HEADER VIRAL PROTEIN/IMMUNE SYSTEM 01-JUL-25 9PDY TITLE HUMAN ANTIBODY FAB MPV510 BOUND TO HMPV DSCAV-ES2-IPDS F PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: FUSION GLYCOPROTEIN F0; COMPND 3 CHAIN: A, B, C; COMPND 4 SYNONYM: DSCAV-ES2-IPDS PRE-FUSION F; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: MPV510 FAB HEAVY CHAIN; COMPND 8 CHAIN: D, E, F; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: MPV510 FAB LIGHT CHAIN; COMPND 12 CHAIN: G, H, I; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN METAPNEUMOVIRUS; SOURCE 3 ORGANISM_TAXID: 162145; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_COMMON: HUMAN; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_COMMON: HUMAN; SOURCE 17 ORGANISM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 19 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HMPV, HUMAN RESPIRATORY DISEASE, CRYOEM, HUMAN METAPNEUMOVIRUS, VIRAL KEYWDS 2 PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR N.GHAZI ESFAHANI,J.MOUSA,A.M.KHALIL REVDAT 1 03-SEP-25 9PDY 0 JRNL AUTH A.M.KHALIL,B.GHAZI ESFAHANI,J.MOUSA JRNL TITL HUMAN METAPNEUMOVIRUS-SPECIFIC ANTIBODIES ISOLATED FROM JRNL TITL 2 INFECTED CHILDREN TARGET DIVERSE EPITOPES AND HAVE JRNL TITL 3 PROPHYLACTIC EFFICACY IN MICE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.85 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) : 2.850 REMARK 3 NUMBER OF PARTICLES : 287000 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 9PDY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUL-25. REMARK 100 THE DEPOSITION ID IS D_1000296520. 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 : MPV510 FAB BOUND TO HMPV DSCAV REMARK 245 -ES2-IPDS PRE-FUSION F 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 : 7.00 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 KRIOS REMARK 245 DETECTOR TYPE : DIRECT ELECTRON APOLLO (4K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2800.00 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) : 6000.00 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: NONAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, G, E, H, F, I 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 ALA A 86 REMARK 465 ASP A 87 REMARK 465 GLN A 88 REMARK 465 LEU A 89 REMARK 465 ALA A 90 REMARK 465 ARG A 91 REMARK 465 GLU A 92 REMARK 465 GLU A 93 REMARK 465 GLN A 94 REMARK 465 ILE A 95 REMARK 465 GLU A 96 REMARK 465 ASN A 97 REMARK 465 PRO A 98 REMARK 465 ARG A 99 REMARK 465 GLN A 100 REMARK 465 SER A 101 REMARK 465 ARG A 102 REMARK 465 ALA B 86 REMARK 465 ASP B 87 REMARK 465 GLN B 88 REMARK 465 LEU B 89 REMARK 465 ALA B 90 REMARK 465 ARG B 91 REMARK 465 GLU B 92 REMARK 465 GLU B 93 REMARK 465 GLN B 94 REMARK 465 ILE B 95 REMARK 465 GLU B 96 REMARK 465 ASN B 97 REMARK 465 PRO B 98 REMARK 465 ARG B 99 REMARK 465 GLN B 100 REMARK 465 SER B 101 REMARK 465 ARG B 102 REMARK 465 ALA C 86 REMARK 465 ASP C 87 REMARK 465 GLN C 88 REMARK 465 LEU C 89 REMARK 465 ALA C 90 REMARK 465 ARG C 91 REMARK 465 GLU C 92 REMARK 465 GLU C 93 REMARK 465 GLN C 94 REMARK 465 ILE C 95 REMARK 465 GLU C 96 REMARK 465 ASN C 97 REMARK 465 PRO C 98 REMARK 465 ARG C 99 REMARK 465 GLN C 100 REMARK 465 SER C 101 REMARK 465 ARG C 102 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 ASN B 178 H ASN B 180 1.53 REMARK 500 O ASN A 178 H ASN A 180 1.53 REMARK 500 O ASN C 178 H ASN C 180 1.53 REMARK 500 O ARG C 304 HE21 GLN C 307 1.58 REMARK 500 O ARG B 304 HE21 GLN B 307 1.58 REMARK 500 O ARG A 304 HE21 GLN A 307 1.58 REMARK 500 N GLY F 101 O TYR F 107 1.99 REMARK 500 N GLY E 101 O TYR E 107 2.00 REMARK 500 N GLY D 101 O TYR D 107 2.00 REMARK 500 OG SER B 37 OG1 THR B 281 2.01 REMARK 500 OG SER A 37 OG1 THR A 281 2.01 REMARK 500 OG SER C 37 OG1 THR C 281 2.01 REMARK 500 O ASN B 178 N ASN B 180 2.01 REMARK 500 O ASN A 178 N ASN A 180 2.01 REMARK 500 O ASN C 178 N ASN C 180 2.02 REMARK 500 OE1 GLU B 51 OG SER B 266 2.07 REMARK 500 OE1 GLU C 51 OG SER C 266 2.07 REMARK 500 OE1 GLU A 51 OG SER A 266 2.07 REMARK 500 O VAL C 