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HEADER HYDROLASE 29-NOV-06 2O2H
TITLE CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE RV2579 FROM
TITLE 2 MYCOBACTERIUM TUBERCULOSIS COMPLEXED WITH 1,2-
TITLE 3 DICHLOROETHANE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE 3;
COMPND 3 CHAIN: A;
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 HALOALKANE DEHALOGENASE, MYCOBACTERIUM TUBERCULOSIS, RV2579,
KEYWDS 2 ALPHA/BETA-HYDROLASE PROTEIN, 1,2-DICHLOROETHANE, X-RAY
KEYWDS 3 CRYSTALLOGRAPHY, TB STRUCTURAL GENOMICS 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 13-NOV-07 2O2H 0
JRNL AUTH P.A.MAZUMDAR,J.HULECKI,M.M.CHERNEY,C.R.GAREN,
JRNL AUTH 2 M.N.G.JAMES
JRNL TITL CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE
JRNL TITL 2 RV2579 FROM MYCOBACTERIUM TUBERCULOSIS COMPLEXED
JRNL TITL 3 WITH 1,2-DICHLOROETHANE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.60 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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.26
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 35833
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) : 0.145
REMARK 3 R VALUE (WORKING SET) : 0.143
REMARK 3 FREE R VALUE : 0.173
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1794
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2473
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.58
REMARK 3 BIN R VALUE (WORKING SET) : 0.1770
REMARK 3 BIN FREE R VALUE SET COUNT : 125
REMARK 3 BIN FREE R VALUE : 0.2700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 2579
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.077
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.078
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.048
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.359
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.962
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2411 ; 0.023 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1665 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3276 ; 1.942 ; 1.947
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4013 ; 1.093 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 293 ; 6.369 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 117 ;32.236 ;22.906
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 371 ;11.703 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;16.289 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 339 ; 0.123 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2712 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 521 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 477 ; 0.226 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1783 ; 0.215 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1176 ; 0.192 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1235 ; 0.091 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 167 ; 0.169 ; 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): 11 ; 0.303 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 34 ; 0.359 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.213 ; 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): 1588 ; 1.412 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 592 ; 0.400 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2362 ; 1.810 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1056 ; 2.756 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 914 ; 4.023 ; 4.500
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 : 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 2O2H COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB040603.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-MAY-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 : SSRL
REMARK 200 BEAMLINE : BL9-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979462
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35880
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
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 (%) : 99.6
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.55400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.280
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 (%): 38.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000, 0.2M MAGNESIUM
REMARK 280 ACETATE, 0.1M TRIS, 5% ETHYLENE GLYCOL, PH 8.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,1/2+Z
REMARK 290 3555 -X,Y,1/2-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 1/2+X,1/2+Y,Z
REMARK 290 6555 1/2-X,1/2-Y,1/2+Z
REMARK 290 7555 1/2-X,1/2+Y,1/2-Z
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 67.10500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 67.10500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 31.06000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 32.23000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 31.06000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 32.23000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 67.10500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 31.06000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 32.23000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 67.10500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 31.06000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 32.23000
REMARK 290 SMTRY3 8 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 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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 511 LIES ON A SPECIAL POSITION.
