HEADER ISOMERASE 30-APR-09 3HA1
TITLE ALANINE RACEMASE FROM BACILLUS ANTHRACIS (AMES)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALANINE RACEMASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 5.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;
SOURCE 3 ORGANISM_COMMON: ANTHRAX,ANTHRAX BACTERIUM;
SOURCE 4 ORGANISM_TAXID: 1392;
SOURCE 5 STRAIN: AMES;
SOURCE 6 GENE: DAL-1, DAL1;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET28-TEV-DAL
KEYWDS ALANINE RACEMASE, ISOMERASE, PLP, PYRIDOXAL PHOSPHATE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.M.COUNAGO,M.DAVLIEVA,U.STRYCH,R.E.HILL,K.L.KRAUSE
REVDAT 3 22-NOV-23 3HA1 1 REMARK
REVDAT 2 06-SEP-23 3HA1 1 REMARK SEQADV LINK
REVDAT 1 15-SEP-09 3HA1 0
JRNL AUTH R.M.COUNAGO,M.DAVLIEVA,U.STRYCH,R.E.HILL,K.L.KRAUSE
JRNL TITL BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF ALANINE
JRNL TITL 2 RACEMASE FROM BACILLUS ANTHRACIS (AMES).
JRNL REF BMC STRUCT.BIOL. V. 9 53 2009
JRNL REFN ESSN 1472-6807
JRNL PMID 19695097
JRNL DOI 10.1186/1472-6807-9-53
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.79
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.1
REMARK 3 NUMBER OF REFLECTIONS : 53387
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) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1627
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2518
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 59.80
REMARK 3 BIN R VALUE (WORKING SET) : 0.1940
REMARK 3 BIN FREE R VALUE SET COUNT : 72
REMARK 3 BIN FREE R VALUE : 0.2340
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6066
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 358
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.12
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.56000
REMARK 3 B22 (A**2) : -1.51000
REMARK 3 B33 (A**2) : 0.20000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.55000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.161
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.144
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.096
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.304
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6222 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8487 ; 1.459 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 770 ; 7.467 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 275 ;33.734 ;23.382
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 966 ;13.200 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;14.626 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 966 ; 0.120 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4750 ; 0.014 ; 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): 3844 ; 1.273 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6211 ; 1.912 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2378 ; 3.226 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2276 ; 4.742 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 4 A 389
REMARK 3 RESIDUE RANGE : B 4 B 389
REMARK 3 ORIGIN FOR THE GROUP (A): 11.9820 -0.9620 12.3810
REMARK 3 T TENSOR
REMARK 3 T11: 0.1105 T22: 0.1302
REMARK 3 T33: 0.0834 T12: -0.0019
REMARK 3 T13: 0.0307 T23: 0.0293
REMARK 3 L TENSOR
REMARK 3 L11: 0.5425 L22: 2.9722
REMARK 3 L33: 0.8029 L12: 0.4525
REMARK 3 L13: -0.2239 L23: -0.9074
REMARK 3 S TENSOR
REMARK 3 S11: -0.0366 S12: 0.0698 S13: 0.0878
REMARK 3 S21: -0.1212 S22: 0.2327 S23: 0.4015
REMARK 3 S31: -0.0113 S32: -0.1290 S33: -0.1961
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ATOM RECORD SHOWS TOTAL B FACTORS.
REMARK 4
REMARK 4 3HA1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAY-09.