169 OG1 THR C 174 2.09 REMARK 500 O VAL B 169 OG1 THR B 174 2.09 REMARK 500 O VAL A 169 OG1 THR A 174 2.09 REMARK 500 OE2 GLU B 305 OG SER B 364 2.10 REMARK 500 OE2 GLU A 305 OG SER A 364 2.10 REMARK 500 OE2 GLU C 305 OG SER C 364 2.10 REMARK 500 NH2 ARG C 82 O GLY C 264 2.15 REMARK 500 OG SER C 27 OG SER C 29 2.15 REMARK 500 OG SER A 27 OG SER A 29 2.15 REMARK 500 NH2 ARG A 82 O GLY A 264 2.15 REMARK 500 OG SER B 27 OG SER B 29 2.15 REMARK 500 NH2 ARG B 82 O GLY B 264 2.15 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 ASP A 62 CB - CG - OD1 ANGL. DEV. = 8.6 DEGREES REMARK 500 ASP B 62 CB - CG - OD1 ANGL. DEV. = 8.5 DEGREES REMARK 500 ASP C 62 CB - CG - OD1 ANGL. DEV. = 8.5 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 ASP A 62 40.49 -141.92 REMARK 500 LYS A 179 -59.11 39.52 REMARK 500 ASN A 180 23.55 145.82 REMARK 500 ASP A 183 55.44 -93.48 REMARK 500 ASP A 306 36.26 -96.55 REMARK 500 GLN A 346 -32.75 -26.26 REMARK 500 ILE A 352 -56.89 -121.24 REMARK 500 LYS A 386 120.21 -29.33 REMARK 500 ASP A 421 84.54 121.96 REMARK 500 ASN A 422 11.27 57.30 REMARK 500 ASN A 457 97.05 -163.43 REMARK 500 ASP B 62 40.47 -141.85 REMARK 500 LYS B 179 -58.99 39.48 REMARK 500 ASN B 180 23.54 145.71 REMARK 500 ASP B 183 55.46 -93.50 REMARK 500 ASP B 306 36.24 -96.52 REMARK 500 GLN B 346 -32.75 -26.27 REMARK 500 ILE B 352 -56.86 -121.23 REMARK 500 LYS B 386 120.20 -29.21 REMARK 500 ASP B 421 84.61 121.90 REMARK 500 ASN B 422 11.19 57.27 REMARK 500 ASN B 457 97.10 -163.43 REMARK 500 ASP C 62 40.55 -141.88 REMARK 500 LYS C 179 -59.16 39.59 REMARK 500 ASN C 180 23.55 145.88 REMARK 500 ASP C 183 55.53 -93.43 REMARK 500 ASP C 306 36.21 -96.50 REMARK 500 GLN C 346 -32.88 -26.29 REMARK 500 ILE C 352 -56.91 -121.28 REMARK 500 LYS C 386 120.09 -29.17 REMARK 500 ASP C 421 84.54 121.89 REMARK 500 ASN C 422 11.30 57.23 REMARK 500 ASN C 457 97.06 -163.53 REMARK 500 SER D 15 -0.55 76.51 REMARK 500 ASP D 33 -63.97 -107.17 REMARK 500 SER D 34 -128.98 175.67 REMARK 500 SER D 35 39.55 28.90 REMARK 500 TRP D 36 104.94 -56.96 REMARK 500 LYS D 45 -151.75 -91.59 REMARK 500 ILE D 50 -60.91 -94.27 REMARK 500 ASN D 102 71.43 -59.50 REMARK 500 TYR D 103 -73.26 -79.51 REMARK 500 ASP D 106 134.46 -170.53 REMARK 500 GLN G 26 -80.73 -88.57 REMARK 500 ASN G 29 -98.04 53.72 REMARK 500 TYR G 31 49.41 -93.19 REMARK 500 ALA G 49 3.02 80.83 REMARK 500 ALA G 50 -7.60 74.11 REMARK 500 ARG G 92 78.56 63.43 REMARK 500 PRO G 94 32.47 -84.88 REMARK 500 REMARK 500 THIS ENTRY HAS 84 RAMACHANDRAN OUTLIERS. 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 ASP D 33 SER D 34 148.20 REMARK 500 ASP E 33 SER E 34 148.20 REMARK 500 ASP F 33 SER F 34 148.26 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 HIS A 435 0.11 SIDE CHAIN REMARK 500 HIS B 435 0.11 SIDE CHAIN REMARK 500 HIS C 435 0.11 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-71548 RELATED DB: EMDB REMARK 900 HUMAN ANTIBODY FAB MPV510 BOUND TO HMPV DSCAV-ES2-IPDS F PROTEIN DBREF 9PDY A 19 466 UNP H6X1Z0 H6X1Z0_9MONO 19 466 DBREF 9PDY B 19 466 UNP H6X1Z0 H6X1Z0_9MONO 19 466 DBREF 9PDY C 19 466 UNP H6X1Z0 H6X1Z0_9MONO 19 466 DBREF 9PDY D 1 121 PDB 9PDY 9PDY 1 121 DBREF 9PDY G 1 107 PDB 9PDY 9PDY 1 107 DBREF 9PDY E 1 121 PDB 9PDY 9PDY 1 121 DBREF 9PDY H 1 107 PDB 9PDY 9PDY 1 107 DBREF 9PDY F 1 121 PDB 9PDY 9PDY 1 121 DBREF 9PDY I 1 107 PDB 9PDY 9PDY 1 107 SEQADV 9PDY CYS A 84 UNP H6X1Z0 VAL 84 CONFLICT SEQADV 9PDY CYS A 110 UNP H6X1Z0 LEU 110 CONFLICT SEQADV 9PDY CYS A 127 UNP H6X1Z0 THR 127 CONFLICT SEQADV 9PDY CYS A 140 UNP H6X1Z0 ALA 140 CONFLICT SEQADV 9PDY CYS A 147 UNP H6X1Z0 ALA 147 CONFLICT SEQADV 9PDY CYS A 153 UNP H6X1Z0 ASN 153 CONFLICT SEQADV 9PDY PRO A 185 UNP H6X1Z0 ALA 185 CONFLICT SEQADV 9PDY LYS A 219 UNP H6X1Z0 LEU 219 CONFLICT SEQADV 9PDY ILE A 231 UNP H6X1Z0 VAL 231 CONFLICT SEQADV 9PDY CYS A 249 UNP H6X1Z0 ALA 249 CONFLICT SEQADV 9PDY CYS A 322 UNP H6X1Z0 ASN 322 CONFLICT SEQADV 9PDY CYS A 365 UNP H6X1Z0 THR 365 CONFLICT SEQADV 9PDY GLN A 453 UNP H6X1Z0 GLU 453 CONFLICT SEQADV 9PDY