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HEADER HYDROLASE 10-JUN-09 3HSS
TITLE A HIGHER RESOLUTION STRUCTURE OF RV0554 FROM MYCOBACTERIUM
TITLE 2 TUBERCULOSIS COMPLEXED WITH MALONIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE BROMOPEROXIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: POSSIBLE PEROXIDASE BPOC (NON-HAEM PEROXIDASE);
COMPND 5 EC: 1.11.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: BPOC, MT0580, RV0554;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA BETA HYDROLASE, OXIDOREDUCTASE, PEROXIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.JOHNSTON,E.N.BAKER
REVDAT 1 26-MAY-10 3HSS 0
JRNL AUTH J.M.JOHNSTON,M.JIANG,Z.GUO,E.N.BAKER
JRNL TITL STRUCTURAL AND FUNCTIONAL ANALYSIS OF RV0554 FROM
JRNL TITL 2 MYCOBACTERIUM TUBERCULOSIS, TESTING A PUTATIVE ROLE IN
JRNL TITL 3 MENAQUINONE BIOSYNTHESIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0078
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.32
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 54732
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2782
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3676
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.20
REMARK 3 BIN R VALUE (WORKING SET) : 0.2950
REMARK 3 BIN FREE R VALUE SET COUNT : 212
REMARK 3 BIN FREE R VALUE : 0.3280
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4092
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 59
REMARK 3 SOLVENT ATOMS : 516
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.11000
REMARK 3 B22 (A**2) : -0.11000
REMARK 3 B33 (A**2) : 0.22000
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): 0.140
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.127
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4269 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5807 ; 1.409 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 543 ; 5.082 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 193 ;32.683 ;23.109
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 636 ;12.453 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 38 ;17.599 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 642 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3343 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 2694 ; 0.843 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4325 ; 1.528 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1575 ; 2.526 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1479 ; 4.197 ; 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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 : 0.00
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3HSS COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUN-09.
REMARK 100 THE RCSB ID CODE IS RCSB053538.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 4.92
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95665
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54772
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
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 (%) : 99.0
REMARK 200 DATA REDUNDANCY : 29.100
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 52.9640
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 25.90
REMARK 200 R MERGE FOR SHELL (I) : 0.67800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 6.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 95% ( 0.1M NAACETATE PH 4.92, 2% MDP,
REMARK 280 15% ETHYLENE GLYCOL) WITH 5% 1.65M MALONIC ACID PROTEIN HAD PEP
REMARK 280 ADDED TO IT AS WELL. , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 67.58100
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 50.22700
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 50.22700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 33.79050
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 50.22700
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 50.22700
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 101.37150
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 50.22700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.22700
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 33.79050
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 50.22700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.22700
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 101.37150
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 67.58100
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 300 REMARK: THE PROTEIN IS MOSTLY A DIMER IN SOLUTION AND PISA PREDICTS
REMARK 300 A DIMER IS LIKELY IN THE CRYSTAL TOO. THIS DIMER IS CONSISTENT WITH
REMARK 300 THE ONE SEEN IN THE RELATED ENTRY STRUCTURE.
