HEADER OXIDOREDUCTASE 12-AUG-03 1OLS
TITLE ROLES OF HIS291-ALPHA AND HIS146-BETA' IN THE REDUCTIVE ACYLATION
TITLE 2 REACTION CATALYZED BY HUMAN BRANCHED-CHAIN ALPHA-KETOACID
TITLE 3 DEHYDROGENASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-OXOISOVALERATE DEHYDROGENASE ALPHA SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BRANCHED-CHAIN ALPHA-KETOACID DEHYDROGENASE E1 COMPONENT
COMPND 5 ALPHA CHAIN, BCKDH E1-ALPHA;
COMPND 6 EC: 1.2.4.4;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: 2-OXOISOVALERATE DEHYDROGENASE BETA SUBUNIT;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE E1 COMPONENT
COMPND 12 BETA CHAIN, BCKDH E1-BETA;
COMPND 13 EC: 1.2.4.4;
COMPND 14 ENGINEERED: 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;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: CG-712 (ES TS);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PE1BETAHIS;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: CG-712 (ES TS);
SOURCE 16 EXPRESSION_SYSTEM_VECTOR: PE1BETAHIS
KEYWDS OXIDOREDUCTASE, KETOACID DEHYDROGENASE, BRANCHED-CHAIN, MULTI-ENZYME
KEYWDS 2 COMPLEX, ACYLATION, OXIDATIVE DECARBOXYLATION, MAPLE SYRUP URINE
KEYWDS 3 DISEASE, THIAMINE PHOSPHATE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.M.WYNN,M.MACHIUS,J.L.CHUANG,J.LI,D.R.TOMCHICK,D.T.CHUANG
REVDAT 9 13-DEC-23 1OLS 1 REMARK
REVDAT 8 04-AUG-21 1OLS 1 COMPND REMARK HET HETNAM
REVDAT 8 2 1 FORMUL LINK SITE ATOM
REVDAT 7 25-SEP-19 1OLS 1 REMARK
REVDAT 6 15-MAY-19 1OLS 1 REMARK
REVDAT 5 01-SEP-09 1OLS 1 REMARK
REVDAT 4 24-FEB-09 1OLS 1 VERSN
REVDAT 3 30-OCT-03 1OLS 1 JRNL
REVDAT 2 28-AUG-03 1OLS 1 SEQRES SEQADV ATOM TER
REVDAT 2 2 1 HETATM CONECT
REVDAT 1 15-AUG-03 1OLS 0
JRNL AUTH R.M.WYNN,M.MACHIUS,J.L.CHUANG,J.LI,D.R.TOMCHICK,D.T.CHUANG
JRNL TITL ROLES OF HIS291-ALPHA AND HIS146-BETA' IN THE REDUCTIVE
JRNL TITL 2 ACYLATION REACTION CATALYZED BY HUMAN BRANCHED-CHAIN
JRNL TITL 3 ALPHA-KETOACID DEHYDROGENASE: REFINED PHOSPHORYLATION LOOP
JRNL TITL 4 STRUCTURE IN THE ACTIVE SITE.
