HEADER VIRAL PROTEIN/IMMUNE SYSTEM 05-DEC-24 9MD3 TITLE NEURAMINIDASE IN COMPLEX WITH MAB 5-12 COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEURAMINIDASE; COMPND 3 CHAIN: A, B, C, D; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: MAB 5-12 HEAVY CHAIN; COMPND 7 CHAIN: H, E, F, G; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: MAB 5-12 LIGHT CHAIN; COMPND 11 CHAIN: L, I, J, K; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 3 ORGANISM_TAXID: 11320; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_TAXID: 10090; SOURCE 9 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 13 ORGANISM_TAXID: 10090; SOURCE 14 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS POLYCLONAL ANTIBODIES, NEURAMINIDASE, INFLUENZA, CRYO-EM, IMMUNE KEYWDS 2 SYSTEM, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR J.A.FERGUSON,S.S.R.RAGHAVAN,A.B.WARD REVDAT 1 27-AUG-25 9MD3 0 JRNL AUTH J.A.FERGUSON,S.S.R.RAGHAVAN,G.P.ALZUA,D.BHAVSAR,J.HUANG, JRNL AUTH 2 A.J.RODRIGUEZ,J.L.TORRES,M.BOTTERMANN,J.HAN,F.KRAMMER, JRNL AUTH 3 F.D.BATISTA,A.B.WARD JRNL TITL FUNCTIONAL AND EPITOPE SPECIFIC MONOCLONAL ANTIBODY JRNL TITL 2 DISCOVERY DIRECTLY FROM IMMUNE SERA USING CRYO-EM. JRNL REF SCI ADV V. 11 V8257 2025 JRNL REFN ESSN 2375-2548 JRNL PMID 40815640 JRNL DOI 10.1126/SCIADV.ADV8257 REMARK 2 REMARK 2 RESOLUTION. 2.90 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) : 2.900 REMARK 3 NUMBER OF PARTICLES : 67241 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 9MD3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1000290602. 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 IND11 IN COMPLEX REMARK 245 WITH MAB 5-12 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 : 7.50 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 : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 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) : 4500.00 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: 12-MERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 12-MERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L, B, E, I, C, F, J, D, REMARK 350 AND CHAINS: G, K, M, N, O, P, Q, R, S, REMARK 350 AND CHAINS: T, U, V, W, X 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 3 REMARK 465 TYR A 4 REMARK 465 SER A 5 REMARK 465 MET A 6 REMARK 465 GLN A 7 REMARK 465 LEU A 8 REMARK 465 ALA A 9 REMARK 465 SER A 10 REMARK 465 CYS A 11 REMARK 465 VAL A 12 REMARK 465 THR A 13 REMARK 465 LEU A 14 REMARK 465 THR A 15 REMARK 465 LEU A 16 REMARK 465 VAL A 17 REMARK 465 LEU A 18 REMARK 465 LEU A 19 REMARK 465 VAL A 20 REMARK 465 ASN A 21 REMARK 465 SER A 22 REMARK 465 GLN A 23 REMARK 465 HIS A 24 REMARK 465 HIS A 25 REMARK 465 HIS A 26 REMARK 465 HIS A 27 REMARK 465 HIS A 28 REMARK 465 HIS A 29 REMARK 465 GLY A 30 REMARK 465 SER A 31 REMARK 465 SER A 32 REMARK 465 SER A 33 REMARK 465 SER A 34 REMARK 465 ASP A 35 REMARK 465 TYR A 36 REMARK 465 SER A 37 REMARK 465 ASP A 38 REMARK 465 LEU A 39 REMARK 465 GLN A 40 REMARK 465 ARG A 41 REMARK 465 VAL A 42 REMARK 465 LYS A 43 REMARK 465 GLN A 44 REMARK 465 GLU A 45 REMARK 465 LEU A 46 REMARK 465 LEU A 47 REMARK 465 GLU A 48 REMARK 465 GLU A 49 REMARK 465 VAL A 50 REMARK 465 LYS A 51 REMARK 465 LYS A 52 REMARK 465 GLU A 53 REMARK 465 LEU A 54 REMARK 465 GLN A 55 REMARK 465 LYS A 56 REMARK 465 VAL A 57 REMARK 465 LYS A 58 REMARK 465 GLU A 59 REMARK 465 GLU A 60 REMARK 465 ILE A 61 REMARK 465 ILE A 62 REMARK 465 GLU A 63 REMARK 465 ALA A 64 REMARK 465 PHE A 65 REMARK 465 VAL A 66 REMARK 465 GLN A 67 REMARK 465 GLU A 68 REMARK 465 LEU A 69 REMARK 465 ARG A 70 REMARK 465 LYS A 71 REMARK 465 ARG A 72 REMARK 465 GLY A 73 REMARK 465 SER A 74 REMARK 465 LEU A 75 REMARK 465 VAL A 76 REMARK 465 PRO A 77 REMARK 465 ARG A 78 REMARK 465 GLY A 79 REMARK 465 SER A 80 REMARK 465 GLY A 81 REMARK 465 MET B 3 REMARK 465 TYR B 4 REMARK 465 SER B 5 REMARK 465 MET B 6 REMARK 465 GLN B 7 REMARK 465 LEU B 8 REMARK 465 ALA B 9 REMARK 465 SER B 10 REMARK 465 CYS B 11 REMARK 465 VAL B 12 REMARK 465 THR B 13 REMARK 465 LEU B 14 REMARK 465 THR B 15 REMARK 465 LEU B 16 REMARK 465 VAL B 17 REMARK 465 LEU B 18 REMARK 465 LEU B 19 REMARK 465 VAL B 20 REMARK 465 ASN B 21 REMARK 465 SER B 22 REMARK 465 GLN B 23 REMARK 465 HIS B 24 REMARK 465 HIS B 25 REMARK 465 HIS B 26 REMARK 465 HIS B 27 REMARK 465 HIS B 28 REMARK 465 HIS B 29 REMARK 465 GLY B 30 REMARK 465 SER B 31 REMARK 465 SER B 32 REMARK 465 SER B 33 REMARK 465 SER B 34 REMARK 465 ASP B 35 REMARK 465 TYR B 36 REMARK 465 SER B 37 REMARK 465 ASP B 38 REMARK 465 LEU B 39 REMARK 465 GLN B 40 REMARK 465 ARG B 41 REMARK 465 VAL B 42 REMARK 465 LYS B 43 REMARK 465 GLN B 44 REMARK 465 GLU B 45 REMARK 465 LEU B 46 REMARK 465 LEU B 47 REMARK 465 GLU B 48 REMARK 465 GLU B 49 REMARK 465 VAL B 50 REMARK 465 LYS B 51 REMARK 465 LYS B 52 REMARK 465 GLU B 53 REMARK 465 LEU B 54 REMARK 465 GLN B 55 REMARK 465 LYS B 56 REMARK 465 VAL B 57 REMARK 465 LYS B 58 REMARK 465 GLU B 59 REMARK 465 GLU B 60 REMARK 465 ILE B 61 REMARK 465 ILE B 62 REMARK 465 GLU B 63 REMARK 465 ALA B 64 REMARK 465 PHE B 65 REMARK 465 VAL B 66 REMARK 465 GLN B 67 REMARK 465 GLU B 68 REMARK 465 LEU B 69 REMARK 465 ARG B 70 REMARK 465 LYS B 71 REMARK 465 ARG B 72 REMARK 465 GLY B 73 REMARK 465 SER B 74 REMARK 465 LEU B 75 REMARK 465 VAL B 76 REMARK 465 PRO B 77 REMARK 465 ARG B 78 REMARK 465 GLY B 79 REMARK 465 SER B 80 REMARK 465 GLY B 81 REMARK 465 MET C 3 REMARK 465 TYR C 4 REMARK 465 SER C 5 REMARK 465 MET C 6 REMARK 465 GLN C 7 REMARK 465 LEU C 8 REMARK 465 ALA C 9 REMARK 465 SER C 10 REMARK 465 CYS C 11 REMARK 465 VAL C 12 REMARK 465 THR C 13 REMARK 465 LEU C 14 REMARK 465 THR C 15 REMARK 465 LEU C 16 REMARK 465 VAL C 17 REMARK 465 LEU C 18 REMARK 465 