HEADER TRANSFERASE 02-FEB-01 1I1L
TITLE CRYSTAL STRUCTURE OF ESCHELICHIA COLI BRANCHED-CHAIN AMINO ACID
TITLE 2 AMINOTRANSFERASE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 EC: 2.6.1.42;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS AMINOTRANSFERASE, HEXAMER, PLP, 2-METHYLLEUCINE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.OKADA,K.HIROTSU,H.HAYASHI,H.KAGAMIYAMA
REVDAT 5 13-MAR-24 1I1L 1 REMARK LINK
REVDAT 4 13-JUL-11 1I1L 1 VERSN
REVDAT 3 24-FEB-09 1I1L 1 VERSN
REVDAT 2 31-DEC-02 1I1L 1 REMARK
REVDAT 1 04-JUL-01 1I1L 0
JRNL AUTH K.OKADA,K.HIROTSU,H.HAYASHI,H.KAGAMIYAMA
JRNL TITL STRUCTURES OF ESCHERICHIA COLI BRANCHED-CHAIN AMINO ACID
JRNL TITL 2 AMINOTRANSFERASE AND ITS COMPLEXES WITH 4-METHYLVALERATE AND
JRNL TITL 3 2-METHYLLEUCINE: INDUCED FIT AND SUBSTRATE RECOGNITION OF
JRNL TITL 4 THE ENZYME.
JRNL REF BIOCHEMISTRY V. 40 7453 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11412098
JRNL DOI 10.1021/BI0028441
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7086
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 75
REMARK 3 SOLVENT ATOMS : 304
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1I1L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-FEB-01.
REMARK 100 THE DEPOSITION ID IS D_1000012789.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JAN-97
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 7.5
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 RU200H
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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 (%): 54.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG400, PH 7.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.78000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.78000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 78.04500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.38500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 78.04500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.38500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 70.78000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 78.04500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 50.38500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 70.78000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 78.04500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 50.38500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 28310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -131.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 -1.000000 0.000000 0.000000 156.09000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 70.78000
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 0
REMARK 465 THR A 1
REMARK 465 THR A 2
