HEADER OXIDOREDUCTASE 26-NOV-07 2VHV
TITLE CRYSTAL STRUCTURE OF THE D270A MUTANT OF L-ALANINE
TITLE 2 DEHYDROGENASE FROM MYCOBACTERIUM TUBERCULOSIS IN
TITLE 3 COMPLEX WITH NADH.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALANINE DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: 40 KDA ANTIGEN, TB43;
COMPND 5 EC: 1.4.1.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET26
KEYWDS NAD, SECRETED, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.AGREN,G.SCHNEIDER
REVDAT 3 24-FEB-09 2VHV 1 VERSN
REVDAT 2 11-NOV-08 2VHV 1 JRNL REMARK HET HETNAM
REVDAT 2 2 FORMUL SCALE1 SCALE2 SCALE3
REVDAT 2 3 TER HETATM CONECT
REVDAT 1 11-MAR-08 2VHV 0
JRNL AUTH D.AGREN,M.STEHR,C.L.BERTHOLD,S.KAPOOR,W.OEHLMANN,
JRNL AUTH 2 M.SINGH,G.SCHNEIDER
JRNL TITL THREE-DIMENSIONAL STRUCTURES OF APO- AND HOLO-L-
JRNL TITL 2 ALANINE DEHYDROGENASE FROM MYCOBACTERIUM
JRNL TITL 3 TUBERCULOSIS REVEAL CONFORMATIONAL CHANGES UPON
JRNL TITL 4 COENZYME BINDING.
JRNL REF J.MOL.BIOL. V. 377 1161 2008
JRNL REFN ISSN 0022-2836
JRNL PMID 18304579
JRNL DOI 10.1016/J.JMB.2008.01.091
REMARK 2
REMARK 2 RESOLUTION. 2.8 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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 21753
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) : 0.200
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1162
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1576
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.22
REMARK 3 BIN R VALUE (WORKING SET) : 0.2750
REMARK 3 BIN FREE R VALUE SET COUNT : 79
REMARK 3 BIN FREE R VALUE : 0.3010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5438
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 88
REMARK 3 SOLVENT ATOMS : 17
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.56
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.349
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.248
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.753
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.904
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5640 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7702 ; 1.375 ; 1.986
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 740 ; 5.640 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 210 ;36.287 ;23.429
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 848 ;17.764 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 38 ;18.954 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 910 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4234 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2766 ; 0.211 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3830 ; 0.308 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 202 ; 0.115 ; 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): 38 ; 0.202 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.349 ; 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): 3743 ; 0.487 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5860 ; 0.835 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2105 ; 1.265 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1842 ; 2.079 ; 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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 100 2
REMARK 3 1 B 1 B 100 2
REMARK 3 2 A 310 A 370 2
REMARK 3 2 B 310 B 370 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 644 ; 0.02 ; 0.05
REMARK 3 MEDIUM POSITIONAL 1 A (A): 558 ; 0.21 ; 0.50
REMARK 3 TIGHT THERMAL 1 A (A**2): 644 ; 0.28 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 558 ; 0.30 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 130 A 280 2
REMARK 3 1 B 130 B 280 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 A (A): 604 ; 0.02 ; 0.05
REMARK 3 MEDIUM POSITIONAL 2 A (A): 478 ; 0.16 ; 0.50
REMARK 3 TIGHT THERMAL 2 A (A**2): 604 ; 0.28 ; 0.50
REMARK 3 MEDIUM THERMAL 2 A (A**2): 478 ; 0.38 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 2VHV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-NOV-07.
