.11 -156.05 REMARK 500 ASN D 412 -161.92 -168.20 REMARK 500 TYR D 419 130.39 -178.96 REMARK 500 TYR D 428 -122.88 61.92 REMARK 500 LEU A 69 55.29 -112.82 REMARK 500 ASN A 88 -156.84 -120.12 REMARK 500 ASN A 151 -106.72 57.37 REMARK 500 VAL A 211 -55.62 73.00 REMARK 500 PRO A 232 46.49 -82.79 REMARK 500 ASN A 240 -78.96 -130.12 REMARK 500 THR A 241 -0.03 79.95 REMARK 500 THR A 248 -167.43 -125.38 REMARK 500 ASP A 263 17.62 56.25 REMARK 500 PRO A 281 156.12 -49.73 REMARK 500 TYR A 294 -162.71 -72.81 REMARK 500 SER A 316 -143.93 -109.71 REMARK 500 SER A 345 -144.97 -135.29 REMARK 500 ASN A 349 -157.63 -128.23 REMARK 500 PRO A 353 -169.60 -79.70 REMARK 500 THR A 364 -153.41 -155.30 REMARK 500 ASN A 393 70.29 59.28 REMARK 500 LEU A 411 -106.01 -149.89 REMARK 500 TYR A 419 129.36 178.81 REMARK 500 TYR A 428 -122.39 57.75 REMARK 500 PRO B 41 103.33 -45.46 REMARK 500 LYS B 43 -150.64 -81.48 REMARK 500 ASP B 103 -155.31 -128.04 REMARK 500 PHE B 106 49.03 -87.17 REMARK 500 ASP B 152 66.30 64.72 REMARK 500 PHE B 154 137.64 -172.31 REMARK 500 LEU C 52 -60.61 -104.61 REMARK 500 ASP C 87 3.59 -62.25 REMARK 500 ASN C 142 73.92 54.44 REMARK 500 LYS C 173 -80.51 -113.37 REMARK 500 LYS E 43 -153.92 -87.00 REMARK 500 ASP E 103 -145.56 -131.43 REMARK 500 ASP E 152 62.83 65.50 REMARK 500 LEU F 52 -62.15 -101.37 REMARK 500 ASN F 142 76.50 50.71 REMARK 500 REMARK 500 THIS ENTRY HAS 51 RAMACHANDRAN OUTLIERS. 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 ASN B 115 10.23 REMARK 500 REMARK 500 REMARK: NULL DBREF 9B2W D 14 461 UNP Q81080 Q81080_9MONO 125 572 DBREF 9B2W A 14 461 UNP Q81080 Q81080_9MONO 125 572 DBREF 9B2W B 1 222 PDB 9B2W 9B2W 1 222 DBREF 9B2W C 0 218 PDB 9B2W 9B2W 0 218 DBREF 9B2W E 1 222 PDB 9B2W 9B2W 1 222 DBREF 9B2W F 0 218 PDB 9B2W 9B2W 0 218 SEQADV 9B2W HIS D 1 UNP Q81080 EXPRESSION TAG SEQADV 9B2W HIS D 2 UNP Q81080 EXPRESSION TAG SEQADV 9B2W HIS D 3 UNP Q81080 EXPRESSION TAG SEQADV 9B2W HIS D 4 UNP Q81080 EXPRESSION TAG SEQADV 9B2W HIS D 5 UNP Q81080 EXPRESSION TAG SEQADV 9B2W HIS D 6 UNP Q81080 EXPRESSION TAG SEQADV 9B2W SER D 7 UNP Q81080 EXPRESSION TAG SEQADV 9B2W LEU D 8 UNP Q81080 EXPRESSION TAG SEQADV 9B2W VAL D 9 UNP Q81080 EXPRESSION TAG SEQADV 9B2W PRO D 10 UNP Q81080 EXPRESSION TAG SEQADV 9B2W ARG D 11 UNP Q81080 EXPRESSION TAG SEQADV 9B2W GLY D 12 UNP Q81080 EXPRESSION TAG SEQADV 9B2W SER D 13 UNP Q81080 EXPRESSION TAG SEQADV 9B2W HIS A 1 UNP Q81080 EXPRESSION TAG SEQADV 9B2W HIS A 2 UNP Q81080 EXPRESSION TAG SEQADV 9B2W HIS A 3 UNP Q81080 EXPRESSION TAG SEQADV 9B2W HIS A 4 UNP Q81080 EXPRESSION TAG SEQADV 9B2W HIS A 5 UNP Q81080 EXPRESSION TAG SEQADV 9B2W HIS A 6 UNP Q81080 EXPRESSION TAG SEQADV 9B2W SER A 7 UNP Q81080 EXPRESSION TAG SEQADV 9B2W LEU A 8 UNP Q81080 EXPRESSION TAG SEQADV 9B2W VAL A 9 UNP Q81080 EXPRESSION TAG SEQADV 9B2W PRO A 10 UNP Q81080 EXPRESSION TAG SEQADV 9B2W ARG A 11 UNP Q81080 EXPRESSION TAG SEQADV 9B2W GLY A 12 UNP Q81080 EXPRESSION TAG SEQADV 9B2W SER A 13 UNP Q81080 EXPRESSION TAG SEQRES 1 D 461 HIS HIS HIS HIS HIS HIS SER LEU VAL PRO ARG GLY SER SEQRES 2 D 461 ILE SER GLU ILE THR ILE