HEADER HYDROLASE 15-SEP-08 2JLQ
TITLE DENGUE VIRUS 4 NS3 HELICASE STRUCTURE, APO ENZYME.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE PROTEASE SUBUNIT NS3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1646-2092;
COMPND 5 SYNONYM: DENV4 NS3 HELICASE, NON-STRUCTURAL PROTEIN 3;
COMPND 6 EC: 3.4.21.91;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DENGUE VIRUS 4;
SOURCE 3 ORGANISM_TAXID: 408688;
SOURCE 4 STRAIN: THAILAND/0348/1991;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS RIBONUCLEOPROTEIN, NUCLEOTIDE-BINDING, VIRAL NUCLEOPROTEIN,
KEYWDS 2 ENDOPLASMIC RETICULUM, HELICASE, PROTEASE, HYDROLASE, TRANSFERASE,
KEYWDS 3 CLEAVAGE ON PAIR OF BASIC RESIDUES, MULTIFUNCTIONAL ENZYME,
KEYWDS 4 TRANSCRIPTION REGULATION, NUCLEOTIDYLTRANSFERASE, NS3 HELICASE
KEYWDS 5 STRUCTURE, VIRION, ATPASE, NUCLEUS, MEMBRANE, SECRETED, ATP-BINDING,
KEYWDS 6 RNA-BINDING, FLAVIVIRUSES, GLYCOPROTEIN, RNA-DIRECTED RNA
KEYWDS 7 POLYMERASE, RNA REPLICATION, SERINE PROTEASE, ENVELOPE PROTEIN,
KEYWDS 8 DENGUE VIRUS, METAL-BINDING, TRANSMEMBRANE, TRANSCRIPTION,
KEYWDS 9 PHOSPHOPROTEIN, CAPSID PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.H.LUO,T.XU,R.P.WATSON,D.S.BECKER,A.SAMPATH,W.JAHNKE,S.S.YEONG,
AUTHOR 2 C.H.WANG,S.P.LIM,S.G.VASUDEVAN,J.LESCAR
REVDAT 4 13-DEC-23 2JLQ 1 REMARK
REVDAT 3 13-JUL-11 2JLQ 1 VERSN
REVDAT 2 13-JAN-09 2JLQ 1 VERSN JRNL
REVDAT 1 25-NOV-08 2JLQ 0
JRNL AUTH D.LUO,T.XU,R.P.WATSON,D.SCHERER-BECKER,A.SAMPATH,W.JAHNKE,
JRNL AUTH 2 S.S.YEONG,C.H.WANG,S.P.LIM,A.STRONGIN,S.G.VASUDEVAN,J.LESCAR
JRNL TITL INSIGHTS INTO RNA UNWINDING AND ATP HYDROLYSIS BY THE
JRNL TITL 2 FLAVIVIRUS NS3 PROTEIN.
JRNL REF EMBO J. V. 27 3209 2008
JRNL REFN ISSN 0261-4189
JRNL PMID 19008861
JRNL DOI 10.1038/EMBOJ.2008.232
REMARK 2
REMARK 2 RESOLUTION. 1.67 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.67
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 56198
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2989
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.67
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.71
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4014
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.4410
REMARK 3 BIN FREE R VALUE SET COUNT : 200
REMARK 3 BIN FREE R VALUE : 0.4660
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3591
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 7
REMARK 3 SOLVENT ATOMS : 348
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.08000
REMARK 3 B22 (A**2) : 0.21000
REMARK 3 B33 (A**2) : -0.29000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.114
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.106
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.075
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.195
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3777 ; 0.002 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5141 ; 0.410 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 484 ; 6.387 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 177 ;34.060 ;22.881