REMARK 100 THE DEPOSITION ID IS D_1000052880.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-NOV-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.2.25
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53396
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 32.790
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.3
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.02900
REMARK 200 R SYM (I) : 0.02900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.5260
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 67.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.15600
REMARK 200 R SYM FOR SHELL (I) : 0.15600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.600
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: PDB ENTRY 1SFT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18 %PEG 8000, 0.2 M SODIUM ACETATE,
REMARK 280 0.1 M SODIUM CACODYLATE, 0.01 M GSH (L-GLUTATHIONE REDUCED),
REMARK 280 0.01 M GSSG (L-GLUTATHIONE OXIDIZED), PH 6.5, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
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
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 70.63550
REMARK 290 SMTRY3 2 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/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 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 1
REMARK 465 GLU A 2
REMARK 465 GLU A 3
REMARK 465 LEU A 390
REMARK 465 GLU A 391
REMARK 465 GLU A 392
REMARK 465 ASN A 393
REMARK 465 LEU A 394
REMARK 465 TYR A 395
REMARK 465 PHE A 396
REMARK 465 GLN A 397
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 GLU B 3
REMARK 465 LEU B 390
REMARK 465 GLU B 391
REMARK 465 GLU B 392
REMARK 465 ASN B 393
REMARK 465 LEU B 394
REMARK 465 TYR B 395
REMARK 465 PHE B 396
REMARK 465 GLN B 397
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 100 CG CD OE1 OE2
REMARK 470 LYS A 145 CG CD CE NZ
REMARK 470 LYS A 152 CG CD CE NZ
REMARK 470 SER A 153 OG
REMARK 470 LYS A 182 CG CD CE NZ
REMARK 470 LYS A 195 CG CD CE NZ
REMARK 470 GLN A 216 CG CD OE1 NE2
REMARK 470 LYS A 245 CG CD CE NZ
REMARK 470 LYS A 378 CG CD CE NZ
REMARK 470 GLU A 381 CG CD OE1 OE2
REMARK 470 LYS B 27 CG CD CE NZ
REMARK 470 ILE B 95 CG1 CG2 CD1
REMARK 470 GLU B 100 CG CD OE1 OE2
REMARK 470 ASP B 121 CG OD1 OD2
REMARK 470 SER B 123 OG
REMARK 470 SER B 124 OG
REMARK 470 LYS B 127 CG CD CE NZ
REMARK 470 LYS B 145 CG CD CE NZ
