HEADER VIRAL PROTEIN 27-NOV-24 9EJE TITLE NCS.1 FAB IN COMPLEX WITH N5 NA OF A/SHOREBIRD/DELAWARE BAY/309/2016 TITLE 2 (DB16, H10N5) -- 3 FABS COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEURAMINIDASE; COMPND 3 CHAIN: A, D, G, P; COMPND 4 EC: 3.2.1.18; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: NCS.1 HEAVY CHAIN; COMPND 8 CHAIN: H, I, S; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: NCS.1 LIGHT CHAIN; COMPND 12 CHAIN: L, M, T; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 3 ORGANISM_TAXID: 11320; SOURCE 4 GENE: NA; 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: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; 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, APO, KEYWDS 2 VIRAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR A.J.BORST REVDAT 1 13-AUG-25 9EJE 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. 4.18 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX 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) : 4.180 REMARK 3 NUMBER OF PARTICLES : 75643 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9EJE 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_1000290600. 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) -- 3 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: DECAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, G, H, I, L, M, P, S, T, REMARK 350 AND CHAINS: B, C, 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 MET A 393 REMARK 465 MET D 393 REMARK 465 VAL G 66 REMARK 465 LYS G 67 REMARK 465 MET G 393 REMARK 465 GLN H -9 REMARK 465 VAL H -8 REMARK 465 GLN H -7 REMARK 465 LEU H -6 REMARK 465 PRO H -5 REMARK 465 GLU H -4 REMARK 465 SER H -3 REMARK 465 GLY H -2 REMARK 465 PRO H -1 REMARK 465 ARG H 0 REMARK 465 GLN I -9 REMARK 465 VAL I -8 REMARK 465 GLN I -7 REMARK 465 LEU I -6 REMARK 465 PRO I -5 REMARK 465 GLU I -4 REMARK 465 SER I -3 REMARK 465 GLY I -2 REMARK 465 PRO I -1 REMARK 465 ARG I 0 REMARK 465 MET P 393 REMARK 465 GLN S -9 REMARK 465 VAL S -8 REMARK 465 GLN S -7 REMARK 465 LEU S -6 REMARK 465 PRO S -5 REMARK 465 GLU S -4 REMARK 465 SER S -3 REMARK 465 GLY S -2 REMARK 465 PRO S -1 REMARK 465 ARG S 0 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ARG G 35 CG CD NE CZ NH1 NH2 REMARK 470 GLU G 36 CG CD OE1 OE2 REMARK 470 ASP G 68 CG OD1 OD2 REMARK 470 GLU G 145 CG CD OE1 OE2 REMARK 470 GLU G 194 CG CD OE1 OE2 REMARK 470 GLU G 195 CG CD OE1 OE2 REMARK 470 ASN G 212 CG OD1 ND2 REMARK 470 LYS G 269 CG CD CE NZ 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 4 22.53 -143.31 REMARK 500 ASN A 58 -4.87 69.07 REMARK 500 ASN D 4 23.30 -143.57 REMARK 500 ARG D 28 -33.37 -130.17 REMARK 500 ASN D 58 -5.60 70.53 REMARK 500 ASN G 4 30.07 -143.81 REMARK 500 ARG G 28 -32.22 -130.15 REMARK 500 ASN G 64 19.74 55.56 REMARK 500 SER G 93 149.39 179.33 REMARK 500 ASP G 118 20.83 -141.33 REMARK 500 GLU G 145 59.56 -90.11 REMARK 500 ASN G 201 111.94 -162.57 REMARK 500 ASN G 214 -0.19 71.09 REMARK 500 THR G 240 42.76 -140.57 REMARK 500 ASN G 265 19.32 -145.53 REMARK 500 SER H 5 -1.44 75.36 REMARK 500 SER H 20 10.74 80.33 REMARK 500 ILE H 40 -63.01 -95.76 REMARK 500 SER I 5 -0.63 75.03 REMARK 500 SER I 20 10.16 80.37 REMARK 500 ILE I 40 -63.52 -96.81 REMARK 500 LEU I 104 57.58 39.39 REMARK 500 ASN P 4 23.92 -145.58 REMARK 500 ASN P 58 -5.59 70.74 REMARK 500 ASN P 63 129.48 -37.56 REMARK 500 TYR P 72 -0.35 -144.03 REMARK 500 ASP P 300 19.69 57.14 REMARK 500 ILE S 40 -62.51 -96.67 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 402 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 211 O REMARK 620 2 GLY A 215 O 96.9 REMARK 620 3 ASP A 241 OD2 95.5 103.0 REMARK 620 4 TYR A 266 O 103.6 149.3 97.5 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA D 