HEADER VIRAL PROTEIN/IMMUNE SYSTEM 28-MAR-24 8YVL TITLE NEURAMINIDASE OF A/CALIFORNIA/04/2009 HIN1 IN COMPLEX WITH CAV-F34 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: VASODILATOR-STIMULATED PHOSPHOPROTEIN,NEURAMINIDASE; COMPND 3 CHAIN: A, B, C, D; COMPND 4 SYNONYM: VASP; COMPND 5 EC: 3.2.1.18; COMPND 6 ENGINEERED: YES; COMPND 7 OTHER_DETAILS: SEQUENCE REFERENCE FOR INFLUENZA A VIRUS COMPND 8 (A/CALIFORNIA/04/2009(H1N1) (TAX ID 641501) IS NOT AVAILABLE IN COMPND 9 UNIPROT AT THE TIME OF BIOCURATION. CURRENT SEQUENCE REFERENCE IS COMPND 10 FROM UNIPROT ID TR:A0A2R4G842 WITH TAX ID 11320 (INFLUENZA A VIRUS).; COMPND 11 MOL_ID: 2; COMPND 12 MOLECULE: CAV-F34 KAPPA CHAIN; COMPND 13 CHAIN: E, F, G, H; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 3; COMPND 16 MOLECULE: CAV-F34 HEAVY CHAIN; COMPND 17 CHAIN: I, J, K, L; COMPND 18 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, INFLUENZA A VIRUS SOURCE 3 (A/CALIFORNIA/04/2009(H1N1)); SOURCE 4 ORGANISM_COMMON: HUMAN; SOURCE 5 ORGANISM_TAXID: 9606, 641501; SOURCE 6 GENE: VASP, NA; SOURCE 7 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS INFLUENZA VIRUS, NEURAMINIDASE, ANTIBODY, VIRAL PROTEIN/IMMUNE KEYWDS 2 SYSTEM, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR X.WANG,J.GE,X.LI REVDAT 1 02-JUL-25 8YVL 0 JRNL AUTH X.WANG,J.GE,X.LI JRNL TITL NEURAMINIDASE OF A/CALIFORNIA/04/2009 HIN1 IN COMPLEX WITH JRNL TITL 2 CAV-F34 FAB JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.47 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) : 2.470 REMARK 3 NUMBER OF PARTICLES : 242813 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 8YVL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 02-APR-24. REMARK 100 THE DEPOSITION ID IS D_1300046015. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : NEURAMINIDASE OF REMARK 245 A/CALIFORNIA/04/2009 HIN1 IN REMARK 245 COMPLEX WITH CAV-F34 FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.20 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1300.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J, REMARK 350 AND CHAINS: K, L 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 4 REMARK 465 GLU A 5 REMARK 465 PHE A 6 REMARK 465 GLY A 7 REMARK 465 LEU A 8 REMARK 465 SER A 9 REMARK 465 TRP A 10 REMARK 465 ILE A 11 REMARK 465 PHE A 12 REMARK 465 LEU A 13 REMARK 465 ALA A 14 REMARK 465 ALA A 15 REMARK 465 ILE A 16 REMARK 465 LEU A 17 REMARK 465 LYS A 18 REMARK 465 GLY A 19 REMARK 465 VAL A 20 REMARK 465 GLN A 21 REMARK 465 CYS A 22 REMARK 465 ALA A 23 REMARK 465 ASP A 24 REMARK 465 PRO A 25 REMARK 465 HIS A 26 REMARK 465 HIS A 27 REMARK 465 HIS A 28 REMARK 465 HIS A 29 REMARK 465 HIS A 30 REMARK 465 HIS 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 GLY A 82 REMARK 465 MET B 4 REMARK 465 GLU B 5 REMARK 465 PHE B 6 REMARK 465 GLY B 7 REMARK 465 LEU B 8 REMARK 465 SER B 9 REMARK 465 TRP B 10 REMARK 465 ILE B 11 REMARK 465 PHE B 12 REMARK 465 LEU B 13 REMARK 465 ALA B 14 REMARK 465 ALA B 15 REMARK 465 ILE B 16 REMARK 465 LEU B 17 REMARK 465 LYS B 18 REMARK 465 GLY B 19 REMARK 465 VAL B 20 REMARK 465 GLN B 21 REMARK 465 CYS B 22 REMARK 465 ALA B 23 REMARK 465 ASP B 24 REMARK 465 PRO B 25 REMARK 465 HIS B 26 REMARK 465 HIS B 27 REMARK 465 HIS B 28 REMARK 465 HIS B 29 REMARK 465 HIS B 30 REMARK 465 HIS 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 GLY B 82 REMARK 465 MET C 4 REMARK 465 GLU C 5 REMARK 465 PHE C 6 REMARK 465 GLY C 7 REMARK 465 LEU C 8 REMARK 465 SER C 9 REMARK 465 TRP C 10 REMARK 465 ILE C 11 REMARK 465 PHE C 12 REMARK 465 LEU C 13 REMARK 465 ALA C 14 REMARK 465 ALA C 15 REMARK 465 ILE C 16 REMARK 465 LEU C 17 REMARK 465 LYS C 18 REMARK 465 GLY C 19 REMARK 465 VAL C 20 REMARK 465 GLN C 21 REMARK 465 CYS C 22 REMARK 465 ALA C 23 REMARK 465 ASP C 24 REMARK 465 PRO C 25 REMARK 465 HIS C 26 REMARK 465 HIS C 27 REMARK 465 HIS C 28 REMARK 465 HIS C 29 REMARK 465 HIS C 30 REMARK 465 HIS 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 GLY C 82 REMARK 465 MET D 4 REMARK 465 GLU D 5 REMARK 465 PHE D 6 REMARK 465 GLY D 7 REMARK 465 LEU D 8 REMARK 465 SER D 9 REMARK 465 TRP D 10 REMARK 465 ILE D 11 REMARK 465 PHE D 12 REMARK 465 LEU D 13 REMARK 465 ALA D 14 REMARK 465 ALA D 15 REMARK 465 ILE D 16 REMARK 465 LEU D 17 REMARK 465 LYS D 18 REMARK 465 GLY D 19 REMARK 465 VAL D 20 REMARK 465 GLN D 21 REMARK 465 CYS D 22 REMARK 465 ALA D 23 REMARK 465 ASP D 24 REMARK 465 PRO D 25 REMARK 465 HIS D 26 REMARK 465 HIS D 27 REMARK 465 HIS D 28 REMARK 465 HIS D 29 REMARK 465 HIS D 30 REMARK 465 HIS 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 465 GLY D 82 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 184 CA - CB - SG ANGL. DEV. = 6.6 DEGREES REMARK 500 CYS A 238 CB - CA - C ANGL. DEV. = 7.4 DEGREES REMARK 500 CYS A 417 CA - CB - SG ANGL. DEV. = 10.3 DEGREES REMARK 500 CYS B 184 CA - CB - SG ANGL. DEV. = 6.7 DEGREES REMARK 500 CYS B 238 CB - CA - C ANGL. DEV. = 7.3 DEGREES REMARK 500 CYS B 417 CA - CB - SG ANGL. DEV. = 10.2 DEGREES REMARK 500 CYS C 184 CA - CB - SG ANGL. DEV. = 6.7 DEGREES REMARK 500 CYS C 238 CB - CA - C ANGL. DEV. = 7.3 DEGREES REMARK 500 CYS C 417 CA - CB - SG ANGL. DEV. = 10.2 DEGREES REMARK 500 CYS D 184 CA - CB - SG ANGL. DEV. = 6.7 DEGREES REMARK 500 CYS D 417 CA - CB - SG ANGL. DEV. = 10.2 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN A 222 -169.16 -116.08 REMARK 500 THR A 226 -166.29 -127.36 REMARK 500 ASN A 235 -115.87 59.69 REMARK 500 ASP A 284 117.14 -162.66 REMARK 500 CYS A 292 -169.23 -125.82 REMARK 500 HIS A 297 28.34 -144.56 REMARK 500 ALA A 343 48.37 -84.47 REMARK 500 ASN A 344 -178.60 -175.39 REMARK 500 ASN B 222 -169.18 -116.04 REMARK 500 THR B 226 -166.39 -127.33 REMARK 500 ASN B 235 -122.76 65.94 REMARK 500 ASP B 284 117.09 -162.67 REMARK 500 CYS B 292 -169.29 -125.82 REMARK 500 HIS B 297 28.32 -144.53 REMARK 500 ALA B 343 48.35 -84.49 REMARK 500 ASN B 344 -178.57 -175.33 REMARK 500 ASN C 222 -169.22 -116.03 REMARK 500 THR C 226 -166.29 -127.36 REMARK 500 ASN C 235 -122.86 65.91 REMARK 500 ASP C 284 117.06 -162.75 REMARK 500 CYS C 292 -169.19 -125.80 REMARK 500 HIS C 297 28.31 -144.59 REMARK 500 ALA C 343 48.31 -84.45 REMARK 500 ASN