HEADER VIRAL PROTEIN/IMMUNE SYSTEM 05-DEC-24 9MD5 TITLE NEURAMINIDASE IN COMPLEX WITH MAB 6-23.2 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 6-23.2 HEAVY CHAIN; COMPND 7 CHAIN: H, E, F, G; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: MAB 6-23.2 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, INFLUENZA, NEURAMINIDASE, 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 9MD5 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 : 77151 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 9MD5 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_1000290604. 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 MAB6-23.2 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: DODECAMERIC 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 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 O ALA C 246 ND2 ASN C 294 2.14 REMARK 500 NH1 ARG B 152 OD2 ASP B 198 2.18 REMARK 500 NH1 ARG C 152 OD2 ASP C 198 2.18 REMARK 500 NH1 ARG A 152 OD2 ASP A 198 2.19 REMARK 500 NH1 ARG D 152 OD2 ASP D 198 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 417 CA - CB - SG ANGL. DEV. = 6.7 DEGREES REMARK 500 CYS B 417 CA - CB - SG ANGL. DEV. = 6.7 DEGREES REMARK 500 CYS C 417 CA - CB - SG ANGL. DEV. = 6.7 DEGREES REMARK 500 CYS D 417 CA - CB - SG ANGL. DEV. = 6.7 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 ARG A 118 -167.29 -160.31 REMARK 500 THR A 148 30.62 -97.82 REMARK 500 ILE A 222 92.39 50.89 REMARK 500 HIS A 347 172.81 62.18 REMARK 500 VAL H 48 -56.66 -124.87 REMARK 500 ASN H 52 -178.20 -66.87 REMARK 500 SER H 65 -3.15 71.05 REMARK 500 ASN H 73 -65.04 61.21 REMARK 500 ASP H 86 53.81 -91.40 REMARK 500 GLU H 100 -2.98 59.24 REMARK 500 TRP H 100D 53.31 -91.33 REMARK 500 ALA L 51 -6.77 68.88 REMARK 500 ARG B 118 -167.31 -160.38 REMARK 500 THR B 148 30.84 -97.56 REMARK 500 ILE B 222 92.40 50.96 REMARK 500 HIS B 347 172.96 62.13 REMARK 500 VAL E 48 -56.71 -124.82 REMARK 500 ASN E 52 -178.25 -66.84 REMARK 500 SER E 65 -3.15 71.05 REMARK 500 ASN E 73 -65.04 61.21 REMARK 500 ASP E 86 53.91 -91.40 REMARK 500 GLU E 100 -2.74 59.44 REMARK 500 TRP E 100D 53.33 -91.35 REMARK 500 ALA I 51 -6.81 68.94 REMARK 500 ARG C 118 -167.31 -160.38 REMARK 500 THR C 148 30.81 -97.57 REMARK 500 ILE C 222 92.45 50.93 REMARK 500 HIS C 347 172.91 62.01 REMARK 500 VAL F 48 -56.71 -124.82 REMARK 500 ASN F 52 -178.25 -66.87 REMARK 500 SER F 65 -3.15 71.05 REMARK 500 ASN F 73 -65.04 61.21 REMARK 500 ASP F 86 53.91 -91.40 REMARK 500 GLU F 100 -2.73 59.35 REMARK 500 TRP F 100D 53.37 -91.35 REMARK 500 ALA J 51 -6.77 68.95 REMARK 500 ARG D 118 -167.32 -160.34 REMARK 500 THR D 148 30.65 -97.85 REMARK 500 ILE D 222 92.42 50.88 REMARK 500 HIS D 347 172.96 62.22 REMARK 500 VAL G 48 -56.66 -124.86 REMARK 500 ASN G 52 -178.20 -66.87 