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HEADER HYDROLASE 08-AUG-07 2QVB
TITLE CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE RV2579 FROM
TITLE 2 MYCOBACTERIUM TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE 3;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: DHAA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PDEST-15
KEYWDS RV2579, HALOALKANE DEHALOGENASE, ALPHA-BETA HYDROLASE
KEYWDS 2 PROTEIN, X-RAY CRYSTALLOGRAPHY, TB STRUCTURAL GENOMICS
KEYWDS 3 CONSORTIUM, TBSGC
EXPDTA X-RAY DIFFRACTION
AUTHOR P.A.MAZUMDAR,J.HULECKI,M.M.CHERNEY,C.R.GAREN,M.N.G.JAMES,TB
AUTHOR 2 STRUCTURAL GENOMICS CONSORTIUM (TBSGC)
REVDAT 1 12-FEB-08 2QVB 0
JRNL AUTH P.A.MAZUMDAR,J.C.HULECKI,M.M.CHERNEY,C.R.GAREN,
JRNL AUTH 2 M.N.JAMES
JRNL TITL X-RAY CRYSTAL STRUCTURE OF MYCOBACTERIUM
JRNL TITL 2 TUBERCULOSIS HALOALKANE DEHALOGENASE RV2579.
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1784 351 2008
JRNL REFN ASTM BBACAQ NE ISSN 0006-3002
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.11
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 127495
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.120
REMARK 3 FREE R VALUE : 0.160
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6695
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.19
REMARK 3 BIN RESOLUTION RANGE LOW : 1.22
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7010
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1500
REMARK 3 BIN FREE R VALUE SET COUNT : 337
REMARK 3 BIN FREE R VALUE : 0.2000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 5421
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.041
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.042
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.023
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.138
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.978
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.968
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4873 ; 0.026 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3380 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6617 ; 2.177 ; 1.947
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8144 ; 1.192 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 595 ; NULL ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 236 ; NULL ;22.627
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 754 ; NULL ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 48 ; NULL ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 682 ; NULL ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5487 ; NULL ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1067 ; NULL ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 975 ; NULL ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3719 ; NULL ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2396 ; NULL ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2520 ; NULL ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 404 ; NULL ; 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): 15 ; NULL ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 89 ; NULL ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 