HEADER VIRAL PROTEIN/IMMUNE SYSTEM 14-APR-22 7UPA TITLE PREFUSION-STABILIZED NIPAH VIRUS FUSION PROTEIN COMPLEXED WITH FAB 1H8 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB 1H8 HEAVY CHAIN; COMPND 3 CHAIN: H, B, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB 1H8 LIGHT CHAIN; COMPND 7 CHAIN: L, E, F; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: FUSION GLYCOPROTEIN F0; COMPND 11 CHAIN: A, D, G; COMPND 12 SYNONYM: PROTEIN F; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_TAXID: 10090; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: NIPAH HENIPAVIRUS; SOURCE 13 ORGANISM_TAXID: 121791; SOURCE 14 EXPRESSION_SYSTEM: NIPAH HENIPAVIRUS; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 121791 KEYWDS HENIPAVIRUS, NIPAH VIRUS, NIV, F, FUSION, PREFUSION, PREF, PRE-F, KEYWDS 2 NEUTRALIZING ANTIBODY, FAB, VIRAL PROTEIN, VIRAL PROTEIN-IMMUNE KEYWDS 3 SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR P.O.BYRNE,J.S.MCLELLAN JRNL AUTH P.O.BYRNE,J.S.MCLELLAN JRNL TITL PREFUSION-STABILIZED NIPAH VIRUS FUSION PROTEIN COMPLEXED JRNL TITL 2 WITH FAB 1H8 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : SERIALEM 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) : 2.500 REMARK 3 NUMBER OF PARTICLES : 305954 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 7UPA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000264570. 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 : PREFUSION-STABILIZED NIPAH REMARK 245 VIRUS FUSION PROTEIN COMPLEXED REMARK 245 WITH FAB 1H8 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 : 8.00 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 : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1500.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00 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) : 80.00 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: H, L, A, D, G, B, E, C, F 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 H -18 REMARK 465 GLU H -17 REMARK 465 PHE H -16 REMARK 465 GLY H -15 REMARK 465 LEU H -14 REMARK 465 SER H -13 REMARK 465 TRP H -12 REMARK 465 ILE H -11 REMARK 465 PHE H -10 REMARK 465 LEU H -9 REMARK 465 ALA H -8 REMARK 465 ALA H -7 REMARK 465 ILE H -6 REMARK 465 LEU H -5 REMARK 465 LYS H -4 REMARK 465 GLY H -3 REMARK 465 VAL H -2 REMARK 465 GLN H -1 REMARK 465 CYS H 0 REMARK 465 SER H 113 REMARK 465 MET L -18 REMARK 465 GLU L -17 REMARK 465 PHE L -16 REMARK 465 GLY L -15 REMARK 465 LEU L -14 REMARK 465 SER L -13 REMARK 465 TRP L -12 REMARK 465 ILE L -11 REMARK 465 PHE L -10 REMARK 465 LEU L -9 REMARK 465 ALA L -8 REMARK 465 ALA L -7 REMARK 465 ILE L -6 REMARK 465 LEU L -5 REMARK 465 LYS L -4 REMARK 465 GLY L -3 REMARK 465 VAL L -2 REMARK 465 GLN L -1 REMARK 465 CYS L 0 REMARK 465 LYS L 107 REMARK 465 MET A 1 REMARK 465 VAL A 2 REMARK 465 VAL A 3 REMARK 465 ILE A 4 REMARK 465 LEU A 5 REMARK 465 ASP A 6 REMARK 465 LYS A 7 REMARK 465 ARG A 8 REMARK 465 CYS A 9 REMARK 465 TYR A 10 REMARK 465 CYS A 11 REMARK 465 ASN A 12 REMARK 465 LEU A 13 REMARK 465 LEU A 14 REMARK 465 ILE A 15 REMARK 465 LEU A 16 REMARK 465 ILE A 17 REMARK 465 LEU A 18 REMARK 465 MET A 19 REMARK 465 ILE A 20 REMARK 465 SER A 21 REMARK 465 GLU A 22 REMARK 465 CYS A 23 REMARK 465 SER A 24 REMARK 465 VAL A 25 REMARK 465 GLY A 26 REMARK 465 ASP A 107 REMARK 465 VAL A 108 REMARK 465 ARG A 109 REMARK 465 LEU A 110 REMARK 465 MET D 1 REMARK 465 VAL D 2 REMARK 465 VAL D 3 REMARK 465 ILE D 4 REMARK 465 LEU D 5 REMARK 465 ASP D 6 REMARK 465 LYS D 7 REMARK 465 ARG D 8 REMARK 465 CYS D 9 REMARK 465 TYR D 10 REMARK 465 CYS D 11 REMARK 465 ASN D 12 REMARK 465 LEU D 13 REMARK 465 LEU D 14 REMARK 465 ILE D 15 REMARK 465 LEU D 16 REMARK 465 ILE D 17 REMARK 465 LEU D 18 REMARK 465 MET D 19 REMARK 465 ILE D 20 REMARK 465 SER D 21 REMARK 465 GLU D 22 REMARK 465 CYS D 23 REMARK 465 SER D 24 REMARK 465 VAL D 25 REMARK 465 GLY D 26 REMARK 465 VAL D 105 REMARK 465 GLY D 106 REMARK 465 ASP D 107 REMARK 465 VAL D 108 REMARK 465 ARG D 109 REMARK 465 LEU D 110 REMARK 465 