HEADER OXIDOREDUCTASE 16-AUG-04 1X7Z
TITLE CRYSTAL STRUCTURE OF THE HUMAN MITOCHONDRIAL BRANCHED-CHAIN ALPHA-
TITLE 2 KETOACID DEHYDROGENASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-OXOISOVALERATE DEHYDROGENASE ALPHA SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE E1 COMPONENT
COMPND 5 ALPHA CHAIN, BCKDH E1-ALPHA, BCKDE1A;
COMPND 6 EC: 1.2.4.4;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: 2-OXOISOVALERATE DEHYDROGENASE BETA SUBUNIT;
COMPND 11 CHAIN: B;
COMPND 12 SYNONYM: BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE E1 COMPONENT
COMPND 13 BETA CHAIN, BCKDH E1-BETA;
COMPND 14 EC: 1.2.4.4;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BCKDHA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTRCHISB;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: BCKDHB;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PTRCHISB
KEYWDS OXIDOREDUCTASE, KETOACID DEHYDROGENASE, BRANCHED-CHAIN, MULTI-ENZYME
KEYWDS 2 COMPLEX, ACYLATION, OXIDATIVE DECARBOXYLATION MAPLE SYRUP URINE
KEYWDS 3 DISEASE, THIAMIN DIPHOSPHATE, PHOSPHORYLATION, FLAVOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.M.WYNN,M.KATO,M.MACHIUS,J.L.CHUANG,J.LI,D.R.TOMCHICK,D.T.CHUANG
REVDAT 7 23-AUG-23 1X7Z 1 REMARK
REVDAT 6 20-OCT-21 1X7Z 1 SEQADV
REVDAT 5 04-AUG-21 1X7Z 1 COMPND REMARK HET HETNAM
REVDAT 5 2 1 FORMUL LINK SITE ATOM
REVDAT 4 13-JUL-11 1X7Z 1 VERSN
REVDAT 3 24-FEB-09 1X7Z 1 VERSN
REVDAT 2 19-APR-05 1X7Z 1 JRNL
REVDAT 1 23-NOV-04 1X7Z 0
JRNL AUTH R.M.WYNN,M.KATO,M.MACHIUS,J.L.CHUANG,J.LI,D.R.TOMCHICK,
JRNL AUTH 2 D.T.CHUANG
JRNL TITL MOLECULAR MECHANISM FOR REGULATION OF THE HUMAN
JRNL TITL 2 MITOCHONDRIAL BRANCHED-CHAIN ALPHA-KETOACID DEHYDROGENASE
JRNL TITL 3 COMPLEX BY PHOSPHORYLATION
JRNL REF STRUCTURE V. 12 2185 2004
JRNL REFN ISSN 0969-2126
JRNL PMID 15576032
JRNL DOI 10.1016/J.STR.2004.09.013
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.LI,R.M.WYNN,M.MACHIUS,J.L.CHUANG,S.KARTHIKEYAN,
REMARK 1 AUTH 2 D.R.TOMCHICK,D.T.CHUANG
REMARK 1 TITL CROSSTALK BETWEEN THIAMIN DIPHOSPHATE BINDING AND
REMARK 1 TITL 2 PHOSPHORYLATION LOOP CONFORMATION IN HUMAN BRANCHED-CHAIN
REMARK 1 TITL 3 A-KETOACID DECARBOXYLASE/DEHYDROGENASE
REMARK 1 REF J.BIOL.CHEM. V. 279 32968 2004
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 2
REMARK 1 AUTH R.M.WYNN,M.MACHIUS,J.L.CHUANG,J.LI,D.R.TOMCHICK,D.T.CHUANG
REMARK 1 TITL ROLES OF HIS291-ALPHA AND HIS146-BETA IN THE REDUCTIVE
REMARK 1 TITL 2 ACYLATION REACTION CATALYZED BY HUMAN BRANCHED-CHAIN
REMARK 1 TITL 3 ALPHA-KETOACID DEHYDROGENASE: REFINED PHOSPHORYLATION LOOP
REMARK 1 TITL 4 STRUCTURE IN THE ACTIVE SITE
REMARK 1 REF J.BIOL.CHEM. V. 278 43402 2003
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 1.72 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0003
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.72
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 87692
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) : 0.154
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.700
REMARK 3 FREE R VALUE TEST SET COUNT : 1514
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) : 1.72
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6360
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.11
REMARK 3 BIN R VALUE (WORKING SET) : 0.2460
REMARK 3 BIN FREE R VALUE SET COUNT : 131
REMARK 3 BIN FREE R VALUE : 0.2910
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5699
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 636
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.94
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.67000
REMARK 3 B22 (A**2) : 0.67000
REMARK 3 B33 (A**2) : -1.01000
REMARK 3 B12 (A**2) : 0.34000
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): 0.087
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.089
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.060
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.508
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6089 ; 0.020 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8286 ; 1.600 ; 1.937
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 762 ; 5.991 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 293 ;35.938 ;23.618
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 993 ;13.367 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 43 ;17.917 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 867 ; 0.123 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4799 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3228 ; 0.222 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4263 ; 0.306 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 603 ; 0.150 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 5 ; 0.111 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 234 ; 0.171 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 64 ; 0.192 ; 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): 3726 ; 0.902 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6035 ; 1.523 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2400 ; 2.715 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2251 ; 4.323 ; 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: NULL
REMARK 4
REMARK 4 1X7Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-AUG-04.