402 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP D 211 O REMARK 620 2 GLY D 215 O 95.7 REMARK 620 3 ASP D 241 OD2 93.2 99.1 REMARK 620 4 TYR D 266 O 99.9 157.5 96.2 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA G 402 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP G 211 O REMARK 620 2 GLY G 215 O 102.7 REMARK 620 3 ASP G 241 OD2 108.0 113.5 REMARK 620 4 TYR G 266 O 94.0 134.1 100.9 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA P 402 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP P 211 O REMARK 620 2 GLY P 215 O 113.2 REMARK 620 3 ASP P 241 OD2 94.6 108.2 REMARK 620 4 TYR P 266 O 99.4 139.4 91.9 REMARK 620 N 1 2 3 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-48101 RELATED DB: EMDB REMARK 900 NCS.1 FAB IN COMPLEX WITH N5 NA OF A/SHOREBIRD/DELAWARE BAY/309/ REMARK 900 2016 (DB16, H10N5) -- 3 FABS DBREF1 9EJE A 0 393 UNP A0A223PX43_9INFA DBREF2 9EJE A A0A223PX43 80 473 DBREF1 9EJE D 0 393 UNP A0A223PX43_9INFA DBREF2 9EJE D A0A223PX43 80 473 DBREF1 9EJE G 0 393 UNP A0A223PX43_9INFA DBREF2 9EJE G A0A223PX43 80 473 DBREF 9EJE H -9 117 PDB 9EJE 9EJE -9 117 DBREF 9EJE I -9 117 PDB 9EJE 9EJE -9 117 DBREF 9EJE L 1 112 PDB 9EJE 9EJE 1 112 DBREF 9EJE M 1 112 PDB 9EJE 9EJE 1 112 DBREF1 9EJE P 0 393 UNP A0A223PX43_9INFA DBREF2 9EJE P A0A223PX43 80 473 DBREF 9EJE S -9 117 PDB 9EJE 9EJE -9 117 DBREF 9EJE T 1 112 PDB 9EJE 9EJE 1 112 SEQRES 1 A 394 GLU PHE LEU ASN ASN THR GLU PRO LEU CYS ASN VAL SER SEQRES 2 A 394 GLY PHE ALA ILE VAL SER LYS ASP ASN GLY ILE ARG ILE SEQRES 3 A 394 GLY SER ARG GLY HIS VAL PHE VAL ILE ARG GLU PRO PHE SEQRES 4 A 394 VAL ALA CYS GLY PRO THR GLU CYS ARG THR PHE PHE LEU SEQRES 5 A 394 THR GLN GLY ALA LEU LEU ASN ASP LYS HIS SER ASN ASN SEQRES 6 A 394 THR VAL LYS ASP ARG SER PRO TYR ARG ALA LEU MET SER SEQRES 7 A 394 VAL PRO LEU GLY SER SER PRO ASN ALA TYR GLN ALA LYS SEQRES 8 A 394 PHE GLU SER VAL ALA TRP SER ALA THR ALA CYS HIS ASP SEQRES 9 A 394 GLY LYS ARG TRP LEU ALA VAL GLY ILE SER GLY ALA ASP SEQRES 10 A 394 ASP ASP ALA TYR ALA VAL ILE HIS TYR GLY GLY MET PRO SEQRES 11 A 394 THR ASP VAL VAL ARG SER TRP ARG LYS GLN ILE LEU ARG SEQRES 12 A 394 THR GLN GLU SER SER CYS VAL CYS MET LYS GLY ASN CYS SEQRES 13 A 394 TYR TRP VAL MET THR ASP GLY PRO ALA ASN SER GLN ALA SEQRES 14 A 394 SER TYR LYS ILE PHE LYS SER HIS LYS GLY MET VAL THR SEQRES 15 A 394 ASN GLU ARG GLU VAL SER PHE GLN GLY GLY HIS ILE GLU SEQRES 16 A 394 GLU CYS SER CYS TYR PRO ASN LEU GLY LYS VAL GLU CYS SEQRES 17 A 394 VAL CYS ARG ASP ASN TRP ASN GLY MET ASN ARG PRO VAL SEQRES 18 A 394 LEU THR PHE ASP GLU ASP LEU ASN TYR GLU VAL GLY TYR SEQRES 19 A 394 LEU CYS ALA GLY ILE PRO THR ASP THR PRO ARG VAL GLN SEQRES 20 A 394 ASP ASN SER PHE ILE GLY SER CYS THR ASN ALA VAL GLY SEQRES 21 A 394 GLY SER GLY THR ASN ASN TYR GLY VAL LYS GLY PHE GLY SEQRES 22 A 394 PHE ARG GLN GLY ASN SER VAL TRP ALA GLY ARG THR VAL SEQRES 23 A 394 SER ILE SER SER ARG SER GLY PHE GLU ILE LEU LEU VAL SEQRES 24 A 394 GLU ASP GLY TRP VAL LYS THR SER LYS ASN VAL VAL LYS SEQRES 25 A 394 LYS VAL GLU VAL LEU ASN ASN LYS ASN TRP SER GLY TYR SEQRES 26 A 394 SER GLY ALA PHE THR ILE PRO ILE THR MET THR SER LYS SEQRES 27 A 394 GLN CYS LEU VAL PRO CYS PHE TRP LEU GLU MET ILE ARG SEQRES 28 A 394 GLY LYS PRO GLU GLU ARG THR SER ILE TRP THR SER SER SEQRES 29 A 394 SER SER THR VAL PHE CYS GLY VAL SER SER GLU VAL PRO SEQRES 30 A 394 GLY TRP SER TRP ASP ASP GLY ALA ILE LEU PRO PHE ASP SEQRES 31 A 394 ILE ASP LYS MET SEQRES 1 D 394 GLU PHE LEU ASN ASN THR GLU PRO LEU CYS ASN VAL SER SEQRES 2 D 394 GLY PHE ALA ILE VAL SER LYS ASP ASN GLY ILE ARG ILE SEQRES 3 D 394 GLY SER ARG GLY HIS VAL PHE VAL ILE ARG GLU PRO PHE SEQRES 4 D 394 VAL ALA CYS GLY PRO THR GLU CYS ARG THR PHE PHE LEU SEQRES 5 D 394 