REMARK 100 THE PDBE ID CODE IS EBI-34559.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-SEP-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : DIAMOND (111), GE(220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22947
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.80
REMARK 200 RESOLUTION RANGE LOW (A) : 40.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 4.1
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 4.4
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.90
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.5
REMARK 200 R MERGE FOR SHELL (I) : 0.40
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.10
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: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS TRIS PROPANE PH 8.2,
REMARK 280 20% PEG 3350 AND 0.2M SODIUM ACETATE. CO CRYSTALLIZED WITH
REMARK 280 10MM NADH WHICH WAS ADDED TO THE PROTEIN SOLUTION
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+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 70.40100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.40100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 70.40100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.40100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 70.40100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 70.40100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 70.40100
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 70.40100
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 70.40100
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 70.40100
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 70.40100
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 70.40100
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 70.40100
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 70.40100
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 70.40100
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 70.40100
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 70.40100
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 70.40100
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 19880 ANGSTROM**2
REMARK 350 TOTAL SURFACE AREA FOR THE COMPLEX: 86410 ANGSTROM**2
REMARK 350 GAIN IN SOLVENT FREE ENERGY: -97 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 350 BIOMT1 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 70.40100
REMARK 350 BIOMT3 2 0.000000 -1.000000 0.000000 70.40100
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 -70.40100
REMARK 350 BIOMT2 3 0.000000 0.000000 -1.000000 70.40100
REMARK 350 BIOMT3 3 -1.000000 0.000000 0.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASP 270 TO ASN
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ASP 270 TO ASN
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 HIS A 372
REMARK 465 HIS A 373
REMARK 465 HIS A 374
REMARK 465 HIS A 375
REMARK 465 HIS A 376
REMARK 465 HIS A 377
REMARK 465 HIS B 372
REMARK 465 HIS B 373
REMARK 465 HIS B 374
REMARK 465 HIS B 375
REMARK 465 HIS B 376
REMARK 465 HIS B 377
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 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 ASN A 12 28.70 45.95
REMARK 500 ALA A 98 -19.63 -49.74