REMARK 500 SER G 65 -3.15 71.05 REMARK 500 ASN G 73 -65.04 61.21 REMARK 500 ASP G 86 53.81 -91.40 REMARK 500 GLU G 100 -2.92 59.25 REMARK 500 TRP G 100D 53.33 -91.38 REMARK 500 ALA K 51 -6.79 68.92 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 CYS A 417 ILE A 418 148.02 REMARK 500 CYS B 417 ILE B 418 148.02 REMARK 500 CYS C 417 ILE C 418 148.02 REMARK 500 CYS D 417 ILE D 418 148.02 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 73.7 REMARK 620 3 ASP A 324 OD2 88.7 85.9 REMARK 620 4 GLY A 345 O 95.9 89.2 172.1 REMARK 620 5 HIS A 347 O 113.1 167.5 104.4 79.7 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 72.6 REMARK 620 3 ASP B 324 OD2 88.1 86.2 REMARK 620 4 GLY B 345 O 95.8 88.9 172.6 REMARK 620 5 HIS B 347 O 114.1 167.5 104.1 80.1 REMARK 620 N 1 2 3 4 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 72.6 REMARK 620 3 ASP C 324 OD2 88.1 85.9 REMARK 620 4 GLY C 345 O 96.4 89.0 171.9 REMARK 620 5 HIS C 347 O 114.0 167.5 104.5 79.9 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 72.7 REMARK 620 3 ASP D 324 OD2 88.7 86.3 REMARK 620 4 GLY D 345 O 96.0 89.0 172.0 REMARK 620 5 HIS D 347 O 114.5 167.0 104.3 79.7 REMARK 620 N 1 2 3 4 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-48168 RELATED DB: EMDB REMARK 900 NEURAMINIDASE IN COMPLEX WITH MAB 6-23.2 DBREF 9MD5 A 3 469 PDB 9MD5 9MD5 3 469 DBREF 9MD5 H 1 113 PDB 9MD5 9MD5 1 113 DBREF 9MD5 L 1 107 PDB 9MD5 9MD5 1 107 DBREF 9MD5 B 3 469 PDB 9MD5 9MD5 3 469 DBREF 9MD5 E 1 113 PDB 9MD5 9MD5 1 113 DBREF 9MD5 I 1 107 PDB 9MD5 9MD5 1 107 DBREF 9MD5 C 3 469 PDB 9MD5 9MD5 3 469 DBREF 9MD5 F 1 113 PDB 9MD5 9MD5 1 113 DBREF 9MD5 J 1 107 PDB 9MD5 9MD5 1 107 DBREF 9MD5 D 3 469 PDB 9MD5 9MD5 3 469 DBREF 9MD5 G 1 113 PDB 9MD5 9MD5 1 113 DBREF 9MD5 K 1 107 PDB 9MD5 9MD5 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 123 GLU MET LYS LEU VAL GLU SER GLU GLY GLY LEU VAL GLN SEQRES 2 H 123 PRO GLY ARG SER MET LYS LEU SER CYS THR ALA SER GLY SEQRES 3 H 123 PHE THR PHE SER ASP TYR TYR MET ALA TRP VAL ARG GLN SEQRES 4 H 123 VAL PRO GLU LYS GLY LEU GLU TRP VAL ALA LYS ILE ASN SEQRES 5 H 123 TYR ASP GLY SER SER THR TYR TYR LEU ASP SER LEU LYS SEQRES 6 H 123 SER ARG PHE PHE ILE SER ARG ASP ASN ALA LYS ASN ILE SEQRES 7 H 123 LEU TYR LEU GLN MET SER SER LEU LYS SER GLU ASP THR SEQRES 8 H 123 ALA THR TYR TYR CYS ALA ARG ALA HIS TYR VAL ASP GLU SEQRES 9 H 123 ARG SER TYR TRP TYR PHE ASP VAL TRP GLY THR GLY THR SEQRES 10 H 123 THR VAL THR VAL SER SER SEQRES 1 L 107 ASP ILE VAL MET THR GLN SER HIS LYS PHE MET SER THR SEQRES 2 L 107 SER VAL GLY ASP ARG VAL SER ILE THR CYS LYS ALA SER SEQRES 3 L 107 GLN ASP VAL GLY PRO ALA VAL ALA TRP TYR ARG GLN LYS SEQRES 4 L 107 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR TRP ALA SER SEQRES 5 L 107 THR ARG HIS THR GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6 L 107 GLY SER GLY THR ASP PHE THR LEU THR ILE SER ASN VAL SEQRES 7 L 107 GLN SER GLU ASP LEU ALA ASP TYR PHE CYS GLN GLN PHE SEQRES 8 L 107 SER SER TYR PRO LEU THR PHE GLY SER GLY THR LYS LEU SEQRES 9 L 107 GLU ILE 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 123 GLU MET LYS LEU VAL GLU SER GLU GLY GLY LEU VAL GLN SEQRES 2 E 123 PRO GLY ARG SER MET LYS LEU SER CYS THR ALA SER GLY SEQRES 3 E 123 PHE THR PHE SER ASP TYR TYR MET ALA TRP VAL ARG GLN SEQRES 4 E 123 VAL PRO GLU LYS GLY LEU GLU TRP VAL ALA LYS ILE ASN SEQRES 5 E 123 TYR ASP GLY SER SER THR TYR TYR LEU ASP SER LEU LYS SEQRES 6 E 123 SER ARG PHE PHE ILE SER ARG ASP ASN ALA LYS ASN ILE SEQRES 7 E 123 LEU TYR LEU GLN MET SER SER LEU LYS SER GLU ASP THR SEQRES 8 E 123 ALA THR TYR TYR CYS ALA ARG ALA HIS TYR VAL ASP GLU SEQRES 9 E 123 ARG SER TYR TRP TYR PHE ASP VAL TRP GLY THR GLY THR SEQRES 10 E 123 THR VAL THR VAL SER SER SEQRES 1 I 107 ASP ILE VAL MET THR GLN SER HIS LYS PHE MET SER THR SEQRES 2 I 107 SER VAL GLY ASP ARG VAL SER ILE THR CYS LYS ALA SER SEQRES 3 I 107 GLN ASP VAL GLY PRO ALA VAL ALA TRP TYR ARG GLN LYS SEQRES 4 I 107 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR TRP ALA SER SEQRES 5 I 107 THR ARG HIS THR GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6 I 107 GLY SER GLY THR ASP PHE THR LEU THR ILE SER ASN VAL SEQRES 7 I 107 GLN SER GLU ASP LEU ALA ASP TYR PHE CYS GLN GLN PHE SEQRES 8 I 107 SER SER TYR PRO LEU THR PHE GLY SER GLY THR LYS LEU SEQRES 9 I 107 GLU ILE 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 123 GLU MET LYS LEU VAL GLU SER GLU GLY GLY LEU VAL GLN SEQRES 2 F 123 PRO GLY ARG SER MET LYS LEU SER CYS THR ALA SER GLY SEQRES 3 F 123 PHE THR PHE SER ASP TYR TYR MET ALA TRP VAL ARG GLN SEQRES 4 F 123 VAL PRO GLU LYS GLY LEU GLU TRP VAL ALA LYS ILE ASN SEQRES 5 F 123 TYR ASP GLY SER SER THR TYR TYR LEU ASP SER LEU LYS SEQRES 6 F 123 SER ARG PHE PHE ILE SER ARG ASP ASN ALA LYS ASN ILE SEQRES 7 F 123 LEU TYR LEU GLN MET SER SER LEU LYS SER GLU ASP THR SEQRES 8 F 123 ALA THR TYR TYR CYS ALA ARG ALA HIS TYR VAL ASP GLU SEQRES 9 F 123 ARG SER TYR TRP TYR PHE ASP VAL TRP GLY THR GLY THR SEQRES 10 F 123 THR VAL THR VAL SER SER SEQRES 1 J 107 ASP ILE VAL MET THR GLN SER HIS LYS PHE MET SER THR SEQRES 2 J 107 SER VAL GLY ASP ARG VAL SER ILE THR CYS LYS ALA SER SEQRES 3 J 107 GLN ASP VAL GLY PRO ALA VAL ALA TRP TYR ARG GLN LYS SEQRES 4 J 107 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR TRP ALA SER SEQRES 5 J 107 THR ARG HIS THR GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6 J 107 GLY SER GLY THR ASP PHE THR LEU THR ILE SER ASN VAL SEQRES 7 J 107 GLN SER GLU ASP LEU ALA ASP TYR PHE CYS GLN GLN PHE SEQRES 8 J 107 SER SER TYR PRO LEU THR PHE