HEADER VIRAL PROTEIN/IMMUNE SYSTEM 18-JUN-24 8ZYX TITLE NEURAMINIDASE OF A/SWITZERLAND/9715293/2013 H3N2 IN COMPLEX WITH CAV- TITLE 2 F6-R54S FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEURAMINIDASE; COMPND 3 CHAIN: A, B, C, D; COMPND 4 EC: 3.2.1.18; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: CAV-F6-R54S HEAVY CHAIN; COMPND 8 CHAIN: F; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: CAV-F6-R54S KAPPA CHAIN; COMPND 12 CHAIN: J; 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_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 INFLUENZA VIRUS, NEURAMINIDASE, ANTIBODY, VIRAL PROTEIN/IMMUNE KEYWDS 2 SYSTEM, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR X.WANG,J.GE,X.LI REVDAT 1 02-JUL-25 8ZYX 0 JRNL AUTH X.WANG,J.GE,X.LI JRNL TITL NEURAMINIDASE OF A/SWITZERLAND/9715293/2013 H3N2 IN COMPLEX JRNL TITL 2 WITH CAV-F6-R54S FAB JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.33 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) : 2.330 REMARK 3 NUMBER OF PARTICLES : 170595 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 8ZYX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 25-JUN-24. REMARK 100 THE DEPOSITION ID IS D_1300048801. 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 : NEURAMINIDASE OF REMARK 245 A/SWITZERLAND/9715293/2013 H3N2 REMARK 245 IN COMPLEX WITH CAV-F6-R54S FAB 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 : 7.20 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 : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1300.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 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) : 300 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, F, J, E, G, H, I, REMARK 350 AND CHAINS: K, L, M, N, O, P, Q, R, S, REMARK 350 AND CHAINS: T, U, V 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 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 VAL J 2 CG1 CG2 REMARK 470 THR J 31 OG1 CG2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OD1 ASP A 103 OG SER A 442 2.16 REMARK 500 OG SER D 179 OE2 GLU D 227 2.16 REMARK 500 O PRO J 8 OG1 THR J 102 2.18 REMARK 500 ND2 ASN C 234 O5 NAG C 502 2.19 REMARK 500 OG SER A 217 OD2 ASP A 243 2.19 REMARK 500 O4 NAG E 1 O5 NAG E 2 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 CYS A 92 CA - CB - SG ANGL. DEV. = 10.2 DEGREES REMARK 500 CYS B 337 CA - CB - SG ANGL. DEV. = 8.6 DEGREES REMARK 500 CYS C 337 CA - CB - SG ANGL. DEV. = 8.2 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 THR A 225 -167.30 -127.59 REMARK 500 LYS A 296 21.67 -144.49 REMARK 500 SER A 404 -169.37 -119.40 REMARK 500 LYS A 431 -9.68 83.63 REMARK 500 ASN B 147 55.23 38.66 REMARK 500 THR B 225 -167.59 -128.37 REMARK 500 HIS B 336 -30.09 -130.94 REMARK 500 CYS B 337 14.75 52.93 REMARK 500 HIS B 347 -169.09 -127.85 REMARK 500 LYS B 387 -27.31 98.00 REMARK 500 SER B 404 -168.37 -125.09 REMARK 500 LYS B 431 -8.24 81.72 REMARK 500 PRO C 126 0.49 -62.53 REMARK 500 ASP C 221 -168.26 -128.31 REMARK 500 GLU C 227 33.20 77.26 REMARK 500 SER C 404 -169.83 -119.15 REMARK 500 LYS C 431 -9.34 74.30 REMARK 500 PHE D 100 -50.30 -120.26 REMARK 500 PRO D 126 -9.55 -57.85 REMARK 500 ASN D 200 46.38 -141.29 REMARK 500 ASP D 221 -168.53 -125.60 REMARK 500 LYS D 296 17.76 -142.03 REMARK 500 CYS D 337 -7.22 72.17 REMARK 500 HIS D 347 -169.65 -129.92 REMARK 500 LYS D 431 -8.47 82.65 REMARK 500 GLU D 432 -39.45 -131.19 REMARK 500 THR J 10 48.24 37.80 REMARK 500 ALA J 52 -6.46 67.87 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 430 0.13 SIDE CHAIN REMARK 500 ARG B 210 0.26 SIDE CHAIN REMARK 500 