REMARK 465 LYS A 3
REMARK 465 GLN A 308
REMARK 465 MET B 500
REMARK 465 THR B 501
REMARK 465 THR B 502
REMARK 465 LYS B 503
REMARK 465 GLN B 808
REMARK 465 MET C 1000
REMARK 465 THR C 1001
REMARK 465 THR C 1002
REMARK 465 LYS C 1003
REMARK 465 GLN C 1308
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 181 CD GLU A 181 OE2 0.077
REMARK 500 GLU B 681 CD GLU B 681 OE2 0.081
REMARK 500 GLU C1181 CD GLU C1181 OE2 0.077
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 ASP A 104 77.25 -69.15
REMARK 500 VAL A 105 -160.11 -113.84
REMARK 500 ASN A 152 50.09 -115.26
REMARK 500 THR A 153 -74.65 -118.09
REMARK 500 SER A 192 -72.17 -102.88
REMARK 500 GLU A 193 -179.36 -177.54
REMARK 500 LYS A 203 -112.67 -96.71
REMARK 500 LEU A 207 -94.05 -62.80
REMARK 500 PHE A 208 121.40 96.08
REMARK 500 PRO A 218 74.86 -67.46
REMARK 500 GLU A 260 -114.98 55.77
REMARK 500 GLU A 274 -24.76 85.93
REMARK 500 SER B 544 -168.40 -119.38
REMARK 500 VAL B 605 -158.26 -113.82
REMARK 500 THR B 653 -76.59 -116.58
REMARK 500 SER B 692 -70.86 -102.59
REMARK 500 GLU B 693 -179.64 -179.95
REMARK 500 LYS B 703 -118.07 -93.92
REMARK 500 LEU B 707 -95.67 -59.44
REMARK 500 PHE B 708 120.79 98.22
REMARK 500 PRO B 718 76.00 -69.27
REMARK 500 GLU B 760 -116.51 56.42
REMARK 500 GLU B 774 -23.82 87.11
REMARK 500 VAL C1105 -159.90 -116.04
REMARK 500 ASN C1152 50.51 -113.62
REMARK 500 THR C1153 -73.64 -119.63
REMARK 500 SER C1192 -70.70 -103.06
REMARK 500 LYS C1203 -113.70 -96.70
REMARK 500 LEU C1207 -96.06 -60.58
REMARK 500 PHE C1208 119.50 95.23
REMARK 500 PRO C1218 74.91 -69.41
REMARK 500 GLU C1260 -117.61 55.01
REMARK 500 GLU C1274 -23.83 84.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR B 664 0.07 SIDE CHAIN
REMARK 500 TYR C1164 0.06 SIDE CHAIN
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 PLP A 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2ML A 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 913
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2ML B 914
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP C 1413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2ML C 1414
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1I1K RELATED DB: PDB
REMARK 900 1I1K CONTAINS THE SAME PROTEIN
REMARK 900 RELATED ID: 1I1M RELATED DB: PDB
REMARK 900 1I1M CONTAINS THE SAME PROTEIN COMPLEXED WITH 4-METHYLVARELATE
DBREF 1I1L A 0 308 UNP P00510 ILVE_ECOLI 1 309
DBREF 1I1L B 500 808 UNP P00510 ILVE_ECOLI 1 309
DBREF 1I1L C 1000 1308 UNP P00510 ILVE_ECOLI 1 309
SEQRES 1 A 309 MET THR THR LYS LYS ALA ASP TYR ILE TRP PHE ASN GLY
SEQRES 2 A 309 GLU MET VAL ARG TRP GLU ASP ALA LYS VAL HIS VAL MET
SEQRES 3 A 309 SER HIS ALA LEU HIS TYR GLY THR SER VAL PHE GLU GLY
SEQRES 4 A 309 ILE ARG CYS TYR ASP SER HIS LYS GLY PRO VAL VAL PHE
