HEADER VIRAL PROTEIN 26-NOV-24 9EIT TITLE NCS.1 FAB IN COMPLEX WITH N5 NA OF A/SHOREBIRD/DELAWARE BAY/309/2016 TITLE 2 (DB16, H10N5) -- 4 FABS COMPND MOL_ID: 1; COMPND 2 MOLECULE: NCS.1 HEAVY CHAIN; COMPND 3 CHAIN: H, I, N, S; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: NCS.1 LIGHT CHAIN; COMPND 7 CHAIN: L, M, O, T; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: NEURAMINIDASE; COMPND 11 CHAIN: A, D, G, P; COMPND 12 EC: 3.2.1.18; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 17 ORGANISM_TAXID: 11320; SOURCE 18 GENE: NA; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS NEURAMINIDASE, NCS.1, TETRAMER, ANTIBODY, FAB, N5, H10N5, DB6, VIRAL KEYWDS 2 PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR A.J.BORST REVDAT 1 13-AUG-25 9EIT 0 JRNL AUTH J.LEDERHOFER,A.J.BORST,L.NGUYEN,R.A.GILLESPIE,C.J.WILLIAMS, JRNL AUTH 2 E.L.WALKER,J.E.RAAB,C.YAP,D.ELLIS,A.CREANGA,H.X.TAN, JRNL AUTH 3 T.H.T.DO,M.RAVICHANDRAN,A.B.MCDERMOTT,V.LE SAGE,S.F.ANDREWS, JRNL AUTH 4 B.S.GRAHAM,A.K.WHEATLEY,D.S.REED,N.P.KING,M.KANEKIYO JRNL TITL STRUCTURAL CONVERGENCE AND WATER-MEDIATED SUBSTRATE MIMICRY JRNL TITL 2 ENABLE BROAD NEURAMINIDASE INHIBITION BY HUMAN ANTIBODIES. JRNL REF NAT COMMUN V. 16 7068 2025 JRNL REFN ESSN 2041-1723 JRNL PMID 40750617 JRNL DOI 10.1038/S41467-025-62339-Z REMARK 2 REMARK 2 RESOLUTION. 3.35 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.350 REMARK 3 NUMBER OF PARTICLES : 96602 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9EIT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1000290594. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : NCS.1 FAB IN COMPLEX WITH N5 NA REMARK 245 OF A/SHOREBIRD/DELAWARE BAY/309/ REMARK 245 2016 (DB16, H10N5) -- 4 FABS REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS GLACIOS REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 200 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. 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: DODECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, A, I, M, D, N, O, G, S, REMARK 350 AND CHAINS: T, P 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 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 TYR L 92 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES REMARK 500 CYS A 46 CA - CB - SG ANGL. DEV. = 9.7 DEGREES REMARK 500 PHE D 188 CB - CG - CD1 ANGL. DEV. = 4.9 DEGREES REMARK 500 LEU D 346 CB - CG - CD2 ANGL. DEV. = -16.0 DEGREES REMARK 500 LEU T 29 CB - CG - CD1 ANGL. DEV. = 11.3 DEGREES REMARK 500 LEU T 51 CB - CG - CD2 ANGL. DEV. = -10.8 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 LEU H 104 58.22 33.92 REMARK 500 SER L 7 -83.40 -69.68 REMARK 500 ASN A 4 23.37 -146.96 REMARK 500 LYS A 19 116.79 -161.61 REMARK 500 ASP A 118 42.26 -157.77 REMARK 500 GLN A 139 -162.22 -127.93 REMARK 500 GLU A 145 47.57 -75.71 REMARK 500 ASN A 152 24.24 48.96 REMARK 500 ALA A 168 -154.33 -111.97 REMARK 500 GLU A 177 55.16 38.99 REMARK 500 GLU A 183 113.89 -169.17 REMARK 500 PHE A 188 87.38 -157.17 REMARK 500 GLU A 194 -60.63 -90.89 REMARK 500 CYS A 196 159.73 -49.00 REMARK 500 CYS A 209 -144.66 -117.23 REMARK 500 ASN A 214 37.64 37.08 REMARK 500 ASP A 224 -153.84 -123.22 REMARK 500 SER A 288 12.93 -146.64 REMARK 500 SER A 322 -157.14 -131.87 REMARK 500 SER A 336 12.13 59.90 REMARK 500 GLN A 338 42.80 -83.94 REMARK 500 SER I 5 6.13 82.03 REMARK 500 LEU I 104 63.46 27.91 REMARK 500 SER M 7 -89.87 -71.93 REMARK 500 ASP M 65 -2.12 -58.59 REMARK 500 ASN D 4 20.74 -146.39 REMARK 500 LYS D 19 115.84 -161.12 REMARK 500 ASN D 63 -13.74 -46.94 REMARK 500 ASN D 64 36.46 -146.63 REMARK 500 SER D 93 136.37 -170.68 REMARK 500 SER D 97 131.22 -172.21 REMARK 500 ASP D 118 38.07 -145.98 REMARK 500 GLN D 139 -156.23 -124.77 REMARK 500 ASN D 152 24.00 48.71 REMARK 500 ALA D 168 -158.87 -122.44 REMARK 500 GLU D 183 125.88 -172.87 REMARK 500 PHE D 188 85.81 -153.78 REMARK 500 CYS D 196 153.70 -49.28 REMARK 500 CYS D 209 -149.60 -120.39 REMARK 500 ASP D 224 -155.34 -141.72 REMARK 500 THR D 305 29.03 47.41 REMARK 500 TYR D 324 173.45 -58.39 REMARK 500 SER D 336 12.30 59.67 REMARK 500 GLN D 338 45.86 -83.96 REMARK 500 GLU D 354 -32.54 -130.65 REMARK 500 ASP N 81 5.61 -63.28 REMARK 500 LEU N 104 63.57 21.41 REMARK 500 ASP O 65 5.71 -67.14 REMARK 500 ASN G 4 27.75 -145.42 REMARK 500 ASN G 64 37.90 -89.82 REMARK 500 REMARK 500 THIS ENTRY HAS 88 