HEADER OXIDOREDUCTASE 05-OCT-05 2C3D
TITLE 2.15 ANGSTROM CRYSTAL STRUCTURE OF 2-KETOPROPYL COENZYME M
TITLE 2 OXIDOREDUCTASE CARBOXYLASE WITH A COENZYME M DISULFIDE
TITLE 3 BOUND AT THE ACTIVE SITE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-OXOPROPYL-COM REDUCTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: NADPH\:2-KETOPROPYL COENZYME M CARBOXYLASE/
COMPND 5 OXIDOREDUCTASE, 2-KPCC, ALIPHATIC EPOXIDE CARBOXYLATION
COMPND 6 COMPONENT II;
COMPND 7 EC: 1.8.1.5
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XANTHOBACTER AUTOTROPHICUS;
SOURCE 3 ORGANISM_TAXID: 78245;
SOURCE 4 STRAIN: PY2;
SOURCE 5 ATCC: 35674
KEYWDS OXIDOREDUCTASE, COENZYME M, COM DISULFIDE, REDOX-ACTIVE
KEYWDS 2 CENTER, FAD
EXPDTA X-RAY DIFFRACTION
AUTHOR A.S.PANDEY,B.NOCEK,D.D.CLARK,S.A.ENSIGN,J.W.PETERS
REVDAT 3 24-FEB-09 2C3D 1 VERSN
REVDAT 2 11-JAN-06 2C3D 1 JRNL
REVDAT 1 07-NOV-05 2C3D 0
JRNL AUTH A.S.PANDEY,B.NOCEK,D.D.CLARK,S.A.ENSIGN,J.W.PETERS
JRNL TITL MECHANISTIC IMPLICATIONS OF THE STRUCTURE OF THE
JRNL TITL 2 MIXED-DISULFIDE INTERMEDIATE OF THE DISULFIDE
JRNL TITL 3 OXIDOREDUCTASE, 2-KETOPROPYL-COENZYME M
JRNL TITL 4 OXIDOREDUCTASE/CARBOXYLASE.
JRNL REF BIOCHEMISTRY V. 45 113 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 16388586
JRNL DOI 10.1021/BI051518O
REMARK 2
REMARK 2 RESOLUTION. 2.15 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) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1257092.13
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 111633
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) : 0.203
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.9
REMARK 3 FREE R VALUE TEST SET COUNT : 2162
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) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.28
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.8
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 16521
REMARK 3 BIN R VALUE (WORKING SET) : 0.248
REMARK 3 BIN FREE R VALUE : 0.272
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.2
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 365
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.014
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8046
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 134
REMARK 3 SOLVENT ATOMS : 654
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.3
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.5
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.22
REMARK 3 B22 (A**2) : 1.08
REMARK 3 B33 (A**2) : 1.14
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 2.36
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.21
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) : 0.29
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.3
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.5
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.78
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) : 1.77 ; 1.50
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.45 ; 2.00
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.07 ; 2.00
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.26 ; 2.50
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.375927
REMARK 3 BSOL : 67.0819
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 : FAD-NEW.PAR
REMARK 3 PARAMETER FILE 3 : COM.PAR
REMARK 3 PARAMETER FILE 4 : WATER.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : COM.TOP
REMARK 3 TOPOLOGY FILE 3 : FAD-NEW.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2C3D COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-OCT-05.
REMARK 100 THE PDBE ID CODE IS EBI-25893.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE (MAR 345)
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58516
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.26000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: PDB ENTRY 1M09
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA):NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.17 M SODIUM ACETATE 0.085M
REMARK 280 TRIS-HCL PH 8.5 25.5% PEG4000 15% GLYCEROL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 30.02500
REMARK 290 SMTRY3 2 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 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 400
REMARK 400 COMPOUND
REMARK 400 CATALYZES THE REDUCTIVE CLEAVAGE OF THE THIOETHER
REMARK 400 LINKAGE OF 2-KETOPROPYL-COENZYME M, AND THE SUBSEQUENT
REMARK 400 CARBOXYLATION OF THE KETOPROPYL CLEAVAGE PRODUCT, YIELDING
REMARK 400 THE PRODUCTS ACETOACETATE AND FREE COENZYME M.
