HEADER HYDROLASE/RNA 15-SEP-08 2JLY
TITLE DENGUE VIRUS 4 NS3 HELICASE IN COMPLEX WITH SSRNA AND ADP-PHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE PROTEASE SUBUNIT NS3;
COMPND 3 CHAIN: A, B;
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;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: 5'-R(*AP*GP*AP*CP*UP*AP*AP*CP*AP*AP*CP*U)-3';
COMPND 10 CHAIN: C, D;
COMPND 11 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;
SOURCE 7 MOL_ID: 2;
SOURCE 8 SYNTHETIC: YES
KEYWDS HYDROLASE-RNA COMPLEX, ENVELOPE PROTEIN, RIBONUCLEOPROTEIN, CAPSID
KEYWDS 2 PROTEIN, RNA REPLICATION, SERINE PROTEASE, GLYCOPROTEIN, DENGUE
KEYWDS 3 VIRUS, METAL-BINDING, TRANSFERASE, ATP-BINDING, RNA-BINDING,
KEYWDS 4 FLAVIVIRUSES, TRANSCRIPTION REGULATION, RNA-DIRECTED RNA POLYMERASE,
KEYWDS 5 NUCLEOTIDE-BINDING, VIRAL NUCLEOPROTEIN, SECRETED, HELICASE,
KEYWDS 6 PROTEASE, HYDROLASE, PHOSPHATE, CLEAVAGE ON PAIR OF BASIC RESIDUES,
KEYWDS 7 ENDOPLASMIC RETICULUM, NUCLEOTIDYLTRANSFERASE, ADP, SSRNA, VIRION,
KEYWDS 8 ATPASE, NUCLEUS, MEMBRANE, TRANSMEMBRANE, TRANSCRIPTION,
KEYWDS 9 PHOSPHOPROTEIN, NS3 HELICASE STRUCTURE, MULTIFUNCTIONAL ENZYME
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 2JLY 1 LINK
REVDAT 3 13-JUL-11 2JLY 1 VERSN
REVDAT 2 13-JAN-09 2JLY 1 VERSN JRNL
REVDAT 1 25-NOV-08 2JLY 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. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 32553
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1726
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2236
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2780
REMARK 3 BIN FREE R VALUE SET COUNT : 123
REMARK 3 BIN FREE R VALUE : 0.3330
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7185
REMARK 3 NUCLEIC ACID ATOMS : 296
REMARK 3 HETEROGEN ATOMS : 78
REMARK 3 SOLVENT ATOMS : 380
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) : 35.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.13000
REMARK 3 B22 (A**2) : -0.12000
REMARK 3 B33 (A**2) : 0.03000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.04000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 1.548
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.308
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.222
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.870
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.900
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7755 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10580 ; 1.134 ; 2.027
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 900 ; 6.313 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 344 ;32.981 ;22.965
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1286 ;15.424 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 78 ;14.062 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1158 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5790 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3449 ; 0.181 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5177 ; 0.296 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 444 ; 0.268 ; 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): 151 ; 0.242 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 33 ; 0.163 ; 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): 4647 ; 0.352 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7318 ; 0.622 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3648 ; 0.799 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3262 ; 1.391 ; 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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 180 A 326 1
REMARK 3 1 B 180 B 326 1
REMARK 3 2 A 327 A 481 1
REMARK 3 2 B 327 B 481 1
REMARK 3 3 A 482 A 618 1
