HEADER TRANSFERASE 17-MAY-05 2COJ
TITLE CRYSTAL STRUCTURE OF REDUCED HUMAN CYTOSOLIC BRANCHED-CHAIN
TITLE 2 AMINOTRANSFERASE COMPLEXED WITH GABAPENTIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BRANCHED CHAIN AMINOTRANSFERASE 1, CYTOSOLIC;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.6.1.42;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PLP-DEPENDENT ENZYME, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.GOTO
REVDAT 5 10-NOV-21 2COJ 1 REMARK SEQADV LINK
REVDAT 4 13-JUL-11 2COJ 1 VERSN
REVDAT 3 24-FEB-09 2COJ 1 VERSN
REVDAT 2 06-DEC-05 2COJ 1 JRNL
REVDAT 1 30-AUG-05 2COJ 0
JRNL AUTH M.GOTO,I.MIYAHARA,K.HIROTSU,M.CONWAY,N.YENNAWAR,M.M.ISLAM,
JRNL AUTH 2 S.M.HUTSON
JRNL TITL STRUCTURAL DETERMINANTS FOR BRANCHED-CHAIN AMINOTRANSFERASE
JRNL TITL 2 ISOZYME-SPECIFIC INHIBITION BY THE ANTICONVULSANT DRUG
JRNL TITL 3 GABAPENTIN
JRNL REF J.BIOL.CHEM. V. 280 37246 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 16141215
JRNL DOI 10.1074/JBC.M506486200
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.44
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2689713.470
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.2
REMARK 3 NUMBER OF REFLECTIONS : 28651
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 SET) : 0.213
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2873
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4594
REMARK 3 BIN R VALUE (WORKING SET) : 0.2670
REMARK 3 BIN FREE R VALUE : 0.3400
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 468
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.016
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5653
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 55
REMARK 3 SOLVENT ATOMS : 148
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -16.26000
REMARK 3 B22 (A**2) : 10.01000
REMARK 3 B33 (A**2) : 6.26000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM SIGMAA (A) : 0.27
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.40
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.40
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.920
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.350 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.110 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 20.130; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 18.620; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 30.65
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : CNS_LOCAL:PARAM.PLP
REMARK 3 PARAMETER FILE 4 : CNS_LOCAL:PARAM.ETC
REMARK 3 PARAMETER FILE 5 : GBP.PAR
REMARK 3 PARAMETER FILE 6 : ION.PARAM
REMARK 3 PARAMETER FILE 7 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 3 : CNS_LOCAL:TOP.PLP
REMARK 3 TOPOLOGY FILE 4 : CNS_LOCAL:TOP.ETC
REMARK 3 TOPOLOGY FILE 5 : GBP.TOP