C 344 -178.59 -175.30 REMARK 500 ASN D 222 -169.16 -116.08 REMARK 500 THR D 226 -166.39 -127.36 REMARK 500 ASN D 235 -122.93 66.06 REMARK 500 ASP D 284 117.06 -162.66 REMARK 500 CYS D 292 -169.22 -125.82 REMARK 500 HIS D 297 28.35 -144.60 REMARK 500 ALA D 343 48.33 -84.47 REMARK 500 ASN D 344 -178.59 -175.37 REMARK 500 ALA E 52 -9.83 72.55 REMARK 500 ALA F 52 -9.85 72.64 REMARK 500 ALA G 52 -9.82 72.57 REMARK 500 ALA H 52 -9.79 72.52 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 ALA D 232 -10.47 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 504 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 294 O REMARK 620 2 GLY A 298 O 101.0 REMARK 620 3 ASP A 324 OD2 96.2 83.8 REMARK 620 4 GLY A 342 O 93.4 90.5 169.6 REMARK 620 5 ASN A 344 O 95.9 160.6 103.9 79.0 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 506 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 376 OD1 REMARK 620 2 ASP A 376 OD2 45.5 REMARK 620 3 ASN A 378 OD1 89.8 109.5 REMARK 620 4 ASP A 384 OD1 165.1 121.5 103.1 REMARK 620 5 ASN A 386 O 77.7 79.2 152.1 93.5 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B 504 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 294 O REMARK 620 2 GLY B 298 O 85.3 REMARK 620 3 ASP B 324 OD2 81.5 76.8 REMARK 620 4 GLY B 342 O 89.1 92.2 166.0 REMARK 620 5 ASN B 344 O 88.1 173.3 101.3 88.6 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B 505 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 376 OD1 REMARK 620 2 ASN B 378 OD1 90.1 REMARK 620 3 ASP B 384 OD1 156.2 112.5 REMARK 620 4 ASN B 386 O 71.0 149.6 90.8 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C 504 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP C 294 O REMARK 620 2 GLY C 298 O 90.5 REMARK 620 3 ASP C 324 OD2 83.9 81.8 REMARK 620 4 GLY C 342 O 87.4 95.2 170.8 REMARK 620 5 ASN C 344 O 83.6 173.7 99.7 82.4 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C 505 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP C 376 OD1 REMARK 620 2 ASN C 378 OD1 89.6 REMARK 620 3 ASP C 384 OD1 157.3 104.8 REMARK 620 4 ASN C 386 O 76.7 158.2 93.7 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA D 504 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP D 294 O REMARK 620 2 GLY D 298 O 85.2 REMARK 620 3 ASP D 324 OD2 82.9 79.6 REMARK 620 4 GLY D 342 O 85.1 90.9 165.2 REMARK 620 5 ASN D 344 O 84.6 168.9 103.2 84.1 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA D 505 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP D 376 OD1 REMARK 620 2 ASP D 376 OD2 45.0 REMARK 620 3 ASN D 378 OD1 92.5 111.3 REMARK 620 4 ASP D 384 OD1 160.9 119.1 104.9 REMARK 620 5 ASN D 386 O 76.3 77.5 153.8 90.7 REMARK 620 N 1 2 3 4 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-39606 RELATED DB: EMDB REMARK 900 NEURAMINIDASE OF A/CALIFORNIA/04/2009 HIN1 IN COMPLEX WITH FF34 FAB DBREF 8YVL A 32 74 UNP P50552 VASP_HUMAN 337 379 DBREF1 8YVL A 83 469 UNP A0A2R4G842_9INFA DBREF2 8YVL A A0A2R4G842 83 469 DBREF 8YVL B 32 74 UNP P50552 VASP_HUMAN 337 379 DBREF1 8YVL B 83 469 UNP A0A2R4G842_9INFA DBREF2 8YVL B A0A2R4G842 83 469 DBREF 8YVL C 32 74 UNP P50552 VASP_HUMAN 337 379 DBREF1 8YVL C 83 469 UNP A0A2R4G842_9INFA DBREF2 8YVL C A0A2R4G842 83 469 DBREF 8YVL D 32 74 UNP P50552 VASP_HUMAN 337 379 DBREF1 8YVL D 83 469 UNP A0A2R4G842_9INFA DBREF2 8YVL D A0A2R4G842 83 469 DBREF 8YVL E 1 107 PDB 8YVL 8YVL 1 107 DBREF 8YVL F 1 107 PDB 8YVL 8YVL 1 107 DBREF 8YVL G 1 107 PDB 8YVL 8YVL 1 107 DBREF 8YVL H 1 107 PDB 8YVL 8YVL 1 107 DBREF 8YVL I 1 123 PDB 8YVL 8YVL 1 123 DBREF 8YVL J 1 123 PDB 8YVL 8YVL 1 123 DBREF 8YVL K 1 123 PDB 8YVL 8YVL 1 123 DBREF 8YVL L 1 123 PDB 8YVL 8YVL 1 123 SEQADV 8YVL MET A 4 UNP P50552 INITIATING METHIONINE SEQADV 8YVL GLU A 5 UNP P50552 EXPRESSION TAG SEQADV 8YVL PHE A 6 UNP P50552 EXPRESSION TAG SEQADV 8YVL GLY A 7 UNP P50552 EXPRESSION TAG SEQADV 8YVL LEU A 8 UNP P50552 EXPRESSION TAG SEQADV 8YVL SER A 9 UNP P50552 EXPRESSION TAG SEQADV 8YVL TRP A 10 UNP P50552 EXPRESSION TAG SEQADV 8YVL ILE A 11 UNP P50552 EXPRESSION TAG SEQADV 8YVL PHE A 12 UNP P50552 EXPRESSION TAG SEQADV 8YVL LEU A 13 UNP P50552 EXPRESSION TAG SEQADV 8YVL ALA A 14 UNP P50552 EXPRESSION TAG SEQADV 8YVL ALA A 15 UNP P50552 EXPRESSION TAG SEQADV 8YVL ILE A 16 UNP P50552 EXPRESSION TAG SEQADV 8YVL LEU A 17 UNP P50552 EXPRESSION TAG SEQADV 8YVL LYS A 18 UNP P50552 EXPRESSION TAG SEQADV 8YVL GLY A 19 UNP P50552 EXPRESSION TAG SEQADV 8YVL VAL A 20 UNP P50552 EXPRESSION TAG SEQADV 8YVL GLN A 21 UNP P50552 EXPRESSION TAG SEQADV 8YVL CYS A 22 UNP P50552 EXPRESSION TAG SEQADV 8YVL ALA A 23 UNP P50552 EXPRESSION TAG SEQADV 8YVL ASP A 24 UNP P50552 EXPRESSION TAG SEQADV 8YVL PRO A 25 UNP P50552 EXPRESSION TAG SEQADV 8YVL HIS A 26 UNP P50552 EXPRESSION TAG SEQADV 8YVL HIS A 27 UNP P50552 EXPRESSION TAG SEQADV 8YVL HIS A 28 UNP P50552 EXPRESSION TAG SEQADV 8YVL HIS A 29 UNP P50552 EXPRESSION TAG SEQADV 8YVL HIS A 30 UNP P50552 EXPRESSION TAG SEQADV 8YVL HIS A 31 UNP P50552 EXPRESSION TAG SEQADV 8YVL LEU A 75 UNP P50552 LINKER SEQADV 8YVL VAL A 76 UNP P50552 LINKER SEQADV 8YVL PRO A 77 UNP P50552 LINKER SEQADV 8YVL ARG A 78 UNP P50552 LINKER SEQADV 8YVL GLY A 79 UNP P50552 LINKER SEQADV 8YVL SER A 80 UNP P50552 LINKER SEQADV 8YVL GLY A 81 UNP P50552 LINKER SEQADV 8YVL GLY A 82 UNP P50552 LINKER SEQADV 8YVL MET B 4 UNP P50552 INITIATING METHIONINE SEQADV 8YVL GLU B 5 UNP P50552 EXPRESSION TAG SEQADV 8YVL PHE B 6 UNP P50552 EXPRESSION TAG SEQADV 8YVL GLY B 7 UNP P50552 EXPRESSION TAG SEQADV 8YVL LEU B 8 UNP P50552 EXPRESSION TAG SEQADV 8YVL SER B 9 UNP P50552 EXPRESSION TAG SEQADV 8YVL TRP B 10 UNP P50552 EXPRESSION TAG SEQADV 8YVL ILE B 11 UNP P50552 EXPRESSION TAG SEQADV 8YVL PHE B 12 UNP P50552 EXPRESSION TAG SEQADV 8YVL LEU B 13 UNP P50552 EXPRESSION TAG SEQADV 8YVL ALA B 14 UNP P50552 EXPRESSION TAG SEQADV 8YVL ALA B 15 UNP P50552 EXPRESSION TAG SEQADV 8YVL ILE B 16 UNP P50552 EXPRESSION TAG SEQADV 8YVL LEU B 17 UNP P50552 EXPRESSION TAG SEQADV 8YVL LYS B 18 UNP P50552 EXPRESSION TAG SEQADV 8YVL GLY B 19 UNP P50552 EXPRESSION TAG SEQADV 8YVL VAL B 20 UNP P50552 EXPRESSION TAG SEQADV 8YVL GLN B 21 UNP P50552 EXPRESSION TAG SEQADV 8YVL CYS B 22 UNP P50552 EXPRESSION