JRNL REF J.BIOL.CHEM. V. 278 43402 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12902323
JRNL DOI 10.1074/JBC.M306204200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.M.WYNN,R.HO,J.L.CHUANG,D.T.CHUANG
REMARK 1 TITL ROLES OF ACTIVE SITE AND NOVEL K+ ION-BINDING SITE RESIDUES
REMARK 1 TITL 2 IN HUMAN MITOCHONDRIAL BRANCHED-CHAIN ALPHA-KETOACID
REMARK 1 TITL 3 DECARBOXYLASE/DEHYDROGENASE
REMARK 1 REF J.BIOL.CHEM. V. 274 4168 2001
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 11069910
REMARK 1 DOI 10.1074/JBC.M008038200
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.AEVARSSON,J.L.CHUANG,R.M.WYNN,S.TURLEY,D.T.CHUANG,
REMARK 1 AUTH 2 W.G.J.HOL
REMARK 1 TITL CRYSTAL STRUCTURE OF HUMAN BRANCHED-CHAIN ALPHA-KETOACID
REMARK 1 TITL 2 DEHYDROGENASE AND THE MOLECULAR BASIS OF MULTIENZYME COMPLEX
REMARK 1 TITL 3 DEFICIENCY IN MAPLE SYRUP URINE DISEASE
REMARK 1 REF STRUCTURE V. 8 277 2000
REMARK 1 REFN ISSN 0969-2126
REMARK 1 PMID 10745006
REMARK 1 DOI 10.1016/S0969-2126(00)00105-2
REMARK 2
REMARK 2 RESOLUTION. 1.85 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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.75
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 427954.550
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.6
REMARK 3 NUMBER OF REFLECTIONS : 67320
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) : 0.172
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.700
REMARK 3 FREE R VALUE TEST SET COUNT : 1178
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.97
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 9994
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
REMARK 3 BIN FREE R VALUE : 0.2880
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 1.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 170
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5729
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 35
REMARK 3 SOLVENT ATOMS : 451
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.06000
REMARK 3 B22 (A**2) : 4.06000
REMARK 3 B33 (A**2) : -8.11000
REMARK 3 B12 (A**2) : 2.79000
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) : 0.18
REMARK 3 ESD FROM SIGMAA (A) : 0.19
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) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.015
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.150
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) : 1.240 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.860 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.990 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.910 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 48.09
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 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : TDP.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 4 : TDP.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE FOLLOWING RESIDUES DID NOT HAVE