REMARK 470 LYS B 152 CG CD CE NZ
REMARK 470 SER B 153 OG
REMARK 470 LYS B 182 CG CD CE NZ
REMARK 470 LEU B 188 CG CD1 CD2
REMARK 470 LYS B 195 CG CD CE NZ
REMARK 470 ASP B 200 CG OD1 OD2
REMARK 470 GLN B 216 CG CD OE1 NE2
REMARK 470 LYS B 378 CG CD CE NZ
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 LLP A 41 161.47 -45.31
REMARK 500 ASP A 48 116.79 98.29
REMARK 500 PHE A 108 11.84 -152.41
REMARK 500 ARG A 138 -82.74 -100.22
REMARK 500 LYS A 202 -55.27 74.28
REMARK 500 PHE A 220 -130.99 53.90
REMARK 500 SER A 269 -174.73 69.94
REMARK 500 THR A 356 -156.21 -140.17
REMARK 500 ASP B 48 123.02 95.29
REMARK 500 PHE B 108 15.19 -150.79
REMARK 500 ARG B 138 -74.75 -104.21
REMARK 500 LYS B 202 -55.83 82.02
REMARK 500 PHE B 220 -132.28 53.54
REMARK 500 SER B 269 -174.32 73.49
REMARK 500 THR B 356 -156.49 -137.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 398
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 399
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 398
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 399
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SFT RELATED DB: PDB
REMARK 900 ALANINE RACEMASE FROM G.STEAROTHERMOPHILUS
REMARK 900 RELATED ID: 2VD8 RELATED DB: PDB
REMARK 900 ALANINE RACEMASE FROM B.ANTHRACIS (BA0252)
REMARK 900 RELATED ID: 1RCQ RELATED DB: PDB
REMARK 900 ALANINE RACEMASE FROM P.AERUGINOSA
REMARK 900 RELATED ID: 1XFC RELATED DB: PDB
REMARK 900 ALANINE RACEMASE FROM M.TUBERCULOSIS
DBREF 3HA1 A 1 389 UNP Q81VF6 Q81VF6_BACAN 1 389
DBREF 3HA1 B 1 389 UNP Q81VF6 Q81VF6_BACAN 1 389
SEQADV 3HA1 LEU A 390 UNP Q81VF6 EXPRESSION TAG
SEQADV 3HA1 GLU A 391 UNP Q81VF6 EXPRESSION TAG
SEQADV 3HA1 GLU A 392 UNP Q81VF6 EXPRESSION TAG
SEQADV 3HA1 ASN A 393 UNP Q81VF6 EXPRESSION TAG
SEQADV 3HA1 LEU A 394 UNP Q81VF6 EXPRESSION TAG
SEQADV 3HA1 TYR A 395 UNP Q81VF6 EXPRESSION TAG
SEQADV 3HA1 PHE A 396 UNP Q81VF6 EXPRESSION TAG
SEQADV 3HA1 GLN A 397 UNP Q81VF6 EXPRESSION TAG
SEQADV 3HA1 LEU B 390 UNP Q81VF6 EXPRESSION TAG
SEQADV 3HA1 GLU B 391 UNP Q81VF6 EXPRESSION TAG
SEQADV 3HA1 GLU B 392 UNP Q81VF6 EXPRESSION TAG
SEQADV 3HA1 ASN B 393 UNP Q81VF6 EXPRESSION TAG
SEQADV 3HA1 LEU B 394 UNP Q81VF6 EXPRESSION TAG
SEQADV 3HA1 TYR B 395 UNP Q81VF6 EXPRESSION TAG
SEQADV 3HA1 PHE B 396 UNP Q81VF6 EXPRESSION TAG
SEQADV 3HA1 GLN B 397 UNP Q81VF6 EXPRESSION TAG
SEQRES 1 A 397 MET GLU GLU ALA PRO PHE TYR ARG ASP THR TRP VAL GLU