REMARK 500 SER A 220 62.87 -67.73
REMARK 500 ALA A 238 46.84 -140.15
REMARK 500 HIS A 291 -131.97 49.27
REMARK 500 CYS A 297 52.99 -141.43
REMARK 500 VAL A 305 53.34 -141.13
REMARK 500 ALA B 238 43.08 -141.54
REMARK 500 HIS B 291 -129.99 44.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI A1372
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI B1372
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VHW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HOLO L-ALANINE DEHYDROGENASE
REMARK 900 FROM MYCOBACTERIUM TUBERCULOSIS IN THE OPEN AND
REMARK 900 CLOSED CONFORMATION
REMARK 900 RELATED ID: 2VHX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE TERNARY COMPLEX OF
REMARK 900 L-ALANINE DEHYDROGENASE FROM MYCOBACTERIUM
REMARK 900 TUBERCULOSIS WITH NAD+ AND PYRUVATE
REMARK 900 RELATED ID: 2VHY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF APO L-ALANINE DEHYDROGENASE
REMARK 900 FROM MYCOBACTERIUM TUBERCULOSIS
REMARK 900 RELATED ID: 2VHZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HOLO L-ALANINE DEHYDROGENASE
REMARK 900 FROM MYCOBACTERIUM TUBERCULOSIS IN THE CLOSED
REMARK 900 CONFORMATION
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 EXPRESSED WITH A C-TERMINAL 6XHIS TAG.
DBREF 2VHV A 1 371 UNP P30234 DHA_MYCTU 1 371
DBREF 2VHV A 372 377 PDB 2VHV 2VHV 372 377
DBREF 2VHV B 1 371 UNP P30234 DHA_MYCTU 1 371
DBREF 2VHV B 372 377 PDB 2VHV 2VHV 372 377
SEQADV 2VHV ASN A 270 UNP P30234 ASP 270 ENGINEERED MUTATION
SEQADV 2VHV ASN B 270 UNP P30234 ASP 270 ENGINEERED MUTATION
SEQRES 1 A 377 MET ARG VAL GLY ILE PRO THR GLU THR LYS ASN ASN GLU
SEQRES 2 A 377 PHE ARG VAL ALA ILE THR PRO ALA GLY VAL ALA GLU LEU
SEQRES 3 A 377 THR ARG ARG GLY HIS GLU VAL LEU ILE GLN ALA GLY ALA
SEQRES 4 A 377 GLY GLU GLY SER ALA ILE THR ASP ALA ASP PHE LYS ALA
SEQRES 5 A 377 ALA GLY ALA GLN LEU VAL GLY THR ALA ASP GLN VAL TRP
SEQRES 6 A 377 ALA ASP ALA ASP LEU LEU LEU LYS VAL LYS GLU PRO ILE
SEQRES 7 A 377 ALA ALA GLU TYR GLY ARG LEU ARG HIS GLY GLN ILE LEU
SEQRES 8 A 377 PHE THR PHE LEU HIS LEU ALA ALA SER ARG ALA CYS THR
SEQRES 9 A 377 ASP ALA LEU LEU ASP SER GLY THR THR SER ILE ALA TYR
SEQRES 10 A 377 GLU THR VAL GLN THR ALA ASP GLY ALA LEU PRO LEU LEU
SEQRES 11 A 377 ALA PRO MET SER GLU VAL ALA GLY ARG LEU ALA ALA GLN
SEQRES 12 A 377 VAL GLY ALA TYR HIS LEU MET ARG THR GLN GLY GLY ARG
SEQRES 13 A 377 GLY VAL LEU MET GLY GLY VAL PRO GLY VAL GLU PRO ALA
SEQRES 14 A 377 ASP VAL VAL VAL ILE GLY ALA GLY THR ALA GLY TYR ASN
SEQRES 15 A 377 ALA ALA ARG ILE ALA ASN GLY MET GLY ALA THR VAL THR
SEQRES 16 A 377 VAL LEU ASP ILE ASN ILE ASP LYS LEU ARG GLN LEU ASP
SEQRES 17 A 377 ALA GLU PHE CYS GLY ARG ILE HIS THR ARG TYR SER SER
SEQRES 18 A 377 ALA TYR GLU LEU GLU GLY ALA VAL LYS ARG ALA ASP LEU
SEQRES 19 A 377 VAL ILE GLY ALA VAL LEU VAL PRO GLY ALA LYS ALA PRO
SEQRES 20 A 377 LYS LEU VAL SER ASN SER LEU VAL ALA HIS MET LYS PRO
SEQRES 21 A 377 GLY ALA VAL LEU VAL ASP ILE ALA ILE ASN GLN GLY GLY
SEQRES 22 A 377 CYS PHE GLU GLY SER ARG PRO THR THR TYR ASP HIS PRO
SEQRES 23 A 377 THR PHE ALA VAL HIS ASP THR LEU PHE TYR CYS VAL ALA
SEQRES 24 A 377 ASN MET PRO ALA SER VAL PRO LYS THR SER THR TYR ALA
SEQRES 25 A 377 LEU THR ASN ALA THR MET PRO TYR VAL LEU GLU LEU ALA