CYS A 463 UNP H6X1Z0 VAL 463 CONFLICT SEQADV 9PDY CYS B 84 UNP H6X1Z0 VAL 84 CONFLICT SEQADV 9PDY CYS B 110 UNP H6X1Z0 LEU 110 CONFLICT SEQADV 9PDY CYS B 127 UNP H6X1Z0 THR 127 CONFLICT SEQADV 9PDY CYS B 140 UNP H6X1Z0 ALA 140 CONFLICT SEQADV 9PDY CYS B 147 UNP H6X1Z0 ALA 147 CONFLICT SEQADV 9PDY CYS B 153 UNP H6X1Z0 ASN 153 CONFLICT SEQADV 9PDY PRO B 185 UNP H6X1Z0 ALA 185 CONFLICT SEQADV 9PDY LYS B 219 UNP H6X1Z0 LEU 219 CONFLICT SEQADV 9PDY ILE B 231 UNP H6X1Z0 VAL 231 CONFLICT SEQADV 9PDY CYS B 249 UNP H6X1Z0 ALA 249 CONFLICT SEQADV 9PDY CYS B 322 UNP H6X1Z0 ASN 322 CONFLICT SEQADV 9PDY CYS B 365 UNP H6X1Z0 THR 365 CONFLICT SEQADV 9PDY GLN B 453 UNP H6X1Z0 GLU 453 CONFLICT SEQADV 9PDY CYS B 463 UNP H6X1Z0 VAL 463 CONFLICT SEQADV 9PDY CYS C 84 UNP H6X1Z0 VAL 84 CONFLICT SEQADV 9PDY CYS C 110 UNP H6X1Z0 LEU 110 CONFLICT SEQADV 9PDY CYS C 127 UNP H6X1Z0 THR 127 CONFLICT SEQADV 9PDY CYS C 140 UNP H6X1Z0 ALA 140 CONFLICT SEQADV 9PDY CYS C 147 UNP H6X1Z0 ALA 147 CONFLICT SEQADV 9PDY CYS C 153 UNP H6X1Z0 ASN 153 CONFLICT SEQADV 9PDY PRO C 185 UNP H6X1Z0 ALA 185 CONFLICT SEQADV 9PDY LYS C 219 UNP H6X1Z0 LEU 219 CONFLICT SEQADV 9PDY ILE C 231 UNP H6X1Z0 VAL 231 CONFLICT SEQADV 9PDY CYS C 249 UNP H6X1Z0 ALA 249 CONFLICT SEQADV 9PDY CYS C 322 UNP H6X1Z0 ASN 322 CONFLICT SEQADV 9PDY CYS C 365 UNP H6X1Z0 THR 365 CONFLICT SEQADV 9PDY GLN C 453 UNP H6X1Z0 GLU 453 CONFLICT SEQADV 9PDY CYS C 463 UNP H6X1Z0 VAL 463 CONFLICT SEQRES 1 A 448 LEU LYS GLU SER TYR LEU GLU GLU SER CYS SER THR ILE SEQRES 2 A 448 THR GLU GLY TYR LEU SER VAL LEU ARG THR GLY TRP TYR SEQRES 3 A 448 THR ASN VAL PHE THR LEU GLU VAL GLY ASP VAL GLU ASN SEQRES 4 A 448 LEU THR CYS ALA ASP GLY PRO SER LEU ILE LYS THR GLU SEQRES 5 A 448 LEU ASP LEU THR LYS SER ALA LEU ARG GLU LEU ARG THR SEQRES 6 A 448 CYS SER ALA ASP GLN LEU ALA ARG GLU GLU GLN ILE GLU SEQRES 7 A 448 ASN PRO ARG GLN SER ARG PHE VAL LEU GLY ALA ILE ALA SEQRES 8 A 448 CYS GLY VAL ALA THR ALA ALA ALA VAL THR ALA GLY VAL SEQRES 9 A 448 ALA ILE ALA LYS CYS ILE ARG LEU GLU SER GLU VAL THR SEQRES 10 A 448 ALA ILE LYS ASN CYS LEU LYS LYS THR ASN GLU CYS VAL SEQRES 11 A 448 SER THR LEU GLY CYS GLY VAL ARG VAL LEU ALA THR ALA SEQRES 12 A 448 VAL ARG GLU LEU LYS ASP PHE VAL SER LYS ASN LEU THR SEQRES 13 A 448 ARG ALA ILE ASN LYS ASN LYS CYS ASP ILE PRO ASP LEU SEQRES 14 A 448 LYS MET ALA VAL SER PHE SER GLN PHE ASN ARG ARG PHE SEQRES 15 A 448 LEU ASN VAL VAL ARG GLN PHE SER ASP ASN ALA GLY ILE SEQRES 16 A 448 THR PRO ALA ILE SER LYS ASP LEU MET THR ASP ALA GLU SEQRES 17 A 448 LEU ALA ARG ALA ILE SER ASN MET PRO THR SER ALA GLY SEQRES 18 A 448 GLN ILE LYS LEU MET LEU GLU ASN ARG CYS MET VAL ARG SEQRES 19 A 448 ARG LYS GLY PHE GLY ILE LEU ILE GLY VAL TYR GLY SER SEQRES 20 A 448 SER VAL ILE TYR MET VAL GLN LEU PRO ILE PHE GLY VAL SEQRES 21 A 448 ILE ASP THR PRO CYS TRP ILE VAL LYS ALA ALA PRO SER SEQRES 22 A 448 CYS SER GLU LYS LYS GLY ASN TYR ALA CYS LEU LEU ARG SEQRES 23 A 448 GLU ASP GLN GLY TRP TYR CYS GLN ASN ALA GLY SER THR SEQRES 24 A 448 VAL TYR TYR PRO CYS GLU LYS ASP CYS GLU THR ARG GLY SEQRES 25 A 448 ASP HIS VAL PHE CYS ASP THR ALA ALA GLY ILE ASN VAL SEQRES 26 A 448 ALA GLU GLN SER LYS GLU CYS ASN ILE ASN ILE SER THR SEQRES 27 A 448 THR ASN TYR PRO CYS LYS VAL SER CYS GLY ARG HIS PRO SEQRES 28 A 448 ILE SER MET VAL ALA LEU SER PRO LEU GLY ALA LEU VAL SEQRES 29 A 448 ALA CYS TYR LYS GLY VAL SER CYS SER ILE GLY SER ASN SEQRES 30 A 448 ARG VAL GLY ILE ILE LYS GLN LEU ASN LYS GLY CYS SER SEQRES 31 A 448 TYR ILE THR ASN GLN ASP ALA ASP THR VAL THR ILE ASP SEQRES 32 A 448 ASN THR VAL TYR GLN LEU SER LYS VAL GLU GLY GLU GLN SEQRES 33 A 448 HIS VAL ILE LYS GLY ARG PRO VAL SER SER SER PHE ASP SEQRES 34 A 448 PRO VAL LYS PHE PRO GLN ASP GLN PHE ASN VAL ALA LEU SEQRES 35 A 448 ASP GLN CYS PHE GLU SER SEQRES 1 B 448 LEU LYS GLU SER TYR LEU GLU GLU SER CYS SER THR ILE SEQRES 2 B 448 THR GLU GLY TYR LEU SER VAL LEU ARG THR GLY TRP TYR SEQRES 3 B 448 THR ASN VAL PHE THR LEU GLU VAL GLY ASP VAL GLU ASN SEQRES 4 B 448 LEU