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 ILE A 34 ARG A 35 149.18 REMARK 500 VAL D 208 CYS D 209 -149.38 REMARK 500 GLN O 6 SER O 7 -145.20 REMARK 500 GLN T 6 SER T 7 -149.34 REMARK 500 ILE P 303 ARG P 304 -147.92 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 D 73 0.08 SIDE CHAIN REMARK 500 ARG G 134 0.10 SIDE CHAIN REMARK 500 ARG G 210 0.09 SIDE CHAIN REMARK 500 ARG P 218 0.13 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 403 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 211 O REMARK 620 2 GLY A 215 O 92.6 REMARK 620 3 ASP A 241 OD2 94.5 102.7 REMARK 620 4 TYR A 266 O 109.9 150.7 94.3 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA D 403 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP D 211 O REMARK 620 2 GLY D 215 O 96.5 REMARK 620 3 ASP D 241 OD2 89.6 104.7 REMARK 620 4 TYR D 266 O 104.6 151.1 95.1 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA G 403 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP G 211 O REMARK 620 2 GLY G 215 O 92.3 REMARK 620 3 ASP G 241 OD2 93.1 105.4 REMARK 620 4 TYR G 266 O 109.1 150.6 93.6 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA P 403 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP P 211 O REMARK 620 2 GLY P 215 O 94.0 REMARK 620 3 ASP P 241 OD2 89.9 104.2 REMARK 620 4 TYR P 266 O 110.7 145.7 99.4 REMARK 620 N 1 2 3 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-48093 RELATED DB: EMDB REMARK 900 NCS.1 FAB IN COMPLEX WITH N5 NA OF A/SHOREBIRD/DELAWARE BAY/309/ REMARK 900 2016 (DB16, H10N5) -- 4 FABS DBREF 9EIT H 1 117 PDB 9EIT 9EIT 1 117 DBREF 9EIT L 1 112 PDB 9EIT 9EIT 1 112 DBREF 9EIT A 0 392 UNP A1ILL9 A1ILL9_I76A2 80 472 DBREF 9EIT I 1 117 PDB 9EIT 9EIT 1 117 DBREF 9EIT M 1 112 PDB 9EIT 9EIT 1 112 DBREF 9EIT D 0 392 UNP A1ILL9 A1ILL9_I76A2 80 472 DBREF 9EIT N 1 117 PDB 9EIT 9EIT 1 117 DBREF 9EIT O 1 112 PDB 9EIT 9EIT 1 112 DBREF 9EIT G 0 392 UNP A1ILL9 A1ILL9_I76A2 80 472 DBREF 9EIT S 1 117 PDB 9EIT 9EIT 1 117 DBREF 9EIT T 1 112 PDB 9EIT 9EIT 1 112 DBREF 9EIT P 0 392 UNP A1ILL9 A1ILL9_I76A2 80 472 SEQRES 1 H 117 LEU VAL LYS PRO SER GLU THR LEU SER LEU THR CYS SER SEQRES 2 H 117 VAL SER GLY GLU SER ILE SER SER GLY GLY TYR TYR TRP SEQRES 3 H 117 THR TRP ILE ARG GLN HIS PRO GLY LYS GLY LEU GLU TRP SEQRES 4 H 117 ILE GLY ASN ILE PHE ASP THR GLY SER THR HIS TYR SER SEQRES 5 H 117 PRO SER LEU LYS THR ARG LEU THR ILE SER ILE ASP THR SEQRES 6 H 117 SER LYS ASN GLN PHE TYR LEU ARG LEU ASN SER ALA THR SEQRES 7 H 117 ALA ALA ASP THR ALA VAL TYR TYR CYS ALA ARG VAL GLY SEQRES 8 H 117 TYR SER LEU GLU THR ASP ARG PRO TYR TYR PHE GLY LEU SEQRES 9 H 117 ASP VAL TRP GLY GLN GLY THR THR VAL THR VAL SER SER SEQRES 1 L 112 ASP ILE VAL MET THR GLN SER PRO LEU SER LEU PRO VAL SEQRES 2 L 112 THR PRO GLY GLU PRO ALA SER ILE SER CYS ARG SER SER SEQRES 3 L 112 GLN SER LEU LEU HIS SER ASN GLY TYR THR TYR LEU ASP SEQRES 4 L 112 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 L 112 ILE TYR LEU ALA SER ASN ARG ALA SER GLY VAL PRO ASP SEQRES 6 L 112 ARG PHE SER GLY SER GLY SER GLY THR TYR PHE THR LEU SEQRES 7 L 112 LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL TYR SEQRES 8 L 112 TYR CYS MET GLN ALA VAL GLN THR PRO TRP THR PHE GLY SEQRES 9 L 112 GLN GLY THR LYS VAL GLU ILE LYS SEQRES 1 A 393 GLU PHE LEU ASN ASN THR GLU PRO LEU CYS ASN VAL SER SEQRES 2 A 393 GLY PHE ALA ILE VAL SER LYS ASP ASN GLY ILE ARG ILE SEQRES 3 A 393 GLY SER ARG GLY HIS VAL PHE VAL ILE ARG GLU PRO PHE SEQRES 4 A 393 VAL ALA CYS GLY PRO THR GLU CYS ARG THR PHE PHE LEU SEQRES 5 A 393 THR GLN GLY ALA LEU LEU ASN ASP LYS HIS SER ASN ASN SEQRES 6 A 393 THR VAL LYS ASP ARG SER PRO TYR ARG ALA LEU MET SER SEQRES 7 A 393 VAL PRO LEU GLY SER SER PRO ASN ALA TYR GLN ALA LYS SEQRES 8 A 393 PHE GLU SER VAL ALA TRP SER ALA THR ALA CYS HIS ASP SEQRES 9 A 393 GLY LYS LYS TRP LEU ALA VAL GLY ILE SER GLY ALA ASP SEQRES 10 A 393 ASP ASP ALA TYR ALA VAL ILE HIS TYR GLY GLY MET PRO SEQRES 11 A 393 THR ASP VAL VAL ARG SER TRP ARG LYS GLN ILE LEU ARG SEQRES 12 A 393 THR GLN GLU SER SER CYS VAL CYS MET ASN GLY ASN CYS SEQRES 13 A 393 TYR TRP VAL MET THR ASP GLY PRO ALA ASN SER GLN ALA SEQRES 14 A 393 SER TYR LYS ILE PHE LYS SER HIS GLU GLY MET VAL THR SEQRES 15 A 393 ASN GLU ARG GLU VAL SER PHE GLN GLY GLY HIS ILE GLU SEQRES 16 A 393 GLU CYS SER CYS TYR PRO ASN LEU GLY LYS VAL GLU CYS SEQRES 17 A 393 VAL CYS ARG ASP ASN TRP ASN GLY MET ASN ARG PRO ILE SEQRES 