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 676 ;13.653 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;11.608 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 564 ; 0.036 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2899 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1851 ; 0.200 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2602 ; 0.317 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 342 ; 0.119 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 55 ; 0.205 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 20 ; 0.097 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2349 ; 0.485 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3767 ; 0.823 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1584 ; 1.193 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1357 ; 1.962 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 180 A 314
REMARK 3 ORIGIN FOR THE GROUP (A): -28.2580 12.1046 1.9707
REMARK 3 T TENSOR
REMARK 3 T11: -0.0930 T22: -0.0987
REMARK 3 T33: -0.0270 T12: 0.0323
REMARK 3 T13: -0.0173 T23: 0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 3.6203 L22: 1.5581
REMARK 3 L33: 0.9478 L12: 0.2600
REMARK 3 L13: -0.4260 L23: 0.3606
REMARK 3 S TENSOR
REMARK 3 S11: -0.0579 S12: -0.1011 S13: 0.2327
REMARK 3 S21: 0.0390 S22: -0.0380 S23: 0.2163
REMARK 3 S31: -0.0276 S32: -0.1000 S33: 0.0959
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 315 A 500
REMARK 3 ORIGIN FOR THE GROUP (A): -6.9008 -2.5382 -2.3628
REMARK 3 T TENSOR
REMARK 3 T11: -0.0565 T22: -0.0634
REMARK 3 T33: -0.0889 T12: 0.0018
REMARK 3 T13: -0.0023 T23: -0.0188
REMARK 3 L TENSOR
REMARK 3 L11: 1.8199 L22: 0.8883
REMARK 3 L33: 1.4558 L12: 0.0688
REMARK 3 L13: 0.7391 L23: 0.0550
REMARK 3 S TENSOR
REMARK 3 S11: 0.0260 S12: 0.1139 S13: -0.1985
REMARK 3 S21: -0.0654 S22: 0.0921 S23: -0.0355
REMARK 3 S31: 0.1235 S32: 0.0900 S33: -0.1181
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 501 A 618
REMARK 3 ORIGIN FOR THE GROUP (A): -27.2791 -9.4516 -18.6444
REMARK 3 T TENSOR
REMARK 3 T11: -0.0182 T22: -0.0152
REMARK 3 T33: -0.1233 T12: -0.0179
REMARK 3 T13: -0.0175 T23: 0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 1.1729 L22: 4.9814
REMARK 3 L33: 1.2855 L12: 1.4324
REMARK 3 L13: 0.6093 L23: 1.3430
REMARK 3 S TENSOR
REMARK 3 S11: -0.0813 S12: 0.1411 S13: 0.0494
REMARK 3 S21: 0.0528 S22: 0.0383 S23: 0.3415
REMARK 3 S31: 0.0715 S32: -0.0306 S33: 0.0431
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2JLQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-SEP-08.
REMARK 100 THE DEPOSITION ID IS D_1290037551.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59272
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 21.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.700
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 0.76000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 2BMF
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 26.41050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.48100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.30700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.48100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.41050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.30700