ARG C 85 0.15 SIDE CHAIN REMARK 500 ARG C 283 0.08 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 503 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 293 O REMARK 620 2 GLY A 297 O 79.9 REMARK 620 3 ASP A 324 OD2 116.3 95.7 REMARK 620 4 GLY A 345 O 89.0 89.2 154.8 REMARK 620 5 HIS A 347 O 114.2 162.4 87.4 81.1 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B 503 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 293 O REMARK 620 2 GLY B 297 O 75.8 REMARK 620 3 ASP B 324 OD2 97.1 92.9 REMARK 620 4 HIS B 347 O 109.7 167.9 97.0 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C 503 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP C 293 O REMARK 620 2 GLY C 297 O 99.9 REMARK 620 3 ASP C 324 OD2 95.8 98.2 REMARK 620 4 GLY C 345 O 100.2 93.6 158.1 REMARK 620 5 HIS C 347 O 94.7 164.3 86.0 78.0 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA D 503 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP D 293 O REMARK 620 2 GLY D 297 O 85.7 REMARK 620 3 ASP D 324 OD2 91.9 93.0 REMARK 620 4 GLY D 345 O 88.0 87.4 179.6 REMARK 620 5 HIS D 347 O 106.7 162.0 99.3 80.3 REMARK 620 N 1 2 3 4 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-60582 RELATED DB: EMDB REMARK 900 NEURAMINIDASE OF A/SWITZERLAND/9715293/2013 H3N2 IN COMPLEX WITH F6_ REMARK 900 R54S FAB DBREF1 8ZYX A 83 469 UNP A0A2P1E3B1_9INFA DBREF2 8ZYX A A0A2P1E3B1 83 469 DBREF1 8ZYX B 83 469 UNP A0A2P1E3B1_9INFA DBREF2 8ZYX B A0A2P1E3B1 83 469 DBREF1 8ZYX C 83 469 UNP A0A2P1E3B1_9INFA DBREF2 8ZYX C A0A2P1E3B1 83 469 DBREF1 8ZYX D 83 469 UNP A0A2P1E3B1_9INFA DBREF2 8ZYX D A0A2P1E3B1 83 469 DBREF 8ZYX F 1 123 PDB 8ZYX 8ZYX 1 123 DBREF 8ZYX J 1 107 PDB 8ZYX 8ZYX 1 107 SEQRES 1 A 387 GLU TYR ARG ASN TRP SER LYS PRO GLN CYS GLY ILE THR SEQRES 2 A 387 GLY PHE ALA PRO PHE SER LYS ASP ASN SER ILE ARG LEU SEQRES 3 A 387 SER ALA GLY GLY ASP ILE TRP VAL THR ARG GLU PRO TYR SEQRES 4 A 387 VAL SER CYS ASP PRO ASP LYS CYS TYR GLN PHE ALA LEU SEQRES 5 A 387 GLY GLN GLY THR THR LEU ASN ASN VAL HIS SER ASN ASN SEQRES 6 A 387 THR VAL ARG ASP ARG THR PRO TYR ARG THR LEU LEU MET SEQRES 7 A 387 ASN GLU LEU GLY VAL PRO PHE HIS LEU GLY THR LYS GLN SEQRES 8 A 387 VAL CYS ILE ALA TRP SER SER SER SER CYS HIS ASP GLY SEQRES 9 A 387 LYS ALA TRP LEU HIS VAL CYS ILE THR GLY ASP ASP LYS SEQRES 10 A 387 ASN ALA THR ALA SER PHE ILE TYR ASN GLY ARG LEU VAL SEQRES 11 A 387 ASP SER VAL VAL SER TRP SER LYS ASP ILE LEU ARG THR SEQRES 12 A 387 GLN GLU SER GLU CYS VAL CYS ILE ASN GLY THR CYS THR SEQRES 13 A 387 VAL VAL MET THR ASP GLY SER ALA SER GLY LYS ALA ASP SEQRES 14 A 387 THR LYS ILE LEU PHE ILE GLU GLU GLY LYS ILE VAL HIS SEQRES 15 A 387 THR SER THR LEU SER GLY SER ALA GLN HIS VAL GLU GLU SEQRES 16 A 387 CYS SER CYS TYR PRO ARG TYR PRO GLY VAL ARG CYS VAL SEQRES 17 A 387 CYS ARG ASP ASN TRP LYS GLY SER ASN ARG PRO ILE VAL SEQRES 18 A 387 ASP ILE ASN ILE LYS ASP HIS SER ILE VAL SER SER TYR SEQRES 19 A 387 VAL CYS SER GLY LEU VAL GLY ASP THR PRO ARG LYS ASN SEQRES 20 A 387 ASP SER SER SER SER SER HIS CYS LEU ASP PRO ASN ASN SEQRES 21 A 387 GLU GLU GLY GLY HIS GLY VAL LYS GLY TRP ALA PHE ASP SEQRES 22 A 387 ASP GLY ASN ASP VAL TRP MET GLY ARG THR ILE ASN GLU SEQRES 23 A 387 THR SER ARG LEU GLY TYR GLU THR PHE LYS VAL ILE GLU SEQRES 24 A 387 GLY TRP SER ASN PRO LYS SER LYS LEU GLN THR ASN ARG SEQRES 25 A 387 GLN VAL ILE VAL ASP ARG GLY ASP ARG SER GLY TYR SER SEQRES 26 A 387 GLY ILE PHE SER VAL GLU GLY LYS SER CYS ILE ASN ARG SEQRES 27 A 387 CYS PHE TYR VAL GLU LEU ILE ARG GLY ARG LYS GLU GLU SEQRES 28 A 387 THR GLU VAL LEU TRP THR SER ASN SER ILE VAL VAL PHE SEQRES 29 A 387 CYS