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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 298
REMARK 465 GLY A 299
REMARK 465 VAL A 300
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 GLU A 7 CG CD OE1 OE2
REMARK 470 GLN A 11 CD OE1 NE2
REMARK 470 ASP A 79 OD2
REMARK 470 ARG A 193 CZ NH1 NH2
REMARK 470 GLU A 227 CD OE1 OE2
REMARK 470 GLU A 245 OE2
REMARK 470 GLU A 281 CG CD OE1 OE2
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
REMARK 500 O HOH A 426 O HOH A 460 1.85
REMARK 500
REMARK 500 REMARK: NULL
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 GLU A 234 CG GLU A 234 CD 0.101
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 ARG A 87 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG A 87 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 192 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 203 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 255 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 255 NE - CZ - NH2 ANGL. DEV. = -4.4 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 52.50 -107.05
REMARK 500 THR A 41 -160.02 -108.01
REMARK 500 ASP A 109 -131.50 60.52
REMARK 500 ARG A 156 40.04 -86.98
REMARK 500 ARG A 173 -50.03 -123.21
REMARK 500 ALA A 248 -69.11 -150.16
REMARK 500 VAL A 272 -89.20 -114.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: RV2579 RELATED DB: TARGETDB
REMARK 900 RELATED ID: 2O2I RELATED DB: PDB
DBREF 2O2H A 1 300 UNP Q50642 DHAA_MYCTU 1 300
SEQRES 1 A 300 MET THR ALA PHE GLY VAL GLU PRO TYR GLY GLN PRO LYS
SEQRES 2 A 300 TYR LEU GLU ILE ALA GLY LYS ARG MET ALA TYR ILE ASP
SEQRES 3 A 300 GLU GLY LYS GLY ASP ALA ILE VAL PHE GLN HIS GLY ASN
SEQRES 4 A 300 PRO THR SER SER TYR LEU TRP ARG ASN ILE MET PRO HIS
SEQRES 5 A 300 LEU GLU GLY LEU GLY ARG LEU VAL ALA CYS ASP LEU ILE
SEQRES 6 A 300 GLY MET GLY ALA SER ASP LYS LEU SER PRO SER GLY PRO
SEQRES 7 A 300 ASP ARG TYR SER TYR GLY GLU GLN ARG ASP PHE LEU PHE
SEQRES 8 A 300 ALA LEU TRP ASP ALA LEU ASP LEU GLY ASP HIS VAL VAL
SEQRES 9 A 300 LEU VAL LEU HIS ASP TRP GLY SER ALA LEU GLY PHE ASP
SEQRES 10 A 300 TRP ALA ASN GLN HIS ARG ASP ARG VAL GLN GLY ILE ALA
SEQRES 11 A 300 PHE MET GLU ALA ILE VAL THR PRO MET THR TRP ALA ASP
SEQRES 12 A 300 TRP PRO PRO ALA VAL ARG GLY VAL PHE GLN GLY PHE ARG
SEQRES 13 A 300 SER PRO GLN GLY GLU PRO MET ALA LEU GLU HIS ASN ILE
SEQRES 14 A 300 PHE VAL GLU ARG VAL LEU PRO GLY ALA ILE LEU ARG GLN
SEQRES 15 A 300 LEU SER ASP GLU GLU MET ASN HIS TYR ARG ARG PRO PHE
SEQRES 16 A 300 VAL ASN GLY GLY GLU ASP ARG ARG PRO THR LEU SER TRP
SEQRES 17 A 300 PRO ARG ASN LEU PRO ILE ASP GLY GLU PRO ALA GLU VAL
SEQRES 18 A 300 VAL ALA LEU VAL ASN GLU TYR ARG SER TRP LEU GLU GLU
SEQRES 19 A 300 THR ASP MET PRO LYS LEU PHE ILE ASN ALA GLU PRO GLY
SEQRES 20 A 300 ALA ILE ILE THR GLY ARG ILE ARG ASP TYR VAL ARG SER
SEQRES 21 A 300 TRP PRO ASN GLN THR GLU ILE THR VAL PRO GLY VAL HIS
SEQRES 22 A 300 PHE VAL GLN GLU ASP SER PRO GLU GLU ILE GLY ALA ALA
SEQRES 23 A 300 ILE ALA GLN PHE VAL ARG ARG LEU ARG SER ALA ALA GLY
SEQRES 24 A 300 VAL
HET CL A 301 1
HET ACT A 302 4
HET DCE A 303 8
HETNAM CL CHLORIDE ION
HETNAM ACT ACETATE ION
HETNAM DCE 1,2-DICHLOROETHANE
HETSYN DCE ETHYLENE DICHLORIDE
FORMUL 2 CL CL 1-
FORMUL 3 ACT C2 H3 O2 1-
FORMUL 4 DCE C2 H4 CL2
FORMUL 5 HOH *233(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 ASN A 211 1 10
HELIX 15 15 PRO A 218 GLU A 233 1 16
HELIX 16 16 THR A 251 ARG A 259 1 9
HELIX 17 17 PHE A 274 ASP A 278 5 5
HELIX 18 18 SER A 279 SER A 296 1 18
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 ILE A 267 N ASN A 243
CISPEP 1 ASN A 39 PRO A 40 0 -2.15
CISPEP 2 SER A 74 PRO A 75 0 -7.76
CISPEP 3 GLU A 217 PRO A 218 0 -4.75
CISPEP 4 GLU A 245 PRO A 246 0 3.50
CRYST1 62.120 64.460 134.210 90.00 90.00 90.00 C 2 2 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 0.016098 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015513 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007451 0.00000
TER 2334 ALA A 297
MASTER 358 0 3 18 8 0 0 6 2579 1 12 24
END |