THR GLN GLY ALA LEU LEU ASN ASP LYS HIS SER ASN ASN SEQRES 6 D 394 THR VAL LYS ASP ARG SER PRO TYR ARG ALA LEU MET SER SEQRES 7 D 394 VAL PRO LEU GLY SER SER PRO ASN ALA TYR GLN ALA LYS SEQRES 8 D 394 PHE GLU SER VAL ALA TRP SER ALA THR ALA CYS HIS ASP SEQRES 9 D 394 GLY LYS ARG TRP LEU ALA VAL GLY ILE SER GLY ALA ASP SEQRES 10 D 394 ASP ASP ALA TYR ALA VAL ILE HIS TYR GLY GLY MET PRO SEQRES 11 D 394 THR ASP VAL VAL ARG SER TRP ARG LYS GLN ILE LEU ARG SEQRES 12 D 394 THR GLN GLU SER SER CYS VAL CYS MET LYS GLY ASN CYS SEQRES 13 D 394 TYR TRP VAL MET THR ASP GLY PRO ALA ASN SER GLN ALA SEQRES 14 D 394 SER TYR LYS ILE PHE LYS SER HIS LYS GLY MET VAL THR SEQRES 15 D 394 ASN GLU ARG GLU VAL SER PHE GLN GLY GLY HIS ILE GLU SEQRES 16 D 394 GLU CYS SER CYS TYR PRO ASN LEU GLY LYS VAL GLU CYS SEQRES 17 D 394 VAL CYS ARG ASP ASN TRP ASN GLY MET ASN ARG PRO VAL SEQRES 18 D 394 LEU THR PHE ASP GLU ASP LEU ASN TYR GLU VAL GLY TYR SEQRES 19 D 394 LEU CYS ALA GLY ILE PRO THR ASP THR PRO ARG VAL GLN SEQRES 20 D 394 ASP ASN SER PHE ILE GLY SER CYS THR ASN ALA VAL GLY SEQRES 21 D 394 GLY SER GLY THR ASN ASN TYR GLY VAL LYS GLY PHE GLY SEQRES 22 D 394 PHE ARG GLN GLY ASN SER VAL TRP ALA GLY ARG THR VAL SEQRES 23 D 394 SER ILE SER SER ARG SER GLY PHE GLU ILE LEU LEU VAL SEQRES 24 D 394 GLU ASP GLY TRP VAL LYS THR SER LYS ASN VAL VAL LYS SEQRES 25 D 394 LYS VAL GLU VAL LEU ASN ASN LYS ASN TRP SER GLY TYR SEQRES 26 D 394 SER GLY ALA PHE THR ILE PRO ILE THR MET THR SER LYS SEQRES 27 D 394 GLN CYS LEU VAL PRO CYS PHE TRP LEU GLU MET ILE ARG SEQRES 28 D 394 GLY LYS PRO GLU GLU ARG THR SER ILE TRP THR SER SER SEQRES 29 D 394 SER SER THR VAL PHE CYS GLY VAL SER SER GLU VAL PRO SEQRES 30 D 394 GLY TRP SER TRP ASP ASP GLY ALA ILE LEU PRO PHE ASP SEQRES 31 D 394 ILE ASP LYS MET SEQRES 1 G 394 GLU PHE LEU ASN ASN THR GLU PRO LEU CYS ASN VAL SER SEQRES 2 G 394 GLY PHE ALA ILE VAL SER LYS ASP ASN GLY ILE ARG ILE SEQRES 3 G 394 GLY SER ARG GLY HIS VAL PHE VAL ILE ARG GLU PRO PHE SEQRES 4 G 394 VAL ALA CYS GLY PRO THR GLU CYS ARG THR PHE PHE LEU SEQRES 5 G 394 THR GLN GLY ALA LEU LEU ASN ASP LYS HIS SER ASN ASN SEQRES 6 G 394 THR VAL LYS ASP ARG SER PRO TYR ARG ALA LEU MET SER SEQRES 7 G 394 VAL PRO LEU GLY SER SER PRO ASN ALA TYR GLN ALA LYS SEQRES 8 G 394 PHE GLU SER VAL ALA TRP SER ALA THR ALA CYS HIS ASP SEQRES 9 G 394 GLY LYS ARG TRP LEU ALA VAL GLY ILE SER GLY ALA ASP SEQRES 10 G 394 ASP ASP ALA TYR ALA VAL ILE HIS TYR GLY GLY MET PRO SEQRES 11 G 394 THR ASP VAL VAL ARG SER TRP ARG LYS GLN ILE LEU ARG SEQRES 12 G 394 THR GLN GLU SER SER CYS VAL CYS MET LYS GLY ASN CYS SEQRES 13 G 394 TYR TRP VAL MET THR ASP GLY PRO ALA ASN SER GLN ALA SEQRES 14 G 394 SER TYR LYS ILE PHE LYS SER HIS LYS GLY MET VAL THR SEQRES 15 G 394 ASN GLU ARG GLU VAL SER PHE GLN GLY GLY HIS ILE GLU SEQRES 16 G 394 GLU CYS SER CYS TYR PRO ASN LEU GLY LYS VAL GLU CYS SEQRES 17 G 394 VAL CYS ARG ASP ASN TRP ASN GLY MET ASN ARG PRO VAL SEQRES 18 G 394 LEU THR PHE ASP GLU ASP LEU ASN TYR GLU VAL GLY TYR SEQRES 19 G 394 LEU CYS ALA GLY ILE PRO THR ASP THR PRO ARG VAL GLN SEQRES 20 G 394 ASP ASN SER PHE ILE GLY SER CYS THR ASN ALA VAL GLY SEQRES 21 G 394 GLY SER GLY THR ASN ASN TYR GLY VAL LYS GLY PHE GLY SEQRES 22 G 394 PHE ARG GLN GLY ASN SER VAL TRP ALA GLY ARG THR VAL SEQRES 23 G 394 SER ILE SER SER ARG SER GLY PHE GLU ILE LEU LEU VAL SEQRES 24 G 394 GLU ASP GLY TRP VAL LYS THR SER LYS ASN VAL VAL LYS SEQRES 25 G 394 LYS VAL GLU VAL LEU ASN ASN LYS ASN TRP SER GLY TYR SEQRES 26 G 394 SER GLY ALA PHE THR ILE PRO ILE THR MET THR SER LYS SEQRES 27 G 394 GLN CYS LEU VAL PRO CYS PHE TRP LEU GLU MET ILE ARG SEQRES 28 G 394 GLY LYS PRO GLU GLU ARG THR SER ILE TRP THR SER SER SEQRES 29 G 394 SER SER THR VAL PHE CYS GLY VAL SER SER