GLY THR SER GLY THR TYR GLY THR GLY SER TRP PRO SEQRES 30 A 387 ASP GLY ALA ASP LEU ASN LEU MET PRO ILE SEQRES 1 B 387 GLU TYR ARG ASN TRP SER LYS PRO GLN CYS GLY ILE THR SEQRES 2 B 387 GLY PHE ALA PRO PHE SER LYS ASP ASN SER ILE ARG LEU SEQRES 3 B 387 SER ALA GLY GLY ASP ILE TRP VAL THR ARG GLU PRO TYR SEQRES 4 B 387 VAL SER CYS ASP PRO ASP LYS CYS TYR GLN PHE ALA LEU SEQRES 5 B 387 GLY GLN GLY THR THR LEU ASN ASN VAL HIS SER ASN ASN SEQRES 6 B 387 THR VAL ARG ASP ARG THR PRO TYR ARG THR LEU LEU MET SEQRES 7 B 387 ASN GLU LEU GLY VAL PRO PHE HIS LEU GLY THR LYS GLN SEQRES 8 B 387 VAL CYS ILE ALA TRP SER SER SER SER CYS HIS ASP GLY SEQRES 9 B 387 LYS ALA TRP LEU HIS VAL CYS ILE THR GLY ASP ASP LYS SEQRES 10 B 387 ASN ALA THR ALA SER PHE ILE TYR ASN GLY ARG LEU VAL SEQRES 11 B 387 ASP SER VAL VAL SER TRP SER LYS ASP ILE LEU ARG THR SEQRES 12 B 387 GLN GLU SER GLU CYS VAL CYS ILE ASN GLY THR CYS THR SEQRES 13 B 387 VAL VAL MET THR ASP GLY SER ALA SER GLY LYS ALA ASP SEQRES 14 B 387 THR LYS ILE LEU PHE ILE GLU GLU GLY LYS ILE VAL HIS SEQRES 15 B 387 THR SER THR LEU SER GLY SER ALA GLN HIS VAL GLU GLU SEQRES 16 B 387 CYS SER CYS TYR PRO ARG TYR PRO GLY VAL ARG CYS VAL SEQRES 17 B 387 CYS ARG ASP ASN TRP LYS GLY SER ASN ARG PRO ILE VAL SEQRES 18 B 387 ASP ILE ASN ILE LYS ASP HIS SER ILE VAL SER SER TYR SEQRES 19 B 387 VAL CYS SER GLY LEU VAL GLY ASP THR PRO ARG LYS ASN SEQRES 20 B 387 ASP SER SER SER SER SER HIS CYS LEU ASP PRO ASN ASN SEQRES 21 B 387 GLU GLU GLY GLY HIS GLY VAL LYS GLY TRP ALA PHE ASP SEQRES 22 B 387 ASP GLY ASN ASP VAL TRP MET GLY ARG THR ILE ASN GLU SEQRES 23 B 387 THR SER ARG LEU GLY TYR GLU THR PHE LYS VAL ILE GLU SEQRES 24 B 387 GLY TRP SER ASN PRO LYS SER LYS LEU GLN THR ASN ARG SEQRES 25 B 387 GLN VAL ILE VAL ASP ARG GLY ASP ARG SER GLY TYR SER SEQRES 26 B 387 GLY ILE PHE SER VAL GLU GLY LYS SER CYS ILE ASN ARG SEQRES 27 B 387 CYS PHE TYR VAL GLU LEU ILE ARG GLY ARG LYS GLU GLU SEQRES 28 B 387 THR GLU VAL LEU TRP THR SER ASN SER ILE VAL VAL PHE SEQRES 29 B 387 CYS GLY THR SER GLY THR TYR GLY THR GLY SER TRP PRO SEQRES 30 B 387 ASP GLY ALA ASP LEU ASN LEU MET PRO ILE SEQRES 1 C 387 GLU TYR ARG ASN TRP SER LYS PRO GLN CYS GLY ILE THR SEQRES 2 C 387 GLY PHE ALA PRO PHE SER LYS ASP ASN SER ILE ARG LEU SEQRES 3 C 387 SER ALA GLY GLY ASP ILE TRP VAL THR ARG GLU PRO TYR SEQRES 4 C 387 VAL SER CYS ASP PRO ASP LYS CYS TYR GLN PHE ALA LEU SEQRES 5 C 387 GLY GLN GLY THR THR LEU ASN ASN VAL HIS SER ASN ASN SEQRES 6 C 387 THR VAL ARG ASP ARG THR PRO TYR ARG THR LEU LEU MET SEQRES 7 C 387 ASN GLU LEU GLY VAL PRO PHE HIS LEU GLY THR LYS GLN SEQRES 8 C 387 VAL CYS ILE ALA TRP SER SER SER SER CYS HIS ASP GLY SEQRES 9 C 387 LYS ALA TRP LEU HIS VAL CYS ILE THR GLY ASP ASP LYS SEQRES 10 C 387 ASN ALA THR ALA SER PHE ILE TYR ASN GLY ARG LEU VAL SEQRES 11 C 387 ASP SER VAL VAL SER TRP SER LYS ASP ILE LEU ARG THR SEQRES 12 C 387 GLN GLU SER GLU CYS VAL CYS ILE ASN GLY THR CYS THR SEQRES 13 C 387 VAL VAL MET THR ASP GLY SER ALA SER GLY LYS ALA ASP SEQRES 14 C 387 THR LYS ILE LEU PHE ILE GLU GLU GLY LYS ILE VAL HIS SEQRES 15 C 387 THR SER THR LEU SER GLY SER ALA GLN HIS VAL GLU GLU SEQRES 16 C 387 CYS SER CYS TYR PRO ARG TYR PRO GLY VAL ARG CYS VAL SEQRES 17 C 387 CYS ARG ASP ASN TRP LYS GLY SER ASN ARG PRO ILE VAL SEQRES 18 C 387 ASP ILE ASN ILE LYS ASP HIS SER ILE VAL SER SER TYR SEQRES 19 C 387 VAL CYS SER GLY LEU VAL GLY ASP THR PRO ARG LYS ASN SEQRES 20 C 387 ASP SER SER SER SER SER HIS CYS LEU ASP PRO ASN ASN SEQRES 21 C 387 GLU GLU GLY GLY HIS GLY VAL LYS GLY TRP ALA PHE ASP SEQRES 22 C 387 ASP GLY ASN ASP VAL TRP MET GLY ARG