THR CYS ALA ASP GLY PRO SER LEU ILE LYS THR GLU SEQRES 5 B 448 LEU ASP LEU THR LYS SER ALA LEU ARG GLU LEU ARG THR SEQRES 6 B 448 CYS SER ALA ASP GLN LEU ALA ARG GLU GLU GLN ILE GLU SEQRES 7 B 448 ASN PRO ARG GLN SER ARG PHE VAL LEU GLY ALA ILE ALA SEQRES 8 B 448 CYS GLY VAL ALA THR ALA ALA ALA VAL THR ALA GLY VAL SEQRES 9 B 448 ALA ILE ALA LYS CYS ILE ARG LEU GLU SER GLU VAL THR SEQRES 10 B 448 ALA ILE LYS ASN CYS LEU LYS LYS THR ASN GLU CYS VAL SEQRES 11 B 448 SER THR LEU GLY CYS GLY VAL ARG VAL LEU ALA THR ALA SEQRES 12 B 448 VAL ARG GLU LEU LYS ASP PHE VAL SER LYS ASN LEU THR SEQRES 13 B 448 ARG ALA ILE ASN LYS ASN LYS CYS ASP ILE PRO ASP LEU SEQRES 14 B 448 LYS MET ALA VAL SER PHE SER GLN PHE ASN ARG ARG PHE SEQRES 15 B 448 LEU ASN VAL VAL ARG GLN PHE SER ASP ASN ALA GLY ILE SEQRES 16 B 448 THR PRO ALA ILE SER LYS ASP LEU MET THR ASP ALA GLU SEQRES 17 B 448 LEU ALA ARG ALA ILE SER ASN MET PRO THR SER ALA GLY SEQRES 18 B 448 GLN ILE LYS LEU MET LEU GLU ASN ARG CYS MET VAL ARG SEQRES 19 B 448 ARG LYS GLY PHE GLY ILE LEU ILE GLY VAL TYR GLY SER SEQRES 20 B 448 SER VAL ILE TYR MET VAL GLN LEU PRO ILE PHE GLY VAL SEQRES 21 B 448 ILE ASP THR PRO CYS TRP ILE VAL LYS ALA ALA PRO SER SEQRES 22 B 448 CYS SER GLU LYS LYS GLY ASN TYR ALA CYS LEU LEU ARG SEQRES 23 B 448 GLU ASP GLN GLY TRP TYR CYS GLN ASN ALA GLY SER THR SEQRES 24 B 448 VAL TYR TYR PRO CYS GLU LYS ASP CYS GLU THR ARG GLY SEQRES 25 B 448 ASP HIS VAL PHE CYS ASP THR ALA ALA GLY ILE ASN VAL SEQRES 26 B 448 ALA GLU GLN SER LYS GLU CYS ASN ILE ASN ILE SER THR SEQRES 27 B 448 THR ASN TYR PRO CYS LYS VAL SER CYS GLY ARG HIS PRO SEQRES 28 B 448 ILE SER MET VAL ALA LEU SER PRO LEU GLY ALA LEU VAL SEQRES 29 B 448 ALA CYS TYR LYS GLY VAL SER CYS SER ILE GLY SER ASN SEQRES 30 B 448 ARG VAL GLY ILE ILE LYS GLN LEU ASN LYS GLY CYS SER SEQRES 31 B 448 TYR ILE THR ASN GLN ASP ALA ASP THR VAL THR ILE ASP SEQRES 32 B 448 ASN THR VAL TYR GLN LEU SER LYS VAL GLU GLY GLU GLN SEQRES 33 B 448 HIS VAL ILE LYS GLY ARG PRO VAL SER SER SER PHE ASP SEQRES 34 B 448 PRO VAL LYS PHE PRO GLN ASP GLN PHE ASN VAL ALA LEU SEQRES 35 B 448 ASP GLN CYS PHE GLU SER SEQRES 1 C 448 LEU LYS GLU SER TYR LEU GLU GLU SER CYS SER THR ILE SEQRES 2 C 448 THR GLU GLY TYR LEU SER VAL LEU ARG THR GLY TRP TYR SEQRES 3 C 448 THR ASN VAL PHE THR LEU GLU VAL GLY ASP VAL GLU ASN SEQRES 4 C 448 LEU THR CYS ALA ASP GLY PRO SER LEU ILE LYS THR GLU SEQRES 5 C 448 LEU ASP LEU THR LYS SER ALA LEU ARG GLU LEU ARG THR SEQRES 6 C 448 CYS SER ALA ASP GLN LEU ALA ARG GLU GLU GLN ILE GLU SEQRES 7 C 448 ASN PRO ARG GLN SER ARG PHE VAL LEU GLY ALA ILE ALA SEQRES 8 C 448 CYS GLY VAL ALA THR ALA ALA ALA VAL THR ALA GLY VAL SEQRES 9 C 448 ALA ILE ALA LYS CYS ILE ARG LEU GLU SER GLU VAL THR SEQRES 10 C 448 ALA ILE LYS ASN CYS LEU LYS LYS THR ASN GLU CYS VAL SEQRES 11 C 448 SER THR LEU GLY CYS GLY VAL ARG VAL LEU ALA THR ALA SEQRES 12 C 448 VAL ARG GLU LEU LYS ASP PHE VAL SER LYS ASN LEU THR SEQRES 13 C 448 ARG ALA ILE ASN LYS ASN LYS CYS ASP ILE PRO ASP LEU SEQRES 14 C 448 LYS MET ALA VAL SER PHE SER GLN PHE ASN ARG ARG PHE SEQRES 15 C 448 LEU ASN VAL VAL ARG GLN PHE SER ASP ASN ALA GLY ILE SEQRES 16 C 448 THR PRO ALA ILE SER LYS ASP LEU MET THR ASP ALA GLU SEQRES 17 C 448 LEU ALA ARG ALA ILE SER ASN MET PRO THR SER ALA GLY SEQRES 18 C 448 GLN ILE LYS LEU MET LEU GLU ASN ARG CYS MET VAL ARG SEQRES 19 C 448 ARG LYS GLY PHE GLY ILE LEU ILE GLY VAL TYR GLY SER SEQRES 20 C 448 SER VAL ILE TYR MET VAL GLN LEU PRO ILE PHE GLY VAL SEQRES 21 C 448 ILE ASP THR PRO CYS TRP ILE VAL LYS ALA ALA PRO SER SEQRES 22 C 448 CYS SER GLU LYS LYS GLY ASN TYR ALA CYS LEU LEU ARG SEQRES 23 C 448 GLU ASP GLN GLY TRP TYR CYS GLN ASN ALA GLY SER THR SEQRES 24 C 448 VAL TYR TYR PRO CYS GLU LYS ASP CYS GLU THR ARG GLY SEQRES 25 C 448 ASP HIS VAL PHE CYS ASP THR ALA ALA GLY ILE ASN VAL SEQRES 26 C 448 ALA GLU GLN SER LYS GLU CYS ASN ILE ASN ILE SER THR SEQRES 27 C 448 THR ASN TYR PRO CYS LYS VAL SER CYS GLY ARG HIS PRO SEQRES 28 C 448 ILE SER MET VAL ALA LEU SER PRO