REMARK 100 THE DEPOSITION ID IS D_1000030053.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-OCT-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.80
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 89234
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.720
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.72
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.64100
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: 1OLS
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: PEG4000, PH 5.80, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, 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 23.10733
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 46.21467
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 46.21467
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 23.10733
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HETEROTETRAMER GENERATED FROM
REMARK 300 THE HETERODIMER IN THE AYSMMETRIC UNIT BY THE OPERATIONS: X-Y,-Y,2/
REMARK 300 3-Z.
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 28080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -191.0 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 46.21467
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 909 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 SBD MOLECULE DETAILS
REMARK 400 MOLECULE: DIHYDROLIPOYLLYSINE-RESIDUE (2-METHYLPROPANOYL)
REMARK 400 TRANSFERASE;
REMARK 400 FRAGMENT: SUBUNIT-BINDING DOMAIN;
REMARK 400 EC: 2.3.1.168;
REMARK 400 GENE: BCATE2;
REMARK 400 THE SBD MOLECULE WAS CREATED FROM A GENETICALLY MODIFIED
REMARK 400 SOURCE CONSISTENT WITH THE THE SOURCE RECORDS OF THE ALPHA
REMARK 400 AND BETA SUBUNITS OF 2-OXOISOVALERATE DEHYDROGENASE FOUND
REMARK 400 IN THIS STRUCTURE.
REMARK 400 SEQUENCE:
REMARK 400 GEIKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYLEKQTLEHHHHHH
REMARK 400 1 58
REMARK 400 RESIDUES 2-50 CORRESPOND TO RESIDUES 165-213 OF SWISSPROT
REMARK 400 ENTRY ODB2_HUMAN, ACCESSION NUMBER P11182. THE FIRST GLYCINE
REMARK 400 RESIDUE IS A CLONING ARTIFACT. THE LAST 8 C-TERMINAL
REMARK 400 RESIDUES (LEHHHHHH) ARE HIS TAG RESIDUES.
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 SER A 302
REMARK 465 VAL A 303
REMARK 465 ASP A 304
REMARK 465 GLU A 305
REMARK 465 VAL B 1
REMARK 465 ALA B 2
REMARK 465 HIS B 3
REMARK 465 PHE B 4
REMARK 465 THR B 5
REMARK 465 PHE B 6
REMARK 465 GLN B 7
REMARK 465 PRO B 8
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 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 6 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 CG GLN A 112 O HOH A 855 1.65
REMARK 500 NE ARG A 220 O HOH A 866 2.07
REMARK 500
REMARK 500 REMARK: NULL
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 ARG A 220 CG ARG A 220 CD 0.165
REMARK 500
REMARK 500 REMARK: NULL
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 B 118 NE - CZ - NH1 ANGL. DEV. = 3.2 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 GLN A 112 -113.84 -147.44
REMARK 500 TYR A 113 -12.82 165.89
REMARK 500 ARG A 114 32.67 -97.31
REMARK 500 ALA A 165 -6.87 73.18
REMARK 500 ILE A 226 -111.59 51.45
REMARK 500 ASP A 313 83.72 -153.08
REMARK 500 CYS B 75 96.33 -161.17
REMARK 500 GLU B 113 -73.90 -110.85
REMARK 500 VAL B 139 18.26 -142.74
REMARK 500 HIS B 141 17.31 -155.48
REMARK 500 ALA B 143 -144.40 55.00