SEQRES 26 A 377 ASP HIS GLY TRP ARG ALA ALA CYS ARG SER ASN PRO ALA
SEQRES 27 A 377 LEU ALA LYS GLY LEU SER THR HIS GLU GLY ALA LEU LEU
SEQRES 28 A 377 SER GLU ARG VAL ALA THR ASP LEU GLY VAL PRO PHE THR
SEQRES 29 A 377 GLU PRO ALA SER VAL LEU ALA HIS HIS HIS HIS HIS HIS
SEQRES 1 B 377 MET ARG VAL GLY ILE PRO THR GLU THR LYS ASN ASN GLU
SEQRES 2 B 377 PHE ARG VAL ALA ILE THR PRO ALA GLY VAL ALA GLU LEU
SEQRES 3 B 377 THR ARG ARG GLY HIS GLU VAL LEU ILE GLN ALA GLY ALA
SEQRES 4 B 377 GLY GLU GLY SER ALA ILE THR ASP ALA ASP PHE LYS ALA
SEQRES 5 B 377 ALA GLY ALA GLN LEU VAL GLY THR ALA ASP GLN VAL TRP
SEQRES 6 B 377 ALA ASP ALA ASP LEU LEU LEU LYS VAL LYS GLU PRO ILE
SEQRES 7 B 377 ALA ALA GLU TYR GLY ARG LEU ARG HIS GLY GLN ILE LEU
SEQRES 8 B 377 PHE THR PHE LEU HIS LEU ALA ALA SER ARG ALA CYS THR
SEQRES 9 B 377 ASP ALA LEU LEU ASP SER GLY THR THR SER ILE ALA TYR
SEQRES 10 B 377 GLU THR VAL GLN THR ALA ASP GLY ALA LEU PRO LEU LEU
SEQRES 11 B 377 ALA PRO MET SER GLU VAL ALA GLY ARG LEU ALA ALA GLN
SEQRES 12 B 377 VAL GLY ALA TYR HIS LEU MET ARG THR GLN GLY GLY ARG
SEQRES 13 B 377 GLY VAL LEU MET GLY GLY VAL PRO GLY VAL GLU PRO ALA
SEQRES 14 B 377 ASP VAL VAL VAL ILE GLY ALA GLY THR ALA GLY TYR ASN
SEQRES 15 B 377 ALA ALA ARG ILE ALA ASN GLY MET GLY ALA THR VAL THR
SEQRES 16 B 377 VAL LEU ASP ILE ASN ILE ASP LYS LEU ARG GLN LEU ASP
SEQRES 17 B 377 ALA GLU PHE CYS GLY ARG ILE HIS THR ARG TYR SER SER
SEQRES 18 B 377 ALA TYR GLU LEU GLU GLY ALA VAL LYS ARG ALA ASP LEU
SEQRES 19 B 377 VAL ILE GLY ALA VAL LEU VAL PRO GLY ALA LYS ALA PRO
SEQRES 20 B 377 LYS LEU VAL SER ASN SER LEU VAL ALA HIS MET LYS PRO
SEQRES 21 B 377 GLY ALA VAL LEU VAL ASP ILE ALA ILE ASN GLN GLY GLY
SEQRES 22 B 377 CYS PHE GLU GLY SER ARG PRO THR THR TYR ASP HIS PRO
SEQRES 23 B 377 THR PHE ALA VAL HIS ASP THR LEU PHE TYR CYS VAL ALA
SEQRES 24 B 377 ASN MET PRO ALA SER VAL PRO LYS THR SER THR TYR ALA
SEQRES 25 B 377 LEU THR ASN ALA THR MET PRO TYR VAL LEU GLU LEU ALA
SEQRES 26 B 377 ASP HIS GLY TRP ARG ALA ALA CYS ARG SER ASN PRO ALA
SEQRES 27 B 377 LEU ALA LYS GLY LEU SER THR HIS GLU GLY ALA LEU LEU
SEQRES 28 B 377 SER GLU ARG VAL ALA THR ASP LEU GLY VAL PRO PHE THR
SEQRES 29 B 377 GLU PRO ALA SER VAL LEU ALA HIS HIS HIS HIS HIS HIS
HET NAI A1372 44
HET NAI B1372 44
HETNAM NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE
FORMUL 3 NAI 2(C21 H29 N7 O14 P2)
FORMUL 4 HOH *17(H2 O1)
HELIX 1 1 THR A 19 ARG A 29 1 11
HELIX 2 2 GLY A 40 ALA A 44 5 5
HELIX 3 3 THR A 46 GLY A 54 1 9
HELIX 4 4 THR A 60 ALA A 68 1 9
HELIX 5 5 ILE A 78 LEU A 85 5 8
HELIX 6 6 HIS A 96 ALA A 99 5 4
HELIX 7 7 SER A 100 GLY A 111 1 12
HELIX 8 8 GLU A 118 VAL A 120 5 3
HELIX 9 9 LEU A 130 LEU A 149 1 20
HELIX 10 10 MET A 150 GLY A 154 5 5
HELIX 11 11 GLY A 177 MET A 190 1 14
HELIX 12 12 ASN A 200 PHE A 211 1 12
HELIX 13 13 SER A 221 ALA A 232 1 12
HELIX 14 14 SER A 251 ALA A 256 1 6
HELIX 15 15 ALA A 268 GLY A 272 5 5
HELIX 16 16 ASN A 300 SER A 304 5 5
HELIX 17 17 VAL A 305 LYS A 341 1 37
HELIX 18 18 SER A 352 GLY A 360 1 9
HELIX 19 19 GLU A 365 VAL A 369 5 5
HELIX 20 20 THR B 19 ARG B 29 1 11
HELIX 21 21 GLY B 40 ALA B 44 5 5
HELIX 22 22 THR B 46 GLY B 54 1 9
HELIX 23 23 THR B 60 ALA B 68 1 9