REMARK 3 CORRESPONDING ELECTRON DENSITY AND WERE OMITTED FROM THE MODEL:
REMARK 3 ALPHA-SUBUNIT: 1-5, 293-294, 299, 302-307 BETA-SUBUNIT: 1,9-13.
REMARK 3 THE FOLLOWING RESIDUES DID HAVE POORLY DEFINED ELECTRON DENSITY
REMARK 3 AND WERE MODELLED STEREOCHEMICALLY: ALPHA- SUBUNIT: LYS19, GLN24,
REMARK 3 ARG39, GLN40, GLU55, ASP296, TYR300, ARG391, TYR308-GLN312,
REMARK 3 GLU331, GLU332, ARG338, LYS339, GLU347, LYS377, LYS400 BETA-
REMARK 3 SUBUNIT: ALA2, PHE6, GLN7, LYS20, ARG235, ILE301
REMARK 4
REMARK 4 1OLS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-AUG-03.
REMARK 100 THE DEPOSITION ID IS D_1290013304.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-FEB-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.50
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 : CARBON
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU-MSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 71059
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 39.080
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.55600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS 1.1
REMARK 200 STARTING MODEL: PDB ENTRY 1DTW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN AT 20C VIA THE
REMARK 280 VAPOR DIFFUSION METHOD BY MIXING EQUAL AMOUNTS OF PROTEIN (20-25
REMARK 280 MG/ML IN 50 MM HEPES/NAOH, PH 7.5, 250 MM KCL, 0.5 MM PMSF, 1 MM
REMARK 280 BENZAMIDINE AND 5% (V/V) GLYCEROL) WITH WELL SOLUTION (1.4-1.6 M
REMARK 280 AMMONIUM SULFATE, 0.1 M NA-CITRATE PH 5.8, 20 MM B-
REMARK 280 MERCAPTOETHANOL). SERIALLY DILUTED CRUSHED CRYSTALS WERE USED
REMARK 280 FOR MICRO-SEEDING ONE DAY AFTER THE DROPS WERE SET UP. CRYSTALS
REMARK 280 APPEARED ONE DAY AFTER SEEDING AND GREW TO A MAXIMUM SIZE OF 120
REMARK 280 X 800 UM WITHIN 10 DAYS. CRYSTALS WERE STABILIZED FOR 12 HOURS
REMARK 280 BY TRANSFER TO FRESH WELL SOLUTION. THEY WERE THEN CRYO-
REMARK 280 PROTECTED BY STEP-WISE TRANSFER INTO CRYO-BUFFER CONTAINING 1.6
REMARK 280 M AMMONIUM SULFATE, 50 MM HEPES, PH 7.5, 100 MM NA-CITRATE, PH
REMARK 280 5.8,100 MM KCL, 50 MM DTT AND UP TO 20% (V/V) GLYCEROL. IT WAS
REMARK 280 FOUND THAT MN2+ IONS COULD REPLACE THE MG2+ REQUIRED FOR THE
REMARK 280 BINDING OF THDP TO THE ENZYME., PH 5.50, TEMPERATURE 293K
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 23.05033
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 46.10067
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 46.10067
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 23.05033
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 27570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -166.0 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 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 46.10067
REMARK 400
REMARK 400 COMPOUND