REMARK 3 TOPOLOGY FILE 6 : ION.TOP
REMARK 3 TOPOLOGY FILE 7 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2COJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024451.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUN-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28933
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.1
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) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
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 (%): 46.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, MAGNESIUM CHLORIDE, PH 7.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
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
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 33.43500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.91000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.31500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.91000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.43500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.31500
REMARK 290 SMTRY3 4 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: 7020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 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 LYS A 2
REMARK 465 ASP A 3
REMARK 465 CYS A 4
REMARK 465 SER A 5
REMARK 465 ASN A 6
REMARK 465 GLY A 7
REMARK 465 CYS A 8
REMARK 465 SER A 9
REMARK 465 ALA A 10
REMARK 465 GLU A 11
REMARK 465 CYS A 12
REMARK 465 THR A 13
REMARK 465 GLY A 14
REMARK 465 GLU A 15
REMARK 465 GLY A 16
REMARK 465 GLY A 17
REMARK 465 SER A 18
REMARK 465 LYS A 19
REMARK 465 GLU A 20
REMARK 465 VAL A 21
REMARK 465 ASN A 46
REMARK 465 SER A 195
REMARK 465 SER A 196
REMARK 465 GLY A 197
REMARK 465 THR A 198
REMARK 465 SER A 386
REMARK 465 MET B 1
REMARK 465 LYS B 2
REMARK 465 ASP B 3
REMARK 465 CYS B 4
REMARK 465 SER B 5
REMARK 465 ASN B 6
REMARK 465 GLY B 7
REMARK 465 CYS B 8
REMARK 465 SER B 9
REMARK 465 ALA B 10
REMARK 465 GLU B 11
REMARK 465 CYS B 12
REMARK 465 THR B 13
REMARK 465 GLY B 14
REMARK 465 GLU B 15
REMARK 465 GLY B 16
REMARK 465 GLY B 17
REMARK 465 SER B 18
REMARK 465 LYS B 19
REMARK 465 GLU B 20
REMARK 465 VAL B 21
REMARK 465 VAL B 22
REMARK 465 GLY B 23
REMARK 465 SER B 195
REMARK 465 SER B 196
REMARK 465 GLY B 197
REMARK 465 THR B 198
REMARK 465 SER B 386
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 LYS A 28 CG CD CE NZ
REMARK 470 GLU A 40 CG CD OE1 OE2
REMARK 470 ASN A 45 CG OD1 ND2
REMARK 470 ARG A 122 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 200 CG OD1 ND2
REMARK 470 LYS A 209 CG CD CE NZ
REMARK 470 LYS A 360 CG CD CE NZ
REMARK 470 LYS B 28 CG CD CE NZ
REMARK 470 GLN B 77 CG CD OE1 NE2
REMARK 470 GLU B 378 CG CD OE1 OE2
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 PRO A 44 -4.01 -56.66
REMARK 500 SER A 85 129.76 -37.61