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: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 MET A -30
REMARK 465 SER A -29
REMARK 465 TYR A -28
REMARK 465 TYR A -27
REMARK 465 HIS A -26
REMARK 465 HIS A -25
REMARK 465 HIS A -24
REMARK 465 HIS A -23
REMARK 465 HIS A -22
REMARK 465 HIS A -21
REMARK 465 ASP A -20
REMARK 465 TYR A -19
REMARK 465 ASP A -18
REMARK 465 ILE A -17
REMARK 465 PRO A -16
REMARK 465 THR A -15
REMARK 465 THR A -14
REMARK 465 GLU A -13
REMARK 465 ALA A 262
REMARK 465 MET B -30
REMARK 465 SER B -29
REMARK 465 TYR B -28
REMARK 465 TYR B -27
REMARK 465 HIS B -26
REMARK 465 HIS B -25
REMARK 465 HIS B -24
REMARK 465 HIS B -23
REMARK 465 HIS B -22
REMARK 465 HIS B -21
REMARK 465 ASP B -20
REMARK 465 TYR B -19
REMARK 465 ASP B -18
REMARK 465 ILE B -17
REMARK 465 PRO B -16
REMARK 465 THR B -15
REMARK 465 THR B -14
REMARK 465 GLU B -13
REMARK 465 ASN B -12
REMARK 465 LEU B -11
REMARK 465 TYR B -10
REMARK 465 PHE B -9
REMARK 465 GLN B -8
REMARK 465 GLY B -7
REMARK 465 ALA B -6
REMARK 465 MET B -5
REMARK 465 ASP B -4
REMARK 465 PRO B -3
REMARK 465 GLU B -2
REMARK 465 PHE B -1
REMARK 465 ARG B 0
REMARK 465 VAL B 1
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 ARG A 26 CA CB CG CD NE CZ NH1
REMARK 480 ARG A 26 NH2
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 SER A 87 -118.07 53.10
REMARK 500 LEU A 240 39.64 -92.09
REMARK 500 SER B 87 -123.00 51.64
REMARK 500 LEU B 240 42.70 -98.94
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 NA A 268 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 223 O
REMARK 620 2 LEU A 226 O 85.5
REMARK 620 3 GLY A 229 O 88.8 100.9
REMARK 620 4 HOH A 544 O 112.7 94.2 154.7
REMARK 620 5 HOH A 537 O 90.2 175.6 80.1 86.4
REMARK 620 6 HOH A 538 O 160.6 93.5 72.3 86.6 90.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 264 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B 223 O
REMARK 620 2 LEU B 226 O 87.0
REMARK 620 3 GLY B 229 O 88.2 94.3
REMARK 620 4 HOH B 465 O 100.8 171.8 83.7
REMARK 620 5 HOH B 466 O 155.7 91.2 67.7 80.6
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 264
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLA A 5188
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 266
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 267
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 268
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 269
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 270
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLA B 5188
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 264
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLA B 265