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 MET B 1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500
REMARK 500 O ALA A 285 OH TYR A 340 1565 2.20
REMARK 500 OH TYR A 340 O ALA A 285 1545 2.20
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 CYS A 82 CB CYS A 82 SG 0.099
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 THR A 393 N - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500 THR B 393 N - CA - C ANGL. DEV. = -16.6 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 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 85 13.50 -157.23
REMARK 500 ALA A 86 -108.81 -119.08
REMARK 500 TYR A 110 -123.48 48.95
REMARK 500 ASN A 163 1.76 -67.55
REMARK 500 ALA A 181 51.17 -142.12
REMARK 500 SER A 223 -177.13 -69.78
REMARK 500 THR A 246 -113.90 -108.62
REMARK 500 THR A 393 -118.57 -125.66
REMARK 500 ASN A 428 49.44 -73.55
REMARK 500 ALA A 430 23.00 -71.59
REMARK 500 SER A 434 -166.63 -179.93
REMARK 500 ARG A 436 1.14 82.55
REMARK 500 ASN B 85 14.15 -157.40
REMARK 500 ALA B 86 -108.85 -119.30
REMARK 500 TYR B 110 -123.66 48.84
REMARK 500 ASN B 163 2.73 -67.26
REMARK 500 ALA B 181 51.29 -142.05
REMARK 500 SER B 223 -176.55 -69.25
REMARK 500 THR B 246 -113.76 -108.19
REMARK 500 THR B 393 -119.08 -125.85
REMARK 500 ALA B 430 23.13 -69.99
REMARK 500 SER B 434 -167.15 179.19
REMARK 500 ARG B 436 0.53 82.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A1524
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COM A1525
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COM A1526
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B1524
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COM B1525
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COM B1526
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MO9 RELATED DB: PDB
REMARK 900 NADPH DEPENDENT 2-KETOPROPYL COENZYME
REMARK 900 MOXIDOREDUCTASE/CARBOXYLASE COMPLEXED WITH 2-
REMARK 900 KETOPROPYLCOENZYME M
REMARK 900 RELATED ID: 1MOK RELATED DB: PDB
REMARK 900 NADPH DEPENDENT 2-KETOPROPYL COENZYME
REMARK 900 MOXIDOREDUCTASE/CARBOXYLASE
REMARK 900 RELATED ID: 2C3D RELATED DB: PDB
REMARK 900 2.15 ANGSTROM CRYSTAL STRUCTURE OF 2-
REMARK 900 KETOPROPYL COENZYME M OXIDOREDUCTASE CARBOXYLASE
REMARK 900 WITH A COENZYME M DISULFIDE BOUND AT THE
REMARK 900 ACTIVE SITE
DBREF 2C3D A 1 523 UNP Q56839 XECC_XANP2 1 523