REMARK 500 ASP A 148 33.96 -99.15
REMARK 500 VAL A 152 103.65 -59.60
REMARK 500 PRO A 153 135.26 -34.56
REMARK 500 PRO A 171 44.05 -74.80
REMARK 500 ASN A 200 85.30 -153.65
REMARK 500 PRO A 201 153.60 -48.42
REMARK 500 THR A 260 47.22 -108.42
REMARK 500 PRO A 287 92.47 -66.70
REMARK 500 VAL A 336 -60.91 71.02
REMARK 500 PRO A 353 19.48 -66.87
REMARK 500 ASN A 357 37.78 -142.72
REMARK 500 GLN B 149 -39.88 -39.95
REMARK 500 THR B 260 49.59 -105.52
REMARK 500 VAL B 336 -64.71 85.21
REMARK 500 TYR B 345 -117.80 -114.80
REMARK 500 LYS B 346 54.45 -68.87
REMARK 500 PRO B 353 22.48 -60.65
REMARK 500 ARG B 379 140.84 -173.68
REMARK 500 ASP B 380 10.92 -54.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 430 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 133 OD1
REMARK 620 2 HOH B 433 O 62.9
REMARK 620 3 HOH B 442 O 66.2 64.6
REMARK 620 4 HOH B 500 O 146.0 87.5 86.8
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 430
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GBN A 420
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GBN B 420
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2COG RELATED DB: PDB
REMARK 900 OXIDIZED CYTOSOLIC BRANCHED-CHAIN AMINOTRANSFERASE COMPLEXED WITH 4-
REMARK 900 METHYLVALERATE
REMARK 900 RELATED ID: 2COI RELATED DB: PDB
REMARK 900 OXIDIZED CYTOSOLIC BRANCHED-CHAIN AMINOTRANSFERASE COMPLEXED WITH
REMARK 900 GABAPENTIN
DBREF 2COJ A 1 386 UNP P54687 BCAT1_HUMAN 1 386
DBREF 2COJ B 1 386 UNP P54687 BCAT1_HUMAN 1 386
SEQADV 2COJ ARG A 379 UNP P54687 SER 379 ENGINEERED MUTATION
SEQADV 2COJ ARG B 379 UNP P54687 SER 379 ENGINEERED MUTATION
SEQRES 1 A 386 MET LYS ASP CYS SER ASN GLY CYS SER ALA GLU CYS THR
SEQRES 2 A 386 GLY GLU GLY GLY SER LYS GLU VAL VAL GLY THR PHE LYS
SEQRES 3 A 386 ALA LYS ASP LEU ILE VAL THR PRO ALA THR ILE LEU LYS
SEQRES 4 A 386 GLU LYS PRO ASP PRO ASN ASN LEU VAL PHE GLY THR VAL
SEQRES 5 A 386 PHE THR ASP HIS MET LEU THR VAL GLU TRP SER SER GLU
SEQRES 6 A 386 PHE GLY TRP GLU LYS PRO HIS ILE LYS PRO LEU GLN ASN
SEQRES 7 A 386 LEU SER LEU HIS PRO GLY SER SER ALA LEU HIS TYR ALA
SEQRES 8 A 386 VAL GLU LEU PHE GLU GLY LEU LYS ALA PHE ARG GLY VAL
SEQRES 9 A 386 ASP ASN LYS ILE ARG LEU PHE GLN PRO ASN LEU ASN MET
SEQRES 10 A 386 ASP ARG MET TYR ARG SER ALA VAL ARG ALA THR LEU PRO
SEQRES 11 A 386 VAL PHE ASP LYS GLU GLU LEU LEU GLU CYS ILE GLN GLN
SEQRES 12 A 386 LEU VAL LYS LEU ASP GLN GLU TRP VAL PRO TYR SER THR
SEQRES 13 A 386 SER ALA SER LEU TYR ILE ARG PRO THR PHE ILE GLY THR
SEQRES 14 A 386 GLU PRO SER LEU GLY VAL LYS LYS PRO THR LYS ALA LEU
SEQRES 15 A 386 LEU PHE VAL LEU LEU SER PRO VAL GLY PRO TYR PHE SER
SEQRES 16 A 386 SER GLY THR PHE ASN PRO VAL SER LEU TRP ALA ASN PRO
SEQRES 17 A 386 LYS TYR VAL ARG ALA TRP LYS GLY GLY THR GLY ASP CYS