REMARK 3 3 B 482 B 618 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 3480 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 3480 ; 0.04 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 1 C 4 1
REMARK 3 1 D 1 D 4 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 C (A): 84 ; 0.02 ; 0.05
REMARK 3 TIGHT THERMAL 2 C (A**2): 84 ; 0.05 ; 0.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
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 168 A 326
REMARK 3 ORIGIN FOR THE GROUP (A): -39.8070 -15.2438 -1.6223
REMARK 3 T TENSOR
REMARK 3 T11: -0.0594 T22: -0.1300
REMARK 3 T33: -0.1639 T12: -0.0008
REMARK 3 T13: 0.0177 T23: -0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 2.5291 L22: 2.8989
REMARK 3 L33: 1.1081 L12: 0.3044
REMARK 3 L13: 0.8065 L23: 0.0985
REMARK 3 S TENSOR
REMARK 3 S11: -0.0685 S12: 0.0821 S13: -0.1342
REMARK 3 S21: -0.0723 S22: 0.0711 S23: 0.0949
REMARK 3 S31: 0.1645 S32: 0.0430 S33: -0.0026
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 327 A 481
REMARK 3 ORIGIN FOR THE GROUP (A): -23.6880 4.8985 3.1881
REMARK 3 T TENSOR
REMARK 3 T11: -0.0744 T22: -0.0838
REMARK 3 T33: -0.0800 T12: -0.0641
REMARK 3 T13: -0.0407 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 3.1519 L22: 0.4704
REMARK 3 L33: 2.4448 L12: -0.2786
REMARK 3 L13: 1.3717 L23: 0.0372
REMARK 3 S TENSOR
REMARK 3 S11: -0.1529 S12: 0.2262 S13: 0.1814
REMARK 3 S21: 0.1218 S22: 0.1105 S23: -0.3142
REMARK 3 S31: -0.1892 S32: 0.4190 S33: 0.0424
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 482 A 618
REMARK 3 ORIGIN FOR THE GROUP (A): -48.4487 11.5662 -12.1645
REMARK 3 T TENSOR
REMARK 3 T11: -0.0989 T22: -0.1052
REMARK 3 T33: -0.1094 T12: -0.0077
REMARK 3 T13: -0.0335 T23: -0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 1.0470 L22: 4.7622
REMARK 3 L33: 3.0123 L12: 0.6736
REMARK 3 L13: -0.7362 L23: -2.8174
REMARK 3 S TENSOR
REMARK 3 S11: -0.0819 S12: 0.0537 S13: 0.0065
REMARK 3 S21: -0.2731 S22: 0.2345 S23: 0.1960
REMARK 3 S31: 0.1809 S32: -0.1548 S33: -0.1525
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 168 B 326
REMARK 3 ORIGIN FOR THE GROUP (A): -21.2442 -5.1328 -36.5091
REMARK 3 T TENSOR
REMARK 3 T11: -0.1162 T22: -0.1107
REMARK 3 T33: -0.0009 T12: 0.0164
REMARK 3 T13: 0.0713 T23: -0.0173
REMARK 3 L TENSOR
REMARK 3 L11: 2.4915 L22: 3.3802
REMARK 3 L33: 1.3425 L12: -0.3278
REMARK 3 L13: 0.8135 L23: -0.4059
REMARK 3 S TENSOR
REMARK 3 S11: 0.0606 S12: -0.1350 S13: 0.4028
REMARK 3 S21: 0.0299 S22: 0.0471 S23: 0.1467
REMARK 3 S31: -0.1382 S32: -0.1496 S33: -0.1078
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 327 B 481
REMARK 3 ORIGIN FOR THE GROUP (A): -7.9675 -25.3895 -26.2141
REMARK 3 T TENSOR
REMARK 3 T11: -0.1211 T22: -0.0350
REMARK 3 T33: -0.0681 T12: 0.0085
REMARK 3 T13: -0.0011 T23: 0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 4.2789 L22: 0.1098
REMARK 3 L33: 0.9982 L12: 0.0065
REMARK 3 L13: 0.4444 L23: -0.2421
REMARK 3 S TENSOR
REMARK 3 S11: 0.0207 S12: -0.5637 S13: -0.1756
REMARK 3 S21: 0.1158 S22: 0.0612 S23: -0.1640
REMARK 3 S31: 0.0573 S32: 0.0745 S33: -0.0819
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 482 B 618
REMARK 3 ORIGIN FOR THE GROUP (A): -34.7905 -32.0136 -37.5611
REMARK 3 T TENSOR
REMARK 3 T11: -0.1259 T22: -0.1027
REMARK 3 T33: -0.0986 T12: 0.0219
REMARK 3 T13: -0.0128 T23: -0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 1.4922 L22: 4.0065
REMARK 3 L33: 2.8330 L12: 1.5271
REMARK 3 L13: -0.7547 L23: -1.8157
REMARK 3 S TENSOR
REMARK 3 S11: -0.0120 S12: 0.0424 S13: 0.0934
REMARK 3 S21: -0.1103 S22: 0.1292 S23: 0.2761
REMARK 3 S31: -0.1432 S32: -0.1520 S33: -0.1172
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 2JLY 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_1290037569.