18 A 393 LEU ILE PHE ASP GLU ASP LEU ASP TYR GLU VAL GLY TYR SEQRES 19 A 393 LEU CYS ALA GLY ILE PRO THR ASP THR PRO ARG VAL GLN SEQRES 20 A 393 ASP SER SER PHE THR GLY SER CYS THR ASN ALA VAL GLY SEQRES 21 A 393 GLY SER GLY THR ASN ASN TYR GLY VAL LYS GLY PHE GLY SEQRES 22 A 393 PHE ARG GLN GLY ASN SER VAL TRP ALA GLY ARG THR VAL SEQRES 23 A 393 SER ILE SER SER ARG SER GLY PHE GLU ILE LEU LEU ILE SEQRES 24 A 393 GLU ASP GLY TRP ILE ARG THR SER LYS THR ILE VAL LYS SEQRES 25 A 393 LYS VAL GLU VAL LEU ASN ASN LYS ASN TRP SER GLY TYR SEQRES 26 A 393 SER GLY ALA PHE THR ILE PRO ILE THR MET THR SER LYS SEQRES 27 A 393 GLN CYS LEU VAL PRO CYS PHE TRP LEU GLU MET ILE ARG SEQRES 28 A 393 GLY LYS PRO GLU GLU ARG THR SER ILE TRP THR SER SER SEQRES 29 A 393 SER SER THR VAL PHE CYS GLY VAL SER SER GLU VAL PRO SEQRES 30 A 393 GLY TRP SER TRP ASP ASP GLY ALA ILE LEU PRO PHE ASP SEQRES 31 A 393 ILE ASP LYS SEQRES 1 I 117 LEU VAL LYS PRO SER GLU THR LEU SER LEU THR CYS SER SEQRES 2 I 117 VAL SER GLY GLU SER ILE SER SER GLY GLY TYR TYR TRP SEQRES 3 I 117 THR TRP ILE ARG GLN HIS PRO GLY LYS GLY LEU GLU TRP SEQRES 4 I 117 ILE GLY ASN ILE PHE ASP THR GLY SER THR HIS TYR SER SEQRES 5 I 117 PRO SER LEU LYS THR ARG LEU THR ILE SER ILE ASP THR SEQRES 6 I 117 SER LYS ASN GLN PHE TYR LEU ARG LEU ASN SER ALA THR SEQRES 7 I 117 ALA ALA ASP THR ALA VAL TYR TYR CYS ALA ARG VAL GLY SEQRES 8 I 117 TYR SER LEU GLU THR ASP ARG PRO TYR TYR PHE GLY LEU SEQRES 9 I 117 ASP VAL TRP GLY GLN GLY THR THR VAL THR VAL SER SER SEQRES 1 M 112 ASP ILE VAL MET THR GLN SER PRO LEU SER LEU PRO VAL SEQRES 2 M 112 THR PRO GLY GLU PRO ALA SER ILE SER CYS ARG SER SER SEQRES 3 M 112 GLN SER LEU LEU HIS SER ASN GLY TYR THR TYR LEU ASP SEQRES 4 M 112 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 M 112 ILE TYR LEU ALA SER ASN ARG ALA SER GLY VAL PRO ASP SEQRES 6 M 112 ARG PHE SER GLY SER GLY SER GLY THR TYR PHE THR LEU SEQRES 7 M 112 LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL TYR SEQRES 8 M 112 TYR CYS MET GLN ALA VAL GLN THR PRO TRP THR PHE GLY SEQRES 9 M 112 GLN GLY THR LYS VAL GLU ILE LYS SEQRES 1 D 393 GLU PHE LEU ASN ASN THR GLU PRO LEU CYS ASN VAL SER SEQRES 2 D 393 GLY PHE ALA ILE VAL SER LYS ASP ASN GLY ILE ARG ILE SEQRES 3 D 393 GLY SER ARG GLY HIS VAL PHE VAL ILE ARG GLU PRO PHE SEQRES 4 D 393 VAL ALA CYS GLY PRO THR GLU CYS ARG THR PHE PHE LEU SEQRES 5 D 393 THR GLN GLY ALA LEU LEU ASN ASP LYS HIS SER ASN ASN SEQRES 6 D 393 THR VAL LYS ASP ARG SER PRO TYR ARG ALA LEU MET SER SEQRES 7 D 393 VAL PRO LEU GLY SER SER PRO ASN ALA TYR GLN ALA LYS SEQRES 8 D 393 PHE GLU SER VAL ALA TRP SER ALA THR ALA CYS HIS ASP SEQRES 9 D 393 GLY LYS LYS TRP LEU ALA VAL GLY ILE SER GLY ALA ASP SEQRES 10 D 393 ASP ASP ALA TYR ALA VAL ILE HIS TYR GLY GLY MET PRO SEQRES 11 D 393 THR ASP VAL VAL ARG SER TRP ARG LYS GLN ILE LEU ARG SEQRES 12 D 393 THR GLN GLU SER SER CYS VAL CYS MET ASN GLY ASN CYS SEQRES 13 D 393 TYR TRP VAL MET THR ASP GLY PRO ALA ASN SER GLN ALA SEQRES 14 D 393 SER TYR LYS ILE PHE LYS SER HIS GLU GLY MET VAL THR SEQRES 15 D 393 ASN GLU ARG GLU VAL SER PHE GLN GLY GLY HIS ILE GLU SEQRES 16 D 393 GLU CYS SER CYS TYR PRO ASN LEU GLY LYS VAL GLU CYS SEQRES 17 D 393 VAL CYS ARG ASP ASN TRP ASN GLY MET ASN ARG PRO ILE SEQRES 18 D 393 LEU ILE PHE ASP GLU ASP LEU ASP TYR GLU VAL GLY TYR SEQRES 19 D 393 LEU CYS ALA GLY ILE PRO THR ASP THR PRO ARG VAL GLN SEQRES 20 D 393 ASP SER SER PHE THR GLY SER CYS THR ASN ALA VAL GLY SEQRES 21 D 393 GLY SER GLY THR ASN ASN TYR GLY VAL LYS GLY PHE GLY SEQRES 22 D 393 PHE ARG GLN GLY ASN SER VAL TRP ALA GLY ARG THR VAL SEQRES 23 D 393 SER ILE SER SER ARG SER GLY PHE GLU ILE LEU LEU ILE SEQRES 24 D 393 GLU ASP GLY TRP ILE ARG THR SER LYS THR ILE VAL LYS SEQRES 25 D 393 LYS VAL GLU VAL LEU ASN ASN LYS ASN TRP SER GLY TYR SEQRES 26 D 393 SER GLY ALA PHE THR ILE PRO ILE THR MET THR SER LYS SEQRES 27 D 393 GLN CYS LEU VAL PRO CYS PHE TRP LEU GLU MET ILE ARG SEQRES 28 D 393 GLY LYS PRO GLU GLU ARG THR SER ILE TRP THR SER SER SEQRES 29 D 393 SER SER THR VAL PHE CYS GLY VAL SER SER GLU VAL PRO SEQRES 30 D 393 GLY TRP SER TRP ASP ASP GLY ALA ILE LEU PRO PHE ASP SEQRES 31 D 393 ILE ASP LYS SEQRES 1 N 117 LEU VAL LYS PRO SER GLU THR LEU SER LEU THR CYS SER SEQRES 2 N 117 VAL SER GLY GLU SER ILE SER SER GLY GLY TYR TYR TRP SEQRES 3 N 117 THR TRP ILE ARG GLN HIS PRO GLY LYS GLY LEU GLU TRP SEQRES 4 N 