LEU C 19 REMARK 465 VAL C 20 REMARK 465 ASN C 21 REMARK 465 SER C 22 REMARK 465 GLN C 23 REMARK 465 HIS C 24 REMARK 465 HIS C 25 REMARK 465 HIS C 26 REMARK 465 HIS C 27 REMARK 465 HIS C 28 REMARK 465 HIS C 29 REMARK 465 GLY C 30 REMARK 465 SER C 31 REMARK 465 SER C 32 REMARK 465 SER C 33 REMARK 465 SER C 34 REMARK 465 ASP C 35 REMARK 465 TYR C 36 REMARK 465 SER C 37 REMARK 465 ASP C 38 REMARK 465 LEU C 39 REMARK 465 GLN C 40 REMARK 465 ARG C 41 REMARK 465 VAL C 42 REMARK 465 LYS C 43 REMARK 465 GLN C 44 REMARK 465 GLU C 45 REMARK 465 LEU C 46 REMARK 465 LEU C 47 REMARK 465 GLU C 48 REMARK 465 GLU C 49 REMARK 465 VAL C 50 REMARK 465 LYS C 51 REMARK 465 LYS C 52 REMARK 465 GLU C 53 REMARK 465 LEU C 54 REMARK 465 GLN C 55 REMARK 465 LYS C 56 REMARK 465 VAL C 57 REMARK 465 LYS C 58 REMARK 465 GLU C 59 REMARK 465 GLU C 60 REMARK 465 ILE C 61 REMARK 465 ILE C 62 REMARK 465 GLU C 63 REMARK 465 ALA C 64 REMARK 465 PHE C 65 REMARK 465 VAL C 66 REMARK 465 GLN C 67 REMARK 465 GLU C 68 REMARK 465 LEU C 69 REMARK 465 ARG C 70 REMARK 465 LYS C 71 REMARK 465 ARG C 72 REMARK 465 GLY C 73 REMARK 465 SER C 74 REMARK 465 LEU C 75 REMARK 465 VAL C 76 REMARK 465 PRO C 77 REMARK 465 ARG C 78 REMARK 465 GLY C 79 REMARK 465 SER C 80 REMARK 465 GLY C 81 REMARK 465 MET D 3 REMARK 465 TYR D 4 REMARK 465 SER D 5 REMARK 465 MET D 6 REMARK 465 GLN D 7 REMARK 465 LEU D 8 REMARK 465 ALA D 9 REMARK 465 SER D 10 REMARK 465 CYS D 11 REMARK 465 VAL D 12 REMARK 465 THR D 13 REMARK 465 LEU D 14 REMARK 465 THR D 15 REMARK 465 LEU D 16 REMARK 465 VAL D 17 REMARK 465 LEU D 18 REMARK 465 LEU D 19 REMARK 465 VAL D 20 REMARK 465 ASN D 21 REMARK 465 SER D 22 REMARK 465 GLN D 23 REMARK 465 HIS D 24 REMARK 465 HIS D 25 REMARK 465 HIS D 26 REMARK 465 HIS D 27 REMARK 465 HIS D 28 REMARK 465 HIS D 29 REMARK 465 GLY D 30 REMARK 465 SER D 31 REMARK 465 SER D 32 REMARK 465 SER D 33 REMARK 465 SER D 34 REMARK 465 ASP D 35 REMARK 465 TYR D 36 REMARK 465 SER D 37 REMARK 465 ASP D 38 REMARK 465 LEU D 39 REMARK 465 GLN D 40 REMARK 465 ARG D 41 REMARK 465 VAL D 42 REMARK 465 LYS D 43 REMARK 465 GLN D 44 REMARK 465 GLU D 45 REMARK 465 LEU D 46 REMARK 465 LEU D 47 REMARK 465 GLU D 48 REMARK 465 GLU D 49 REMARK 465 VAL D 50 REMARK 465 LYS D 51 REMARK 465 LYS D 52 REMARK 465 GLU D 53 REMARK 465 LEU D 54 REMARK 465 GLN D 55 REMARK 465 LYS D 56 REMARK 465 VAL D 57 REMARK 465 LYS D 58 REMARK 465 GLU D 59 REMARK 465 GLU D 60 REMARK 465 ILE D 61 REMARK 465 ILE D 62 REMARK 465 GLU D 63 REMARK 465 ALA D 64 REMARK 465 PHE D 65 REMARK 465 VAL D 66 REMARK 465 GLN D 67 REMARK 465 GLU D 68 REMARK 465 LEU D 69 REMARK 465 ARG D 70 REMARK 465 LYS D 71 REMARK 465 ARG D 72 REMARK 465 GLY D 73 REMARK 465 SER D 74 REMARK 465 LEU D 75 REMARK 465 VAL D 76 REMARK 465 PRO D 77 REMARK 465 ARG D 78 REMARK 465 GLY D 79 REMARK 465 SER D 80 REMARK 465 GLY D 81 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 OD2 ASP D 293 OH TYR D 316 2.17 REMARK 500 OD2 ASP C 293 OH TYR C 316 2.17 REMARK 500 OD2 ASP A 293 OH TYR A 316 2.18 REMARK 500 OD2 ASP B 293 OH TYR B 316 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN A 93 41.81 -106.61 REMARK 500 ILE A 222 90.73 50.72 REMARK 500 TRP A 295 -60.15 -94.32 REMARK 500 HIS A 347 172.39 64.05 REMARK 500 GLU A 368 -0.76 64.00 REMARK 500 PRO H 41 -7.40 -58.31 REMARK 500 ALA L 51 -3.74 69.03 REMARK 500 ASN B 93 41.79 -106.59 REMARK 500 ILE B 222 90.78 50.78 REMARK 500 TRP B 295 -60.07 -94.26 REMARK 500 HIS B 347 172.50 64.08 REMARK 500 GLU B 368 -0.62 64.00 REMARK 500 PRO E 41 -7.64 -58.79 REMARK 500 ALA I 51 -3.77 69.12 REMARK 500 ASN C 93 41.81 -106.64 REMARK 500 ILE C 222 90.87 50.82 REMARK 500 TRP C 295 -60.09 -94.26 REMARK 500 HIS C 347 172.45 64.07 REMARK 500 GLU C 368 -0.63 64.03 REMARK 500 PRO F 41 -7.74 -58.62 REMARK 500 ALA J 51 -3.85 68.97 REMARK 500 ASN D 93 41.81 -106.64 REMARK 500 ILE D 222 90.68 50.84 REMARK 500 HIS D 347 172.50 64.04 REMARK 500 GLU D 368 -0.59 63.96 REMARK 500 PRO G 41 -7.71 -58.83 REMARK 500 ALA K 51 -3.79 69.00 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 J 94 PRO J 95 141.87 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 501 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 293 O REMARK 620 2 GLY A 297 O 75.4 REMARK 620 3 ASP A 324 OD2 88.5 91.3 REMARK 620 4 GLY A 345 O 85.5 91.5 172.5 REMARK 620 5 HIS A 347 O 103.3 163.6 105.1 72.1 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B 501 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 293 O REMARK 620 2 GLY B 297 O 75.4 REMARK 620 3 ASP B 324 OD2 88.2 91.0 REMARK 620 4 GLY B 345 O 85.8 91.6 172.6 REMARK 620 5 HIS B 347 O 103.4 163.8 105.1 72.2 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C 501 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP C 293 O REMARK 620 2 GLY C 297 O 74.9 REMARK 620 3 ASP C 324 OD2 88.0 90.3 REMARK 620 4 GLY C 345 O 86.1 92.3 172.8 REMARK 620 5 HIS C 347 O 103.5 164.4 105.2 72.2 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA D 501 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP D 293 O REMARK 620 2 GLY D 297 O 75.8 REMARK 620 3 ASP D 324 OD2 87.9 90.6 REMARK 620 4 GLY D 345 O 86.0 92.0 172.6 REMARK 620 5 HIS D 347 O 103.3 164.2 105.1 72.2 REMARK 620 N 1 2 3 4 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-48166 RELATED DB: EMDB REMARK 900 NEURAMINIDASE IN COMPLEX WITH MAB 5-12 DBREF 9MD3 A 3 469 PDB 9MD3 9MD3 3 469 DBREF 9MD3 H 1 113 PDB 9MD3 9MD3 1 113 DBREF 9MD3 L 1 107 PDB 9MD3 9MD3 1 107 DBREF 9MD3 B 3 469 PDB 9MD3 9MD3 3 469 DBREF 9MD3 E 1 113 PDB 9MD3 9MD3 1 113 DBREF 9MD3 I 1 107 PDB 9MD3 9MD3 1 107 DBREF 9MD3 C 3 469 PDB 9MD3 9MD3 3 469 DBREF 9MD3 F 1 113 PDB 9MD3 9MD3 1 113 DBREF 9MD3 J 1 107 PDB 9MD3 9MD3 1 107 DBREF 9MD3 D 3 469 PDB 9MD3 