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 : 188211
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 40.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.72000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
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 2JLU
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 65.87400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.79550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 65.87400
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 52.79550
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 2260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 2200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 C C 8
REMARK 465 A C 9
REMARK 465 A C 10
REMARK 465 C C 11
REMARK 465 U C 12
REMARK 465 C D 8
REMARK 465 A D 9
REMARK 465 A D 10
REMARK 465 C D 11
REMARK 465 U D 12
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 ARG A 254 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 254 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 418 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 519 CB CG1 CG2 CD1
REMARK 470 ARG B 538 CG CD NE CZ NH1 NH2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 SER A 321 CA CB OG
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 O4 PO4 B 1620 O HOH B 2178 2.00
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 ARG A 268 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 268 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 268 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG B 268 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 U D 5 O4' - C1' - N1 ANGL. DEV. = 4.5 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 LYS A 186 4.62 80.58
REMARK 500 ASP A 192 68.12 -101.67
REMARK 500 GLN A 243 59.83 -111.62
REMARK 500 THR A 315 140.77 -170.22
REMARK 500 LYS A 398 36.48 -80.69
REMARK 500 ASP A 401 32.89 -95.15
REMARK 500 ASP A 409 5.68 -66.92
REMARK 500 ASN A 416 70.65 -116.14
REMARK 500 GLN A 517 99.08 -64.70
REMARK 500 ALA A 518 -92.00 -26.99
REMARK 500 LYS B 186 4.31 81.25
REMARK 500 ASP B 192 68.82 -102.38
REMARK 500 PRO B 239 79.13 -69.59
REMARK 500 GLN B 243 59.88 -112.56
REMARK 500 THR B 315 141.06 -170.90
REMARK 500 LYS B 398 36.32 -79.06
REMARK 500 ASP B 401 33.58 -95.83
REMARK 500 ASN B 416 70.17 -116.62
REMARK 500 GLN B 517 97.71 -63.97
REMARK 500 ALA B 518 -109.10 -37.12
REMARK 500 ILE B 519 -95.82 -174.20
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 THR A 273 ARG A 274 -126.59
REMARK 500 ALA A 518 ILE A 519 -34.17
REMARK 500 THR B 273 ARG B 274 -69.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A1621 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 200 OG1
REMARK 620 2 ADP A1619 O1B 88.2
REMARK 620 3 HOH A2186 O 80.0 162.3
REMARK 620 4 HOH A2187 O 94.0 109.6 84.5
REMARK 620 5 HOH A2188 O 82.7 84.4 81.1 165.6
REMARK 620 6 HOH A2189 O 170.9 96.5 93.6 91.8 90.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B1621 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 200 OG1
REMARK 620 2 ADP B1619 O1B 90.9
REMARK 620 3 HOH B2179 O 95.3 98.5
REMARK 620 4 HOH B2180 O 80.3 169.2 88.6
REMARK 620 5 HOH B2181 O 166.6 93.9 96.5 93.4
REMARK 620 6 HOH B2182 O 84.7 88.2 173.4 84.9 82.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A1619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A1620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A1621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B1619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B1620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B1621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1622
REMARK 900
REMARK 900 RELATED ENTRIES
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: 2JLQ RELATED DB: PDB
REMARK 900 DENGUE VIRUS 4 NS3 HELICASE STRUCTURE, APO ENZYME.