ARG ASN ASP ASN GLN GLU VAL SEQRES 3 D 461 LEU PRO GLN ARG ILE THR HIS ASP VAL GLY ILE LYS PRO SEQRES 4 D 461 LEU ASN PRO ASP ASP PHE TRP ARG CYS THR SER GLY LEU SEQRES 5 D 461 PRO SER LEU MET LYS THR PRO LYS ILE ARG LEU MET PRO SEQRES 6 D 461 GLY PRO GLY LEU LEU ALA MET PRO THR THR VAL ASP GLY SEQRES 7 D 461 CYS VAL ARG THR PRO SER LEU VAL ILE ASN ASP LEU ILE SEQRES 8 D 461 TYR ALA TYR THR SER ASN LEU ILE THR ARG GLY CYS GLN SEQRES 9 D 461 ASP ILE GLY LYS SER TYR GLN VAL LEU GLN ILE GLY ILE SEQRES 10 D 461 ILE THR VAL ASN SER ASP LEU VAL PRO ASP LEU ASN PRO SEQRES 11 D 461 ARG ILE SER HIS THR PHE ASN ILE ASN ASP ASN ARG LYS SEQRES 12 D 461 SER CYS SER LEU ALA LEU LEU ASN THR ASP VAL TYR GLN SEQRES 13 D 461 LEU CYS SER THR PRO LYS VAL ASP GLU ARG SER ASP TYR SEQRES 14 D 461 ALA SER SER GLY ILE GLU ASP ILE VAL LEU ASP ILE VAL SEQRES 15 D 461 ASN TYR ASP GLY SER ILE SER THR THR ARG PHE LYS ASN SEQRES 16 D 461 ASN ASN ILE SER PHE ASP GLN PRO TYR ALA ALA LEU TYR SEQRES 17 D 461 PRO SER VAL GLY PRO GLY ILE TYR TYR LYS GLY LYS ILE SEQRES 18 D 461 ILE PHE LEU GLY TYR GLY GLY LEU GLU HIS PRO ILE ASN SEQRES 19 D 461 GLU ASN VAL ILE CYS ASN THR THR GLY CYS PRO GLY LYS SEQRES 20 D 461 THR GLN ARG ASP CYS ASN GLN ALA SER HIS SER PRO TRP SEQRES 21 D 461 PHE SER ASP ARG ARG MET VAL ASN SER ILE ILE VAL ALA SEQRES 22 D 461 ASP LYS GLY LEU ASN SER ILE PRO LYS LEU LYS VAL TRP SEQRES 23 D 461 THR ILE SER MET ARG GLN ASN TYR TRP GLY SER GLU GLY SEQRES 24 D 461 ARG LEU LEU LEU LEU GLY ASN LYS ILE TYR ILE TYR THR SEQRES 25 D 461 ARG SER THR SER TRP HIS SER LYS LEU GLN LEU GLY ILE SEQRES 26 D 461 ILE ASP ILE THR ASP TYR SER ASP ILE ARG ILE LYS TRP SEQRES 27 D 461 THR TRP HIS ASN VAL LEU SER ARG PRO GLY ASN ASN GLU SEQRES 28 D 461 CYS PRO TRP GLY HIS SER CYS PRO ASP GLY CYS ILE THR SEQRES 29 D 461 GLY VAL TYR THR ASP ALA TYR PRO LEU ASN PRO THR GLY SEQRES 30 D 461 SER ILE VAL SER SER VAL ILE LEU ASP SER GLN LYS SER SEQRES 31 D 461 ARG VAL ASN PRO VAL ILE THR TYR SER THR ALA THR GLU SEQRES 32 D 461 ARG VAL ASN GLU LEU ALA ILE LEU ASN ARG THR LEU SER SEQRES 33 D 461 ALA GLY TYR THR THR THR SER CYS ILE THR HIS TYR ASN SEQRES 34 D 461 LYS GLY TYR CYS PHE HIS ILE VAL GLU ILE ASN HIS LYS SEQRES 35 D 461 SER LEU ASN THR PHE GLN PRO MET LEU PHE LYS THR GLU SEQRES 36 D 461 ILE PRO LYS SER CYS SER SEQRES 1 A 461 HIS HIS HIS HIS HIS HIS SER LEU VAL PRO ARG GLY SER SEQRES 2 A 461 ILE SER GLU ILE THR ILE ARG ASN ASP ASN GLN GLU VAL SEQRES 3 A 461 LEU PRO GLN ARG ILE THR HIS ASP VAL GLY ILE LYS PRO SEQRES 4 A 461 LEU ASN PRO ASP ASP PHE TRP ARG CYS THR SER GLY LEU SEQRES 5 A 461 PRO SER LEU MET LYS THR PRO LYS ILE ARG LEU MET PRO SEQRES 6 A 461 GLY PRO GLY LEU LEU ALA MET PRO THR THR VAL ASP GLY SEQRES 7 A 461 CYS VAL ARG THR PRO SER LEU VAL ILE ASN ASP LEU ILE SEQRES 8 A 461 TYR ALA TYR THR SER ASN LEU ILE THR ARG GLY CYS GLN SEQRES 9 A 461 ASP ILE GLY LYS SER TYR GLN VAL LEU GLN ILE GLY ILE SEQRES 10 A 461 ILE THR VAL ASN SER ASP LEU VAL PRO ASP LEU ASN PRO SEQRES 11 A 461 ARG ILE SER HIS THR PHE ASN ILE ASN ASP ASN ARG LYS SEQRES 12 A 461 SER CYS SER LEU ALA