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: RCSB048820 RELATED DB: PDB
REMARK 900 THE STRUCTURE OF RV0554 FROM MYCOBACTERIUM TUBERCULOSIS
DBREF 3HSS A 2 262 UNP O06420 O06420_MYCTU 2 262
DBREF 3HSS B 2 262 UNP O06420 O06420_MYCTU 2 262
SEQADV 3HSS MET A -30 UNP O06420 EXPRESSION TAG
SEQADV 3HSS SER A -29 UNP O06420 EXPRESSION TAG
SEQADV 3HSS TYR A -28 UNP O06420 EXPRESSION TAG
SEQADV 3HSS TYR A -27 UNP O06420 EXPRESSION TAG
SEQADV 3HSS HIS A -26 UNP O06420 EXPRESSION TAG
SEQADV 3HSS HIS A -25 UNP O06420 EXPRESSION TAG
SEQADV 3HSS HIS A -24 UNP O06420 EXPRESSION TAG
SEQADV 3HSS HIS A -23 UNP O06420 EXPRESSION TAG
SEQADV 3HSS HIS A -22 UNP O06420 EXPRESSION TAG
SEQADV 3HSS HIS A -21 UNP O06420 EXPRESSION TAG
SEQADV 3HSS ASP A -20 UNP O06420 EXPRESSION TAG
SEQADV 3HSS TYR A -19 UNP O06420 EXPRESSION TAG
SEQADV 3HSS ASP A -18 UNP O06420 EXPRESSION TAG
SEQADV 3HSS ILE A -17 UNP O06420 EXPRESSION TAG
SEQADV 3HSS PRO A -16 UNP O06420 EXPRESSION TAG
SEQADV 3HSS THR A -15 UNP O06420 EXPRESSION TAG
SEQADV 3HSS THR A -14 UNP O06420 EXPRESSION TAG
SEQADV 3HSS GLU A -13 UNP O06420 EXPRESSION TAG
SEQADV 3HSS ASN A -12 UNP O06420 EXPRESSION TAG
SEQADV 3HSS LEU A -11 UNP O06420 EXPRESSION TAG
SEQADV 3HSS TYR A -10 UNP O06420 EXPRESSION TAG
SEQADV 3HSS PHE A -9 UNP O06420 EXPRESSION TAG
SEQADV 3HSS GLN A -8 UNP O06420 EXPRESSION TAG
SEQADV 3HSS GLY A -7 UNP O06420 EXPRESSION TAG
SEQADV 3HSS ALA A -6 UNP O06420 EXPRESSION TAG
SEQADV 3HSS MET A -5 UNP O06420 EXPRESSION TAG
SEQADV 3HSS ASP A -4 UNP O06420 EXPRESSION TAG
SEQADV 3HSS PRO A -3 UNP O06420 EXPRESSION TAG
SEQADV 3HSS GLU A -2 UNP O06420 EXPRESSION TAG
SEQADV 3HSS PHE A -1 UNP O06420 EXPRESSION TAG
SEQADV 3HSS ARG A 0 UNP O06420 EXPRESSION TAG
SEQADV 3HSS VAL A 1 UNP O06420 EXPRESSION TAG
SEQADV 3HSS MET B -30 UNP O06420 EXPRESSION TAG
SEQADV 3HSS SER B -29 UNP O06420 EXPRESSION TAG
SEQADV 3HSS TYR B -28 UNP O06420 EXPRESSION TAG
SEQADV 3HSS TYR B -27 UNP O06420 EXPRESSION TAG
SEQADV 3HSS HIS B -26 UNP O06420 EXPRESSION TAG
SEQADV 3HSS HIS B -25 UNP O06420 EXPRESSION TAG
SEQADV 3HSS HIS B -24 UNP O06420 EXPRESSION TAG
SEQADV 3HSS HIS B -23 UNP O06420 EXPRESSION TAG
SEQADV 3HSS HIS B -22 UNP O06420 EXPRESSION TAG
SEQADV 3HSS HIS B -21 UNP O06420 EXPRESSION TAG
SEQADV 3HSS ASP B -20 UNP O06420 EXPRESSION TAG
SEQADV 3HSS TYR B -19 UNP O06420 EXPRESSION TAG
SEQADV 3HSS ASP B -18 UNP O06420 EXPRESSION TAG
SEQADV 3HSS ILE B -17 UNP O06420 EXPRESSION TAG
SEQADV 3HSS PRO B -16 UNP O06420 EXPRESSION TAG
SEQADV 3HSS THR B -15 UNP O06420 EXPRESSION TAG
SEQADV 3HSS THR B -14 UNP O06420 EXPRESSION TAG
SEQADV 3HSS GLU B -13 UNP O06420 EXPRESSION TAG
SEQADV 3HSS ASN B -12 UNP O06420 EXPRESSION TAG