TAG SEQADV 8YVL ALA B 23 UNP P50552 EXPRESSION TAG SEQADV 8YVL ASP B 24 UNP P50552 EXPRESSION TAG SEQADV 8YVL PRO B 25 UNP P50552 EXPRESSION TAG SEQADV 8YVL HIS B 26 UNP P50552 EXPRESSION TAG SEQADV 8YVL HIS B 27 UNP P50552 EXPRESSION TAG SEQADV 8YVL HIS B 28 UNP P50552 EXPRESSION TAG SEQADV 8YVL HIS B 29 UNP P50552 EXPRESSION TAG SEQADV 8YVL HIS B 30 UNP P50552 EXPRESSION TAG SEQADV 8YVL HIS B 31 UNP P50552 EXPRESSION TAG SEQADV 8YVL LEU B 75 UNP P50552 LINKER SEQADV 8YVL VAL B 76 UNP P50552 LINKER SEQADV 8YVL PRO B 77 UNP P50552 LINKER SEQADV 8YVL ARG B 78 UNP P50552 LINKER SEQADV 8YVL GLY B 79 UNP P50552 LINKER SEQADV 8YVL SER B 80 UNP P50552 LINKER SEQADV 8YVL GLY B 81 UNP P50552 LINKER SEQADV 8YVL GLY B 82 UNP P50552 LINKER SEQADV 8YVL MET C 4 UNP P50552 INITIATING METHIONINE SEQADV 8YVL GLU C 5 UNP P50552 EXPRESSION TAG SEQADV 8YVL PHE C 6 UNP P50552 EXPRESSION TAG SEQADV 8YVL GLY C 7 UNP P50552 EXPRESSION TAG SEQADV 8YVL LEU C 8 UNP P50552 EXPRESSION TAG SEQADV 8YVL SER C 9 UNP P50552 EXPRESSION TAG SEQADV 8YVL TRP C 10 UNP P50552 EXPRESSION TAG SEQADV 8YVL ILE C 11 UNP P50552 EXPRESSION TAG SEQADV 8YVL PHE C 12 UNP P50552 EXPRESSION TAG SEQADV 8YVL LEU C 13 UNP P50552 EXPRESSION TAG SEQADV 8YVL ALA C 14 UNP P50552 EXPRESSION TAG SEQADV 8YVL ALA C 15 UNP P50552 EXPRESSION TAG SEQADV 8YVL ILE C 16 UNP P50552 EXPRESSION TAG SEQADV 8YVL LEU C 17 UNP P50552 EXPRESSION TAG SEQADV 8YVL LYS C 18 UNP P50552 EXPRESSION TAG SEQADV 8YVL GLY C 19 UNP P50552 EXPRESSION TAG SEQADV 8YVL VAL C 20 UNP P50552 EXPRESSION TAG SEQADV 8YVL GLN C 21 UNP P50552 EXPRESSION TAG SEQADV 8YVL CYS C 22 UNP P50552 EXPRESSION TAG SEQADV 8YVL ALA C 23 UNP P50552 EXPRESSION TAG SEQADV 8YVL ASP C 24 UNP P50552 EXPRESSION TAG SEQADV 8YVL PRO C 25 UNP P50552 EXPRESSION TAG SEQADV 8YVL HIS C 26 UNP P50552 EXPRESSION TAG SEQADV 8YVL HIS C 27 UNP P50552 EXPRESSION TAG SEQADV 8YVL HIS C 28 UNP P50552 EXPRESSION TAG SEQADV 8YVL HIS C 29 UNP P50552 EXPRESSION TAG SEQADV 8YVL HIS C 30 UNP P50552 EXPRESSION TAG SEQADV 8YVL HIS C 31 UNP P50552 EXPRESSION TAG SEQADV 8YVL LEU C 75 UNP P50552 LINKER SEQADV 8YVL VAL C 76 UNP P50552 LINKER SEQADV 8YVL PRO C 77 UNP P50552 LINKER SEQADV 8YVL ARG C 78 UNP P50552 LINKER SEQADV 8YVL GLY C 79 UNP P50552 LINKER SEQADV 8YVL SER C 80 UNP P50552 LINKER SEQADV 8YVL GLY C 81 UNP P50552 LINKER SEQADV 8YVL GLY C 82 UNP P50552 LINKER SEQADV 8YVL MET D 4 UNP P50552 INITIATING METHIONINE SEQADV 8YVL GLU D 5 UNP P50552 EXPRESSION TAG SEQADV 8YVL PHE D 6 UNP P50552 EXPRESSION TAG SEQADV 8YVL GLY D 7 UNP P50552 EXPRESSION TAG SEQADV 8YVL LEU D 8 UNP P50552 EXPRESSION TAG SEQADV 8YVL SER D 9 UNP P50552 EXPRESSION TAG SEQADV 8YVL TRP D 10 UNP P50552 EXPRESSION TAG SEQADV 8YVL ILE D 11 UNP P50552 EXPRESSION TAG SEQADV 8YVL PHE D 12 UNP P50552 EXPRESSION TAG SEQADV 8YVL LEU D 13 UNP P50552 EXPRESSION TAG SEQADV 8YVL ALA D 14 UNP P50552 EXPRESSION TAG SEQADV 8YVL ALA D 15 UNP P50552 EXPRESSION TAG SEQADV 8YVL ILE D 16 UNP P50552 EXPRESSION TAG SEQADV 8YVL LEU D 17 UNP P50552 EXPRESSION TAG SEQADV 8YVL LYS D 18 UNP P50552 EXPRESSION TAG SEQADV 8YVL GLY D 19 UNP P50552 EXPRESSION TAG SEQADV 8YVL VAL D 20 UNP P50552 EXPRESSION TAG SEQADV 8YVL GLN D 21 UNP P50552 EXPRESSION TAG SEQADV 8YVL CYS D 22 UNP P50552 EXPRESSION TAG SEQADV 8YVL ALA D 23 UNP P50552 EXPRESSION TAG SEQADV 8YVL ASP D 24 UNP P50552 EXPRESSION TAG SEQADV 8YVL PRO D 25 UNP P50552 EXPRESSION TAG SEQADV 8YVL HIS D 26 UNP P50552 EXPRESSION TAG SEQADV 8YVL HIS D 27 UNP P50552 EXPRESSION TAG SEQADV 8YVL HIS D 28 UNP P50552 EXPRESSION TAG SEQADV 8YVL HIS D 29 UNP P50552 EXPRESSION TAG SEQADV 8YVL HIS D 30 UNP P50552 EXPRESSION TAG SEQADV 8YVL HIS D 31 UNP P50552 EXPRESSION TAG SEQADV 8YVL LEU D 75 UNP P50552 LINKER SEQADV 8YVL VAL D 76 UNP P50552 LINKER SEQADV 8YVL PRO D 77 UNP P50552 LINKER SEQADV 8YVL ARG D 78 UNP P50552 LINKER SEQADV 8YVL GLY D 79 UNP P50552 LINKER SEQADV 8YVL SER D 80 UNP P50552 LINKER SEQADV 8YVL GLY D 81 UNP P50552 LINKER SEQADV 8YVL GLY D 82 UNP P50552 LINKER SEQRES 1 A 466 MET GLU PHE GLY LEU SER TRP ILE PHE LEU ALA ALA ILE SEQRES 2 A 466 LEU LYS GLY VAL GLN CYS ALA ASP PRO HIS HIS HIS HIS SEQRES 3 A 466 HIS HIS SER SER SER ASP TYR SER ASP LEU GLN ARG VAL SEQRES 4 A 466 LYS GLN GLU LEU LEU GLU GLU VAL LYS LYS GLU LEU GLN SEQRES 5 A 466 LYS VAL LYS GLU GLU ILE ILE GLU ALA PHE VAL GLN GLU SEQRES 6 A 466 LEU ARG LYS ARG GLY SER LEU VAL PRO ARG GLY SER GLY SEQRES 7 A 466 GLY VAL LYS LEU ALA GLY ASN SER SER LEU CYS PRO VAL SEQRES 8 A 466 SER GLY TRP ALA ILE TYR SER LYS ASP ASN SER VAL ARG SEQRES 9 A 466 ILE GLY SER LYS GLY ASP VAL PHE VAL ILE ARG GLU PRO SEQRES 10 A 466 PHE ILE SER CYS SER PRO LEU GLU CYS ARG THR PHE PHE SEQRES 11 A 466 LEU THR GLN GLY ALA LEU LEU ASN ASP LYS HIS SER ASN SEQRES 12 A 466 GLY THR ILE LYS ASP ARG SER PRO TYR ARG THR LEU MET SEQRES 13 A 466 SER CYS PRO ILE GLY GLU VAL PRO SER PRO TYR ASN SER SEQRES 14 A 466 ARG PHE GLU SER VAL ALA TRP SER ALA SER ALA CYS HIS SEQRES 15 A 466 ASP GLY ILE ASN TRP LEU THR ILE GLY ILE SER GLY PRO SEQRES 16 A 466 ASP SER GLY ALA VAL ALA VAL LEU LYS TYR ASN GLY ILE SEQRES 17 A 466 ILE THR ASP THR ILE LYS SER TRP ARG ASN ASN ILE LEU SEQRES 18 A 466 ARG THR GLN GLU SER GLU CYS ALA CYS VAL ASN GLY SER SEQRES 19 A 466 CYS PHE THR ILE MET THR ASP GLY PRO SER ASP GLY GLN SEQRES 20 A 466 ALA SER TYR LYS ILE PHE ARG ILE GLU LYS GLY LYS ILE SEQRES 21 A 466 VAL LYS SER VAL GLU MET ASN ALA PRO ASN TYR HIS TYR SEQRES 22 A 466 GLU GLU CYS SER CYS TYR PRO ASP SER SER GLU ILE THR SEQRES 23 A 466 CYS VAL CYS ARG ASP ASN TRP HIS GLY SER ASN ARG PRO SEQRES 24 A 466 TRP VAL SER PHE ASN GLN ASN LEU GLU TYR GLN ILE GLY SEQRES 25 A 466 TYR ILE CYS SER GLY VAL PHE GLY ASP ASN PRO ARG PRO SEQRES 26 A 466 ASN ASP LYS THR GLY SER CYS GLY PRO VAL SER SER ASN SEQRES 27 A 466 GLY ALA ASN GLY VAL LYS GLY PHE SER PHE LYS TYR GLY SEQRES 28 A 466 ASN GLY VAL TRP ILE GLY ARG THR LYS SER ILE SER SER SEQRES 29 A 466 ARG LYS GLY PHE GLU MET ILE TRP ASP PRO ASN GLY TRP SEQRES 30 A 466 THR GLY THR ASP ASN ASN PHE SER ILE LYS GLN ASP ILE SEQRES 31 A 466 VAL GLY ILE ASN GLU TRP SER GLY TYR SER GLY SER PHE SEQRES 32 A 466 VAL GLN HIS PRO GLU LEU THR