HEADER HYDROLASE/DNA 17-NOV-09 3KQH
TITLE THREE CONFORMATIONAL SNAPSHOTS OF THE HEPATITIS C VIRUS NS3 HELICASE
TITLE 2 REVEAL A RATCHET TRANSLOCATION MECHANISM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE PROTEASE/NTPASE/HELICASE NS3;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CORE PROTEIN P21, CAPSID PROTEIN C, P21, CORE PROTEIN P19,
COMPND 5 ENVELOPE GLYCOPROTEIN E1, GP32, GP35, ENVELOPE GLYCOPROTEIN E2, NS1,
COMPND 6 GP68, GP70, P7, PROTEASE NS2-3, P23, SERINE PROTEASE/NTPASE/HELICASE
COMPND 7 NS3, HEPACIVIRIN, NS3P, P70, NON-STRUCTURAL PROTEIN 4A, NS4A, P8,
COMPND 8 NON-STRUCTURAL PROTEIN 4B, NS4B, P27, NON-STRUCTURAL PROTEIN 5A,
COMPND 9 NS5A, P56, RNA-DIRECTED RNA POLYMERASE, NS5B, P68;
COMPND 10 EC: 3.4.21.98, 3.6.1.15, 3.6.1.-;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 2;
COMPND 13 MOLECULE: 5'-D(*AP*AP*AP*AP*AP*A)-3';
COMPND 14 CHAIN: C, D;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HEPATITIS C VIRUS;
SOURCE 3 ORGANISM_COMMON: HCV;
SOURCE 4 ORGANISM_TAXID: 333284;
SOURCE 5 STRAIN: CON1;
SOURCE 6 GENE: NS3;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET28;
SOURCE 12 MOL_ID: 2;
SOURCE 13 SYNTHETIC: YES
KEYWDS HCV, NS3 PROTEIN, HELICASE, DNA-BINDING, HYDROLASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.GU,C.M.RICE
REVDAT 3 21-FEB-24 3KQH 1 REMARK
REVDAT 2 01-NOV-17 3KQH 1 REMARK
REVDAT 1 26-JAN-10 3KQH 0
JRNL AUTH M.GU,C.M.RICE
JRNL TITL THREE CONFORMATIONAL SNAPSHOTS OF THE HEPATITIS C VIRUS NS3
JRNL TITL 2 HELICASE REVEAL A RATCHET TRANSLOCATION MECHANISM.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 107 521 2010
JRNL REFN ISSN 0027-8424
JRNL PMID 20080715
JRNL DOI 10.1073/PNAS.0913380107
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.5
REMARK 3 NUMBER OF REFLECTIONS : 38741
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 1917
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6550
REMARK 3 NUCLEIC ACID ATOMS : 246
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 138
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02000
REMARK 3 B22 (A**2) : -7.69000
REMARK 3 B33 (A**2) : 7.67000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 28.68
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : CNS_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 5 : CNS_TOPPAR:CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : CNS_TOPPAR:PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CNS_TOPPAR:DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : CNS_TOPPAR:WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : CNS_TOPPAR:ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3KQH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-NOV-09.