DBREF 2C3D B 1 523 UNP Q56839 XECC_XANP2 1 523
SEQRES 1 A 523 MET LYS VAL TRP ASN ALA ARG ASN ASP HIS LEU THR ILE
SEQRES 2 A 523 ASN GLN TRP ALA THR ARG ILE ASP GLU ILE LEU GLU ALA
SEQRES 3 A 523 PRO ASP GLY GLY GLU VAL ILE TYR ASN VAL ASP GLU ASN
SEQRES 4 A 523 ASP PRO ARG GLU TYR ASP ALA ILE PHE ILE GLY GLY GLY
SEQRES 5 A 523 ALA ALA GLY ARG PHE GLY SER ALA TYR LEU ARG ALA MET
SEQRES 6 A 523 GLY GLY ARG GLN LEU ILE VAL ASP ARG TRP PRO PHE LEU
SEQRES 7 A 523 GLY GLY SER CYS PRO HIS ASN ALA CYS VAL PRO HIS HIS
SEQRES 8 A 523 LEU PHE SER ASP CYS ALA ALA GLU LEU MET LEU ALA ARG
SEQRES 9 A 523 THR PHE SER GLY GLN TYR TRP PHE PRO ASP MET THR GLU
SEQRES 10 A 523 LYS VAL VAL GLY ILE LYS GLU VAL VAL ASP LEU PHE ARG
SEQRES 11 A 523 ALA GLY ARG ASN GLY PRO HIS GLY ILE MET ASN PHE GLN
SEQRES 12 A 523 SER LYS GLU GLN LEU ASN LEU GLU TYR ILE LEU ASN CYS
SEQRES 13 A 523 PRO ALA LYS VAL ILE ASP ASN HIS THR VAL GLU ALA ALA
SEQRES 14 A 523 GLY LYS VAL PHE LYS ALA LYS ASN LEU ILE LEU ALA VAL
SEQRES 15 A 523 GLY ALA GLY PRO GLY THR LEU ASP VAL PRO GLY VAL ASN
SEQRES 16 A 523 ALA LYS GLY VAL PHE ASP HIS ALA THR LEU VAL GLU GLU
SEQRES 17 A 523 LEU ASP TYR GLU PRO GLY SER THR VAL VAL VAL VAL GLY
SEQRES 18 A 523 GLY SER LYS THR ALA VAL GLU TYR GLY CYS PHE PHE ASN
SEQRES 19 A 523 ALA THR GLY ARG ARG THR VAL MET LEU VAL ARG THR GLU
SEQRES 20 A 523 PRO LEU LYS LEU ILE LYS ASP ASN GLU THR ARG ALA TYR
SEQRES 21 A 523 VAL LEU ASP ARG MET LYS GLU GLN GLY MET GLU ILE ILE
SEQRES 22 A 523 SER GLY SER ASN VAL THR ARG ILE GLU GLU ASP ALA ASN
SEQRES 23 A 523 GLY ARG VAL GLN ALA VAL VAL ALA MET THR PRO ASN GLY
SEQRES 24 A 523 GLU MET ARG ILE GLU THR ASP PHE VAL PHE LEU GLY LEU
SEQRES 25 A 523 GLY GLU GLN PRO ARG SER ALA GLU LEU ALA LYS ILE LEU
SEQRES 26 A 523 GLY LEU ASP LEU GLY PRO LYS GLY GLU VAL LEU VAL ASN
SEQRES 27 A 523 GLU TYR LEU GLN THR SER VAL PRO ASN VAL TYR ALA VAL
SEQRES 28 A 523 GLY ASP LEU ILE GLY GLY PRO MET GLU MET PHE LYS ALA
SEQRES 29 A 523 ARG LYS SER GLY CYS TYR ALA ALA ARG ASN VAL MET GLY
SEQRES 30 A 523 GLU LYS ILE SER TYR THR PRO LYS ASN TYR PRO ASP PHE
SEQRES 31 A 523 LEU HIS THR HIS TYR GLU VAL SER PHE LEU GLY MET GLY
SEQRES 32 A 523 GLU GLU GLU ALA ARG ALA ALA GLY HIS GLU ILE VAL THR
SEQRES 33 A 523 ILE LYS MET PRO PRO ASP THR GLU ASN GLY LEU ASN VAL
SEQRES 34 A 523 ALA LEU PRO ALA SER ASP ARG THR MET LEU TYR ALA PHE