THR ILE ASN GLU SEQRES 23 C 387 THR SER ARG LEU GLY TYR GLU THR PHE LYS VAL ILE GLU SEQRES 24 C 387 GLY TRP SER ASN PRO LYS SER LYS LEU GLN THR ASN ARG SEQRES 25 C 387 GLN VAL ILE VAL ASP ARG GLY ASP ARG SER GLY TYR SER SEQRES 26 C 387 GLY ILE PHE SER VAL GLU GLY LYS SER CYS ILE ASN ARG SEQRES 27 C 387 CYS PHE TYR VAL GLU LEU ILE ARG GLY ARG LYS GLU GLU SEQRES 28 C 387 THR GLU VAL LEU TRP THR SER ASN SER ILE VAL VAL PHE SEQRES 29 C 387 CYS GLY THR SER GLY THR TYR GLY THR GLY SER TRP PRO SEQRES 30 C 387 ASP GLY ALA ASP LEU ASN LEU MET PRO ILE SEQRES 1 D 387 GLU TYR ARG ASN TRP SER LYS PRO GLN CYS GLY ILE THR SEQRES 2 D 387 GLY PHE ALA PRO PHE SER LYS ASP ASN SER ILE ARG LEU SEQRES 3 D 387 SER ALA GLY GLY ASP ILE TRP VAL THR ARG GLU PRO TYR SEQRES 4 D 387 VAL SER CYS ASP PRO ASP LYS CYS TYR GLN PHE ALA LEU SEQRES 5 D 387 GLY GLN GLY THR THR LEU ASN ASN VAL HIS SER ASN ASN SEQRES 6 D 387 THR VAL ARG ASP ARG THR PRO TYR ARG THR LEU LEU MET SEQRES 7 D 387 ASN GLU LEU GLY VAL PRO PHE HIS LEU GLY THR LYS GLN SEQRES 8 D 387 VAL CYS ILE ALA TRP SER SER SER SER CYS HIS ASP GLY SEQRES 9 D 387 LYS ALA TRP LEU HIS VAL CYS ILE THR GLY ASP ASP LYS SEQRES 10 D 387 ASN ALA THR ALA SER PHE ILE TYR ASN GLY ARG LEU VAL SEQRES 11 D 387 ASP SER VAL VAL SER TRP SER LYS ASP ILE LEU ARG THR SEQRES 12 D 387 GLN GLU SER GLU CYS VAL CYS ILE ASN GLY THR CYS THR SEQRES 13 D 387 VAL VAL MET THR ASP GLY SER ALA SER GLY LYS ALA ASP SEQRES 14 D 387 THR LYS ILE LEU PHE ILE GLU GLU GLY LYS ILE VAL HIS SEQRES 15 D 387 THR SER THR LEU SER GLY SER ALA GLN HIS VAL GLU GLU SEQRES 16 D 387 CYS SER CYS TYR PRO ARG TYR PRO GLY VAL ARG CYS VAL SEQRES 17 D 387 CYS ARG ASP ASN TRP LYS GLY SER ASN ARG PRO ILE VAL SEQRES 18 D 387 ASP ILE ASN ILE LYS ASP HIS SER ILE VAL SER SER TYR SEQRES 19 D 387 VAL CYS SER GLY LEU VAL GLY ASP THR PRO ARG LYS ASN SEQRES 20 D 387 ASP SER SER SER SER SER HIS CYS LEU ASP PRO ASN ASN SEQRES 21 D 387 GLU GLU GLY GLY HIS GLY VAL LYS GLY TRP ALA PHE ASP SEQRES 22 D 387 ASP GLY ASN ASP VAL TRP MET GLY ARG THR ILE ASN GLU SEQRES 23 D 387 THR SER ARG LEU GLY TYR GLU THR PHE LYS VAL ILE GLU SEQRES 24 D 387 GLY TRP SER ASN PRO LYS SER LYS LEU GLN THR ASN ARG SEQRES 25 D 387 GLN VAL ILE VAL ASP ARG GLY ASP ARG SER GLY TYR SER SEQRES 26 D 387 GLY ILE PHE SER VAL GLU GLY LYS SER CYS ILE ASN ARG SEQRES 27 D 387 CYS PHE TYR VAL GLU LEU ILE ARG GLY ARG LYS GLU GLU SEQRES 28 D 387 THR GLU VAL LEU TRP THR SER ASN SER ILE VAL VAL PHE SEQRES 29 D 387 CYS GLY THR SER GLY THR TYR GLY THR GLY SER TRP PRO SEQRES 30 D 387 ASP GLY ALA ASP LEU ASN LEU MET PRO ILE SEQRES 1 F 123 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 F 123 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 F 123 PHE SER PHE THR THR TYR GLU MET ASN TRP VAL ARG GLN SEQRES 4 F 123 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER HIS ILE SER SEQRES 5 F 123 SER SER GLY LEU VAL ILE TYR TYR ALA ASP SER VAL LYS SEQRES 6 F 123 GLY ARG PHE THR MET SER ARG ASP THR ALA LYS ASN SER SEQRES 7 F 123 LEU TYR LEU GLN MET ASP SER LEU THR VAL ALA ASP THR SEQRES 8 F 123 ALA VAL TYR TYR CYS ALA ARG HIS TYR PHE ASP ARG ASP SEQRES 9 F 123 TRP GLY TYR SER GLY MET ASP LEU TRP GLY GLN GLY THR SEQRES 10 F 123 THR VAL THR VAL SER SER SEQRES 1 J 107 GLU VAL VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 J 107 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 J 107 GLN SER LEU GLY THR ASN TYR LEU ALA TRP TYR GLN HIS SEQRES 4 J 107 LYS PRO GLY GLN SER PRO ARG LEU LEU ILE ASP GLY ALA SEQRES 5 J 107 SER THR ARG ALA ILE GLY ILE PRO ASP ARG PHE SER ALA SEQRES 6 J 107 SER GLY SER GLY THR ASP PHE THR LEU