REMARK 400 THE BRANCHED-CHAIN ALPHA-KETO DEHYDROGENASE COMPLEX
REMARK 400 CATALYZES CONVERSION OF ALPHA-KETO ACIDS TO ACYL-COA
REMARK 400 AND CO(2). CONTAINS MULTIPLE COPIES OF 3 ENZYMATIC COMPONENTS:
REMARK 400 BRANCHED-CHAIN ALPHA-KETO ACID DECARBOXYLASE (E1), LIPOAMIDE
REMARK 400 ACYLTRANSFERASE (E2) AND LIPOAMIDE DEHYDROGENASE (E3).
REMARK 400 REQUIRES THIAMINE PYROPHOSPHATE AS A COFACTOR AND EXISTS
REMARK 400 AS A HETERODIMER OF AN ALPHA AND A BETA CHAIN.
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 SER A 1
REMARK 465 SER A 2
REMARK 465 LEU A 3
REMARK 465 ASP A 4
REMARK 465 ASP A 5
REMARK 465 THR A 293
REMARK 465 SER A 294
REMARK 465 ALA A 299
REMARK 465 SER A 302
REMARK 465 VAL A 303
REMARK 465 ASP A 304
REMARK 465 GLU A 305
REMARK 465 VAL A 306
REMARK 465 ASN A 307
REMARK 465 VAL B 1
REMARK 465 ASP B 9
REMARK 465 PRO B 10
REMARK 465 GLU B 11
REMARK 465 PRO B 12
REMARK 465 ARG B 13
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 LEU A 363 CA - CB - CG ANGL. DEV. = 16.1 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 SER A 29 73.34 -119.43
REMARK 500 GLN A 112 -109.94 -139.94
REMARK 500 GLN A 112 -108.92 -139.94
REMARK 500 ALA A 165 -3.88 70.37
REMARK 500 GLU A 212 72.44 48.10
REMARK 500 ILE A 226 -108.83 56.46
REMARK 500 ASP A 313 72.61 -157.62
REMARK 500 GLN B 7 -70.22 -132.49
REMARK 500 CYS B 75 97.31 -160.45
REMARK 500 GLU B 113 -70.91 -109.01
REMARK 500 HIS B 141 19.70 -151.35
REMARK 500 ALA B 143 -150.08 60.28
REMARK 500 LYS B 182 36.55 -93.10
REMARK 500 ALA B 197 125.00 32.67
REMARK 500 ARG B 255 -59.67 66.88
REMARK 500 HIS B 319 -79.79 -71.31
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 K A 501 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 112 OE1
REMARK 620 2 SER A 161 O 69.9
REMARK 620 3 SER A 161 OG 134.7 64.9
REMARK 620 4 PRO A 163 O 83.1 93.4 96.4
REMARK 620 5 THR A 166 OG1 138.6 128.2 73.7 61.1
REMARK 620 6 GLN A 167 OE1 80.0 145.5 143.5 99.4 85.7
REMARK 620 7 HOH A2078 O 89.5 78.8 84.8 170.7 127.8 84.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 503 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 193 OE2
REMARK 620 2 ASN A 222 OD1 86.0
REMARK 620 3 TYR A 224 O 121.0 81.3
REMARK 620 4 TPP A 601 O1A 89.8 171.1 107.6
REMARK 620 5 TPP A 601 O3B 156.2 91.3 81.8 89.3
REMARK 620 6 HOH A2250 O 72.7 81.5 157.1 89.7 83.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 502 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 128 O
REMARK 620 2 LEU B 130 O 87.9
REMARK 620 3 CYS B 178 O 150.0 120.6
REMARK 620 4 ASP B 181 O 66.5 154.4 84.9
REMARK 620 5 ASN B 183 O 72.2 83.2 116.8 87.3
REMARK 620 6 HOH B2117 O 97.9 76.9 81.6 107.0 158.1
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TPP A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 701
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DTW RELATED DB: PDB