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 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 TYR A 499 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 526 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 576 CG OD1 ND2
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 OE2 GLU A 285 O HOH A 2098 2.02
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 LYS A 186 -2.57 84.81
REMARK 500 THR A 315 145.97 -174.27
REMARK 500 ARG A 592 76.26 -152.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1620
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2JLR RELATED DB: PDB
REMARK 900 DENGUE VIRUS 4 NS3 HELICASE IN COMPLEX WITH AMPPNP
REMARK 900 RELATED ID: 2JLS RELATED DB: PDB
REMARK 900 DENGUE VIRUS 4 NS3 HELICASE IN COMPLEX WITH ADP
REMARK 900 RELATED ID: 2JLU RELATED DB: PDB
REMARK 900 DENGUE VIRUS 4 NS3 HELICASE IN COMPLEX WITH SSRNA
REMARK 900 RELATED ID: 2JLV RELATED DB: PDB
REMARK 900 DENGUE VIRUS 4 NS3 HELICASE IN COMPLEX WITH SSRNA AND AMPPNP
REMARK 900 RELATED ID: 2JLW RELATED DB: PDB
REMARK 900 DENGUE VIRUS 4 NS3 HELICASE IN COMPLEX WITH SSRNA2
REMARK 900 RELATED ID: 2JLX RELATED DB: PDB
REMARK 900 DENGUE VIRUS 4 NS3 HELICASE IN COMPLEX WITH SSRNA AND ADP-VANADATE
REMARK 900 RELATED ID: 2JLY RELATED DB: PDB
REMARK 900 DENGUE VIRUS 4 NS3 HELICASE IN COMPLEX WITH SSRNA AND ADP-PHOSPHATE
REMARK 900 RELATED ID: 2JLZ RELATED DB: PDB
REMARK 900 DENGUE VIRUS 4 NS3 HELICASE IN COMPLEX WITH SSRNA AND ADP
DBREF 2JLQ A 168 171 PDB 2JLQ 2JLQ 168 171
DBREF 2JLQ A 172 618 UNP Q2YHF0 POLG_DEN4T 1646 2092
SEQADV 2JLQ LEU A 213 UNP Q2YHF0 LYS 1687 CONFLICT
SEQADV 2JLQ ASP A 250 UNP Q2YHF0 GLU 1724 CONFLICT
SEQADV 2JLQ CYS A 292 UNP Q2YHF0 SER 1766 CONFLICT
SEQADV 2JLQ SER A 321 UNP Q2YHF0 THR 1795 CONFLICT
SEQADV 2JLQ ARG A 381 UNP Q2YHF0 LYS 1855 CONFLICT
SEQADV 2JLQ LYS A 480 UNP Q2YHF0 ARG 1954 CONFLICT
SEQRES 1 A 451 GLY SER ALA MET GLY GLU PRO ASP TYR GLU VAL ASP GLU
SEQRES 2 A 451 ASP ILE PHE ARG LYS LYS ARG LEU THR ILE MET ASP LEU
SEQRES 3 A 451 HIS PRO GLY ALA GLY LYS THR LYS ARG ILE LEU PRO SER
SEQRES 4 A 451 ILE VAL ARG GLU ALA LEU LEU ARG ARG LEU ARG THR LEU
SEQRES 5 A 451 ILE LEU ALA PRO THR ARG VAL VAL ALA ALA GLU MET GLU
SEQRES 6 A 451 GLU ALA LEU ARG GLY LEU PRO ILE ARG TYR GLN THR PRO
SEQRES 7 A 451 ALA VAL LYS SER ASP HIS THR GLY ARG GLU ILE VAL ASP
SEQRES 8 A 451 LEU MET CYS HIS ALA THR PHE THR THR ARG LEU LEU SER
SEQRES 9 A 451 SER THR ARG VAL PRO ASN TYR ASN LEU ILE VAL MET ASP
SEQRES 10 A 451 GLU ALA HIS PHE THR ASP PRO CYS SER VAL ALA ALA ARG
SEQRES 11 A 451 GLY TYR ILE SER THR ARG VAL GLU MET GLY GLU ALA ALA
SEQRES 12 A 451 ALA ILE PHE MET THR ALA THR PRO PRO GLY SER THR ASP
SEQRES 13 A 451 PRO PHE PRO GLN SER ASN SER PRO ILE GLU ASP ILE GLU
SEQRES 14 A 451 ARG GLU ILE PRO GLU ARG SER TRP ASN THR GLY PHE ASP
SEQRES 15 A 451 TRP ILE THR ASP TYR GLN GLY LYS THR VAL TRP PHE VAL
SEQRES 16 A 451 PRO SER ILE LYS ALA GLY ASN ASP ILE ALA ASN CYS LEU
SEQRES 17 A 451 ARG LYS SER GLY LYS ARG VAL ILE GLN LEU SER ARG LYS
SEQRES 18 A 451 THR PHE ASP THR GLU TYR PRO LYS THR LYS LEU THR ASP
SEQRES 19 A 451 TRP ASP PHE VAL VAL THR THR ASP ILE SER GLU MET GLY
SEQRES 20 A 451 ALA ASN PHE ARG ALA GLY ARG VAL ILE ASP PRO ARG ARG
SEQRES 21 A 451 CYS LEU LYS PRO VAL ILE LEU THR ASP GLY PRO GLU ARG