9MD3 3 469 DBREF 9MD3 G 1 113 PDB 9MD3 9MD3 1 113 DBREF 9MD3 K 1 107 PDB 9MD3 9MD3 1 107 SEQRES 1 A 467 MET TYR SER MET GLN LEU ALA SER CYS VAL THR LEU THR SEQRES 2 A 467 LEU VAL LEU LEU VAL ASN SER GLN HIS HIS HIS HIS HIS SEQRES 3 A 467 HIS GLY SER SER SER SER ASP TYR SER ASP LEU GLN ARG SEQRES 4 A 467 VAL LYS GLN GLU LEU LEU GLU GLU VAL LYS LYS GLU LEU SEQRES 5 A 467 GLN LYS VAL LYS GLU GLU ILE ILE GLU ALA PHE VAL GLN SEQRES 6 A 467 GLU LEU ARG LYS ARG GLY SER LEU VAL PRO ARG GLY SER SEQRES 7 A 467 GLY GLY GLU TYR ARG ASN TRP SER LYS PRO GLN CYS ASN SEQRES 8 A 467 ILE THR GLY PHE ALA PRO PHE SER LYS ASP ASN SER ILE SEQRES 9 A 467 ARG LEU SER ALA GLY GLY ASP ILE TRP VAL THR ARG GLU SEQRES 10 A 467 PRO TYR VAL SER CYS ASP PRO ASP LYS CYS TYR GLN PHE SEQRES 11 A 467 ALA LEU GLY GLN GLY THR THR LEU ASN ASN GLY HIS SER SEQRES 12 A 467 ASN ASN THR VAL HIS ASP ARG THR PRO TYR ARG THR LEU SEQRES 13 A 467 LEU MET ASN GLU LEU GLY VAL PRO PHE HIS LEU GLY THR SEQRES 14 A 467 ARG GLN VAL CYS MET ALA TRP SER SER SER SER CYS HIS SEQRES 15 A 467 ASP GLY LYS ALA TRP LEU HIS VAL CYS ILE THR GLY ASN SEQRES 16 A 467 ASP ASN ASN ALA THR ALA SER PHE ILE TYR ASN GLY ARG SEQRES 17 A 467 LEU VAL ASP SER ILE GLY SER TRP SER LYS ASN ILE LEU SEQRES 18 A 467 ARG THR GLN GLU SER GLU CYS VAL CYS ILE ASN GLY THR SEQRES 19 A 467 CYS THR VAL VAL MET THR ASP GLY SER ALA SER GLY LYS SEQRES 20 A 467 ALA ASP THR LYS ILE LEU PHE VAL GLU GLU GLY LYS ILE SEQRES 21 A 467 VAL HIS ILE SER THR LEU SER GLY SER ALA GLN HIS VAL SEQRES 22 A 467 GLU GLU CYS SER CYS TYR PRO ARG PHE PRO GLY VAL ARG SEQRES 23 A 467 CYS VAL CYS ARG ASP ASN TRP LYS GLY SER ASN ARG PRO SEQRES 24 A 467 ILE VAL ASP ILE ASN VAL LYS ASN TYR SER ILE VAL SER SEQRES 25 A 467 SER TYR VAL CYS SER GLY LEU VAL GLY ASP THR PRO ARG SEQRES 26 A 467 LYS SER ASP SER VAL SER SER SER TYR CYS LEU ASP PRO SEQRES 27 A 467 ASN ASN GLU LYS GLY GLY HIS GLY VAL LYS GLY TRP ALA SEQRES 28 A 467 PHE ASP ASP GLY ASN ASP VAL TRP MET GLY ARG THR ILE SEQRES 29 A 467 ASN GLU THR LEU ARG LEU GLY TYR GLU THR PHE LYS VAL SEQRES 30 A 467 ILE GLU GLY TRP SER LYS ALA ASN SER LYS LEU GLN THR SEQRES 31 A 467 ASN ARG GLN VAL ILE VAL GLU LYS GLY ASP ARG SER GLY SEQRES 32 A 467 TYR SER GLY ILE PHE SER VAL GLU GLY LYS SER CYS ILE SEQRES 33 A 467 ASN ARG CYS PHE TYR VAL GLU LEU ILE ARG GLY ARG LYS SEQRES 34 A 467 GLU GLU THR LYS VAL TRP TRP THR SER ASN SER ILE VAL SEQRES 35 A 467 VAL PHE CYS GLY THR SER GLY THR TYR GLY THR GLY SER SEQRES 36 A 467 TRP PRO ASP GLY ALA ASP ILE ASN LEU MET PRO ILE SEQRES 1 H 118 GLU VAL LYS LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 118 PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 H 118 PHE THR PHE SER ASP TYR TYR MET TYR TRP VAL ARG GLN SEQRES 4 H 118 THR PRO GLU LYS ARG LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 H 118 ASN GLY GLY GLY SER THR TYR TYR PRO ASP THR VAL LYS SEQRES 6 H 118 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 H 118 LEU TYR LEU GLN MET SER ARG LEU LYS SER GLU ASP THR SEQRES 8 H 118 ALA MET TYR TYR CYS ALA ARG SER ASP ASP GLY ASP TYR SEQRES 9 H 118 PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SEQRES 10 H 118 SER SEQRES 1 L 111 ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU ALA VAL SEQRES 2 L 111 SER LEU GLY GLN ARG ALA THR ILE SER CYS ARG ALA SER SEQRES 3 L 111 GLN SER VAL SER THR SER SER TYR SER TYR MET HIS TRP SEQRES 4 L 111 TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE SEQRES 5 L 111 LYS TYR ALA SER ASN LEU GLU SER GLY VAL PRO ALA ARG SEQRES 6 L 111 PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU ASN SEQRES 7 L 111 ILE HIS PRO VAL GLU GLU GLU ASP THR ALA THR TYR TYR SEQRES 8 L 111 CYS GLN HIS SER TRP GLU ILE PRO LEU THR PHE GLY ALA SEQRES 9 L 111 GLY THR LYS LEU GLU LEU LYS SEQRES 1 B 467 MET TYR SER MET GLN LEU ALA SER CYS VAL THR LEU THR SEQRES 2 B 467 LEU VAL LEU LEU VAL ASN SER GLN HIS HIS HIS HIS HIS SEQRES 3 B 467 HIS GLY SER SER SER SER ASP TYR SER ASP LEU GLN ARG SEQRES 4 B 467 VAL LYS GLN GLU LEU LEU GLU GLU VAL LYS LYS GLU LEU SEQRES 5 B 467 GLN LYS VAL LYS GLU GLU ILE ILE GLU ALA PHE VAL GLN SEQRES 6 B 467 GLU LEU ARG LYS ARG GLY SER LEU VAL PRO ARG GLY SER SEQRES 7 B 467 GLY GLY GLU TYR ARG ASN TRP SER LYS PRO GLN CYS ASN SEQRES 8 B 467 ILE THR GLY PHE ALA PRO PHE SER LYS ASP ASN SER ILE SEQRES 9 B 467 ARG LEU SER ALA GLY GLY ASP ILE TRP VAL THR ARG GLU SEQRES 10 B 467 PRO TYR VAL SER CYS ASP PRO ASP LYS CYS TYR GLN PHE SEQRES 11 B 467 ALA LEU GLY GLN GLY THR THR LEU ASN ASN GLY HIS SER SEQRES 12 B 467 ASN ASN THR VAL HIS ASP ARG THR PRO TYR ARG THR LEU SEQRES 13 B 467 LEU MET ASN GLU LEU GLY VAL PRO PHE HIS LEU GLY THR SEQRES 14 B 467 ARG GLN VAL CYS MET ALA TRP SER SER SER SER CYS HIS SEQRES 15 B 467 ASP GLY LYS ALA TRP LEU HIS VAL CYS ILE THR GLY ASN SEQRES 16 B 467 ASP ASN ASN ALA THR ALA SER PHE ILE TYR ASN GLY ARG SEQRES 17 B 467 LEU VAL ASP SER ILE GLY SER TRP SER LYS ASN ILE LEU SEQRES 18 B 467 ARG THR GLN GLU SER GLU CYS VAL CYS ILE ASN GLY THR SEQRES 19 B 467 CYS THR VAL VAL MET THR ASP GLY SER ALA SER GLY LYS SEQRES 20 B 467 ALA ASP THR LYS ILE LEU PHE VAL GLU GLU GLY LYS ILE SEQRES 21 B 467 VAL HIS ILE SER THR LEU SER GLY SER ALA GLN HIS VAL SEQRES 22 B 467 GLU GLU CYS SER CYS TYR PRO ARG PHE PRO GLY VAL ARG SEQRES 23 B 467 CYS VAL CYS ARG ASP ASN TRP LYS GLY SER ASN ARG PRO SEQRES 24 B 467 ILE VAL ASP ILE ASN VAL LYS ASN TYR SER ILE VAL SER SEQRES 25 B 467 SER TYR VAL CYS SER GLY LEU VAL GLY ASP THR PRO ARG SEQRES 26 B 467 LYS SER ASP SER VAL SER SER SER TYR CYS LEU ASP PRO SEQRES 27 B 467 ASN ASN GLU LYS GLY GLY HIS GLY VAL LYS GLY TRP ALA SEQRES 28 B 467 PHE ASP ASP GLY ASN ASP VAL TRP MET GLY ARG THR ILE SEQRES 29 B 467 ASN GLU THR LEU