REMARK 100 THE DEPOSITION ID IS D_1000056319.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0809
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40398
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -0.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5, 22% (V/V) GLYCEROL,
REMARK 280 10% (W/V) PEG 8000, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 22.60200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 98.65750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.69050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 98.65750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.60200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 57.69050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
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 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 THR A 206 100.13 62.96
REMARK 500 SER A 208 -64.11 -151.64
REMARK 500 THR A 212 -60.68 -130.21
REMARK 500 CYS A 292 -2.10 -56.96
REMARK 500 ALA A 310 -70.96 -44.04
REMARK 500 PHE A 349 -103.70 -118.54
REMARK 500 LYS A 352 -154.85 -129.96
REMARK 500 LEU A 384 29.35 -78.63
REMARK 500 VAL A 406 149.71 -174.39
REMARK 500 THR A 411 -167.04 -101.89
REMARK 500 ASP A 421 99.12 58.70
REMARK 500 THR A 443 -100.95 -125.27
REMARK 500 VAL A 451 146.34 179.43
REMARK 500 GLU A 480 141.64 -176.66
REMARK 500 GLU A 503 48.70 36.70
REMARK 500 LYS A 583 -8.39 -52.22
REMARK 500 LEU A 602 65.36 -119.07
REMARK 500 THR B 206 88.76 20.65
REMARK 500 SER B 208 -41.41 172.27
REMARK 500 THR B 212 -62.42 -137.12
REMARK 500 ILE B 248 102.67 -171.84
REMARK 500 ASN B 335 41.23 -101.32
REMARK 500 SER B 342 -169.88 -122.54
REMARK 500 PHE B 349 -106.82 -118.99
REMARK 500 LYS B 352 -150.63 -128.12
REMARK 500 GLU B 357 20.13 -76.99
REMARK 500 THR B 443 -99.30 -109.87
REMARK 500 VAL B 451 144.06 -173.12
REMARK 500 ARG B 469 -164.29 -109.23
REMARK 500 GLU B 480 127.78 -170.36
REMARK 500 PHE B 557 77.33 -116.14
REMARK 500 GLN B 572 19.69 52.54
REMARK 500 ASP B 579 -174.80 -67.33
REMARK 500 LEU B 602 52.80 -105.11
REMARK 500 ASN B 607 167.34 -42.25
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 TYR A 563 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KQK RELATED DB: PDB
REMARK 900 RELATED ID: 3KQL RELATED DB: PDB
REMARK 900 RELATED ID: 3KQN RELATED DB: PDB
REMARK 900 RELATED ID: 3KQU RELATED DB: PDB
DBREF 3KQH A 189 624 UNP Q9WMX2 POLG_HCVCO 1215 1650
DBREF 3KQH B 189 624 UNP Q9WMX2 POLG_HCVCO 1215 1650
DBREF 3KQH C 1 6 PDB 3KQH 3KQH 1 6
DBREF 3KQH D 1 6 PDB 3KQH 3KQH 1 6
SEQRES 1 A 436 SER PRO PRO ALA VAL PRO GLN THR PHE GLN VAL ALA HIS
SEQRES 2 A 436 LEU HIS ALA PRO THR GLY SER GLY LYS SER THR LYS VAL