SEQRES 22 A 451 VAL ILE LEU ALA GLY PRO ILE PRO VAL THR PRO ALA SER
SEQRES 23 A 451 ALA ALA GLN ARG ARG GLY ARG ILE GLY ARG ASN PRO ALA
SEQRES 24 A 451 GLN GLU ASP ASP GLN TYR VAL PHE SER GLY ASP PRO LEU
SEQRES 25 A 451 LYS ASN ASP GLU ASP HIS ALA HIS TRP THR GLU ALA LYS
SEQRES 26 A 451 MET LEU LEU ASP ASN ILE TYR THR PRO GLU GLY ILE ILE
SEQRES 27 A 451 PRO THR LEU PHE GLY PRO GLU ARG GLU LYS THR GLN ALA
SEQRES 28 A 451 ILE ASP GLY GLU PHE ARG LEU ARG GLY GLU GLN ARG LYS
SEQRES 29 A 451 THR PHE VAL GLU LEU MET ARG ARG GLY ASP LEU PRO VAL
SEQRES 30 A 451 TRP LEU SER TYR LYS VAL ALA SER ALA GLY ILE SER TYR
SEQRES 31 A 451 LYS ASP ARG GLU TRP CYS PHE THR GLY GLU ARG ASN ASN
SEQRES 32 A 451 GLN ILE LEU GLU GLU ASN MET GLU VAL GLU ILE TRP THR
SEQRES 33 A 451 ARG GLU GLY GLU LYS LYS LYS LEU ARG PRO LYS TRP LEU
SEQRES 34 A 451 ASP ALA ARG VAL TYR ALA ASP PRO MET ALA LEU LYS ASP
SEQRES 35 A 451 PHE LYS GLU PHE ALA SER GLY ARG LYS
HET CL A1619 1
HET GOL A1620 6
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 CL CL 1-
FORMUL 3 GOL C3 H8 O3
FORMUL 4 HOH *348(H2 O)
HELIX 1 1 ASP A 179 ARG A 184 5 6
HELIX 2 2 ARG A 202 ARG A 214 1 13
HELIX 3 3 THR A 224 LEU A 235 1 12
HELIX 4 4 HIS A 262 SER A 272 1 11
HELIX 5 5 ASP A 290 MET A 306 1 17
HELIX 6 6 PHE A 348 TYR A 354 1 7
HELIX 7 7 SER A 364 LYS A 377 1 14
HELIX 8 8 THR A 389 TYR A 394 1 6
HELIX 9 9 PRO A 395 LEU A 399 5 5
HELIX 10 10 ASP A 409 MET A 413 5 5
HELIX 11 11 THR A 450 GLY A 459 1 10
HELIX 12 12 HIS A 485 ASP A 496 1 12
HELIX 13 13 PHE A 509 THR A 516 5 8
HELIX 14 14 ARG A 526 ARG A 539 1 14
HELIX 15 15 PRO A 543 ALA A 553 1 11
HELIX 16 16 ARG A 560 PHE A 564 5 5
HELIX 17 17 GLU A 567 GLN A 571 5 5
HELIX 18 18 ALA A 598 TYR A 601 5 4
HELIX 19 19 ASP A 603 SER A 615 1 13
SHEET 1 AA 6 LEU A 188 MET A 191 0
SHEET 2 AA 6 ALA A 310 MET A 314 1 O ALA A 311 N THR A 189
SHEET 3 AA 6 LEU A 280 ASP A 284 1 O ILE A 281 N ILE A 312
SHEET 4 AA 6 THR A 218 ALA A 222 1 O LEU A 219 N VAL A 282
SHEET 5 AA 6 VAL A 257 CYS A 261 1 O ASP A 258 N ILE A 220
SHEET 6 AA 6 ILE A 240 TYR A 242 1 O ARG A 241 N LEU A 259
SHEET 1 AB 6 ILE A 332 GLU A 336 0
SHEET 2 AB 6 ASP A 470 PHE A 474 1 O ASP A 470 N GLU A 333
SHEET 3 AB 6 ARG A 421 ASP A 424 1 O VAL A 422 N VAL A 473
SHEET 4 AB 6 THR A 358 PHE A 361 1 O VAL A 359 N ILE A 423
SHEET 5 AB 6 PHE A 404 THR A 407 1 O VAL A 405 N TRP A 360
SHEET 6 AB 6 VAL A 382 LEU A 385 1 O ILE A 383 N VAL A 406
SHEET 1 AC 2 ARG A 427 LEU A 434 0
SHEET 2 AC 2 ARG A 440 PRO A 448 -1 O ARG A 440 N LEU A 434
SHEET 1 AD 2 LEU A 573 GLU A 574 0
SHEET 2 AD 2 MET A 577 GLU A 578 -1 O MET A 577 N GLU A 574
SHEET 1 AE 2 GLU A 580 TRP A 582 0
SHEET 2 AE 2 LYS A 588 LYS A 590 -1 O LYS A 589 N ILE A 581
CISPEP 1 ALA A 197 GLY A 198 0 -14.45
CISPEP 2 GLY A 445 PRO A 446 0 6.05
SITE 1 AC1 2 ARG A 387 THR A 408
SITE 1 AC2 9 GLY A 320 SER A 321 ALA A 452 ASP A 482
SITE 2 AC2 9 LYS A 515 HOH A2261 HOH A2282 HOH A2347
SITE 3 AC2 9 HOH A2348
CRYST1 52.821 92.614 102.962 90.00 90.00 90.00 P 21 21 21 4
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 0.018932 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010798 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009712 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