GLU VAL PRO SEQRES 30 G 394 GLY TRP SER TRP ASP ASP GLY ALA ILE LEU PRO PHE ASP SEQRES 31 G 394 ILE ASP LYS MET SEQRES 1 H 127 GLN VAL GLN LEU PRO GLU SER GLY PRO ARG LEU VAL LYS SEQRES 2 H 127 PRO SER GLU THR LEU SER LEU THR CYS SER VAL SER GLY SEQRES 3 H 127 GLU SER ILE SER SER GLY GLY TYR TYR TRP THR TRP ILE SEQRES 4 H 127 ARG GLN HIS PRO GLY LYS GLY LEU GLU TRP ILE GLY ASN SEQRES 5 H 127 ILE PHE ASP THR GLY SER THR HIS TYR SER PRO SER LEU SEQRES 6 H 127 LYS THR ARG LEU THR ILE SER ILE ASP THR SER LYS ASN SEQRES 7 H 127 GLN PHE TYR LEU ARG LEU ASN SER ALA THR ALA ALA ASP SEQRES 8 H 127 THR ALA VAL TYR TYR CYS ALA ARG VAL GLY TYR SER LEU SEQRES 9 H 127 GLU THR ASP ARG PRO TYR TYR PHE GLY LEU ASP VAL TRP SEQRES 10 H 127 GLY GLN GLY THR THR VAL THR VAL SER SER SEQRES 1 I 127 GLN VAL GLN LEU PRO GLU SER GLY PRO ARG LEU VAL LYS SEQRES 2 I 127 PRO SER GLU THR LEU SER LEU THR CYS SER VAL SER GLY SEQRES 3 I 127 GLU SER ILE SER SER GLY GLY TYR TYR TRP THR TRP ILE SEQRES 4 I 127 ARG GLN HIS PRO GLY LYS GLY LEU GLU TRP ILE GLY ASN SEQRES 5 I 127 ILE PHE ASP THR GLY SER THR HIS TYR SER PRO SER LEU SEQRES 6 I 127 LYS THR ARG LEU THR ILE SER ILE ASP THR SER LYS ASN SEQRES 7 I 127 GLN PHE TYR LEU ARG LEU ASN SER ALA THR ALA ALA ASP SEQRES 8 I 127 THR ALA VAL TYR TYR CYS ALA ARG VAL GLY TYR SER LEU SEQRES 9 I 127 GLU THR ASP ARG PRO TYR TYR PHE GLY LEU ASP VAL TRP SEQRES 10 I 127 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 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 P 394 GLU PHE LEU ASN ASN THR GLU PRO LEU CYS ASN VAL SER SEQRES 2 P 394 GLY PHE ALA ILE VAL SER LYS ASP ASN GLY ILE ARG ILE SEQRES 3 P 394 GLY SER ARG GLY HIS VAL PHE VAL ILE ARG GLU PRO PHE SEQRES 4 P 394 VAL ALA CYS GLY PRO THR GLU CYS ARG THR PHE PHE LEU SEQRES 5 P 394 THR GLN GLY ALA LEU LEU ASN ASP LYS HIS SER ASN ASN SEQRES 6 P 394 THR VAL LYS ASP ARG SER PRO TYR ARG ALA LEU MET SER SEQRES 7 P 394 VAL PRO LEU GLY SER SER PRO ASN ALA TYR GLN ALA LYS SEQRES 8 P 394 PHE GLU SER VAL ALA TRP SER ALA THR ALA CYS HIS ASP SEQRES 9 P 394 GLY LYS ARG TRP LEU ALA VAL GLY ILE SER GLY ALA ASP SEQRES 10 P 394 ASP ASP ALA TYR ALA VAL ILE HIS TYR GLY GLY MET PRO SEQRES 11 P 394 THR ASP VAL VAL ARG SER TRP ARG LYS GLN ILE LEU ARG SEQRES 12 P 394 THR GLN GLU SER SER CYS VAL CYS MET LYS GLY ASN CYS SEQRES 13 P 394 TYR TRP VAL MET THR ASP GLY PRO ALA ASN SER GLN ALA SEQRES 14 P 394 SER TYR LYS ILE PHE LYS SER HIS LYS GLY MET VAL THR SEQRES 15 P 394 ASN GLU ARG GLU VAL SER PHE GLN GLY GLY HIS ILE GLU SEQRES 16 P 394 GLU CYS SER CYS TYR PRO ASN LEU GLY LYS VAL GLU CYS SEQRES 17 P 394 VAL CYS ARG ASP ASN TRP ASN GLY MET ASN ARG PRO VAL SEQRES 18 P 394 LEU THR PHE ASP GLU ASP LEU ASN TYR GLU VAL GLY TYR SEQRES 19 P 394 LEU CYS ALA GLY ILE PRO THR ASP THR PRO ARG VAL GLN SEQRES 20 P 394 ASP ASN SER PHE ILE GLY SER CYS THR ASN ALA VAL GLY SEQRES 21 P 394 GLY SER GLY THR ASN ASN TYR GLY VAL LYS GLY PHE GLY SEQRES 22 P 394 PHE ARG GLN GLY ASN SER VAL TRP ALA GLY ARG THR VAL SEQRES 23 P 394 SER ILE SER SER ARG SER GLY PHE GLU ILE LEU LEU VAL SEQRES 24 P 394 GLU ASP GLY TRP VAL LYS THR SER LYS ASN VAL VAL LYS SEQRES 25 P 394 LYS VAL GLU VAL LEU ASN ASN LYS ASN TRP SER GLY TYR SEQRES 26 P 394 SER GLY ALA PHE THR ILE PRO ILE THR MET THR SER LYS SEQRES 27 P 394 GLN CYS LEU VAL PRO CYS PHE TRP LEU GLU MET ILE ARG SEQRES 28 P 394 GLY LYS PRO GLU GLU ARG THR SER ILE TRP THR SER SER SEQRES 29 P 394 SER SER THR VAL PHE CYS GLY VAL SER SER GLU VAL PRO SEQRES 30 P 394 GLY TRP SER TRP ASP ASP GLY ALA ILE LEU PRO PHE ASP SEQRES 31 P 394 ILE ASP LYS MET SEQRES 1 S 127 GLN VAL GLN LEU PRO GLU SER GLY PRO ARG LEU VAL LYS SEQRES 2 S 127 PRO SER GLU THR LEU SER LEU THR CYS SER VAL SER GLY SEQRES 3 S 127 GLU SER ILE SER SER GLY GLY TYR