117 ILE GLY ASN ILE PHE ASP THR GLY SER THR HIS TYR SER SEQRES 5 N 117 PRO SER LEU LYS THR ARG LEU THR ILE SER ILE ASP THR SEQRES 6 N 117 SER LYS ASN GLN PHE TYR LEU ARG LEU ASN SER ALA THR SEQRES 7 N 117 ALA ALA ASP THR ALA VAL TYR TYR CYS ALA ARG VAL GLY SEQRES 8 N 117 TYR SER LEU GLU THR ASP ARG PRO TYR TYR PHE GLY LEU SEQRES 9 N 117 ASP VAL TRP GLY GLN GLY THR THR VAL THR VAL SER SER SEQRES 1 O 112 ASP ILE VAL MET THR GLN SER PRO LEU SER LEU PRO VAL SEQRES 2 O 112 THR PRO GLY GLU PRO ALA SER ILE SER CYS ARG SER SER SEQRES 3 O 112 GLN SER LEU LEU HIS SER ASN GLY TYR THR TYR LEU ASP SEQRES 4 O 112 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 O 112 ILE TYR LEU ALA SER ASN ARG ALA SER GLY VAL PRO ASP SEQRES 6 O 112 ARG PHE SER GLY SER GLY SER GLY THR TYR PHE THR LEU SEQRES 7 O 112 LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL TYR SEQRES 8 O 112 TYR CYS MET GLN ALA VAL GLN THR PRO TRP THR PHE GLY SEQRES 9 O 112 GLN GLY THR LYS VAL GLU ILE LYS SEQRES 1 G 393 GLU PHE LEU ASN ASN THR GLU PRO LEU CYS ASN VAL SER SEQRES 2 G 393 GLY PHE ALA ILE VAL SER LYS ASP ASN GLY ILE ARG ILE SEQRES 3 G 393 GLY SER ARG GLY HIS VAL PHE VAL ILE ARG GLU PRO PHE SEQRES 4 G 393 VAL ALA CYS GLY PRO THR GLU CYS ARG THR PHE PHE LEU SEQRES 5 G 393 THR GLN GLY ALA LEU LEU ASN ASP LYS HIS SER ASN ASN SEQRES 6 G 393 THR VAL LYS ASP ARG SER PRO TYR ARG ALA LEU MET SER SEQRES 7 G 393 VAL PRO LEU GLY SER SER PRO ASN ALA TYR GLN ALA LYS SEQRES 8 G 393 PHE GLU SER VAL ALA TRP SER ALA THR ALA CYS HIS ASP SEQRES 9 G 393 GLY LYS LYS TRP LEU ALA VAL GLY ILE SER GLY ALA ASP SEQRES 10 G 393 ASP ASP ALA TYR ALA VAL ILE HIS TYR GLY GLY MET PRO SEQRES 11 G 393 THR ASP VAL VAL ARG SER TRP ARG LYS GLN ILE LEU ARG SEQRES 12 G 393 THR GLN GLU SER SER CYS VAL CYS MET ASN GLY ASN CYS SEQRES 13 G 393 TYR TRP VAL MET THR ASP GLY PRO ALA ASN SER GLN ALA SEQRES 14 G 393 SER TYR LYS ILE PHE LYS SER HIS GLU GLY MET VAL THR SEQRES 15 G 393 ASN GLU ARG GLU VAL SER PHE GLN GLY GLY HIS ILE GLU SEQRES 16 G 393 GLU CYS SER CYS TYR PRO ASN LEU GLY LYS VAL GLU CYS SEQRES 17 G 393 VAL CYS ARG ASP ASN TRP ASN GLY MET ASN ARG PRO ILE SEQRES 18 G 393 LEU ILE PHE ASP GLU ASP LEU ASP TYR GLU VAL GLY TYR SEQRES 19 G 393 LEU CYS ALA GLY ILE PRO THR ASP THR PRO ARG VAL GLN SEQRES 20 G 393 ASP SER SER PHE THR GLY SER CYS THR ASN ALA VAL GLY SEQRES 21 G 393 GLY SER GLY THR ASN ASN TYR GLY VAL LYS GLY PHE GLY SEQRES 22 G 393 PHE ARG GLN GLY ASN SER VAL TRP ALA GLY ARG THR VAL SEQRES 23 G 393 SER ILE SER SER ARG SER GLY PHE GLU ILE LEU LEU ILE SEQRES 24 G 393 GLU ASP GLY TRP ILE ARG THR SER LYS THR ILE VAL LYS SEQRES 25 G 393 LYS VAL GLU VAL LEU ASN ASN LYS ASN TRP SER GLY TYR SEQRES 26 G 393 SER GLY ALA PHE THR ILE PRO ILE THR MET THR SER LYS SEQRES 27 G 393 GLN CYS LEU VAL PRO CYS PHE TRP LEU GLU MET ILE ARG SEQRES 28 G 393 GLY LYS PRO GLU GLU ARG THR SER ILE TRP THR SER SER SEQRES 29 G 393 SER SER THR VAL PHE CYS GLY VAL SER SER GLU VAL PRO SEQRES 30 G 393 GLY TRP SER TRP ASP ASP GLY ALA ILE LEU PRO PHE ASP SEQRES 31 G 393 ILE ASP LYS SEQRES 1 S 117 LEU VAL LYS PRO SER GLU THR LEU SER LEU THR CYS SER SEQRES 2 S 117 VAL SER GLY GLU SER ILE SER SER GLY GLY TYR TYR TRP SEQRES 3 S 117 THR TRP ILE ARG GLN HIS PRO GLY LYS GLY LEU GLU TRP SEQRES 4 S 117 ILE GLY ASN ILE PHE ASP THR GLY SER THR HIS TYR SER SEQRES 5 S 117 PRO SER LEU LYS THR ARG LEU THR ILE SER ILE ASP THR SEQRES 6 S 117 SER LYS ASN GLN PHE TYR LEU ARG LEU ASN SER ALA THR SEQRES 7 S 117 ALA ALA ASP THR ALA VAL TYR TYR CYS ALA ARG VAL GLY SEQRES 8 S 117 TYR SER LEU GLU THR ASP ARG PRO TYR TYR PHE GLY LEU SEQRES 9 S 117 ASP VAL TRP GLY GLN GLY THR THR VAL THR VAL SER SER SEQRES 1 T 112 ASP ILE VAL MET THR GLN SER PRO LEU SER LEU PRO VAL SEQRES 2 T 112 THR PRO GLY GLU PRO ALA SER ILE SER CYS ARG SER SER SEQRES 3 T 112 GLN SER LEU LEU HIS SER ASN GLY TYR THR TYR LEU ASP SEQRES 4 T 112 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 T 112 ILE TYR LEU ALA SER ASN ARG ALA SER GLY VAL PRO ASP SEQRES 6 T 112 ARG PHE SER GLY SER GLY SER GLY THR TYR PHE THR LEU SEQRES 7 T 112 LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL TYR SEQRES 8 T 112 TYR CYS MET GLN ALA VAL GLN THR PRO TRP THR PHE GLY SEQRES 9 T 112 GLN GLY THR LYS VAL GLU ILE LYS SEQRES 1 P 393 GLU PHE LEU ASN ASN THR GLU PRO LEU CYS ASN VAL SER SEQRES 2 P 393 GLY PHE ALA ILE VAL SER LYS ASP ASN GLY ILE ARG ILE SEQRES 3 P 393 