REMARK 900 RELATED ID: 2JLW RELATED DB: PDB
REMARK 900 DENGUE VIRUS 4 NS3 HELICASE IN COMPLEX WITH SSRNA2
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: 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: 2JLZ RELATED DB: PDB
REMARK 900 DENGUE VIRUS 4 NS3 HELICASE IN COMPLEX WITH SSRNA AND ADP
DBREF 2JLY A 168 171 PDB 2JLY 2JLY 168 171
DBREF 2JLY A 172 618 UNP Q2YHF0 POLG_DEN4T 1646 2092
DBREF 2JLY B 168 171 PDB 2JLY 2JLY 168 171
DBREF 2JLY B 172 618 UNP Q2YHF0 POLG_DEN4T 1646 2092
DBREF 2JLY C 1 12 PDB 2JLY 2JLY 1 12
DBREF 2JLY D 1 12 PDB 2JLY 2JLY 1 12
SEQADV 2JLY LEU A 213 UNP Q2YHF0 LYS 1687 CONFLICT
SEQADV 2JLY ASP A 250 UNP Q2YHF0 GLU 1724 CONFLICT
SEQADV 2JLY CYS A 292 UNP Q2YHF0 SER 1766 CONFLICT
SEQADV 2JLY SER A 321 UNP Q2YHF0 THR 1795 CONFLICT
SEQADV 2JLY ARG A 381 UNP Q2YHF0 LYS 1855 CONFLICT
SEQADV 2JLY LYS A 480 UNP Q2YHF0 ARG 1954 CONFLICT
SEQADV 2JLY LEU B 213 UNP Q2YHF0 LYS 1687 CONFLICT
SEQADV 2JLY ASP B 250 UNP Q2YHF0 GLU 1724 CONFLICT
SEQADV 2JLY CYS B 292 UNP Q2YHF0 SER 1766 CONFLICT
SEQADV 2JLY SER B 321 UNP Q2YHF0 THR 1795 CONFLICT
SEQADV 2JLY ARG B 381 UNP Q2YHF0 LYS 1855 CONFLICT
SEQADV 2JLY LYS B 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
SEQRES 1 B 451 GLY SER ALA MET GLY GLU PRO ASP TYR GLU VAL ASP GLU
SEQRES 2 B 451 ASP ILE PHE ARG LYS LYS ARG LEU THR ILE MET ASP LEU
SEQRES 3 B 451 HIS PRO GLY ALA GLY LYS THR LYS ARG ILE LEU PRO SER
SEQRES 4 B 451 ILE VAL ARG GLU ALA LEU LEU ARG ARG LEU ARG THR LEU
SEQRES 5 B 451 ILE LEU ALA PRO THR ARG VAL VAL ALA ALA GLU MET GLU
SEQRES 6 B 451 GLU ALA LEU ARG GLY LEU PRO ILE ARG TYR GLN THR PRO
SEQRES 7 B 451 ALA VAL LYS SER ASP HIS THR GLY ARG GLU ILE VAL ASP
SEQRES 8 B 451 LEU MET CYS HIS ALA THR PHE THR THR ARG LEU LEU SER
SEQRES 9 B 451 SER THR ARG VAL PRO ASN TYR ASN LEU ILE VAL MET ASP
SEQRES 10 B 451 GLU ALA HIS PHE THR ASP PRO CYS SER VAL ALA ALA ARG
SEQRES 11 B 451 GLY TYR ILE SER THR ARG VAL GLU MET GLY GLU ALA ALA
SEQRES 12 B 451 ALA ILE PHE MET THR ALA THR PRO PRO GLY SER THR ASP
SEQRES 13 B 451 PRO PHE PRO GLN SER ASN SER PRO ILE GLU ASP ILE GLU
SEQRES 14 B 451 ARG GLU ILE PRO GLU ARG SER TRP ASN THR GLY PHE ASP
SEQRES 15 B 451 TRP ILE THR ASP TYR GLN GLY LYS THR VAL TRP PHE VAL
SEQRES 16 B 451 PRO SER ILE LYS ALA GLY ASN ASP ILE ALA ASN CYS LEU
SEQRES 17 B 451 ARG LYS SER GLY LYS ARG VAL ILE GLN LEU SER ARG LYS
SEQRES 18 B 451 THR PHE ASP THR GLU TYR PRO LYS THR LYS LEU THR ASP
SEQRES 19 B 451 TRP ASP PHE VAL VAL THR THR ASP ILE SER GLU MET GLY
SEQRES 20 B 451 ALA ASN PHE ARG ALA GLY ARG VAL ILE ASP PRO ARG ARG
SEQRES 21 B 451 CYS LEU LYS PRO VAL ILE LEU THR ASP GLY PRO GLU ARG
SEQRES 22 B 451 VAL ILE LEU ALA GLY PRO ILE PRO VAL THR PRO ALA SER
SEQRES 23 B 451 ALA ALA GLN ARG ARG GLY ARG ILE GLY ARG ASN PRO ALA