ALA D 111 REMARK 465 MET G 1 REMARK 465 VAL G 2 REMARK 465 VAL G 3 REMARK 465 ILE G 4 REMARK 465 LEU G 5 REMARK 465 ASP G 6 REMARK 465 LYS G 7 REMARK 465 ARG G 8 REMARK 465 CYS G 9 REMARK 465 TYR G 10 REMARK 465 CYS G 11 REMARK 465 ASN G 12 REMARK 465 LEU G 13 REMARK 465 LEU G 14 REMARK 465 ILE G 15 REMARK 465 LEU G 16 REMARK 465 ILE G 17 REMARK 465 LEU G 18 REMARK 465 MET G 19 REMARK 465 ILE G 20 REMARK 465 SER G 21 REMARK 465 GLU G 22 REMARK 465 CYS G 23 REMARK 465 SER G 24 REMARK 465 VAL G 25 REMARK 465 GLY G 26 REMARK 465 VAL G 105 REMARK 465 GLY G 106 REMARK 465 ASP G 107 REMARK 465 VAL G 108 REMARK 465 ARG G 109 REMARK 465 LEU G 110 REMARK 465 ALA G 111 REMARK 465 MET B -18 REMARK 465 GLU B -17 REMARK 465 PHE B -16 REMARK 465 GLY B -15 REMARK 465 LEU B -14 REMARK 465 SER B -13 REMARK 465 TRP B -12 REMARK 465 ILE B -11 REMARK 465 PHE B -10 REMARK 465 LEU B -9 REMARK 465 ALA B -8 REMARK 465 ALA B -7 REMARK 465 ILE B -6 REMARK 465 LEU B -5 REMARK 465 LYS B -4 REMARK 465 GLY B -3 REMARK 465 VAL B -2 REMARK 465 GLN B -1 REMARK 465 CYS B 0 REMARK 465 SER B 113 REMARK 465 MET E -18 REMARK 465 GLU E -17 REMARK 465 PHE E -16 REMARK 465 GLY E -15 REMARK 465 LEU E -14 REMARK 465 SER E -13 REMARK 465 TRP E -12 REMARK 465 ILE E -11 REMARK 465 PHE E -10 REMARK 465 LEU E -9 REMARK 465 ALA E -8 REMARK 465 ALA E -7 REMARK 465 ILE E -6 REMARK 465 LEU E -5 REMARK 465 LYS E -4 REMARK 465 GLY E -3 REMARK 465 VAL E -2 REMARK 465 GLN E -1 REMARK 465 CYS E 0 REMARK 465 LYS E 107 REMARK 465 MET C -18 REMARK 465 GLU C -17 REMARK 465 PHE C -16 REMARK 465 GLY C -15 REMARK 465 LEU C -14 REMARK 465 SER C -13 REMARK 465 TRP C -12 REMARK 465 ILE C -11 REMARK 465 PHE C -10 REMARK 465 LEU C -9 REMARK 465 ALA C -8 REMARK 465 ALA C -7 REMARK 465 ILE C -6 REMARK 465 LEU C -5 REMARK 465 LYS C -4 REMARK 465 GLY C -3 REMARK 465 VAL C -2 REMARK 465 GLN C -1 REMARK 465 CYS C 0 REMARK 465 SER C 113 REMARK 465 MET F -18 REMARK 465 GLU F -17 REMARK 465 PHE F -16 REMARK 465 GLY F -15 REMARK 465 LEU F -14 REMARK 465 SER F -13 REMARK 465 TRP F -12 REMARK 465 ILE F -11 REMARK 465 PHE F -10 REMARK 465 LEU F -9 REMARK 465 ALA F -8 REMARK 465 ALA F -7 REMARK 465 ILE F -6 REMARK 465 LEU F -5 REMARK 465 LYS F -4 REMARK 465 GLY F -3 REMARK 465 VAL F -2 REMARK 465 GLN F -1 REMARK 465 CYS F 0 REMARK 465 LYS F 107 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ALA H 96 CB REMARK 470 ALA B 96 CB REMARK 470 ALA C 96 CB 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 D 56 CB - CG - OD2 ANGL. DEV. = 5.9 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 ILE H 48 -61.18 -98.81 REMARK 500 THR L 51 -14.82 72.93 REMARK 500 ALA L 84 -167.60 -162.66 REMARK 500 ASN A 51 71.46 56.94 REMARK 500 HIS A 102 -169.15 -161.31 REMARK 500 ASP A 252 37.10 -99.12 REMARK 500 TYR A 274 64.85 60.06 REMARK 500 ASP A 304 -58.20 -122.50 REMARK 500 ASN A 305 16.52 -143.58 REMARK 500 ASN D 51 75.54 53.54 REMARK 500 GLU D 163 -60.70 -93.61 REMARK 500 ASN D 238 76.27 -100.42 REMARK 500 ASP D 252 33.13 -95.83 REMARK 500 TYR D 274 64.38 60.33 REMARK 500 ASP D 304 -102.79 55.39 REMARK 500 ASN D 320 -102.01 54.91 REMARK 500 ASN G 51 74.85 53.97 REMARK 500 ASP G 252 36.72 -99.40 REMARK 500 TYR G 274 63.09 61.17 REMARK 500 ASN G 305 12.59 -144.30 REMARK 500 ASN G 320 -102.81 54.60 REMARK 500 ILE B 48 -60.98 -96.45 REMARK 500 TYR B 98 -63.44 -97.96 REMARK 500 THR E 51 -14.46 72.56 REMARK 500 GLU E 79 -169.06 -119.22 REMARK 500 ALA E 84 -167.50 -162.28 REMARK 500 ILE C 48 -60.92 -97.02 REMARK 500 THR F 51 -14.92 72.92 REMARK 500 ALA F 84 -168.10 -161.99 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-26659 RELATED DB: EMDB REMARK 900 PREFUSION-STABILIZED NIPAH VIRUS FUSION PROTEIN COMPLEXED WITH FAB REMARK 900 1H8 DBREF 7UPA H -18 113 PDB 7UPA 7UPA -18 113 DBREF 7UPA L -18 107 PDB 7UPA 7UPA -18 107 DBREF 7UPA A 1 480 UNP Q9IH63 FUS_NIPAV 1 480 DBREF 7UPA D 1 480 UNP Q9IH63 FUS_NIPAV 1 480 DBREF 7UPA G 1 480 UNP Q9IH63 FUS_NIPAV 1 480 DBREF 7UPA B -18 113 PDB 7UPA 7UPA -18 113 DBREF 7UPA E -18 107 PDB 