52 ; NULL ; 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): 3036 ; NULL ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1203 ; NULL ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4772 ; NULL ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2123 ; NULL ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1845 ; NULL ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 9463 ; NULL ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 676 ; NULL ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 8117 ; NULL ; 3.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2QVB COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB044100.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-2006
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 8.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.115869
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 134255
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.190
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 81.1
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.05300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.19
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 62.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.27800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: PDB ENTRY 1MJ5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, MAGNESIUM ACETATE, 0.1M
REMARK 280 TRIS, 5% ETHYLENE GLYCOL , PH 8.5, VAPOR DIFFUSION, HANGING
REMARK 280 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 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-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 30.35000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.85000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.85000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.85000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.35000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.85000
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: MONOMER
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMER
REMARK 350 SOFTWARE USED: PISA
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMER
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 ALA A 3 N CA CB
REMARK 470 GLU A 7 CG CD OE1 OE2
REMARK 470 GLN A 11 CB CG CD OE1 NE2
REMARK 470 ASP A 79 OD2
REMARK 470 ASP A 124 OD2
REMARK 470 GLN A 153 CG CD NE2
REMARK 470 GLN A 182 CG CD OE1 NE2
REMARK 470 GLU A 186 CD OE1 OE2
REMARK 470 ARG A 193 NH1
REMARK 470 GLU A 227 CD OE2
REMARK 470 ASP A 236 OD1 OD2
REMARK 470 GLU A 281 OE2
REMARK 470 PHE B 4 CD1 CE1
REMARK 470 GLU B 7 CG CD OE2
REMARK 470 GLY B 10 O
REMARK 470 GLN B 11 CG CD OE1 NE2
REMARK 470 LYS B 20 NZ
REMARK 470 LYS B 29 NZ
REMARK 470 ASP B 79 OD2
REMARK 470 ASP B 124 OD2
REMARK 470 GLN B 182 CD NE2
REMARK 470 GLU B 227 CD OE2
REMARK 470 ASP B 236 OD1
REMARK 470 GLU B 281 CD OE1 OE2
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 GLY A 28 O
REMARK 480 LEU A 224 CD1
REMARK 480 MET A 237 CE
REMARK 480 LYS B 29 CE
REMARK 480 ASP B 31 CB CG OD1 OD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLY A 28 C GLY A 28 O 0.124
REMARK 500 ASP A 79 CB ASP A 79 CG 0.151