SEQRES 3 A 436 PRO ALA ALA TYR ALA ALA GLN GLY TYR LYS VAL LEU VAL
SEQRES 4 A 436 LEU ASN PRO SER VAL ALA ALA THR LEU GLY PHE GLY ALA
SEQRES 5 A 436 TYR MET SER LYS ALA HIS GLY ILE ASP PRO ASN ILE ARG
SEQRES 6 A 436 THR GLY VAL ARG THR ILE THR THR GLY ALA PRO ILE THR
SEQRES 7 A 436 TYR SER THR TYR GLY LYS PHE LEU ALA ASP GLY GLY CYS
SEQRES 8 A 436 SER GLY GLY ALA TYR ASP ILE ILE ILE CYS ASP GLU CYS
SEQRES 9 A 436 HIS SER THR ASP SER THR THR ILE LEU GLY ILE GLY THR
SEQRES 10 A 436 VAL LEU ASP GLN ALA GLU THR ALA GLY ALA ARG LEU VAL
SEQRES 11 A 436 VAL LEU ALA THR ALA THR PRO PRO GLY SER VAL THR VAL
SEQRES 12 A 436 PRO HIS PRO ASN ILE GLU GLU VAL ALA LEU SER SER THR
SEQRES 13 A 436 GLY GLU ILE PRO PHE TYR GLY LYS ALA ILE PRO ILE GLU
SEQRES 14 A 436 THR ILE LYS GLY GLY ARG HIS LEU ILE PHE CYS HIS SER
SEQRES 15 A 436 LYS LYS LYS CYS ASP GLU LEU ALA ALA LYS LEU SER GLY
SEQRES 16 A 436 LEU GLY LEU ASN ALA VAL ALA TYR TYR ARG GLY LEU ASP
SEQRES 17 A 436 VAL SER VAL ILE PRO THR SER GLY ASP VAL ILE VAL VAL
SEQRES 18 A 436 ALA THR ASP ALA LEU MET THR GLY PHE THR GLY ASP PHE
SEQRES 19 A 436 ASP SER VAL ILE ASP CYS ASN THR CYS VAL THR GLN THR
SEQRES 20 A 436 VAL ASP PHE SER LEU ASP PRO THR PHE THR ILE GLU THR
SEQRES 21 A 436 THR THR VAL PRO GLN ASP ALA VAL SER ARG SER GLN ARG
SEQRES 22 A 436 ARG GLY ARG THR GLY ARG GLY ARG MET GLY ILE TYR ARG
SEQRES 23 A 436 PHE VAL THR PRO GLY GLU ARG PRO SER GLY MET PHE ASP
SEQRES 24 A 436 SER SER VAL LEU CYS GLU CYS TYR ASP ALA GLY CYS ALA
SEQRES 25 A 436 TRP TYR GLU LEU THR PRO ALA GLU THR SER VAL ARG LEU
SEQRES 26 A 436 ARG ALA TYR LEU ASN THR PRO GLY LEU PRO VAL CYS GLN
SEQRES 27 A 436 ASP HIS LEU GLU PHE TRP GLU SER VAL PHE THR GLY LEU
SEQRES 28 A 436 THR HIS ILE ASP ALA HIS PHE LEU SER GLN THR LYS GLN
SEQRES 29 A 436 ALA GLY ASP ASN PHE PRO TYR LEU VAL ALA TYR GLN ALA
SEQRES 30 A 436 THR VAL CYS ALA ARG ALA GLN ALA PRO PRO PRO SER TRP
SEQRES 31 A 436 ASP GLN MET TRP LYS CYS LEU ILE ARG LEU LYS PRO THR
SEQRES 32 A 436 LEU HIS GLY PRO THR PRO LEU LEU TYR ARG LEU GLY ALA
SEQRES 33 A 436 VAL GLN ASN GLU VAL THR THR THR HIS PRO ILE THR LYS
SEQRES 34 A 436 TYR ILE MET ALA CYS MET SER
SEQRES 1 B 436 SER PRO PRO ALA VAL PRO GLN THR PHE GLN VAL ALA HIS
SEQRES 2 B 436 LEU HIS ALA PRO THR GLY SER GLY LYS SER THR LYS VAL
SEQRES 3 B 436 PRO ALA ALA TYR ALA ALA GLN GLY TYR LYS VAL LEU VAL
SEQRES 4 B 436 LEU ASN PRO SER VAL ALA ALA THR LEU GLY PHE GLY ALA
SEQRES 5 B 436 TYR MET SER LYS ALA HIS GLY ILE ASP PRO ASN ILE ARG
SEQRES 6 B 436 THR GLY VAL ARG THR ILE THR THR GLY ALA PRO ILE THR
SEQRES 7 B 436 TYR SER THR TYR GLY LYS PHE LEU ALA ASP GLY GLY CYS
SEQRES 8 B 436 SER GLY GLY ALA TYR ASP ILE ILE ILE CYS ASP GLU CYS
