HEADER TRANSFERASE 01-APR-06 2CJG
TITLE LYSINE AMINOTRANSFERASE FROM M. TUBERCULOSIS IN BOUND PMP FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: L-LYSINE-EPSILON AMINOTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: L-LYSINE AMINOTRANSFERASE, LYSINE 6-AMINOTRANSFERASE;
COMPND 5 EC: 2.6.1.36;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: C41;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET23A
KEYWDS TRANSFERASE, INTERNAL ALDIMINE, PYRIDOXAL PHOSPHATE, PLP, RV3290C,
KEYWDS 2 AMINOTRANSFERASE, LYSINE AMINO TRANSFERASE, MYCOBACTERIUM
KEYWDS 3 TUBERCULOSIS
EXPDTA X-RAY DIFFRACTION
AUTHOR S.M.TRIPATHI,R.RAMACHANDRAN
REVDAT 3 24-JAN-18 2CJG 1 SOURCE
REVDAT 2 24-FEB-09 2CJG 1 VERSN
REVDAT 1 14-AUG-06 2CJG 0
JRNL AUTH S.M.TRIPATHI,R.RAMACHANDRAN
JRNL TITL DIRECT EVIDENCE FOR A GLUTAMATE SWITCH NECESSARY FOR
JRNL TITL 2 SUBSTRATE RECOGNITION: CRYSTAL STRUCTURES OF LYSINE
JRNL TITL 3 EPSILON-AMINOTRANSFERASE (RV3290C) FROM MYCOBACTERIUM
JRNL TITL 4 TUBERCULOSIS H37RV.
JRNL REF J.MOL.BIOL. V. 362 877 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16950391
JRNL DOI 10.1016/J.JMB.2006.08.019
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 89.44
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 42208
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) : 0.159
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2243
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) : 3082
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2340
REMARK 3 BIN FREE R VALUE SET COUNT : 162
REMARK 3 BIN FREE R VALUE : 0.2690
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3350
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 244
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.10000
REMARK 3 B22 (A**2) : -0.10000
REMARK 3 B33 (A**2) : 0.15000
REMARK 3 B12 (A**2) : -0.05000
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): 0.114
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.108
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.075
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.632
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3441 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4682 ; 1.544 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 434 ; 5.791 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 159 ;34.537 ;22.579
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 532 ;17.469 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;21.881 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 524 ; 0.124 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2671 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1466 ; 0.212 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2383 ; 0.308 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 215 ; 0.122 ; 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): 72 ; 0.244 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 19 ; 0.082 ; 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): 2212 ; 0.888 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3475 ; 1.528 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1361 ; 2.627 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1207 ; 4.291 ; 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 : 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 : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. RESIDUE 1-14 ARE DISORDERED.
REMARK 4
REMARK 4 2CJG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1290028390.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 293.0
REMARK 200 PH : NULL
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 RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44486