GLY SER ARG GLY HIS VAL PHE VAL ILE ARG GLU PRO PHE SEQRES 4 P 393 VAL ALA CYS GLY PRO THR GLU CYS ARG THR PHE PHE LEU SEQRES 5 P 393 THR GLN GLY ALA LEU LEU ASN ASP LYS HIS SER ASN ASN SEQRES 6 P 393 THR VAL LYS ASP ARG SER PRO TYR ARG ALA LEU MET SER SEQRES 7 P 393 VAL PRO LEU GLY SER SER PRO ASN ALA TYR GLN ALA LYS SEQRES 8 P 393 PHE GLU SER VAL ALA TRP SER ALA THR ALA CYS HIS ASP SEQRES 9 P 393 GLY LYS LYS TRP LEU ALA VAL GLY ILE SER GLY ALA ASP SEQRES 10 P 393 ASP ASP ALA TYR ALA VAL ILE HIS TYR GLY GLY MET PRO SEQRES 11 P 393 THR ASP VAL VAL ARG SER TRP ARG LYS GLN ILE LEU ARG SEQRES 12 P 393 THR GLN GLU SER SER CYS VAL CYS MET ASN GLY ASN CYS SEQRES 13 P 393 TYR TRP VAL MET THR ASP GLY PRO ALA ASN SER GLN ALA SEQRES 14 P 393 SER TYR LYS ILE PHE LYS SER HIS GLU GLY MET VAL THR SEQRES 15 P 393 ASN GLU ARG GLU VAL SER PHE GLN GLY GLY HIS ILE GLU SEQRES 16 P 393 GLU CYS SER CYS TYR PRO ASN LEU GLY LYS VAL GLU CYS SEQRES 17 P 393 VAL CYS ARG ASP ASN TRP ASN GLY MET ASN ARG PRO ILE SEQRES 18 P 393 LEU ILE PHE ASP GLU ASP LEU ASP TYR GLU VAL GLY TYR SEQRES 19 P 393 LEU CYS ALA GLY ILE PRO THR ASP THR PRO ARG VAL GLN SEQRES 20 P 393 ASP SER SER PHE THR GLY SER CYS THR ASN ALA VAL GLY SEQRES 21 P 393 GLY SER GLY THR ASN ASN TYR GLY VAL LYS GLY PHE GLY SEQRES 22 P 393 PHE ARG GLN GLY ASN SER VAL TRP ALA GLY ARG THR VAL SEQRES 23 P 393 SER ILE SER SER ARG SER GLY PHE GLU ILE LEU LEU ILE SEQRES 24 P 393 GLU ASP GLY TRP ILE ARG THR SER LYS THR ILE VAL LYS SEQRES 25 P 393 LYS VAL GLU VAL LEU ASN ASN LYS ASN TRP SER GLY TYR SEQRES 26 P 393 SER GLY ALA PHE THR ILE PRO ILE THR MET THR SER LYS SEQRES 27 P 393 GLN CYS LEU VAL PRO CYS PHE TRP LEU GLU MET ILE ARG SEQRES 28 P 393 GLY LYS PRO GLU GLU ARG THR SER ILE TRP THR SER SER SEQRES 29 P 393 SER SER THR VAL PHE CYS GLY VAL SER SER GLU VAL PRO SEQRES 30 P 393 GLY TRP SER TRP ASP ASP GLY ALA ILE LEU PRO PHE ASP SEQRES 31 P 393 ILE ASP LYS HET NAG A 401 28 HET NAG A 402 28 HET CA A 403 1 HET NAG D 401 28 HET NAG D 402 28 HET CA D 403 1 HET NAG G 401 28 HET NAG G 402 28 HET CA G 403 1 HET NAG P 401 28 HET NAG P 402 28 HET CA P 403 1 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM CA CALCIUM 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 FORMUL 13 NAG 8(C8 H15 N O6) FORMUL 15 CA 4(CA 2+) FORMUL 25 HOH *136(H2 O) HELIX 1 AA1 PRO H 53 LYS H 56 5 4 HELIX 2 AA2 THR H 78 THR H 82 5 5 HELIX 3 AA3 GLU L 84 VAL L 88 5 5 HELIX 4 AA4 ASN A 21 SER A 27 1 7 HELIX 5 AA5 ASP A 59 ASN A 63 5 5 HELIX 6 AA6 ALA A 115 ASP A 118 5 4 HELIX 7 AA7 PRO A 331 SER A 336 1 6 HELIX 8 AA8 PRO I 53 LYS I 56 5 4 HELIX 9 AA9 THR I 78 THR I 82 5 5 HELIX 10 AB1 ASN D 21 GLY D 26 1 6 HELIX 11 AB2 ASP D 59 ASN D 63 5 5 HELIX 12 AB3 ALA D 115 ASP D 118 5 4 HELIX 13 AB4 PRO D 331 SER D 336 1 6 HELIX 14 AB5 PHE D 388 LYS D 392 5 5 HELIX 15 AB6 PRO N 53 LYS N 56 5 4 HELIX 16 AB7 THR N 65 LYS N 67 5 3 HELIX 17 AB8 THR N 78 THR N 82 5 5 HELIX 18 AB9 GLU O 84 VAL O 88 5 5 HELIX 19 AC1 ASN G 21 GLY G 26 1 6 HELIX 20 AC2 ASP G 59 ASN G 63 5 5 HELIX 21 AC3 ALA G 115 ASP G 118 5 4 HELIX 22 AC4 PRO G 331 SER G 336 1 6 HELIX 23 AC5 PRO S 53 LYS S 56 5 4 HELIX 24 AC6 THR S 78 THR S 82 5 5 HELIX 25 AC7 GLU T 84 VAL T 88 5 5 HELIX 26 AC8 ASN P 21 GLY P 26 1 6 HELIX 27 AC9 ASP P 59 ASN P 63 5 5 HELIX 28 AD1 ALA P 115 ASP P 118 5 4 HELIX 29 AD2 PRO P 331 SER P 336 1 6 HELIX 30 AD3 PHE P 388 LYS P 392 5 5 SHEET 1 AA1 3 LEU H 8 SER H 13 0 SHEET 2 AA1 3 GLN H 69 LEU H 74 -1 O LEU H 74 N LEU H 8 SHEET 3 AA1 3 LEU H 59 ASP H 64 -1 N SER H 62 O TYR H 71 SHEET 1 AA2 5 THR H 49 TYR H 51 0 SHEET 2 AA2 5 LEU H 37 PHE H 44 -1 N ASN H 42 O HIS H 50 SHEET 3 AA2 5 TYR H 25 GLN H 31 -1 N ARG H 30 O GLU H 38 SHEET 4 AA2 5 ALA H 83 SER H 93 -1 O TYR H 86 N ILE H 29 SHEET 5 AA2 5 TYR H 100 TRP H 107 -1 O PHE H 102 N GLY H 91 SHEET 1 AA3 5 THR H 49 TYR H 51 0 SHEET 2 AA3 5 LEU H 37 PHE H 44 -1 N ASN H 42 O HIS H 50 SHEET 3 AA3 5 TYR H 25 GLN H 31 -1 N ARG H 30 O GLU H 38 SHEET 4 AA3 5 ALA H 83 SER H 93 -1 O TYR H 86 N ILE H 29 SHEET 5 AA3 5 THR H 111 VAL H 113 -1 O THR H 111 N TYR H 85 SHEET 1 AA4 4 MET L 4 GLN L 6 0 SHEET 2 AA4 4 ALA L 19 SER L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA4 4 TYR L 75 ILE L 80 -1 O LEU L 78 N ILE L 21 SHEET 4 AA4 4 PHE L 67 SER L 72 -1 N SER L 68 O LYS L 79 SHEET 1 AA5 6 SER L 10 VAL L 13 0 SHEET 2 AA5 6 THR L 107 ILE L 111 1 O LYS L 108 N LEU L 11 SHEET 3 AA5 6 VAL