ARG LEU GLY TYR GLU THR PHE LYS VAL SEQRES 30 B 467 ILE GLU GLY TRP SER LYS ALA ASN SER LYS LEU GLN THR SEQRES 31 B 467 ASN ARG GLN VAL ILE VAL GLU LYS GLY ASP ARG SER GLY SEQRES 32 B 467 TYR SER GLY ILE PHE SER VAL GLU GLY LYS SER CYS ILE SEQRES 33 B 467 ASN ARG CYS PHE TYR VAL GLU LEU ILE ARG GLY ARG LYS SEQRES 34 B 467 GLU GLU THR LYS VAL TRP TRP THR SER ASN SER ILE VAL SEQRES 35 B 467 VAL PHE CYS GLY THR SER GLY THR TYR GLY THR GLY SER SEQRES 36 B 467 TRP PRO ASP GLY ALA ASP ILE ASN LEU MET PRO ILE SEQRES 1 E 118 GLU VAL LYS LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 E 118 PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 E 118 PHE THR PHE SER ASP TYR TYR MET TYR TRP VAL ARG GLN SEQRES 4 E 118 THR PRO GLU LYS ARG LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 E 118 ASN GLY GLY GLY SER THR TYR TYR PRO ASP THR VAL LYS SEQRES 6 E 118 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 E 118 LEU TYR LEU GLN MET SER ARG LEU LYS SER GLU ASP THR SEQRES 8 E 118 ALA MET TYR TYR CYS ALA ARG SER ASP ASP GLY ASP TYR SEQRES 9 E 118 PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SEQRES 10 E 118 SER SEQRES 1 I 111 ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU ALA VAL SEQRES 2 I 111 SER LEU GLY GLN ARG ALA THR ILE SER CYS ARG ALA SER SEQRES 3 I 111 GLN SER VAL SER THR SER SER TYR SER TYR MET HIS TRP SEQRES 4 I 111 TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE SEQRES 5 I 111 LYS TYR ALA SER ASN LEU GLU SER GLY VAL PRO ALA ARG SEQRES 6 I 111 PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU ASN SEQRES 7 I 111 ILE HIS PRO VAL GLU GLU GLU ASP THR ALA THR TYR TYR SEQRES 8 I 111 CYS GLN HIS SER TRP GLU ILE PRO LEU THR PHE GLY ALA SEQRES 9 I 111 GLY THR LYS LEU GLU LEU LYS SEQRES 1 C 467 MET TYR SER MET GLN LEU ALA SER CYS VAL THR LEU THR SEQRES 2 C 467 LEU VAL LEU LEU VAL ASN SER GLN HIS HIS HIS HIS HIS SEQRES 3 C 467 HIS GLY SER SER SER SER ASP TYR SER ASP LEU GLN ARG SEQRES 4 C 467 VAL LYS GLN GLU LEU LEU GLU GLU VAL LYS LYS GLU LEU SEQRES 5 C 467 GLN LYS VAL LYS GLU GLU ILE ILE GLU ALA PHE VAL GLN SEQRES 6 C 467 GLU LEU ARG LYS ARG GLY SER LEU VAL PRO ARG GLY SER SEQRES 7 C 467 GLY GLY GLU TYR ARG ASN TRP SER LYS PRO GLN CYS ASN SEQRES 8 C 467 ILE THR GLY PHE ALA PRO PHE SER LYS ASP ASN SER ILE SEQRES 9 C 467 ARG LEU SER ALA GLY GLY ASP ILE TRP VAL THR ARG GLU SEQRES 10 C 467 PRO TYR VAL SER CYS ASP PRO ASP LYS CYS TYR GLN PHE SEQRES 11 C 467 ALA LEU GLY GLN GLY THR THR LEU ASN ASN GLY HIS SER SEQRES 12 C 467 ASN ASN THR VAL HIS ASP ARG THR PRO TYR ARG THR LEU SEQRES 13 C 467 LEU MET ASN GLU LEU GLY VAL PRO PHE HIS LEU GLY THR SEQRES 14 C 467 ARG GLN VAL CYS MET ALA TRP SER SER SER SER CYS HIS SEQRES 15 C 467 ASP GLY LYS ALA TRP LEU HIS VAL CYS ILE THR GLY ASN SEQRES 16 C 467 ASP ASN ASN ALA THR ALA SER PHE ILE TYR ASN GLY ARG SEQRES 17 C 467 LEU VAL ASP SER ILE GLY SER TRP SER LYS ASN ILE LEU SEQRES 18 C 467 ARG THR GLN GLU SER GLU CYS VAL CYS ILE ASN GLY THR SEQRES 19 C 467 CYS THR VAL VAL MET THR ASP GLY SER ALA SER GLY LYS SEQRES 20 C 467 ALA ASP THR LYS ILE LEU PHE VAL GLU GLU GLY LYS ILE SEQRES 21 C 467 VAL HIS ILE SER THR LEU SER GLY SER ALA GLN HIS VAL SEQRES 22 C 467 GLU GLU CYS SER CYS TYR PRO ARG PHE PRO GLY VAL ARG SEQRES 23 C 467 CYS VAL CYS ARG ASP ASN TRP LYS GLY SER ASN ARG PRO SEQRES 24 C 467 ILE VAL ASP ILE ASN VAL LYS ASN TYR SER ILE VAL SER SEQRES 25 C 467 SER TYR VAL CYS SER GLY LEU VAL GLY ASP THR PRO ARG SEQRES 26 C 467 LYS SER ASP SER VAL SER SER SER TYR CYS LEU ASP PRO SEQRES 27 C 467 ASN ASN GLU LYS GLY GLY HIS GLY VAL LYS GLY TRP ALA SEQRES 28 C 467 PHE ASP ASP GLY ASN ASP VAL TRP MET GLY ARG THR ILE SEQRES 29 C 467 ASN GLU THR LEU ARG LEU GLY TYR GLU THR PHE LYS VAL SEQRES 30 C 467 ILE GLU GLY TRP SER LYS ALA ASN SER LYS LEU GLN THR SEQRES 31 C 467 ASN ARG GLN VAL ILE VAL GLU LYS GLY ASP ARG SER GLY SEQRES 32 C 467 TYR SER GLY ILE PHE SER VAL GLU GLY LYS SER CYS ILE SEQRES 33 C 467 ASN ARG CYS PHE TYR VAL GLU LEU ILE ARG GLY ARG LYS SEQRES 34 C 467 GLU GLU THR LYS VAL TRP TRP THR SER ASN SER ILE VAL SEQRES 35 C 467 VAL PHE CYS GLY THR SER GLY THR TYR GLY THR GLY SER SEQRES 36 C 467 TRP PRO ASP GLY ALA ASP ILE ASN LEU MET PRO ILE SEQRES 1 F 118 GLU VAL LYS LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 F 118 PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 F 118 PHE THR PHE SER ASP TYR TYR MET TYR TRP VAL ARG GLN SEQRES 4 F 118 THR PRO GLU LYS ARG LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 F 118 ASN GLY GLY GLY SER THR TYR TYR PRO ASP THR VAL LYS SEQRES 6 F 118 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 F 118 LEU TYR LEU GLN MET SER ARG LEU LYS SER GLU ASP THR SEQRES 8 F 118 ALA MET TYR TYR CYS ALA ARG SER ASP ASP GLY ASP TYR SEQRES 9 F 118 PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SEQRES 10 F 118 SER SEQRES 1 J 111 ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU ALA VAL SEQRES 2 J 111 SER LEU GLY GLN ARG ALA THR ILE SER CYS ARG ALA SER SEQRES 3 J 111 GLN SER VAL SER THR SER SER TYR SER TYR MET HIS TRP SEQRES 4 J 111 TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE SEQRES 5 J 111 LYS TYR ALA SER ASN LEU GLU SER GLY VAL PRO ALA ARG SEQRES 6 J 111 PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU ASN SEQRES 7 J 111 ILE HIS PRO VAL GLU GLU GLU ASP THR ALA THR TYR TYR SEQRES 8 J 111 CYS GLN HIS SER TRP GLU ILE PRO LEU THR PHE GLY ALA SEQRES 9 J 111 GLY THR LYS LEU GLU LEU LYS SEQRES 1 D 467 MET TYR SER MET GLN LEU ALA SER CYS VAL THR LEU THR SEQRES 2 D 467 LEU VAL LEU LEU VAL ASN SER GLN HIS HIS HIS HIS HIS SEQRES 3 D 467 HIS GLY SER SER SER SER ASP TYR SER ASP LEU GLN ARG SEQRES 4 D 467 VAL LYS GLN GLU LEU LEU GLU GLU VAL LYS LYS GLU LEU SEQRES 