LEU GLY ALA LEU VAL SEQRES 29 C 448 ALA CYS TYR LYS GLY VAL SER CYS SER ILE GLY SER ASN SEQRES 30 C 448 ARG VAL GLY ILE ILE LYS GLN LEU ASN LYS GLY CYS SER SEQRES 31 C 448 TYR ILE THR ASN GLN ASP ALA ASP THR VAL THR ILE ASP SEQRES 32 C 448 ASN THR VAL TYR GLN LEU SER LYS VAL GLU GLY GLU GLN SEQRES 33 C 448 HIS VAL ILE LYS GLY ARG PRO VAL SER SER SER PHE ASP SEQRES 34 C 448 PRO VAL LYS PHE PRO GLN ASP GLN PHE ASN VAL ALA LEU SEQRES 35 C 448 ASP GLN CYS PHE GLU SER SEQRES 1 D 121 GLN VAL GLN LEU GLN GLU SER GLY SER GLY LEU VAL LYS SEQRES 2 D 121 PRO SER GLN THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 D 121 GLY SER ILE SER SER GLY ASP SER SER TRP SER TRP ILE SEQRES 4 D 121 ARG GLN PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY HIS SEQRES 5 D 121 VAL TYR GLU SER GLY ASN THR TYR TYR ASP PRO SER LEU SEQRES 6 D 121 GLN SER ARG VAL THR ILE SER VAL ASP ARG SER ARG ASN SEQRES 7 D 121 GLN PHE SER LEU LYS LEU THR SER VAL THR VAL ALA ASP SEQRES 8 D 121 THR ALA VAL TYR TYR CYS ALA ARG GLU GLY ASN TYR GLY SEQRES 9 D 121 TRP ASP TYR PHE ASP TYR TRP GLY GLN GLY THR LEU VAL SEQRES 10 D 121 THR VAL SER SER SEQRES 1 G 107 ASP ILE GLN MET THR SER PRO PHE SER LEU SER ALA SER SEQRES 2 G 107 VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER GLN SEQRES 3 G 107 SER ILE ASN SER TYR LEU ASN TRP TYR GLN GLN LYS PRO SEQRES 4 G 107 GLY LYS ALA PRO ARG LEU LEU ILE TYR ALA ALA SER SER SEQRES 5 G 107 LEU GLN SER GLY VAL PRO SER ARG PHE ARG GLY SER GLY SEQRES 6 G 107 SER GLY THR ASP PHE ALA LEU THR ILE SER SER LEU GLN SEQRES 7 G 107 PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER TYR SEQRES 8 G 107 ARG PRO PRO SER ARG THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 G 107 GLU MET LYS SEQRES 1 E 121 GLN VAL GLN LEU GLN GLU SER GLY SER GLY LEU VAL LYS SEQRES 2 E 121 PRO SER GLN THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 E 121 GLY SER ILE SER SER GLY ASP SER SER TRP SER TRP ILE SEQRES 4 E 121 ARG GLN PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY HIS SEQRES 5 E 121 VAL TYR GLU SER GLY ASN THR TYR TYR ASP PRO SER LEU SEQRES 6 E 121 GLN SER ARG VAL THR ILE SER VAL ASP ARG SER ARG ASN SEQRES 7 E 121 GLN PHE SER LEU LYS LEU THR SER VAL THR VAL ALA ASP SEQRES 8 E 121 THR ALA VAL TYR TYR CYS ALA ARG GLU GLY ASN TYR GLY SEQRES 9 E 121 TRP ASP TYR PHE ASP TYR TRP GLY GLN GLY THR LEU VAL SEQRES 10 E 121 THR VAL SER SER SEQRES 1 H 107 ASP ILE GLN MET THR SER PRO PHE SER LEU SER ALA SER SEQRES 2 H 107 VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER GLN SEQRES 3 H 107 SER ILE ASN SER TYR LEU ASN TRP TYR GLN GLN LYS PRO SEQRES 4 H 107 GLY LYS ALA PRO ARG LEU LEU ILE TYR ALA ALA SER SER SEQRES 5 H 107 LEU GLN SER GLY VAL PRO SER ARG PHE ARG GLY SER GLY SEQRES 6 H 107 SER GLY THR ASP PHE ALA LEU THR ILE SER SER LEU GLN SEQRES 7 H 107 PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER TYR SEQRES 8 H 107 ARG PRO PRO SER ARG THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 H 107 GLU MET LYS SEQRES 1 F 121 GLN VAL GLN LEU GLN GLU SER GLY SER GLY LEU VAL LYS SEQRES 2 F 121 PRO SER GLN THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 F 121 GLY SER ILE SER SER GLY ASP SER SER TRP SER TRP ILE SEQRES 4 F 121 ARG GLN PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY HIS SEQRES 5 F 121 VAL TYR GLU SER GLY ASN THR TYR TYR ASP PRO SER LEU SEQRES 6 F 121 GLN SER ARG VAL THR ILE SER VAL ASP ARG SER ARG ASN SEQRES 7 F 121 GLN PHE SER LEU LYS LEU THR SER VAL THR VAL ALA ASP SEQRES 8 F 121 THR ALA VAL TYR TYR CYS ALA ARG GLU GLY ASN TYR GLY SEQRES 9 F 121 TRP ASP TYR PHE ASP TYR TRP GLY GLN GLY THR LEU VAL SEQRES 10 F 121 THR VAL SER SER SEQRES 1 I 107 ASP ILE GLN MET THR SER PRO PHE SER LEU SER ALA SER SEQRES 2 I 107 VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER GLN SEQRES 3 I 107 SER ILE ASN SER TYR LEU ASN TRP TYR GLN GLN LYS PRO SEQRES 4 I 107 GLY LYS ALA PRO ARG LEU LEU ILE TYR ALA ALA SER SER SEQRES 5 I 107 LEU GLN SER GLY VAL PRO SER ARG PHE ARG GLY SER GLY SEQRES 6 I 107 SER