GLY SER GLY THR LYS LEU SEQRES 9 J 107 GLU ILE 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 123 GLU MET LYS LEU VAL GLU SER GLU GLY GLY LEU VAL GLN SEQRES 2 G 123 PRO GLY ARG SER MET LYS LEU SER CYS THR ALA SER GLY SEQRES 3 G 123 PHE THR PHE SER ASP TYR TYR MET ALA TRP VAL ARG GLN SEQRES 4 G 123 VAL PRO GLU LYS GLY LEU GLU TRP VAL ALA LYS ILE ASN SEQRES 5 G 123 TYR ASP GLY SER SER THR TYR TYR LEU ASP SER LEU LYS SEQRES 6 G 123 SER ARG PHE PHE ILE SER ARG ASP ASN ALA LYS ASN ILE SEQRES 7 G 123 LEU TYR LEU GLN MET SER SER LEU LYS SER GLU ASP THR SEQRES 8 G 123 ALA THR TYR TYR CYS ALA ARG ALA HIS TYR VAL ASP GLU SEQRES 9 G 123 ARG SER TYR TRP TYR PHE ASP VAL TRP GLY THR GLY THR SEQRES 10 G 123 THR VAL THR VAL SER SER SEQRES 1 K 107 ASP ILE VAL MET THR GLN SER HIS LYS PHE MET SER THR SEQRES 2 K 107 SER VAL GLY ASP ARG VAL SER ILE THR CYS LYS ALA SER SEQRES 3 K 107 GLN ASP VAL GLY PRO ALA VAL ALA TRP TYR ARG GLN LYS SEQRES 4 K 107 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR TRP ALA SER SEQRES 5 K 107 THR ARG HIS THR GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6 K 107 GLY SER GLY THR ASP PHE THR LEU THR ILE SER ASN VAL SEQRES 7 K 107 GLN SER GLU ASP LEU ALA ASP TYR PHE CYS GLN GLN PHE SEQRES 8 K 107 SER SER TYR PRO LEU THR PHE GLY SER GLY THR LYS LEU SEQRES 9 K 107 GLU ILE LYS HET NAG M 1 14 HET NAG M 2 14 HET BMA M 3 11 HET MAN M 4 11 HET NAG M 5 14 HET MAN M 6 11 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 NAG O 1 14 HET NAG O 2 14 HET BMA O 3 11 HET MAN O 4 11 HET NAG O 5 14 HET MAN O 6 11 HET NAG P 1 14 HET NAG P 2 14 HET BMA P 3 11 HET MAN P 4 11 HET NAG P 5 14 HET MAN P 6 11 HET NAG A 501 14 HET NAG A 502 14 HET CA A 503 1 HET NAG A 504 14 HET NAG A 505 14 HET NAG A 506 14 HET NAG B 501 14 HET NAG B 502 14 HET CA B 503 1 HET NAG B 504 14 HET NAG B 505 14 HET NAG B 506 14 HET NAG C 501 14 HET NAG C 502 14 HET CA C 503 1 HET NAG C 504 14 HET NAG C 505 14 HET NAG C 506 14 HET NAG D 501 14 HET NAG D 502 14 HET CA D 503 1 HET NAG D 504 14 HET NAG D 505 14 HET NAG D 506 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 32(C8 H15 N O6) FORMUL 13 BMA 4(C6 H12 O6) FORMUL 13 MAN 8(C6 H12 O6) FORMUL 19 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 ASN B 104 ALA B 110 1 7 HELIX 5 AA5 ASN B 142 ASN B 146 5 5 HELIX 6 AA6 THR E 28 TYR E 32 5 5 HELIX 7 AA7 ASN C 104 ALA C 110 1 7 HELIX 8 AA8 ASN C 142 ASN C 146 5 5 HELIX 9 AA9 THR F 28 TYR F 32 5 5 HELIX 10 AB1 ASN D 104 ALA D 110 1 7 HELIX 11 AB2 ASN D 142 ASN D 146 5 5 HELIX 12 AB3 THR G 28 TYR G 32 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 GLN A 173 -1 O ARG A 172 N MET A 160 SHEET 1 AA3 4 SER A 179 HIS A 184 0 SHEET 2 AA3 4 TRP A 189 GLY A 196 -1 O ILE A 194 N SER A 179 SHEET 3 AA3 4 ALA A 201 TYR A 207 -1 O SER A 204 