SEQRES 35 A 523 GLY LYS GLY THR ALA HIS MET SER GLY PHE GLN LYS ILE
SEQRES 36 A 523 VAL ILE ASP ALA LYS THR ARG LYS VAL LEU GLY ALA HIS
SEQRES 37 A 523 HIS VAL GLY TYR GLY ALA LYS ASP ALA PHE GLN TYR LEU
SEQRES 38 A 523 ASN VAL LEU ILE LYS GLN GLY LEU THR VAL ASP GLU LEU
SEQRES 39 A 523 GLY ASP MET ASP GLU LEU PHE LEU ASN PRO THR HIS PHE
SEQRES 40 A 523 ILE GLN LEU SER ARG LEU ARG ALA GLY SER LYS ASN LEU
SEQRES 41 A 523 VAL SER LEU
SEQRES 1 B 523 MET LYS VAL TRP ASN ALA ARG ASN ASP HIS LEU THR ILE
SEQRES 2 B 523 ASN GLN TRP ALA THR ARG ILE ASP GLU ILE LEU GLU ALA
SEQRES 3 B 523 PRO ASP GLY GLY GLU VAL ILE TYR ASN VAL ASP GLU ASN
SEQRES 4 B 523 ASP PRO ARG GLU TYR ASP ALA ILE PHE ILE GLY GLY GLY
SEQRES 5 B 523 ALA ALA GLY ARG PHE GLY SER ALA TYR LEU ARG ALA MET
SEQRES 6 B 523 GLY GLY ARG GLN LEU ILE VAL ASP ARG TRP PRO PHE LEU
SEQRES 7 B 523 GLY GLY SER CYS PRO HIS ASN ALA CYS VAL PRO HIS HIS
SEQRES 8 B 523 LEU PHE SER ASP CYS ALA ALA GLU LEU MET LEU ALA ARG
SEQRES 9 B 523 THR PHE SER GLY GLN TYR TRP PHE PRO ASP MET THR GLU
SEQRES 10 B 523 LYS VAL VAL GLY ILE LYS GLU VAL VAL ASP LEU PHE ARG
SEQRES 11 B 523 ALA GLY ARG ASN GLY PRO HIS GLY ILE MET ASN PHE GLN
SEQRES 12 B 523 SER LYS GLU GLN LEU ASN LEU GLU TYR ILE LEU ASN CYS
SEQRES 13 B 523 PRO ALA LYS VAL ILE ASP ASN HIS THR VAL GLU ALA ALA
SEQRES 14 B 523 GLY LYS VAL PHE LYS ALA LYS ASN LEU ILE LEU ALA VAL
SEQRES 15 B 523 GLY ALA GLY PRO GLY THR LEU ASP VAL PRO GLY VAL ASN
SEQRES 16 B 523 ALA LYS GLY VAL PHE ASP HIS ALA THR LEU VAL GLU GLU
SEQRES 17 B 523 LEU ASP TYR GLU PRO GLY SER THR VAL VAL VAL VAL GLY
SEQRES 18 B 523 GLY SER LYS THR ALA VAL GLU TYR GLY CYS PHE PHE ASN
SEQRES 19 B 523 ALA THR GLY ARG ARG THR VAL MET LEU VAL ARG THR GLU
SEQRES 20 B 523 PRO LEU LYS LEU ILE LYS ASP ASN GLU THR ARG ALA TYR
SEQRES 21 B 523 VAL LEU ASP ARG MET LYS GLU GLN GLY MET GLU ILE ILE
SEQRES 22 B 523 SER GLY SER ASN VAL THR ARG ILE GLU GLU ASP ALA ASN
SEQRES 23 B 523 GLY ARG VAL GLN ALA VAL VAL ALA MET THR PRO ASN GLY
SEQRES 24 B 523 GLU MET ARG ILE GLU THR ASP PHE VAL PHE LEU GLY LEU
SEQRES 25 B 523 GLY GLU GLN PRO ARG SER ALA GLU LEU ALA LYS ILE LEU
SEQRES 26 B 523 GLY LEU ASP LEU GLY PRO LYS GLY GLU VAL LEU VAL ASN
SEQRES 27 B 523 GLU TYR LEU GLN THR SER VAL PRO ASN VAL TYR ALA VAL
SEQRES 28 B 523 GLY ASP LEU ILE GLY GLY PRO MET GLU MET PHE LYS ALA