7UPA 7UPA -18 107 DBREF 7UPA C -18 113 PDB 7UPA 7UPA -18 113 DBREF 7UPA F -18 107 PDB 7UPA 7UPA -18 107 SEQADV 7UPA CYS A 104 UNP Q9IH63 LEU 104 CONFLICT SEQADV 7UPA CYS A 114 UNP Q9IH63 ILE 114 CONFLICT SEQADV 7UPA PHE A 172 UNP Q9IH63 LEU 172 CONFLICT SEQADV 7UPA PRO A 191 UNP Q9IH63 SER 191 CONFLICT SEQADV 7UPA CYS D 104 UNP Q9IH63 LEU 104 CONFLICT SEQADV 7UPA CYS D 114 UNP Q9IH63 ILE 114 CONFLICT SEQADV 7UPA PHE D 172 UNP Q9IH63 LEU 172 CONFLICT SEQADV 7UPA PRO D 191 UNP Q9IH63 SER 191 CONFLICT SEQADV 7UPA CYS G 104 UNP Q9IH63 LEU 104 CONFLICT SEQADV 7UPA CYS G 114 UNP Q9IH63 ILE 114 CONFLICT SEQADV 7UPA PHE G 172 UNP Q9IH63 LEU 172 CONFLICT SEQADV 7UPA PRO G 191 UNP Q9IH63 SER 191 CONFLICT SEQRES 1 H 138 MET GLU PHE GLY LEU SER TRP ILE PHE LEU ALA ALA ILE SEQRES 2 H 138 LEU LYS GLY VAL GLN CYS GLU VAL GLN LEU GLN GLN SER SEQRES 3 H 138 GLY PRO GLU LEU VAL LYS PRO GLY ALA SER VAL LYS ILE SEQRES 4 H 138 SER CYS LYS ALA SER GLY TYR SER PHE THR GLY TYR THR SEQRES 5 H 138 MET ASN TRP VAL LYS GLN SER HIS GLY LYS ASN LEU GLU SEQRES 6 H 138 TRP ILE GLY LEU ILE ASN PRO PHE ILE GLY GLY THR ARG SEQRES 7 H 138 TYR ASN GLN LYS PHE LYS GLY LYS ALA THR LEU THR VAL SEQRES 8 H 138 ASP LYS SER SER ARG THR ALA TYR MET GLU LEU LEU SER SEQRES 9 H 138 LEU THR SER GLU ASP SER ALA VAL TYR TYR CYS ALA ARG SEQRES 10 H 138 GLU ALA ASP TYR ASP TRP TYR PHE ASP VAL TRP GLY ALA SEQRES 11 H 138 GLY THR THR VAL THR VAL SER SER SEQRES 1 L 126 MET GLU PHE GLY LEU SER TRP ILE PHE LEU ALA ALA ILE SEQRES 2 L 126 LEU LYS GLY VAL GLN CYS ASP ILE GLN MET THR GLN THR SEQRES 3 L 126 THR SER SER LEU SER ALA SER LEU GLY ASP ARG VAL THR SEQRES 4 L 126 ILE SER CYS ARG ALA SER GLN ASP ILE SER ASN TYR LEU SEQRES 5 L 126 HIS TRP TYR GLN GLN LYS PRO ASP GLY THR VAL ASN LEU SEQRES 6 L 126 LEU ILE PHE TYR THR SER ARG LEU HIS SER GLY VAL PRO SEQRES 7 L 126 SER ARG PHE SER GLY SER GLY SER GLY THR ASP TYR SER SEQRES 8 L 126 LEU THR ILE SER ASN LEU GLU GLN GLU ASP ILE ALA THR SEQRES 9 L 126 TYR PHE CYS GLN GLN GLY ASN THR LEU PRO ARG THR PHE SEQRES 10 L 126 GLY GLY GLY THR LYS LEU GLU ILE LYS SEQRES 1 A 480 MET VAL VAL ILE LEU ASP LYS ARG CYS TYR CYS ASN LEU SEQRES 2 A 480 LEU ILE LEU ILE LEU MET ILE SER GLU CYS SER VAL GLY SEQRES 3 A 480 ILE LEU HIS TYR GLU LYS LEU SER LYS ILE GLY LEU VAL SEQRES 4 A 480 LYS GLY VAL THR ARG LYS TYR LYS ILE LYS SER ASN PRO SEQRES 5 A 480 LEU THR LYS ASP ILE VAL ILE LYS MET ILE PRO ASN VAL SEQRES 6 A 480 SER ASN MET SER GLN CYS THR GLY SER VAL MET GLU ASN SEQRES 7 A 480 TYR LYS THR ARG LEU ASN GLY ILE LEU THR PRO ILE LYS SEQRES 8 A 480 GLY ALA LEU GLU ILE TYR LYS ASN ASN THR HIS ASP CYS SEQRES 9 A 480 VAL GLY ASP VAL ARG LEU ALA GLY VAL CYS MET ALA GLY SEQRES 10 A 480 VAL ALA ILE GLY ILE ALA THR ALA ALA GLN ILE THR ALA SEQRES 11 A 480 GLY VAL ALA LEU TYR GLU ALA MET LYS ASN ALA ASP ASN SEQRES 12 A 480 ILE ASN LYS LEU LYS SER SER ILE GLU SER THR ASN GLU SEQRES 13 A 480 ALA VAL VAL LYS LEU GLN GLU THR ALA GLU LYS THR VAL SEQRES 14 A 480 TYR VAL PHE THR ALA LEU GLN ASP TYR ILE ASN THR ASN SEQRES 15 A 480 LEU VAL PRO THR ILE ASP LYS ILE PRO CYS LYS GLN THR SEQRES 16 A 480 GLU LEU SER LEU ASP LEU ALA LEU SER LYS TYR LEU SER SEQRES 17 A 480 ASP LEU LEU PHE VAL PHE GLY PRO ASN LEU GLN ASP PRO SEQRES 18 A 480 VAL SER ASN SER MET THR ILE GLN ALA ILE SER GLN ALA SEQRES 19 A 480 PHE GLY GLY ASN TYR GLU THR LEU LEU ARG THR LEU GLY SEQRES 20 A 480 TYR ALA THR GLU ASP PHE ASP ASP LEU LEU GLU SER ASP SEQRES 21 A 480 SER ILE THR GLY GLN ILE ILE TYR VAL ASP LEU SER SER SEQRES 22 A 480 TYR TYR ILE ILE VAL ARG VAL TYR PHE PRO ILE LEU THR SEQRES 23 A 480 GLU ILE GLN GLN ALA TYR ILE GLN GLU LEU LEU PRO VAL SEQRES 24 A 480 SER PHE ASN ASN ASP ASN SER GLU TRP ILE SER ILE VAL SEQRES 25 A 480 PRO ASN PHE ILE LEU VAL ARG ASN THR LEU ILE SER ASN SEQRES 26 A 480 ILE GLU ILE GLY PHE CYS LEU ILE THR LYS ARG SER VAL SEQRES 27 A 480 ILE CYS ASN GLN ASP TYR ALA THR PRO MET THR ASN ASN SEQRES 28 A 480 MET ARG GLU CYS LEU THR GLY SER THR GLU LYS CYS PRO SEQRES 29 A 480 ARG GLU LEU VAL