LEU LEU ASN THR ASP VAL TYR GLN SEQRES 13 A 461 LEU CYS SER THR PRO LYS VAL ASP GLU ARG SER ASP TYR SEQRES 14 A 461 ALA SER SER GLY ILE GLU ASP ILE VAL LEU ASP ILE VAL SEQRES 15 A 461 ASN TYR ASP GLY SER ILE SER THR THR ARG PHE LYS ASN SEQRES 16 A 461 ASN ASN ILE SER PHE ASP GLN PRO TYR ALA ALA LEU TYR SEQRES 17 A 461 PRO SER VAL GLY PRO GLY ILE TYR TYR LYS GLY LYS ILE SEQRES 18 A 461 ILE PHE LEU GLY TYR GLY GLY LEU GLU HIS PRO ILE ASN SEQRES 19 A 461 GLU ASN VAL ILE CYS ASN THR THR GLY CYS PRO GLY LYS SEQRES 20 A 461 THR GLN ARG ASP CYS ASN GLN ALA SER HIS SER PRO TRP SEQRES 21 A 461 PHE SER ASP ARG ARG MET VAL ASN SER ILE ILE VAL ALA SEQRES 22 A 461 ASP LYS GLY LEU ASN SER ILE PRO LYS LEU LYS VAL TRP SEQRES 23 A 461 THR ILE SER MET ARG GLN ASN TYR TRP GLY SER GLU GLY SEQRES 24 A 461 ARG LEU LEU LEU LEU GLY ASN LYS ILE TYR ILE TYR THR SEQRES 25 A 461 ARG SER THR SER TRP HIS SER LYS LEU GLN LEU GLY ILE SEQRES 26 A 461 ILE ASP ILE THR ASP TYR SER ASP ILE ARG ILE LYS TRP SEQRES 27 A 461 THR TRP HIS ASN VAL LEU SER ARG PRO GLY ASN ASN GLU SEQRES 28 A 461 CYS PRO TRP GLY HIS SER CYS PRO ASP GLY CYS ILE THR SEQRES 29 A 461 GLY VAL TYR THR ASP ALA TYR PRO LEU ASN PRO THR GLY SEQRES 30 A 461 SER ILE VAL SER SER VAL ILE LEU ASP SER GLN LYS SER SEQRES 31 A 461 ARG VAL ASN PRO VAL ILE THR TYR SER THR ALA THR GLU SEQRES 32 A 461 ARG VAL ASN GLU LEU ALA ILE LEU ASN ARG THR LEU SER SEQRES 33 A 461 ALA GLY TYR THR THR THR SER CYS ILE THR HIS TYR ASN SEQRES 34 A 461 LYS GLY TYR CYS PHE HIS ILE VAL GLU ILE ASN HIS LYS SEQRES 35 A 461 SER LEU ASN THR PHE GLN PRO MET LEU PHE LYS THR GLU SEQRES 36 A 461 ILE PRO LYS SER CYS SER SEQRES 1 B 222 GLU VAL GLN LEU LEU GLU SER GLY GLY ALA LEU VAL GLN SEQRES 2 B 222 PRO GLY GLY SER LEU ARG VAL SER CYS ALA ALA SER GLY SEQRES 3 B 222 PHE SER PHE SER SER TYR ALA MET SER TRP LEU ARG GLN SEQRES 4 B 222 THR PRO GLY LYS GLY LEU GLU TRP VAL SER ALA ILE GLY SEQRES 5 B 222 GLY SER GLY HIS SER THR TYR TYR ALA ASP SER VAL GLN SEQRES 6 B 222 GLY ARG PHE THR VAL SER ARG ASP ASN SER LYS ASP THR SEQRES 7 B 222 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 B 222 ALA VAL TYR TYR CYS ALA LYS PHE PHE ARG SER ASP GLY SEQRES 9 B 222 VAL PHE HIS PHE ASP TYR TRP GLY PRO GLY ASN PRO GLY SEQRES 10 B 222 SER PRO SER PRO ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 B 222 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 B 222 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 B 222 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 B 222 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 B 222 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 B 222 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 B 222 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 18 B 222 LYS SEQRES 1 C 219 ASP ASP ILE VAL MET THR GLN SER PRO LEU SER LEU PRO SEQRES 2 C 219 VAL THR PRO GLY GLU PRO ALA SER ILE SER CYS ARG SER SEQRES 3 C 219 SER GLN SER LEU ARG HIS SER ASP GLY ASN ASN TYR LEU SEQRES 4 C 219 ASP TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU SEQRES 5 C 219 LEU ILE TYR LEU GLY SER ASN ARG ALA SER