N CYS A 193 SHEET 4 AA3 4 LEU A 211 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 LYS A 261 N GLU A 258 SHEET 1 AA6 4 GLU A 276 ARG A 283 0 SHEET 2 AA6 4 GLY A 286 ARG A 292 -1 O GLY A 286 N ARG A 283 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 TRP A 352 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 VAL A 379 -1 O GLU A 375 N ARG A 364 SHEET 4 AA7 4 GLN A 391 ARG A 403 -1 O THR A 392 N LYS A 378 SHEET 1 AA8 4 LYS H 3 GLU H 6 0 SHEET 2 AA8 4 LEU H 20 SER H 25 -1 O SER H 25 N LYS H 3 SHEET 3 AA8 4 ILE H 77 MET H 82 -1 O LEU H 78 N CYS H 22 SHEET 4 AA8 4 PHE H 67 ARG H 71 -1 N PHE H 68 O GLN H 81 SHEET 1 AA9 6 GLY H 10 VAL H 12 0 SHEET 2 AA9 6 THR H 107 VAL H 111 1 O THR H 108 N GLY H 10 SHEET 3 AA9 6 ALA H 88 VAL H 98 -1 N TYR H 90 O THR H 107 SHEET 4 AA9 6 MET H 34 ARG H 38 -1 N VAL H 37 O TYR H 91 SHEET 5 AA9 6 GLU H 46 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA9 6 TYR H 58 TYR H 59 -1 O TYR H 58 N LYS H 50 SHEET 1 AB1 4 GLY H 10 VAL H 12 0 SHEET 2 AB1 4 THR H 107 VAL H 111 1 O THR H 108 N GLY H 10 SHEET 3 AB1 4 ALA H 88 VAL H 98 -1 N TYR H 90 O THR H 107 SHEET 4 AB1 4 ARG H 100A VAL H 102 -1 O TYR H 100E N HIS H 96 SHEET 1 AB2 4 MET L 4 THR L 5 0 SHEET 2 AB2 4 VAL L 19 ALA L 25 -1 O LYS L 24 N THR L 5 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 THR L 63 O THR L 74 SHEET 1 AB3 6 PHE L 10 THR L 13 0 SHEET 2 AB3 6 THR L 102 ILE L 106 1 O GLU L 105 N MET L 11 SHEET 3 AB3 6 ASP L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB3 6 VAL L 33 GLN L 38 -1 N GLN L 38 O ASP L 85 SHEET 5 AB3 6 LYS L 45 TYR L 49 -1 O ILE L 48 N TRP L 35 SHEET 6 AB3 6 THR L 53 ARG L 54 -1 O THR L 53 N TYR 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 GLN B 173 -1 O ARG B 172 N MET B 160 SHEET 1 AB6 4 SER B 179 HIS B 184 0 SHEET 2 AB6 4 TRP B 189 GLY B 196 -1 O ILE B 194 N SER B 179 SHEET 3 AB6 4 ALA B 201 TYR B 207 -1 O SER B 204 N CYS B 193 SHEET 4 AB6 4 LEU B 211 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 LYS B 261 N GLU B 258 SHEET 1 AB9 4 GLU B 276 ARG B 283 0 SHEET 2 AB9 4 GLY B 286 ARG B 292 -1 O GLY B 286 N ARG B 283 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 TRP B 352 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 VAL B 379 -1 O GLU B 375 N ARG B 364 SHEET 4 AC1 4 GLN B 391 ARG B 403 -1 O THR B 392 N LYS B 378 SHEET 1 AC2 4 LYS E 3 GLU E 6 0 SHEET 2 AC2 4 LEU E 20 SER E 25 -1 O SER E 25 N LYS E 3 SHEET 3 AC2 4 ILE E 77 MET E 82 -1 O LEU E 78 N CYS E 22 SHEET 4 AC2 4 PHE E 67 ARG E 71 -1 N PHE E 68 O GLN E 81 SHEET 1 AC3 6 GLY E 10 VAL E 12 0 SHEET 2 AC3 6 THR E 107 VAL E 111 1 O THR E 108 N GLY E 10 SHEET 3 AC3 6 ALA E 88 VAL E 98 -1 N TYR E 90 O THR E 107 SHEET 4 AC3 6 MET E 34 ARG E 38 -1 N VAL E 37 O TYR E 91 SHEET 5 AC3 6 GLU E 46 ILE E 51 -1 O