L 90 GLN L 95 -1 N TYR L 91 O THR L 107 SHEET 4 AA5 6 LEU L 38 GLN L 43 -1 N TYR L 41 O TYR L 92 SHEET 5 AA5 6 PRO L 49 LEU L 55 -1 O GLN L 50 N LEU L 42 SHEET 6 AA5 6 ASN L 58 ARG L 59 -1 O ASN L 58 N TYR L 54 SHEET 1 AA6 4 SER L 10 VAL L 13 0 SHEET 2 AA6 4 THR L 107 ILE L 111 1 O LYS L 108 N LEU L 11 SHEET 3 AA6 4 VAL L 90 GLN L 95 -1 N TYR L 91 O THR L 107 SHEET 4 AA6 4 THR L 102 PHE L 103 -1 O THR L 102 N GLN L 95 SHEET 1 AA7 4 GLY A 13 LYS A 19 0 SHEET 2 AA7 4 THR A 361 VAL A 371 -1 O VAL A 371 N GLY A 13 SHEET 3 AA7 4 VAL A 341 GLY A 351 -1 N PHE A 344 O PHE A 368 SHEET 4 AA7 4 SER A 325 ILE A 330 -1 N PHE A 328 O CYS A 343 SHEET 1 AA8 4 PRO A 37 CYS A 41 0 SHEET 2 AA8 4 CYS A 46 THR A 52 -1 O ARG A 47 N ALA A 40 SHEET 3 AA8 4 ALA A 74 PRO A 79 -1 O VAL A 78 N THR A 48 SHEET 4 AA8 4 LYS A 90 VAL A 94 -1 O LYS A 90 N SER A 77 SHEET 1 AA9 4 SER A 97 HIS A 102 0 SHEET 2 AA9 4 TRP A 107 SER A 113 -1 O LEU A 108 N CYS A 101 SHEET 3 AA9 4 TYR A 120 TYR A 125 -1 O HIS A 124 N ALA A 109 SHEET 4 AA9 4 PRO A 129 ARG A 134 -1 O VAL A 133 N ALA A 121 SHEET 1 AB1 3 ARG A 142 THR A 143 0 SHEET 2 AB1 3 ASN A 154 ASP A 161 -1 O THR A 160 N ARG A 142 SHEET 3 AB1 3 VAL A 149 MET A 151 -1 N VAL A 149 O TYR A 156 SHEET 1 AB2 4 ARG A 142 THR A 143 0 SHEET 2 AB2 4 ASN A 154 ASP A 161 -1 O THR A 160 N ARG A 142 SHEET 3 AB2 4 SER A 169 HIS A 176 -1 O LYS A 171 N MET A 159 SHEET 4 AB2 4 MET A 179 GLU A 185 -1 O ARG A 184 N ILE A 172 SHEET 1 AB3 4 SER A 197 ASN A 201 0 SHEET 2 AB3 4 LYS A 204 VAL A 208 -1 O LYS A 204 N ASN A 201 SHEET 3 AB3 4 PRO A 219 PHE A 223 -1 O LEU A 221 N CYS A 207 SHEET 4 AB3 4 TYR A 229 TYR A 233 -1 O GLY A 232 N ILE A 220 SHEET 1 AB4 4 GLY A 272 GLN A 275 0 SHEET 2 AB4 4 SER A 278 ARG A 283 -1 O SER A 278 N GLN A 275 SHEET 3 AB4 4 SER A 291 ILE A 298 -1 O GLU A 294 N ARG A 283 SHEET 4 AB4 4 ILE A 309 TRP A 321 -1 O VAL A 310 N LEU A 297 SHEET 1 AB5 3 LEU I 8 SER I 13 0 SHEET 2 AB5 3 GLN I 69 LEU I 74 -1 O LEU I 74 N LEU I 8 SHEET 3 AB5 3 LEU I 59 ASP I 64 -1 N SER I 62 O TYR I 71 SHEET 1 AB6 5 THR I 49 TYR I 51 0 SHEET 2 AB6 5 LEU I 37 ILE I 43 -1 N ASN I 42 O HIS I 50 SHEET 3 AB6 5 TYR I 25 GLN I 31 -1 N ARG I 30 O GLU I 38 SHEET 4 AB6 5 ALA I 83 SER I 93 -1 O TYR I 86 N ILE I 29 SHEET 5 AB6 5 TYR I 100 TRP I 107 -1 O PHE I 102 N GLY I 91 SHEET 1 AB7 5 THR I 49 TYR I 51 0 SHEET 2 AB7 5 LEU I 37 ILE I 43 -1 N ASN I 42 O HIS I 50 SHEET 3 AB7 5 TYR I 25 GLN I 31 -1 N ARG I 30 O GLU I 38 SHEET 4 AB7 5 ALA I 83 SER I 93 -1 O TYR I 86 N ILE I 29 SHEET 5 AB7 5 THR I 111 VAL I 113 -1 O THR I 111 N TYR I 85 SHEET 1 AB8 4 MET M 4 GLN M 6 0 SHEET 2 AB8 4 ALA M 19 SER M 25 -1 O ARG M 24 N THR M 5 SHEET 3 AB8 4 TYR M 75 ILE M 80 -1 O PHE M 76 N CYS M 23 SHEET 4 AB8 4 PHE M 67 SER M 72 -1 N SER M 68 O LYS M 79 SHEET 1 AB9 6 SER M 10 VAL M 13 0 SHEET 2 AB9 6 THR M 107 ILE M 111 1 O LYS M 108 N LEU M 11 SHEET 3 AB9 6 GLY M 89 GLN M 95 -1 N TYR M 91 O THR M 107 SHEET 4 AB9 6 LEU M 38 GLN M 43 -1 N TYR M 41 O TYR M 92 SHEET 5 AB9 6 PRO M 49 LEU M 55 -1 O GLN M 50 N LEU M 42 SHEET 6 AB9 6 ASN M 58 ARG M 59 -1 O ASN M 58 N TYR M 54 SHEET 1 AC1 4 SER M 10 VAL M 13 0 SHEET 2 AC1 4 THR M 107 ILE M 111 1 O LYS M 108 N LEU M 11 SHEET 3 AC1 4 GLY M 89 GLN M 95 -1 N TYR M 91 O THR M 107 SHEET 4 AC1 4 THR M 102 PHE M 103 -1 O THR M 102 N GLN M 95 SHEET 1 AC2 4 GLY D 13 LYS D 19 0 SHEET 2 AC2 4 THR D 361 VAL D 371 -1 O VAL D 371 N GLY D 13 SHEET 3 AC2 4 VAL D 341 GLY D 351 -1 N PRO D 342 O GLY D 370 SHEET 4 AC2 4 SER D 325 ILE D 330 -1 N PHE D 328 O CYS D 343 SHEET 1 AC3 4 PHE D 32 CYS D 41 0 SHEET 2 AC3 4 CYS D 46 LEU D 56 -1 O ARG D 47 N ALA D 40 SHEET 3 AC3 4 ALA D 74 PRO D 79 -1 O VAL D 78 N THR D 48 SHEET 4 AC3 4 LYS D 90 SER D 93 -1 O SER D 93 N LEU D 75 SHEET 1 AC4 4 SER D 97 HIS D 102 0 SHEET 2 AC4 4 TRP D 107 SER D 113 -1 O VAL D 110 N THR D 99 SHEET 3 AC4 4 TYR D 120 TYR D 125 -1 O HIS D 124 N ALA D 109 SHEET 4 AC4 4 PRO D 129 ARG D 134 -1 O VAL D 133 N ALA D 121 SHEET 1 AC5 3 ARG D 142 THR D 143 0 SHEET 2 AC5 3 ASN D 154 ASP D 161 -1 O THR D 160 N ARG D 142 SHEET 3 AC5 3 VAL D 149 MET D 151 -1 N MET D 151 O ASN D 154 SHEET 1 AC6 4 ARG D 142 THR D 143 0 SHEET 2 AC6 4 ASN D 154 ASP D 161 -1 O THR D 160 N ARG D 142 SHEET 3 AC6 4 SER D 169 HIS D 176 -1 O SER D 175 N CYS D 155 SHEET 4 AC6 4 MET D 179 VAL D 186 -1 O ARG D 184 N ILE D 172 SHEET 1 AC7 4 SER D 197 ASN D 201 0 SHEET 2 AC7 4 LYS D 204 VAL D 