GLY LEU ASP CYS ILE ARG SEQRES 33 A 466 PRO CYS PHE TRP VAL GLU LEU ILE ARG GLY ARG PRO GLU SEQRES 34 A 466 GLU ASN THR ILE TRP THR SER GLY SER SER ILE SER PHE SEQRES 35 A 466 CYS GLY VAL ASN SER ASP THR VAL GLY TRP SER TRP PRO SEQRES 36 A 466 ASP GLY ALA GLU LEU PRO PHE THR ILE ASP LYS SEQRES 1 B 466 MET GLU PHE GLY LEU SER TRP ILE PHE LEU ALA ALA ILE SEQRES 2 B 466 LEU LYS GLY VAL GLN CYS ALA ASP PRO HIS HIS HIS HIS SEQRES 3 B 466 HIS HIS SER SER SER ASP TYR SER ASP LEU GLN ARG VAL SEQRES 4 B 466 LYS GLN GLU LEU LEU GLU GLU VAL LYS LYS GLU LEU GLN SEQRES 5 B 466 LYS VAL LYS GLU GLU ILE ILE GLU ALA PHE VAL GLN GLU SEQRES 6 B 466 LEU ARG LYS ARG GLY SER LEU VAL PRO ARG GLY SER GLY SEQRES 7 B 466 GLY VAL LYS LEU ALA GLY ASN SER SER LEU CYS PRO VAL SEQRES 8 B 466 SER GLY TRP ALA ILE TYR SER LYS ASP ASN SER VAL ARG SEQRES 9 B 466 ILE GLY SER LYS GLY ASP VAL PHE VAL ILE ARG GLU PRO SEQRES 10 B 466 PHE ILE SER CYS SER PRO LEU GLU CYS ARG THR PHE PHE SEQRES 11 B 466 LEU THR GLN GLY ALA LEU LEU ASN ASP LYS HIS SER ASN SEQRES 12 B 466 GLY THR ILE LYS ASP ARG SER PRO TYR ARG THR LEU MET SEQRES 13 B 466 SER CYS PRO ILE GLY GLU VAL PRO SER PRO TYR ASN SER SEQRES 14 B 466 ARG PHE GLU SER VAL ALA TRP SER ALA SER ALA CYS HIS SEQRES 15 B 466 ASP GLY ILE ASN TRP LEU THR ILE GLY ILE SER GLY PRO SEQRES 16 B 466 ASP SER GLY ALA VAL ALA VAL LEU LYS TYR ASN GLY ILE SEQRES 17 B 466 ILE THR ASP THR ILE LYS SER TRP ARG ASN ASN ILE LEU SEQRES 18 B 466 ARG THR GLN GLU SER GLU CYS ALA CYS VAL ASN GLY SER SEQRES 19 B 466 CYS PHE THR ILE MET THR ASP GLY PRO SER ASP GLY GLN SEQRES 20 B 466 ALA SER TYR LYS ILE PHE ARG ILE GLU LYS GLY LYS ILE SEQRES 21 B 466 VAL LYS SER VAL GLU MET ASN ALA PRO ASN TYR HIS TYR SEQRES 22 B 466 GLU GLU CYS SER CYS TYR PRO ASP SER SER GLU ILE THR SEQRES 23 B 466 CYS VAL CYS ARG ASP ASN TRP HIS GLY SER ASN ARG PRO SEQRES 24 B 466 TRP VAL SER PHE ASN GLN ASN LEU GLU TYR GLN ILE GLY SEQRES 25 B 466 TYR ILE CYS SER GLY VAL PHE GLY ASP ASN PRO ARG PRO SEQRES 26 B 466 ASN ASP LYS THR GLY SER CYS GLY PRO VAL SER SER ASN SEQRES 27 B 466 GLY ALA ASN GLY VAL LYS GLY PHE SER PHE LYS TYR GLY SEQRES 28 B 466 ASN GLY VAL TRP ILE GLY ARG THR LYS SER ILE SER SER SEQRES 29 B 466 ARG LYS GLY PHE GLU MET ILE TRP ASP PRO ASN GLY TRP SEQRES 30 B 466 THR GLY THR ASP ASN ASN PHE SER ILE LYS GLN ASP ILE SEQRES 31 B 466 VAL GLY ILE ASN GLU TRP SER GLY TYR SER GLY SER PHE SEQRES 32 B 466 VAL GLN HIS PRO GLU LEU THR GLY LEU ASP CYS ILE ARG SEQRES 33 B 466 PRO CYS PHE TRP VAL GLU LEU ILE ARG GLY ARG PRO GLU SEQRES 34 B 466 GLU ASN THR ILE TRP THR SER GLY SER SER ILE SER PHE SEQRES 35 B 466 CYS GLY VAL ASN SER ASP THR VAL GLY TRP SER TRP PRO SEQRES 36 B 466 ASP GLY ALA GLU LEU PRO PHE THR ILE ASP LYS SEQRES 1 C 466 MET GLU PHE GLY LEU SER TRP ILE PHE LEU ALA ALA ILE SEQRES 2 C 466 LEU LYS GLY VAL GLN CYS ALA ASP PRO HIS HIS HIS HIS SEQRES 3 C 466 HIS HIS SER SER SER ASP TYR SER ASP LEU GLN ARG VAL SEQRES 4 C 466 LYS GLN GLU LEU LEU GLU GLU VAL LYS LYS GLU LEU GLN SEQRES 5 C 466 LYS VAL LYS GLU GLU ILE ILE GLU ALA PHE VAL GLN GLU SEQRES 6 C 466 LEU ARG LYS ARG GLY SER LEU VAL PRO ARG GLY SER GLY SEQRES 7 C 466 GLY VAL LYS LEU ALA GLY ASN SER SER LEU CYS PRO VAL SEQRES 8 C 466 SER GLY TRP ALA ILE TYR SER LYS ASP ASN SER VAL ARG SEQRES 9 C 466 ILE GLY SER LYS GLY ASP VAL PHE VAL ILE ARG GLU PRO SEQRES 10 C 466 PHE ILE SER CYS SER PRO LEU GLU CYS ARG THR PHE PHE SEQRES 11 C 466 LEU THR GLN GLY ALA LEU LEU ASN ASP LYS HIS SER ASN SEQRES 12 C 466 GLY THR ILE LYS ASP ARG SER PRO TYR ARG THR LEU MET SEQRES 13 C 466 SER CYS PRO ILE GLY GLU VAL PRO SER PRO TYR ASN SER SEQRES 14 C 466 ARG PHE GLU SER VAL ALA TRP SER ALA SER ALA CYS HIS SEQRES 15 C 466 ASP GLY ILE ASN TRP LEU THR ILE GLY ILE SER GLY PRO SEQRES 16 C 466 ASP SER GLY ALA VAL ALA VAL LEU LYS TYR ASN GLY ILE SEQRES 17 C 466 ILE THR ASP THR ILE LYS SER TRP ARG ASN ASN ILE LEU SEQRES 18 C 466 ARG THR GLN GLU SER GLU CYS ALA CYS VAL ASN GLY SER SEQRES 19 C 466 CYS PHE THR ILE MET THR ASP GLY PRO SER ASP GLY GLN SEQRES 20 C 466 ALA SER TYR LYS ILE PHE ARG ILE GLU LYS GLY LYS ILE SEQRES 21 C 466 VAL LYS SER VAL GLU MET ASN ALA PRO ASN TYR HIS TYR SEQRES 22 C 466 GLU GLU CYS SER CYS TYR PRO ASP SER SER GLU ILE THR SEQRES 23 C 466 CYS VAL CYS ARG ASP ASN TRP HIS GLY SER ASN ARG PRO SEQRES 24 C 466 TRP VAL SER PHE ASN GLN ASN LEU GLU TYR GLN ILE GLY SEQRES 25 C 466 TYR ILE CYS SER GLY VAL PHE GLY ASP ASN PRO ARG PRO SEQRES 26 C 466 ASN ASP LYS THR GLY SER CYS GLY PRO VAL SER SER ASN SEQRES 27 C 466 GLY ALA ASN GLY VAL LYS GLY PHE SER PHE LYS TYR GLY SEQRES 28 C 466 ASN GLY VAL TRP ILE GLY ARG THR LYS SER ILE SER SER SEQRES 29 C 466 ARG LYS GLY PHE GLU MET ILE TRP ASP PRO ASN GLY TRP SEQRES 30 C 466 THR GLY THR ASP ASN ASN PHE SER ILE LYS GLN ASP ILE SEQRES 31 C 466 VAL GLY ILE ASN GLU TRP SER GLY TYR SER GLY SER PHE SEQRES 32 C 466 VAL GLN HIS PRO GLU LEU THR GLY LEU ASP CYS ILE ARG SEQRES 33 C 466 PRO CYS PHE TRP VAL GLU LEU ILE ARG GLY ARG PRO GLU SEQRES 34 C 466 GLU ASN THR ILE TRP THR SER GLY SER SER ILE SER PHE SEQRES 35 C 466 CYS GLY VAL ASN SER ASP THR VAL GLY TRP SER TRP PRO SEQRES 36 C 466 ASP GLY ALA GLU LEU PRO PHE THR ILE ASP LYS SEQRES 1 D 466 MET GLU PHE GLY LEU SER TRP ILE PHE LEU ALA ALA ILE SEQRES 2 D 466 LEU LYS GLY VAL GLN CYS ALA ASP PRO HIS HIS HIS HIS SEQRES 3 D 466 HIS HIS SER SER SER ASP TYR SER ASP LEU GLN ARG VAL SEQRES 4 D 466 LYS GLN GLU LEU LEU GLU GLU VAL LYS LYS GLU LEU GLN SEQRES 5 D 466 LYS VAL LYS GLU GLU ILE ILE GLU ALA PHE VAL GLN GLU SEQRES 6 D 466 LEU ARG LYS ARG GLY SER LEU VAL PRO ARG GLY SER GLY SEQRES 7 D 466 GLY VAL LYS LEU ALA GLY ASN SER SER LEU CYS PRO VAL SEQRES 8 D 466 SER GLY TRP ALA ILE TYR SER LYS ASP ASN SER VAL ARG SEQRES 9 D 466 ILE GLY SER LYS GLY ASP VAL PHE VAL ILE ARG GLU PRO SEQRES 10 D 466 PHE ILE SER CYS SER PRO LEU GLU CYS ARG THR PHE PHE SEQRES 11 D 466 LEU THR GLN GLY ALA LEU LEU ASN ASP LYS HIS SER ASN SEQRES 12 D 466 GLY THR ILE LYS ASP ARG SER PRO TYR ARG THR LEU MET SEQRES 13 D 466 SER CYS PRO ILE GLY GLU VAL PRO SER PRO TYR ASN SER SEQRES 14 D 466 ARG PHE GLU SER VAL ALA TRP SER ALA SER ALA CYS HIS SEQRES 15 D 466 ASP GLY ILE ASN TRP LEU THR ILE