REMARK 900 HUMAN BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE
DBREF 1OLS A 1 400 UNP P12694 ODBA_HUMAN 46 445
DBREF 1OLS B 1 342 UNP P21953 ODBB_HUMAN 51 392
SEQRES 1 A 400 SER SER LEU ASP ASP LYS PRO GLN PHE PRO GLY ALA SER
SEQRES 2 A 400 ALA GLU PHE ILE ASP LYS LEU GLU PHE ILE GLN PRO ASN
SEQRES 3 A 400 VAL ILE SER GLY ILE PRO ILE TYR ARG VAL MET ASP ARG
SEQRES 4 A 400 GLN GLY GLN ILE ILE ASN PRO SER GLU ASP PRO HIS LEU
SEQRES 5 A 400 PRO LYS GLU LYS VAL LEU LYS LEU TYR LYS SER MET THR
SEQRES 6 A 400 LEU LEU ASN THR MET ASP ARG ILE LEU TYR GLU SER GLN
SEQRES 7 A 400 ARG GLN GLY ARG ILE SER PHE TYR MET THR ASN TYR GLY
SEQRES 8 A 400 GLU GLU GLY THR HIS VAL GLY SER ALA ALA ALA LEU ASP
SEQRES 9 A 400 ASN THR ASP LEU VAL PHE GLY GLN TYR ARG GLU ALA GLY
SEQRES 10 A 400 VAL LEU MET TYR ARG ASP TYR PRO LEU GLU LEU PHE MET
SEQRES 11 A 400 ALA GLN CYS TYR GLY ASN ILE SER ASP LEU GLY LYS GLY
SEQRES 12 A 400 ARG GLN MET PRO VAL HIS TYR GLY CYS LYS GLU ARG HIS
SEQRES 13 A 400 PHE VAL THR ILE SER SER PRO LEU ALA THR GLN ILE PRO
SEQRES 14 A 400 GLN ALA VAL GLY ALA ALA TYR ALA ALA LYS ARG ALA ASN
SEQRES 15 A 400 ALA ASN ARG VAL VAL ILE CYS TYR PHE GLY GLU GLY ALA
SEQRES 16 A 400 ALA SER GLU GLY ASP ALA HIS ALA GLY PHE ASN PHE ALA
SEQRES 17 A 400 ALA THR LEU GLU CYS PRO ILE ILE PHE PHE CYS ARG ASN
SEQRES 18 A 400 ASN GLY TYR ALA ILE SER THR PRO THR SER GLU GLN TYR
SEQRES 19 A 400 ARG GLY ASP GLY ILE ALA ALA ARG GLY PRO GLY TYR GLY
SEQRES 20 A 400 ILE MET SER ILE ARG VAL ASP GLY ASN ASP VAL PHE ALA
SEQRES 21 A 400 VAL TYR ASN ALA THR LYS GLU ALA ARG ARG ARG ALA VAL
SEQRES 22 A 400 ALA GLU ASN GLN PRO PHE LEU ILE GLU ALA MET THR TYR
SEQRES 23 A 400 ARG ILE GLY HIS HIS SER THR SER ASP ASP SER SER ALA
SEQRES 24 A 400 TYR ARG SER VAL ASP GLU VAL ASN TYR TRP ASP LYS GLN
SEQRES 25 A 400 ASP HIS PRO ILE SER ARG LEU ARG HIS TYR LEU LEU SER
SEQRES 26 A 400 GLN GLY TRP TRP ASP GLU GLU GLN GLU LYS ALA TRP ARG
SEQRES 27 A 400 LYS GLN SER ARG ARG LYS VAL MET GLU ALA PHE GLU GLN
SEQRES 28 A 400 ALA GLU ARG LYS PRO LYS PRO ASN PRO ASN LEU LEU PHE
SEQRES 29 A 400 SER ASP VAL TYR GLN GLU MET PRO ALA GLN LEU ARG LYS
SEQRES 30 A 400 GLN GLN GLU SER LEU ALA ARG HIS LEU GLN THR TYR GLY
SEQRES 31 A 400 GLU HIS TYR PRO LEU ASP HIS PHE ASP LYS
SEQRES 1 B 342 VAL ALA HIS PHE THR PHE GLN PRO ASP PRO GLU PRO ARG
SEQRES 2 B 342 GLU TYR GLY GLN THR GLN LYS MET ASN LEU PHE GLN SER
SEQRES 3 B 342 VAL THR SER ALA LEU ASP ASN SER LEU ALA LYS ASP PRO
SEQRES 4 B 342 THR ALA VAL ILE PHE GLY GLU ASP VAL ALA PHE GLY GLY
SEQRES 5 B 342 VAL PHE ARG CYS THR VAL GLY LEU ARG ASP LYS TYR GLY
SEQRES 6 B 342 LYS ASP ARG VAL PHE ASN THR PRO LEU CYS GLU GLN GLY
SEQRES 7 B 342 ILE VAL GLY PHE GLY ILE GLY ILE ALA VAL THR GLY ALA
SEQRES 8 B 342 THR ALA ILE ALA GLU ILE GLN PHE ALA ASP TYR ILE PHE
SEQRES 9 B 342 PRO ALA PHE ASP GLN ILE VAL ASN GLU ALA ALA LYS TYR