SEQRES 29 B 523 ARG LYS SER GLY CYS TYR ALA ALA ARG ASN VAL MET GLY
SEQRES 30 B 523 GLU LYS ILE SER TYR THR PRO LYS ASN TYR PRO ASP PHE
SEQRES 31 B 523 LEU HIS THR HIS TYR GLU VAL SER PHE LEU GLY MET GLY
SEQRES 32 B 523 GLU GLU GLU ALA ARG ALA ALA GLY HIS GLU ILE VAL THR
SEQRES 33 B 523 ILE LYS MET PRO PRO ASP THR GLU ASN GLY LEU ASN VAL
SEQRES 34 B 523 ALA LEU PRO ALA SER ASP ARG THR MET LEU TYR ALA PHE
SEQRES 35 B 523 GLY LYS GLY THR ALA HIS MET SER GLY PHE GLN LYS ILE
SEQRES 36 B 523 VAL ILE ASP ALA LYS THR ARG LYS VAL LEU GLY ALA HIS
SEQRES 37 B 523 HIS VAL GLY TYR GLY ALA LYS ASP ALA PHE GLN TYR LEU
SEQRES 38 B 523 ASN VAL LEU ILE LYS GLN GLY LEU THR VAL ASP GLU LEU
SEQRES 39 B 523 GLY ASP MET ASP GLU LEU PHE LEU ASN PRO THR HIS PHE
SEQRES 40 B 523 ILE GLN LEU SER ARG LEU ARG ALA GLY SER LYS ASN LEU
SEQRES 41 B 523 VAL SER LEU
HET FAD A1524 53
HET COM A1525 7
HET COM A1526 7
HET FAD B1524 53
HET COM B1525 7
HET COM B1526 7
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM COM 1-THIOETHANESULFONIC ACID
FORMUL 3 FAD 2(C27 H33 N9 O15 P2)
FORMUL 4 COM 4(C2 H6 O3 S2)
FORMUL 9 HOH *654(H2 O1)
HELIX 1 1 THR A 12 ALA A 26 1 15
HELIX 2 2 GLY A 52 MET A 65 1 14
HELIX 3 3 GLY A 80 ALA A 86 1 7
HELIX 4 4 ALA A 86 PHE A 106 1 21
HELIX 5 5 GLY A 121 ARG A 133 1 13
HELIX 6 6 ARG A 133 GLN A 147 1 15
HELIX 7 7 ASP A 201 LEU A 209 1 9
HELIX 8 8 SER A 223 THR A 236 1 14
HELIX 9 9 ASP A 254 GLN A 268 1 15
HELIX 10 10 SER A 318 GLY A 326 1 9
HELIX 11 11 GLY A 352 GLY A 356 5 5
HELIX 12 12 GLU A 360 MET A 376 1 17
HELIX 13 13 GLY A 403 ALA A 410 1 8
HELIX 14 14 THR A 437 GLY A 443 1 7
HELIX 15 15 THR A 446 GLY A 451 5 6
HELIX 16 16 ALA A 474 GLN A 487 1 14
HELIX 17 17 THR A 490 ASP A 496 1 7
HELIX 18 18 HIS A 506 ALA A 515 1 10
HELIX 19 19 THR B 12 ALA B 26 1 15
HELIX 20 20 GLY B 52 MET B 65 1 14
HELIX 21 21 GLY B 80 ALA B 86 1 7
HELIX 22 22 ALA B 86 PHE B 106 1 21
HELIX 23 23 GLY B 121 ARG B 133 1 13
HELIX 24 24 ARG B 133 GLN B 147 1 15
HELIX 25 25 ASP B 201 LEU B 209 1 9
HELIX 26 26 SER B 223 THR B 236 1 14
HELIX 27 27 ASP B 254 GLN B 268 1 15
HELIX 28 28 SER B 318 GLY B 326 1 9
HELIX 29 29 GLY B 352 GLY B 356 5 5
HELIX 30 30 GLU B 360 MET B 376 1 17
HELIX 31 31 GLY B 403 ALA B 410 1 8
HELIX 32 32 THR B 437 GLY B 443 1 7
HELIX 33 33 THR B 446 GLY B 451 5 6
HELIX 34 34 ALA B 474 GLN B 487 1 14
HELIX 35 35 THR B 490 ASP B 496 1 7