SEQRES 5 A 309 ARG HIS ARG GLU HIS MET GLN ARG LEU HIS ASP SER ALA
SEQRES 6 A 309 LYS ILE TYR ARG PHE PRO VAL SER GLN SER ILE ASP GLU
SEQRES 7 A 309 LEU MET GLU ALA CYS ARG ASP VAL ILE ARG LYS ASN ASN
SEQRES 8 A 309 LEU THR SER ALA TYR ILE ARG PRO LEU ILE PHE VAL GLY
SEQRES 9 A 309 ASP VAL GLY MET GLY VAL ASN PRO PRO ALA GLY TYR SER
SEQRES 10 A 309 THR ASP VAL ILE ILE ALA ALA PHE PRO TRP GLY ALA TYR
SEQRES 11 A 309 LEU GLY ALA GLU ALA LEU GLU GLN GLY ILE ASP ALA MET
SEQRES 12 A 309 VAL SER SER TRP ASN ARG ALA ALA PRO ASN THR ILE PRO
SEQRES 13 A 309 THR ALA ALA LYS ALA GLY GLY ASN TYR LEU SER SER LEU
SEQRES 14 A 309 LEU VAL GLY SER GLU ALA ARG ARG HIS GLY TYR GLN GLU
SEQRES 15 A 309 GLY ILE ALA LEU ASP VAL ASN GLY TYR ILE SER GLU GLY
SEQRES 16 A 309 ALA GLY GLU ASN LEU PHE GLU VAL LYS ASP GLY VAL LEU
SEQRES 17 A 309 PHE THR PRO PRO PHE THR SER SER ALA LEU PRO GLY ILE
SEQRES 18 A 309 THR ARG ASP ALA ILE ILE LYS LEU ALA LYS GLU LEU GLY
SEQRES 19 A 309 ILE GLU VAL ARG GLU GLN VAL LEU SER ARG GLU SER LEU
SEQRES 20 A 309 TYR LEU ALA ASP GLU VAL PHE MET SER GLY THR ALA ALA
SEQRES 21 A 309 GLU ILE THR PRO VAL ARG SER VAL ASP GLY ILE GLN VAL
SEQRES 22 A 309 GLY GLU GLY ARG CYS GLY PRO VAL THR LYS ARG ILE GLN
SEQRES 23 A 309 GLN ALA PHE PHE GLY LEU PHE THR GLY GLU THR GLU ASP
SEQRES 24 A 309 LYS TRP GLY TRP LEU ASP GLN VAL ASN GLN
SEQRES 1 B 309 MET THR THR LYS LYS ALA ASP TYR ILE TRP PHE ASN GLY
SEQRES 2 B 309 GLU MET VAL ARG TRP GLU ASP ALA LYS VAL HIS VAL MET
SEQRES 3 B 309 SER HIS ALA LEU HIS TYR GLY THR SER VAL PHE GLU GLY
SEQRES 4 B 309 ILE ARG CYS TYR ASP SER HIS LYS GLY PRO VAL VAL PHE
SEQRES 5 B 309 ARG HIS ARG GLU HIS MET GLN ARG LEU HIS ASP SER ALA
SEQRES 6 B 309 LYS ILE TYR ARG PHE PRO VAL SER GLN SER ILE ASP GLU
SEQRES 7 B 309 LEU MET GLU ALA CYS ARG ASP VAL ILE ARG LYS ASN ASN
SEQRES 8 B 309 LEU THR SER ALA TYR ILE ARG PRO LEU ILE PHE VAL GLY
SEQRES 9 B 309 ASP VAL GLY MET GLY VAL ASN PRO PRO ALA GLY TYR SER
SEQRES 10 B 309 THR ASP VAL ILE ILE ALA ALA PHE PRO TRP GLY ALA TYR
SEQRES 11 B 309 LEU GLY ALA GLU ALA LEU GLU GLN GLY ILE ASP ALA MET
SEQRES 12 B 309 VAL SER SER TRP ASN ARG ALA ALA PRO ASN THR ILE PRO
SEQRES 13 B 309 THR ALA ALA LYS ALA GLY GLY ASN TYR LEU SER SER LEU
SEQRES 14 B 309 LEU VAL GLY SER GLU ALA ARG ARG HIS GLY TYR GLN GLU
SEQRES 15 B 309 GLY ILE ALA LEU ASP VAL ASN GLY TYR ILE SER GLU GLY
SEQRES 16 B 309 ALA GLY GLU ASN LEU PHE GLU VAL LYS ASP GLY VAL LEU
SEQRES 17 B 309 PHE THR PRO PRO PHE THR SER SER ALA LEU PRO GLY ILE
SEQRES 18 B 309 THR ARG ASP ALA ILE ILE LYS LEU ALA LYS GLU LEU GLY
SEQRES 19 B 309 ILE GLU VAL ARG GLU GLN VAL LEU SER ARG GLU SER LEU
SEQRES 20 B 309 TYR LEU ALA ASP GLU VAL PHE MET SER GLY THR ALA ALA