VAL SER SER HIS VAL PRO ARG PHE ALA SEQRES 30 A 480 LEU SER ASN GLY VAL LEU PHE ALA ASN CYS ILE SER VAL SEQRES 31 A 480 THR CYS GLN CYS GLN THR THR GLY ARG ALA ILE SER GLN SEQRES 32 A 480 SER GLY GLU GLN THR LEU LEU MET ILE ASP ASN THR THR SEQRES 33 A 480 CYS PRO THR ALA VAL LEU GLY ASN VAL ILE ILE SER LEU SEQRES 34 A 480 GLY LYS TYR LEU GLY SER VAL ASN TYR ASN SER GLU GLY SEQRES 35 A 480 ILE ALA ILE GLY PRO PRO VAL PHE THR ASP LYS VAL ASP SEQRES 36 A 480 ILE SER SER GLN ILE SER SER MET ASN GLN SER LEU GLN SEQRES 37 A 480 GLN SER LYS ASP TYR ILE LYS GLU ALA GLN ARG LEU SEQRES 1 D 480 MET VAL VAL ILE LEU ASP LYS ARG CYS TYR CYS ASN LEU SEQRES 2 D 480 LEU ILE LEU ILE LEU MET ILE SER GLU CYS SER VAL GLY SEQRES 3 D 480 ILE LEU HIS TYR GLU LYS LEU SER LYS ILE GLY LEU VAL SEQRES 4 D 480 LYS GLY VAL THR ARG LYS TYR LYS ILE LYS SER ASN PRO SEQRES 5 D 480 LEU THR LYS ASP ILE VAL ILE LYS MET ILE PRO ASN VAL SEQRES 6 D 480 SER ASN MET SER GLN CYS THR GLY SER VAL MET GLU ASN SEQRES 7 D 480 TYR LYS THR ARG LEU ASN GLY ILE LEU THR PRO ILE LYS SEQRES 8 D 480 GLY ALA LEU GLU ILE TYR LYS ASN ASN THR HIS ASP CYS SEQRES 9 D 480 VAL GLY ASP VAL ARG LEU ALA GLY VAL CYS MET ALA GLY SEQRES 10 D 480 VAL ALA ILE GLY ILE ALA THR ALA ALA GLN ILE THR ALA SEQRES 11 D 480 GLY VAL ALA LEU TYR GLU ALA MET LYS ASN ALA ASP ASN SEQRES 12 D 480 ILE ASN LYS LEU LYS SER SER ILE GLU SER THR ASN GLU SEQRES 13 D 480 ALA VAL VAL LYS LEU GLN GLU THR ALA GLU LYS THR VAL SEQRES 14 D 480 TYR VAL PHE THR ALA LEU GLN ASP TYR ILE ASN THR ASN SEQRES 15 D 480 LEU VAL PRO THR ILE ASP LYS ILE PRO CYS LYS GLN THR SEQRES 16 D 480 GLU LEU SER LEU ASP LEU ALA LEU SER LYS TYR LEU SER SEQRES 17 D 480 ASP LEU LEU PHE VAL PHE GLY PRO ASN LEU GLN ASP PRO SEQRES 18 D 480 VAL SER ASN SER MET THR ILE GLN ALA ILE SER GLN ALA SEQRES 19 D 480 PHE GLY GLY ASN TYR GLU THR LEU LEU ARG THR LEU GLY SEQRES 20 D 480 TYR ALA THR GLU ASP PHE ASP ASP LEU LEU GLU SER ASP SEQRES 21 D 480 SER ILE THR GLY GLN ILE ILE TYR VAL ASP LEU SER SER SEQRES 22 D 480 TYR TYR ILE ILE VAL ARG VAL TYR PHE PRO ILE LEU THR SEQRES 23 D 480 GLU ILE GLN GLN ALA TYR ILE GLN GLU LEU LEU PRO VAL SEQRES 24 D 480 SER PHE ASN ASN ASP ASN SER GLU TRP ILE SER ILE VAL SEQRES 25 D 480 PRO ASN PHE ILE LEU VAL ARG ASN THR LEU ILE SER ASN SEQRES 26 D 480 ILE GLU ILE GLY PHE CYS LEU ILE THR LYS ARG SER VAL SEQRES 27 D 480 ILE CYS ASN GLN ASP TYR ALA THR PRO MET THR ASN ASN SEQRES 28 D 480 MET ARG GLU CYS LEU THR GLY SER THR GLU LYS CYS PRO SEQRES 29 D 480 ARG GLU LEU VAL VAL SER SER HIS VAL PRO ARG PHE ALA SEQRES 30 D 480 LEU SER ASN GLY VAL LEU PHE ALA ASN CYS ILE SER VAL SEQRES 31 D 480 THR CYS GLN CYS GLN THR THR GLY ARG ALA ILE SER GLN SEQRES 32 D 480 SER GLY GLU GLN THR LEU LEU MET ILE ASP ASN THR THR SEQRES 33 D 480 CYS PRO THR ALA VAL LEU GLY ASN VAL ILE ILE SER LEU SEQRES 34 D 480 GLY LYS TYR LEU GLY SER VAL ASN TYR ASN SER GLU GLY SEQRES 35 D 480 ILE ALA ILE GLY PRO PRO VAL PHE THR ASP LYS VAL ASP SEQRES 36 D 480 ILE SER SER GLN ILE SER SER MET ASN GLN SER LEU GLN SEQRES 37 D 480 GLN SER LYS ASP TYR ILE LYS GLU ALA GLN ARG LEU SEQRES 1 G 480 MET VAL VAL ILE LEU ASP LYS ARG CYS TYR CYS ASN LEU SEQRES 2 G 480 LEU ILE LEU ILE LEU MET ILE SER GLU CYS SER VAL GLY SEQRES 3 G 480 ILE LEU HIS TYR GLU LYS LEU SER LYS ILE GLY LEU VAL SEQRES 4 G 480 LYS GLY VAL THR ARG LYS TYR LYS ILE LYS SER ASN PRO SEQRES 5 G 480 LEU THR LYS ASP ILE VAL ILE LYS MET ILE PRO ASN VAL SEQRES 6 G 480 SER ASN MET SER GLN CYS THR GLY SER VAL MET GLU ASN SEQRES 7 G 480 TYR LYS THR ARG LEU ASN GLY ILE LEU THR PRO ILE LYS SEQRES 8 G 480 GLY ALA LEU GLU ILE TYR LYS ASN ASN THR HIS ASP CYS SEQRES 9 G 480 VAL GLY ASP VAL ARG LEU ALA GLY VAL CYS MET ALA GLY SEQRES 10 G 480 VAL ALA ILE GLY ILE ALA THR ALA ALA GLN ILE THR ALA SEQRES 11 G 480 GLY VAL ALA LEU TYR GLU ALA MET LYS ASN ALA ASP ASN SEQRES 12 G 480 ILE ASN LYS LEU LYS SER SER ILE GLU SER THR ASN GLU SEQRES 13 G 480 ALA VAL VAL LYS LEU GLN GLU THR ALA GLU LYS THR VAL SEQRES 14 G 480 TYR VAL PHE THR ALA LEU GLN ASP TYR