GLY VAL PRO SEQRES 6 C 219 ASP ARG PHE SER GLY SER GLY SER GLY SER ASP PHE THR SEQRES 7 C 219 LEU LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL SEQRES 8 C 219 TYR TYR CYS MET GLN ALA LEU GLN THR PRO THR PHE GLY SEQRES 9 C 219 GLN GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 C 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 C 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 C 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 C 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 C 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 C 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 C 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 C 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 E 222 GLU VAL GLN LEU LEU GLU SER GLY GLY ALA LEU VAL GLN SEQRES 2 E 222 PRO GLY GLY SER LEU ARG VAL SER CYS ALA ALA SER GLY SEQRES 3 E 222 PHE SER PHE SER SER TYR ALA MET SER TRP LEU ARG GLN SEQRES 4 E 222 THR PRO GLY LYS GLY LEU GLU TRP VAL SER ALA ILE GLY SEQRES 5 E 222 GLY SER GLY HIS SER THR TYR TYR ALA ASP SER VAL GLN SEQRES 6 E 222 GLY ARG PHE THR VAL SER ARG ASP ASN SER LYS ASP THR SEQRES 7 E 222 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 E 222 ALA VAL TYR TYR CYS ALA LYS PHE PHE ARG SER ASP GLY SEQRES 9 E 222 VAL PHE HIS PHE ASP TYR TRP GLY PRO GLY ASN PRO GLY SEQRES 10 E 222 SER PRO SER PRO ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 E 222 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 E 222 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 E 222 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 E 222 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 E 222 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 E 222 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 E 222 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 18 E 222 LYS SEQRES 1 F 219 ASP ASP ILE VAL MET THR GLN SER PRO LEU SER LEU PRO SEQRES 2 F 219 VAL THR PRO GLY GLU PRO ALA SER ILE SER CYS ARG SER SEQRES 3 F 219 SER GLN SER LEU ARG HIS SER ASP GLY ASN ASN TYR LEU SEQRES 4 F 219 ASP TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU SEQRES 5 F 219 LEU ILE TYR LEU GLY SER ASN ARG ALA SER GLY VAL PRO SEQRES 6 F 219 ASP ARG PHE SER GLY SER GLY SER GLY SER ASP PHE THR SEQRES 7 F 219 LEU LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL SEQRES 8 F 219 TYR TYR CYS MET GLN ALA LEU GLN THR PRO THR PHE GLY SEQRES 9 F 219 GLN GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 F 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 F 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 F 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 F 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 F 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 F 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 F 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 F 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS HET NAG H 1 14 HET NAG H 2 14 HET NAG G 1 14 HET NAG G 2 14 HET BMA G 3 11 HET NAG I 1 14 HET NAG I 2 14 HET BMA I 3 11 HET FUC I 4 10 HET NAG J 1 14 HET