5 D 467 GLN LYS VAL LYS GLU GLU ILE ILE GLU ALA PHE VAL GLN SEQRES 6 D 467 GLU LEU ARG LYS ARG GLY SER LEU VAL PRO ARG GLY SER SEQRES 7 D 467 GLY GLY GLU TYR ARG ASN TRP SER LYS PRO GLN CYS ASN SEQRES 8 D 467 ILE THR GLY PHE ALA PRO PHE SER LYS ASP ASN SER ILE SEQRES 9 D 467 ARG LEU SER ALA GLY GLY ASP ILE TRP VAL THR ARG GLU SEQRES 10 D 467 PRO TYR VAL SER CYS ASP PRO ASP LYS CYS TYR GLN PHE SEQRES 11 D 467 ALA LEU GLY GLN GLY THR THR LEU ASN ASN GLY HIS SER SEQRES 12 D 467 ASN ASN THR VAL HIS ASP ARG THR PRO TYR ARG THR LEU SEQRES 13 D 467 LEU MET ASN GLU LEU GLY VAL PRO PHE HIS LEU GLY THR SEQRES 14 D 467 ARG GLN VAL CYS MET ALA TRP SER SER SER SER CYS HIS SEQRES 15 D 467 ASP GLY LYS ALA TRP LEU HIS VAL CYS ILE THR GLY ASN SEQRES 16 D 467 ASP ASN ASN ALA THR ALA SER PHE ILE TYR ASN GLY ARG SEQRES 17 D 467 LEU VAL ASP SER ILE GLY SER TRP SER LYS ASN ILE LEU SEQRES 18 D 467 ARG THR GLN GLU SER GLU CYS VAL CYS ILE ASN GLY THR SEQRES 19 D 467 CYS THR VAL VAL MET THR ASP GLY SER ALA SER GLY LYS SEQRES 20 D 467 ALA ASP THR LYS ILE LEU PHE VAL GLU GLU GLY LYS ILE SEQRES 21 D 467 VAL HIS ILE SER THR LEU SER GLY SER ALA GLN HIS VAL SEQRES 22 D 467 GLU GLU CYS SER CYS TYR PRO ARG PHE PRO GLY VAL ARG SEQRES 23 D 467 CYS VAL CYS ARG ASP ASN TRP LYS GLY SER ASN ARG PRO SEQRES 24 D 467 ILE VAL ASP ILE ASN VAL LYS ASN TYR SER ILE VAL SER SEQRES 25 D 467 SER TYR VAL CYS SER GLY LEU VAL GLY ASP THR PRO ARG SEQRES 26 D 467 LYS SER ASP SER VAL SER SER SER TYR CYS LEU ASP PRO SEQRES 27 D 467 ASN ASN GLU LYS GLY GLY HIS GLY VAL LYS GLY TRP ALA SEQRES 28 D 467 PHE ASP ASP GLY ASN ASP VAL TRP MET GLY ARG THR ILE SEQRES 29 D 467 ASN GLU THR LEU ARG LEU GLY TYR GLU THR PHE LYS VAL SEQRES 30 D 467 ILE GLU GLY TRP SER LYS ALA ASN SER LYS LEU GLN THR SEQRES 31 D 467 ASN ARG GLN VAL ILE VAL GLU LYS GLY ASP ARG SER GLY SEQRES 32 D 467 TYR SER GLY ILE PHE SER VAL GLU GLY LYS SER CYS ILE SEQRES 33 D 467 ASN ARG CYS PHE TYR VAL GLU LEU ILE ARG GLY ARG LYS SEQRES 34 D 467 GLU GLU THR LYS VAL TRP TRP THR SER ASN SER ILE VAL SEQRES 35 D 467 VAL PHE CYS GLY THR SER GLY THR TYR GLY THR GLY SER SEQRES 36 D 467 TRP PRO ASP GLY ALA ASP ILE ASN LEU MET PRO ILE SEQRES 1 G 118 GLU VAL LYS LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 G 118 PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 G 118 PHE THR PHE SER ASP TYR TYR MET TYR TRP VAL ARG GLN SEQRES 4 G 118 THR PRO GLU LYS ARG LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 G 118 ASN GLY GLY GLY SER THR TYR TYR PRO ASP THR VAL LYS SEQRES 6 G 118 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 G 118 LEU TYR LEU GLN MET SER ARG LEU LYS SER GLU ASP THR SEQRES 8 G 118 ALA MET TYR TYR CYS ALA ARG SER ASP ASP GLY ASP TYR SEQRES 9 G 118 PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SEQRES 10 G 118 SER SEQRES 1 K 111 ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU ALA VAL SEQRES 2 K 111 SER LEU GLY GLN ARG ALA THR ILE SER CYS ARG ALA SER SEQRES 3 K 111 GLN SER VAL SER THR SER SER TYR SER TYR MET HIS TRP SEQRES 4 K 111 TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE SEQRES 5 K 111 LYS TYR ALA SER ASN LEU GLU SER GLY VAL PRO ALA ARG SEQRES 6 K 111 PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU ASN SEQRES 7 K 111 ILE HIS PRO VAL GLU GLU GLU ASP THR ALA THR TYR TYR SEQRES 8 K 111 CYS GLN HIS SER TRP GLU ILE PRO LEU THR PHE GLY ALA SEQRES 9 K 111 GLY THR LYS LEU GLU LEU LYS 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 NAG N 5 14 HET MAN N 6 11 HET MAN N 7 11 HET NAG O 1 14 HET NAG O 2 14 HET BMA O 3 11 HET MAN O 4 11 HET MAN O 5 11 HET NAG P 1 14 HET NAG P 2 14 HET NAG Q 1 14 HET NAG Q 2 14 HET BMA Q 3 11 HET MAN Q 4 11 HET NAG Q 5 14 HET MAN Q 6 11 HET MAN Q 7 11 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 NAG S 1 14 HET NAG S 2 14 HET NAG T 1 14 HET NAG T 2 14 HET BMA T 3 11 HET MAN T 4 11 HET NAG T 5 14 HET MAN T 6 11 HET MAN T 7 11 HET NAG U 1 14 HET NAG U 2 14 HET BMA U 3 11 HET MAN U 4 11 HET MAN U 5 11 HET NAG V 1 14 HET NAG V 2 14 HET NAG W 1 14 HET NAG W 2 14 HET BMA W 3 11 HET MAN W 4 11 HET NAG W 5 14 HET MAN W 6 11 HET MAN W 7 11 HET NAG X 1 14 HET NAG X 2 14 HET BMA X 3 11 HET MAN X 4 11 HET MAN X 5 11 HET CA A 501 1 HET NAG A 502 14 HET NAG A 503 14 HET NAG A 504 14 HET CA B 501 1 HET NAG B 502 14 HET NAG B 503 14 HET NAG B 504 14 HET CA C 501 1 HET NAG C 502 14 HET NAG C 503 14 HET NAG C 504 14 HET CA D 501 1 HET NAG D 502 14 HET NAG D 503 14 HET NAG D 504 14 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 13 NAG 40(C8 H15 N O6) FORMUL 14 BMA 8(C6 H12 O6) FORMUL 14 MAN 20(C6 H12 O6) FORMUL 25 CA 4(CA 2+) HELIX 1 AA1 ASN A 104 ALA A 110 1 7 HELIX 2 AA2 ASN A 142 ASN A 146 5 5 HELIX 3 AA3 THR H 28 TYR H 32 5 5 HELIX 4 AA4 LYS H 83 THR H 87 5 5 HELIX 5 AA5 GLU L 79 THR L 83 5 5 HELIX 6 AA6 ASN B 104 ALA B 110 1 7 HELIX 7 AA7 ASN B 142 ASN B 146 5 5 HELIX 8 AA8 THR E 28 TYR E 32 5 5 HELIX 9 AA9 LYS E 83 THR E 87 5 5 HELIX 10 AB1 GLU I 79 THR I 83 5 5 HELIX 11 AB2 ASN C 104 ALA C 110 1 7 HELIX 12 AB3 ASN C 142 ASN C 146 5 5 HELIX 13 AB4 THR F 28 TYR F 32 5 5 HELIX 14 AB5 LYS F 83 THR F 87 5 5 HELIX 15 AB6 GLU J 79 THR J 83 5 5 HELIX 16 AB7 ASN D 104 ALA D 110 1 7 HELIX 17 AB8 ASN D 142 ASN D 146 5 5 HELIX 18 AB9 THR G 28 TYR G 32 5 5 HELIX 19 AC1 LYS G 83 THR G 87 5 5 HELIX 20 AC2 GLU K 79 THR K 83 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 CYS A 447 N ALA A 98 SHEET 3 AA1 4 ILE A 418 GLY A 429 -1 N PHE A 422 O PHE A 446 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 TYR A 130 N SER A 123 SHEET 3 AA2 4 THR A 157 GLU A 162 -1 O ASN A 161 N GLN A 131 SHEET 4 AA2 4 ARG A 172 MET A 176 -1 O VAL A 174 N LEU A 158 SHEET 1 AA3 4 SER A 179 HIS A 184 0 SHEET 2 AA3 4 TRP A 