ILE ASN THR ASN SEQRES 15 G 480 LEU VAL PRO THR ILE ASP LYS ILE PRO CYS LYS GLN THR SEQRES 16 G 480 GLU LEU SER LEU ASP LEU ALA LEU SER LYS TYR LEU SER SEQRES 17 G 480 ASP LEU LEU PHE VAL PHE GLY PRO ASN LEU GLN ASP PRO SEQRES 18 G 480 VAL SER ASN SER MET THR ILE GLN ALA ILE SER GLN ALA SEQRES 19 G 480 PHE GLY GLY ASN TYR GLU THR LEU LEU ARG THR LEU GLY SEQRES 20 G 480 TYR ALA THR GLU ASP PHE ASP ASP LEU LEU GLU SER ASP SEQRES 21 G 480 SER ILE THR GLY GLN ILE ILE TYR VAL ASP LEU SER SER SEQRES 22 G 480 TYR TYR ILE ILE VAL ARG VAL TYR PHE PRO ILE LEU THR SEQRES 23 G 480 GLU ILE GLN GLN ALA TYR ILE GLN GLU LEU LEU PRO VAL SEQRES 24 G 480 SER PHE ASN ASN ASP ASN SER GLU TRP ILE SER ILE VAL SEQRES 25 G 480 PRO ASN PHE ILE LEU VAL ARG ASN THR LEU ILE SER ASN SEQRES 26 G 480 ILE GLU ILE GLY PHE CYS LEU ILE THR LYS ARG SER VAL SEQRES 27 G 480 ILE CYS ASN GLN ASP TYR ALA THR PRO MET THR ASN ASN SEQRES 28 G 480 MET ARG GLU CYS LEU THR GLY SER THR GLU LYS CYS PRO SEQRES 29 G 480 ARG GLU LEU VAL VAL SER SER HIS VAL PRO ARG PHE ALA SEQRES 30 G 480 LEU SER ASN GLY VAL LEU PHE ALA ASN CYS ILE SER VAL SEQRES 31 G 480 THR CYS GLN CYS GLN THR THR GLY ARG ALA ILE SER GLN SEQRES 32 G 480 SER GLY GLU GLN THR LEU LEU MET ILE ASP ASN THR THR SEQRES 33 G 480 CYS PRO THR ALA VAL LEU GLY ASN VAL ILE ILE SER LEU SEQRES 34 G 480 GLY LYS TYR LEU GLY SER VAL ASN TYR ASN SER GLU GLY SEQRES 35 G 480 ILE ALA ILE GLY PRO PRO VAL PHE THR ASP LYS VAL ASP SEQRES 36 G 480 ILE SER SER GLN ILE SER SER MET ASN GLN SER LEU GLN SEQRES 37 G 480 GLN SER LYS ASP TYR ILE LYS GLU ALA GLN ARG LEU SEQRES 1 B 138 MET GLU PHE GLY LEU SER TRP ILE PHE LEU ALA ALA ILE SEQRES 2 B 138 LEU LYS GLY VAL GLN CYS GLU VAL GLN LEU GLN GLN SER SEQRES 3 B 138 GLY PRO GLU LEU VAL LYS PRO GLY ALA SER VAL LYS ILE SEQRES 4 B 138 SER CYS LYS ALA SER GLY TYR SER PHE THR GLY TYR THR SEQRES 5 B 138 MET ASN TRP VAL LYS GLN SER HIS GLY LYS ASN LEU GLU SEQRES 6 B 138 TRP ILE GLY LEU ILE ASN PRO PHE ILE GLY GLY THR ARG SEQRES 7 B 138 TYR ASN GLN LYS PHE LYS GLY LYS ALA THR LEU THR VAL SEQRES 8 B 138 ASP LYS SER SER ARG THR ALA TYR MET GLU LEU LEU SER SEQRES 9 B 138 LEU THR SER GLU ASP SER ALA VAL TYR TYR CYS ALA ARG SEQRES 10 B 138 GLU ALA ASP TYR ASP TRP TYR PHE ASP VAL TRP GLY ALA SEQRES 11 B 138 GLY THR THR VAL THR VAL SER SER SEQRES 1 E 126 MET GLU PHE GLY LEU SER TRP ILE PHE LEU ALA ALA ILE SEQRES 2 E 126 LEU LYS GLY VAL GLN CYS ASP ILE GLN MET THR GLN THR SEQRES 3 E 126 THR SER SER LEU SER ALA SER LEU GLY ASP ARG VAL THR SEQRES 4 E 126 ILE SER CYS ARG ALA SER GLN ASP ILE SER ASN TYR LEU SEQRES 5 E 126 HIS TRP TYR GLN GLN LYS PRO ASP GLY THR VAL ASN LEU SEQRES 6 E 126 LEU ILE PHE TYR THR SER ARG LEU HIS SER GLY VAL PRO SEQRES 7 E 126 SER ARG PHE SER GLY SER GLY SER GLY THR ASP TYR SER SEQRES 8 E 126 LEU THR ILE SER ASN LEU GLU GLN GLU ASP ILE ALA THR SEQRES 9 E 126 TYR PHE CYS GLN GLN GLY ASN THR LEU PRO ARG THR PHE SEQRES 10 E 126 GLY GLY GLY THR LYS LEU GLU ILE LYS SEQRES 1 C 138 MET GLU PHE GLY LEU SER TRP ILE PHE LEU ALA ALA ILE SEQRES 2 C 138 LEU LYS GLY VAL GLN CYS GLU VAL GLN LEU GLN GLN SER SEQRES 3 C 138 GLY PRO GLU LEU VAL LYS PRO GLY ALA SER VAL LYS ILE SEQRES 4 C 138 SER CYS LYS ALA SER GLY TYR SER PHE THR GLY TYR THR SEQRES 5 C 138 MET ASN TRP VAL LYS GLN SER HIS GLY LYS ASN LEU GLU SEQRES 6 C 138 TRP ILE GLY LEU ILE ASN PRO PHE ILE GLY GLY THR ARG SEQRES 7 C 138 TYR ASN GLN LYS PHE LYS GLY LYS ALA THR LEU THR VAL SEQRES 8 C 138 ASP LYS SER SER ARG THR ALA TYR MET GLU LEU LEU SER SEQRES 9 C 138 LEU THR SER GLU ASP SER ALA VAL TYR TYR CYS ALA ARG SEQRES 10 C 138 GLU ALA ASP TYR ASP TRP TYR PHE ASP VAL TRP GLY ALA SEQRES 11 C 138 GLY THR THR VAL THR VAL SER SER SEQRES 1 F 126 MET GLU PHE GLY LEU SER TRP ILE PHE LEU ALA ALA ILE SEQRES 2 F 126 LEU LYS GLY VAL GLN CYS ASP ILE GLN MET THR GLN THR SEQRES 3 F 126 THR SER SER LEU SER ALA SER LEU GLY ASP ARG VAL THR SEQRES 4 F 126 ILE SER CYS ARG ALA SER GLN ASP ILE SER ASN TYR LEU SEQRES 5 F 126 HIS TRP TYR GLN GLN LYS PRO ASP GLY THR VAL ASN LEU