GLY THR ASP PHE ALA LEU THR ILE SER SER LEU GLN SEQRES 7 I 107 PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER TYR SEQRES 8 I 107 ARG PRO PRO SER ARG THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 I 107 GLU MET LYS HET NAG A 601 28 HET NAG A 602 28 HET NAG B 601 28 HET NAG B 602 28 HET NAG C 601 28 HET NAG C 602 28 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE 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 10 NAG 6(C8 H15 N O6) HELIX 1 AA1 SER A 65 THR A 83 1 19 HELIX 2 AA2 VAL A 104 LEU A 130 1 27 HELIX 3 AA3 LEU A 130 LEU A 141 1 12 HELIX 4 AA4 ARG A 163 ASN A 172 1 10 HELIX 5 AA5 ASN A 172 ILE A 177 1 6 HELIX 6 AA6 ASP A 186 ALA A 211 1 26 HELIX 7 AA7 THR A 223 ASN A 233 1 11 HELIX 8 AA8 SER A 237 ASN A 247 1 11 HELIX 9 AA9 ASN A 247 GLY A 255 1 9 HELIX 10 AB1 ALA A 338 GLY A 340 5 3 HELIX 11 AB2 ALA A 344 LYS A 348 5 5 HELIX 12 AB3 GLU A 349 ILE A 354 1 6 HELIX 13 AB4 PRO A 441 PHE A 446 1 6 HELIX 14 AB5 LEU A 460 PHE A 464 1 5 HELIX 15 AB6 SER B 65 THR B 83 1 19 HELIX 16 AB7 VAL B 104 LEU B 130 1 27 HELIX 17 AB8 LEU B 130 LEU B 141 1 12 HELIX 18 AB9 ARG B 163 ASN B 172 1 10 HELIX 19 AC1 ASN B 172 ILE B 177 1 6 HELIX 20 AC2 ASP B 186 ALA B 211 1 26 HELIX 21 AC3 THR B 223 ASN B 233 1 11 HELIX 22 AC4 SER B 237 ASN B 247 1 11 HELIX 23 AC5 ASN B 247 GLY B 255 1 9 HELIX 24 AC6 ALA B 338 GLY B 340 5 3 HELIX 25 AC7 ALA B 344 LYS B 348 5 5 HELIX 26 AC8 GLU B 349 ILE B 354 1 6 HELIX 27 AC9 PRO B 441 PHE B 446 1 6 HELIX 28 AD1 LEU B 460 PHE B 464 1 5 HELIX 29 AD2 SER C 65 THR C 83 1 19 HELIX 30 AD3 VAL C 104 LEU C 130 1 27 HELIX 31 AD4 LEU C 130 LEU C 141 1 12 HELIX 32 AD5 ARG C 163 ASN C 172 1 10 HELIX 33 AD6 ASN C 172 ILE C 177 1 6 HELIX 34 AD7 ASP C 186 ALA C 211 1 26 HELIX 35 AD8 THR C 223 ASN C 233 1 11 HELIX 36 AD9 SER C 237 ASN C 247 1 11 HELIX 37 AE1 ASN C 247 GLY C 255 1 9 HELIX 38 AE2 ALA C 338 GLY C 340 5 3 HELIX 39 AE3 ALA C 344 LYS C 348 5 5 HELIX 40 AE4 GLU C 349 ILE C 354 1 6 HELIX 41 AE5 PRO C 441 PHE C 446 1 6 HELIX 42 AE6 LEU C 460 PHE C 464 1 5 HELIX 43 AE7 THR D 88 THR D 92 5 5 HELIX 44 AE8 THR E 88 THR E 92 5 5 HELIX 45 AE9 THR F 88 THR F 92 5 5 SHEET 1 AA1 7 GLU A 327 ARG A 329 0 SHEET 2 AA1 7 HIS A 332 ASP A 336 -1 O PHE A 334 N GLU A 327 SHEET 3 AA1 7 SER A 29 ARG A 40 1 N VAL A 38 O CYS A 335 SHEET 4 AA1 7 VAL A 278 ALA A 288 -1 O THR A 281 N SER A 37 SHEET 5 AA1 7 GLY A 308 ASN A 313 -1 O GLN A 312 N PRO A 282 SHEET 6 AA1 7 SER A 316 TYR A 320 -1 O SER A 316 N ASN A 313 SHEET 7 AA1 7 ILE A 341 VAL A 343 -1 O ILE A 341 N TYR A 319 SHEET 1 AA2 5 GLU A 327 ARG A 329 0 SHEET 2 AA2 5 HIS A 332 ASP A 336 -1 O PHE A 334 N GLU A 327 SHEET 3 AA2 5 SER A 29 ARG A 40 1 N VAL A 38 O CYS A 335 SHEET 4 AA2 5 LYS A 20 LEU A 24 -1 N LEU A 24 O SER A 29 SHEET 5 AA2 5 GLU A 433 ILE A 437 1 O HIS A 435 N TYR A 23 SHEET 1 AA3 5 GLU A 146 THR A 150 0 SHEET 2 AA3 5 ARG A 156 VAL A 162 -1 O VAL A 157 N SER A 149 SHEET 3 AA3 5 TYR A 44 GLU A 51 1 N VAL A 47 O THR A 160 SHEET 4 AA3 5 SER A 266 LEU A 273 -1 O TYR A 269 N PHE A 48 SHEET 5 AA3 5 PHE A 256 TYR A 263 -1 N ILE A 258 O MET A 270 SHEET 1 AA4 2 GLU A 294 LYS A 295 0 SHEET 2 AA4 2 ASN A 298 TYR A 299 -1 O ASN A 298 N LYS A 295 SHEET 1 AA5 3 CYS A 301 ARG A 304 0 SHEET 2 AA5 3 LYS A 362 GLY A 366 -1 O SER A 364 N LEU A 303 SHEET 3 AA5 3 GLN A 455 ALA A 459 -1 O VAL A 458 N VAL A 363 SHEET 1 AA6 3 MET A 372 LEU A 375 0 SHEET 2 AA6 3 GLY A 379 CYS A 384 -1 O ALA A 383 N MET A 372 SHEET 3 AA6 3 GLY A 406 THR A 411 -1 O SER A 408 N VAL A 382 SHEET 1 AA7 3 SER A 391 GLY A 393 0 SHEET 2 AA7 3 THR A 417 THR A 419 -1 O THR A 419 N SER A 391 SHEET 3 AA7 3 VAL A 424 GLN A 426 -1 O TYR A 425 N VAL A 418 SHEET 1 AA8 7 GLU B 327 ARG B 329 0 SHEET 2 AA8 7 HIS B 332 ASP B 336 -1 O PHE B 334 N GLU B 327 SHEET 3 AA8 7 SER B 29 ARG B 40 1 N VAL B 38 O CYS B 335 SHEET 4 AA8 7 VAL B 278 ALA B 288 -1 O THR B 281 N SER B 37 SHEET 5 AA8 7 GLY B 308 ASN B 313 -1 O TYR B 310 N TRP B 284 SHEET 6 AA8 7 SER B 316 TYR B 320 -1 O SER B 316 N ASN B 313 SHEET 7 AA8 7 ILE