SEQRES 18 A 386 LYS MET GLY GLY ASN TYR GLY SER SER LEU PHE ALA GLN
SEQRES 19 A 386 CYS GLU ALA VAL ASP ASN GLY CYS GLN GLN VAL LEU TRP
SEQRES 20 A 386 LEU TYR GLY GLU ASP HIS GLN ILE THR GLU VAL GLY THR
SEQRES 21 A 386 MET ASN LEU PHE LEU TYR TRP ILE ASN GLU ASP GLY GLU
SEQRES 22 A 386 GLU GLU LEU ALA THR PRO PRO LEU ASP GLY ILE ILE LEU
SEQRES 23 A 386 PRO GLY VAL THR ARG ARG CYS ILE LEU ASP LEU ALA HIS
SEQRES 24 A 386 GLN TRP GLY GLU PHE LYS VAL SER GLU ARG TYR LEU THR
SEQRES 25 A 386 MET ASP ASP LEU THR THR ALA LEU GLU GLY ASN ARG VAL
SEQRES 26 A 386 ARG GLU MET PHE GLY SER GLY THR ALA CYS VAL VAL CYS
SEQRES 27 A 386 PRO VAL SER ASP ILE LEU TYR LYS GLY GLU THR ILE HIS
SEQRES 28 A 386 ILE PRO THR MET GLU ASN GLY PRO LYS LEU ALA SER ARG
SEQRES 29 A 386 ILE LEU SER LYS LEU THR ASP ILE GLN TYR GLY ARG GLU
SEQRES 30 A 386 GLU ARG ASP TRP THR ILE VAL LEU SER
SEQRES 1 B 386 MET LYS ASP CYS SER ASN GLY CYS SER ALA GLU CYS THR
SEQRES 2 B 386 GLY GLU GLY GLY SER LYS GLU VAL VAL GLY THR PHE LYS
SEQRES 3 B 386 ALA LYS ASP LEU ILE VAL THR PRO ALA THR ILE LEU LYS
SEQRES 4 B 386 GLU LYS PRO ASP PRO ASN ASN LEU VAL PHE GLY THR VAL
SEQRES 5 B 386 PHE THR ASP HIS MET LEU THR VAL GLU TRP SER SER GLU
SEQRES 6 B 386 PHE GLY TRP GLU LYS PRO HIS ILE LYS PRO LEU GLN ASN
SEQRES 7 B 386 LEU SER LEU HIS PRO GLY SER SER ALA LEU HIS TYR ALA
SEQRES 8 B 386 VAL GLU LEU PHE GLU GLY LEU LYS ALA PHE ARG GLY VAL
SEQRES 9 B 386 ASP ASN LYS ILE ARG LEU PHE GLN PRO ASN LEU ASN MET
SEQRES 10 B 386 ASP ARG MET TYR ARG SER ALA VAL ARG ALA THR LEU PRO
SEQRES 11 B 386 VAL PHE ASP LYS GLU GLU LEU LEU GLU CYS ILE GLN GLN
SEQRES 12 B 386 LEU VAL LYS LEU ASP GLN GLU TRP VAL PRO TYR SER THR
SEQRES 13 B 386 SER ALA SER LEU TYR ILE ARG PRO THR PHE ILE GLY THR
SEQRES 14 B 386 GLU PRO SER LEU GLY VAL LYS LYS PRO THR LYS ALA LEU
SEQRES 15 B 386 LEU PHE VAL LEU LEU SER PRO VAL GLY PRO TYR PHE SER
SEQRES 16 B 386 SER GLY THR PHE ASN PRO VAL SER LEU TRP ALA ASN PRO
SEQRES 17 B 386 LYS TYR VAL ARG ALA TRP LYS GLY GLY THR GLY ASP CYS
SEQRES 18 B 386 LYS MET GLY GLY ASN TYR GLY SER SER LEU PHE ALA GLN
SEQRES 19 B 386 CYS GLU ALA VAL ASP ASN GLY CYS GLN GLN VAL LEU TRP
SEQRES 20 B 386 LEU TYR GLY GLU ASP HIS GLN ILE THR GLU VAL GLY THR
SEQRES 21 B 386 MET ASN LEU PHE LEU TYR TRP ILE ASN GLU ASP GLY GLU
SEQRES 22 B 386 GLU GLU LEU ALA THR PRO PRO LEU ASP GLY ILE ILE LEU
SEQRES 23 B 386 PRO GLY VAL THR ARG ARG CYS ILE LEU ASP LEU ALA HIS
SEQRES 24 B 386 GLN TRP GLY GLU PHE LYS VAL SER GLU ARG TYR LEU THR
SEQRES 25 B 386 MET ASP ASP LEU THR THR ALA LEU GLU GLY ASN ARG VAL
SEQRES 26 B 386 ARG GLU MET PHE GLY SER GLY THR ALA CYS VAL VAL CYS
SEQRES 27 B 386 PRO VAL SER ASP ILE LEU TYR LYS GLY GLU THR ILE HIS
SEQRES 28 B 386 ILE PRO THR MET GLU ASN GLY PRO LYS LEU ALA SER ARG
SEQRES 29 B 386 ILE LEU SER LYS LEU THR ASP ILE GLN TYR GLY ARG GLU