GLU E 46 N ARG E 38 SHEET 6 AC3 6 TYR E 58 TYR E 59 -1 O TYR E 58 N LYS E 50 SHEET 1 AC4 4 GLY E 10 VAL E 12 0 SHEET 2 AC4 4 THR E 107 VAL E 111 1 O THR E 108 N GLY E 10 SHEET 3 AC4 4 ALA E 88 VAL E 98 -1 N TYR E 90 O THR E 107 SHEET 4 AC4 4 ARG E 100A VAL E 102 -1 O TYR E 100E N HIS E 96 SHEET 1 AC5 4 MET I 4 THR I 5 0 SHEET 2 AC5 4 VAL I 19 ALA I 25 -1 O LYS 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 THR I 63 O THR I 74 SHEET 1 AC6 6 PHE I 10 THR I 13 0 SHEET 2 AC6 6 THR I 102 ILE I 106 1 O GLU I 105 N MET I 11 SHEET 3 AC6 6 ASP I 85 GLN I 90 -1 N TYR I 86 O THR I 102 SHEET 4 AC6 6 VAL I 33 GLN I 38 -1 N GLN I 38 O ASP I 85 SHEET 5 AC6 6 LYS I 45 TYR I 49 -1 O ILE I 48 N TRP I 35 SHEET 6 AC6 6 THR I 53 ARG I 54 -1 O THR I 53 N TYR 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 GLN C 173 -1 O ARG C 172 N MET C 160 SHEET 1 AC9 4 SER C 179 HIS C 184 0 SHEET 2 AC9 4 TRP C 189 GLY C 196 -1 O ILE C 194 N SER C 179 SHEET 3 AC9 4 ALA C 201 TYR C 207 -1 O SER C 204 N CYS C 193 SHEET 4 AC9 4 LEU C 211 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 LYS C 261 N GLU C 258 SHEET 1 AD3 4 GLU C 276 ARG C 283 0 SHEET 2 AD3 4 GLY C 286 ARG C 292 -1 O GLY C 286 N ARG C 283 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 TRP C 352 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 VAL C 379 -1 O GLU C 375 N ARG C 364 SHEET 4 AD4 4 GLN C 391 ARG C 403 -1 O THR C 392 N LYS C 378 SHEET 1 AD5 4 LYS F 3 GLU F 6 0 SHEET 2 AD5 4 LEU F 20 SER F 25 -1 O SER F 25 N LYS F 3 SHEET 3 AD5 4 ILE F 77 MET F 82 -1 O LEU F 78 N CYS F 22 SHEET 4 AD5 4 PHE F 67 ARG F 71 -1 N PHE F 68 O GLN F 81 SHEET 1 AD6 6 GLY F 10 VAL F 12 0 SHEET 2 AD6 6 THR F 107 VAL F 111 1 O THR F 108 N GLY F 10 SHEET 3 AD6 6 ALA F 88 VAL F 98 -1 N TYR F 90 O THR F 107 SHEET 4 AD6 6 MET F 34 ARG F 38 -1 N VAL F 37 O TYR F 91 SHEET 5 AD6 6 GLU F 46 ILE F 51 -1 O GLU F 46 N ARG F 38 SHEET 6 AD6 6 TYR F 58 TYR F 59 -1 O TYR F 58 N LYS F 50 SHEET 1 AD7 4 GLY F 10 VAL F 12 0 SHEET 2 AD7 4 THR F 107 VAL F 111 1 O THR F 108 N GLY F 10 SHEET 3 AD7 4 ALA F 88 VAL F 98 -1 N TYR F 90 O THR F 107 SHEET 4 AD7 4 ARG F 100A VAL F 102 -1 O TYR F 100E N HIS F 96 SHEET 1 AD8 4 MET J 4 THR J 5 0 SHEET 2 AD8 4 VAL J 19 ALA J 25 -1 O LYS 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 THR J 63 O THR J 74 SHEET 1 AD9 6 PHE J 10 THR J 13 0 SHEET 2 AD9 6 THR J 102 ILE J 106 1 O GLU J 105 N MET J 11 SHEET 3 AD9 6 ASP J 85 GLN J 90 -1 N TYR J 86 O THR J 102 SHEET 4 AD9 6 VAL J 33 GLN J 38 -1 N GLN J 38 O ASP J 85 SHEET 5 AD9 6 LYS J 45 TYR J 49 -1 O ILE J 48 N TRP J 35 SHEET 6 AD9 6 THR J 53 ARG J 54 -1 O THR J 53 N TYR 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 GLN D 173 -1 O ARG D 172 N MET D 160 SHEET 1 AE3 4 SER D 179 HIS D 184 0 SHEET 2 AE3 4 TRP D 189 