B 341 VAL B 343 -1 O ILE B 341 N TYR B 319 SHEET 1 AA9 5 GLU B 327 ARG B 329 0 SHEET 2 AA9 5 HIS B 332 ASP B 336 -1 O PHE B 334 N GLU B 327 SHEET 3 AA9 5 SER B 29 ARG B 40 1 N VAL B 38 O CYS B 335 SHEET 4 AA9 5 LYS B 20 LEU B 24 -1 N LEU B 24 O SER B 29 SHEET 5 AA9 5 GLU B 433 ILE B 437 1 O HIS B 435 N TYR B 23 SHEET 1 AB1 5 GLU B 146 THR B 150 0 SHEET 2 AB1 5 ARG B 156 VAL B 162 -1 O VAL B 157 N SER B 149 SHEET 3 AB1 5 TYR B 44 GLU B 51 1 N VAL B 47 O THR B 160 SHEET 4 AB1 5 SER B 266 LEU B 273 -1 O TYR B 269 N PHE B 48 SHEET 5 AB1 5 PHE B 256 TYR B 263 -1 N ILE B 258 O MET B 270 SHEET 1 AB2 2 GLU B 294 LYS B 295 0 SHEET 2 AB2 2 ASN B 298 TYR B 299 -1 O ASN B 298 N LYS B 295 SHEET 1 AB3 3 CYS B 301 ARG B 304 0 SHEET 2 AB3 3 LYS B 362 GLY B 366 -1 O SER B 364 N LEU B 303 SHEET 3 AB3 3 GLN B 455 ALA B 459 -1 O VAL B 458 N VAL B 363 SHEET 1 AB4 3 MET B 372 LEU B 375 0 SHEET 2 AB4 3 GLY B 379 CYS B 384 -1 O ALA B 383 N MET B 372 SHEET 3 AB4 3 GLY B 406 THR B 411 -1 O SER B 408 N VAL B 382 SHEET 1 AB5 3 SER B 391 GLY B 393 0 SHEET 2 AB5 3 THR B 417 THR B 419 -1 O THR B 419 N SER B 391 SHEET 3 AB5 3 VAL B 424 GLN B 426 -1 O TYR B 425 N VAL B 418 SHEET 1 AB6 7 GLU C 327 ARG C 329 0 SHEET 2 AB6 7 HIS C 332 ASP C 336 -1 O PHE C 334 N GLU C 327 SHEET 3 AB6 7 SER C 29 ARG C 40 1 N VAL C 38 O CYS C 335 SHEET 4 AB6 7 VAL C 278 ALA C 288 -1 O THR C 281 N SER C 37 SHEET 5 AB6 7 GLY C 308 ASN C 313 -1 O TYR C 310 N TRP C 284 SHEET 6 AB6 7 SER C 316 TYR C 320 -1 O SER C 316 N ASN C 313 SHEET 7 AB6 7 ILE C 341 VAL C 343 -1 O ILE C 341 N TYR C 319 SHEET 1 AB7 5 GLU C 327 ARG C 329 0 SHEET 2 AB7 5 HIS C 332 ASP C 336 -1 O PHE C 334 N GLU C 327 SHEET 3 AB7 5 SER C 29 ARG C 40 1 N VAL C 38 O CYS C 335 SHEET 4 AB7 5 LYS C 20 LEU C 24 -1 N LEU C 24 O SER C 29 SHEET 5 AB7 5 GLU C 433 ILE C 437 1 O HIS C 435 N TYR C 23 SHEET 1 AB8 5 GLU C 146 THR C 150 0 SHEET 2 AB8 5 ARG C 156 VAL C 162 -1 O VAL C 157 N SER C 149 SHEET 3 AB8 5 TYR C 44 GLU C 51 1 N VAL C 47 O THR C 160 SHEET 4 AB8 5 SER C 266 LEU C 273 -1 O TYR C 269 N PHE C 48 SHEET 5 AB8 5 PHE C 256 TYR C 263 -1 N ILE C 258 O MET C 270 SHEET 1 AB9 2 GLU C 294 LYS C 295 0 SHEET 2 AB9 2 ASN C 298 TYR C 299 -1 O ASN C 298 N LYS C 295 SHEET 1 AC1 3 CYS C 301 ARG C 304 0 SHEET 2 AC1 3 LYS C 362 GLY C 366 -1 O SER C 364 N LEU C 303 SHEET 3 AC1 3 GLN C 455 ALA C 459 -1 O VAL C 458 N VAL C 363 SHEET 1 AC2 3 MET C 372 LEU C 375 0 SHEET 2 AC2 3 GLY C 379 CYS C 384 -1 O ALA C 383 N MET C 372 SHEET 3 AC2 3 GLY C 406 THR C 411 -1 O SER C 408 N VAL C 382 SHEET 1 AC3 3 SER C 391 GLY C 393 0 SHEET 2 AC3 3 THR C 417 THR C 419 -1 O THR C 419 N SER C 391 SHEET 3 AC3 3 VAL C 424 GLN C 426 -1 O TYR C 425 N VAL C 418 SHEET 1 AC4 2 GLN D 3 LEU D 4 0 SHEET 2 AC4 2 VAL D 24 SER D 25 -1 O SER D 25 N GLN D 3 SHEET 1 AC5 3 LEU D 18 THR D 21 0 SHEET 2 AC5 3 GLN D 79 LEU D 84 -1 O LEU D 84 N LEU D 18 SHEET 3 AC5 3 SER D 72 ASP D 74 -1 N ASP D 74 O GLN D 79 SHEET 1 AC6 5 THR D 59 TYR D 61 0 SHEET 2 AC6 5 GLU D 48 VAL D 53 -1 N HIS D 52 O TYR D 60 SHEET 3 AC6 5 TRP D 36 GLN D 41 -1 N ARG D 40 O GLU D 48 SHEET 4 AC6 5 VAL D 94 GLU D 100 -1 O TYR D 96 N ILE D 39 SHEET 5 AC6 5 PHE D 108 TRP D 111 -1 O ASP D 109 N ARG D 99 SHEET 1 AC7 6 SER G 9 ALA G 12 0 SHEET 2 AC7 6 THR G 102 MET G 106 1 O GLU G 105 N LEU G 10 SHEET 3 AC7 6 THR G 84 GLN G 89 -1 N TYR G 85 O THR G 102 SHEET 4 AC7 6 LEU G 32 GLN G 37 -1 N GLN G 37 O THR G 84 SHEET 5 AC7 6 ARG G 44 TYR G 48 -1 O ILE G 47 N TRP G 34 SHEET 6 AC7 6 SER G 52 LEU G 53 -1 O SER G 52 N TYR G 48 SHEET 1 AC8 3 VAL G 18 ILE G 20 0 SHEET 2 AC8 3 ALA G 71 ILE G 74 -1 O ILE G 74 N VAL G 18 SHEET 3 AC8 3 PHE G 61 SER G 64 -1 N ARG G 62 O THR G 73 SHEET 1 AC9 2 GLN E 3 LEU E 4 0 SHEET 2 AC9 2 VAL E 24 SER E 25 -1 O SER E 25 N GLN E 3 SHEET 1 AD1 3 LEU E 18 THR E 21 0 SHEET 2 AD1 3 GLN E 79 LEU E 84 -1 O LEU E 84 N LEU E 18 SHEET 3 AD1 3 SER E 72 ASP E 74 -1 N ASP E 74 O GLN E 79 SHEET 1 AD2 5 THR E 59 TYR E 61 0 SHEET 2 AD2 5 GLU E 48 VAL E 53 -1 N HIS E 52 O TYR E 60 SHEET 3 AD2 5 TRP E 36 GLN