REMARK 500 ASP A 79 CG ASP A 79 OD1 0.147
REMARK 500 ARG A 87 CZ ARG A 87 NH1 0.095
REMARK 500 VAL A 151 CB VAL A 151 CG1 -0.149
REMARK 500 GLU A 220 CD GLU A 220 OE2 0.135
REMARK 500 GLU A 233 CG GLU A 233 CD 0.103
REMARK 500 GLU A 266 CD GLU A 266 OE1 0.070
REMARK 500 GLU B 54 CD GLU B 54 OE2 0.070
REMARK 500 ASP B 79 CB ASP B 79 CG 0.134
REMARK 500 VAL B 151 CB VAL B 151 CG1 -0.134
REMARK 500 GLU B 220 CD GLU B 220 OE2 0.090
REMARK 500 ARG B 253 NE ARG B 253 CZ 0.123
REMARK 500 ARG B 253 CZ ARG B 253 NH2 0.088
REMARK 500 ARG B 295 CZ ARG B 295 NH2 0.083
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 NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLU A 27 OE1 - CD - OE2 ANGL. DEV. = -8.9 DEGREES
REMARK 500 LYS A 29 CB - CA - C ANGL. DEV. = -12.2 DEGREES
REMARK 500 ARG A 58 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ASP A 71 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 79 CB - CG - OD1 ANGL. DEV. = 9.8 DEGREES
REMARK 500 ARG A 87 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG A 87 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG A 156 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG A 202 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 MET A 237 CG - SD - CE ANGL. DEV. = -19.3 DEGREES
REMARK 500 ARG A 253 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 292 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG A 295 NE - CZ - NH1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG B 21 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG B 47 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ASP B 79 CB - CG - OD1 ANGL. DEV. = 10.7 DEGREES
REMARK 500 ARG B 87 NE - CZ - NH2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP B 109 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG B 123 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG B 123 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG B 193 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 MET B 237 CG - SD - CE ANGL. DEV. = -18.2 DEGREES
REMARK 500 ARG B 253 NH1 - CZ - NH2 ANGL. DEV. = -8.2 DEGREES
REMARK 500 ARG B 253 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG B 253 NE - CZ - NH2 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG B 293 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG B 293 NE - CZ - NH2 ANGL. DEV. = -3.8 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 PRO A 40 52.34 -105.14
REMARK 500 THR A 41 -160.21 -102.94
REMARK 500 ASP A 109 -132.42 57.77
REMARK 500 ALA A 248 -71.71 -144.56
REMARK 500 VAL A 272 -91.84 -107.23
REMARK 500 PHE B 4 68.14 -107.45
REMARK 500 PRO B 40 52.30 -107.21
REMARK 500 THR B 41 -161.37 -105.87
REMARK 500 ASP B 109 -132.08 52.63
REMARK 500 ARG B 156 37.45 -88.48
REMARK 500 ALA B 248 -65.38 -147.25
REMARK 500 VAL B 272 -88.16 -109.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLY A 28 16.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: CL BINDING SITE FOR RESIDUE A 2
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: CL BINDING SITE FOR RESIDUE B 2
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: EDO BINDING SITE FOR RESIDUE A 1