189 THR A 195 -1 O LEU A 190 N CYS A 183 SHEET 3 AA3 4 THR A 202 TYR A 207 -1 O SER A 204 N CYS A 193 SHEET 4 AA3 4 ARG A 210 GLY A 216 -1 O ILE A 215 N ALA A 203 SHEET 1 AA4 3 LEU A 223 ARG A 224 0 SHEET 2 AA4 3 THR A 236 GLY A 244 -1 O THR A 242 N ARG A 224 SHEET 3 AA4 3 VAL A 231 ILE A 233 -1 N VAL A 231 O THR A 238 SHEET 1 AA5 4 LEU A 223 ARG A 224 0 SHEET 2 AA5 4 THR A 236 GLY A 244 -1 O THR A 242 N ARG A 224 SHEET 3 AA5 4 ALA A 250 GLU A 258 -1 O VAL A 257 N CYS A 237 SHEET 4 AA5 4 LYS A 261 THR A 267 -1 O SER A 266 N ILE A 254 SHEET 1 AA6 4 GLU A 276 ARG A 283 0 SHEET 2 AA6 4 GLY A 286 ARG A 292 -1 O ARG A 292 N GLU A 276 SHEET 3 AA6 4 PRO A 301 ILE A 305 -1 O ILE A 305 N VAL A 287 SHEET 4 AA6 4 ILE A 312 TYR A 316 -1 O SER A 315 N ILE A 302 SHEET 1 AA7 4 ALA A 353 ASP A 355 0 SHEET 2 AA7 4 VAL A 360 ARG A 364 -1 O TRP A 361 N PHE A 354 SHEET 3 AA7 4 LEU A 372 ILE A 380 -1 O GLU A 375 N ARG A 364 SHEET 4 AA7 4 LEU A 390 ARG A 403 -1 O THR A 392 N LYS A 378 SHEET 1 AA8 4 LYS H 3 SER H 7 0 SHEET 2 AA8 4 SER H 17 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AA8 4 THR H 77 SER H 82A-1 O LEU H 78 N CYS H 22 SHEET 4 AA8 4 PHE H 67 ASP H 72 -1 N THR H 68 O GLN H 81 SHEET 1 AA9 6 LEU H 11 VAL H 12 0 SHEET 2 AA9 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA9 6 ALA H 88 SER H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA9 6 TYR H 33 THR H 40 -1 N VAL H 37 O TYR H 91 SHEET 5 AA9 6 ARG H 44 ILE H 51 -1 O VAL H 48 N TRP H 36 SHEET 6 AA9 6 THR H 57 TYR H 58 -1 O TYR H 58 N TYR H 50 SHEET 1 AB1 4 LEU H 11 VAL H 12 0 SHEET 2 AB1 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AB1 4 ALA H 88 SER H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AB1 4 TYR H 102 TRP H 103 -1 O TYR H 102 N ARG H 94 SHEET 1 AB2 4 LEU L 4 SER L 7 0 SHEET 2 AB2 4 ILE L 21 ALA L 25 -1 O SER L 22 N SER L 7 SHEET 3 AB2 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AB2 4 PHE L 62 SER L 67 -1 N SER L 63 O ASN L 74 SHEET 1 AB3 6 SER L 10 VAL L 13 0 SHEET 2 AB3 6 THR L 102 LEU L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AB3 6 THR L 85 HIS L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB3 6 MET L 33 GLN L 38 -1 N HIS L 34 O GLN L 89 SHEET 5 AB3 6 LYS L 45 LYS L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AB3 6 ASN L 53 LEU L 54 -1 O ASN L 53 N LYS L 49 SHEET 1 AB4 4 GLY B 96 LYS B 102 0 SHEET 2 AB4 4 THR B 439 THR B 449 -1 O CYS B 447 N ALA B 98 SHEET 3 AB4 4 ILE B 418 GLY B 429 -1 N PHE B 422 O PHE B 446 SHEET 4 AB4 4 SER B 407 GLU B 413 -1 N VAL B 412 O ASN B 419 SHEET 1 AB5 4 TRP B 115 CYS B 124 0 SHEET 2 AB5 4 CYS B 129 THR B 139 -1 O TYR B 130 N SER B 123 SHEET 3 AB5 4 THR B 157 GLU B 162 -1 O ASN B 161 N GLN B 131 SHEET 4 AB5 4 ARG B 172 MET B 176 -1 O VAL B 174 N LEU B 158 SHEET 1 AB6 4 SER B 179 HIS B 184 0 SHEET 2 AB6 4 TRP B 189 THR B 195 -1 O LEU B 190 N CYS B 183 SHEET 3 AB6 4 THR B 202 TYR B 207 -1 O SER B 204 N CYS B 193 SHEET 4 AB6 4 ARG B 210 GLY B 216 -1 O ILE B 215 N ALA B 203 SHEET 1 AB7 3 LEU B 223 ARG B 224 0 SHEET 2 AB7 3 THR B 236 GLY B 244 -1 O THR B 242 N ARG B 224 SHEET 3 AB7 3 VAL B 231 ILE B 233 -1 N VAL B 231 O THR B 238 SHEET 1 AB8 4 LEU B 223 ARG B 224 0 SHEET 2 AB8 4 THR B 236 GLY B 244 -1 O THR B 242 N ARG B 224 SHEET 3 AB8 4 ALA B 250 GLU B 258 -1 O VAL B 257 N CYS B 237 SHEET 4 AB8 4 LYS B 261 THR B 267 -1 O SER B 266 N ILE B 254 SHEET 1 AB9 4 GLU B 276 ARG B 283 0 SHEET 2 AB9 4 GLY B 286 ARG B 292 -1 O ARG B 292 N GLU B 276 SHEET 3 AB9 4 PRO B 301 ILE B 305 -1 O ILE B 305 N VAL B 287 SHEET 4 AB9 4 ILE B 312 TYR B 316 -1 O SER B 315 N ILE B 302 SHEET 1 AC1 4 ALA B 353 ASP B 355 0 SHEET 2 AC1 4 VAL B 360 ARG B 364 -1 O TRP B 361 N PHE B 354 SHEET 3 AC1 4 LEU B 372 ILE B 380 -1 O GLU B 375 N ARG B 364 SHEET 4 AC1 4 LEU B 390 ARG B 403 -1 O THR B 392 N LYS B 378 SHEET 1 AC2 4 LYS E 3 SER E 7 0 SHEET 2 AC2 4 SER E 17 SER E 25 -1 O ALA E 23 N VAL E 5 SHEET 3 AC2 4 THR E 77 SER E 82A-1 O LEU E 78 N CYS E 22 SHEET 4 AC2 4 PHE E 67 ASP E 72 -1 N THR E 68 O GLN E 81 SHEET 1 AC3 6 LEU E 11 VAL E 12 0 SHEET 2 AC3 6 THR E 107 VAL E 111 1 O THR E 110 N VAL E 12 SHEET 3 AC3 6 ALA E 88 SER E 95 -1 N TYR E 90 O THR E 107 SHEET 4 AC3 6 TYR E 33 THR E 40 -1 N VAL E 37 O TYR E 91 SHEET 5 AC3 6 ARG E 44 ILE E 51 -1 O VAL E 48 N TRP E 36 SHEET 6 AC3 6 THR E 57 TYR E 58 -1 O TYR E 58 N TYR E 50 SHEET 1 AC4 4 LEU E 11 VAL E 12 0 SHEET 2 AC4 4 THR E 107 VAL E 111 1 O THR E 110 N VAL E 12 SHEET 3 AC4 4 ALA E 88 SER E 95 -1 N TYR E 90 O THR E 107 SHEET 4 AC4 4 TYR E 102 TRP E 103 -1 O TYR E 102 N ARG E 94 SHEET 1 AC5 4 LEU I 4 SER I 7 0 SHEET 2 AC5 4 ILE I 21 ALA I 25 -1 O ARG I 24 N THR I 5 SHEET 3 AC5 4 ASP I 70 ILE I 75 -1 O LEU I 73 N ILE I 21 SHEET 4 AC5 4 PHE I 62 SER I 67 -1 N SER I 63 O ASN I 74 SHEET 1 AC6 6 SER I 10 VAL I 13 0 SHEET 2 AC6 6 THR I 102 LEU I 106 1 O GLU I 105 N LEU I 11 SHEET 3 AC6 6 THR I 85 HIS I 90 -1 N TYR I 86 O THR I 102 SHEET 4 AC6 6 MET I 33 GLN I 38 -1 N HIS I 34 O GLN I 89 SHEET 5 AC6 6 LYS I 45 LYS I 49 -1 O LYS I 45 N GLN I 37 SHEET 6 AC6 6 ASN I 53 LEU I 54 -1 O ASN I 53 N LYS I 49 SHEET 1 AC7 4 GLY C 96 LYS C 102 0 SHEET 2 AC7 4 THR C 439 THR C 449 -1 O CYS C 447 N ALA C 98 SHEET 3 AC7 4 ILE C 418 GLY C 429 -1 N PHE C 422 O PHE C 446 SHEET 4 AC7 4 SER C 407 GLU C 413 -1 N VAL C 412 O ASN C 419 SHEET 1 AC8 4 TRP C 115 CYS C 124 0 SHEET 2 AC8 4 CYS C 129 THR C 139 -1 O TYR C 130 N SER C 123 SHEET 3 AC8 4 THR C 157 GLU C 162 -1 O ASN C 161 N GLN C 131 SHEET 4 AC8 4 ARG C 172 MET C 176 -1 O VAL C 174 N LEU C 158 SHEET 1 AC9 4 SER C 179 HIS C 184 0 SHEET 2 AC9 4 TRP C 189 THR C 195 -1 O LEU C 190 N CYS C 183 SHEET 3 AC9 4 THR C 202 TYR C 207 -1 O SER C 204 N CYS C 193 SHEET 4 AC9 4 ARG C 210 GLY C 216 -1 O ILE