SEQRES 2 A 397 VAL ASP LEU ASP ALA ILE TYR ASN ASN VAL THR HIS ILE
SEQRES 3 A 397 LYS GLU PHE ILE PRO SER ASP VAL GLU ILE PHE ALA VAL
SEQRES 4 A 397 VAL LLP GLY ASN ALA TYR GLY HIS ASP TYR VAL PRO VAL
SEQRES 5 A 397 ALA LYS ILE ALA LEU GLU ALA GLY ALA THR ARG LEU ALA
SEQRES 6 A 397 VAL ALA PHE LEU ASP GLU ALA LEU VAL LEU ARG ARG ALA
SEQRES 7 A 397 GLY ILE THR ALA PRO ILE LEU VAL LEU GLY PRO SER PRO
SEQRES 8 A 397 PRO ARG ASP ILE ASN VAL ALA ALA GLU ASN ASP VAL ALA
SEQRES 9 A 397 LEU THR VAL PHE GLN LYS GLU TRP VAL ASP GLU ALA ILE
SEQRES 10 A 397 LYS LEU TRP ASP GLY SER SER THR MET LYS TYR HIS ILE
SEQRES 11 A 397 ASN PHE ASP SER GLY MET GLY ARG ILE GLY ILE ARG GLU
SEQRES 12 A 397 ARG LYS GLU LEU LYS GLY PHE LEU LYS SER LEU GLU GLY
SEQRES 13 A 397 ALA PRO PHE LEU GLU LEU GLU GLY VAL TYR THR HIS PHE
SEQRES 14 A 397 ALA THR ALA ASP GLU VAL GLU THR SER TYR PHE ASP LYS
SEQRES 15 A 397 GLN TYR ASN THR PHE LEU GLU GLN LEU SER TRP LEU LYS
SEQRES 16 A 397 GLU PHE GLY VAL ASP PRO LYS PHE VAL HIS THR ALA ASN
SEQRES 17 A 397 SER ALA ALA THR LEU ARG PHE GLN GLY ILE THR PHE ASN
SEQRES 18 A 397 ALA VAL ARG ILE GLY ILE ALA MET TYR GLY LEU SER PRO
SEQRES 19 A 397 SER VAL GLU ILE ARG PRO PHE LEU PRO PHE LYS LEU GLU
SEQRES 20 A 397 PRO ALA LEU SER LEU HIS THR LYS VAL ALA HIS ILE LYS
SEQRES 21 A 397 GLN VAL ILE LYS GLY ASP GLY ILE SER TYR ASN VAL THR
SEQRES 22 A 397 TYR ARG THR LYS THR GLU GLU TRP ILE ALA THR VAL ALA
SEQRES 23 A 397 ILE GLY TYR ALA ASP GLY TRP LEU ARG ARG LEU GLN GLY
SEQRES 24 A 397 PHE GLU VAL LEU VAL ASN GLY LYS ARG VAL PRO ILE VAL
SEQRES 25 A 397 GLY ARG VAL THR MET ASP GLN PHE MET ILE HIS LEU PRO
SEQRES 26 A 397 CYS GLU VAL PRO LEU GLY THR LYS VAL THR LEU ILE GLY
SEQRES 27 A 397 ARG GLN GLY ASP GLU TYR ILE SER ALA THR GLU VAL ALA
SEQRES 28 A 397 GLU TYR SER GLY THR ILE ASN TYR GLU ILE ILE THR THR
SEQRES 29 A 397 ILE SER PHE ARG VAL PRO ARG ILE PHE ILE ARG ASN GLY
SEQRES 30 A 397 LYS VAL VAL GLU VAL ILE ASN TYR LEU ASN ASP ILE LEU
SEQRES 31 A 397 GLU GLU ASN LEU TYR PHE GLN
SEQRES 1 B 397 MET GLU GLU ALA PRO PHE TYR ARG ASP THR TRP VAL GLU
SEQRES 2 B 397 VAL ASP LEU ASP ALA ILE TYR ASN ASN VAL THR HIS ILE
SEQRES 3 B 397 LYS GLU PHE ILE PRO SER ASP VAL GLU ILE PHE ALA VAL
SEQRES 4 B 397 VAL LLP GLY ASN ALA TYR GLY HIS ASP TYR VAL PRO VAL
SEQRES 5 B 397 ALA LYS ILE ALA LEU GLU ALA GLY ALA THR ARG LEU ALA