SEQRES 10 B 342 ARG TYR ARG SER GLY ASP LEU PHE ASN CYS GLY SER LEU
SEQRES 11 B 342 THR ILE ARG SER PRO TRP GLY CYS VAL GLY HIS GLY ALA
SEQRES 12 B 342 LEU TYR HIS SER GLN SER PRO GLU ALA PHE PHE ALA HIS
SEQRES 13 B 342 CYS PRO GLY ILE LYS VAL VAL ILE PRO ARG SER PRO PHE
SEQRES 14 B 342 GLN ALA LYS GLY LEU LEU LEU SER CYS ILE GLU ASP LYS
SEQRES 15 B 342 ASN PRO CYS ILE PHE PHE GLU PRO LYS ILE LEU TYR ARG
SEQRES 16 B 342 ALA ALA ALA GLU GLU VAL PRO ILE GLU PRO TYR ASN ILE
SEQRES 17 B 342 PRO LEU SER GLN ALA GLU VAL ILE GLN GLU GLY SER ASP
SEQRES 18 B 342 VAL THR LEU VAL ALA TRP GLY THR GLN VAL HIS VAL ILE
SEQRES 19 B 342 ARG GLU VAL ALA SER MET ALA LYS GLU LYS LEU GLY VAL
SEQRES 20 B 342 SER CYS GLU VAL ILE ASP LEU ARG THR ILE ILE PRO TRP
SEQRES 21 B 342 ASP VAL ASP THR ILE CYS LYS SER VAL ILE LYS THR GLY
SEQRES 22 B 342 ARG LEU LEU ILE SER HIS GLU ALA PRO LEU THR GLY GLY
SEQRES 23 B 342 PHE ALA SER GLU ILE SER SER THR VAL GLN GLU GLU CYS
SEQRES 24 B 342 PHE LEU ASN LEU GLU ALA PRO ILE SER ARG VAL CYS GLY
SEQRES 25 B 342 TYR ASP THR PRO PHE PRO HIS ILE PHE GLU PRO PHE TYR
SEQRES 26 B 342 ILE PRO ASP LYS TRP LYS CYS TYR ASP ALA LEU ARG LYS
SEQRES 27 B 342 MET ILE ASN TYR
HET K A 501 1
HET MN A 503 1
HET TPP A 601 26
HET GOL A 701 6
HET K B 502 1
HETNAM K POTASSIUM ION
HETNAM MN MANGANESE (II) ION
HETNAM TPP THIAMINE DIPHOSPHATE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 K 2(K 1+)
FORMUL 4 MN MN 2+
FORMUL 5 TPP C12 H19 N4 O7 P2 S 1+
FORMUL 6 GOL C3 H8 O3
FORMUL 8 HOH *451(H2 O)
HELIX 1 1 ASN A 45 ASP A 49 5 5
HELIX 2 2 PRO A 53 GLN A 80 1 28
HELIX 3 3 GLU A 92 ALA A 102 1 11
HELIX 4 4 GLU A 115 ARG A 122 1 8
HELIX 5 5 PRO A 125 GLY A 135 1 11
HELIX 6 6 THR A 166 ASN A 182 1 17
HELIX 7 7 GLY A 194 SER A 197 5 4
HELIX 8 8 GLU A 198 LEU A 211 1 14
HELIX 9 9 SER A 231 GLN A 233 5 3
HELIX 10 10 ILE A 239 GLY A 243 5 5
HELIX 11 11 GLY A 243 GLY A 247 5 5
HELIX 12 12 ASP A 257 ASN A 276 1 20
HELIX 13 13 HIS A 314 GLN A 326 1 13
HELIX 14 14 ASP A 330 LYS A 355 1 26
HELIX 15 15 ASN A 359 PHE A 364 5 6
HELIX 16 16 PRO A 372 GLY A 390 1 19
HELIX 17 17 GLU A 391 TYR A 393 5 3
HELIX 18 18 PRO A 394 HIS A 397 5 4
HELIX 19 19 ASN B 22 ASP B 38 1 17
HELIX 20 20 GLY B 59 GLY B 65 1 7
HELIX 21 21 CYS B 75 THR B 89 1 15
HELIX 22 22 PHE B 99 ILE B 103 5 5
HELIX 23 23 ILE B 103 PRO B 105 5 3
HELIX 24 24 ALA B 106 ASN B 112 1 7
HELIX 25 25 GLU B 113 ALA B 115 5 3
HELIX 26 26 LYS B 116 SER B 121 1 6
HELIX 27 27 GLY B 142 HIS B 146 5 5
HELIX 28 28 PRO B 150 HIS B 156 1 7
HELIX 29 29 SER B 167 ASP B 181 1 15
HELIX 30 30 ILE B 192 TYR B 194 5 3
HELIX 31 31 THR B 229 GLY B 246 1 18
HELIX 32 32 ASP B 261 GLY B 273 1 13
HELIX 33 33 GLY B 286 PHE B 300 1 15
HELIX 34 34 PHE B 321 ILE B 326 1 6
HELIX 35 35 ASP B 328 ASN B 341 1 14
SHEET 1 AA 5 LEU A 108 PHE A 110 0
SHEET 2 AA 5 VAL A 187 GLY A 192 1 O ILE A 188 N PHE A 110