SEQADV 3HSS LEU B -11 UNP O06420 EXPRESSION TAG
SEQADV 3HSS TYR B -10 UNP O06420 EXPRESSION TAG
SEQADV 3HSS PHE B -9 UNP O06420 EXPRESSION TAG
SEQADV 3HSS GLN B -8 UNP O06420 EXPRESSION TAG
SEQADV 3HSS GLY B -7 UNP O06420 EXPRESSION TAG
SEQADV 3HSS ALA B -6 UNP O06420 EXPRESSION TAG
SEQADV 3HSS MET B -5 UNP O06420 EXPRESSION TAG
SEQADV 3HSS ASP B -4 UNP O06420 EXPRESSION TAG
SEQADV 3HSS PRO B -3 UNP O06420 EXPRESSION TAG
SEQADV 3HSS GLU B -2 UNP O06420 EXPRESSION TAG
SEQADV 3HSS PHE B -1 UNP O06420 EXPRESSION TAG
SEQADV 3HSS ARG B 0 UNP O06420 EXPRESSION TAG
SEQADV 3HSS VAL B 1 UNP O06420 EXPRESSION TAG
SEQRES 1 A 293 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 A 293 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET
SEQRES 3 A 293 ASP PRO GLU PHE ARG VAL ILE ASN LEU ALA TYR ASP ASP
SEQRES 4 A 293 ASN GLY THR GLY ASP PRO VAL VAL PHE ILE ALA GLY ARG
SEQRES 5 A 293 GLY GLY ALA GLY ARG THR TRP HIS PRO HIS GLN VAL PRO
SEQRES 6 A 293 ALA PHE LEU ALA ALA GLY TYR ARG CYS ILE THR PHE ASP
SEQRES 7 A 293 ASN ARG GLY ILE GLY ALA THR GLU ASN ALA GLU GLY PHE
SEQRES 8 A 293 THR THR GLN THR MET VAL ALA ASP THR ALA ALA LEU ILE
SEQRES 9 A 293 GLU THR LEU ASP ILE ALA PRO ALA ARG VAL VAL GLY VAL
SEQRES 10 A 293 SER MET GLY ALA PHE ILE ALA GLN GLU LEU MET VAL VAL
SEQRES 11 A 293 ALA PRO GLU LEU VAL SER SER ALA VAL LEU MET ALA THR
SEQRES 12 A 293 ARG GLY ARG LEU ASP ARG ALA ARG GLN PHE PHE ASN LYS
SEQRES 13 A 293 ALA GLU ALA GLU LEU TYR ASP SER GLY VAL GLN LEU PRO
SEQRES 14 A 293 PRO THR TYR ASP ALA ARG ALA ARG LEU LEU GLU ASN PHE
SEQRES 15 A 293 SER ARG LYS THR LEU ASN ASP ASP VAL ALA VAL GLY ASP
SEQRES 16 A 293 TRP ILE ALA MET PHE SER MET TRP PRO ILE LYS SER THR
SEQRES 17 A 293 PRO GLY LEU ARG CYS GLN LEU ASP CYS ALA PRO GLN THR
SEQRES 18 A 293 ASN ARG LEU PRO ALA TYR ARG ASN ILE ALA ALA PRO VAL
SEQRES 19 A 293 LEU VAL ILE GLY PHE ALA ASP ASP VAL VAL THR PRO PRO
SEQRES 20 A 293 TYR LEU GLY ARG GLU VAL ALA ASP ALA LEU PRO ASN GLY
SEQRES 21 A 293 ARG TYR LEU GLN ILE PRO ASP ALA GLY HIS LEU GLY PHE
SEQRES 22 A 293 PHE GLU ARG PRO GLU ALA VAL ASN THR ALA MET LEU LYS
SEQRES 23 A 293 PHE PHE ALA SER VAL LYS ALA
SEQRES 1 B 293 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 B 293 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET
SEQRES 3 B 293 ASP PRO GLU PHE ARG VAL ILE ASN LEU ALA TYR ASP ASP
SEQRES 4 B 293 ASN GLY THR GLY ASP PRO VAL VAL PHE ILE ALA GLY ARG
SEQRES 5 B 293 GLY GLY ALA GLY ARG THR TRP HIS PRO HIS GLN VAL PRO
SEQRES 6 B 293 ALA PHE LEU ALA ALA GLY TYR ARG CYS ILE THR PHE ASP
SEQRES 7 B 293 ASN ARG GLY ILE GLY ALA THR GLU ASN ALA GLU GLY PHE
SEQRES 8 B 293 THR THR GLN THR MET VAL ALA ASP THR ALA ALA LEU ILE