SEQRES 6 B 397 VAL ALA PHE LEU ASP GLU ALA LEU VAL LEU ARG ARG ALA
SEQRES 7 B 397 GLY ILE THR ALA PRO ILE LEU VAL LEU GLY PRO SER PRO
SEQRES 8 B 397 PRO ARG ASP ILE ASN VAL ALA ALA GLU ASN ASP VAL ALA
SEQRES 9 B 397 LEU THR VAL PHE GLN LYS GLU TRP VAL ASP GLU ALA ILE
SEQRES 10 B 397 LYS LEU TRP ASP GLY SER SER THR MET LYS TYR HIS ILE
SEQRES 11 B 397 ASN PHE ASP SER GLY MET GLY ARG ILE GLY ILE ARG GLU
SEQRES 12 B 397 ARG LYS GLU LEU LYS GLY PHE LEU LYS SER LEU GLU GLY
SEQRES 13 B 397 ALA PRO PHE LEU GLU LEU GLU GLY VAL TYR THR HIS PHE
SEQRES 14 B 397 ALA THR ALA ASP GLU VAL GLU THR SER TYR PHE ASP LYS
SEQRES 15 B 397 GLN TYR ASN THR PHE LEU GLU GLN LEU SER TRP LEU LYS
SEQRES 16 B 397 GLU PHE GLY VAL ASP PRO LYS PHE VAL HIS THR ALA ASN
SEQRES 17 B 397 SER ALA ALA THR LEU ARG PHE GLN GLY ILE THR PHE ASN
SEQRES 18 B 397 ALA VAL ARG ILE GLY ILE ALA MET TYR GLY LEU SER PRO
SEQRES 19 B 397 SER VAL GLU ILE ARG PRO PHE LEU PRO PHE LYS LEU GLU
SEQRES 20 B 397 PRO ALA LEU SER LEU HIS THR LYS VAL ALA HIS ILE LYS
SEQRES 21 B 397 GLN VAL ILE LYS GLY ASP GLY ILE SER TYR ASN VAL THR
SEQRES 22 B 397 TYR ARG THR LYS THR GLU GLU TRP ILE ALA THR VAL ALA
SEQRES 23 B 397 ILE GLY TYR ALA ASP GLY TRP LEU ARG ARG LEU GLN GLY
SEQRES 24 B 397 PHE GLU VAL LEU VAL ASN GLY LYS ARG VAL PRO ILE VAL
SEQRES 25 B 397 GLY ARG VAL THR MET ASP GLN PHE MET ILE HIS LEU PRO
SEQRES 26 B 397 CYS GLU VAL PRO LEU GLY THR LYS VAL THR LEU ILE GLY
SEQRES 27 B 397 ARG GLN GLY ASP GLU TYR ILE SER ALA THR GLU VAL ALA
SEQRES 28 B 397 GLU TYR SER GLY THR ILE ASN TYR GLU ILE ILE THR THR
SEQRES 29 B 397 ILE SER PHE ARG VAL PRO ARG ILE PHE ILE ARG ASN GLY
SEQRES 30 B 397 LYS VAL VAL GLU VAL ILE ASN TYR LEU ASN ASP ILE LEU
SEQRES 31 B 397 GLU GLU ASN LEU TYR PHE GLN
MODRES 3HA1 LLP A 41 LYS
MODRES 3HA1 LLP B 41 LYS
HET LLP A 41 24
HET LLP B 41 24
HET ACT A 398 4
HET CL A 399 1
HET ACT B 398 4
HET CL B 399 1
HETNAM LLP (2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-
HETNAM 2 LLP (PHOSPHONOOXYMETHYL)PYRIDIN-4-
HETNAM 3 LLP YL]METHYLIDENEAMINO]HEXANOIC ACID
HETNAM ACT ACETATE ION
HETNAM CL CHLORIDE ION
HETSYN LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE
FORMUL 1 LLP 2(C14 H22 N3 O7 P)
FORMUL 3 ACT 2(C2 H3 O2 1-)
FORMUL 4 CL 2(CL 1-)
FORMUL 7 HOH *358(H2 O)
HELIX 1 1 LEU A 16 ILE A 30 1 15
HELIX 2 2 VAL A 40 GLY A 46 1 7
HELIX 3 3 ASP A 48 ALA A 59 1 12
HELIX 4 4 PHE A 68 ALA A 78 1 11