SEQRES 6 F 126 LEU ILE PHE TYR THR SER ARG LEU HIS SER GLY VAL PRO SEQRES 7 F 126 SER ARG PHE SER GLY SER GLY SER GLY THR ASP TYR SER SEQRES 8 F 126 LEU THR ILE SER ASN LEU GLU GLN GLU ASP ILE ALA THR SEQRES 9 F 126 TYR PHE CYS GLN GLN GLY ASN THR LEU PRO ARG THR PHE SEQRES 10 F 126 GLY GLY GLY THR LYS LEU GLU ILE LYS HET NAG A 501 14 HET NAG A 502 14 HET NAG A 503 14 HET NAG A 504 14 HET NAG D 501 14 HET NAG D 502 14 HET NAG D 503 14 HET NAG D 504 14 HET NAG G 501 14 HET NAG G 502 14 HET NAG G 503 14 HET NAG G 504 14 HETNAM NAG N-ACETYL-D-GLUCOSAMINE FORMUL 10 NAG 12(C8 H15 N O6) HELIX 1 AA1 SER H 28 TYR H 32 5 5 HELIX 2 AA2 GLN H 61 LYS H 64 5 4 HELIX 3 AA3 THR H 83 SER H 87 5 5 HELIX 4 AA4 GLU L 79 ILE L 83 5 5 HELIX 5 AA5 HIS A 29 GLY A 37 1 9 HELIX 6 AA6 MET A 68 THR A 72 5 5 HELIX 7 AA7 SER A 74 ASN A 100 1 27 HELIX 8 AA8 GLY A 117 GLY A 121 1 5 HELIX 9 AA9 ALA A 125 ASN A 145 1 21 HELIX 10 AB1 LEU A 147 SER A 153 1 7 HELIX 11 AB2 LEU A 175 ASN A 182 1 8 HELIX 12 AB3 PRO A 191 GLY A 215 1 25 HELIX 13 AB4 ILE A 228 SER A 232 1 5 HELIX 14 AB5 GLN A 233 GLY A 236 5 4 HELIX 15 AB6 ASN A 238 LEU A 246 1 9 HELIX 16 AB7 ASP A 252 SER A 259 1 8 HELIX 17 AB8 ILE A 328 CYS A 331 5 4 HELIX 18 AB9 THR A 349 THR A 357 1 9 HELIX 19 AC1 SER A 359 CYS A 363 5 5 HELIX 20 AC2 ASN A 437 GLU A 441 5 5 HELIX 21 AC3 ASP A 452 LEU A 480 1 29 HELIX 22 AC4 HIS D 29 GLY D 37 1 9 HELIX 23 AC5 VAL D 65 THR D 72 5 8 HELIX 24 AC6 SER D 74 ASN D 100 1 27 HELIX 25 AC7 GLY D 117 GLY D 121 1 5 HELIX 26 AC8 ALA D 125 ASN D 145 1 21 HELIX 27 AC9 LEU D 147 SER D 153 1 7 HELIX 28 AD1 LEU D 175 ASN D 182 1 8 HELIX 29 AD2 PRO D 191 GLY D 215 1 25 HELIX 30 AD3 ILE D 228 SER D 232 1 5 HELIX 31 AD4 GLN D 233 GLY D 236 5 4 HELIX 32 AD5 ASN D 238 LEU D 246 1 9 HELIX 33 AD6 ASP D 252 SER D 259 1 8 HELIX 34 AD7 ILE D 328 CYS D 331 5 4 HELIX 35 AD8 THR D 349 THR D 357 1 9 HELIX 36 AD9 SER D 359 CYS D 363 5 5 HELIX 37 AE1 ASN D 437 GLU D 441 5 5 HELIX 38 AE2 ASP D 452 LEU D 480 1 29 HELIX 39 AE3 HIS G 29 GLY G 37 1 9 HELIX 40 AE4 VAL G 65 SER G 69 5 5 HELIX 41 AE5 SER G 74 ASN G 99 1 26 HELIX 42 AE6 GLY G 117 GLY G 121 1 5 HELIX 43 AE7 ALA G 125 ASN G 145 1 21 HELIX 44 AE8 LEU G 147 SER G 153 1 7 HELIX 45 AE9 LEU G 175 ASN G 182 1 8 HELIX 46 AF1 PRO G 191 GLY G 215 1 25 HELIX 47 AF2 ILE G 228 SER G 232 1 5 HELIX 48 AF3 GLN G 233 GLY G 236 5 4 HELIX 49 AF4 ASN G 238 LEU G 246 1 9 HELIX 50 AF5 ASP G 252 SER G 259 1 8 HELIX 51 AF6 ILE G 328 CYS G 331 5 4 HELIX 52 AF7 THR G 349 THR G 357 1 9 HELIX 53 AF8 SER G 359 CYS G 363 5 5 HELIX 54 AF9 ASN G 437 GLU G 441 5 5 HELIX 55 AG1 ASP G 452 LEU G 480 1 29 HELIX 56 AG2 SER B 28 TYR B 32 5 5 HELIX 57 AG3 GLN B 61 LYS B 64 5 4 HELIX 58 AG4 THR B 83 SER B 87 5 5 HELIX 59 AG5 GLU E 79 ILE E 83 5 5 HELIX 60 AG6 SER C 28 TYR C 32 5 5 HELIX 61 AG7 GLN C 61 LYS C 64 5 4 HELIX 62 AG8 THR C 83 SER C 87 5 5 HELIX 63 AG9 GLU F 79 ILE F 83 5 5 SHEET 1 AA1 4 GLN H 3 GLN H 6 0 SHEET 2 AA1 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AA1 4 THR H 77 LEU H 82 -1 O MET H 80 N ILE H 20 SHEET 4 AA1 4 ALA H 67 ASP H 72 -1 N THR H 70 O TYR H 79 SHEET 1 AA219 GLU H 10 VAL H 12 0 SHEET 2 AA219 MET H 34 GLN H 39 0 SHEET 3 AA219 LEU H 45 ASN H 52 -1 O GLU H 46 N LYS H 38 SHEET 4 AA219 GLY H 56 TYR H 59 -1 O GLY H 56 N ASN H 52 SHEET 5 AA219 ALA H 88 GLU H 95 -1 O VAL H 89 N GLN H 39 SHEET 6 AA219 PHE H 100B TRP H 103 -1 O VAL H 102 N ARG H 94 SHEET 7 AA219 THR H 107 VAL H 111 -1 O VAL H 109 N ALA H 88 SHEET 8 AA219 LEU A 38 LYS A 60 0 SHEET 9 AA219 VAL A 158 GLN A 162 0 SHEET 10 AA219 THR A 168 THR A 173 -1 O VAL A 169 N LEU A 161 SHEET 11 AA219 MET A 226 THR A 227 0 SHEET 12 AA219 THR A 263 ASP A 270 -1 O GLY A 264 N MET A 226 SHEET 13 AA219 TYR A 275 ILE A 288 -1 O ARG A 279 N GLN A 265 SHEET 14 AA219 ALA A 291 PRO A 298 -1 O LEU A 297 N VAL A 39 SHEET 15 AA219 PHE A 315 ARG A 319 -1 O VAL A 318 N TYR A 292 SHEET 16 AA219 LEU A 322 ILE A 326 -1 O SER A 324 N LEU A 317 SHEET 17 AA219 LEU A 332 ILE A 333 0 SHEET 18 AA219 SER A 337 CYS A 340 -1 O ILE