SHEET 3 AA 5 ILE A 215 ASN A 221 1 O ILE A 216 N CYS A 189
SHEET 4 AA 5 PHE A 279 MET A 284 1 O PHE A 279 N PHE A 217
SHEET 5 AA 5 MET A 249 ASP A 254 1 O MET A 249 N LEU A 280
SHEET 1 AB 2 TYR A 224 ALA A 225 0
SHEET 2 AB 2 THR A 228 PRO A 229 -1 O THR A 228 N ALA A 225
SHEET 1 BA 2 THR B 18 MET B 21 0
SHEET 2 BA 2 GLU B 199 PRO B 202 -1 O GLU B 199 N MET B 21
SHEET 1 BB 7 VAL B 69 ASN B 71 0
SHEET 2 BB 7 VAL B 42 GLY B 45 1 O ILE B 43 N PHE B 70
SHEET 3 BB 7 ALA B 93 GLU B 96 1 O ILE B 94 N PHE B 44
SHEET 4 BB 7 LEU B 130 TRP B 136 1 O THR B 131 N ALA B 95
SHEET 5 BB 7 CYS B 185 PRO B 190 1 O CYS B 185 N ILE B 132
SHEET 6 BB 7 LYS B 161 VAL B 163 1 O LYS B 161 N ILE B 186
SHEET 7 BB 7 THR B 256 ILE B 258 -1 N ILE B 257 O VAL B 162
SHEET 1 BC 5 GLU B 214 GLN B 217 0
SHEET 2 BC 5 CYS B 249 ASP B 253 -1 O VAL B 251 N ILE B 216
SHEET 3 BC 5 VAL B 222 ALA B 226 1 O VAL B 222 N GLU B 250
SHEET 4 BC 5 LEU B 275 PRO B 282 1 O LEU B 276 N VAL B 225
SHEET 5 BC 5 SER B 308 GLY B 312 1 O SER B 308 N ILE B 277
LINK OE1 GLN A 112 K K A 501 1555 1555 2.97
LINK O SER A 161 K K A 501 1555 1555 2.93
LINK OG SER A 161 K K A 501 1555 1555 2.92
LINK O PRO A 163 K K A 501 1555 1555 2.76
LINK OG1 THR A 166 K K A 501 1555 1555 3.07
LINK OE1 GLN A 167 K K A 501 1555 1555 2.93
LINK OE2 GLU A 193 MN MN A 503 1555 1555 2.21
LINK OD1 ASN A 222 MN MN A 503 1555 1555 2.22
LINK O TYR A 224 MN MN A 503 1555 1555 2.19
LINK K K A 501 O HOH A2078 1555 1555 2.73
LINK MN MN A 503 O1A TPP A 601 1555 1555 2.20
LINK MN MN A 503 O3B TPP A 601 1555 1555 2.22
LINK MN MN A 503 O HOH A2250 1555 1555 2.43
LINK O GLY B 128 K K B 502 1555 1555 2.79
LINK O LEU B 130 K K B 502 1555 1555 2.98
LINK O CYS B 178 K K B 502 1555 1555 2.86
LINK O ASP B 181 K K B 502 1555 1555 2.92
LINK O ASN B 183 K K B 502 1555 1555 2.79
LINK K K B 502 O HOH B2117 1555 1555 2.94
CISPEP 1 ILE B 258 PRO B 259 0 -0.93
SITE 1 AC1 6 GLN A 112 SER A 161 PRO A 163 THR A 166
SITE 2 AC1 6 GLN A 167 HOH A2078
SITE 1 AC2 5 GLU A 193 ASN A 222 TYR A 224 TPP A 601
SITE 2 AC2 5 HOH A2250
SITE 1 AC3 7 GLY B 128 LEU B 130 THR B 131 CYS B 178
SITE 2 AC3 7 ASP B 181 ASN B 183 HOH B2117
SITE 1 AC4 24 TYR A 113 ARG A 114 SER A 162 LEU A 164
SITE 2 AC4 24 GLY A 192 GLU A 193 GLY A 194 ALA A 195
SITE 3 AC4 24 GLU A 198 ARG A 220 ASN A 222 TYR A 224
SITE 4 AC4 24 ALA A 225 ILE A 226 HIS A 291 MN A 503
SITE 5 AC4 24 HOH A2152 HOH A2250 HOH A2251 GLU B 46
SITE 6 AC4 24 LEU B 74 GLU B 76 GLN B 98 TYR B 102
SITE 1 AC5 8 GLN A 374 HOH A2252 TRP B 260 THR B 284
SITE 2 AC5 8 GLU B 290 THR B 294 ARG B 309 HOH B2170
CRYST1 144.721 144.721 69.151 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 0.006910 0.003989 0.000000 0.00000
SCALE2 0.000000 0.007979 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014461 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