SEQRES 21 B 309 GLU ILE THR PRO VAL ARG SER VAL ASP GLY ILE GLN VAL
SEQRES 22 B 309 GLY GLU GLY ARG CYS GLY PRO VAL THR LYS ARG ILE GLN
SEQRES 23 B 309 GLN ALA PHE PHE GLY LEU PHE THR GLY GLU THR GLU ASP
SEQRES 24 B 309 LYS TRP GLY TRP LEU ASP GLN VAL ASN GLN
SEQRES 1 C 309 MET THR THR LYS LYS ALA ASP TYR ILE TRP PHE ASN GLY
SEQRES 2 C 309 GLU MET VAL ARG TRP GLU ASP ALA LYS VAL HIS VAL MET
SEQRES 3 C 309 SER HIS ALA LEU HIS TYR GLY THR SER VAL PHE GLU GLY
SEQRES 4 C 309 ILE ARG CYS TYR ASP SER HIS LYS GLY PRO VAL VAL PHE
SEQRES 5 C 309 ARG HIS ARG GLU HIS MET GLN ARG LEU HIS ASP SER ALA
SEQRES 6 C 309 LYS ILE TYR ARG PHE PRO VAL SER GLN SER ILE ASP GLU
SEQRES 7 C 309 LEU MET GLU ALA CYS ARG ASP VAL ILE ARG LYS ASN ASN
SEQRES 8 C 309 LEU THR SER ALA TYR ILE ARG PRO LEU ILE PHE VAL GLY
SEQRES 9 C 309 ASP VAL GLY MET GLY VAL ASN PRO PRO ALA GLY TYR SER
SEQRES 10 C 309 THR ASP VAL ILE ILE ALA ALA PHE PRO TRP GLY ALA TYR
SEQRES 11 C 309 LEU GLY ALA GLU ALA LEU GLU GLN GLY ILE ASP ALA MET
SEQRES 12 C 309 VAL SER SER TRP ASN ARG ALA ALA PRO ASN THR ILE PRO
SEQRES 13 C 309 THR ALA ALA LYS ALA GLY GLY ASN TYR LEU SER SER LEU
SEQRES 14 C 309 LEU VAL GLY SER GLU ALA ARG ARG HIS GLY TYR GLN GLU
SEQRES 15 C 309 GLY ILE ALA LEU ASP VAL ASN GLY TYR ILE SER GLU GLY
SEQRES 16 C 309 ALA GLY GLU ASN LEU PHE GLU VAL LYS ASP GLY VAL LEU
SEQRES 17 C 309 PHE THR PRO PRO PHE THR SER SER ALA LEU PRO GLY ILE
SEQRES 18 C 309 THR ARG ASP ALA ILE ILE LYS LEU ALA LYS GLU LEU GLY
SEQRES 19 C 309 ILE GLU VAL ARG GLU GLN VAL LEU SER ARG GLU SER LEU
SEQRES 20 C 309 TYR LEU ALA ASP GLU VAL PHE MET SER GLY THR ALA ALA
SEQRES 21 C 309 GLU ILE THR PRO VAL ARG SER VAL ASP GLY ILE GLN VAL
SEQRES 22 C 309 GLY GLU GLY ARG CYS GLY PRO VAL THR LYS ARG ILE GLN
SEQRES 23 C 309 GLN ALA PHE PHE GLY LEU PHE THR GLY GLU THR GLU ASP
SEQRES 24 C 309 LYS TRP GLY TRP LEU ASP GLN VAL ASN GLN
HET PLP A 413 15
HET 2ML A 414 10
HET PLP B 913 15
HET 2ML B 914 10
HET PLP C1413 15
HET 2ML C1414 10
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETNAM 2ML 2-METHYLLEUCINE
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 4 PLP 3(C8 H10 N O6 P)
FORMUL 5 2ML 3(C7 H15 N O2)
FORMUL 10 HOH *304(H2 O)
HELIX 1 1 GLU A 18 ALA A 20 5 3
HELIX 2 2 SER A 26 GLY A 32 1 7
HELIX 3 3 ARG A 52 ARG A 68 1 17
HELIX 4 4 SER A 74 ASN A 89 1 16
HELIX 5 5 ASN A 163 HIS A 177 1 15
HELIX 6 6 PRO A 211 SER A 215 5 5
HELIX 7 7 GLY A 219 LEU A 232 1 14
HELIX 8 8 GLU A 244 ALA A 249 1 6
HELIX 9 9 GLY A 273 ARG A 276 5 4
HELIX 10 10 GLY A 278 GLY A 290 1 13
HELIX 11 11 GLU B 518 ALA B 520 5 3
HELIX 12 12 SER B 526 GLY B 532 1 7
HELIX 13 13 ARG B 552 ARG B 568 1 17
HELIX 14 14 SER B 574 ASN B 589 1 16
HELIX 15 15 ALA B 632 GLU B 636 5 5