GLY ILE SER GLY PRO SEQRES 16 D 466 ASP SER GLY ALA VAL ALA VAL LEU LYS TYR ASN GLY ILE SEQRES 17 D 466 ILE THR ASP THR ILE LYS SER TRP ARG ASN ASN ILE LEU SEQRES 18 D 466 ARG THR GLN GLU SER GLU CYS ALA CYS VAL ASN GLY SER SEQRES 19 D 466 CYS PHE THR ILE MET THR ASP GLY PRO SER ASP GLY GLN SEQRES 20 D 466 ALA SER TYR LYS ILE PHE ARG ILE GLU LYS GLY LYS ILE SEQRES 21 D 466 VAL LYS SER VAL GLU MET ASN ALA PRO ASN TYR HIS TYR SEQRES 22 D 466 GLU GLU CYS SER CYS TYR PRO ASP SER SER GLU ILE THR SEQRES 23 D 466 CYS VAL CYS ARG ASP ASN TRP HIS GLY SER ASN ARG PRO SEQRES 24 D 466 TRP VAL SER PHE ASN GLN ASN LEU GLU TYR GLN ILE GLY SEQRES 25 D 466 TYR ILE CYS SER GLY VAL PHE GLY ASP ASN PRO ARG PRO SEQRES 26 D 466 ASN ASP LYS THR GLY SER CYS GLY PRO VAL SER SER ASN SEQRES 27 D 466 GLY ALA ASN GLY VAL LYS GLY PHE SER PHE LYS TYR GLY SEQRES 28 D 466 ASN GLY VAL TRP ILE GLY ARG THR LYS SER ILE SER SER SEQRES 29 D 466 ARG LYS GLY PHE GLU MET ILE TRP ASP PRO ASN GLY TRP SEQRES 30 D 466 THR GLY THR ASP ASN ASN PHE SER ILE LYS GLN ASP ILE SEQRES 31 D 466 VAL GLY ILE ASN GLU TRP SER GLY TYR SER GLY SER PHE SEQRES 32 D 466 VAL GLN HIS PRO GLU LEU THR GLY LEU ASP CYS ILE ARG SEQRES 33 D 466 PRO CYS PHE TRP VAL GLU LEU ILE ARG GLY ARG PRO GLU SEQRES 34 D 466 GLU ASN THR ILE TRP THR SER GLY SER SER ILE SER PHE SEQRES 35 D 466 CYS GLY VAL ASN SER ASP THR VAL GLY TRP SER TRP PRO SEQRES 36 D 466 ASP GLY ALA GLU LEU PRO PHE THR ILE ASP LYS SEQRES 1 E 107 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 E 107 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 E 107 GLN TYR ILE SER SER MET ASN LEU ALA TRP TYR GLN GLN SEQRES 4 E 107 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE SER ALA ALA SEQRES 5 E 107 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 E 107 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER GLY SEQRES 7 E 107 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN LYS SEQRES 8 E 107 TYR GLY SER PRO TYR THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 E 107 GLU ILE LYS SEQRES 1 F 107 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 F 107 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 F 107 GLN TYR ILE SER SER MET ASN LEU ALA TRP TYR GLN GLN SEQRES 4 F 107 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE SER ALA ALA SEQRES 5 F 107 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 F 107 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER GLY SEQRES 7 F 107 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN LYS SEQRES 8 F 107 TYR GLY SER PRO TYR THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 F 107 GLU ILE LYS SEQRES 1 G 107 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 G 107 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 G 107 GLN TYR ILE SER SER MET ASN LEU ALA TRP TYR GLN GLN SEQRES 4 G 107 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE SER ALA ALA SEQRES 5 G 107 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 G 107 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER GLY SEQRES 7 G 107 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN LYS SEQRES 8 G 107 TYR GLY SER PRO TYR THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 G 107 GLU ILE LYS SEQRES 1 H 107 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 H 107 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 H 107 GLN TYR ILE SER SER MET ASN LEU ALA TRP TYR GLN GLN SEQRES 4 H 107 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE SER ALA ALA SEQRES 5 H 107 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 H 107 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER GLY SEQRES 7 H 107 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN LYS SEQRES 8 H 107 TYR GLY SER PRO TYR THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 H 107 GLU ILE LYS SEQRES 1 I 123 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLU SEQRES 2 I 123 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 I 123 LEU THR PHE SER THR TYR GLU MET ASN TRP VAL ARG GLN SEQRES 4 I 123 ALA PRO GLY LYS GLY LEU GLU TRP ILE SER HIS ILE SER SEQRES 5 I 123 SER SER GLY PHE ALA ILE TYR TYR ALA ASP SER VAL ARG SEQRES 6 I 123 GLY ARG PHE THR ILE SER ARG ASP ILE ALA LYS GLN SER SEQRES 7 I 123 LEU ASP LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 I 123 ALA VAL TYR TYR CYS ALA ARG ASP TYR TYR ASN ARG ASP SEQRES 9 I 123 LEU GLY TYR SER GLY MET ASP VAL TRP GLY GLN GLY THR SEQRES 10 I 123 THR VAL THR VAL SER SER SEQRES 1 J 123 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLU SEQRES 2 J 123 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 J 123 LEU THR PHE SER THR TYR GLU MET ASN TRP VAL ARG GLN SEQRES 4 J 123 ALA PRO GLY LYS GLY LEU GLU TRP ILE SER HIS ILE SER SEQRES 5 J 123 SER SER GLY PHE ALA ILE TYR TYR ALA ASP SER VAL ARG SEQRES 6 J 123 GLY ARG PHE THR ILE SER ARG ASP ILE ALA LYS GLN SER SEQRES 7 J 123 LEU ASP LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 J 123 ALA VAL TYR TYR CYS ALA ARG ASP TYR TYR ASN ARG ASP SEQRES 9 J 123 LEU GLY TYR SER GLY MET ASP VAL TRP GLY GLN GLY THR SEQRES 10 J 123 THR VAL THR VAL SER SER SEQRES 1 K 123 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLU SEQRES 2 K 123 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 K 123 LEU THR PHE SER THR TYR GLU MET ASN TRP VAL ARG GLN SEQRES 4 K 123 ALA PRO GLY LYS GLY LEU GLU TRP ILE SER HIS ILE SER SEQRES 5 K 123 SER SER GLY PHE ALA ILE TYR TYR ALA ASP SER VAL ARG SEQRES 6 K 123 GLY ARG PHE THR ILE SER ARG ASP ILE ALA LYS GLN SER SEQRES 7 K 123 LEU ASP LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 K 123 ALA VAL TYR TYR CYS ALA ARG ASP TYR TYR ASN ARG ASP SEQRES 9 K 123 LEU GLY TYR SER GLY MET ASP VAL TRP GLY GLN GLY THR SEQRES 10 K 123 THR VAL THR VAL SER SER SEQRES 1 L 123 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLU SEQRES 2 L 123 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 L 123 LEU THR PHE SER THR TYR GLU MET ASN TRP VAL ARG GLN SEQRES 4 L 123 ALA PRO GLY LYS GLY LEU GLU TRP ILE SER HIS ILE SER SEQRES 5 L 123 SER SER GLY PHE ALA ILE TYR TYR ALA ASP SER VAL ARG SEQRES 6 L 123 GLY ARG PHE THR ILE SER ARG ASP ILE ALA LYS GLN SER SEQRES 7 L 123 LEU ASP LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 L 123 ALA VAL TYR TYR CYS ALA ARG ASP TYR TYR ASN ARG ASP SEQRES 9 L 123 LEU GLY TYR SER GLY MET ASP VAL TRP GLY GLN GLY THR SEQRES 10 L 123 THR VAL THR VAL SER SER HET NAG A 501 14 HET NAG A 502 14 HET NAG A 503 14 HET CA A 504 1 HET CA A 505 1 HET CA A 506 1 HET NAG B 501 14 HET NAG B 502 14 HET NAG B 503 14 HET CA B 504 1 HET CA B 505 1 HET NAG C 501 14 HET NAG C 502 14 HET NAG C 503 14 HET CA C 504 1 HET CA C 505 1 HET NAG D 501 14 HET NAG D 502 14 HET NAG D 503 14 HET CA D 504 1 HET CA D 505 1 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM CA CALCIUM ION HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE FORMUL 13 NAG 12(C8 H15 N O6) FORMUL 16 CA 9(CA 2+) HELIX 1 AA1 ASN A 104 SER A 110 1 7 HELIX 2 AA2 ASP A 142 ASN A 146 5 5 HELIX 3 AA3 HIS A 409 GLY A 414 1 6 HELIX 4 AA4 PHE A 465 LYS A 469 5 5 HELIX 5 AA5 ASN B 104 SER B 110 1 7 HELIX 6 AA6 ASP B 142 ASN B 146 5 5 HELIX 7 AA7 HIS B 409 GLY B 414 1 6 HELIX 8 AA8 PHE B 465 LYS B 469 5 5 HELIX 9 AA9 ASN C 104 SER C 110 1 7 HELIX 10 AB1 ASP C 142 ASN C 146 5 5 HELIX 11 AB2 HIS C 409 GLY C 414 1 6 HELIX 12 AB3 PHE C 465 LYS C 469 5 5 HELIX 13 AB4 ASN D 104 SER D 110 1 7 HELIX 14 AB5 ASP D 142 ASN D 146 5 5 HELIX 15 AB6 HIS D 409 GLY D 414 1 6 HELIX 16 AB7 PHE D 465 LYS D 469 5 5 HELIX 17 AB8 SER E 30 MET E 32 5 3 HELIX 18 AB9 GLU E 80 PHE E 84 5 5 HELIX 19 AC1 SER F 30 MET F 32 5 3 HELIX 20 AC2 GLU F 80 PHE F 84 5 5 HELIX 21 AC3 SER G 30 MET G 32 5 3 HELIX 22 AC4 GLU G 80 PHE G 84 5 5 HELIX 23 AC5 SER H 30 MET H 32 5 3 HELIX 24 AC6 GLU H 80 PHE H 84 5 5 HELIX 25 AC7 SER I 25 TYR I 32 1 8 HELIX 26 AC8 ARG I 87 THR I 91 5 5 HELIX 27 AC9 SER J 25 TYR J 32 1 8 HELIX 28 AD1 ARG J 87 THR J 91 5 5 HELIX 29 AD2 SER K 25 TYR K 32 1 8 HELIX 30 AD3 ARG K 87 THR K 91 5 5 HELIX 31 AD4 SER L 25 TYR L 32 1 8 HELIX 32 AD5 ARG L 87 THR L 91 5 5 SHEET 1 AA1 4 GLY A 96 LYS A 102 0 SHEET 2 AA1 4 THR A 438 VAL A 448 -1 O SER A 444 N TYR A 100 SHEET 3 AA1 4 ARG A 419 GLY A 429 -1 N ARG A 428 O SER A 439 SHEET 4 AA1 4 SER A 403 GLN A 408 -1 N GLN A 408 O ARG A 419 SHEET 1 AA2 4 PHE A 115 CYS A 124 0 SHEET 2 AA2 4 CYS A 129 LEU A 139 -1 O PHE A 132 N PHE A 121 SHEET 3 AA2 4 THR A 157 PRO A 162 -1 O THR A 157 N THR A 135 SHEET 4 AA2 4 ARG A 173 VAL A 177 -1 O ARG A 173 N SER A 160 SHEET 1 AA3 4 SER A 180 HIS A 185 0 SHEET 2 AA3 4 TRP A 190 SER A 196 -1 O ILE A 195 N SER A 180 SHEET 3 AA3 4 VAL A 203 TYR A 208 -1 O VAL A 205 N GLY A 194 SHEET 4 AA3 4 ILE A 211 LYS A 217 -1 O THR A 213 N LEU A 206 SHEET 1 AA4 4 ALA A 232 VAL A 234 0 SHEET 2 AA4 4 SER A 237 ASP A 244 -1 O PHE A 239 N ALA A 232 SHEET 3 AA4 4 SER A 252 GLU A 259 -1 O SER A 252 N ASP A 244 SHEET 4 AA4 4 LYS A 262 GLU A 268 -1 O LYS A 262 N GLU A 259 SHEET 1 AA5 4 GLU A 277 ASP A 284 0 SHEET 2 AA5 4 GLU A 287 ARG A 293 -1 O VAL A 291 N SER A 280 SHEET 3 AA5 4 PRO A 302 PHE A 306 -1 O PRO A 302 N CYS A 292 SHEET 4 AA5 4 TYR A 312 TYR A 316 -1 O GLY A 315 N TRP A 303 SHEET 1 AA6 4 PHE A 349 TYR A 353 0 SHEET 2 AA6 4 GLY A 356 ARG A 361 -1 O GLY A 356 N TYR A 353 SHEET 3 AA6 4 LYS A 369 ASP A 376 -1 O ILE A 374 N ILE A 359 SHEET 4 AA6 4 ILE A 389 TRP A 399 -1 O GLN A 391 N MET A 373 SHEET 1 AA7 4 GLY B 96 LYS B 102 0 SHEET 2 AA7 4 THR B 438 VAL B 448 -1 O SER B 444 N TYR B 100 SHEET 3 AA7 4 ARG B 419 GLY B 429 -1 N ARG B 428 O SER B 439 SHEET 4 AA7 4 SER B 403 GLN B 408 -1 N GLN B 408 O ARG B 419 SHEET 1 AA8 4 PHE B 115 CYS B 124 0 SHEET 2 AA8 4 CYS B 129 LEU B 139 -1 O PHE B 132 N PHE B 121 SHEET 3 AA8 4 THR B 157 PRO B 162 -1 O THR B 157 N THR B 135 SHEET 4 AA8 4 ARG B 173 VAL B 177 -1 O ARG B 173 N SER B 160 SHEET 1 AA9 4 SER B 180 HIS B 185 0 SHEET 2 AA9 4 TRP B 190 SER B 196 -1 O ILE B 195 N SER B 180 SHEET 3 AA9 4 VAL B 203 TYR B 208 -1 O VAL B 205 N GLY B 194 SHEET 4 AA9 4 ILE B 211 LYS B 217 -1 O THR B 213 N LEU B 206 SHEET 1 AB1 4 ALA B 232 VAL B 234 0 SHEET 2 AB1 4 SER B 237 ASP B 244 -1 O PHE B 239 N ALA B 232 SHEET 3 AB1 4 SER B 252 GLU B 259 -1 O SER B 252 N ASP B 244 SHEET 4 AB1 4 LYS B 262 GLU B 268 -1 O LYS B 262 N GLU B 259 SHEET 1 AB2 4 GLU B 277 ASP B 284 0 SHEET 2 AB2 4 GLU B 287 ARG B 293 -1 O VAL B 291 N SER B 280 SHEET 3 AB2 4 PRO B 302 PHE B 306 -1 O PRO B 302 N CYS B 292 SHEET 4 AB2 4 TYR B 312 TYR B 316 -1 O GLY B 315 N TRP B 303 SHEET 1 AB3 4 PHE B 349 TYR B 353 0 SHEET 2 AB3 4 GLY B 356 ARG B 361 -1 O GLY B 356 N TYR B 353 SHEET 3 AB3 4 LYS B 369 ASP B 376 -1 O ILE B 374 N ILE B 359 SHEET 4 AB3 4 ILE B 389 TRP B 399 -1 O GLN B 391 N MET B 373 SHEET 1 AB4 4 GLY C 96 LYS C 102 0 SHEET 2 AB4 4 THR C 438 VAL C 448 -1 O SER C 444 N TYR C 100 SHEET 3 AB4 4 ARG C 419 GLY C 429 -1 N ARG C 428 O SER C 439 SHEET 4 AB4 4 SER C 403 GLN C 408 -1 N GLN C 408 O ARG C 419 SHEET 1 AB5 4 PHE C 115 CYS C 124 0 SHEET 2 AB5 4 CYS C 129 LEU C 139 -1 O PHE C 132 N PHE C 121 SHEET 3 AB5 4 THR C 157 PRO C 162 -1 O THR C 157 N THR C 135 SHEET 4 AB5 4 ARG C 173 VAL C 177 -1 O ARG C 173 N SER C 160 SHEET 1 AB6 4 SER C 180 HIS C 185 0 SHEET 2 AB6 4 TRP C 190 SER C 196 -1 O ILE C 195 N SER C 180 SHEET 3 AB6 4 VAL C 203 TYR C 208 -1 O VAL C 205 N GLY C 194 SHEET 4 AB6 4 ILE C 211 LYS C 217 -1 O THR C 213 N LEU C 206 SHEET 1 AB7 4 ALA C 232 VAL C 234 0 SHEET 2 AB7 4 SER C 237 ASP C 244 -1 O PHE C 239 N ALA C 232 SHEET 3 AB7 4 SER C 252 GLU C 259 -1 O SER C 252 N ASP C 244 SHEET 4 AB7 4 LYS C 262 GLU C 268 -1 O LYS C 262 N GLU C 259 SHEET 1 AB8 4 GLU C 277 ASP C 284 0 SHEET 2 AB8 4 GLU C 287 ARG C 293 -1 O VAL C 291 N SER C 280 SHEET 3 AB8 4 PRO C 302 PHE C 306 -1 O PRO C 302 N CYS C 292 SHEET 4 AB8 4 TYR C 312 TYR C 316 -1 O GLY C 315 N TRP C 303 SHEET 1 AB9 4 PHE C 349 TYR C 353 0 SHEET 2 AB9 4 GLY C 356 ARG C 361 -1 O GLY C 356 N TYR C 353 SHEET 3 AB9 4 LYS C 369 ASP C 376 -1 O ILE C 374 N ILE C 359 SHEET 4 AB9 4 ILE C 389 TRP C 399 -1 O GLN C 391 N MET C 373 SHEET 1 AC1 4 GLY D 96 LYS D 102 0 SHEET 2 AC1 4 THR D 438 VAL D 448 -1 O SER D 444 N TYR D 100 SHEET 3 AC1 4 ARG D 419 GLY D 429 -1 N ARG D 428 O SER D 439 SHEET 4 AC1 4 SER D 403 GLN D 408 -1 N GLN D 408 O ARG D 419 SHEET 1 AC2 4 PHE D 115 CYS D 124 0 SHEET 2 AC2 4 CYS D 129 LEU D 139 -1 O PHE D 132 N PHE D 121 SHEET 3 AC2 4 THR D 