E 41 -1 N ARG E 40 O GLU E 48 SHEET 4 AD2 5 VAL E 94 GLU E 100 -1 O TYR E 96 N ILE E 39 SHEET 5 AD2 5 PHE E 108 TRP E 111 -1 O ASP E 109 N ARG E 99 SHEET 1 AD3 6 SER H 9 ALA H 12 0 SHEET 2 AD3 6 THR H 102 MET H 106 1 O GLU H 105 N LEU H 10 SHEET 3 AD3 6 THR H 84 GLN H 89 -1 N TYR H 85 O THR H 102 SHEET 4 AD3 6 LEU H 32 GLN H 37 -1 N GLN H 37 O THR H 84 SHEET 5 AD3 6 ARG H 44 TYR H 48 -1 O ILE H 47 N TRP H 34 SHEET 6 AD3 6 SER H 52 LEU H 53 -1 O SER H 52 N TYR H 48 SHEET 1 AD4 3 VAL H 18 ILE H 20 0 SHEET 2 AD4 3 ALA H 71 ILE H 74 -1 O ILE H 74 N VAL H 18 SHEET 3 AD4 3 PHE H 61 SER H 64 -1 N ARG H 62 O THR H 73 SHEET 1 AD5 2 GLN F 3 LEU F 4 0 SHEET 2 AD5 2 VAL F 24 SER F 25 -1 O SER F 25 N GLN F 3 SHEET 1 AD6 3 LEU F 18 THR F 21 0 SHEET 2 AD6 3 GLN F 79 LEU F 84 -1 O LEU F 84 N LEU F 18 SHEET 3 AD6 3 SER F 72 ASP F 74 -1 N ASP F 74 O GLN F 79 SHEET 1 AD7 5 THR F 59 TYR F 61 0 SHEET 2 AD7 5 GLU F 48 VAL F 53 -1 N HIS F 52 O TYR F 60 SHEET 3 AD7 5 TRP F 36 GLN F 41 -1 N ARG F 40 O GLU F 48 SHEET 4 AD7 5 VAL F 94 GLU F 100 -1 O TYR F 96 N ILE F 39 SHEET 5 AD7 5 PHE F 108 TRP F 111 -1 O ASP F 109 N ARG F 99 SHEET 1 AD8 6 SER I 9 ALA I 12 0 SHEET 2 AD8 6 THR I 102 MET I 106 1 O GLU I 105 N LEU I 10 SHEET 3 AD8 6 THR I 84 GLN I 89 -1 N TYR I 85 O THR I 102 SHEET 4 AD8 6 LEU I 32 GLN I 37 -1 N GLN I 37 O THR I 84 SHEET 5 AD8 6 ARG I 44 TYR I 48 -1 O ILE I 47 N TRP I 34 SHEET 6 AD8 6 SER I 52 LEU I 53 -1 O SER I 52 N TYR I 48 SHEET 1 AD9 3 VAL I 18 ILE I 20 0 SHEET 2 AD9 3 ALA I 71 ILE I 74 -1 O ILE I 74 N VAL I 18 SHEET 3 AD9 3 PHE I 61 SER I 64 -1 N ARG I 62 O THR I 73 SSBOND 1 CYS A 28 CYS A 407 1555 1555 2.03 SSBOND 2 CYS A 60 CYS A 182 1555 1555 2.03 SSBOND 3 CYS A 84 CYS C 249 1555 1555 2.02 SSBOND 4 CYS A 110 CYS A 322 1555 1555 2.04 SSBOND 5 CYS A 127 CYS A 153 1555 1555 2.03 SSBOND 6 CYS A 140 CYS A 147 1555 1555 2.09 SSBOND 7 CYS A 249 CYS B 84 1555 1555 2.03 SSBOND 8 CYS A 283 CYS A 311 1555 1555 2.03 SSBOND 9 CYS A 292 CYS A 301 1555 1555 2.03 SSBOND 10 CYS A 326 CYS A 335 1555 1555 2.03 SSBOND 11 CYS A 350 CYS A 361 1555 1555 2.03 SSBOND 12 CYS A 365 CYS A 463 1555 1555 2.03 SSBOND 13 CYS A 384 CYS A 390 1555 1555 2.03 SSBOND 14 CYS B 28 CYS B 407 1555 1555 2.03 SSBOND 15 CYS B 60 CYS B 182 1555 1555 2.03 SSBOND 16 CYS B 110 CYS B 322 1555 1555 2.04 SSBOND 17 CYS B 127 CYS B 153 1555 1555 2.03 SSBOND 18 CYS B 140 CYS B 147 1555 1555 2.09 SSBOND 19 CYS B 249 CYS C 84 1555 1555 2.06 SSBOND 20 CYS B 283 CYS B 311 1555 1555 2.03 SSBOND 21 CYS B 292 CYS B 301 1555 1555 2.03 SSBOND 22 CYS B 326 CYS B 335 1555 1555 2.03 SSBOND 23 CYS B 350 CYS B 361 1555 1555 2.03 SSBOND 24 CYS B 365 CYS B 463 1555 1555 2.03 SSBOND 25 CYS B 384 CYS B 390 1555 1555 2.03 SSBOND 26 CYS C 28 CYS C 407 1555 1555 2.03 SSBOND 27 CYS C 60 CYS C 182 1555 1555 2.03 SSBOND 28 CYS C 110 CYS C 322 1555 1555 2.04 SSBOND 29 CYS C 127 CYS C 153 1555 1555 2.03 SSBOND 30 CYS C 140 CYS C 147 1555 1555 2.09 SSBOND 31 CYS C 283 CYS C 311 1555 1555 2.03 SSBOND 32 CYS C 292 CYS C 301 1555 1555 2.03 SSBOND 33 CYS C 326 CYS C 335 1555 1555 2.03 SSBOND 34 CYS C 350 CYS C 361 1555 1555 2.03 SSBOND 35 CYS C 365 CYS C 463 1555 1555 2.03 SSBOND 36 CYS C 384 CYS C 390 1555 1555 2.03 SSBOND 37 CYS D 22 CYS D 97 1555 1555 2.03 SSBOND 38 CYS G 22 CYS G 87 1555 1555 2.03 SSBOND 39 CYS E 22 CYS E 97 1555 1555 2.03 SSBOND 40 CYS H 22 CYS H 87 1555 1555 2.03 SSBOND 41 CYS F 22 CYS F 97 1555 1555 2.03 SSBOND 42 CYS I 22 CYS I 87 1555 1555 2.03 LINK ND2 ASN A 57 C1 NAG A 602 1555 1555 1.45 LINK ND2 ASN A 353 C1 NAG A 601 1555 1555 1.44 LINK ND2 ASN B 57 C1 NAG B 602 1555 1555 1.45 LINK ND2 ASN B 353 C1 NAG B 601 1555 1555 1.44 LINK ND2 ASN C 57 C1 NAG C 602 1555 1555 1.45 LINK ND2 ASN C 353 C1 NAG C 601 1555 1555 1.44 CISPEP 1 PHE A 451 PRO A 452 0 -5.82 CISPEP 2 PHE B 451 PRO B 452 0 -5.68 CISPEP 3 PHE C 451 PRO C 452 0 -5.79 CISPEP 4 PRO G 93 PRO G 94 0 -2.37 CISPEP 5 PRO H 93 PRO H 94 0 -2.37 CISPEP 6 PRO I 93 PRO I 94 0 -2.37 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