HELIX 5 5 PRO A 91 ARG A 93 5 3
HELIX 6 6 ASP A 94 ASN A 101 1 8
HELIX 7 7 GLN A 109 TRP A 120 1 12
HELIX 8 8 GLU A 143 GLU A 155 1 13
HELIX 9 9 THR A 177 PHE A 197 1 21
HELIX 10 10 ASN A 208 PHE A 215 1 8
HELIX 11 11 ILE A 238 LEU A 242 5 5
HELIX 12 12 SER A 269 THR A 273 5 5
HELIX 13 13 GLY A 288 GLY A 292 5 5
HELIX 14 14 LEU A 294 GLN A 298 5 5
HELIX 15 15 SER A 346 SER A 354 1 9
HELIX 16 16 ILE A 357 THR A 364 1 8
HELIX 17 17 ASN A 384 ILE A 389 5 6
HELIX 18 18 LEU B 16 ILE B 30 1 15
HELIX 19 19 VAL B 40 GLY B 46 1 7
HELIX 20 20 ASP B 48 ALA B 59 1 12
HELIX 21 21 PHE B 68 ALA B 78 1 11
HELIX 22 22 PRO B 91 ARG B 93 5 3
HELIX 23 23 ASP B 94 ASN B 101 1 8
HELIX 24 24 GLN B 109 TRP B 120 1 12
HELIX 25 25 GLU B 143 GLU B 155 1 13
HELIX 26 26 THR B 177 PHE B 197 1 21
HELIX 27 27 ASN B 208 PHE B 215 1 8
HELIX 28 28 GLY B 226 GLY B 231 5 6
HELIX 29 29 ILE B 238 LEU B 242 5 5
HELIX 30 30 SER B 269 THR B 273 5 5
HELIX 31 31 GLY B 288 GLY B 292 5 5
HELIX 32 32 LEU B 294 GLN B 298 5 5
HELIX 33 33 SER B 346 GLY B 355 1 10
HELIX 34 34 ILE B 357 THR B 364 1 8
HELIX 35 35 ASN B 384 ILE B 389 5 6
SHEET 1 A 6 GLU A 343 ILE A 345 0
SHEET 2 A 6 LYS A 333 GLN A 340 -1 N GLY A 338 O ILE A 345
SHEET 3 A 6 LEU A 250 VAL A 262 -1 N THR A 254 O VAL A 334
SHEET 4 A 6 THR A 10 ASP A 15 -1 N GLU A 13 O SER A 251
SHEET 5 A 6 ARG A 371 ARG A 375 1 O ILE A 372 N VAL A 14
SHEET 6 A 6 LYS A 378 ILE A 383 -1 O GLU A 381 N PHE A 373
SHEET 1 B10 GLU A 343 ILE A 345 0
SHEET 2 B10 LYS A 333 GLN A 340 -1 N GLY A 338 O ILE A 345
SHEET 3 B10 GLU A 301 VAL A 304 -1 N LEU A 303 O THR A 335
SHEET 4 B10 LYS A 307 VAL A 312 -1 O VAL A 309 N VAL A 302
SHEET 5 B10 PHE A 320 LEU A 324 -1 O MET A 321 N VAL A 312
SHEET 6 B10 GLU A 280 VAL A 285 -1 N ALA A 283 O ILE A 322
SHEET 7 B10 LEU A 250 VAL A 262 -1 N VAL A 262 O GLU A 280
SHEET 8 B10 THR A 10 ASP A 15 -1 N GLU A 13 O SER A 251
SHEET 9 B10 ARG A 371 ARG A 375 1 O ILE A 372 N VAL A 14
SHEET 10 B10 LYS A 378 ILE A 383 -1 O GLU A 381 N PHE A 373
SHEET 1 C 9 GLU A 35 VAL A 39 0
SHEET 2 C 9 ARG A 63 VAL A 66 1 O ARG A 63 N ALA A 38
SHEET 3 C 9 ILE A 84 VAL A 86 1 O LEU A 85 N LEU A 64
SHEET 4 C 9 VAL A 103 THR A 106 1 O ALA A 104 N VAL A 86
SHEET 5 C 9 MET A 126 ASN A 131 1 O HIS A 129 N LEU A 105
SHEET 6 C 9 LEU A 160 TYR A 166 1 O TYR A 166 N ILE A 130
SHEET 7 C 9 VAL A 204 ALA A 207 1 O HIS A 205 N VAL A 165
SHEET 8 C 9 ALA A 222 ILE A 225 1 O ARG A 224 N ALA A 207