NAG J 2 14 HET BMA J 3 11 HET NAG K 1 14 HET NAG K 2 14 HET FUC K 3 10 HET SO4 D 501 5 HET SO4 A 501 5 HET SO4 A 502 5 HET NAG A 503 14 HET SO4 F 301 5 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE HETNAM SO4 SULFATE ION 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 FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L- HETSYN 2 FUC FUCOSE; FUCOSE FORMUL 7 NAG 11(C8 H15 N O6) FORMUL 8 BMA 3(C6 H12 O6) FORMUL 9 FUC 2(C6 H12 O5) FORMUL 12 SO4 4(O4 S 2-) FORMUL 17 HOH *13(H2 O) HELIX 1 AA1 ASN D 41 TRP D 46 1 6 HELIX 2 AA2 ASP D 164 SER D 171 1 8 HELIX 3 AA3 LYS D 194 ILE D 198 5 5 HELIX 4 AA4 THR D 248 SER D 256 1 9 HELIX 5 AA5 HIS D 257 SER D 262 5 6 HELIX 6 AA6 ASN A 41 TRP A 46 1 6 HELIX 7 AA7 ASP A 164 SER A 171 1 8 HELIX 8 AA8 LYS A 194 ILE A 198 5 5 HELIX 9 AA9 THR A 248 SER A 256 1 9 HELIX 10 AB1 SER A 258 SER A 262 5 5 HELIX 11 AB2 SER B 28 TYR B 32 5 5 HELIX 12 AB3 ARG B 87 THR B 91 5 5 HELIX 13 AB4 SER B 164 ALA B 166 5 3 HELIX 14 AB5 PRO B 193 LEU B 197 5 5 HELIX 15 AB6 LYS B 209 ASN B 212 5 4 HELIX 16 AB7 GLU C 84 VAL C 88 5 5 HELIX 17 AB8 SER C 125 LYS C 130 1 6 HELIX 18 AB9 LYS C 187 LYS C 192 1 6 HELIX 19 AC1 SER E 28 TYR E 32 5 5 HELIX 20 AC2 ASP E 62 GLN E 65 5 4 HELIX 21 AC3 ARG E 87 THR E 91 5 5 HELIX 22 AC4 SER E 164 ALA E 166 5 3 HELIX 23 AC5 PRO E 193 LEU E 197 5 5 HELIX 24 AC6 LYS E 209 ASN E 212 5 4 HELIX 25 AC7 GLU F 84 VAL F 88 5 5 HELIX 26 AC8 SER F 125 SER F 131 1 7 HELIX 27 AC9 LYS F 187 LYS F 192 1 6 SHEET 1 AA1 4 ILE D 37 PRO D 39 0 SHEET 2 AA1 4 ALA D 417 HIS D 427 -1 O THR D 426 N LYS D 38 SHEET 3 AA1 4 LYS D 430 HIS D 441 -1 O TYR D 432 N ILE D 425 SHEET 4 AA1 4 THR D 446 GLU D 455 -1 O THR D 446 N HIS D 441 SHEET 1 AA2 2 LEU D 52 LEU D 55 0 SHEET 2 AA2 2 LYS D 458 SER D 461 -1 O SER D 461 N LEU D 52 SHEET 1 AA3 4 CYS D 79 ILE D 87 0 SHEET 2 AA3 4 TYR D 92 ILE D 99 -1 O ASN D 97 N ARG D 81 SHEET 3 AA3 4 TYR D 110 VAL D 120 -1 O GLN D 114 N TYR D 94 SHEET 4 AA3 4 PRO D 126 PHE D 136 -1 O PHE D 136 N GLN D 111 SHEET 1 AA4 4 LYS D 143 LEU D 150 0 SHEET 2 AA4 4 ASP D 153 SER D 159 -1 O SER D 159 N LYS D 143 SHEET 3 AA4 4 ILE D 177 VAL D 182 -1 O VAL D 178 N CYS D 158 SHEET 4 AA4 4 ILE D 188 PHE D 193 -1 O SER D 189 N ILE D 181 SHEET 1 AA5 5 SER D 199 PHE D 200 0 SHEET 2 AA5 5 LYS D 282 THR D 287 1 O VAL D 285 N SER D 199 SHEET 3 AA5 5 MET D 266 ASP D 274 -1 N ILE D 270 O TRP D 286 SHEET 4 AA5 5 LYS D 220 LEU D 229 -1 N PHE D 223 O ILE D 271 SHEET 5 AA5 5 TYR D 204 PRO D 209 -1 N ALA D 205 O GLY D 228 SHEET 1 AA6 5 SER D 199 PHE D 200 0 SHEET 2 AA6 5 LYS D 282 THR D 287 1 O VAL D 285 N SER D 199 SHEET 3 AA6 5 MET D 266 ASP D 274 -1 N ILE D 270 O TRP D 286 SHEET 4 AA6 5 LYS D 220 LEU D 229 -1 N PHE D 223 O ILE D 271 SHEET 5 AA6 5 ILE D 215 TYR D 217 -1 N ILE D 215 O ILE D 222 SHEET 1 AA7 4 GLY D 299 LEU D 304 0 SHEET 2 AA7 4 LYS D 307 THR D 312 -1 O TYR D 309 N LEU D 302 SHEET 3 AA7 4 GLN D 322 ASP D 327 -1 O ILE D 326 N ILE D 308 SHEET 4 AA7 4 ARG D 335 TRP D 338 -1 O LYS D 337 N ILE D 325 SHEET 1 AA8 4 ALA D 370 PRO D 372 0 SHEET 2 AA8 4 VAL D 380 LEU D 385 -1 O SER D 381 N TYR D 