GLY D 196 -1 O ILE D 194 N SER D 179 SHEET 3 AE3 4 ALA D 201 TYR D 207 -1 O SER D 204 N CYS D 193 SHEET 4 AE3 4 LEU D 211 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 LYS D 261 N GLU D 258 SHEET 1 AE6 4 GLU D 276 ARG D 283 0 SHEET 2 AE6 4 GLY D 286 ARG D 292 -1 O GLY D 286 N ARG D 283 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 TRP D 352 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 VAL D 379 -1 O GLU D 375 N ARG D 364 SHEET 4 AE7 4 GLN D 391 ARG D 403 -1 O THR D 392 N LYS D 378 SHEET 1 AE8 4 LYS G 3 GLU G 6 0 SHEET 2 AE8 4 LEU G 20 SER G 25 -1 O SER G 25 N LYS G 3 SHEET 3 AE8 4 ILE G 77 MET G 82 -1 O LEU G 78 N CYS G 22 SHEET 4 AE8 4 PHE G 67 ARG G 71 -1 N PHE G 68 O GLN G 81 SHEET 1 AE9 6 GLY G 10 VAL G 12 0 SHEET 2 AE9 6 THR G 107 VAL G 111 1 O THR G 108 N GLY G 10 SHEET 3 AE9 6 ALA G 88 VAL G 98 -1 N TYR G 90 O THR G 107 SHEET 4 AE9 6 MET G 34 ARG G 38 -1 N VAL G 37 O TYR G 91 SHEET 5 AE9 6 GLU G 46 ILE G 51 -1 O GLU G 46 N ARG G 38 SHEET 6 AE9 6 TYR G 58 TYR G 59 -1 O TYR G 58 N LYS G 50 SHEET 1 AF1 4 GLY G 10 VAL G 12 0 SHEET 2 AF1 4 THR G 107 VAL G 111 1 O THR G 108 N GLY G 10 SHEET 3 AF1 4 ALA G 88 VAL G 98 -1 N TYR G 90 O THR G 107 SHEET 4 AF1 4 ARG G 100A VAL G 102 -1 O TYR G 100E N HIS G 96 SHEET 1 AF2 4 MET K 4 THR K 5 0 SHEET 2 AF2 4 VAL K 19 ALA K 25 -1 O LYS K 24 N THR K 5 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 THR K 63 O THR K 74 SHEET 1 AF3 6 PHE K 10 THR K 13 0 SHEET 2 AF3 6 THR K 102 ILE K 106 1 O GLU K 105 N MET K 11 SHEET 3 AF3 6 ASP K 85 GLN K 90 -1 N TYR K 86 O THR K 102 SHEET 4 AF3 6 VAL K 33 GLN K 38 -1 N GLN K 38 O ASP K 85 SHEET 5 AF3 6 LYS K 45 TYR K 49 -1 O ILE K 48 N TRP K 35 SHEET 6 AF3 6 THR K 53 ARG K 54 -1 O THR K 53 N TYR 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 2.02 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 2.03 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 2.02 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 2.02 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 2.03 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 2.02 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 2.03 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 504 1555 1555 1.44 LINK ND2 ASN A 146 C1 NAG A 501 1555 1555 1.44 LINK ND2 ASN A 200 C1 NAG M 1 1555 1555 1.45 LINK ND2 ASN A 234 C1 NAG A 505 1555 1555 1.44 LINK ND2 ASN A 309 C1 NAG A 506 1555 1555 1.44 LINK ND2 ASN A 367 C1 NAG A 502 1555 1555 1.44 LINK ND2 ASN B 93 C1 NAG B 504 1555 1555 1.44 LINK ND2 ASN B 146 C1 NAG B 501 1555 1555 1.44 LINK ND2 ASN B 200 C1 NAG N 1 1555 1555 1.45 LINK ND2 ASN B 234 C1 NAG B 505 1555 1555 1.44 LINK ND2 ASN B 309 C1 NAG B 506 1555 1555 1.44 LINK ND2 ASN B 367 C1 NAG B 502 1555 1555 1.44 LINK ND2 ASN C 93 C1 NAG C 504 1555 1555 