208 -1 O LYS D 204 N ASN D 201 SHEET 3 AC7 4 PRO D 219 PHE D 223 -1 O PHE D 223 N VAL D 205 SHEET 4 AC7 4 TYR D 229 TYR D 233 -1 O GLY D 232 N ILE D 220 SHEET 1 AC8 4 GLY D 272 GLN D 275 0 SHEET 2 AC8 4 SER D 278 THR D 284 -1 O SER D 278 N GLN D 275 SHEET 3 AC8 4 SER D 291 ILE D 298 -1 O GLU D 294 N ARG D 283 SHEET 4 AC8 4 ILE D 309 TRP D 321 -1 O VAL D 310 N LEU D 297 SHEET 1 AC9 3 LEU N 8 SER N 13 0 SHEET 2 AC9 3 GLN N 69 LEU N 74 -1 O LEU N 74 N LEU N 8 SHEET 3 AC9 3 LEU N 59 ASP N 64 -1 N SER N 62 O TYR N 71 SHEET 1 AD1 5 THR N 49 TYR N 51 0 SHEET 2 AD1 5 LEU N 37 PHE N 44 -1 N ASN N 42 O HIS N 50 SHEET 3 AD1 5 TYR N 25 GLN N 31 -1 N TRP N 26 O ILE N 43 SHEET 4 AD1 5 ALA N 83 SER N 93 -1 O TYR N 86 N ILE N 29 SHEET 5 AD1 5 TYR N 100 TRP N 107 -1 O PHE N 102 N GLY N 91 SHEET 1 AD2 5 THR N 49 TYR N 51 0 SHEET 2 AD2 5 LEU N 37 PHE N 44 -1 N ASN N 42 O HIS N 50 SHEET 3 AD2 5 TYR N 25 GLN N 31 -1 N TRP N 26 O ILE N 43 SHEET 4 AD2 5 ALA N 83 SER N 93 -1 O TYR N 86 N ILE N 29 SHEET 5 AD2 5 THR N 111 VAL N 113 -1 O THR N 111 N TYR N 85 SHEET 1 AD3 4 MET O 4 GLN O 6 0 SHEET 2 AD3 4 ALA O 19 SER O 25 -1 O ARG O 24 N THR O 5 SHEET 3 AD3 4 TYR O 75 ILE O 80 -1 O LEU O 78 N ILE O 21 SHEET 4 AD3 4 PHE O 67 SER O 72 -1 N SER O 68 O LYS O 79 SHEET 1 AD4 6 SER O 10 VAL O 13 0 SHEET 2 AD4 6 THR O 107 ILE O 111 1 O GLU O 110 N VAL O 13 SHEET 3 AD4 6 GLY O 89 GLN O 95 -1 N TYR O 91 O THR O 107 SHEET 4 AD4 6 LEU O 38 GLN O 43 -1 N TYR O 41 O TYR O 92 SHEET 5 AD4 6 PRO O 49 LEU O 55 -1 O GLN O 50 N LEU O 42 SHEET 6 AD4 6 ASN O 58 ARG O 59 -1 O ASN O 58 N TYR O 54 SHEET 1 AD5 4 SER O 10 VAL O 13 0 SHEET 2 AD5 4 THR O 107 ILE O 111 1 O GLU O 110 N VAL O 13 SHEET 3 AD5 4 GLY O 89 GLN O 95 -1 N TYR O 91 O THR O 107 SHEET 4 AD5 4 THR O 102 PHE O 103 -1 O THR O 102 N GLN O 95 SHEET 1 AD6 4 GLY G 13 LYS G 19 0 SHEET 2 AD6 4 THR G 361 VAL G 371 -1 O VAL G 367 N VAL G 17 SHEET 3 AD6 4 VAL G 341 GLY G 351 -1 N PHE G 344 O PHE G 368 SHEET 4 AD6 4 SER G 325 ILE G 330 -1 N PHE G 328 O CYS G 343 SHEET 1 AD7 4 PHE G 32 CYS G 41 0 SHEET 2 AD7 4 CYS G 46 LEU G 56 -1 O ARG G 47 N ALA G 40 SHEET 3 AD7 4 ALA G 74 PRO G 79 -1 O VAL G 78 N THR G 48 SHEET 4 AD7 4 LYS G 90 VAL G 94 -1 O GLU G 92 N LEU G 75 SHEET 1 AD8 4 ALA G 98 HIS G 102 0 SHEET 2 AD8 4 TRP G 107 SER G 113 -1 O VAL G 110 N THR G 99 SHEET 3 AD8 4 TYR G 120 TYR G 125 -1 O HIS G 124 N ALA G 109 SHEET 4 AD8 4 PRO G 129 ARG G 134 -1 O VAL G 133 N ALA G 121 SHEET 1 AD9 3 LEU G 141 THR G 143 0 SHEET 2 AD9 3 ASN G 154 ASP G 161 -1 O THR G 160 N ARG G 142 SHEET 3 AD9 3 VAL G 149 MET G 151 -1 N MET G 151 O ASN G 154 SHEET 1 AE1 4 LEU G 141 THR G 143 0 SHEET 2 AE1 4 ASN G 154 ASP G 161 -1 O THR G 160 N ARG G 142 SHEET 3 AE1 4 SER G 169 HIS G 176 -1 O PHE G 173 N TRP G 157 SHEET 4 AE1 4 MET G 179 VAL G 186 -1 O THR G 181 N LYS G 174 SHEET 1 AE2 4 SER G 197 ASN G 201 0 SHEET 2 AE2 4 LYS G 204 VAL G 208 -1 O GLU G 206 N TYR G 199 SHEET 3 AE2 4 PRO G 219 PHE G 223 -1 O PHE G 223 N VAL G 205 SHEET 4 AE2 4 TYR G 229 TYR G 233 -1 O GLY G 232 N ILE G 220 SHEET 1 AE3 4 GLY G 272 GLN G 275 0 SHEET 2 AE3 4 SER G 278 ARG G 283 -1 O SER G 278 N GLN G 275 SHEET 3 AE3 4 SER G 291 ILE G 298 -1 O GLU G 294 N ARG G 283 SHEET 4 AE3 4 ILE G 309 TRP G 321 -1 O VAL G 310 N LEU G 297 SHEET 1 AE4 3 LEU S 8 SER S 13 0 SHEET 2 AE4 3 GLN S 69 LEU S 74 -1 O LEU S 74 N LEU S 8 SHEET 3 AE4 3 LEU S 59 ASP S 64 -1 N SER S 62 O TYR S 71 SHEET 1 AE5 5 THR S 49 TYR S 51 0 SHEET 2 AE5 5 LEU S 37 ILE S 43 -1 N ASN S 42 O HIS S 50 SHEET 3 AE5 5 TYR S 25 GLN S 31 -1 N TRP S 26 O ILE S 43 SHEET 4 AE5 5 ALA S 83 SER S 93 -1 O TYR S 86 N ILE S 29 SHEET 5 AE5 5 TYR S 100 TRP S 107 -1 O PHE S 102 N GLY S 91 SHEET 1 AE6 5 THR S 49 TYR S 51 0 SHEET 2 AE6 5 LEU S 37 ILE S 43 -1 N ASN S 42 O HIS S 50 SHEET 3 AE6 5 TYR S 25 GLN S 31 -1 N TRP S 26 O ILE S 43 SHEET 4 AE6 5 ALA S 83 SER S 93 -1 O TYR S 86 N ILE S 29 SHEET 5 AE6 5 THR S 111 VAL S 113 -1 O THR S 111 N TYR S 85 SHEET 1 AE7 4 MET T 4 GLN T 6 0 SHEET 2 AE7 4 ALA T 19 SER T 25 -1 O ARG T 24 N THR T 5 SHEET 3 AE7 4 TYR T 75 ILE T 80 -1 O LEU T 78 N ILE T 21 SHEET 4 AE7 4 PHE T 67 SER T 72 -1 N SER T 68 O LYS T 79 SHEET 1 AE8 5 SER T 10 VAL T 13 0 SHEET 2 AE8 5 THR T 107 ILE T 111 1 O LYS T 108 N LEU T 11 SHEET 3 AE8 5 VAL T 90 GLN T 95 -1 N TYR T 91 O THR T 107 SHEET 4 AE8 5 LEU T 38 GLN T 43 -1 N TYR T 41 O TYR T 92 SHEET 5 AE8 5 GLN T 50 ILE T 53 -1 O GLN T 50 