371 SHEET 3 AA8 4 PRO D 394 SER D 399 -1 O THR D 397 N SER D 382 SHEET 4 AA8 4 ARG D 404 ALA D 409 -1 O ASN D 406 N TYR D 398 SHEET 1 AA9 4 ILE A 37 PRO A 39 0 SHEET 2 AA9 4 ALA A 417 HIS A 427 -1 O THR A 426 N LYS A 38 SHEET 3 AA9 4 LYS A 430 HIS A 441 -1 O GLU A 438 N TYR A 419 SHEET 4 AA9 4 THR A 446 GLU A 455 -1 O THR A 446 N HIS A 441 SHEET 1 AB1 2 LEU A 52 LEU A 55 0 SHEET 2 AB1 2 LYS A 458 SER A 461 -1 O SER A 461 N LEU A 52 SHEET 1 AB2 4 CYS A 79 ILE A 87 0 SHEET 2 AB2 4 TYR A 92 ILE A 99 -1 O ASN A 97 N ARG A 81 SHEET 3 AB2 4 TYR A 110 VAL A 120 -1 O GLN A 114 N TYR A 94 SHEET 4 AB2 4 PRO A 126 PHE A 136 -1 O PHE A 136 N GLN A 111 SHEET 1 AB3 4 LYS A 143 LEU A 150 0 SHEET 2 AB3 4 ASP A 153 THR A 160 -1 O SER A 159 N LYS A 143 SHEET 3 AB3 4 ASP A 176 VAL A 182 -1 O VAL A 182 N VAL A 154 SHEET 4 AB3 4 ILE A 188 PHE A 193 -1 O PHE A 193 N ILE A 177 SHEET 1 AB4 5 SER A 199 PHE A 200 0 SHEET 2 AB4 5 LYS A 282 THR A 287 1 O VAL A 285 N SER A 199 SHEET 3 AB4 5 ARG A 265 ASP A 274 -1 N VAL A 272 O LYS A 284 SHEET 4 AB4 5 LYS A 220 LEU A 229 -1 N PHE A 223 O ILE A 271 SHEET 5 AB4 5 TYR A 204 PRO A 209 -1 N TYR A 208 O TYR A 226 SHEET 1 AB5 5 SER A 199 PHE A 200 0 SHEET 2 AB5 5 LYS A 282 THR A 287 1 O VAL A 285 N SER A 199 SHEET 3 AB5 5 ARG A 265 ASP A 274 -1 N VAL A 272 O LYS A 284 SHEET 4 AB5 5 LYS A 220 LEU A 229 -1 N PHE A 223 O ILE A 271 SHEET 5 AB5 5 ILE A 215 TYR A 217 -1 N ILE A 215 O ILE A 222 SHEET 1 AB6 4 GLY A 299 LEU A 304 0 SHEET 2 AB6 4 LYS A 307 THR A 312 -1 O TYR A 309 N LEU A 302 SHEET 3 AB6 4 GLN A 322 ASP A 327 -1 O ILE A 326 N ILE A 308 SHEET 4 AB6 4 ARG A 335 TRP A 338 -1 O LYS A 337 N ILE A 325 SHEET 1 AB7 4 ALA A 370 PRO A 372 0 SHEET 2 AB7 4 ILE A 379 LEU A 385 -1 O SER A 381 N TYR A 371 SHEET 3 AB7 4 PRO A 394 THR A 400 -1 O THR A 397 N SER A 382 SHEET 4 AB7 4 ARG A 404 ALA A 409 -1 O LEU A 408 N ILE A 396 SHEET 1 AB8 4 GLN B 3 SER B 7 0 SHEET 2 AB8 4 LEU B 18 SER B 25 -1 O SER B 21 N SER B 7 SHEET 3 AB8 4 THR B 78 MET B 83 -1 O MET B 83 N LEU B 18 SHEET 4 AB8 4 PHE B 68 ASP B 73 -1 N THR B 69 O GLN B 82 SHEET 1 AB9 6 LEU B 11 VAL B 12 0 SHEET 2 AB9 6 ASN B 115 PRO B 119 1 O SER B 118 N VAL B 12 SHEET 3 AB9 6 ALA B 92 PHE B 99 -1 N TYR B 94 O ASN B 115 SHEET 4 AB9 6 MET B 34 GLN B 39 -1 N GLN B 39 O VAL B 93 SHEET 5 AB9 6 LEU B 45 ILE B 51 -1 O VAL B 48 N TRP B 36 SHEET 6 AB9 6 THR B 58 TYR B 60 -1 O TYR B 59 N ALA B 50 SHEET 1 AC1 4 LEU B 11 VAL B 12 0 SHEET 2 AC1 4 ASN B 115 PRO B 119 1 O SER B 118 N VAL B 12 SHEET 3 AC1 4 ALA B 92 PHE B 99 -1 N TYR B 94 O ASN B 115 SHEET 4 AC1 4 PHE B 108 TRP B 111 -1 O ASP B 109 N LYS B 98 SHEET 1 AC2 4 SER B 128 LEU B 132 0 SHEET 2 AC2 4 ALA B 144 TYR B 153 -1 O LEU B 149 N PHE B 130 SHEET 3 AC2 4 TYR B 184 VAL B 192 -1 O VAL B 192 N ALA B 144 SHEET 4 AC2 4 VAL B 171 THR B 173 -1 N HIS B 172 O VAL B 189 SHEET 1 AC3 4 SER B 128 LEU B 132 0 SHEET 2 AC3 4 ALA B 144 TYR B 153 -1 O LEU B 149 N PHE B 130 SHEET 3 AC3 4 TYR B 184 VAL B 192 -1 O VAL B 192 N ALA B 144 SHEET 4 AC3 4 VAL B 177 LEU B 178 -1 N VAL B 177 O SER B 185 SHEET 1 AC4 3 THR B 159 TRP B 162 0 SHEET 2 