C 215 N ALA C 203 SHEET 1 AD1 3 LEU C 223 ARG C 224 0 SHEET 2 AD1 3 THR C 236 GLY C 244 -1 O THR C 242 N ARG C 224 SHEET 3 AD1 3 VAL C 231 ILE C 233 -1 N VAL C 231 O THR C 238 SHEET 1 AD2 4 LEU C 223 ARG C 224 0 SHEET 2 AD2 4 THR C 236 GLY C 244 -1 O THR C 242 N ARG C 224 SHEET 3 AD2 4 ALA C 250 GLU C 258 -1 O VAL C 257 N CYS C 237 SHEET 4 AD2 4 LYS C 261 THR C 267 -1 O SER C 266 N ILE C 254 SHEET 1 AD3 4 GLU C 276 ARG C 283 0 SHEET 2 AD3 4 GLY C 286 ARG C 292 -1 O ARG C 292 N GLU C 276 SHEET 3 AD3 4 PRO C 301 ILE C 305 -1 O ILE C 305 N VAL C 287 SHEET 4 AD3 4 ILE C 312 TYR C 316 -1 O SER C 315 N ILE C 302 SHEET 1 AD4 4 ALA C 353 ASP C 355 0 SHEET 2 AD4 4 VAL C 360 ARG C 364 -1 O TRP C 361 N PHE C 354 SHEET 3 AD4 4 LEU C 372 ILE C 380 -1 O GLU C 375 N ARG C 364 SHEET 4 AD4 4 LEU C 390 ARG C 403 -1 O THR C 392 N LYS C 378 SHEET 1 AD5 4 LYS F 3 SER F 7 0 SHEET 2 AD5 4 SER F 17 SER F 25 -1 O ALA F 23 N VAL F 5 SHEET 3 AD5 4 THR F 77 SER F 82A-1 O LEU F 78 N CYS F 22 SHEET 4 AD5 4 PHE F 67 ASP F 72 -1 N THR F 68 O GLN F 81 SHEET 1 AD6 6 LEU F 11 VAL F 12 0 SHEET 2 AD6 6 THR F 107 VAL F 111 1 O THR F 110 N VAL F 12 SHEET 3 AD6 6 ALA F 88 SER F 95 -1 N TYR F 90 O THR F 107 SHEET 4 AD6 6 TYR F 33 THR F 40 -1 N VAL F 37 O TYR F 91 SHEET 5 AD6 6 ARG F 44 ILE F 51 -1 O VAL F 48 N TRP F 36 SHEET 6 AD6 6 THR F 57 TYR F 58 -1 O TYR F 58 N TYR F 50 SHEET 1 AD7 4 LEU F 11 VAL F 12 0 SHEET 2 AD7 4 THR F 107 VAL F 111 1 O THR F 110 N VAL F 12 SHEET 3 AD7 4 ALA F 88 SER F 95 -1 N TYR F 90 O THR F 107 SHEET 4 AD7 4 TYR F 102 TRP F 103 -1 O TYR F 102 N ARG F 94 SHEET 1 AD8 4 LEU J 4 SER J 7 0 SHEET 2 AD8 4 ILE J 21 ALA J 25 -1 O ARG J 24 N THR J 5 SHEET 3 AD8 4 ASP J 70 ILE J 75 -1 O LEU J 73 N ILE J 21 SHEET 4 AD8 4 PHE J 62 SER J 67 -1 N SER J 63 O ASN J 74 SHEET 1 AD9 6 SER J 10 VAL J 13 0 SHEET 2 AD9 6 THR J 102 LEU J 106 1 O GLU J 105 N LEU J 11 SHEET 3 AD9 6 THR J 85 HIS J 90 -1 N TYR J 86 O THR J 102 SHEET 4 AD9 6 MET J 33 GLN J 38 -1 N HIS J 34 O GLN J 89 SHEET 5 AD9 6 LYS J 45 LYS J 49 -1 O LYS J 45 N GLN J 37 SHEET 6 AD9 6 ASN J 53 LEU J 54 -1 O ASN J 53 N LYS J 49 SHEET 1 AE1 4 GLY D 96 LYS D 102 0 SHEET 2 AE1 4 THR D 439 THR D 449 -1 O CYS D 447 N ALA D 98 SHEET 3 AE1 4 ILE D 418 GLY D 429 -1 N PHE D 422 O PHE D 446 SHEET 4 AE1 4 SER D 407 GLU D 413 -1 N VAL D 412 O ASN D 419 SHEET 1 AE2 4 TRP D 115 CYS D 124 0 SHEET 2 AE2 4 CYS D 129 THR D 139 -1 O TYR D 130 N SER D 123 SHEET 3 AE2 4 THR D 157 GLU D 162 -1 O ASN D 161 N GLN D 131 SHEET 4 AE2 4 ARG D 172 MET D 176 -1 O VAL D 174 N LEU D 158 SHEET 1 AE3 4 SER D 179 HIS D 184 0 SHEET 2 AE3 4 TRP D 189 THR D 195 -1 O LEU D 190 N CYS D 183 SHEET 3 AE3 4 THR D 202 TYR D 207 -1 O SER D 204 N CYS D 193 SHEET 4 AE3 4 ARG D 210 GLY D 216 -1 O ILE D 215 N ALA D 203 SHEET 1 AE4 3 LEU D 223 ARG D 224 0 SHEET 2 AE4 3 THR D 236 GLY D 244 -1 O THR D 242 N ARG D 224 SHEET 3 AE4 3 VAL D 231 ILE D 233 -1 N VAL D 231 O THR D 238 SHEET 1 AE5 4 LEU D 223 ARG D 224 0 SHEET 2 AE5 4 THR D 236 GLY D 244 -1 O THR D 242 N ARG D 224 SHEET 3 AE5 4 ALA D 250 GLU D 258 -1 O VAL D 257 N CYS D 237 SHEET 4 AE5 4 LYS D 261 THR D 267 -1 O SER D 266 N ILE D 254 SHEET 1 AE6 4 GLU D 276 ARG D 283 0 SHEET 2 AE6 4 GLY D 286 ARG D 292 -1 O ARG D 292 N GLU D 276 SHEET 3 AE6 4 PRO D 301 ILE D 305 -1 O ILE D 305 N VAL D 287 SHEET 4 AE6 4 ILE D 312 TYR D 316 -1 O SER D 315 N ILE D 302 SHEET 1 AE7 4 ALA D 353 ASP D 355 0 SHEET 2 AE7 4 VAL D 360 ARG D 364 -1 O TRP D 361 N PHE D 354 SHEET 3 AE7 4 LEU D 372 ILE D 380 -1 O GLU D 375 N ARG D 364 SHEET 4 AE7 4 LEU D 390 ARG D 403 -1 O THR D 392 N LYS D 378 SHEET 1 AE8 4 LYS G 3 SER G 7 0 SHEET 2 AE8 4 SER G 17 SER G 25 -1 O ALA G 23 N VAL G 5 SHEET 3 AE8 4 THR G 77 SER G 82A-1 O LEU G 78 N CYS G 22 SHEET 4 AE8 4 PHE G 67 ASP G 72 -1 N THR G 68 O GLN G 81 SHEET 1 AE9 6 LEU G 11 VAL G 12 0 SHEET 2 AE9 6 THR G 107 VAL G 111 1 O THR G 110 N VAL G 12 SHEET 3 AE9 6 ALA G 88 SER G 95 -1 N TYR G 90 O THR G 107 SHEET 4 AE9 6 TYR G 33 THR G 40 -1 N VAL G 37 O TYR G 91 SHEET 5 AE9 6 ARG G 44 ILE G 51 -1 O VAL G 48 N TRP G 36 SHEET 6 AE9 6 THR G 57 TYR G 58 -1 O TYR G 58 N TYR G 50 SHEET 1 AF1 4 LEU G 11 VAL G 12 0 SHEET 2 AF1 4 THR G 107 VAL G 111 1 O THR G 110 N VAL G 12 SHEET 3 AF1 4 ALA G 88 SER G 95 -1 N TYR G 90 O THR G 107 SHEET 4 AF1 4 TYR G 102 TRP G 103 -1 O TYR G 102 N ARG G 94 SHEET 1 AF2 4 LEU K 4 SER K 7 0 SHEET 2 AF2 4 ILE K 21 ALA K 25 -1 O SER K 22 N SER K 7 SHEET 3 AF2 4 ASP K 70 ILE K 75 -1 O LEU K 73 N ILE K 21 SHEET 4 AF2 4 PHE K 62 SER K 67 -1 N SER K 63 O ASN K 74 SHEET 1 AF3 6 SER K 10 VAL K 13 0 SHEET 2 AF3 6 THR K 102 LEU K 106 1 O GLU K 105 N LEU K 11 SHEET 3 AF3 6 THR K 85 HIS K 90 -1 N TYR K 86 O THR K 102 SHEET 4 AF3 6 MET K 33 GLN K 38 -1 N HIS K 34 O GLN K 89 SHEET 5 AF3 6 LYS K 45 LYS K 49 -1 O LYS K 45 N GLN K 37 SHEET 6 AF3 6 ASN K 53 LEU K 54 -1 O ASN K 53 N LYS K 49 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 2.03 SSBOND 4 CYS A 183 CYS A 230 1555 1555 2.03 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 2.04 SSBOND 9 CYS A 421 CYS A 447 1555 1555 2.03 SSBOND 10 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 11 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 12 CYS B 92 CYS B 417 1555 1555 2.03 SSBOND 13 CYS B 124 CYS B 129 1555 1555 2.03 SSBOND 14 CYS B 175 CYS B 193 1555 1555 2.03 SSBOND 15 CYS B 183 CYS B 230 1555 1555 2.03 SSBOND 16 CYS B 232 CYS B 237 1555 1555 2.03 SSBOND 17 CYS B 278 CYS B 291 1555 1555 2.03 SSBOND 18 CYS B 280 CYS B 289 1555 1555 2.03 SSBOND 19 CYS B 318 CYS B 337 1555 1555 2.03 SSBOND 20 CYS B 421 CYS B 447 1555 1555 2.03 SSBOND 21 CYS E 22 CYS E 92 1555 1555 2.03 SSBOND 22 CYS I 23 CYS I 88 1555 1555 2.03 SSBOND 23 CYS C 92 CYS C 417 1555 1555 2.03 SSBOND 24 