N LEU T 42 SHEET 1 AE9 4 SER T 10 VAL T 13 0 SHEET 2 AE9 4 THR T 107 ILE T 111 1 O LYS T 108 N LEU T 11 SHEET 3 AE9 4 VAL T 90 GLN T 95 -1 N TYR T 91 O THR T 107 SHEET 4 AE9 4 THR T 102 PHE T 103 -1 O THR T 102 N GLN T 95 SHEET 1 AF1 4 GLY P 13 LYS P 19 0 SHEET 2 AF1 4 THR P 361 VAL P 371 -1 O VAL P 371 N GLY P 13 SHEET 3 AF1 4 VAL P 341 GLY P 351 -1 N PHE P 344 O PHE P 368 SHEET 4 AF1 4 SER P 325 ILE P 330 -1 N PHE P 328 O CYS P 343 SHEET 1 AF2 4 PRO P 37 CYS P 41 0 SHEET 2 AF2 4 CYS P 46 THR P 52 -1 O ARG P 47 N ALA P 40 SHEET 3 AF2 4 ALA P 74 PRO P 79 -1 O VAL P 78 N THR P 48 SHEET 4 AF2 4 LYS P 90 VAL P 94 -1 O LYS P 90 N SER P 77 SHEET 1 AF3 4 ALA P 98 HIS P 102 0 SHEET 2 AF3 4 TRP P 107 SER P 113 -1 O LEU P 108 N CYS P 101 SHEET 3 AF3 4 TYR P 120 TYR P 125 -1 O HIS P 124 N ALA P 109 SHEET 4 AF3 4 PRO P 129 ARG P 134 -1 O VAL P 133 N ALA P 121 SHEET 1 AF4 3 ARG P 142 THR P 143 0 SHEET 2 AF4 3 ASN P 154 ASP P 161 -1 O THR P 160 N ARG P 142 SHEET 3 AF4 3 VAL P 149 MET P 151 -1 N VAL P 149 O TYR P 156 SHEET 1 AF5 4 ARG P 142 THR P 143 0 SHEET 2 AF5 4 ASN P 154 ASP P 161 -1 O THR P 160 N ARG P 142 SHEET 3 AF5 4 SER P 169 HIS P 176 -1 O PHE P 173 N TRP P 157 SHEET 4 AF5 4 MET P 179 VAL P 186 -1 O ARG P 184 N ILE P 172 SHEET 1 AF6 4 CYS P 198 ASN P 201 0 SHEET 2 AF6 4 LYS P 204 VAL P 208 -1 O LYS P 204 N ASN P 201 SHEET 3 AF6 4 PRO P 219 PHE P 223 -1 O PHE P 223 N VAL P 205 SHEET 4 AF6 4 TYR P 229 TYR P 233 -1 O GLY P 232 N ILE P 220 SHEET 1 AF7 4 GLY P 272 GLN P 275 0 SHEET 2 AF7 4 SER P 278 ARG P 283 -1 O TRP P 280 N PHE P 273 SHEET 3 AF7 4 SER P 291 ILE P 298 -1 O GLU P 294 N ARG P 283 SHEET 4 AF7 4 ILE P 309 TRP P 321 -1 O VAL P 310 N LEU P 297 SSBOND 1 CYS H 12 CYS H 87 1555 1555 2.04 SSBOND 2 CYS A 41 CYS A 46 1555 1555 2.04 SSBOND 3 CYS A 101 CYS A 148 1555 1555 2.03 SSBOND 4 CYS A 150 CYS A 155 1555 1555 2.04 SSBOND 5 CYS A 196 CYS A 209 1555 1555 2.03 SSBOND 6 CYS A 198 CYS A 207 1555 1555 2.03 SSBOND 7 CYS A 235 CYS A 254 1555 1555 2.03 SSBOND 8 CYS A 343 CYS A 369 1555 1555 2.04 SSBOND 9 CYS I 12 CYS I 87 1555 1555 2.04 SSBOND 10 CYS D 41 CYS D 46 1555 1555 2.03 SSBOND 11 CYS D 101 CYS D 148 1555 1555 2.02 SSBOND 12 CYS D 150 CYS D 155 1555 1555 2.04 SSBOND 13 CYS D 196 CYS D 209 1555 1555 2.03 SSBOND 14 CYS D 198 CYS D 207 1555 1555 2.03 SSBOND 15 CYS D 235 CYS D 254 1555 1555 2.03 SSBOND 16 CYS D 343 CYS D 369 1555 1555 2.03 SSBOND 17 CYS N 12 CYS N 87 1555 1555 2.04 SSBOND 18 CYS G 41 CYS G 46 1555 1555 2.04 SSBOND 19 CYS G 101 CYS G 148 1555 1555 2.02 SSBOND 20 CYS G 150 CYS G 155 1555 1555 2.04 SSBOND 21 CYS G 196 CYS G 209 1555 1555 2.03 SSBOND 22 CYS G 198 CYS G 207 1555 1555 2.03 SSBOND 23 CYS G 235 CYS G 254 1555 1555 2.03 SSBOND 24 CYS G 343 CYS G 369 1555 1555 2.03 SSBOND 25 CYS S 12 CYS S 87 1555 1555 2.04 SSBOND 26 CYS P 41 CYS P 46 1555 1555 2.04 SSBOND 27 CYS P 101 CYS P 148 1555 1555 2.03 SSBOND 28 CYS P 150 CYS P 155 1555 1555 2.03 SSBOND 29 CYS P 196 CYS P 209 1555 1555 2.03 SSBOND 30 CYS P 198 CYS P 207 1555 1555 2.03 SSBOND 31 CYS P 235 CYS P 254 1555 1555 2.03 SSBOND 32 CYS P 343 CYS P 369 1555 1555 2.03 LINK ND2 ASN A 3 C1 NAG A 402 1555 1555 1.44 LINK ND2 ASN A 63 C1 NAG A 401 1555 1555 1.44 LINK ND2 ASN D 3 C1 NAG D 402 1555 1555 1.45 LINK ND2 ASN D 63 C1 NAG D 401 1555 1555 1.45 LINK ND2 ASN G 3 C1 NAG G 402 1555 1555 1.44 LINK ND2 ASN G 63 C1 NAG G 401 1555 1555 1.45 LINK ND2 ASN P 3 C1 NAG P 402 1555 1555 1.44 LINK ND2 ASN P 63 C1 NAG P 401 1555 1555 1.43 LINK O ASP A 211 CA CA A 403 1555 1555 2.58 LINK O GLY A 215 CA CA A 403 1555 1555 2.35 LINK OD2 ASP A 241 CA CA A 403 1555 1555 2.37 LINK O TYR A 266 CA CA A 403 1555 1555 2.43 LINK O ASP D 211 CA CA D 403 1555 1555 2.57 LINK O GLY D 215 CA CA D 403 1555 1555 2.39 LINK OD2 ASP D 241 CA CA D 403 1555 1555 2.37 LINK O TYR D 266 CA CA D 403 1555 1555 2.50 LINK O ASP G 211 CA CA G 403 1555 1555 2.56 LINK O GLY G 215 CA CA G 403 1555 1555 2.36 LINK OD2 ASP G 241 CA CA G 403 1555 1555 2.37 LINK O TYR G 266 CA CA G 403 1555 1555 2.40 LINK O ASP P 211 CA CA P 403 1555 1555 2.54 LINK O GLY P 215 CA CA P 403 1555 1555 2.43 LINK OD2 ASP P 241 CA CA P 403 1555 1555 2.50 LINK O TYR P 266 CA CA P 403 1555 1555 2.41 CISPEP 1 LEU A 386 PRO A 387 0 6.53 CISPEP 2 LEU D 386 PRO D 387 0 1.89 CISPEP 3 LEU G 386 PRO G 387 0 7.72 CISPEP 4 LEU P 386 PRO P 387 0 3.46 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000