TYR TRP THR TRP ILE SEQRES 4 S 127 ARG GLN HIS PRO GLY LYS GLY LEU GLU TRP ILE GLY ASN SEQRES 5 S 127 ILE PHE ASP THR GLY SER THR HIS TYR SER PRO SER LEU SEQRES 6 S 127 LYS THR ARG LEU THR ILE SER ILE ASP THR SER LYS ASN SEQRES 7 S 127 GLN PHE TYR LEU ARG LEU ASN SER ALA THR ALA ALA ASP SEQRES 8 S 127 THR ALA VAL TYR TYR CYS ALA ARG VAL GLY TYR SER LEU SEQRES 9 S 127 GLU THR ASP ARG PRO TYR TYR PHE GLY LEU ASP VAL TRP SEQRES 10 S 127 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 HET NAG B 1 27 HET NAG B 2 27 HET BMA B 3 22 HET NAG C 1 27 HET NAG C 2 27 HET BMA C 3 22 HET NAG E 1 27 HET NAG E 2 27 HET BMA E 3 22 HET NAG F 1 27 HET NAG F 2 27 HET BMA F 3 22 HET NAG A 401 28 HET CA A 402 1 HET NAG D 401 28 HET CA D 402 1 HET NAG G 401 28 HET CA G 402 1 HET NAG P 401 28 HET CA P 402 1 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE 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 HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 11 NAG 12(C8 H15 N O6) FORMUL 11 BMA 4(C6 H12 O6) FORMUL 16 CA 4(CA 2+) HELIX 1 AA1 ASN A 21 SER A 27 1 7 HELIX 2 AA2 ASP A 59 ASN A 63 5 5 HELIX 3 AA3 PRO A 331 SER A 336 1 6 HELIX 4 AA4 PHE A 388 LYS A 392 5 5 HELIX 5 AA5 ASN D 21 SER D 27 1 7 HELIX 6 AA6 ASP D 59 ASN D 63 5 5 HELIX 7 AA7 PRO D 331 SER D 336 1 6 HELIX 8 AA8 ASN G 21 SER G 27 1 7 HELIX 9 AA9 ASP G 59 ASN G 63 5 5 HELIX 10 AB1 PRO G 331 SER G 336 1 6 HELIX 11 AB2 PHE G 388 LYS G 392 5 5 HELIX 12 AB3 PRO H 53 LYS H 56 5 4 HELIX 13 AB4 THR H 78 THR H 82 5 5 HELIX 14 AB5 PRO I 53 LYS I 56 5 4 HELIX 15 AB6 THR I 78 THR I 82 5 5 HELIX 16 AB7 GLU L 84 VAL L 88 5 5 HELIX 17 AB8 GLU M 84 VAL M 88 5 5 HELIX 18 AB9 ASN P 21 SER P 27 1 7 HELIX 19 AC1 ASP P 59 ASN P 63 5 5 HELIX 20 AC2 PRO P 331 SER P 336 1 6 HELIX 21 AC3 PRO S 53 LYS S 56 5 4 HELIX 22 AC4 THR S 78 THR S 82 5 5 HELIX 23 AC5 GLU T 84 VAL T 88 5 5 SHEET 1 AA1 4 GLY A 13 LYS A 19 0 SHEET 2 AA1 4 THR A 361 VAL A 371 -1 O VAL A 367 N VAL A 17 SHEET 3 AA1 4 VAL A 341 GLY A 351 -1 N PRO A 342 O GLY A 370 SHEET 4 AA1 4 SER A 325 ILE A 330 -1 N GLY A 326 O TRP A 345 SHEET 1 AA2 4 PHE A 32 CYS A 41 0 SHEET 2 AA2 4 CYS A 46 LEU A 56 -1 O ARG A 47 N ALA A 40 SHEET 3 AA2 4 ALA A 74 PRO A 79 -1 O VAL A 78 N THR A 48 SHEET 4 AA2 4 LYS A 90 VAL A 94 -1 O LYS A 90 N SER A 77 SHEET 1 AA3 4 SER A 97 HIS A 102 0 SHEET 2 AA3 4 TRP A 107 SER A 113 -1 O VAL A 110 N THR A 99 SHEET 3 AA3 4 TYR A 120 TYR A 125 -1 O TYR A 120 N SER A 113 SHEET 4 AA3 4 PRO A 129 ARG A 134 -1 O VAL A 133 N ALA A 121 SHEET 1 AA4 3 LEU A 141 THR A 143 0 SHEET 2 AA4 3 ASN A 154 ASP A 161 -1 O THR A 160 N ARG A 142 SHEET 3 AA4 3 VAL A 149 MET A 151 -1 N MET A 151 O ASN A 154 SHEET 1 AA5 4 LEU A 141 THR A 143 0 SHEET 2 AA5 4 ASN A 154 ASP A 161 -1 O THR A 160 N ARG A 142 SHEET 3 AA5 4 SER A 169 HIS A 176 -1 O PHE A 173 N TRP A 157 SHEET 4 AA5 4 MET A 179 VAL A 186 -1 O ARG A 184 N ILE A 172 SHEET 1 AA6 4 SER A 197 ASN A 201 0 SHEET 2 AA6 4 LYS A 204 VAL A 208 -1 O GLU A 206 N TYR A 199 SHEET 3 AA6 4 PRO A 219 PHE A 223 -1 O PHE A 223 N VAL A 205 SHEET 4 AA6 4 TYR A 229 TYR A 233 -1 O GLU A 230 N THR A 222 SHEET 1 AA7 4 ARG A 274 GLN A 275 0 SHEET 2 AA7 4 SER A 278 ARG A 283 -1 O SER A 278 N GLN A 275 SHEET 3 AA7 4 SER A 291 VAL A 298 -1 O LEU A 296 N ALA A 281 SHEET 4 AA7 4 VAL A 309 TRP A 321 -1 O VAL A 310 N LEU A 297 SHEET 1 AA8 4 GLY D 13 LYS D 19 0 SHEET 2 AA8 4 THR D 361 VAL D 371 -1 O VAL D 367 N VAL D 17 SHEET 3 AA8 4 VAL D 341 GLY D 351 -1 N ARG D 350 O SER D 362 SHEET 4 AA8 4 SER D 325 ILE D 330 -1 N GLY D 326 O TRP D 345 SHEET 1 AA9 4 PHE D 32 CYS D 41 0 SHEET 2 AA9 4 CYS D 46 LEU D 56 -1 O ARG D 47 N ALA D 40 SHEET 3 AA9 4 ALA D 74 PRO D 79 -1 O VAL D 78 N THR D 48 SHEET 4 AA9 4 LYS D 90 VAL D 94 -1 O LYS D 90 N SER D 77 SHEET 1 AB1 4 SER