CYS C 124 CYS C 129 1555 1555 2.03 SSBOND 25 CYS C 175 CYS C 193 1555 1555 2.03 SSBOND 26 CYS C 183 CYS C 230 1555 1555 2.03 SSBOND 27 CYS C 232 CYS C 237 1555 1555 2.03 SSBOND 28 CYS C 278 CYS C 291 1555 1555 2.03 SSBOND 29 CYS C 280 CYS C 289 1555 1555 2.03 SSBOND 30 CYS C 318 CYS C 337 1555 1555 2.04 SSBOND 31 CYS C 421 CYS C 447 1555 1555 2.03 SSBOND 32 CYS F 22 CYS F 92 1555 1555 2.03 SSBOND 33 CYS J 23 CYS J 88 1555 1555 2.03 SSBOND 34 CYS D 92 CYS D 417 1555 1555 2.03 SSBOND 35 CYS D 124 CYS D 129 1555 1555 2.03 SSBOND 36 CYS D 175 CYS D 193 1555 1555 2.03 SSBOND 37 CYS D 183 CYS D 230 1555 1555 2.03 SSBOND 38 CYS D 232 CYS D 237 1555 1555 2.03 SSBOND 39 CYS D 278 CYS D 291 1555 1555 2.03 SSBOND 40 CYS D 280 CYS D 289 1555 1555 2.03 SSBOND 41 CYS D 318 CYS D 337 1555 1555 2.04 SSBOND 42 CYS D 421 CYS D 447 1555 1555 2.03 SSBOND 43 CYS G 22 CYS G 92 1555 1555 2.03 SSBOND 44 CYS K 23 CYS K 88 1555 1555 2.03 LINK ND2 ASN A 93 C1 NAG A 502 1555 1555 1.44 LINK ND2 ASN A 146 C1 NAG M 1 1555 1555 1.44 LINK ND2 ASN A 200 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN A 234 C1 NAG A 503 1555 1555 1.44 LINK ND2 ASN A 309 C1 NAG A 504 1555 1555 1.44 LINK ND2 ASN A 367 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN B 93 C1 NAG B 502 1555 1555 1.44 LINK ND2 ASN B 146 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN B 200 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN B 234 C1 NAG B 503 1555 1555 1.44 LINK ND2 ASN B 309 C1 NAG B 504 1555 1555 1.44 LINK ND2 ASN B 367 C1 NAG R 1 1555 1555 1.43 LINK ND2 ASN C 93 C1 NAG C 502 1555 1555 1.44 LINK ND2 ASN C 146 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN C 200 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN C 234 C1 NAG C 503 1555 1555 1.44 LINK ND2 ASN C 309 C1 NAG C 504 1555 1555 1.44 LINK ND2 ASN C 367 C1 NAG U 1 1555 1555 1.43 LINK ND2 ASN D 93 C1 NAG D 502 1555 1555 1.44 LINK ND2 ASN D 146 C1 NAG V 1 1555 1555 1.44 LINK ND2 ASN D 200 C1 NAG W 1 1555 1555 1.44 LINK ND2 ASN D 234 C1 NAG D 503 1555 1555 1.44 LINK ND2 ASN D 309 C1 NAG D 504 1555 1555 1.44 LINK ND2 ASN D 367 C1 NAG X 1 1555 1555 1.43 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.44 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 1.45 LINK O2 MAN N 4 C1 NAG N 5 1555 1555 1.44 LINK O3 MAN N 6 C1 MAN N 7 1555 1555 1.44 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.44 LINK O4 NAG O 2 C1 BMA O 3 1555 1555 1.44 LINK O3 BMA O 3 C1 MAN O 4 1555 1555 1.45 LINK O6 BMA O 3 C1 MAN O 5 1555 1555 1.45 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.44 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.44 LINK O4 NAG Q 2 C1 BMA Q 3 1555 1555 1.45 LINK O3 BMA Q 3 C1 MAN Q 4 1555 1555 1.45 LINK O6 BMA Q 3 C1 MAN Q 6 1555 1555 1.45 LINK O2 MAN Q 4 C1 NAG Q 5 1555 1555 1.44 LINK O3 MAN Q 6 C1 MAN Q 7 1555 1555 1.44 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.44 LINK O4 NAG R 2 C1 BMA R 3 1555 1555 1.44 LINK O3 BMA R 3 C1 MAN R 4 1555 1555 1.45 LINK O6 BMA R 3 C1 MAN R 5 1555 1555 1.44 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.44 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.44 LINK O4 NAG T 2 C1 BMA T 3 1555 1555 1.45 LINK O3 BMA T 3 C1 MAN T 4 1555 1555 1.45 LINK O6 BMA T 3 C1 MAN T 6 1555 1555 1.45 LINK O2 MAN T 4 C1 NAG T 5 1555 1555 1.44 LINK O3 MAN T 6 C1 MAN T 7 1555 1555 1.44 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.44 LINK O4 NAG U 2 C1 BMA U 3 1555 1555 1.44 LINK O3 BMA U 3 C1 MAN U 4 1555 1555 1.45 LINK O6 BMA U 3 C1 MAN U 5 1555 1555 1.44 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.44 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.44 LINK O4 NAG W 2 C1 BMA W 3 1555 1555 1.45 LINK O3 BMA W 3 C1 MAN W 4 1555 1555 1.45 LINK O6 BMA W 3 C1 MAN W 6 1555 1555 1.45 LINK O2 MAN W 4 C1 NAG W 5 1555 1555 1.44 LINK O3 MAN W 6 C1 MAN W 7 1555 1555 1.44 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.44 LINK O4 NAG X 2 C1 BMA X 3 1555 1555 1.44 LINK O3 BMA X 3 C1 MAN X 4 1555 1555 1.45 LINK O6 BMA X 3 C1 MAN X 5 1555 1555 1.44 LINK O ASP A 293 CA CA A 501 1555 1555 2.43 LINK O GLY A 297 CA CA A 501 1555 1555 2.44 LINK OD2 ASP A 324 CA CA A 501 1555 1555 2.43 LINK O GLY A 345 CA CA A 501 1555 1555 2.80 LINK O HIS A 347 CA CA A 501 1555 1555 2.43 LINK O ASP B 293 CA CA B 501 1555 1555 2.43 LINK O GLY B 297 CA CA B 501 1555 1555 2.44 LINK OD2 ASP B 324 CA CA B 501 1555 1555 2.43 LINK O GLY B 345 CA CA B 501 1555 1555 2.79 LINK O HIS B 347 CA CA B 501 1555 1555 2.43 LINK O ASP C 293 CA CA C 501 1555 1555 2.43 LINK O GLY C 297 CA CA C 501 1555 1555 2.45 LINK OD2 ASP C 324 CA CA C 501 1555 1555 2.43 LINK O GLY C 345 CA CA C 501 1555 1555 2.79 LINK O HIS C 347 CA CA C 501 1555 1555 2.43 LINK O ASP D 293 CA CA D 501 1555 1555 2.43 LINK O GLY D 297 CA CA D 501 1555 1555 2.44 LINK OD2 ASP D 324 CA CA D 501 1555 1555 2.43 LINK O GLY D 345 CA CA D 501 1555 1555 2.79 LINK O HIS D 347 CA CA D 501 1555 1555 2.43 CISPEP 1 PHE A 284 PRO A 285 0 2.98 CISPEP 2 THR A 325 PRO A 326 0 6.52 CISPEP 3 ARG A 430 LYS A 431 0 4.07 CISPEP 4 SER L 7 PRO L 8 0 -1.82 CISPEP 5 HIS L 76 PRO L 77 0 -2.22 CISPEP 6 PHE B 284 PRO B 285 0 2.88 CISPEP 7 THR B 325 PRO B 326 0 6.34 CISPEP 8 ARG B 430 LYS B 431 0 4.21 CISPEP 9 SER I 7 PRO I 8 0 -2.11 CISPEP 10 HIS I 76 PRO I 77 0 -2.23 CISPEP 11 PHE C 284 PRO C 285 0 2.86 CISPEP 12 THR C 325 PRO C 326 0 6.37 CISPEP 13 ARG C 430 LYS C 431 0 4.20 CISPEP 14 SER J 7 PRO J 8 0 -1.95 CISPEP 15 HIS J 76 PRO J 77 0 -2.25 CISPEP 16 PHE D 284 PRO D 285 0 2.92 CISPEP 17 THR D 325 PRO D 326 0 6.34 CISPEP 18 ARG D 430 LYS D 431 0 4.20 CISPEP 19 SER K 7 PRO K 8 0 -2.02 CISPEP 20 HIS K 76 PRO K 77 0 -2.17 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