157 PRO D 162 -1 O THR D 157 N THR D 135 SHEET 4 AC2 4 ARG D 173 VAL D 177 -1 O ARG D 173 N SER D 160 SHEET 1 AC3 4 SER D 180 HIS D 185 0 SHEET 2 AC3 4 TRP D 190 SER D 196 -1 O ILE D 195 N SER D 180 SHEET 3 AC3 4 VAL D 203 TYR D 208 -1 O VAL D 205 N GLY D 194 SHEET 4 AC3 4 ILE D 211 LYS D 217 -1 O THR D 213 N LEU D 206 SHEET 1 AC4 4 ALA D 232 VAL D 234 0 SHEET 2 AC4 4 SER D 237 ASP D 244 -1 O PHE D 239 N ALA D 232 SHEET 3 AC4 4 SER D 252 GLU D 259 -1 O SER D 252 N ASP D 244 SHEET 4 AC4 4 LYS D 262 GLU D 268 -1 O LYS D 262 N GLU D 259 SHEET 1 AC5 4 GLU D 277 ASP D 284 0 SHEET 2 AC5 4 GLU D 287 ARG D 293 -1 O VAL D 291 N SER D 280 SHEET 3 AC5 4 PRO D 302 PHE D 306 -1 O PRO D 302 N CYS D 292 SHEET 4 AC5 4 TYR D 312 TYR D 316 -1 O GLY D 315 N TRP D 303 SHEET 1 AC6 4 PHE D 349 TYR D 353 0 SHEET 2 AC6 4 GLY D 356 ARG D 361 -1 O GLY D 356 N TYR D 353 SHEET 3 AC6 4 LYS D 369 ASP D 376 -1 O ILE D 374 N ILE D 359 SHEET 4 AC6 4 ILE D 389 TRP D 399 -1 O GLN D 391 N MET D 373 SHEET 1 AC7 4 LEU E 4 SER E 7 0 SHEET 2 AC7 4 ALA E 19 ALA E 25 -1 O ARG E 24 N THR E 5 SHEET 3 AC7 4 ASP E 71 ILE E 76 -1 O LEU E 74 N LEU E 21 SHEET 4 AC7 4 PHE E 63 SER E 68 -1 N SER E 64 O THR E 75 SHEET 1 AC8 6 THR E 10 LEU E 13 0 SHEET 2 AC8 6 THR E 102 ILE E 106 1 O LYS E 103 N LEU E 11 SHEET 3 AC8 6 VAL E 86 LYS E 91 -1 N TYR E 87 O THR E 102 SHEET 4 AC8 6 LEU E 34 GLN E 39 -1 N GLN E 39 O VAL E 86 SHEET 5 AC8 6 ARG E 46 SER E 50 -1 O LEU E 48 N TRP E 36 SHEET 6 AC8 6 SER E 54 ARG E 55 -1 O SER E 54 N SER E 50 SHEET 1 AC9 4 THR E 10 LEU E 13 0 SHEET 2 AC9 4 THR E 102 ILE E 106 1 O LYS E 103 N LEU E 11 SHEET 3 AC9 4 VAL E 86 LYS E 91 -1 N TYR E 87 O THR E 102 SHEET 4 AC9 4 THR E 97 PHE E 98 -1 O THR E 97 N LYS E 91 SHEET 1 AD1 4 LEU F 4 SER F 7 0 SHEET 2 AD1 4 ALA F 19 ALA F 25 -1 O ARG F 24 N THR F 5 SHEET 3 AD1 4 ASP F 71 ILE F 76 -1 O LEU F 74 N LEU F 21 SHEET 4 AD1 4 PHE F 63 SER F 68 -1 N SER F 64 O THR F 75 SHEET 1 AD2 6 THR F 10 LEU F 13 0 SHEET 2 AD2 6 THR F 102 ILE F 106 1 O LYS F 103 N LEU F 11 SHEET 3 AD2 6 VAL F 86 LYS F 91 -1 N TYR F 87 O THR F 102 SHEET 4 AD2 6 LEU F 34 GLN F 39 -1 N GLN F 39 O VAL F 86 SHEET 5 AD2 6 ARG F 46 SER F 50 -1 O LEU F 48 N TRP F 36 SHEET 6 AD2 6 SER F 54 ARG F 55 -1 O SER F 54 N SER F 50 SHEET 1 AD3 4 THR F 10 LEU F 13 0 SHEET 2 AD3 4 THR F 102 ILE F 106 1 O LYS F 103 N LEU F 11 SHEET 3 AD3 4 VAL F 86 LYS F 91 -1 N TYR F 87 O THR F 102 SHEET 4 AD3 4 THR F 97 PHE F 98 -1 O THR F 97 N LYS F 91 SHEET 1 AD4 4 LEU G 4 SER G 7 0 SHEET 2 AD4 4 ALA G 19 ALA G 25 -1 O ARG G 24 N THR G 5 SHEET 3 AD4 4 ASP G 71 ILE G 76 -1 O LEU G 74 N LEU G 21 SHEET 4 AD4 4 PHE G 63 SER G 68 -1 N SER G 64 O THR G 75 SHEET 1 AD5 6 THR G 10 LEU G 13 0 SHEET 2 AD5 6 THR G 102 ILE G 106 1 O LYS G 103 N LEU G 11 SHEET 3 AD5 6 VAL G 86 LYS G 91 -1 N TYR G 87 O THR G 102 SHEET 4 AD5 6 LEU G 34 GLN G 39 -1 N GLN G 39 O VAL G 86 SHEET 5 AD5 6 ARG G 46 SER G 50 -1 O LEU G 48 N TRP G 36 SHEET 6 AD5 6 SER G 54 ARG G 55 -1 O SER G 54 N SER G 50 SHEET 1 AD6 4 THR G 10 LEU G 13 0 SHEET 2 AD6 4 THR G 102 ILE G 106 1 O LYS G 103 N LEU G 11 SHEET 3 AD6 4 VAL G 86 LYS G 91 -1 N TYR G 87 O THR G 102 SHEET 4 AD6 4 THR G 97 PHE G 98 -1 O THR G 97 N LYS G 91 SHEET 1 AD7 4 LEU H 4 SER H 7 0 SHEET 2 AD7 4 ALA H 19 ALA H 25 -1 O ARG H 24 N THR H 5 SHEET 3 AD7 4 ASP H 71 ILE H 76 -1 O LEU H 74 N LEU H 21 SHEET 4 AD7 4 PHE H 63 SER H 68 -1 N SER H 64 O THR H 75 SHEET 1 AD8 6 THR H 10 LEU H 13 0 SHEET 2 AD8 6 THR H 102 ILE H 106 1 O LYS H 103 N LEU H 11 SHEET 3 AD8 6 VAL H 86 LYS H 91 -1 N TYR H 87 O THR H 102 SHEET 4 AD8 6 LEU H 34 GLN H 39 -1 N GLN H 39 O VAL H 86 SHEET 5 AD8 6 ARG H 46 SER H 50 -1 O LEU H 48 N TRP H 36 SHEET 6 AD8 6 SER H 54 ARG H 55 -1 O SER H 54 N SER H 50 SHEET 1 AD9 4 THR H 10 LEU H 13 0 SHEET 2 AD9 4 THR H 102 ILE H 106 1 O LYS H 103 N LEU H 11 SHEET 3 AD9 4 VAL H 86 LYS H 91 -1 N TYR H 87 O THR H 102 SHEET 4 AD9 4 THR H 97 PHE H 98 -1 O THR H 97 N LYS H 91 SHEET 1 AE1 4 LEU I 4 SER I 7 0 SHEET 2 AE1 4 SER I 17 ALA I 24 -1 O SER I 21 N SER I 7 SHEET 3 AE1 4 SER I 78 ASN I 84 -1 O MET I 83 N LEU I 18 SHEET 4 AE1 4 PHE I 68 ASP I 73 -1 N THR I 69 O GLN I 82 SHEET 1 AE2 6 GLY I 10 VAL I 12 0 SHEET 2 AE2 6 THR I 117 VAL I 121 1 O THR I 120 N GLY I 10 SHEET 3 AE2 6 ALA I 92 ASP I 99 -1 N TYR I 94 O THR I 117 SHEET 4 AE2 6 GLU I 33 GLN I 39 -1 N VAL I 37 O TYR I 95 SHEET 5 AE2 6 LEU I 45 ILE I 51 -1 O GLU I 46 N ARG I 38 SHEET 6 AE2 6 ILE I 58 TYR I 60 -1 O TYR I 59 N HIS I 50 SHEET 1 AE3 4 GLY I 10 VAL I 12 0 SHEET 2 AE3 4 THR I 117 VAL I 121 1 O THR I 120 N GLY I 10 SHEET 3 AE3 4 ALA I 92 ASP I 99 -1 N TYR I 94 O THR I 117 SHEET 4 AE3 4 VAL I 112 TRP I 113 -1 O VAL I 112 N ARG I 98 SHEET 1 AE4 2 TYR I 101 ASN I 102 0 SHEET 2 AE4 2 GLY I 106 TYR I 107 -1 O GLY I 106 N ASN I 102 SHEET 1 AE5 4 LEU J 4 SER J 7 0 SHEET 2 AE5 4 SER J 17 ALA J 24 -1 O SER J 21 N SER J 7 SHEET 3 AE5 4 SER J 78 ASN J 84 -1 O MET J 83 N LEU J 18 SHEET 4 AE5 4 PHE J 68 ASP J 73 -1 N THR J 69 O GLN J 82 SHEET 1 AE6 6 GLY J 10 VAL J 12 0 SHEET 2 AE6 6 THR J 117 VAL J 121 1 O THR J 120 N GLY J 10 SHEET 3 AE6 6 ALA J 92 ASP J 99 -1 N TYR J 94 O THR J 117 SHEET 4 AE6 6 GLU J 33 GLN J 39 -1 N VAL J 37 O TYR J 95 SHEET 5 AE6 6 LEU J 45 ILE J 51 -1 O GLU J 46 N ARG J 38 SHEET 6 AE6 6 ILE J 58 TYR J 60 -1 O TYR J 59 N HIS J 50 SHEET 1 AE7 4 GLY J 10 VAL J 12 0 SHEET 2 AE7 4 THR J 117 VAL J 121 1 O THR J 120 N GLY J 10 SHEET 3 AE7 4 ALA J 92 ASP J 99 -1 N TYR J 94 O THR J 117 SHEET 4 AE7 4 VAL J 112 TRP J 113 -1 O VAL J 112 N ARG J 98 SHEET 1 AE8 2 TYR J 101 ASN J 102 0 SHEET 2 AE8 2 GLY J 106 TYR J 107 -1 O GLY J 106 N ASN J 102 SHEET 1 AE9 4 LEU K 4 SER K 7 0 SHEET 2 AE9 4 SER K 17 ALA K 24 -1 O SER K 21 N SER K 7 SHEET 3 AE9 4 SER K 78 ASN K 84 -1 O MET K 83 N LEU K 18 SHEET 4 AE9 4 PHE K 68 ASP K 73 -1 N THR K 69 O GLN K 82 SHEET 1 AF1 6 GLY K 10 VAL K 12 0 SHEET 2 AF1 6 THR K 117 VAL K 121 1 O THR K 120 N GLY K 10 SHEET 3 AF1 6 ALA K 92 ASP K 99 -1 N TYR K 94 O THR K 117 SHEET 4 AF1 6 GLU K 33 GLN K 39 -1 N VAL K 37 O TYR K 95 SHEET 5 AF1 6 LEU K 45 ILE K 51 -1 O GLU K 46 N ARG K 38 SHEET 6 AF1 6 ILE K 58 TYR K 60 -1 O TYR K 59 N HIS K 50 SHEET 1 AF2 4 GLY K 10 VAL K 12 0 SHEET 2 AF2 4 