D 97 HIS D 102 0 SHEET 2 AB1 4 TRP D 107 SER D 113 -1 O LEU D 108 N CYS D 101 SHEET 3 AB1 4 TYR D 120 TYR D 125 -1 O TYR D 120 N SER D 113 SHEET 4 AB1 4 PRO D 129 ARG D 134 -1 O VAL D 133 N ALA D 121 SHEET 1 AB2 3 LEU D 141 THR D 143 0 SHEET 2 AB2 3 ASN D 154 ASP D 161 -1 O THR D 160 N ARG D 142 SHEET 3 AB2 3 VAL D 149 MET D 151 -1 N VAL D 149 O TYR D 156 SHEET 1 AB3 4 LEU D 141 THR D 143 0 SHEET 2 AB3 4 ASN D 154 ASP D 161 -1 O THR D 160 N ARG D 142 SHEET 3 AB3 4 SER D 169 HIS D 176 -1 O LYS D 171 N MET D 159 SHEET 4 AB3 4 MET D 179 VAL D 186 -1 O ARG D 184 N ILE D 172 SHEET 1 AB4 4 SER D 197 ASN D 201 0 SHEET 2 AB4 4 LYS D 204 VAL D 208 -1 O VAL D 208 N SER D 197 SHEET 3 AB4 4 PRO D 219 PHE D 223 -1 O LEU D 221 N CYS D 207 SHEET 4 AB4 4 TYR D 229 TYR D 233 -1 O GLY D 232 N VAL D 220 SHEET 1 AB5 4 ARG D 274 GLN D 275 0 SHEET 2 AB5 4 SER D 278 ARG D 283 -1 O SER D 278 N GLN D 275 SHEET 3 AB5 4 SER D 291 VAL D 298 -1 O LEU D 296 N ALA D 281 SHEET 4 AB5 4 VAL D 309 TRP D 321 -1 O VAL D 310 N LEU D 297 SHEET 1 AB6 4 GLY G 13 LYS G 19 0 SHEET 2 AB6 4 THR G 366 VAL G 371 -1 O VAL G 367 N VAL G 17 SHEET 3 AB6 4 VAL G 341 LEU G 346 -1 N PHE G 344 O PHE G 368 SHEET 4 AB6 4 SER G 325 ILE G 330 -1 N GLY G 326 O TRP G 345 SHEET 1 AB7 4 PHE G 32 CYS G 41 0 SHEET 2 AB7 4 CYS G 46 LEU G 56 -1 O ARG G 47 N ALA G 40 SHEET 3 AB7 4 ALA G 74 PRO G 79 -1 O VAL G 78 N THR G 48 SHEET 4 AB7 4 LYS G 90 VAL G 94 -1 O LYS G 90 N SER G 77 SHEET 1 AB8 4 SER G 97 HIS G 102 0 SHEET 2 AB8 4 TRP G 107 SER G 113 -1 O LEU G 108 N CYS G 101 SHEET 3 AB8 4 TYR G 120 TYR G 125 -1 O HIS G 124 N ALA G 109 SHEET 4 AB8 4 MET G 128 ARG G 134 -1 O MET G 128 N TYR G 125 SHEET 1 AB9 3 ARG G 142 THR G 143 0 SHEET 2 AB9 3 ASN G 154 ASP G 161 -1 O THR G 160 N ARG G 142 SHEET 3 AB9 3 VAL G 149 MET G 151 -1 N VAL G 149 O TYR G 156 SHEET 1 AC1 4 ARG G 142 THR G 143 0 SHEET 2 AC1 4 ASN G 154 ASP G 161 -1 O THR G 160 N ARG G 142 SHEET 3 AC1 4 SER G 169 HIS G 176 -1 O SER G 175 N CYS G 155 SHEET 4 AC1 4 VAL G 180 GLU G 185 -1 O ARG G 184 N ILE G 172 SHEET 1 AC2 4 CYS G 196 ASN G 201 0 SHEET 2 AC2 4 LYS G 204 CYS G 209 -1 O LYS G 204 N ASN G 201 SHEET 3 AC2 4 PRO G 219 PHE G 223 -1 O LEU G 221 N CYS G 207 SHEET 4 AC2 4 TYR G 229 TYR G 233 -1 O GLY G 232 N VAL G 220 SHEET 1 AC3 4 GLY G 272 GLN G 275 0 SHEET 2 AC3 4 SER G 278 ARG G 283 -1 O SER G 278 N GLN G 275 SHEET 3 AC3 4 SER G 291 VAL G 298 -1 O LEU G 296 N ALA G 281 SHEET 4 AC3 4 VAL G 309 TRP G 321 -1 O ASN G 320 N GLY G 292 SHEET 1 AC4 2 MET G 348 GLY G 351 0 SHEET 2 AC4 2 THR G 361 SER G 364 -1 O SER G 364 N MET G 348 SHEET 1 AC5 3 LEU H 8 SER H 13 0 SHEET 2 AC5 3 GLN H 69 LEU H 74 -1 O LEU H 74 N LEU H 8 SHEET 3 AC5 3 LEU H 59 ASP H 64 -1 N ASP H 64 O GLN H 69 SHEET 1 AC6 5 THR H 49 TYR H 51 0 SHEET 2 AC6 5 LEU H 37 ILE H 43 -1 N ASN H 42 O HIS H 50 SHEET 3 AC6 5 TYR H 25 GLN H 31 -1 N TRP H 26 O ILE H 43 SHEET 4 AC6 5 ALA H 83 SER H 93 -1 O TYR H 86 N ILE H 29 SHEET 5 AC6 5 TYR H 100 TRP H 107 -1 O TYR H 100 N SER H 93 SHEET 1 AC7 5 THR H 49 TYR H 51 0 SHEET 2 AC7 5 LEU H 37 ILE H 43 -1 N ASN H 42 O HIS H 50 SHEET 3 AC7 5 TYR H 25 GLN H 31 -1 N TRP H 26 O ILE H 43 SHEET 4 AC7 5 ALA H 83 SER H 93 -1 O TYR H 86 N ILE H 29 SHEET 5 AC7 5 THR H 111 VAL H 113 -1 O THR H 111 N TYR H 85 SHEET 1 AC8 3 LEU I 8 SER I 13 0 SHEET 2 AC8 3 GLN I 69 LEU I 74 -1 O LEU I 74 N LEU I 8 SHEET 3 AC8 3 LEU I 59 ASP I 64 -1 N ASP I 64 O GLN I 69 SHEET 1 AC9 5 THR I 49 TYR I 51 0 SHEET 2 AC9 5 LEU I 37 ILE I 43 -1 N ASN I 42 O HIS I 50 SHEET 3 AC9 5 TYR I 25 GLN I 31 -1 N ARG I 30 O GLU I 38 SHEET 4 AC9 5 ALA I 83 SER I 93 -1 O VAL I 90 N TYR I 25 SHEET 5 AC9 5 TYR I 100 TRP I 107 -1 O PHE I 102 N GLY I 91 SHEET 1 AD1 5 THR I 49 TYR I 51 0 SHEET 2 AD1 5 LEU I 37 ILE I 43 -1 N ASN I 