SEQRES 9 B 293 GLU THR LEU ASP ILE ALA PRO ALA ARG VAL VAL GLY VAL
SEQRES 10 B 293 SER MET GLY ALA PHE ILE ALA GLN GLU LEU MET VAL VAL
SEQRES 11 B 293 ALA PRO GLU LEU VAL SER SER ALA VAL LEU MET ALA THR
SEQRES 12 B 293 ARG GLY ARG LEU ASP ARG ALA ARG GLN PHE PHE ASN LYS
SEQRES 13 B 293 ALA GLU ALA GLU LEU TYR ASP SER GLY VAL GLN LEU PRO
SEQRES 14 B 293 PRO THR TYR ASP ALA ARG ALA ARG LEU LEU GLU ASN PHE
SEQRES 15 B 293 SER ARG LYS THR LEU ASN ASP ASP VAL ALA VAL GLY ASP
SEQRES 16 B 293 TRP ILE ALA MET PHE SER MET TRP PRO ILE LYS SER THR
SEQRES 17 B 293 PRO GLY LEU ARG CYS GLN LEU ASP CYS ALA PRO GLN THR
SEQRES 18 B 293 ASN ARG LEU PRO ALA TYR ARG ASN ILE ALA ALA PRO VAL
SEQRES 19 B 293 LEU VAL ILE GLY PHE ALA ASP ASP VAL VAL THR PRO PRO
SEQRES 20 B 293 TYR LEU GLY ARG GLU VAL ALA ASP ALA LEU PRO ASN GLY
SEQRES 21 B 293 ARG TYR LEU GLN ILE PRO ASP ALA GLY HIS LEU GLY PHE
SEQRES 22 B 293 PHE GLU ARG PRO GLU ALA VAL ASN THR ALA MET LEU LYS
SEQRES 23 B 293 PHE PHE ALA SER VAL LYS ALA
HET TRS A 263 8
HET EDO A 264 4
HET MLA A5188 7
HET EDO A 265 4
HET EDO A 266 4
HET EDO A 267 4
HET NA A 268 1
HET ACT A 269 4
HET EDO A 270 4
HET MLA B5188 7
HET EDO B 263 4
HET NA B 264 1
HET MLA B 265 7
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM MLA MALONIC ACID
HETNAM NA SODIUM ION
HETNAM ACT ACETATE ION
HETSYN TRS TRIS BUFFER
HETSYN EDO ETHYLENE GLYCOL
HETSYN MLA DICARBOXYLIC ACID C3; PROPANEDIOLIC ACID;
HETSYN 2 MLA METAHNEDICARBOXYLIC ACID
FORMUL 3 TRS C4 H12 N O3 1+
FORMUL 4 EDO 6(C2 H6 O2)
FORMUL 5 MLA 3(C3 H4 O4)
FORMUL 9 NA 2(NA 1+)
FORMUL 10 ACT C2 H3 O2 1-
FORMUL 16 HOH *516(H2 O)
HELIX 1 1 ALA A 24 HIS A 29 5 6
HELIX 2 2 GLN A 32 ALA A 39 1 8
HELIX 3 3 ILE A 51 GLU A 55 5 5
HELIX 4 4 THR A 61 ASP A 77 1 17
HELIX 5 5 SER A 87 ALA A 100 1 14
HELIX 6 6 ASP A 117 GLY A 134 1 18
HELIX 7 7 PRO A 138 PHE A 151 1 14
HELIX 8 8 SER A 152 ASN A 157 1 6
HELIX 9 9 ASP A 158 TRP A 172 1 15
HELIX 10 10 THR A 177 ASP A 185 1 9
HELIX 11 11 ARG A 192 ARG A 197 1 6
HELIX 12 12 PRO A 215 LEU A 226 1 12
HELIX 13 13 LEU A 240 ARG A 245 1 6
HELIX 14 14 ARG A 245 SER A 259 1 15
HELIX 15 15 ALA B 24 HIS B 29 5 6
HELIX 16 16 GLN B 32 ALA B 39 1 8
HELIX 17 17 ILE B 51 GLU B 55 5 5
HELIX 18 18 THR B 61 LEU B 76 1 16
HELIX 19 19 SER B 87 ALA B 100 1 14
HELIX 20 20 ASP B 117 GLY B 134 1 18
HELIX 21 21 PRO B 138 PHE B 151 1 14
HELIX 22 22 SER B 152 ASN B 157 1 6
HELIX 23 23 ASP B 158 TRP B 172 1 15
HELIX 24 24 THR B 177 LEU B 184 1 8
HELIX 25 25 ARG B 192 ARG B 197 1 6
HELIX 26 26 PRO B 215 LEU B 226 1 12
HELIX 27 27 LEU B 240 ARG B 245 1 6
HELIX 28 28 ARG B 245 VAL B 260 1 16
SHEET 1 A 8 LEU A -11 MET A -5 0