A 339 N LEU A 332 SHEET 19 AA219 ALA A 345 THR A 346 -1 O THR A 346 N ASN A 325 SHEET 1 AA3 4 MET L 4 THR L 5 0 SHEET 2 AA3 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA3 4 ASP L 70 ILE L 75 -1 O ILE L 75 N VAL L 19 SHEET 4 AA3 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AA4 7 SER L 10 SER L 12 0 SHEET 2 AA4 7 LEU L 33 GLN L 38 0 SHEET 3 AA4 7 VAL L 44 PHE L 49 -1 O ILE L 48 N TRP L 35 SHEET 4 AA4 7 ARG L 53 LEU L 54 -1 O ARG L 53 N PHE L 49 SHEET 5 AA4 7 THR L 85 GLN L 90 -1 O THR L 85 N GLN L 38 SHEET 6 AA4 7 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 7 AA4 7 THR L 102 GLU L 105 -1 O THR L 102 N TYR L 86 SHEET 1 AA5 6 THR A 101 HIS A 102 0 SHEET 2 AA5 6 VAL A 113 ALA A 116 -1 O CYS A 114 N HIS A 102 SHEET 3 AA5 6 VAL G 425 SER G 428 1 O ILE G 426 N VAL A 113 SHEET 4 AA5 6 THR G 419 LEU G 422 -1 N ALA G 420 O ILE G 427 SHEET 5 AA5 6 GLN G 393 CYS G 394 -1 N GLN G 393 O VAL G 421 SHEET 6 AA5 6 ARG G 399 ALA G 400 -1 O ARG G 399 N CYS G 394 SHEET 1 AA6 4 ILE A 122 THR A 124 0 SHEET 2 AA6 4 PHE G 376 SER G 379 -1 O LEU G 378 N ALA A 123 SHEET 3 AA6 4 VAL G 382 ALA G 385 -1 O PHE G 384 N ALA G 377 SHEET 4 AA6 4 LEU G 410 ILE G 412 -1 O ILE G 412 N LEU G 383 SHEET 1 AA7 3 PHE A 301 ASN A 302 0 SHEET 2 AA7 3 GLU A 307 SER A 310 -1 O TRP A 308 N PHE A 301 SHEET 3 AA7 3 ARG A 365 LEU A 367 -1 O GLU A 366 N ILE A 309 SHEET 1 AA8 4 LEU A 410 ILE A 412 0 SHEET 2 AA8 4 VAL A 382 ALA A 385 -1 N ALA A 385 O LEU A 410 SHEET 3 AA8 4 PHE A 376 SER A 379 -1 N SER A 379 O VAL A 382 SHEET 4 AA8 4 ILE D 122 THR D 124 -1 O ALA D 123 N LEU A 378 SHEET 1 AA9 5 GLN A 393 CYS A 394 0 SHEET 2 AA9 5 THR A 419 LEU A 422 -1 O VAL A 421 N GLN A 393 SHEET 3 AA9 5 VAL A 425 SER A 428 -1 O ILE A 427 N ALA A 420 SHEET 4 AA9 5 CYS D 114 ALA D 116 1 O MET D 115 N SER A 428 SHEET 5 AA9 5 THR D 101 HIS D 102 -1 N HIS D 102 O CYS D 114 SHEET 1 AB119 LEU D 38 LYS D 60 0 SHEET 2 AB119 VAL D 158 THR D 164 0 SHEET 3 AB119 LYS D 167 THR D 173 -1 O VAL D 171 N VAL D 159 SHEET 4 AB119 MET D 226 THR D 227 0 SHEET 5 AB119 THR D 263 ASP D 270 -1 O GLY D 264 N MET D 226 SHEET 6 AB119 TYR D 275 ILE D 288 -1 O TYR D 275 N ASP D 270 SHEET 7 AB119 ALA D 291 PRO D 298 -1 O LEU D 297 N VAL D 39 SHEET 8 AB119 PHE D 315 ARG D 319 -1 O VAL D 318 N TYR D 292 SHEET 9 AB119 LEU D 322 ILE D 326 -1 O SER D 324 N LEU D 317 SHEET 10 AB119 LEU D 332 ILE D 333 0 SHEET 11 AB119 SER D 337 CYS D 340 -1 O ILE D 339 N LEU D 332 SHEET 12 AB119 ALA D 345 THR D 346 -1 O THR D 346 N ASN D 325 SHEET 13 AB119 GLU C 10 VAL C 12 0 SHEET 14 AB119 MET C 34 GLN C 39 0 SHEET 15 AB119 LEU C 45 ASN C 52 -1 O GLU C 46 N LYS C 38 SHEET 16 AB119 GLY C 56 TYR C 59 -1 O GLY C 56 N ASN C 52 SHEET 17 AB119 ALA C 88 GLU C 95 -1 O VAL C 89 N GLN C 39 SHEET 18 AB119 PHE C 100B TRP C 103 -1 O VAL C 102 N ARG C 94 SHEET 19 AB119 THR C 107 VAL C 111 -1 O VAL C 109 N ALA C 88 SHEET 1 AB2 3 PHE D 301 ASN D 303 0 SHEET 2 AB2 3 SER D 306 SER D 310 -1 O SER D 306 N ASN D 303 SHEET 3 AB2 3 ARG D 365 LEU D 367 -1 O GLU D 366 N ILE D 309 SHEET 1 AB3 4 LEU D 410 ILE D 412 0 SHEET 2 AB3 4 VAL D 382 ALA D 385 -1 N LEU D 383 O ILE D 412 SHEET 3 AB3 4 PHE D 376 SER D 379 -1 N ALA D 377 O PHE D 384 SHEET 4 AB3 4 ILE G 122 THR G 124 -1 O ALA G 123 N LEU D 378 SHEET 1 AB4 6 ARG D 399 ALA D 400 0 SHEET 2 AB4 6 GLN D 393 CYS D 394 -1 N CYS D 394 O ARG D 399 SHEET 3 AB4 6 THR D 419 VAL D 421 -1 O VAL D 421 N GLN D 393 SHEET 4 AB4 6 VAL D 425 SER D 428 -1 O ILE D 427 N ALA D 420 SHEET 5 AB4 6 VAL G 113 ALA G 116 1 O MET G 115 N ILE D 426 SHEET 6 AB4 6 THR G 101 HIS G 102 -1 N HIS G 102 O CYS G 114 SHEET 1 AB519 LEU G 38 LYS G 60 0 SHEET 2 AB519 VAL G 158 GLN G 162 0 SHEET 3 AB519 THR G 168 THR G 173 -1 O VAL G 171 N VAL G 159 SHEET 4 AB519 MET G 226 THR G 227 0 SHEET 5 AB519 THR G 263 ASP G 270 -1 O GLY G 264 N MET G 226 SHEET 6 AB519 TYR G 275 ILE G 288 -1 O TYR G 275 N ASP G 270 SHEET 7 AB519 ALA G 291 PRO G 298 -1 O LEU G 297 N VAL G 39 SHEET 8 AB519 PHE G 315 ARG G 319 -1 O VAL G 318 N TYR G 292 SHEET 9 AB519 LEU G 