42 O HIS I 50 SHEET 3 AD1 5 TYR I 25 GLN I 31 -1 N ARG I 30 O GLU I 38 SHEET 4 AD1 5 ALA I 83 SER I 93 -1 O VAL I 90 N TYR I 25 SHEET 5 AD1 5 THR I 111 VAL I 113 -1 O THR I 111 N TYR I 85 SHEET 1 AD2 4 MET L 4 GLN L 6 0 SHEET 2 AD2 4 ALA L 19 SER L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AD2 4 TYR L 75 ILE L 80 -1 O ILE L 80 N ALA L 19 SHEET 4 AD2 4 PHE L 67 SER L 72 -1 N SER L 70 O THR L 77 SHEET 1 AD3 5 SER L 10 VAL L 13 0 SHEET 2 AD3 5 THR L 107 ILE L 111 1 O LYS L 108 N LEU L 11 SHEET 3 AD3 5 GLY L 89 GLN L 95 -1 N TYR L 91 O THR L 107 SHEET 4 AD3 5 LEU L 38 GLN L 43 -1 N TYR L 41 O TYR L 92 SHEET 5 AD3 5 GLN L 50 ILE L 53 -1 O ILE L 53 N TRP L 40 SHEET 1 AD4 4 SER L 10 VAL L 13 0 SHEET 2 AD4 4 THR L 107 ILE L 111 1 O LYS L 108 N LEU L 11 SHEET 3 AD4 4 GLY L 89 GLN L 95 -1 N TYR L 91 O THR L 107 SHEET 4 AD4 4 THR L 102 PHE L 103 -1 O THR L 102 N GLN L 95 SHEET 1 AD5 4 MET M 4 GLN M 6 0 SHEET 2 AD5 4 ALA M 19 SER M 25 -1 O ARG M 24 N THR M 5 SHEET 3 AD5 4 TYR M 75 ILE M 80 -1 O LEU M 78 N ILE M 21 SHEET 4 AD5 4 PHE M 67 SER M 72 -1 N SER M 70 O THR M 77 SHEET 1 AD6 5 SER M 10 VAL M 13 0 SHEET 2 AD6 5 THR M 107 ILE M 111 1 O LYS M 108 N LEU M 11 SHEET 3 AD6 5 GLY M 89 GLN M 95 -1 N TYR M 91 O THR M 107 SHEET 4 AD6 5 LEU M 38 GLN M 43 -1 N TYR M 41 O TYR M 92 SHEET 5 AD6 5 GLN M 50 ILE M 53 -1 O LEU M 52 N TRP M 40 SHEET 1 AD7 4 SER M 10 VAL M 13 0 SHEET 2 AD7 4 THR M 107 ILE M 111 1 O LYS M 108 N LEU M 11 SHEET 3 AD7 4 GLY M 89 GLN M 95 -1 N TYR M 91 O THR M 107 SHEET 4 AD7 4 THR M 102 PHE M 103 -1 O THR M 102 N GLN M 95 SHEET 1 AD8 4 GLY P 13 LYS P 19 0 SHEET 2 AD8 4 THR P 361 VAL P 371 -1 O VAL P 367 N VAL P 17 SHEET 3 AD8 4 VAL P 341 GLY P 351 -1 N LEU P 346 O THR P 366 SHEET 4 AD8 4 SER P 325 ILE P 330 -1 N GLY P 326 O TRP P 345 SHEET 1 AD9 4 PHE P 32 CYS P 41 0 SHEET 2 AD9 4 CYS P 46 LEU P 56 -1 O ARG P 47 N ALA P 40 SHEET 3 AD9 4 ALA P 74 PRO P 79 -1 O VAL P 78 N THR P 48 SHEET 4 AD9 4 LYS P 90 VAL P 94 -1 O LYS P 90 N SER P 77 SHEET 1 AE1 4 SER P 97 HIS P 102 0 SHEET 2 AE1 4 TRP P 107 SER P 113 -1 O VAL P 110 N THR P 99 SHEET 3 AE1 4 TYR P 120 TYR P 125 -1 O VAL P 122 N GLY P 111 SHEET 4 AE1 4 PRO P 129 ARG P 134 -1 O VAL P 133 N ALA P 121 SHEET 1 AE2 3 LEU P 141 THR P 143 0 SHEET 2 AE2 3 ASN P 154 ASP P 161 -1 O THR P 160 N ARG P 142 SHEET 3 AE2 3 VAL P 149 MET P 151 -1 N MET P 151 O ASN P 154 SHEET 1 AE3 4 LEU P 141 THR P 143 0 SHEET 2 AE3 4 ASN P 154 ASP P 161 -1 O THR P 160 N ARG P 142 SHEET 3 AE3 4 SER P 169 HIS P 176 -1 O PHE P 173 N TRP P 157 SHEET 4 AE3 4 MET P 179 VAL P 186 -1 O ARG P 184 N ILE P 172 SHEET 1 AE4 4 SER P 197 ASN P 201 0 SHEET 2 AE4 4 LYS P 204 VAL P 208 -1 O GLU P 206 N TYR P 199 SHEET 3 AE4 4 PRO P 219 PHE P 223 -1 O PHE P 223 N VAL P 205 SHEET 4 AE4 4 TYR P 229 TYR P 233 -1 O GLU P 230 N THR P 222 SHEET 1 AE5 4 ARG P 274 GLN P 275 0 SHEET 2 AE5 4 SER P 278 ARG P 283 -1 O SER P 278 N GLN P 275 SHEET 3 AE5 4 SER P 291 VAL P 298 -1 O LEU P 296 N ALA P 281 SHEET 4 AE5 4 VAL P 309 TRP P 321 -1 O VAL P 310 N LEU P 297 SHEET 1 AE6 3 LEU S 8 SER S 13 0 SHEET 2 AE6 3 GLN S 69 LEU S 74 -1 O LEU S 74 N LEU S 8 SHEET 3 AE6 3 LEU S 59 ASP S 64 -1 N ASP S 64 O GLN S 69 SHEET 1 AE7 5 THR S 49 TYR S 51 0 SHEET 2 AE7 5 LEU S 37 ILE S 43 -1 N ASN S 42 O HIS S 50 SHEET 3 AE7 5 TYR S 25 GLN S 31 -1 N TRP S 26 O ILE S 43 SHEET 4 AE7 5 ALA S 83 SER S 93 -1 O TYR S 86 N ILE S 29 SHEET 5 AE7 5 TYR S 100 TRP S 107 -1 O PHE S 102 N GLY S 91 SHEET 1 AE8 5 THR S 49 TYR S 51 0 SHEET 2 AE8 5 LEU S 37 ILE S 43 -1 N ASN S 42 O HIS S 50 SHEET 3 AE8 5 TYR S 25 GLN S 31 -1 N TRP S 26 O ILE S 43 SHEET 4 AE8 5 ALA S 83 SER S 93 -1 O TYR S 86 N ILE S 29 SHEET 5 AE8 5 THR S 111 VAL S 113 -1 O THR S 111 N TYR S 85 SHEET 1 AE9 4 MET T 4 GLN T 6 0 SHEET 2 AE9 