SHEET 2 A 8 VAL A 1 ASN A 9 -1 O ILE A 2 N GLY A -7
SHEET 3 A 8 TYR A 41 PHE A 46 -1 O CYS A 43 N ASN A 9
SHEET 4 A 8 ASP A 13 ILE A 18 1 N VAL A 15 O ILE A 44
SHEET 5 A 8 ALA A 81 VAL A 86 1 O VAL A 84 N ILE A 18
SHEET 6 A 8 VAL A 104 MET A 110 1 O MET A 110 N GLY A 85
SHEET 7 A 8 VAL A 203 PHE A 208 1 O LEU A 204 N LEU A 109
SHEET 8 A 8 GLY A 229 ILE A 234 1 O ARG A 230 N VAL A 205
SHEET 1 B 7 TYR B 6 ASN B 9 0
SHEET 2 B 7 ARG B 42 PHE B 46 -1 O THR B 45 N ASP B 7
SHEET 3 B 7 PRO B 14 ILE B 18 1 N VAL B 15 O ILE B 44
SHEET 4 B 7 ALA B 81 VAL B 86 1 O ARG B 82 N VAL B 16
SHEET 5 B 7 VAL B 104 MET B 110 1 O MET B 110 N GLY B 85
SHEET 6 B 7 VAL B 203 PHE B 208 1 O LEU B 204 N LEU B 109
SHEET 7 B 7 GLY B 229 ILE B 234 1 O ARG B 230 N VAL B 205
LINK O ALA A 223 NA NA A 268 1555 1555 2.31
LINK O LEU A 226 NA NA A 268 1555 1555 2.40
LINK O GLY A 229 NA NA A 268 1555 1555 2.70
LINK O ALA B 223 NA NA B 264 1555 1555 2.37
LINK O LEU B 226 NA NA B 264 1555 1555 2.30
LINK O GLY B 229 NA NA B 264 1555 1555 2.97
LINK NA NA A 268 O HOH A 544 1555 1555 2.44
LINK NA NA A 268 O HOH A 537 1555 1555 2.42
LINK NA NA A 268 O HOH A 538 1555 1555 2.26
LINK NA NA B 264 O HOH B 465 1555 1555 2.40
LINK NA NA B 264 O HOH B 466 1555 1555 2.14
CISPEP 1 ALA A 79 PRO A 80 0 -9.96
CISPEP 2 ALA B 79 PRO B 80 0 -1.77
SITE 1 AC1 9 ARG A 21 SER A 87 MET A 88 ARG A 113
SITE 2 AC1 9 GLN A 183 LEU A 184 ACT A 269 HOH A 425
SITE 3 AC1 9 HOH A 430
SITE 1 AC2 6 LEU A 156 HOH A 352 HOH A 353 HOH A 354
SITE 2 AC2 6 ARG B 118 ALA B 119
SITE 1 AC3 7 THR A 27 ARG A 146 MET A 168 LEU A 240
SITE 2 AC3 7 PHE A 243 EDO A 265 HOH A 467
SITE 1 AC4 5 ARG A 21 GLY A 23 EDO A 266 HOH A 421
SITE 2 AC4 5 MLA A5188
SITE 1 AC5 2 ARG A 21 EDO A 265
SITE 1 AC6 4 ALA A 161 ASP A 164 TRP A 165 HOH A 337
SITE 1 AC7 6 ALA A 223 LEU A 226 GLY A 229 HOH A 537
SITE 2 AC7 6 HOH A 538 HOH A 544
SITE 1 AC8 6 ARG A 113 LEU A 116 ASN A 124 ALA A 187
SITE 2 AC8 6 TRS A 263 HOH A 427
SITE 1 AC9 2 ASN A 198 MET B 171
SITE 1 BC1 9 ARG B 21 SER B 87 MET B 88 ARG B 120
SITE 2 BC1 9 PHE B 123 HIS B 239 HOH B 438 HOH B 439
SITE 3 BC1 9 HOH B 448
SITE 1 BC2 4 GLY B 12 ASP B 13 GLY B 40 HOH B 312
SITE 1 BC3 6 ALA B 223 ASP B 224 LEU B 226 GLY B 229
SITE 2 BC3 6 HOH B 465 HOH B 466
SITE 1 BC4 4 ARG B 146 LEU B 240 PHE B 243 HOH B 389
CRYST1 100.454 100.454 135.162 90.00 90.00 90.00 P 41 21 2 16
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 0.009955 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009955 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007399 0.00000
TER 2130 LYS A 261
TER 4132 ALA B 262
MASTER 424 0 13 28 15 0 23 6 4667 2 72 46
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