SEQRES 30 B 386 GLU ARG ASP TRP THR ILE VAL LEU SER
HET PLP A 410 15
HET GBN A 420 12
HET MG B 430 1
HET PLP B 410 15
HET GBN B 420 12
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETNAM GBN [1-(AMINOMETHYL)CYCLOHEXYL]ACETIC ACID
HETNAM MG MAGNESIUM ION
HETSYN PLP VITAMIN B6 PHOSPHATE
HETSYN GBN GABAPENTIN
FORMUL 3 PLP 2(C8 H10 N O6 P)
FORMUL 4 GBN 2(C9 H17 N O2)
FORMUL 5 MG MG 2+
FORMUL 8 HOH *148(H2 O)
HELIX 1 1 LYS A 26 LEU A 30 5 5
HELIX 2 2 SER A 85 TYR A 90 1 6
HELIX 3 3 GLN A 112 THR A 128 1 17
HELIX 4 4 ASP A 133 ASP A 148 1 16
HELIX 5 5 GLN A 149 VAL A 152 5 4
HELIX 6 6 GLY A 224 SER A 229 1 6
HELIX 7 7 SER A 230 ASN A 240 1 11
HELIX 8 8 GLY A 288 GLY A 302 1 15
HELIX 9 9 THR A 312 GLU A 321 1 10
HELIX 10 10 THR A 354 GLY A 358 5 5
HELIX 11 11 PRO A 359 TYR A 374 1 16
HELIX 12 12 LYS B 26 LEU B 30 5 5
HELIX 13 13 SER B 85 TYR B 90 1 6
HELIX 14 14 GLN B 112 THR B 128 1 17
HELIX 15 15 ASP B 133 ASP B 148 1 16
HELIX 16 16 GLN B 149 VAL B 152 5 4
HELIX 17 17 MET B 223 TYR B 227 5 5
HELIX 18 18 SER B 230 ASP B 239 1 10
HELIX 19 19 GLY B 288 GLY B 302 1 15
HELIX 20 20 THR B 312 GLU B 321 1 10
HELIX 21 21 THR B 354 GLY B 358 5 5
HELIX 22 22 PRO B 359 TYR B 374 1 16
SHEET 1 A 6 ILE A 31 VAL A 32 0
SHEET 2 A 6 HIS A 72 PRO A 75 1 O ILE A 73 N ILE A 31
SHEET 3 A 6 HIS A 56 SER A 63 -1 N MET A 57 O LYS A 74
SHEET 4 A 6 LYS A 180 VAL A 190 -1 O ALA A 181 N TRP A 62
SHEET 5 A 6 SER A 159 GLY A 168 -1 N SER A 159 O VAL A 190
SHEET 6 A 6 GLU A 93 PHE A 95 -1 N LEU A 94 O PHE A 166
SHEET 1 B 7 GLY A 67 TRP A 68 0
SHEET 2 B 7 HIS A 56 SER A 63 -1 N SER A 63 O GLY A 67
SHEET 3 B 7 LYS A 180 VAL A 190 -1 O ALA A 181 N TRP A 62
SHEET 4 B 7 SER A 159 GLY A 168 -1 N SER A 159 O VAL A 190
SHEET 5 B 7 LEU A 98 ARG A 102 -1 N LEU A 98 O ILE A 162
SHEET 6 B 7 ILE A 108 PHE A 111 -1 O ARG A 109 N PHE A 101
SHEET 7 B 7 THR A 382 VAL A 384 -1 O ILE A 383 N LEU A 110
SHEET 1 C 2 LEU A 79 LEU A 81 0
SHEET 2 C 2 LEU B 79 LEU B 81 -1 O LEU B 81 N LEU A 79
SHEET 1 D 8 LYS A 305 GLU A 308 0
SHEET 2 D 8 GLU A 274 THR A 278 1 N LEU A 276 O LYS A 305
SHEET 3 D 8 MET A 261 ILE A 268 -1 N TRP A 267 O GLU A 275
SHEET 4 D 8 GLN A 254 VAL A 258 -1 N VAL A 258 O MET A 261
SHEET 5 D 8 GLN A 244 TYR A 249 -1 N TYR A 249 O GLN A 254
SHEET 6 D 8 VAL A 202 ALA A 206 1 N TRP A 205 O LEU A 246
SHEET 7 D 8 VAL A 336 TYR A 345 1 O LEU A 344 N LEU A 204
SHEET 8 D 8 GLU A 348 HIS A 351 -1 O GLU A 348 N TYR A 345
SHEET 1 E 6 LYS A 305 GLU A 308 0
SHEET 2 E 6 GLU A 274 THR A 278 1 N LEU A 276 O LYS A 305
SHEET 3 E 6 MET A 261 ILE A 268 -1 N TRP A 267 O GLU A 275
SHEET 4 E 6 VAL A 325 GLY A 332 -1 O PHE A 329 N PHE A 264
SHEET 5 E 6 VAL A 336 TYR A 345 -1 O CYS A 338 N GLY A 330
SHEET 6 E 6 GLU A 348 HIS A 351 -1 O GLU A 348 N TYR A 345
SHEET 1 F 6 ILE B 31 VAL B 32 0