REMARK 500 LYS B 182 38.52 -88.34
REMARK 500 ALA B 196 -163.03 -70.48
REMARK 500 ARG B 255 -61.80 70.61
REMARK 500 HIS B 319 -77.16 -74.03
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 701 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 112 OE1
REMARK 620 2 SER A 161 O 67.0
REMARK 620 3 SER A 161 OG 133.0 66.1
REMARK 620 4 PRO A 163 O 79.3 90.3 97.5
REMARK 620 5 THR A 166 OG1 138.3 128.8 74.0 64.0
REMARK 620 6 GLN A 167 OE1 83.0 145.4 142.2 101.1 85.1
REMARK 620 7 HOH A 802 O 90.0 77.2 83.1 166.0 129.0 86.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 703 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 193 OE1
REMARK 620 2 ASN A 222 OD1 88.1
REMARK 620 3 TYR A 224 O 117.9 78.8
REMARK 620 4 TPP A 801 O1A 89.8 174.1 107.0
REMARK 620 5 TPP A 801 O2B 160.4 90.5 80.9 89.6
REMARK 620 6 HOH A 813 O 76.7 85.2 157.6 89.0 83.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 702 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 128 O
REMARK 620 2 LEU B 130 O 84.3
REMARK 620 3 THR B 131 OG1 135.7 63.8
REMARK 620 4 CYS B 178 O 150.1 123.0 61.8
REMARK 620 5 ASP B 181 O 68.1 152.2 140.4 84.7
REMARK 620 6 ASN B 183 O 72.5 83.0 127.9 118.9 85.5
REMARK 620 7 HOH B 915 O 93.3 74.3 50.5 84.0 109.4 154.4
REMARK 620 N 1 2 3 4 5 6
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 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TPP A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 901
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1U5B RELATED DB: PDB
REMARK 900 WILD-TYPE PROTEIN
REMARK 900 RELATED ID: 1X7W RELATED DB: PDB
REMARK 900 RELATED ID: 1X7X RELATED DB: PDB
REMARK 900 RELATED ID: 1X7Y RELATED DB: PDB
REMARK 900 RELATED ID: 1X80 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SUBUNIT-BINDING DOMAIN (SBD) OF THE E2 PROTEIN BINDS TO
REMARK 999 THE C-TERMINAL REGION OF THE E1 BETA SUBUNIT. HOWEVER, THE
REMARK 999 ELECTRON DENSITY OF THIS DOMAIN IS TOO WEAK TO BUILD A
REMARK 999 MODEL, THEREFORE THIS MOLECULE HAS NOT BEEN MODELED IN THE
REMARK 999 COORDINATES.
REMARK 999 FURTHER INFORMATION ON THIS MOLECULE CAN BE FOUND IN REMARK
REMARK 999 400.
DBREF 1X7Z A 1 400 UNP P12694 ODBA_HUMAN 46 445
DBREF 1X7Z B 1 342 UNP P21953 ODBB_HUMAN 51 392
SEQADV 1X7Z ASP A 292 UNP P12694 SER 337 ENGINEERED MUTATION
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 ASP 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 701 1
HET MN A 703 1
HET CL A 704 1
HET TPP A 801 26
HET K B 702 1
HET GOL B 901 6
HETNAM K POTASSIUM ION
HETNAM MN MANGANESE (II) ION
HETNAM CL CHLORIDE 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 CL CL 1-
FORMUL 6 TPP C12 H19 N4 O7 P2 S 1+
FORMUL 8 GOL C3 H8 O3
FORMUL 9 HOH *636(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 LEU A 103 1 12
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 247 5 9
HELIX 11 11 ASP A 257 ASN A 276 1 20
HELIX 12 12 ASP A 296 TYR A 300 5 5
HELIX 13 13 VAL A 306 ASP A 313 1 8
HELIX 14 14 HIS A 314 GLY A 327 1 14
HELIX 15 15 ASP A 330 LYS A 355 1 26
HELIX 16 16 ASN A 359 PHE A 364 5 6
HELIX 17 17 PRO A 372 GLY A 390 1 19
HELIX 18 18 GLU A 391 TYR A 393 5 3
HELIX 19 19 PRO A 394 PHE A 398 5 5
HELIX 20 20 ASN B 22 ASP B 38 1 17
HELIX 21 21 GLY B 59 GLY B 65 1 7
HELIX 22 22 CYS B 75 THR B 89 1 15
HELIX 23 23 PHE B 99 PRO B 105 5 7
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 PRO B 150 HIS B 156 1 7