THR VAL SER ARG SEQRES 7 J 107 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN HIS SEQRES 8 J 107 TYR GLY ASN PRO TYR THR PHE GLY GLN GLY THR LYS LEU SEQRES 9 J 107 GLU ILE LYS HET NAG E 1 14 HET NAG E 2 14 HET NAG G 1 14 HET NAG G 2 14 HET NAG H 1 14 HET NAG H 2 14 HET NAG I 1 14 HET NAG I 2 14 HET BMA I 3 11 HET MAN I 4 11 HET MAN I 5 11 HET MAN I 6 11 HET MAN I 7 11 HET NAG K 1 14 HET NAG K 2 14 HET NAG L 1 14 HET NAG L 2 14 HET NAG M 1 14 HET NAG M 2 14 HET NAG N 1 14 HET NAG N 2 14 HET BMA N 3 11 HET MAN N 4 11 HET MAN N 5 11 HET MAN N 6 11 HET MAN N 7 11 HET NAG O 1 14 HET NAG O 2 14 HET NAG P 1 14 HET NAG P 2 14 HET NAG Q 1 14 HET NAG Q 2 14 HET NAG R 1 14 HET NAG R 2 14 HET BMA R 3 11 HET MAN R 4 11 HET MAN R 5 11 HET MAN R 6 11 HET MAN R 7 11 HET NAG S 1 14 HET NAG S 2 14 HET NAG T 1 14 HET NAG T 2 14 HET NAG U 1 14 HET NAG U 2 14 HET NAG V 1 14 HET NAG V 2 14 HET BMA V 3 11 HET MAN V 4 11 HET MAN V 5 11 HET MAN V 6 11 HET MAN V 7 11 HET NAG A 501 14 HET NAG A 502 14 HET CA A 503 1 HET NAG B 501 14 HET NAG B 502 14 HET CA B 503 1 HET NAG C 501 14 HET NAG C 502 14 HET CA C 503 1 HET NAG D 501 14 HET NAG D 502 14 HET CA D 503 1 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-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 HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 7 NAG 40(C8 H15 N O6) FORMUL 10 BMA 4(C6 H12 O6) FORMUL 10 MAN 16(C6 H12 O6) FORMUL 25 CA 4(CA 2+) HELIX 1 AA1 ASN A 104 GLY A 111 1 8 HELIX 2 AA2 ASN A 142 ASN A 146 5 5 HELIX 3 AA3 ASN B 104 ALA B 110 1 7 HELIX 4 AA4 ASN B 142 ASN B 146 5 5 HELIX 5 AA5 ASN C 104 ALA C 110 1 7 HELIX 6 AA6 ASN C 142 ASN C 146 5 5 HELIX 7 AA7 ASN D 104 ALA D 110 1 7 HELIX 8 AA8 ASN D 142 ASN D 146 5 5 HELIX 9 AA9 THR F 87 THR F 91 5 5 HELIX 10 AB1 GLU J 80 PHE J 84 5 5 SHEET 1 AA1 4 GLY A 96 LYS A 102 0 SHEET 2 AA1 4 THR A 439 THR A 449 -1 O VAL A 445 N SER A 101 SHEET 3 AA1 4 ILE A 418 GLY A 429 -1 N LEU A 426 O SER A 442 SHEET 4 AA1 4 SER A 407 GLU A 413 -1 N VAL A 412 O ASN A 419 SHEET 1 AA2 4 TRP A 115 CYS A 124 0 SHEET 2 AA2 4 CYS A 129 THR A 139 -1 O PHE A 132 N TYR A 121 SHEET 3 AA2 4 THR A 157 GLU A 162 -1 O LEU A 159 N ALA A 133 SHEET 4 AA2 4 LYS A 172 ILE A 176 -1 O CYS A 175 N LEU A 158 SHEET 1 AA3 4 SER A 179 HIS A 184 0 SHEET 2 AA3 4 TRP A 189 GLY A 196 -1 O LEU A 190 N CYS A 183 SHEET 3 AA3 4 ALA A 201 TYR A 207 -1 O SER A 204 N CYS A 193 SHEET 4 AA3 4 ARG A 210 VAL A 216 -1 O VAL A 212 N PHE A 205 SHEET 1 AA4 4 VAL A 231 ILE A 233 0 SHEET 2 AA4 4 THR A 236 GLY A 244 -1 O THR A 238 N VAL A 231 SHEET 3 AA4 4 ALA A 250 GLU A 258 -1 O ILE A 257 N CYS A 237 SHEET 4 AA4 4 LYS A 261 THR A 267 -1 O SER A 266 N ILE A 254 SHEET 1 AA5 4 GLU A 276 ARG A 283 0 SHEET 2 AA5 4 GLY A 286 ARG A 292 -1 O VAL A 290 N SER A 279 SHEET 3 AA5 4 PRO A 301 ASN A 306 -1 O ILE A 305 N VAL A 287 SHEET 4 AA5 4 ILE A 312 TYR A 316 -1 O SER A 315 N ILE A 302 SHEET 1 AA6 4 TRP A 352 ASP A 356 0 SHEET 2 AA6 4 ASP A 359 ARG A 364 -1 O TRP A 361 N PHE A 354 SHEET 3 AA6 4 LEU A 372 VAL A 379 -1 O GLU A 375 N ARG A 364 SHEET 4 AA6 4 GLN A 391 ARG A 403 -1 O ASP A 402 N GLY A 373 SHEET 1 AA7 4 GLY B 96 LYS B 102 0 SHEET 2 AA7 4 THR B 439 THR B 449 -1 O VAL B 445 N SER B 101 SHEET 3 AA7 4 ILE B 418 GLY B 429 -1 N LEU B 426 O SER B 442 SHEET 4 AA7 4 SER B 407 GLU B 413 -1 N VAL B 412 O ASN B 419 SHEET 1 AA8 4 TRP B 115 CYS B 124 0 SHEET 2 AA8 4 CYS B 129 THR B 139 -1 O TYR B 130 N SER B 123 SHEET 3 AA8 4 THR B 157 GLU B 162 -1 O LEU B 159 N ALA B 133 SHEET 4 AA8 4 LYS B 172 ILE B 176 -1 O VAL B 174 N LEU B 158 SHEET 1 AA9 4 SER B 179 HIS B 184 0 SHEET 2 AA9 4 TRP B 189 GLY B 