SHEET 2 F 6 HIS B 72 PRO B 75 1 O ILE B 73 N ILE B 31
SHEET 3 F 6 HIS B 56 SER B 63 -1 N THR B 59 O HIS B 72
SHEET 4 F 6 LYS B 180 VAL B 190 -1 O ALA B 181 N TRP B 62
SHEET 5 F 6 SER B 159 GLY B 168 -1 N THR B 165 O PHE B 184
SHEET 6 F 6 GLU B 93 PHE B 95 -1 N LEU B 94 O PHE B 166
SHEET 1 G 7 GLY B 67 TRP B 68 0
SHEET 2 G 7 HIS B 56 SER B 63 -1 N SER B 63 O GLY B 67
SHEET 3 G 7 LYS B 180 VAL B 190 -1 O ALA B 181 N TRP B 62
SHEET 4 G 7 SER B 159 GLY B 168 -1 N THR B 165 O PHE B 184
SHEET 5 G 7 LEU B 98 ARG B 102 -1 N LEU B 98 O ILE B 162
SHEET 6 G 7 ILE B 108 PHE B 111 -1 O ARG B 109 N PHE B 101
SHEET 7 G 7 THR B 382 VAL B 384 -1 O ILE B 383 N LEU B 110
SHEET 1 H 8 LYS B 305 GLU B 308 0
SHEET 2 H 8 GLU B 274 THR B 278 1 N LEU B 276 O SER B 307
SHEET 3 H 8 MET B 261 ILE B 268 -1 N TRP B 267 O GLU B 275
SHEET 4 H 8 GLN B 254 VAL B 258 -1 N VAL B 258 O MET B 261
SHEET 5 H 8 GLN B 244 TYR B 249 -1 N TYR B 249 O GLN B 254
SHEET 6 H 8 VAL B 202 TRP B 205 1 N TRP B 205 O GLN B 244
SHEET 7 H 8 VAL B 336 LEU B 344 1 O LEU B 344 N LEU B 204
SHEET 8 H 8 THR B 349 HIS B 351 -1 O ILE B 350 N ILE B 343
SHEET 1 I 6 LYS B 305 GLU B 308 0
SHEET 2 I 6 GLU B 274 THR B 278 1 N LEU B 276 O SER B 307
SHEET 3 I 6 MET B 261 ILE B 268 -1 N TRP B 267 O GLU B 275
SHEET 4 I 6 VAL B 325 GLY B 332 -1 O GLU B 327 N TYR B 266
SHEET 5 I 6 VAL B 336 LEU B 344 -1 O VAL B 336 N GLY B 332
SHEET 6 I 6 THR B 349 HIS B 351 -1 O ILE B 350 N ILE B 343
LINK NZ LYS A 222 C4A PLP A 410 1555 1555 1.38
LINK NZ LYS B 222 C4A PLP B 410 1555 1555 1.38
LINK OD1 ASP B 133 MG MG B 430 1555 1555 2.35
LINK MG MG B 430 O HOH B 433 1555 1555 2.46
LINK MG MG B 430 O HOH B 442 1555 1555 2.38
LINK MG MG B 430 O HOH B 500 1555 1555 2.38
CISPEP 1 GLY A 358 PRO A 359 0 -0.03
CISPEP 2 GLY B 358 PRO B 359 0 -0.15
SITE 1 AC1 5 ASP B 133 GLU B 274 HOH B 433 HOH B 442
SITE 2 AC1 5 HOH B 500
SITE 1 AC2 14 ARG A 119 LYS A 222 TYR A 227 GLU A 257
SITE 2 AC2 14 THR A 260 LEU A 286 GLY A 288 VAL A 289
SITE 3 AC2 14 THR A 290 GLY A 332 THR A 333 HOH A 421
SITE 4 AC2 14 HOH A 426 HOH A 466
SITE 1 AC3 14 ARG B 119 ARG B 212 LYS B 222 TYR B 227
SITE 2 AC3 14 GLU B 257 THR B 260 LEU B 286 GLY B 288
SITE 3 AC3 14 VAL B 289 THR B 290 THR B 333 HOH B 432
SITE 4 AC3 14 HOH B 434 HOH B 477
SITE 1 AC4 9 TYR A 161 THR A 260 MET A 261 GLY A 332
SITE 2 AC4 9 THR A 333 ALA A 334 HOH A 469 TYR B 90
SITE 3 AC4 9 VAL B 175
SITE 1 AC5 9 TYR A 90 TYR B 161 ARG B 163 THR B 260
SITE 2 AC5 9 MET B 261 GLY B 332 THR B 333 ALA B 334
SITE 3 AC5 9 HOH B 509
CRYST1 66.870 106.630 109.820 90.00 90.00 90.00 P 21 21 21 8
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 0.014954 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009378 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009106 0.00000
(ATOM LINES ARE NOT SHOWN.)
END