HELIX 16 16 ASN B 663 HIS B 677 1 15
HELIX 17 17 PRO B 711 SER B 715 5 5
HELIX 18 18 GLY B 719 LEU B 732 1 14
HELIX 19 19 GLU B 744 ALA B 749 1 6
HELIX 20 20 GLY B 773 ARG B 776 5 4
HELIX 21 21 GLY B 778 GLY B 790 1 13
HELIX 22 22 GLU C 1018 ALA C 1020 5 3
HELIX 23 23 SER C 1026 GLY C 1032 1 7
HELIX 24 24 ARG C 1052 ARG C 1068 1 17
HELIX 25 25 SER C 1074 ASN C 1089 1 16
HELIX 26 26 ASN C 1163 HIS C 1177 1 15
HELIX 27 27 PRO C 1211 SER C 1215 5 5
HELIX 28 28 GLY C 1219 LEU C 1232 1 14
HELIX 29 29 GLU C 1244 ALA C 1249 1 6
HELIX 30 30 GLY C 1273 ARG C 1276 5 4
HELIX 31 31 GLY C 1278 GLY C 1290 1 13
SHEET 1 A 5 GLU A 13 ARG A 16 0
SHEET 2 A 5 TYR A 7 PHE A 10 -1 N ILE A 8 O VAL A 15
SHEET 3 A 5 ASP A 118 PHE A 124 -1 N ILE A 121 O TRP A 9
SHEET 4 A 5 ALA A 94 PHE A 101 -1 N TYR A 95 O PHE A 124
SHEET 5 A 5 SER A 34 PHE A 36 -1 O VAL A 35 N ILE A 100
SHEET 1 B 7 GLU A 13 ARG A 16 0
SHEET 2 B 7 TYR A 7 PHE A 10 -1 N ILE A 8 O VAL A 15
SHEET 3 B 7 ASP A 118 PHE A 124 -1 N ILE A 121 O TRP A 9
SHEET 4 B 7 ALA A 94 PHE A 101 -1 N TYR A 95 O PHE A 124
SHEET 5 B 7 ILE A 39 SER A 44 -1 O ILE A 39 N ILE A 96
SHEET 6 B 7 GLY A 47 PHE A 51 -1 N GLY A 47 O SER A 44
SHEET 7 B 7 LEU A 303 GLN A 305 -1 O ASP A 304 N VAL A 50
SHEET 1 C 6 ASN A 198 VAL A 202 0
SHEET 2 C 6 GLU A 251 GLY A 256 -1 N GLU A 251 O VAL A 202
SHEET 3 C 6 GLU A 260 VAL A 267 -1 N GLU A 260 O GLY A 256
SHEET 4 C 6 ILE A 139 VAL A 143 1 O ILE A 139 N ARG A 265
SHEET 5 C 6 GLU A 181 LEU A 185 1 O GLU A 181 N MET A 142
SHEET 6 C 6 ILE A 191 GLY A 194 -1 N SER A 192 O ALA A 184
SHEET 1 D 4 ASN A 198 VAL A 202 0
SHEET 2 D 4 GLU A 251 GLY A 256 -1 N GLU A 251 O VAL A 202
SHEET 3 D 4 GLU A 260 VAL A 267 -1 N GLU A 260 O GLY A 256
SHEET 4 D 4 ILE A 270 GLN A 271 -1 O ILE A 270 N VAL A 267
SHEET 1 E 5 GLU B 513 ARG B 516 0
SHEET 2 E 5 TYR B 507 PHE B 510 -1 N ILE B 508 O VAL B 515
SHEET 3 E 5 ASP B 618 PHE B 624 -1 O ILE B 621 N TRP B 509
SHEET 4 E 5 ALA B 594 PHE B 601 -1 N TYR B 595 O PHE B 624
SHEET 5 E 5 SER B 534 PHE B 536 -1 O VAL B 535 N ILE B 600
SHEET 1 F 7 GLU B 513 ARG B 516 0
SHEET 2 F 7 TYR B 507 PHE B 510 -1 N ILE B 508 O VAL B 515
SHEET 3 F 7 ASP B 618 PHE B 624 -1 O ILE B 621 N TRP B 509
SHEET 4 F 7 ALA B 594 PHE B 601 -1 N TYR B 595 O PHE B 624
SHEET 5 F 7 ILE B 539 SER B 544 -1 O ILE B 539 N ILE B 596
SHEET 6 F 7 GLY B 547 PHE B 551 -1 N GLY B 547 O SER B 544
SHEET 7 F 7 LEU B 803 GLN B 805 -1 O ASP B 804 N VAL B 550
SHEET 1 G 6 ASN B 698 VAL B 702 0
SHEET 2 G 6 GLU B 751 GLY B 756 -1 N GLU B 751 O VAL B 702
SHEET 3 G 6 GLU B 760 VAL B 767 -1 N GLU B 760 O GLY B 756
SHEET 4 G 6 ILE B 639 VAL B 643 1 O ILE B 639 N ARG B 765
SHEET 5 G 6 GLU B 681 LEU B 685 1 O GLU B 681 N MET B 642
SHEET 6 G 6 ILE B 691 GLY B 694 -1 N SER B 692 O ALA B 684