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 20.520
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 20.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.3000
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.58000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 32.75533
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 65.51067
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 65.51067
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 32.75533
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: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 98.26600
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 ALA A 2
REMARK 465 ALA A 3
REMARK 465 VAL A 4
REMARK 465 VAL A 5
REMARK 465 LYS A 6
REMARK 465 SER A 7
REMARK 465 VAL A 8
REMARK 465 ALA A 9
REMARK 465 LEU A 10
REMARK 465 ALA A 11
REMARK 465 GLY A 12
REMARK 465 ARG A 13
REMARK 465 PRO A 14
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 ARG A 79 CG CD NE CZ NH1 NH2
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 NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 55 NE - CZ - NH1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG A 55 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG A 112 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 222 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 258 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG A 258 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG A 340 NE - CZ - NH1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG A 340 NE - CZ - NH2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 ARG A 385 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG A 422 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 422 NE - CZ - NH2 ANGL. DEV. = -3.4 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 ASN A 179 80.00 -151.95
REMARK 500 THR A 180 -90.34 -117.49
REMARK 500 LYS A 300 -102.33 54.58
REMARK 500 GLN A 303 -57.71 72.03
REMARK 500 ARG A 311 -118.96 44.73
REMARK 500 ASP A 318 40.39 -103.90
REMARK 500 ASP A 419 18.05 -144.09
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 PMP A1450
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2CIN RELATED DB: PDB
REMARK 900 LYSINE AMINOTRANSFERASE FROM M. TUBERCULOSIS IN THE INTERNAL
REMARK 900 ALDIMINE FORM
REMARK 900 RELATED ID: 2CJD RELATED DB: PDB
REMARK 900 LYSINE AMINOTRANSFERASE FROM M. TUBERCULOSIS IN EXTERNAL ALDIMINE
REMARK 900 FORM
REMARK 900 RELATED ID: 2CJH RELATED DB: PDB
REMARK 900 LYSINE AMINOTRANSFERASE FROM M. TUBERCULOSIS IN THE INTERNAL
REMARK 900 ALDIMINE FORM WITH BOUND SUBSTRATE 2-KETOGLUTARATE
DBREF 2CJG A 1 449 UNP P63509 LAT_MYCTU 1 449
SEQRES 1 A 449 MET ALA ALA VAL VAL LYS SER VAL ALA LEU ALA GLY ARG
SEQRES 2 A 449 PRO THR THR PRO ASP ARG VAL HIS GLU VAL LEU GLY ARG
SEQRES 3 A 449 SER MET LEU VAL ASP GLY LEU ASP ILE VAL LEU ASP LEU
SEQRES 4 A 449 THR ARG SER GLY GLY SER TYR LEU VAL ASP ALA ILE THR
SEQRES 5 A 449 GLY ARG ARG TYR LEU ASP MET PHE THR PHE VAL ALA SER
SEQRES 6 A 449 SER ALA LEU GLY MET ASN PRO PRO ALA LEU VAL ASP ASP
SEQRES 7 A 449 ARG GLU PHE HIS ALA GLU LEU MET GLN ALA ALA LEU ASN
SEQRES 8 A 449 LYS PRO SER ASN SER ASP VAL TYR SER VAL ALA MET ALA
SEQRES 9 A 449 ARG PHE VAL GLU THR PHE ALA ARG VAL LEU GLY ASP PRO
SEQRES 10 A 449 ALA LEU PRO HIS LEU PHE PHE VAL GLU GLY GLY ALA LEU
SEQRES 11 A 449 ALA VAL GLU ASN ALA LEU LYS ALA ALA PHE ASP TRP LYS
SEQRES 12 A 449 SER ARG HIS ASN GLN ALA HIS GLY ILE ASP PRO ALA LEU
SEQRES 13 A 449 GLY THR GLN VAL LEU HIS LEU ARG GLY ALA PHE HIS GLY