HELIX 36 36 HIS B 506 ALA B 515 1 10
SHEET 1 AA 7 VAL A 3 ASN A 5 0
SHEET 2 AA 7 VAL A 32 ASN A 35 1 O VAL A 32 N TRP A 4
SHEET 3 AA 7 TYR A 152 LEU A 154 -1 O TYR A 152 N ASN A 35
SHEET 4 AA 7 GLN A 69 ASP A 73 1 O ILE A 71 N ILE A 153
SHEET 5 AA 7 ALA A 46 ILE A 49 1 O ALA A 46 N LEU A 70
SHEET 6 AA 7 LEU A 178 LEU A 180 1 O ILE A 179 N ILE A 49
SHEET 7 AA 7 VAL A 348 ALA A 350 1 O TYR A 349 N LEU A 180
SHEET 1 AB 3 LYS A 159 ASP A 162 0
SHEET 2 AB 3 THR A 165 ALA A 168 -1 O THR A 165 N ILE A 161
SHEET 3 AB 3 LYS A 171 LYS A 174 -1 O LYS A 171 N ALA A 168
SHEET 1 AC 2 ALA A 184 GLY A 185 0
SHEET 2 AC 2 GLN A 315 PRO A 316 -1 O GLN A 315 N GLY A 185
SHEET 1 AD 5 VAL A 199 PHE A 200 0
SHEET 2 AD 5 VAL A 308 LEU A 310 1 O VAL A 308 N PHE A 200
SHEET 3 AD 5 THR A 216 VAL A 220 1 O VAL A 218 N PHE A 309
SHEET 4 AD 5 ARG A 239 LEU A 243 1 O ARG A 239 N VAL A 217
SHEET 5 AD 5 GLU A 271 ILE A 273 1 O GLU A 271 N MET A 242
SHEET 1 AE 3 ASN A 277 GLU A 283 0
SHEET 2 AE 3 VAL A 289 THR A 296 -1 N GLN A 290 O GLU A 282
SHEET 3 AE 3 GLY A 299 GLU A 304 -1 O GLY A 299 N THR A 296
SHEET 1 AF 5 ASP A 389 HIS A 392 0
SHEET 2 AF 5 GLU A 396 GLY A 401 -1 O VAL A 397 N LEU A 391
SHEET 3 AF 5 VAL A 464 GLY A 471 -1 O ALA A 467 N LEU A 400
SHEET 4 AF 5 PHE A 452 ASP A 458 -1 O PHE A 452 N VAL A 470
SHEET 5 AF 5 ILE A 414 MET A 419 -1 O VAL A 415 N ILE A 457
SHEET 1 BA 7 VAL B 3 ASN B 5 0
SHEET 2 BA 7 VAL B 32 ASN B 35 1 O VAL B 32 N TRP B 4
SHEET 3 BA 7 TYR B 152 LEU B 154 -1 O TYR B 152 N ASN B 35
SHEET 4 BA 7 GLN B 69 ASP B 73 1 O ILE B 71 N ILE B 153
SHEET 5 BA 7 ALA B 46 ILE B 49 1 O ALA B 46 N LEU B 70
SHEET 6 BA 7 LEU B 178 LEU B 180 1 O ILE B 179 N ILE B 49
SHEET 7 BA 7 VAL B 348 ALA B 350 1 O TYR B 349 N LEU B 180
SHEET 1 BB 3 LYS B 159 ASP B 162 0
SHEET 2 BB 3 THR B 165 ALA B 168 -1 O THR B 165 N ILE B 161
SHEET 3 BB 3 LYS B 171 LYS B 174 -1 O LYS B 171 N ALA B 168
SHEET 1 BC 2 ALA B 184 GLY B 185 0
SHEET 2 BC 2 GLN B 315 PRO B 316 -1 O GLN B 315 N GLY B 185
SHEET 1 BD 5 VAL B 199 PHE B 200 0
SHEET 2 BD 5 VAL B 308 LEU B 310 1 O VAL B 308 N PHE B 200
SHEET 3 BD 5 THR B 216 VAL B 220 1 O VAL B 218 N PHE B 309
SHEET 4 BD 5 ARG B 239 LEU B 243 1 O ARG B 239 N VAL B 217
SHEET 5 BD 5 GLU B 271 ILE B 273 1 O GLU B 271 N MET B 242
SHEET 1 BE 3 ASN B 277 GLU B 283 0
SHEET 2 BE 3 VAL B 289 THR B 296 -1 N GLN B 290 O GLU B 282