HELIX 24 24 ILE B 78 LEU B 85 5 8
HELIX 25 25 HIS B 96 ALA B 99 5 4
HELIX 26 26 SER B 100 GLY B 111 1 12
HELIX 27 27 GLU B 118 VAL B 120 5 3
HELIX 28 28 LEU B 130 LEU B 149 1 20
HELIX 29 29 MET B 150 GLY B 154 5 5
HELIX 30 30 GLY B 177 MET B 190 1 14
HELIX 31 31 ASN B 200 PHE B 211 1 12
HELIX 32 32 SER B 221 ALA B 232 1 12
HELIX 33 33 SER B 251 ALA B 256 1 6
HELIX 34 34 ALA B 268 GLY B 272 5 5
HELIX 35 35 ASN B 300 SER B 304 5 5
HELIX 36 36 VAL B 305 LYS B 341 1 37
HELIX 37 37 SER B 352 GLY B 360 1 9
HELIX 38 38 GLU B 365 VAL B 369 5 5
SHEET 1 AA 8 GLN A 56 VAL A 58 0
SHEET 2 AA 8 GLU A 32 GLN A 36 1 O VAL A 33 N GLN A 56
SHEET 3 AA 8 ARG A 2 ILE A 5 1 O VAL A 3 N LEU A 34
SHEET 4 AA 8 LEU A 70 LEU A 72 1 O LEU A 70 N GLY A 4
SHEET 5 AA 8 ILE A 90 THR A 93 1 O ILE A 90 N LEU A 71
SHEET 6 AA 8 THR A 113 ALA A 116 1 O THR A 113 N LEU A 91
SHEET 7 AA 8 LEU A 343 HIS A 346 -1 N SER A 344 O SER A 114
SHEET 8 AA 8 ALA A 349 LEU A 350 -1 O ALA A 349 N HIS A 346
SHEET 1 AB 7 HIS A 216 TYR A 219 0
SHEET 2 AB 7 THR A 193 ASP A 198 1 O VAL A 194 N HIS A 216
SHEET 3 AB 7 ASP A 170 ILE A 174 1 O VAL A 171 N THR A 195
SHEET 4 AB 7 LEU A 234 GLY A 237 1 O LEU A 234 N VAL A 172
SHEET 5 AB 7 VAL A 263 ASP A 266 1 O VAL A 263 N VAL A 235
SHEET 6 AB 7 THR A 293 TYR A 296 1 O LEU A 294 N LEU A 264
SHEET 7 AB 7 THR A 287 VAL A 290 -1 O PHE A 288 N PHE A 295
SHEET 1 BA 8 GLN B 56 VAL B 58 0
SHEET 2 BA 8 GLU B 32 GLN B 36 1 O VAL B 33 N GLN B 56
SHEET 3 BA 8 ARG B 2 ILE B 5 1 O VAL B 3 N LEU B 34
SHEET 4 BA 8 LEU B 70 LEU B 72 1 O LEU B 70 N GLY B 4
SHEET 5 BA 8 ILE B 90 THR B 93 1 O ILE B 90 N LEU B 71
SHEET 6 BA 8 THR B 113 ALA B 116 1 O THR B 113 N LEU B 91
SHEET 7 BA 8 LEU B 343 HIS B 346 -1 N SER B 344 O SER B 114
SHEET 8 BA 8 ALA B 349 LEU B 350 -1 O ALA B 349 N HIS B 346
SHEET 1 BB 7 HIS B 216 TYR B 219 0
SHEET 2 BB 7 THR B 193 ASP B 198 1 O VAL B 194 N HIS B 216
SHEET 3 BB 7 ASP B 170 ILE B 174 1 O VAL B 171 N THR B 195
SHEET 4 BB 7 LEU B 234 GLY B 237 1 O LEU B 234 N VAL B 172
SHEET 5 BB 7 VAL B 263 ASP B 266 1 O VAL B 263 N VAL B 235
SHEET 6 BB 7 THR B 293 TYR B 296 1 O LEU B 294 N LEU B 264
SHEET 7 BB 7 THR B 287 VAL B 290 -1 O PHE B 288 N PHE B 295
SITE 1 AC1 22 LEU A 130 MET A 133 SER A 134 ALA A 137
SITE 2 AC1 22 GLY A 177 THR A 178 ALA A 179 ASP A 198
SITE 3 AC1 22 LYS A 203 SER A 220 ALA A 238 VAL A 239
SITE 4 AC1 22 LEU A 240 LEU A 249 ILE A 267 ASN A 270
SITE 5 AC1 22 GLN A 271 VAL A 298 ALA A 299 ASN A 300
SITE 6 AC1 22 MET A 301 PRO A 302
SITE 1 AC2 21 MET B 133 SER B 134 ALA B 137 GLY B 177
SITE 2 AC2 21 THR B 178 ALA B 179 ASP B 198 ILE B 199
SITE 3 AC2 21 LYS B 203 SER B 220 ALA B 238 VAL B 239
SITE 4 AC2 21 LEU B 240 LEU B 249 ILE B 267 ASN B 270
SITE 5 AC2 21 GLN B 271 VAL B 298 ALA B 299 MET B 301
SITE 6 AC2 21 PRO B 302
CRYST1 140.802 140.802 140.802 90.00 90.00 90.00 P 21 3 24
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 0.007102 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007102 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007102 0.00000
MTRIX1 1 -1.000000 0.000290 0.000640 -35.21101 1
MTRIX2 1 0.000640 0.000480 1.000000 35.20195 1
MTRIX3 1 0.000290 1.000000 -0.000480 -35.18603 1
(ATOM LINES ARE NOT SHOWN.)
END