SEQRES 14 A 449 ARG SER GLY TYR THR LEU SER LEU THR ASN THR LYS PRO
SEQRES 15 A 449 THR ILE THR ALA ARG PHE PRO LYS PHE ASP TRP PRO ARG
SEQRES 16 A 449 ILE ASP ALA PRO TYR MET ARG PRO GLY LEU ASP GLU PRO
SEQRES 17 A 449 ALA MET ALA ALA LEU GLU ALA GLU ALA LEU ARG GLN ALA
SEQRES 18 A 449 ARG ALA ALA PHE GLU THR ARG PRO HIS ASP ILE ALA CYS
SEQRES 19 A 449 PHE VAL ALA GLU PRO ILE GLN GLY GLU GLY GLY ASP ARG
SEQRES 20 A 449 HIS PHE ARG PRO GLU PHE PHE ALA ALA MET ARG GLU LEU
SEQRES 21 A 449 CYS ASP GLU PHE ASP ALA LEU LEU ILE PHE ASP GLU VAL
SEQRES 22 A 449 GLN THR GLY CYS GLY LEU THR GLY THR ALA TRP ALA TYR
SEQRES 23 A 449 GLN GLN LEU ASP VAL ALA PRO ASP ILE VAL ALA PHE GLY
SEQRES 24 A 449 LYS LYS THR GLN VAL CYS GLY VAL MET ALA GLY ARG ARG
SEQRES 25 A 449 VAL ASP GLU VAL ALA ASP ASN VAL PHE ALA VAL PRO SER
SEQRES 26 A 449 ARG LEU ASN SER THR TRP GLY GLY ASN LEU THR ASP MET
SEQRES 27 A 449 VAL ARG ALA ARG ARG ILE LEU GLU VAL ILE GLU ALA GLU
SEQRES 28 A 449 GLY LEU PHE GLU ARG ALA VAL GLN HIS GLY LYS TYR LEU
SEQRES 29 A 449 ARG ALA ARG LEU ASP GLU LEU ALA ALA ASP PHE PRO ALA
SEQRES 30 A 449 VAL VAL LEU ASP PRO ARG GLY ARG GLY LEU MET CYS ALA
SEQRES 31 A 449 PHE SER LEU PRO THR THR ALA ASP ARG ASP GLU LEU ILE
SEQRES 32 A 449 ARG GLN LEU TRP GLN ARG ALA VAL ILE VAL LEU PRO ALA
SEQRES 33 A 449 GLY ALA ASP THR VAL ARG PHE ARG PRO PRO LEU THR VAL
SEQRES 34 A 449 SER THR ALA GLU ILE ASP ALA ALA ILE ALA ALA VAL ARG
SEQRES 35 A 449 SER ALA LEU PRO VAL VAL THR
HET PMP A1450 16
HETNAM PMP 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE
HETSYN PMP PYRIDOXAMINE-5'-PHOSPHATE
FORMUL 2 PMP C8 H13 N2 O5 P
FORMUL 3 HOH *244(H2 O)
HELIX 1 1 THR A 16 ASP A 18 5 3
HELIX 2 2 ARG A 19 ARG A 26 1 8
HELIX 3 3 PHE A 60 SER A 65 1 6
HELIX 4 4 PRO A 72 ASP A 77 1 6
HELIX 5 5 ASP A 78 LEU A 90 1 13
HELIX 6 6 SER A 100 GLY A 115 1 16
HELIX 7 7 GLY A 127 HIS A 150 1 24
HELIX 8 8 TYR A 173 LEU A 177 5 5
HELIX 9 9 LYS A 181 ALA A 186 1 6
HELIX 10 10 ASP A 206 ARG A 228 1 23
HELIX 11 11 ARG A 250 PHE A 264 1 15
HELIX 12 12 ALA A 285 ASP A 290 1 6
HELIX 13 13 GLY A 299 GLN A 303 5 5
HELIX 14 14 ARG A 311 VAL A 316 5 6
HELIX 15 15 ASN A 334 GLY A 352 1 19
HELIX 16 16 GLY A 352 PHE A 375 1 24
HELIX 17 17 THR A 395 ARG A 409 1 15
HELIX 18 18 SER A 430 THR A 449 1 20
SHEET 1 AA 3 TYR A 46 VAL A 48 0
SHEET 2 AA 3 ARG A 55 ASP A 58 -1 O TYR A 56 N LEU A 47
SHEET 3 AA 3 VAL A 411 ILE A 412 1 N ILE A 412 O LEU A 57
SHEET 1 AB 7 HIS A 121 VAL A 125 0
SHEET 2 AB 7 CYS A 305 ALA A 309 -1 O CYS A 305 N VAL A 125
SHEET 3 AB 7 ILE A 295 PHE A 298 -1 O VAL A 296 N MET A 308
SHEET 4 AB 7 LEU A 267 ASP A 271 1 O PHE A 270 N ALA A 297
SHEET 5 AB 7 ILE A 232 ALA A 237 1 O ALA A 233 N LEU A 267
SHEET 6 AB 7 GLN A 159 LEU A 163 1 O GLN A 159 N ALA A 233
SHEET 7 AB 7 ARG A 195 ILE A 196 1 N ILE A 196 O HIS A 162
SHEET 1 AC 2 ILE A 240 GLN A 241 0
SHEET 2 AC 2 ARG A 247 HIS A 248 -1 O ARG A 247 N GLN A 241
SHEET 1 AD 4 LEU A 380 ARG A 385 0
SHEET 2 AD 4 MET A 388 SER A 392 -1 O MET A 388 N ARG A 385
SHEET 3 AD 4 THR A 420 PHE A 423 -1 O VAL A 421 N PHE A 391
SHEET 4 AD 4 LEU A 414 ALA A 416 -1 O LEU A 414 N ARG A 422
SITE 1 AC1 17 GLY A 128 ALA A 129 PHE A 167 HIS A 168
SITE 2 AC1 17 GLU A 238 GLU A 243 ASP A 271 VAL A 273
SITE 3 AC1 17 GLN A 274 LYS A 300 THR A 330 HOH A2129
SITE 4 AC1 17 HOH A2240 HOH A2241 HOH A2242 HOH A2243
SITE 5 AC1 17 HOH A2244
CRYST1 103.270 103.270 98.266 90.00 90.00 120.00 P 31 2 1 6
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 0.009683 0.005591 0.000000 0.00000
SCALE2 0.000000 0.011181 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010176 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