SEQRES 9 B 436 HIS SER THR ASP SER THR THR ILE LEU GLY ILE GLY THR
SEQRES 10 B 436 VAL LEU ASP GLN ALA GLU THR ALA GLY ALA ARG LEU VAL
SEQRES 11 B 436 VAL LEU ALA THR ALA THR PRO PRO GLY SER VAL THR VAL
SEQRES 12 B 436 PRO HIS PRO ASN ILE GLU GLU VAL ALA LEU SER SER THR
SEQRES 13 B 436 GLY GLU ILE PRO PHE TYR GLY LYS ALA ILE PRO ILE GLU
SEQRES 14 B 436 THR ILE LYS GLY GLY ARG HIS LEU ILE PHE CYS HIS SER
SEQRES 15 B 436 LYS LYS LYS CYS ASP GLU LEU ALA ALA LYS LEU SER GLY
SEQRES 16 B 436 LEU GLY LEU ASN ALA VAL ALA TYR TYR ARG GLY LEU ASP
SEQRES 17 B 436 VAL SER VAL ILE PRO THR SER GLY ASP VAL ILE VAL VAL
SEQRES 18 B 436 ALA THR ASP ALA LEU MET THR GLY PHE THR GLY ASP PHE
SEQRES 19 B 436 ASP SER VAL ILE ASP CYS ASN THR CYS VAL THR GLN THR
SEQRES 20 B 436 VAL ASP PHE SER LEU ASP PRO THR PHE THR ILE GLU THR
SEQRES 21 B 436 THR THR VAL PRO GLN ASP ALA VAL SER ARG SER GLN ARG
SEQRES 22 B 436 ARG GLY ARG THR GLY ARG GLY ARG MET GLY ILE TYR ARG
SEQRES 23 B 436 PHE VAL THR PRO GLY GLU ARG PRO SER GLY MET PHE ASP
SEQRES 24 B 436 SER SER VAL LEU CYS GLU CYS TYR ASP ALA GLY CYS ALA
SEQRES 25 B 436 TRP TYR GLU LEU THR PRO ALA GLU THR SER VAL ARG LEU
SEQRES 26 B 436 ARG ALA TYR LEU ASN THR PRO GLY LEU PRO VAL CYS GLN
SEQRES 27 B 436 ASP HIS LEU GLU PHE TRP GLU SER VAL PHE THR GLY LEU
SEQRES 28 B 436 THR HIS ILE ASP ALA HIS PHE LEU SER GLN THR LYS GLN
SEQRES 29 B 436 ALA GLY ASP ASN PHE PRO TYR LEU VAL ALA TYR GLN ALA
SEQRES 30 B 436 THR VAL CYS ALA ARG ALA GLN ALA PRO PRO PRO SER TRP
SEQRES 31 B 436 ASP GLN MET TRP LYS CYS LEU ILE ARG LEU LYS PRO THR
SEQRES 32 B 436 LEU HIS GLY PRO THR PRO LEU LEU TYR ARG LEU GLY ALA
SEQRES 33 B 436 VAL GLN ASN GLU VAL THR THR THR HIS PRO ILE THR LYS
SEQRES 34 B 436 TYR ILE MET ALA CYS MET SER
SEQRES 1 C 6 DA DA DA DA DA DA
SEQRES 1 D 6 DA DA DA DA DA DA
FORMUL 5 HOH *138(H2 O)
HELIX 1 1 SER A 208 SER A 211 5 4
HELIX 2 2 THR A 212 GLN A 221 1 10
HELIX 3 3 SER A 231 GLY A 247 1 17
HELIX 4 4 TYR A 270 ASP A 276 1 7
HELIX 5 5 ASP A 296 ALA A 310 1 15
HELIX 6 6 SER A 370 LEU A 384 1 15
HELIX 7 7 ASP A 396 ILE A 400 5 5
HELIX 8 8 ASP A 454 GLY A 463 1 10
HELIX 9 9 ASP A 487 TRP A 501 1 15
HELIX 10 10 THR A 505 ASN A 518 1 14
HELIX 11 11 HIS A 528 GLY A 538 1 11
HELIX 12 12 ASP A 543 ALA A 553 1 11
HELIX 13 13 PHE A 557 ALA A 571 1 15
HELIX 14 14 ASP A 579 LEU A 592 5 14
HELIX 15 15 HIS A 613 MET A 623 1 11
HELIX 16 16 THR B 212 GLN B 221 1 10
HELIX 17 17 SER B 231 HIS B 246 1 16
HELIX 18 18 TYR B 270 ASP B 276 1 7
HELIX 19 19 ASP B 296 ALA B 310 1 15
HELIX 20 20 GLU B 311 GLY B 314 5 4
HELIX 21 21 PRO B 355 ILE B 359 5 5
HELIX 22 22 SER B 370 LEU B 381 1 12
HELIX 23 23 SER B 382 GLY B 385 5 4