SEQRES 24 B 451 GLN GLU ASP ASP GLN TYR VAL PHE SER GLY ASP PRO LEU
SEQRES 25 B 451 LYS ASN ASP GLU ASP HIS ALA HIS TRP THR GLU ALA LYS
SEQRES 26 B 451 MET LEU LEU ASP ASN ILE TYR THR PRO GLU GLY ILE ILE
SEQRES 27 B 451 PRO THR LEU PHE GLY PRO GLU ARG GLU LYS THR GLN ALA
SEQRES 28 B 451 ILE ASP GLY GLU PHE ARG LEU ARG GLY GLU GLN ARG LYS
SEQRES 29 B 451 THR PHE VAL GLU LEU MET ARG ARG GLY ASP LEU PRO VAL
SEQRES 30 B 451 TRP LEU SER TYR LYS VAL ALA SER ALA GLY ILE SER TYR
SEQRES 31 B 451 LYS ASP ARG GLU TRP CYS PHE THR GLY GLU ARG ASN ASN
SEQRES 32 B 451 GLN ILE LEU GLU GLU ASN MET GLU VAL GLU ILE TRP THR
SEQRES 33 B 451 ARG GLU GLY GLU LYS LYS LYS LEU ARG PRO LYS TRP LEU
SEQRES 34 B 451 ASP ALA ARG VAL TYR ALA ASP PRO MET ALA LEU LYS ASP
SEQRES 35 B 451 PHE LYS GLU PHE ALA SER GLY ARG LYS
SEQRES 1 C 12 A G A C U A A C A A C U
SEQRES 1 D 12 A G A C U A A C A A C U
HET ADP A1619 27
HET PO4 A1620 5
HET MN A1621 1
HET GOL A1622 6
HET ADP B1619 27
HET PO4 B1620 5
HET MN B1621 1
HET GOL B1622 6
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM PO4 PHOSPHATE ION
HETNAM MN MANGANESE (II) ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 ADP 2(C10 H15 N5 O10 P2)
FORMUL 6 PO4 2(O4 P 3-)
FORMUL 7 MN 2(MN 2+)
FORMUL 8 GOL 2(C3 H8 O3)
FORMUL 13 HOH *380(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 ARG A 236 1 13
HELIX 4 4 HIS A 262 SER A 271 1 10
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 LYS A 398 1 10
HELIX 9 9 ASP A 409 GLU A 412 5 4
HELIX 10 10 THR A 450 GLY A 459 1 10
HELIX 11 11 ALA A 486 ASP A 496 1 11
HELIX 12 12 PHE A 509 ARG A 513 5 5
HELIX 13 13 ARG A 526 ARG A 539 1 14
HELIX 14 14 PRO A 543 ALA A 553 1 11
HELIX 15 15 ARG A 560 PHE A 564 5 5
HELIX 16 16 GLU A 567 GLN A 571 5 5
HELIX 17 17 ALA A 598 TYR A 601 5 4
HELIX 18 18 ASP A 603 GLY A 616 1 14
HELIX 19 19 ASP B 179 ARG B 184 5 6
HELIX 20 20 ARG B 202 ARG B 214 1 13
HELIX 21 21 THR B 224 ARG B 236 1 13
HELIX 22 22 HIS B 262 SER B 271 1 10
HELIX 23 23 ASP B 290 MET B 306 1 17
HELIX 24 24 PHE B 348 TYR B 354 1 7
HELIX 25 25 SER B 364 LYS B 377 1 14
HELIX 26 26 THR B 389 LYS B 398 1 10
HELIX 27 27 ASP B 409 GLU B 412 5 4
HELIX 28 28 THR B 450 GLY B 459 1 10
HELIX 29 29 ALA B 486 ASP B 496 1 11
HELIX 30 30 PHE B 509 ARG B 513 5 5
HELIX 31 31 ARG B 526 ARG B 539 1 14
HELIX 32 32 PRO B 543 ALA B 553 1 11
HELIX 33 33 ARG B 560 PHE B 564 5 5
HELIX 34 34 GLU B 567 GLN B 571 5 5
HELIX 35 35 ALA B 598 TYR B 601 5 4
HELIX 36 36 ASP B 603 GLY B 616 1 14
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
SHEET 1 BA 6 LEU B 188 MET B 191 0
SHEET 2 BA 6 ALA B 310 MET B 314 1 O ALA B 311 N THR B 189
SHEET 3 BA 6 LEU B 280 ASP B 284 1 O ILE B 281 N ILE B 312
SHEET 4 BA 6 THR B 218 ALA B 222 1 O LEU B 219 N VAL B 282