196 -1 O LEU B 190 N CYS B 183 SHEET 3 AA9 4 ALA B 201 TYR B 207 -1 O SER B 204 N CYS B 193 SHEET 4 AA9 4 ARG B 210 VAL B 216 -1 O VAL B 215 N ALA B 203 SHEET 1 AB1 4 VAL B 231 ILE B 233 0 SHEET 2 AB1 4 THR B 236 GLY B 244 -1 O THR B 236 N ILE B 233 SHEET 3 AB1 4 ALA B 250 GLU B 258 -1 O LYS B 253 N MET B 241 SHEET 4 AB1 4 LYS B 261 THR B 267 -1 O SER B 266 N ILE B 254 SHEET 1 AB2 4 GLU B 276 ARG B 283 0 SHEET 2 AB2 4 GLY B 286 ARG B 292 -1 O ARG B 288 N TYR B 281 SHEET 3 AB2 4 PRO B 301 ASN B 306 -1 O ILE B 305 N VAL B 287 SHEET 4 AB2 4 SER B 311 TYR B 316 -1 O SER B 315 N ILE B 302 SHEET 1 AB3 4 TRP B 352 ASP B 356 0 SHEET 2 AB3 4 ASP B 359 ARG B 364 -1 O ASP B 359 N ASP B 356 SHEET 3 AB3 4 LEU B 372 VAL B 379 -1 O GLU B 375 N ARG B 364 SHEET 4 AB3 4 GLN B 391 ARG B 403 -1 O GLN B 395 N THR B 376 SHEET 1 AB4 4 GLY C 96 LYS C 102 0 SHEET 2 AB4 4 THR C 439 THR C 449 -1 O VAL C 445 N PHE C 100 SHEET 3 AB4 4 ILE C 418 GLY C 429 -1 N LEU C 426 O SER C 442 SHEET 4 AB4 4 SER C 407 GLU C 413 -1 N PHE C 410 O CYS C 421 SHEET 1 AB5 4 TRP C 115 CYS C 124 0 SHEET 2 AB5 4 CYS C 129 THR C 139 -1 O PHE C 132 N TYR C 121 SHEET 3 AB5 4 THR C 157 GLU C 162 -1 O LEU C 159 N ALA C 133 SHEET 4 AB5 4 LYS C 172 ILE C 176 -1 O VAL C 174 N LEU C 158 SHEET 1 AB6 4 SER C 179 HIS C 184 0 SHEET 2 AB6 4 TRP C 189 GLY C 196 -1 O LEU C 190 N CYS C 183 SHEET 3 AB6 4 ALA C 201 TYR C 207 -1 O SER C 204 N CYS C 193 SHEET 4 AB6 4 ARG C 210 VAL C 216 -1 O VAL C 215 N ALA C 203 SHEET 1 AB7 4 VAL C 231 ILE C 233 0 SHEET 2 AB7 4 THR C 236 GLY C 244 -1 O THR C 238 N VAL C 231 SHEET 3 AB7 4 ALA C 250 GLU C 258 -1 O ASP C 251 N ASP C 243 SHEET 4 AB7 4 LYS C 261 THR C 267 -1 O SER C 266 N ILE C 254 SHEET 1 AB8 4 GLU C 276 ARG C 283 0 SHEET 2 AB8 4 GLY C 286 ARG C 292 -1 O VAL C 290 N SER C 279 SHEET 3 AB8 4 PRO C 301 ASN C 306 -1 O ILE C 305 N VAL C 287 SHEET 4 AB8 4 ILE C 312 TYR C 316 -1 O SER C 315 N ILE C 302 SHEET 1 AB9 4 ALA C 353 ASP C 356 0 SHEET 2 AB9 4 ASP C 359 ARG C 364 -1 O TRP C 361 N PHE C 354 SHEET 3 AB9 4 LEU C 372 VAL C 379 -1 O GLU C 375 N ARG C 364 SHEET 4 AB9 4 GLN C 391 ARG C 403 -1 O GLN C 395 N THR C 376 SHEET 1 AC1 4 GLY D 96 LYS D 102 0 SHEET 2 AC1 4 THR D 439 THR D 449 -1 O VAL D 445 N PHE D 100 SHEET 3 AC1 4 ILE D 418 GLY D 429 -1 N LEU D 426 O SER D 442 SHEET 4 AC1 4 SER D 407 GLU D 413 -1 N VAL D 412 O ASN D 419 SHEET 1 AC2 4 TRP D 115 CYS D 124 0 SHEET 2 AC2 4 CYS D 129 THR D 139 -1 O TYR D 130 N SER D 123 SHEET 3 AC2 4 THR D 157 GLU D 162 -1 O LEU D 159 N ALA D 133 SHEET 4 AC2 4 LYS D 172 ILE D 176 -1 O VAL D 174 N LEU D 158 SHEET 1 AC3 4 SER D 179 HIS D 184 0 SHEET 2 AC3 4 TRP D 189 GLY D 196 -1 O LEU D 190 N CYS D 183 SHEET 3 AC3 4 ALA D 201 TYR D 207 -1 O SER D 204 N CYS D 193 SHEET 4 AC3 4 ARG D 210 VAL D 216 -1 O VAL D 215 N ALA D 203 SHEET 1 AC4 4 VAL D 231 ILE D 233 0 SHEET 2 AC4 4 THR D 236 GLY D 244 -1 O THR D 236 N ILE D 233 SHEET 3 AC4 4 ALA D 250 GLU D 258 -1 O ILE D 257 N CYS D 237 SHEET 4 AC4 4 LYS D 261 THR D 267 -1 O SER D 266 N ILE D 254 SHEET 1 AC5 4 GLU D 276 ARG D 283 0 SHEET 2 AC5 4 GLY D 286 ARG D 292 -1 O VAL D 290 N SER D 279 SHEET 3 AC5 4 PRO D 301 ASN D 306 -1 O ILE D 305 N VAL D 287 SHEET 4 AC5 4 SER D 311 TYR D 316 -1 O VAL D 313 N ASP D 304 SHEET 1 AC6 4 TRP D 352 ASP D 356 0 SHEET 2 AC6 4 ASP D 359 ARG D 364 -1 O TRP D 361 N PHE D 354 SHEET 3 AC6 4 LEU D 372 VAL D 379 -1 O GLU D 375 N ARG D 364 SHEET 4 AC6 4 GLN D 391 ARG D 403 -1 O GLN D 395 N THR D 376 SHEET 1 AC7 4 LEU F 4 SER F 7 0 SHEET 2 AC7 4 SER F 17 ALA F 24 -1 O SER F 21 N SER F 7 SHEET 3 AC7 4 SER F 78 ASP F 84 -1 O MET F 83 N LEU F 18 SHEET 4 AC7 