SHEET 9 C 9 GLU A 35 VAL A 39 1 N VAL A 39 O ILE A 225
SHEET 1 D 2 GLY A 267 ILE A 268 0
SHEET 2 D 2 TYR A 274 ARG A 275 -1 O TYR A 274 N ILE A 268
SHEET 1 E 6 GLU B 343 ILE B 345 0
SHEET 2 E 6 LYS B 333 GLN B 340 -1 N GLN B 340 O GLU B 343
SHEET 3 E 6 LEU B 250 VAL B 262 -1 N LEU B 252 O LEU B 336
SHEET 4 E 6 TRP B 11 ASP B 15 -1 N GLU B 13 O SER B 251
SHEET 5 E 6 ARG B 371 ARG B 375 1 O ILE B 372 N VAL B 12
SHEET 6 E 6 LYS B 378 ILE B 383 -1 O GLU B 381 N PHE B 373
SHEET 1 F10 GLU B 343 ILE B 345 0
SHEET 2 F10 LYS B 333 GLN B 340 -1 N GLN B 340 O GLU B 343
SHEET 3 F10 GLU B 301 VAL B 304 -1 N LEU B 303 O THR B 335
SHEET 4 F10 LYS B 307 VAL B 312 -1 O LYS B 307 N VAL B 304
SHEET 5 F10 PHE B 320 LEU B 324 -1 O MET B 321 N VAL B 312
SHEET 6 F10 GLU B 280 VAL B 285 -1 N TRP B 281 O LEU B 324
SHEET 7 F10 LEU B 250 VAL B 262 -1 N LYS B 260 O ILE B 282
SHEET 8 F10 TRP B 11 ASP B 15 -1 N GLU B 13 O SER B 251
SHEET 9 F10 ARG B 371 ARG B 375 1 O ILE B 372 N VAL B 12
SHEET 10 F10 LYS B 378 ILE B 383 -1 O GLU B 381 N PHE B 373
SHEET 1 G 9 GLU B 35 VAL B 39 0
SHEET 2 G 9 ARG B 63 VAL B 66 1 O ARG B 63 N ALA B 38
SHEET 3 G 9 ILE B 84 VAL B 86 1 O LEU B 85 N LEU B 64
SHEET 4 G 9 VAL B 103 THR B 106 1 O ALA B 104 N VAL B 86
SHEET 5 G 9 MET B 126 ASN B 131 1 O HIS B 129 N LEU B 105
SHEET 6 G 9 LEU B 160 TYR B 166 1 O GLU B 163 N TYR B 128
SHEET 7 G 9 VAL B 204 ALA B 207 1 O HIS B 205 N VAL B 165
SHEET 8 G 9 ALA B 222 ILE B 225 1 O ARG B 224 N ALA B 207
SHEET 9 G 9 GLU B 35 VAL B 39 1 N PHE B 37 O VAL B 223
SHEET 1 H 2 GLY B 267 ILE B 268 0
SHEET 2 H 2 TYR B 274 ARG B 275 -1 O TYR B 274 N ILE B 268
LINK C VAL A 40 N LLP A 41 1555 1555 1.33
LINK C LLP A 41 N GLY A 42 1555 1555 1.34
LINK C VAL B 40 N LLP B 41 1555 1555 1.33
LINK C LLP B 41 N GLY B 42 1555 1555 1.33
SITE 1 AC1 7 TYR A 270 TYR A 289 THR A 316 MET A 317
SITE 2 AC1 7 HOH A 404 HOH A 496 LLP B 41
SITE 1 AC2 2 ASN A 131 ARG A 138
SITE 1 AC3 9 LLP A 41 TYR A 359 TYR B 270 TYR B 289
SITE 2 AC3 9 THR B 316 MET B 317 HOH B 465 HOH B 535
SITE 3 AC3 9 HOH B 570
SITE 1 AC4 2 ASN B 131 ARG B 138
CRYST1 49.624 141.271 60.124 90.00 103.11 90.00 P 1 21 1 4
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 0.020152 0.000000 0.004692 0.00000
SCALE2 0.000000 0.007079 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017077 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