THR K 117 VAL K 121 1 O THR K 120 N GLY K 10 SHEET 3 AF2 4 ALA K 92 ASP K 99 -1 N TYR K 94 O THR K 117 SHEET 4 AF2 4 VAL K 112 TRP K 113 -1 O VAL K 112 N ARG K 98 SHEET 1 AF3 2 TYR K 101 ASN K 102 0 SHEET 2 AF3 2 GLY K 106 TYR K 107 -1 O GLY K 106 N ASN K 102 SHEET 1 AF4 4 LEU L 4 SER L 7 0 SHEET 2 AF4 4 SER L 17 ALA L 24 -1 O SER L 21 N SER L 7 SHEET 3 AF4 4 SER L 78 ASN L 84 -1 O MET L 83 N LEU L 18 SHEET 4 AF4 4 PHE L 68 ASP L 73 -1 N THR L 69 O GLN L 82 SHEET 1 AF5 6 GLY L 10 VAL L 12 0 SHEET 2 AF5 6 THR L 117 VAL L 121 1 O THR L 120 N GLY L 10 SHEET 3 AF5 6 ALA L 92 ASP L 99 -1 N TYR L 94 O THR L 117 SHEET 4 AF5 6 GLU L 33 GLN L 39 -1 N VAL L 37 O TYR L 95 SHEET 5 AF5 6 LEU L 45 ILE L 51 -1 O GLU L 46 N ARG L 38 SHEET 6 AF5 6 ILE L 58 TYR L 60 -1 O TYR L 59 N HIS L 50 SHEET 1 AF6 4 GLY L 10 VAL L 12 0 SHEET 2 AF6 4 THR L 117 VAL L 121 1 O THR L 120 N GLY L 10 SHEET 3 AF6 4 ALA L 92 ASP L 99 -1 N TYR L 94 O THR L 117 SHEET 4 AF6 4 VAL L 112 TRP L 113 -1 O VAL L 112 N ARG L 98 SHEET 1 AF7 2 TYR L 101 ASN L 102 0 SHEET 2 AF7 2 GLY L 106 TYR L 107 -1 O GLY L 106 N ASN L 102 SSBOND 1 CYS A 92 CYS A 417 1555 1555 2.04 SSBOND 2 CYS A 124 CYS A 129 1555 1555 2.03 SSBOND 3 CYS A 184 CYS A 231 1555 1555 2.12 SSBOND 4 CYS A 184 CYS A 233 1555 1555 2.84 SSBOND 5 CYS A 233 CYS A 238 1555 1555 2.08 SSBOND 6 CYS A 279 CYS A 292 1555 1555 2.03 SSBOND 7 CYS A 281 CYS A 290 1555 1555 2.03 SSBOND 8 CYS A 318 CYS A 335 1555 1555 2.07 SSBOND 9 CYS A 421 CYS A 446 1555 1555 2.04 SSBOND 10 CYS B 92 CYS B 417 1555 1555 2.04 SSBOND 11 CYS B 124 CYS B 129 1555 1555 2.03 SSBOND 12 CYS B 184 CYS B 231 1555 1555 2.04 SSBOND 13 CYS B 184 CYS B 233 1555 1555 2.88 SSBOND 14 CYS B 233 CYS B 238 1555 1555 2.08 SSBOND 15 CYS B 279 CYS B 292 1555 1555 2.03 SSBOND 16 CYS B 281 CYS B 290 1555 1555 2.03 SSBOND 17 CYS B 318 CYS B 335 1555 1555 2.07 SSBOND 18 CYS B 421 CYS B 446 1555 1555 2.04 SSBOND 19 CYS C 92 CYS C 417 1555 1555 2.04 SSBOND 20 CYS C 124 CYS C 129 1555 1555 2.03 SSBOND 21 CYS C 184 CYS C 231 1555 1555 2.04 SSBOND 22 CYS C 184 CYS C 233 1555 1555 2.88 SSBOND 23 CYS C 233 CYS C 238 1555 1555 2.08 SSBOND 24 CYS C 279 CYS C 292 1555 1555 2.03 SSBOND 25 CYS C 281 CYS C 290 1555 1555 2.03 SSBOND 26 CYS C 318 CYS C 335 1555 1555 2.07 SSBOND 27 CYS C 421 CYS C 446 1555 1555 2.04 SSBOND 28 CYS D 92 CYS D 417 1555 1555 2.04 SSBOND 29 CYS D 124 CYS D 129 1555 1555 2.03 SSBOND 30 CYS D 184 CYS D 231 1555 1555 2.04 SSBOND 31 CYS D 184 CYS D 233 1555 1555 2.85 SSBOND 32 CYS D 233 CYS D 238 1555 1555 2.08 SSBOND 33 CYS D 279 CYS D 292 1555 1555 2.03 SSBOND 34 CYS D 281 CYS D 290 1555 1555 2.03 SSBOND 35 CYS D 318 CYS D 335 1555 1555 2.07 SSBOND 36 CYS D 421 CYS D 446 1555 1555 2.04 SSBOND 37 CYS E 23 CYS E 89 1555 1555 2.04 SSBOND 38 CYS F 23 CYS F 89 1555 1555 2.04 SSBOND 39 CYS G 23 CYS G 89 1555 1555 2.04 SSBOND 40 CYS H 23 CYS H 89 1555 1555 2.04 SSBOND 41 CYS I 22 CYS I 96 1555 1555 2.04 SSBOND 42 CYS J 22 CYS J 96 1555 1555 2.04 SSBOND 43 CYS K 22 CYS K 96 1555 1555 2.04 SSBOND 44 CYS L 22 CYS L 96 1555 1555 2.04 LINK ND2 ASN A 88 C1 NAG A 501 1555 1555 1.47 LINK ND2 ASN A 146 C1 NAG A 502 1555 1555 1.45 LINK ND2 ASN A 235 C1 NAG A 503 1555 1555 1.27 LINK ND2 ASN B 88 C1 NAG B 501 1555 1555 1.44 LINK ND2 ASN B 146 C1 NAG B 502 1555 1555 1.45 LINK ND2 ASN B 235 C1 NAG B 503 1555 1555 1.45 LINK ND2 ASN C 88 C1 NAG C 501 1555 1555 1.44 LINK ND2 ASN C 146 C1 NAG C 502 1555 1555 1.45 LINK ND2 ASN C 235 C1 NAG C 503 1555 1555 1.45 LINK ND2 ASN D 88 C1 NAG D 501 1555 1555 1.47 LINK ND2 ASN D 146 C1 NAG D 502 1555 1555 1.45 LINK ND2 ASN D 235 C1 NAG D 503 1555 1555 1.45 LINK O ASP A 294 CA CA A 504 1555 1555 1.85 LINK O GLY A 298 CA CA A 504 1555 1555 2.40 LINK OD2 ASP A 324 CA CA A 504 1555 1555 2.96 LINK O GLY A 342 CA CA A 504 1555 1555 2.73 LINK O ASN A 344 CA CA A 504 1555 1555 2.09 LINK OD1 ASP A 376 CA CA A 506 1555 1555 2.21 LINK OD2 ASP A 376 CA CA A 506 1555 1555 3.06 LINK OD1 ASN A 378 CA CA A 506 1555 1555 2.32 LINK OD1 ASP A 384 CA CA A 506 1555 1555 2.42 LINK O ASN A 386 CA CA A 506 1555 1555 2.36 LINK O ASP B 294 CA CA B 504 1555 1555 2.31 LINK O GLY B 298 CA CA B 504 1555 1555 2.55 LINK OD2 ASP B 324 CA CA B 504 1555 1555 3.20 LINK O GLY B 342 CA CA B 504 1555 1555 2.51 LINK O ASN B 344 CA CA B 504 1555 1555 1.88 LINK OD1 ASP B 376 CA CA B 505 1555 1555 2.37 LINK OD1 ASN B 378 CA CA B 505 1555 1555 2.14 LINK OD1 ASP B 384 CA CA B 505 1555 1555 2.32 LINK O ASN B 386 CA CA B 505 1555 1555 2.56 LINK O ASP C 294 CA CA C 504 1555 1555 2.30 LINK O GLY C 298 CA CA C 504 1555 1555 2.34 LINK OD2 ASP C 324 CA CA C 504 1555 1555 3.10 LINK O GLY C 342 CA CA C 504 1555 1555 2.59 LINK O ASN C 344 CA CA C 504 1555 1555 2.09 LINK OD1 ASP C 376 CA CA C 505 1555 1555 2.26 LINK OD1 ASN C 378 CA CA C 505 1555 1555 2.27 LINK OD1 ASP C 384 CA CA C 505 1555 1555 2.41 LINK O ASN C 386 CA CA C 505 1555 1555 2.35 LINK O ASP D 294 CA CA D 504 1555 1555 2.38 LINK O GLY D 298 CA CA D 504 1555 1555 2.49 LINK OD2 ASP D 324 CA CA D 504 1555 1555 3.09 LINK O GLY D 342 CA CA D 504 1555 1555 2.62 LINK O ASN D 344 CA CA D 504 1555 1555 1.95 LINK OD1 ASP D 376 CA CA D 505 1555 1555 2.19 LINK OD2 ASP D 376 CA CA D 505 1555 1555 3.09 LINK OD1 ASN D 378 CA CA D 505 1555 1555 2.23 LINK OD1 ASP D 384 CA CA D 505 1555 1555 2.45 LINK O ASN D 386 CA CA D 505 1555 1555 2.43 CISPEP 1 ASN A 325 PRO A 326 0 -29.75 CISPEP 2 ARG A 430 PRO A 431 0 -0.18 CISPEP 3 LEU A 463 PRO A 464 0 -1.34 CISPEP 4 ASN B 325 PRO B 326 0 -29.76 CISPEP 5 ARG B 430 PRO B 431 0 -0.20 CISPEP 6 LEU B 463 PRO B 464 0 -1.30 CISPEP 7 ASN C 325 PRO C 326 0 -29.75 CISPEP 8 ARG C 430 PRO C 431 0 -0.20 CISPEP 9 LEU C 463 PRO C 464 0 -1.26 CISPEP 10 ASN D 325 PRO D 326 0 -29.79 CISPEP 11 ARG D 430 PRO D 431 0 -0.19 CISPEP 12 LEU D 463 PRO D 464 0 -1.24 CISPEP 13 SER E 7 PRO E 8 0 -8.16 CISPEP 14 SER E 94 PRO E 95 0 -0.01 CISPEP 15 SER F 7 PRO F 8 0 -8.11 CISPEP 16 SER F 94 PRO F 95 0 0.06 CISPEP 17 SER G 7 PRO G 8 0 -8.10 CISPEP 18 SER G 94 PRO G 95 0 0.00 CISPEP 19 SER H 7 PRO H 8 0 -8.12 CISPEP 20 SER H 94 PRO H 95 0 0.06 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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