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: EDO BINDING SITE FOR RESIDUE B 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: RV2579 RELATED DB: TARGETDB
DBREF 2QVB A 3 299 UNP Q50642 DHAA_MYCTU 3 299
DBREF 2QVB B 3 299 UNP Q50642 DHAA_MYCTU 3 299
SEQRES 1 A 297 ALA PHE GLY VAL GLU PRO TYR GLY GLN PRO LYS TYR LEU
SEQRES 2 A 297 GLU ILE ALA GLY LYS ARG MET ALA TYR ILE ASP GLU GLY
SEQRES 3 A 297 LYS GLY ASP ALA ILE VAL PHE GLN HIS GLY ASN PRO THR
SEQRES 4 A 297 SER SER TYR LEU TRP ARG ASN ILE MET PRO HIS LEU GLU
SEQRES 5 A 297 GLY LEU GLY ARG LEU VAL ALA CYS ASP LEU ILE GLY MET
SEQRES 6 A 297 GLY ALA SER ASP LYS LEU SER PRO SER GLY PRO ASP ARG
SEQRES 7 A 297 TYR SER TYR GLY GLU GLN ARG ASP PHE LEU PHE ALA LEU
SEQRES 8 A 297 TRP ASP ALA LEU ASP LEU GLY ASP HIS VAL VAL LEU VAL
SEQRES 9 A 297 LEU HIS ASP TRP GLY SER ALA LEU GLY PHE ASP TRP ALA
SEQRES 10 A 297 ASN GLN HIS ARG ASP ARG VAL GLN GLY ILE ALA PHE MET
SEQRES 11 A 297 GLU ALA ILE VAL THR PRO MET THR TRP ALA ASP TRP PRO
SEQRES 12 A 297 PRO ALA VAL ARG GLY VAL PHE GLN GLY PHE ARG SER PRO
SEQRES 13 A 297 GLN GLY GLU PRO MET ALA LEU GLU HIS ASN ILE PHE VAL
SEQRES 14 A 297 GLU ARG VAL LEU PRO GLY ALA ILE LEU ARG GLN LEU SER
SEQRES 15 A 297 ASP GLU GLU MET ASN HIS TYR ARG ARG PRO PHE VAL ASN
SEQRES 16 A 297 GLY GLY GLU ASP ARG ARG PRO THR LEU SER TRP PRO ARG
SEQRES 17 A 297 ASN LEU PRO ILE ASP GLY GLU PRO ALA GLU VAL VAL ALA
SEQRES 18 A 297 LEU VAL ASN GLU TYR ARG SER TRP LEU GLU GLU THR ASP
SEQRES 19 A 297 MET PRO LYS LEU PHE ILE ASN ALA GLU PRO GLY ALA ILE
SEQRES 20 A 297 ILE THR GLY ARG ILE ARG ASP TYR VAL ARG SER TRP PRO
SEQRES 21 A 297 ASN GLN THR GLU ILE THR VAL PRO GLY VAL HIS PHE VAL
SEQRES 22 A 297 GLN GLU ASP SER PRO GLU GLU ILE GLY ALA ALA ILE ALA
SEQRES 23 A 297 GLN PHE VAL ARG ARG LEU ARG SER ALA ALA GLY
SEQRES 1 B 297 ALA PHE GLY VAL GLU PRO TYR GLY GLN PRO LYS TYR LEU
SEQRES 2 B 297 GLU ILE ALA GLY LYS ARG MET ALA TYR ILE ASP GLU GLY
SEQRES 3 B 297 LYS GLY ASP ALA ILE VAL PHE GLN HIS GLY ASN PRO THR
SEQRES 4 B 297 SER SER TYR LEU TRP ARG ASN ILE MET PRO HIS LEU GLU
SEQRES 5 B 297 GLY LEU GLY ARG LEU VAL ALA CYS ASP LEU ILE GLY MET
SEQRES 6 B 297 GLY ALA SER ASP LYS LEU SER PRO SER GLY PRO ASP ARG
SEQRES 7 B 297 TYR SER TYR GLY GLU GLN ARG ASP PHE LEU PHE ALA LEU
SEQRES 8 B 297 TRP ASP ALA LEU ASP LEU GLY ASP HIS VAL VAL LEU VAL
SEQRES 9 B 297 LEU HIS ASP TRP GLY SER ALA LEU GLY PHE ASP TRP ALA
SEQRES 10 B 297 ASN GLN HIS ARG ASP ARG VAL GLN GLY ILE ALA PHE MET
SEQRES 11 B 297 GLU ALA ILE VAL THR PRO MET THR TRP ALA ASP TRP PRO
SEQRES 12 B 297 PRO ALA VAL ARG GLY VAL PHE GLN GLY PHE ARG SER PRO
SEQRES 13 B 297 GLN GLY GLU PRO MET ALA LEU GLU HIS ASN ILE PHE VAL
SEQRES 14 B 297 GLU ARG VAL LEU PRO GLY ALA ILE LEU ARG GLN LEU SER
SEQRES 15 B 297 ASP GLU GLU MET ASN HIS TYR ARG ARG PRO PHE VAL ASN
SEQRES 16 B 297 GLY GLY GLU ASP ARG ARG PRO THR LEU SER TRP PRO ARG
SEQRES 17 B 297 ASN LEU PRO ILE ASP GLY GLU PRO ALA GLU VAL VAL ALA
SEQRES 18 B 297 LEU VAL ASN GLU TYR ARG SER TRP LEU GLU GLU THR ASP
SEQRES 19 B 297 MET PRO LYS LEU PHE ILE ASN ALA GLU PRO GLY ALA ILE
SEQRES 20 B 297 ILE THR GLY ARG ILE ARG ASP TYR VAL ARG SER TRP PRO
SEQRES 21 B 297 ASN GLN THR GLU ILE THR VAL PRO GLY VAL HIS PHE VAL