SHEET 3 BE 3 GLY B 299 GLU B 304 -1 O GLY B 299 N THR B 296
SHEET 1 BF 5 ASP B 389 HIS B 392 0
SHEET 2 BF 5 GLU B 396 GLY B 401 -1 O VAL B 397 N LEU B 391
SHEET 3 BF 5 VAL B 464 GLY B 471 -1 O ALA B 467 N LEU B 400
SHEET 4 BF 5 PHE B 452 ASP B 458 -1 O PHE B 452 N VAL B 470
SHEET 5 BF 5 ILE B 414 MET B 419 -1 O VAL B 415 N ILE B 457
SSBOND 1 CYS A 82 CYS A 87 1555 1555 2.27
SSBOND 2 CYS B 82 CYS B 87 1555 1555 2.21
CISPEP 1 GLY A 357 PRO A 358 0 -0.15
CISPEP 2 MET A 419 PRO A 420 0 -0.28
CISPEP 3 LEU A 431 PRO A 432 0 -0.79
CISPEP 4 PHE A 501 LEU A 502 0 -0.92
CISPEP 5 GLY B 357 PRO B 358 0 -0.02
CISPEP 6 MET B 419 PRO B 420 0 0.37
CISPEP 7 LEU B 431 PRO B 432 0 -0.96
CISPEP 8 PHE B 501 LEU B 502 0 -0.66
SITE 1 AC1 34 GLY A 50 GLY A 52 ALA A 53 ALA A 54
SITE 2 AC1 34 ASP A 73 ARG A 74 TRP A 75 GLY A 80
SITE 3 AC1 34 SER A 81 ALA A 86 CYS A 87 HIS A 90
SITE 4 AC1 34 HIS A 91 ALA A 158 ALA A 181 VAL A 182
SITE 5 AC1 34 HIS A 202 THR A 225 GLU A 314 GLY A 352
SITE 6 AC1 34 ASP A 353 MET A 359 GLU A 360 MET A 361
SITE 7 AC1 34 ALA A 364 PHE A 390 HOH A2080 HOH A2082
SITE 8 AC1 34 HOH A2141 HOH A2232 HOH A2323 HOH A2324
SITE 9 AC1 34 PHE B 501 HOH B2309
SITE 1 AC2 8 ARG A 56 PHE A 57 GLY A 79 MET A 140
SITE 2 AC2 8 MET A 361 ARG A 365 COM B1525 HOH B2328
SITE 1 AC3 9 MET A 419 LEU A 431 PHE A 501 HIS A 506
SITE 2 AC3 9 GLN A 509 HOH A2325 HOH A2326 MET B 140
SITE 3 AC3 9 COM B1526
SITE 1 AC4 34 PHE A 501 HOH A2313 GLY B 50 GLY B 52
SITE 2 AC4 34 ALA B 53 ALA B 54 ASP B 73 ARG B 74
SITE 3 AC4 34 TRP B 75 GLY B 80 SER B 81 ALA B 86
SITE 4 AC4 34 CYS B 87 HIS B 90 HIS B 91 ALA B 158
SITE 5 AC4 34 ALA B 181 VAL B 182 GLY B 183 HIS B 202
SITE 6 AC4 34 THR B 225 GLU B 314 GLY B 352 ASP B 353
SITE 7 AC4 34 MET B 359 GLU B 360 MET B 361 ALA B 364
SITE 8 AC4 34 PHE B 390 HOH B2038 HOH B2212 HOH B2218
SITE 9 AC4 34 HOH B2325 HOH B2326
SITE 1 AC5 9 MET A 140 COM A1525 MET B 419 LEU B 431
SITE 2 AC5 9 PHE B 501 HIS B 506 GLN B 509 HOH B2327
SITE 3 AC5 9 HOH B2328
SITE 1 AC6 7 COM A1526 HOH A2325 ARG B 56 PHE B 57
SITE 2 AC6 7 GLY B 79 MET B 361 ARG B 365
CRYST1 87.790 60.050 105.630 90.00 99.91 90.00 P 1 21 1 4
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 0.011391 0.000000 0.001990 0.00000
SCALE2 0.000000 0.016653 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009610 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