4 ALA T 19 SER T 25 -1 O ARG T 24 N THR T 5 SHEET 3 AE9 4 TYR T 75 ILE T 80 -1 O LEU T 78 N ILE T 21 SHEET 4 AE9 4 PHE T 67 SER T 72 -1 N SER T 68 O LYS T 79 SHEET 1 AF1 5 SER T 10 VAL T 13 0 SHEET 2 AF1 5 THR T 107 ILE T 111 1 O LYS T 108 N LEU T 11 SHEET 3 AF1 5 GLY T 89 GLN T 95 -1 N TYR T 91 O THR T 107 SHEET 4 AF1 5 LEU T 38 GLN T 43 -1 N TYR T 41 O TYR T 92 SHEET 5 AF1 5 GLN T 50 ILE T 53 -1 O LEU T 52 N TRP T 40 SHEET 1 AF2 4 SER T 10 VAL T 13 0 SHEET 2 AF2 4 THR T 107 ILE T 111 1 O LYS T 108 N LEU T 11 SHEET 3 AF2 4 GLY T 89 GLN T 95 -1 N TYR T 91 O THR T 107 SHEET 4 AF2 4 THR T 102 PHE T 103 -1 O THR T 102 N GLN T 95 SSBOND 1 CYS A 41 CYS A 46 1555 1555 2.03 SSBOND 2 CYS A 101 CYS A 148 1555 1555 2.03 SSBOND 3 CYS A 150 CYS A 155 1555 1555 2.04 SSBOND 4 CYS A 196 CYS A 209 1555 1555 2.03 SSBOND 5 CYS A 198 CYS A 207 1555 1555 2.03 SSBOND 6 CYS A 235 CYS A 254 1555 1555 2.04 SSBOND 7 CYS A 343 CYS A 369 1555 1555 2.03 SSBOND 8 CYS D 41 CYS D 46 1555 1555 2.03 SSBOND 9 CYS D 101 CYS D 148 1555 1555 2.03 SSBOND 10 CYS D 150 CYS D 155 1555 1555 2.04 SSBOND 11 CYS D 196 CYS D 209 1555 1555 2.03 SSBOND 12 CYS D 198 CYS D 207 1555 1555 2.03 SSBOND 13 CYS D 235 CYS D 254 1555 1555 2.03 SSBOND 14 CYS D 343 CYS D 369 1555 1555 2.03 SSBOND 15 CYS G 41 CYS G 46 1555 1555 2.03 SSBOND 16 CYS G 101 CYS G 148 1555 1555 2.03 SSBOND 17 CYS G 150 CYS G 155 1555 1555 2.04 SSBOND 18 CYS G 196 CYS G 209 1555 1555 2.03 SSBOND 19 CYS G 198 CYS G 207 1555 1555 2.03 SSBOND 20 CYS G 235 CYS G 254 1555 1555 2.04 SSBOND 21 CYS G 343 CYS G 369 1555 1555 2.03 SSBOND 22 CYS H 12 CYS H 87 1555 1555 2.03 SSBOND 23 CYS I 12 CYS I 87 1555 1555 2.03 SSBOND 24 CYS P 41 CYS P 46 1555 1555 2.04 SSBOND 25 CYS P 101 CYS P 148 1555 1555 2.03 SSBOND 26 CYS P 150 CYS P 155 1555 1555 2.04 SSBOND 27 CYS P 196 CYS P 209 1555 1555 2.03 SSBOND 28 CYS P 198 CYS P 207 1555 1555 2.03 SSBOND 29 CYS P 235 CYS P 254 1555 1555 2.04 SSBOND 30 CYS P 343 CYS P 369 1555 1555 2.04 SSBOND 31 CYS S 12 CYS S 87 1555 1555 2.03 LINK ND2 ASN A 3 C1 NAG A 401 1555 1555 1.43 LINK ND2 ASN A 63 C1 NAG B 1 1555 1555 1.45 LINK ND2 ASN D 3 C1 NAG D 401 1555 1555 1.43 LINK ND2 ASN D 63 C1 NAG C 1 1555 1555 1.45 LINK ND2 ASN G 3 C1 NAG G 401 1555 1555 1.43 LINK ND2 ASN G 63 C1 NAG E 1 1555 1555 1.45 LINK ND2 ASN P 3 C1 NAG P 401 1555 1555 1.43 LINK ND2 ASN P 63 C1 NAG F 1 1555 1555 1.45 LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.44 LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.45 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44 LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.45 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44 LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.45 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44 LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.45 LINK O ASP A 211 CA CA A 402 1555 1555 2.42 LINK O GLY A 215 CA CA A 402 1555 1555 2.47 LINK OD2 ASP A 241 CA CA A 402 1555 1555 2.18 LINK O TYR A 266 CA CA A 402 1555 1555 2.28 LINK O ASP D 211 CA CA D 402 1555 1555 2.58 LINK O GLY D 215 CA CA D 402 1555 1555 2.43 LINK OD2 ASP D 241 CA CA D 402 1555 1555 2.26 LINK O TYR D 266 CA CA D 402 1555 1555 2.20 LINK O ASP G 211 CA CA G 402 1555 1555 2.77 LINK O GLY G 215 CA CA G 402 1555 1555 2.11 LINK OD2 ASP G 241 CA CA G 402 1555 1555 2.16 LINK O TYR G 266 CA CA G 402 1555 1555 2.48 LINK O ASP P 211 CA CA P 402 1555 1555 2.29 LINK O GLY P 215 CA CA P 402 1555 1555 2.14 LINK OD2 ASP P 241 CA CA P 402 1555 1555 2.23 LINK O TYR P 266 CA CA P 402 1555 1555 2.67 CISPEP 1 LEU A 386 PRO A 387 0 -1.14 CISPEP 2 LEU D 386 PRO D 387 0 -1.03 CISPEP 3 LEU G 386 PRO G 387 0 -2.67 CISPEP 4 LEU P 386 PRO P 387 0 -0.38 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