SEQRES 22 B 297 GLN GLU ASP SER PRO GLU GLU ILE GLY ALA ALA ILE ALA
SEQRES 23 B 297 GLN PHE VAL ARG ARG LEU ARG SER ALA ALA GLY
HET CL A 2 1
HET CL B 2 1
HET EDO A 1 8
HET EDO B 1 8
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 CL 2(CL 1-)
FORMUL 5 EDO 2(C2 H6 O2)
FORMUL 7 HOH *669(H2 O)
HELIX 1 1 SER A 42 ARG A 47 5 6
HELIX 2 2 ILE A 49 GLU A 54 5 6
HELIX 3 3 SER A 82 LEU A 97 1 16
HELIX 4 4 ASP A 109 HIS A 122 1 14
HELIX 5 5 THR A 140 TRP A 144 5 5
HELIX 6 6 PRO A 145 ALA A 147 5 3
HELIX 7 7 VAL A 148 ARG A 156 1 9
HELIX 8 8 GLN A 159 GLU A 166 1 8
HELIX 9 9 ASN A 168 ARG A 173 1 6
HELIX 10 10 ARG A 173 ALA A 178 1 6
HELIX 11 11 SER A 184 ARG A 193 1 10
HELIX 12 12 PRO A 194 VAL A 196 5 3
HELIX 13 13 GLY A 199 ASP A 201 5 3
HELIX 14 14 ARG A 202 LEU A 212 1 11
HELIX 15 15 PRO A 218 THR A 235 1 18
HELIX 16 16 THR A 251 SER A 260 1 10
HELIX 17 17 PHE A 274 ASP A 278 5 5
HELIX 18 18 SER A 279 ALA A 298 1 20
HELIX 19 19 SER B 42 ARG B 47 5 6
HELIX 20 20 ILE B 49 GLU B 54 5 6
HELIX 21 21 SER B 82 LEU B 97 1 16
HELIX 22 22 ASP B 109 HIS B 122 1 14
HELIX 23 23 THR B 140 TRP B 144 5 5
HELIX 24 24 PRO B 145 ALA B 147 5 3
HELIX 25 25 VAL B 148 ARG B 156 1 9
HELIX 26 26 GLN B 159 GLU B 166 1 8
HELIX 27 27 ASN B 168 ARG B 173 1 6
HELIX 28 28 ARG B 173 ALA B 178 1 6
HELIX 29 29 SER B 184 ARG B 193 1 10
HELIX 30 30 PRO B 194 VAL B 196 5 3
HELIX 31 31 GLY B 199 ASP B 201 5 3
HELIX 32 32 ARG B 202 LEU B 212 1 11
HELIX 33 33 PRO B 218 THR B 235 1 18
HELIX 34 34 THR B 251 SER B 260 1 10
HELIX 35 35 PHE B 274 ASP B 278 5 5
HELIX 36 36 SER B 279 GLY B 299 1 21
SHEET 1 A 8 LYS A 13 ILE A 17 0
SHEET 2 A 8 LYS A 20 GLU A 27 -1 O LYS A 20 N ILE A 17
SHEET 3 A 8 ARG A 58 CYS A 62 -1 O LEU A 59 N GLU A 27
SHEET 4 A 8 ALA A 32 GLN A 36 1 N ILE A 33 O ARG A 58
SHEET 5 A 8 VAL A 103 HIS A 108 1 O VAL A 106 N VAL A 34
SHEET 6 A 8 VAL A 126 MET A 132 1 O ALA A 130 N LEU A 105
SHEET 7 A 8 LYS A 239 PRO A 246 1 O ILE A 242 N PHE A 131
SHEET 8 A 8 GLN A 264 GLY A 271 1 O THR A 265 N PHE A 241
SHEET 1 B 8 LYS B 13 ILE B 17 0
SHEET 2 B 8 LYS B 20 GLU B 27 -1 O LYS B 20 N ILE B 17
SHEET 3 B 8 ARG B 58 CYS B 62 -1 O LEU B 59 N GLU B 27
SHEET 4 B 8 ALA B 32 GLN B 36 1 N PHE B 35 O VAL B 60
SHEET 5 B 8 VAL B 103 HIS B 108 1 O VAL B 106 N VAL B 34
SHEET 6 B 8 VAL B 126 MET B 132 1 O ALA B 130 N LEU B 105
SHEET 7 B 8 LYS B 239 PRO B 246 1 O ILE B 242 N PHE B 131
SHEET 8 B 8 GLN B 264 GLY B 271 1 O THR B 265 N PHE B 241
CISPEP 1 ASN A 39 PRO A 40 0 -6.10
CISPEP 2 SER A 74 PRO A 75 0 -16.24
CISPEP 3 GLU A 217 PRO A 218 0 -4.47
CISPEP 4 GLU A 245 PRO A 246 0 4.73
CISPEP 5 ASN B 39 PRO B 40 0 -3.35
CISPEP 6 SER B 74 PRO B 75 0 -5.05
CISPEP 7 GLU B 217 PRO B 218 0 -6.60
CISPEP 8 GLU B 245 PRO B 246 0 7.30
SITE 1 AC1 5 ASN A 39 TRP A 110 TRP A 208 PRO A 209
SITE 2 AC1 5 HOH A 632
SITE 1 AC2 5 ASN B 39 TRP B 110 TRP B 208 PRO B 209
SITE 2 AC2 5 HOH B 629
SITE 1 AC3 2 HIS A 273 HOH A 637
SITE 1 AC4 2 HIS B 273 HOH B 630
CRYST1 60.700 65.700 129.700 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 0.016482 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015229 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007713 0.00000
END |