AC4 3 ILE B 203 HIS B 208 -1 O ASN B 205 N SER B 161 SHEET 3 AC4 3 THR B 213 LYS B 218 -1 O THR B 213 N HIS B 208 SHEET 1 AC5 4 MET C 4 SER C 7 0 SHEET 2 AC5 4 ALA C 19 SER C 25 -1 O ARG C 24 N THR C 5 SHEET 3 AC5 4 ASP C 75 ILE C 80 -1 O LEU C 78 N ILE C 21 SHEET 4 AC5 4 PHE C 67 SER C 72 -1 N SER C 68 O LYS C 79 SHEET 1 AC6 6 SER C 10 VAL C 13 0 SHEET 2 AC6 6 THR C 106 ILE C 110 1 O GLU C 109 N LEU C 11 SHEET 3 AC6 6 GLY C 89 GLN C 95 -1 N GLY C 89 O VAL C 108 SHEET 4 AC6 6 LEU C 38 GLN C 43 -1 N ASP C 39 O MET C 94 SHEET 5 AC6 6 GLN C 50 TYR C 54 -1 O LEU C 52 N TRP C 40 SHEET 6 AC6 6 ASN C 58 ARG C 59 -1 O ASN C 58 N TYR C 54 SHEET 1 AC7 4 SER C 10 VAL C 13 0 SHEET 2 AC7 4 THR C 106 ILE C 110 1 O GLU C 109 N LEU C 11 SHEET 3 AC7 4 GLY C 89 GLN C 95 -1 N GLY C 89 O VAL C 108 SHEET 4 AC7 4 THR C 101 PHE C 102 -1 O THR C 101 N GLN C 95 SHEET 1 AC8 4 SER C 118 PHE C 122 0 SHEET 2 AC8 4 THR C 133 PHE C 143 -1 O LEU C 139 N PHE C 120 SHEET 3 AC8 4 TYR C 177 SER C 186 -1 O TYR C 177 N PHE C 143 SHEET 4 AC8 4 SER C 163 VAL C 167 -1 N GLN C 164 O THR C 182 SHEET 1 AC9 4 ALA C 157 LEU C 158 0 SHEET 2 AC9 4 LYS C 149 VAL C 154 -1 N VAL C 154 O ALA C 157 SHEET 3 AC9 4 VAL C 195 THR C 201 -1 O GLU C 199 N GLN C 151 SHEET 4 AC9 4 VAL C 209 ASN C 214 -1 O VAL C 209 N VAL C 200 SHEET 1 AD1 4 GLN E 3 SER E 7 0 SHEET 2 AD1 4 LEU E 18 SER E 25 -1 O ALA E 23 N LEU E 5 SHEET 3 AD1 4 THR E 78 MET E 83 -1 O MET E 83 N LEU E 18 SHEET 4 AD1 4 PHE E 68 ASP E 73 -1 N ASP E 73 O THR E 78 SHEET 1 AD2 6 LEU E 11 VAL E 12 0 SHEET 2 AD2 6 ASN E 115 PRO E 119 1 O SER E 118 N VAL E 12 SHEET 3 AD2 6 ALA E 92 PHE E 99 -1 N ALA E 92 O GLY E 117 SHEET 4 AD2 6 MET E 34 GLN E 39 -1 N LEU E 37 O TYR E 95 SHEET 5 AD2 6 LEU E 45 ILE E 51 -1 O SER E 49 N TRP E 36 SHEET 6 AD2 6 THR E 58 TYR E 60 -1 O TYR E 59 N ALA E 50 SHEET 1 AD3 4 LEU E 11 VAL E 12 0 SHEET 2 AD3 4 ASN E 115 PRO E 119 1 O SER E 118 N VAL E 12 SHEET 3 AD3 4 ALA E 92 PHE E 99 -1 N ALA E 92 O GLY E 117 SHEET 4 AD3 4 PHE E 108 TRP E 111 -1 O ASP E 109 N LYS E 98 SHEET 1 AD4 4 SER E 128 LEU E 132 0 SHEET 2 AD4 4 ALA E 144 TYR E 153 -1 O LEU E 149 N PHE E 130 SHEET 3 AD4 4 TYR E 184 VAL E 192 -1 O TYR E 184 N TYR E 153 SHEET 4 AD4 4 VAL E 171 THR E 173 -1 N HIS E 172 O VAL E 189 SHEET 1 AD5 4 SER E 128 LEU E 132 0 SHEET 2 AD5 4 ALA E 144 TYR E 153 -1 O LEU E 149 N PHE E 130 SHEET 3 AD5 4 TYR E 184 VAL E 192 -1 O TYR E 184 N TYR E 153 SHEET 4 AD5 4 VAL E 177 LEU E 178 -1 N VAL E 177 O SER E 185 SHEET 1 AD6 3 THR E 159 TRP E 162 0 SHEET 2 AD6 3 ILE E 203 HIS E 208 -1 O ASN E 205 N SER E 161 SHEET 3 AD6 3 THR E 213 LYS E 218 -1 O THR E 213 N HIS E 208 SHEET 1 AD7 4 MET F 4 SER F 7 0 SHEET 2 AD7 4 ALA F 19 SER F 25 -1 O ARG F 24 N THR F 5 SHEET 3 AD7 4 ASP F 75 ILE F 80 -1 O LEU F 78 N ILE F 21 SHEET 4 AD7 4 PHE F 67 SER F 72 -1 N SER F 68 O LYS F 79 SHEET 1 AD8 6 SER F 10 VAL F 13 0 SHEET 2 AD8 6 THR F 106 ILE F 110 1 O LYS F 107 N LEU F 11 SHEET 3 AD8 6 GLY F 89 GLN F 95 -1 N GLY F 89 O VAL F 108 SHEET 4 AD8 6 LEU F 38 GLN F 43 -1 N TYR F 41 O TYR F 92 SHEET 5 AD8 6 GLN F 50 TYR F 54 -1 O GLN F 50 N LEU F 