SHEET 1 H 4 ASN B 698 VAL B 702 0
SHEET 2 H 4 GLU B 751 GLY B 756 -1 N GLU B 751 O VAL B 702
SHEET 3 H 4 GLU B 760 VAL B 767 -1 N GLU B 760 O GLY B 756
SHEET 4 H 4 ILE B 770 GLN B 771 -1 O ILE B 770 N VAL B 767
SHEET 1 I 5 GLU C1013 ARG C1016 0
SHEET 2 I 5 TYR C1007 PHE C1010 -1 N ILE C1008 O VAL C1015
SHEET 3 I 5 ASP C1118 PHE C1124 -1 O ILE C1121 N TRP C1009
SHEET 4 I 5 ALA C1094 PHE C1101 -1 N TYR C1095 O PHE C1124
SHEET 5 I 5 SER C1034 PHE C1036 -1 O VAL C1035 N ILE C1100
SHEET 1 J 7 GLU C1013 ARG C1016 0
SHEET 2 J 7 TYR C1007 PHE C1010 -1 N ILE C1008 O VAL C1015
SHEET 3 J 7 ASP C1118 PHE C1124 -1 O ILE C1121 N TRP C1009
SHEET 4 J 7 ALA C1094 PHE C1101 -1 N TYR C1095 O PHE C1124
SHEET 5 J 7 ILE C1039 SER C1044 -1 O ILE C1039 N ILE C1096
SHEET 6 J 7 GLY C1047 PHE C1051 -1 N GLY C1047 O SER C1044
SHEET 7 J 7 LEU C1303 GLN C1305 -1 O ASP C1304 N VAL C1050
SHEET 1 K 6 ASN C1198 VAL C1202 0
SHEET 2 K 6 GLU C1251 GLY C1256 -1 N GLU C1251 O VAL C1202
SHEET 3 K 6 GLU C1260 VAL C1267 -1 N GLU C1260 O GLY C1256
SHEET 4 K 6 ILE C1139 VAL C1143 1 O ILE C1139 N ARG C1265
SHEET 5 K 6 GLU C1181 LEU C1185 1 O GLU C1181 N MET C1142
SHEET 6 K 6 ILE C1191 GLY C1194 -1 N SER C1192 O ALA C1184
SHEET 1 L 4 ASN C1198 VAL C1202 0
SHEET 2 L 4 GLU C1251 GLY C1256 -1 N GLU C1251 O VAL C1202
SHEET 3 L 4 GLU C1260 VAL C1267 -1 N GLU C1260 O GLY C1256
SHEET 4 L 4 ILE C1270 GLN C1271 -1 O ILE C1270 N VAL C1267
LINK C4A PLP A 413 N 2ML A 414 1555 1555 1.40
LINK C4A PLP B 913 N 2ML B 914 1555 1555 1.38
LINK C4A PLP C1413 N 2ML C1414 1555 1555 1.42
SITE 1 AC1 13 ARG A 59 LYS A 159 TYR A 164 GLU A 193
SITE 2 AC1 13 GLY A 196 ASN A 198 GLY A 219 ILE A 220
SITE 3 AC1 13 THR A 221 THR A 257 2ML A 414 HOH A 415
SITE 4 AC1 13 HOH A 421
SITE 1 AC2 8 GLY A 38 TYR A 95 LYS A 159 GLY A 196
SITE 2 AC2 8 THR A 257 ALA A 258 PLP A 413 HOH A 443
SITE 1 AC3 13 HOH B 30 HOH B 83 ARG B 559 LYS B 659
SITE 2 AC3 13 TYR B 664 GLU B 693 GLY B 696 ASN B 698
SITE 3 AC3 13 GLY B 719 ILE B 720 THR B 721 THR B 757
SITE 4 AC3 13 2ML B 914
SITE 1 AC4 8 TYR A 31 HOH B 30 GLY B 538 TYR B 595
SITE 2 AC4 8 LYS B 659 THR B 757 ALA B 758 PLP B 913
SITE 1 AC5 14 HOH C 5 HOH C 58 ARG C1059 LYS C1159
SITE 2 AC5 14 TYR C1164 GLU C1193 GLY C1196 ASN C1198
SITE 3 AC5 14 GLY C1219 ILE C1220 THR C1221 GLY C1256
SITE 4 AC5 14 THR C1257 2ML C1414
SITE 1 AC6 8 HOH C 132 GLY C1038 TYR C1095 LYS C1159
SITE 2 AC6 8 GLY C1196 THR C1257 ALA C1258 PLP C1413
CRYST1 156.090 100.770 141.560 90.00 90.00 90.00 C 2 2 21 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 0.006407 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009924 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007064 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