SHEET 5 BA 6 VAL B 257 CYS B 261 1 O ASP B 258 N ILE B 220
SHEET 6 BA 6 ILE B 240 TYR B 242 1 O ARG B 241 N LEU B 259
SHEET 1 BB 6 ILE B 332 GLU B 336 0
SHEET 2 BB 6 ASP B 470 PHE B 474 1 O ASP B 470 N GLU B 333
SHEET 3 BB 6 ARG B 421 ASP B 424 1 O VAL B 422 N VAL B 473
SHEET 4 BB 6 THR B 358 PHE B 361 1 O VAL B 359 N ILE B 423
SHEET 5 BB 6 PHE B 404 THR B 407 1 O VAL B 405 N TRP B 360
SHEET 6 BB 6 VAL B 382 LEU B 385 1 O ILE B 383 N VAL B 406
SHEET 1 BC 2 ARG B 427 LEU B 434 0
SHEET 2 BC 2 ARG B 440 PRO B 448 -1 O ARG B 440 N LEU B 434
SHEET 1 BD 2 LEU B 573 GLU B 574 0
SHEET 2 BD 2 MET B 577 GLU B 578 -1 O MET B 577 N GLU B 574
SHEET 1 BE 2 GLU B 580 TRP B 582 0
SHEET 2 BE 2 LYS B 588 LYS B 590 -1 O LYS B 589 N ILE B 581
LINK OG1 THR A 200 MN MN A1621 1555 1555 2.14
LINK O1B ADP A1619 MN MN A1621 1555 1555 2.12
LINK MN MN A1621 O HOH A2186 1555 1555 2.09
LINK MN MN A1621 O HOH A2187 1555 1555 2.09
LINK MN MN A1621 O HOH A2188 1555 1555 2.15
LINK MN MN A1621 O HOH A2189 1555 1555 2.02
LINK OG1 THR B 200 MN MN B1621 1555 1555 2.12
LINK O1B ADP B1619 MN MN B1621 1555 1555 2.22
LINK MN MN B1621 O HOH B2179 1555 1555 2.20
LINK MN MN B1621 O HOH B2180 1555 1555 2.12
LINK MN MN B1621 O HOH B2181 1555 1555 2.11
LINK MN MN B1621 O HOH B2182 1555 1555 2.08
CISPEP 1 GLY A 445 PRO A 446 0 3.35
CISPEP 2 GLY B 445 PRO B 446 0 5.51
CISPEP 3 ILE B 519 ASP B 520 0 -21.48
SITE 1 AC1 14 GLY A 196 ALA A 197 GLY A 198 LYS A 199
SITE 2 AC1 14 THR A 200 LYS A 201 ASN A 329 ASN A 416
SITE 3 AC1 14 ARG A 418 ARG A 463 PO4 A1620 MN A1621
SITE 4 AC1 14 HOH A2188 HOH A2189
SITE 1 AC2 12 HIS A 194 PRO A 195 LYS A 199 GLU A 285
SITE 2 AC2 12 ALA A 316 GLN A 456 ARG A 460 ARG A 463
SITE 3 AC2 12 ADP A1619 HOH A2184 HOH A2185 HOH A2189
SITE 1 AC3 7 THR A 200 GLU A 285 ADP A1619 HOH A2186
SITE 2 AC3 7 HOH A2187 HOH A2188 HOH A2189
SITE 1 AC4 8 GLY A 168 PRO A 174 TYR A 176 ILE A 442
SITE 2 AC4 8 LEU A 443 ALA A 598 ALA A 602 HOH A2003
SITE 1 AC5 13 GLY B 196 ALA B 197 GLY B 198 LYS B 199
SITE 2 AC5 13 THR B 200 LYS B 201 ASN B 329 ASN B 416
SITE 3 AC5 13 ARG B 463 PO4 B1620 MN B1621 HOH B2181
SITE 4 AC5 13 HOH B2182
SITE 1 AC6 12 HIS B 194 PRO B 195 LYS B 199 GLU B 285
SITE 2 AC6 12 ALA B 316 GLN B 456 ARG B 460 ARG B 463
SITE 3 AC6 12 ADP B1619 HOH B2177 HOH B2178 HOH B2181
SITE 1 AC7 7 THR B 200 GLU B 285 ADP B1619 HOH B2179
SITE 2 AC7 7 HOH B2180 HOH B2181 HOH B2182
SITE 1 AC8 7 GLY B 168 GLU B 173 TYR B 176 ILE B 442
SITE 2 AC8 7 LEU B 443 ALA B 598 ALA B 602
CRYST1 131.748 105.591 72.671 90.00 117.68 90.00 C 1 2 1 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 0.007590 0.000000 0.003982 0.00000
SCALE2 0.000000 0.009471 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015539 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