322 ILE G 326 -1 O SER G 324 N LEU G 317 SHEET 10 AB519 LEU G 332 ILE G 333 0 SHEET 11 AB519 SER G 337 CYS G 340 -1 O ILE G 339 N LEU G 332 SHEET 12 AB519 ALA G 345 THR G 346 -1 O THR G 346 N ASN G 325 SHEET 13 AB519 GLU B 10 VAL B 12 0 SHEET 14 AB519 MET B 34 SER B 40 0 SHEET 15 AB519 ASN B 44 ASN B 52 -1 O GLU B 46 N LYS B 38 SHEET 16 AB519 GLY B 56 TYR B 59 -1 O GLY B 56 N ASN B 52 SHEET 17 AB519 ALA B 88 GLU B 95 -1 O TYR B 91 N VAL B 37 SHEET 18 AB519 PHE B 100B TRP B 103 -1 O VAL B 102 N ARG B 94 SHEET 19 AB519 THR B 107 VAL B 111 -1 O VAL B 109 N ALA B 88 SHEET 1 AB6 3 PHE G 301 ASN G 302 0 SHEET 2 AB6 3 GLU G 307 SER G 310 -1 O TRP G 308 N PHE G 301 SHEET 3 AB6 3 ARG G 365 LEU G 367 -1 O GLU G 366 N ILE G 309 SHEET 1 AB7 4 GLN B 3 GLN B 6 0 SHEET 2 AB7 4 VAL B 18 SER B 25 -1 O LYS B 23 N GLN B 5 SHEET 3 AB7 4 THR B 77 LEU B 82 -1 O MET B 80 N ILE B 20 SHEET 4 AB7 4 ALA B 67 ASP B 72 -1 N THR B 70 O TYR B 79 SHEET 1 AB8 4 MET E 4 THR E 5 0 SHEET 2 AB8 4 VAL E 19 ALA E 25 -1 O ARG E 24 N THR E 5 SHEET 3 AB8 4 ASP E 70 ILE E 75 -1 O ILE E 75 N VAL E 19 SHEET 4 AB8 4 PHE E 62 SER E 67 -1 N SER E 65 O SER E 72 SHEET 1 AB9 6 SER E 10 SER E 12 0 SHEET 2 AB9 6 THR E 102 GLU E 105 1 O LYS E 103 N LEU E 11 SHEET 3 AB9 6 THR E 85 GLN E 90 -1 N TYR E 86 O THR E 102 SHEET 4 AB9 6 LEU E 33 GLN E 38 -1 N GLN E 38 O THR E 85 SHEET 5 AB9 6 VAL E 44 PHE E 49 -1 O ILE E 48 N TRP E 35 SHEET 6 AB9 6 ARG E 53 LEU E 54 -1 O ARG E 53 N PHE E 49 SHEET 1 AC1 4 GLN C 3 GLN C 6 0 SHEET 2 AC1 4 VAL C 18 SER C 25 -1 O LYS C 23 N GLN C 5 SHEET 3 AC1 4 THR C 77 LEU C 82 -1 O ALA C 78 N CYS C 22 SHEET 4 AC1 4 ALA C 67 ASP C 72 -1 N THR C 70 O TYR C 79 SHEET 1 AC2 4 MET F 4 THR F 5 0 SHEET 2 AC2 4 ARG F 18 ALA F 25 -1 O ARG F 24 N THR F 5 SHEET 3 AC2 4 ASP F 70 SER F 76 -1 O ILE F 75 N VAL F 19 SHEET 4 AC2 4 PHE F 62 SER F 67 -1 N SER F 65 O SER F 72 SHEET 1 AC3 7 SER F 10 SER F 12 0 SHEET 2 AC3 7 LEU F 33 GLN F 38 0 SHEET 3 AC3 7 VAL F 44 PHE F 49 -1 O ILE F 48 N TRP F 35 SHEET 4 AC3 7 ARG F 53 LEU F 54 -1 O ARG F 53 N PHE F 49 SHEET 5 AC3 7 THR F 85 GLN F 90 -1 O THR F 85 N GLN F 38 SHEET 6 AC3 7 THR F 97 PHE F 98 -1 O THR F 97 N GLN F 90 SHEET 7 AC3 7 THR F 102 GLU F 105 -1 O THR F 102 N TYR F 86 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 2 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 3 CYS A 71 CYS A 192 1555 1555 2.03 SSBOND 4 CYS A 104 CYS A 114 1555 1555 2.03 SSBOND 5 CYS A 331 CYS A 340 1555 1555 2.03 SSBOND 6 CYS A 355 CYS A 363 1555 1555 2.03 SSBOND 7 CYS A 387 CYS A 392 1555 1555 2.04 SSBOND 8 CYS A 394 CYS A 417 1555 1555 2.03 SSBOND 9 CYS D 71 CYS D 192 1555 1555 2.03 SSBOND 10 CYS D 104 CYS D 114 1555 1555 2.03 SSBOND 11 CYS D 331 CYS D 340 1555 1555 2.03 SSBOND 12 CYS D 355 CYS D 363 1555 1555 2.03 SSBOND 13 CYS D 387 CYS D 392 1555 1555 2.03 SSBOND 14 CYS D 394 CYS D 417 1555 1555 2.03 SSBOND 15 CYS G 71 CYS G 192 1555 1555 2.03 SSBOND 16 CYS G 104 CYS G 114 1555 1555 2.03 SSBOND 17 CYS G 331 CYS G 340 1555 1555 2.03 SSBOND 18 CYS G 355 CYS G 363 1555 1555 2.03 SSBOND 19 CYS G 387 CYS G 392 1555 1555 2.04 SSBOND 20 CYS G 394 CYS G 417 1555 1555 2.03 SSBOND 21 CYS B 22 CYS B 92 1555 1555 2.04 SSBOND 22 CYS E 23 CYS E 88 1555 1555 2.05 SSBOND 23 CYS C 22 CYS C 92 1555 1555 2.04 SSBOND 24 CYS F 23 CYS F 88 1555 1555 2.05 LINK ND2 ASN A 67 C1 NAG A 501 1555 1555 1.45 LINK ND2 ASN A 99 C1 NAG A 502 1555 1555 1.44 LINK ND2 ASN A 414 C1 NAG A 503 1555 1555 1.44 LINK ND2 ASN A 464 C1 NAG A 504 1555 1555 1.44 LINK ND2 ASN D 67 C1 NAG D 501 1555 1555 1.44 LINK ND2 ASN D 99 C1 NAG D 502 1555 1555 1.45 LINK ND2 ASN D 414 C1 NAG D 503 1555 1555 1.44 LINK ND2 ASN D 464 C1 NAG D 504 1555 1555 1.44 LINK ND2 ASN G 67 C1 NAG G 501 1555 1555 1.46 LINK ND2 ASN G 99 C1 NAG G 502 1555 1555 1.44 LINK ND2 ASN G 414 C1 NAG G 503 1555 1555 1.44 LINK ND2 ASN G 464 C1 NAG G 504 1555 1555 1.44 CISPEP 1 LEU L 94 PRO L 95 0 -2.27 CISPEP 2 LEU E 94 PRO E 95 0 -2.33 CISPEP 3 LEU F 94 PRO F 95 0 -2.47 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