HELIX 24 24 ASP B 396 ILE B 400 5 5
HELIX 25 25 ASP B 454 GLY B 463 1 10
HELIX 26 26 ASP B 487 TRP B 501 1 15
HELIX 27 27 THR B 505 THR B 519 1 15
HELIX 28 28 HIS B 528 GLY B 538 1 11
HELIX 29 29 ASP B 543 ALA B 553 1 11
HELIX 30 30 PHE B 557 ALA B 571 1 15
HELIX 31 31 ASP B 579 ILE B 586 5 8
HELIX 32 32 HIS B 613 SER B 624 1 12
SHEET 1 A 7 GLN A 198 HIS A 203 0
SHEET 2 A 7 LEU A 317 THR A 322 1 O VAL A 318 N ALA A 200
SHEET 3 A 7 ILE A 286 CYS A 289 1 N CYS A 289 O VAL A 319
SHEET 4 A 7 VAL A 225 ASN A 229 1 N LEU A 226 O ILE A 288
SHEET 5 A 7 ILE A 265 THR A 269 1 O THR A 266 N VAL A 227
SHEET 6 A 7 ASN A 251 ARG A 253 1 N ASN A 251 O TYR A 267
SHEET 7 A 7 THR A 258 ILE A 259 -1 O ILE A 259 N ILE A 252
SHEET 1 B 6 ILE A 336 ALA A 340 0
SHEET 2 B 6 GLY A 471 PHE A 475 1 O TYR A 473 N VAL A 339
SHEET 3 B 6 SER A 424 ASP A 427 1 N VAL A 425 O ARG A 474
SHEET 4 B 6 ARG A 363 PHE A 367 1 N PHE A 367 O ILE A 426
SHEET 5 B 6 VAL A 406 ALA A 410 1 O VAL A 408 N ILE A 366
SHEET 6 B 6 ALA A 388 TYR A 391 1 N VAL A 389 O ILE A 407
SHEET 1 C 2 ILE A 347 PRO A 348 0
SHEET 2 C 2 ALA A 353 ILE A 354 -1 O ILE A 354 N ILE A 347
SHEET 1 D 2 THR A 430 ASP A 437 0
SHEET 2 D 2 THR A 445 PRO A 452 -1 O THR A 449 N THR A 433
SHEET 1 E 2 THR A 596 PRO A 597 0
SHEET 2 E 2 VAL A 609 THR A 610 1 O THR A 610 N THR A 596
SHEET 1 F 7 GLN B 198 HIS B 203 0
SHEET 2 F 7 LEU B 317 THR B 322 1 O LEU B 320 N ALA B 200
SHEET 3 F 7 ILE B 286 CYS B 289 1 N CYS B 289 O VAL B 319
SHEET 4 F 7 VAL B 225 ASN B 229 1 N LEU B 226 O ILE B 288
SHEET 5 F 7 ILE B 265 THR B 269 1 O THR B 266 N VAL B 227
SHEET 6 F 7 ASN B 251 ARG B 253 1 N ASN B 251 O TYR B 267
SHEET 7 F 7 THR B 258 ILE B 259 -1 O ILE B 259 N ILE B 252
SHEET 1 G 6 ILE B 336 ALA B 340 0
SHEET 2 G 6 GLY B 471 PHE B 475 1 O TYR B 473 N GLU B 337
SHEET 3 G 6 SER B 424 ASP B 427 1 N VAL B 425 O ILE B 472
SHEET 4 G 6 ARG B 363 PHE B 367 1 N LEU B 365 O ILE B 426
SHEET 5 G 6 VAL B 406 ALA B 410 1 O VAL B 408 N ILE B 366
SHEET 6 G 6 ALA B 388 TYR B 391 1 N TYR B 391 O VAL B 409
SHEET 1 H 2 ILE B 347 PRO B 348 0
SHEET 2 H 2 ALA B 353 ILE B 354 -1 O ILE B 354 N ILE B 347
SHEET 1 I 2 THR B 430 ASP B 437 0
SHEET 2 I 2 THR B 445 PRO B 452 -1 O THR B 445 N ASP B 437
SHEET 1 J 2 THR B 596 PRO B 597 0
SHEET 2 J 2 VAL B 609 THR B 610 1 O THR B 610 N THR B 596
CISPEP 1 ASP A 441 PRO A 442 0 0.60
CISPEP 2 ASP B 441 PRO B 442 0 0.51
CRYST1 45.204 115.381 197.315 90.00 90.00 90.00 P 21 21 21 8
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 0.022122 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008667 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005068 0.00000
(ATOM LINES ARE NOT SHOWN.)
END