42 SHEET 6 AD8 6 ASN F 58 ARG F 59 -1 O ASN F 58 N TYR F 54 SHEET 1 AD9 4 SER F 10 VAL F 13 0 SHEET 2 AD9 4 THR F 106 ILE F 110 1 O LYS F 107 N LEU F 11 SHEET 3 AD9 4 GLY F 89 GLN F 95 -1 N GLY F 89 O VAL F 108 SHEET 4 AD9 4 THR F 101 PHE F 102 -1 O THR F 101 N GLN F 95 SHEET 1 AE1 4 SER F 118 PHE F 122 0 SHEET 2 AE1 4 THR F 133 PHE F 143 -1 O LEU F 139 N PHE F 120 SHEET 3 AE1 4 TYR F 177 SER F 186 -1 O LEU F 185 N ALA F 134 SHEET 4 AE1 4 SER F 163 VAL F 167 -1 N SER F 166 O SER F 180 SHEET 1 AE2 4 ALA F 157 LEU F 158 0 SHEET 2 AE2 4 ALA F 148 VAL F 154 -1 N VAL F 154 O ALA F 157 SHEET 3 AE2 4 VAL F 195 HIS F 202 -1 O ALA F 197 N LYS F 153 SHEET 4 AE2 4 VAL F 209 ASN F 214 -1 O VAL F 209 N VAL F 200 SSBOND 1 CYS D 48 CYS D 460 1555 1555 2.03 SSBOND 2 CYS D 79 CYS D 103 1555 1555 2.03 SSBOND 3 CYS D 145 CYS D 158 1555 1555 2.03 SSBOND 4 CYS D 239 CYS D 252 1555 1555 2.03 SSBOND 5 CYS D 244 CYS D 358 1555 1555 2.03 SSBOND 6 CYS D 352 CYS D 362 1555 1555 2.04 SSBOND 7 CYS D 424 CYS D 433 1555 1555 2.03 SSBOND 8 CYS A 48 CYS A 460 1555 1555 2.04 SSBOND 9 CYS A 79 CYS A 103 1555 1555 2.04 SSBOND 10 CYS A 145 CYS A 158 1555 1555 2.03 SSBOND 11 CYS A 239 CYS A 252 1555 1555 2.04 SSBOND 12 CYS A 244 CYS A 358 1555 1555 2.03 SSBOND 13 CYS A 352 CYS A 362 1555 1555 2.02 SSBOND 14 CYS A 424 CYS A 433 1555 1555 2.04 SSBOND 15 CYS B 22 CYS B 96 1555 1555 2.04 SSBOND 16 CYS B 148 CYS B 204 1555 1555 2.03 SSBOND 17 CYS C 23 CYS C 93 1555 1555 2.04 SSBOND 18 CYS C 138 CYS C 198 1555 1555 2.04 SSBOND 19 CYS E 22 CYS E 96 1555 1555 2.03 SSBOND 20 CYS E 148 CYS E 204 1555 1555 2.03 SSBOND 21 CYS F 23 CYS F 93 1555 1555 2.03 SSBOND 22 CYS F 138 CYS F 198 1555 1555 2.04 LINK ND2 ASN D 197 C1 NAG H 1 1555 1555 1.44 LINK ND2 ASN D 240 C1 NAG G 1 1555 1555 1.45 LINK ND2 ASN D 412 C1 NAG I 1 1555 1555 1.44 LINK ND2 ASN A 197 C1 NAG A 503 1555 1555 1.44 LINK ND2 ASN A 240 C1 NAG J 1 1555 1555 1.45 LINK ND2 ASN A 412 C1 NAG K 1 1555 1555 1.45 LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.44 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44 LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.44 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.45 LINK O6 NAG I 1 C1 FUC I 4 1555 1555 1.44 LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.45 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.44 LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.45 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.45 LINK O6 NAG K 1 C1 FUC K 3 1555 1555 1.44 CISPEP 1 THR D 58 PRO D 59 0 -1.16 CISPEP 2 THR A 58 PRO A 59 0 -0.81 CISPEP 3 PHE B 154 PRO B 155 0 -3.38 CISPEP 4 GLU B 156 PRO B 157 0 4.45 CISPEP 5 SER C 7 PRO C 8 0 -0.48 CISPEP 6 TYR C 144 PRO C 145 0 4.20 CISPEP 7 PHE E 154 PRO E 155 0 -1.92 CISPEP 8 GLU E 156 PRO E 157 0 -0.53 CISPEP 9 SER F 7 PRO F 8 0 -1.94 CISPEP 10 TYR F 144 PRO F 145 0 4.75 CRYST1 81.273 129.353 89.454 90.00 93.57 90.00 P 1 21 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.012304 0.000000 0.000768 0.00000 SCALE2 0.000000 0.007731 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011201 0.00000