1.44 LINK ND2 ASN C 146 C1 NAG C 501 1555 1555 1.44 LINK ND2 ASN C 200 C1 NAG O 1 1555 1555 1.45 LINK ND2 ASN C 234 C1 NAG C 505 1555 1555 1.44 LINK ND2 ASN C 309 C1 NAG C 506 1555 1555 1.44 LINK ND2 ASN C 367 C1 NAG C 502 1555 1555 1.44 LINK ND2 ASN D 93 C1 NAG D 504 1555 1555 1.44 LINK ND2 ASN D 146 C1 NAG D 501 1555 1555 1.44 LINK ND2 ASN D 200 C1 NAG P 1 1555 1555 1.45 LINK ND2 ASN D 234 C1 NAG D 505 1555 1555 1.44 LINK ND2 ASN D 309 C1 NAG D 506 1555 1555 1.44 LINK ND2 ASN D 367 C1 NAG D 502 1555 1555 1.44 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.44 LINK O4 NAG M 2 C1 BMA M 3 1555 1555 1.45 LINK O3 BMA M 3 C1 MAN M 4 1555 1555 1.45 LINK O6 BMA M 3 C1 MAN M 6 1555 1555 1.45 LINK O2 MAN M 4 C1 NAG M 5 1555 1555 1.45 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 1.45 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.44 LINK O4 NAG O 2 C1 BMA O 3 1555 1555 1.45 LINK O3 BMA O 3 C1 MAN O 4 1555 1555 1.45 LINK O6 BMA O 3 C1 MAN O 6 1555 1555 1.45 LINK O2 MAN O 4 C1 NAG O 5 1555 1555 1.45 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.44 LINK O4 NAG P 2 C1 BMA P 3 1555 1555 1.45 LINK O3 BMA P 3 C1 MAN P 4 1555 1555 1.45 LINK O6 BMA P 3 C1 MAN P 6 1555 1555 1.45 LINK O2 MAN P 4 C1 NAG P 5 1555 1555 1.45 LINK O ASP A 293 CA CA A 503 1555 1555 2.23 LINK O GLY A 297 CA CA A 503 1555 1555 2.93 LINK OD2 ASP A 324 CA CA A 503 1555 1555 2.88 LINK O GLY A 345 CA CA A 503 1555 1555 2.46 LINK O HIS A 347 CA CA A 503 1555 1555 2.29 LINK O ASP B 293 CA CA B 503 1555 1555 2.22 LINK O GLY B 297 CA CA B 503 1555 1555 2.92 LINK OD2 ASP B 324 CA CA B 503 1555 1555 2.88 LINK O GLY B 345 CA CA B 503 1555 1555 2.45 LINK O HIS B 347 CA CA B 503 1555 1555 2.28 LINK O ASP C 293 CA CA C 503 1555 1555 2.22 LINK O GLY C 297 CA CA C 503 1555 1555 2.92 LINK OD2 ASP C 324 CA CA C 503 1555 1555 2.87 LINK O GLY C 345 CA CA C 503 1555 1555 2.45 LINK O HIS C 347 CA CA C 503 1555 1555 2.28 LINK O ASP D 293 CA CA D 503 1555 1555 2.24 LINK O GLY D 297 CA CA D 503 1555 1555 2.91 LINK OD2 ASP D 324 CA CA D 503 1555 1555 2.87 LINK O GLY D 345 CA CA D 503 1555 1555 2.45 LINK O HIS D 347 CA CA D 503 1555 1555 2.29 CISPEP 1 PHE A 284 PRO A 285 0 2.37 CISPEP 2 THR A 325 PRO A 326 0 7.83 CISPEP 3 ARG A 430 LYS A 431 0 7.36 CISPEP 4 TYR L 94 PRO L 95 0 3.93 CISPEP 5 PHE B 284 PRO B 285 0 2.24 CISPEP 6 THR B 325 PRO B 326 0 7.92 CISPEP 7 ARG B 430 LYS B 431 0 7.36 CISPEP 8 TYR I 94 PRO I 95 0 3.88 CISPEP 9 PHE C 284 PRO C 285 0 2.27 CISPEP 10 THR C 325 PRO C 326 0 7.93 CISPEP 11 ARG C 430 LYS C 431 0 7.36 CISPEP 12 TYR J 94 PRO J 95 0 3.93 CISPEP 13 PHE D 284 PRO D 285 0 2.36 CISPEP 14 THR D 325 PRO D 326 0 7.85 CISPEP 15 ARG D 430 LYS D 431 0 7.36 CISPEP 16 TYR K 94 PRO K 95 0 3.97 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