HELIX 28 28 SER B 167 ASP B 181 1 15
HELIX 29 29 ILE B 192 TYR B 194 5 3
HELIX 30 30 THR B 229 GLY B 246 1 18
HELIX 31 31 ASP B 261 GLY B 273 1 13
HELIX 32 32 GLY B 286 PHE B 300 1 15
HELIX 33 33 LEU B 301 LEU B 303 5 3
HELIX 34 34 PHE B 321 ILE B 326 1 6
HELIX 35 35 ASP B 328 ASN B 341 1 14
SHEET 1 A 5 LEU A 108 PHE A 110 0
SHEET 2 A 5 VAL A 187 GLY A 192 1 O ILE A 188 N PHE A 110
SHEET 3 A 5 ILE A 215 ASN A 221 1 O PHE A 218 N CYS A 189
SHEET 4 A 5 PHE A 279 MET A 284 1 O ALA A 283 N CYS A 219
SHEET 5 A 5 MET A 249 ASP A 254 1 N VAL A 253 O MET A 284
SHEET 1 B 2 TYR A 224 ALA A 225 0
SHEET 2 B 2 THR A 228 PRO A 229 -1 O THR A 228 N ALA A 225
SHEET 1 C 2 THR B 18 MET B 21 0
SHEET 2 C 2 GLU B 199 PRO B 202 -1 O GLU B 199 N MET B 21
SHEET 1 D 7 VAL B 69 ASN B 71 0
SHEET 2 D 7 VAL B 42 GLY B 45 1 N ILE B 43 O PHE B 70
SHEET 3 D 7 ALA B 93 GLU B 96 1 O ILE B 94 N VAL B 42
SHEET 4 D 7 LEU B 130 TRP B 136 1 O ARG B 133 N ALA B 95
SHEET 5 D 7 CYS B 185 PRO B 190 1 O PHE B 187 N ILE B 132
SHEET 6 D 7 LYS B 161 VAL B 163 1 N LYS B 161 O ILE B 186
SHEET 7 D 7 THR B 256 ILE B 258 -1 O ILE B 257 N VAL B 162
SHEET 1 E 5 GLU B 214 GLN B 217 0
SHEET 2 E 5 CYS B 249 ASP B 253 -1 O ASP B 253 N GLU B 214
SHEET 3 E 5 VAL B 222 ALA B 226 1 N VAL B 222 O GLU B 250
SHEET 4 E 5 LEU B 275 PRO B 282 1 O LEU B 276 N THR B 223
SHEET 5 E 5 SER B 308 GLY B 312 1 O SER B 308 N ILE B 277
LINK OE1AGLN A 112 K K A 701 1555 1555 2.95
LINK O SER A 161 K K A 701 1555 1555 2.82
LINK OG SER A 161 K K A 701 1555 1555 2.91
LINK O PRO A 163 K K A 701 1555 1555 2.64
LINK OG1 THR A 166 K K A 701 1555 1555 3.04
LINK OE1 GLN A 167 K K A 701 1555 1555 2.83
LINK OE1 GLU A 193 MN MN A 703 1555 1555 2.23
LINK OD1 ASN A 222 MN MN A 703 1555 1555 2.27
LINK O TYR A 224 MN MN A 703 1555 1555 2.20
LINK K K A 701 O HOH A 802 1555 1555 2.65
LINK MN MN A 703 O1A TPP A 801 1555 1555 2.14
LINK MN MN A 703 O2B TPP A 801 1555 1555 2.13
LINK MN MN A 703 O HOH A 813 1555 1555 2.37
LINK O GLY B 128 K K B 702 1555 1555 2.72
LINK O LEU B 130 K K B 702 1555 1555 2.92
LINK OG1 THR B 131 K K B 702 1555 1555 3.47
LINK O CYS B 178 K K B 702 1555 1555 2.75
LINK O ASP B 181 K K B 702 1555 1555 2.81
LINK O ASN B 183 K K B 702 1555 1555 2.68
LINK K K B 702 O HOH B 915 1555 1555 2.93
CISPEP 1 ILE B 258 PRO B 259 0 -13.23
SITE 1 AC1 6 GLN A 112 SER A 161 PRO A 163 THR A 166
SITE 2 AC1 6 GLN A 167 HOH A 802
SITE 1 AC2 7 GLY B 128 LEU B 130 THR B 131 CYS B 178
SITE 2 AC2 7 ASP B 181 ASN B 183 HOH B 915
SITE 1 AC3 5 GLU A 193 ASN A 222 TYR A 224 TPP A 801
SITE 2 AC3 5 HOH A 813
SITE 1 AC4 4 TYR A 113 TPP A 801 TYR B 102 HIS B 146
SITE 1 AC5 26 GLN A 112 TYR A 113 ARG A 114 SER A 162
SITE 2 AC5 26 LEU A 164 GLY A 192 GLU A 193 GLY A 194
SITE 3 AC5 26 ALA A 195 GLU A 198 ARG A 220 ASN A 222
SITE 4 AC5 26 TYR A 224 ALA A 225 ILE A 226 HIS A 291
SITE 5 AC5 26 MN A 703 CL A 704 HOH A 813 HOH A 840
SITE 6 AC5 26 HOH A 866 GLU B 46 LEU B 74 GLU B 76
SITE 7 AC5 26 GLN B 98 TYR B 102
SITE 1 AC6 7 GLN A 374 TRP B 260 THR B 284 GLU B 290
SITE 2 AC6 7 THR B 294 ARG B 309 HOH B 954
CRYST1 145.310 145.310 69.322 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 0.006882 0.003973 0.000000 0.00000
SCALE2 0.000000 0.007946 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014425 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