4 PHE F 68 ASP F 73 -1 N THR F 69 O GLN F 82 SHEET 1 AC8 6 LEU F 11 VAL F 12 0 SHEET 2 AC8 6 THR F 117 VAL F 121 1 O THR F 120 N VAL F 12 SHEET 3 AC8 6 ALA F 92 HIS F 99 -1 N TYR F 94 O THR F 117 SHEET 4 AC8 6 GLU F 33 GLN F 39 -1 N VAL F 37 O TYR F 95 SHEET 5 AC8 6 LEU F 45 ILE F 51 -1 O ILE F 51 N MET F 34 SHEET 6 AC8 6 VAL F 57 TYR F 60 -1 O TYR F 59 N HIS F 50 SHEET 1 AC9 4 LEU F 11 VAL F 12 0 SHEET 2 AC9 4 THR F 117 VAL F 121 1 O THR F 120 N VAL F 12 SHEET 3 AC9 4 ALA F 92 HIS F 99 -1 N TYR F 94 O THR F 117 SHEET 4 AC9 4 LEU F 112 TRP F 113 -1 O LEU F 112 N ARG F 98 SHEET 1 AD1 2 PHE F 101 ASP F 102 0 SHEET 2 AD1 2 GLY F 106 TYR F 107 -1 O GLY F 106 N ASP F 102 SHEET 1 AD2 6 LEU J 11 LEU J 13 0 SHEET 2 AD2 6 THR J 102 ILE J 106 1 O GLU J 105 N LEU J 13 SHEET 3 AD2 6 VAL J 86 HIS J 91 -1 N TYR J 87 O THR J 102 SHEET 4 AD2 6 LEU J 34 HIS J 39 -1 N HIS J 39 O VAL J 86 SHEET 5 AD2 6 ARG J 46 ASP J 50 -1 O ARG J 46 N GLN J 38 SHEET 6 AD2 6 THR J 54 ARG J 55 -1 O THR J 54 N ASP J 50 SHEET 1 AD3 4 LEU J 11 LEU J 13 0 SHEET 2 AD3 4 THR J 102 ILE J 106 1 O GLU J 105 N LEU J 13 SHEET 3 AD3 4 VAL J 86 HIS J 91 -1 N TYR J 87 O THR J 102 SHEET 4 AD3 4 THR J 97 PHE J 98 -1 O THR J 97 N HIS J 91 SHEET 1 AD4 3 ALA J 19 ARG J 24 0 SHEET 2 AD4 3 ASP J 71 VAL J 76 -1 O LEU J 74 N LEU J 21 SHEET 3 AD4 3 PHE J 63 SER J 68 -1 N SER J 64 O THR J 75 SSBOND 1 CYS A 92 CYS A 417 1555 1555 2.03 SSBOND 2 CYS A 124 CYS A 129 1555 1555 2.03 SSBOND 3 CYS A 175 CYS A 193 1555 1555 2.02 SSBOND 4 CYS A 183 CYS A 230 1555 1555 2.02 SSBOND 5 CYS A 232 CYS A 237 1555 1555 2.03 SSBOND 6 CYS A 278 CYS A 291 1555 1555 2.03 SSBOND 7 CYS A 280 CYS A 289 1555 1555 2.03 SSBOND 8 CYS A 318 CYS A 337 1555 1555 2.03 SSBOND 9 CYS A 421 CYS A 447 1555 1555 2.03 SSBOND 10 CYS B 92 CYS B 417 1555 1555 2.03 SSBOND 11 CYS B 124 CYS B 129 1555 1555 2.03 SSBOND 12 CYS B 175 CYS B 193 1555 1555 2.02 SSBOND 13 CYS B 183 CYS B 230 1555 1555 2.02 SSBOND 14 CYS B 232 CYS B 237 1555 1555 2.03 SSBOND 15 CYS B 278 CYS B 291 1555 1555 2.03 SSBOND 16 CYS B 280 CYS B 289 1555 1555 2.03 SSBOND 17 CYS B 318 CYS B 337 1555 1555 2.03 SSBOND 18 CYS B 421 CYS B 447 1555 1555 2.03 SSBOND 19 CYS C 92 CYS C 417 1555 1555 2.03 SSBOND 20 CYS C 124 CYS C 129 1555 1555 2.03 SSBOND 21 CYS C 175 CYS C 193 1555 1555 2.02 SSBOND 22 CYS C 183 CYS C 230 1555 1555 2.02 SSBOND 23 CYS C 232 CYS C 237 1555 1555 2.03 SSBOND 24 CYS C 278 CYS C 291 1555 1555 2.03 SSBOND 25 CYS C 280 CYS C 289 1555 1555 2.03 SSBOND 26 CYS C 318 CYS C 337 1555 1555 2.04 SSBOND 27 CYS C 421 CYS C 447 1555 1555 2.03 SSBOND 28 CYS D 92 CYS D 417 1555 1555 2.04 SSBOND 29 CYS D 124 CYS D 129 1555 1555 2.06 SSBOND 30 CYS D 175 CYS D 193 1555 1555 2.03 SSBOND 31 CYS D 183 CYS D 230 1555 1555 2.02 SSBOND 32 CYS D 232 CYS D 237 1555 1555 2.03 SSBOND 33 CYS D 278 CYS D 291 1555 1555 2.03 SSBOND 34 CYS D 280 CYS D 289 1555 1555 2.03 SSBOND 35 CYS D 318 CYS D 337 1555 1555 2.04 SSBOND 36 CYS D 421 CYS D 447 1555 1555 2.03 SSBOND 37 CYS F 22 CYS F 96 1555 1555 2.04 SSBOND 38 CYS J 23 CYS J 89 1555 1555 2.03 LINK ND2 ASN A 86 C1 NAG A 501 1555 1555 1.43 LINK ND2 ASN A 146 C1 NAG E 1 1555 1555 1.43 LINK ND2 ASN A 200 C1 NAG I 1 1555 1555 1.43 LINK ND2 ASN A 234 C1 NAG A 502 1555 1555 1.43 LINK ND2 ASN A 329 C1 NAG H 1 1555 1555 1.43 LINK ND2 ASN A 367 C1 NAG G 1 1555 1555 1.44 LINK ND2 ASN B 86 C1 NAG B 501 1555 1555 1.44 LINK ND2 ASN B 146 C1 NAG K 1 1555 1555 1.42 LINK ND2 ASN B 200 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN B 234 C1 NAG B 502 1555 1555 1.43 LINK ND2 ASN B 329 C1 NAG M 1 1555 1555 1.44 LINK ND2 ASN B 367 C1 NAG L 1 1555 1555 1.42 LINK ND2 ASN C 86 C1 NAG C 501 1555 1555 1.44 LINK ND2 ASN C 146 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN C 200 C1 NAG R 1 1555 1555 1.43 LINK ND2 ASN C 234 C1 NAG C 502 1555 1555 1.43 LINK ND2 ASN C 329 C1 NAG Q 1 1555 1555 1.42 LINK ND2 ASN C 367 C1 NAG P 1 1555 1555 1.45 LINK ND2 ASN D 86 C1 NAG D 501 1555 1555 1.45 LINK ND2 ASN D 146 C1 NAG S 1 1555 1555 1.43 LINK ND2 ASN D 200 C1 NAG V 1 1555 1555 1.45 LINK ND2 ASN D 234 C1 NAG D 502 1555 1555 1.44 LINK ND2 ASN D 329 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN D 367 C1 NAG T 1 1555 1555 1.44 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.39 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.39 LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.39 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44 LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.46 LINK O3 BMA I 3 C1 MAN I 4 1555 1555 1.44 LINK O6 BMA I 3 C1 MAN I 6 1555 1555 1.44 LINK O2 MAN I 4 C1 MAN I 5 1555 1555 1.45 LINK O3 MAN I 6 C1 MAN I 7 1555 1555 1.45 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.39 LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.39 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.39 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44 LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.45 LINK O3 BMA N 3 C1 MAN N 4 1555 1555 1.45 LINK O6 BMA N 3 C1 MAN N 6 1555 1555 1.44 LINK O2 MAN N 4 C1 MAN N 5 1555 1555 1.45 LINK O3 MAN N 6 C1 MAN N 7 1555 1555 1.45 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.39 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.39 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.39 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.44 LINK O4 NAG R 2 C1 BMA R 3 1555 1555 1.45 LINK O3 BMA R 3 C1 MAN R 4 1555 1555 1.45 LINK O6 BMA R 3 C1 MAN R 6 1555 1555 1.45 LINK O2 MAN R 4 C1 MAN R 5 1555 1555 1.44 LINK O3 MAN R 6 C1 MAN R 7 1555 1555 1.45 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.39 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.40 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.39 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.38 LINK O4 NAG V 2 C1 BMA V 3 1555 1555 1.39 LINK O3 BMA V 3 C1 MAN V 4 1555 1555 1.40 LINK O6 BMA V 3 C1 MAN V 6 1555 1555 1.40 LINK O2 MAN V 4 C1 MAN V 5 1555 1555 1.39 LINK O3 MAN V 6 C1 MAN V 7 1555 1555 1.40 LINK O ASP A 293 CA CA A 503 1555 1555 1.96 LINK O GLY A 297 CA CA A 503 1555 1555 2.50 LINK OD2 ASP A 324 CA CA A 503 1555 1555 2.57 LINK O GLY A 345 CA CA A 503 1555 1555 2.84 LINK O HIS A 347 CA CA A 503 1555 1555 2.05 LINK O ASP B 293 CA CA B 503 1555 1555 2.20 LINK O GLY B 297 CA CA B 503 1555 1555 2.61 LINK OD2 ASP B 324 CA CA B 503 1555 1555 2.40 LINK O HIS B 347 CA CA B 503 1555 1555 2.15 LINK O ASP C 293 CA CA C 503 1555 1555 2.06 LINK O GLY C 297 CA CA C 503 1555 1555 2.38 LINK OD2 ASP C 324 CA CA C 503 1555 1555 2.46 LINK O GLY C 345 CA CA C 503 1555 1555 2.92 LINK O HIS C 347 CA CA C 503 1555 1555 2.28 LINK O ASP D 293 CA CA D 503 1555 1555 1.98 LINK O GLY D 297 CA CA D 503 1555 1555 2.51 LINK OD2 ASP D 324 CA CA D 503 1555 1555 2.63 LINK O GLY D 345 CA CA D 503 1555 1555 3.11 LINK O HIS D 347 CA CA D 503 1555 1555 2.22 CISPEP 1 TYR A 284 PRO A 285 0 6.28 CISPEP 2 THR A 325 PRO A 326 0 5.16 CISPEP 3 TYR B 284 PRO B 285 0 5.74 CISPEP 4 THR B 325 PRO B 326 0 5.20 CISPEP 5 TYR C 284 PRO C 285 0 6.49 CISPEP 6 THR C 325 PRO C 326 0 6.29 CISPEP 7 TYR D 284 PRO D 285 0 7.97 CISPEP 8 THR D 325 PRO D 326 0 5.68 CISPEP 9 ASN J 94 PRO J 95 0 0.93 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