HEADER OXIDOREDUCTASE 28-SEP-07 2VCY
TITLE CRYSTAL STRUCTURE OF 2-ENOYL THIOESTER REDUCTASE OF HUMAN FAS II
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANS-2-ENOYL-COA REDUCTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 31-373;
COMPND 5 SYNONYM: HSNRBF-1, NRBF-1;
COMPND 6 EC: 1.3.1.38;
COMPND 7 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: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET23
KEYWDS NADP, POLYMORPHISM, MITOCHONDRION, OXIDOREDUCTASE, FATTY ACID
KEYWDS 2 BIOSYNTHESIS, ENOYL THIOESTER REDUCTASE, LIPID SYNTHESIS, TRANSIT
KEYWDS 3 PEPTIDE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.M.HAAPALAINEN,R.PUDAS,O.S.SMART,R.K.WIERENGA
REVDAT 3 24-JUL-19 2VCY 1 REMARK
REVDAT 2 24-FEB-09 2VCY 1 VERSN
REVDAT 1 03-JUN-08 2VCY 0
JRNL AUTH Z.J.CHEN,R.PUDAS,S.SHARMA,O.S.SMART,A.H.JUFFER,J.K.HILTUNEN,
JRNL AUTH 2 R.K.WIERENGA,A.M.HAAPALAINEN
JRNL TITL STRUCTURAL ENZYMOLOGICAL STUDIES OF 2-ENOYL THIOESTER
JRNL TITL 2 REDUCTASE OF THE HUMAN MITOCHONDRIAL FAS II PATHWAY: NEW
JRNL TITL 3 INSIGHTS INTO ITS SUBSTRATE RECOGNITION PROPERTIES.
JRNL REF J.MOL.BIOL. V. 379 830 2008
JRNL REFN ISSN 0022-2836
JRNL PMID 18479707
JRNL DOI 10.1016/J.JMB.2008.04.041
REMARK 2
REMARK 2 RESOLUTION. 2.41 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT 2.1.1
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.41
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.79
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 84.4
REMARK 3 NUMBER OF REFLECTIONS : 27176
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) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1391
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL
REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5056
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 55
REMARK 3 SOLVENT ATOMS : 290
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : NULL ; NULL ; NULL
REMARK 3 BOND ANGLES : NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS : NULL ; NULL ; NULL
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : NULL ; NULL ; NULL
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : NULL ; NULL ; NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL
REMARK 3 OTHER TORSION ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESIDUES 31-41 ARE NOT PRESENT IN THE
REMARK 3 STRUCTURE
REMARK 4
REMARK 4 2VCY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-SEP-07.
REMARK 100 THE DEPOSITION ID IS D_1290031931.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-OCT-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9421
REMARK 200 MONOCHROMATOR : FIXED WITH DOUBLE CRYSTAL SI 111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32130
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.410
REMARK 200 RESOLUTION RANGE LOW (A) : 33.790
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 8.200
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.41
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.70
REMARK 200 R MERGE FOR SHELL (I) : 0.35000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1GUF
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULFATE, 100 MM TRIS HCL,
REMARK 280 PH 8.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 52.31000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 52.31000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 73.28000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 52.31000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 52.31000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 73.28000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 52.31000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 52.31000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 73.28000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 52.31000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 52.31000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 73.28000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 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: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 2550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.6 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 30
REMARK 465 ALA A 31
REMARK 465 SER A 32
REMARK 465 SER A 33
REMARK 465 TYR A 34
REMARK 465 SER A 35
REMARK 465 ALA A 36
REMARK 465 SER A 37
REMARK 465 ALA A 38
REMARK 465 GLU A 39
REMARK 465 PRO A 40
REMARK 465 ALA A 41
REMARK 465 MET B 30
REMARK 465 ALA B 31
REMARK 465 SER B 32
REMARK 465 SER B 33
REMARK 465 TYR B 34
REMARK 465 SER B 35
REMARK 465 ALA B 36
REMARK 465 SER B 37
REMARK 465 ALA B 38
REMARK 465 GLU B 39
REMARK 465 PRO B 40
REMARK 465 ALA B 41
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 PRO A 292 C - N - CA ANGL. DEV. = 11.7 DEGREES
REMARK 500 PRO A 292 C - N - CD ANGL. DEV. = -16.6 DEGREES
REMARK 500 PRO A 343 C - N - CD ANGL. DEV. = -20.2 DEGREES
REMARK 500 PRO B 130 C - N - CD ANGL. DEV. = -14.8 DEGREES
REMARK 500 PRO B 157 C - N - CA ANGL. DEV. = -9.6 DEGREES
REMARK 500 PRO B 292 C - N - CA ANGL. DEV. = 9.6 DEGREES
REMARK 500 PRO B 292 C - N - CD ANGL. DEV. = -16.7 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 ASN A 93 79.91 -107.57
REMARK 500 SER A 117 -37.79 -34.76
REMARK 500 VAL A 166 -81.34 -116.00
REMARK 500 ALA A 206 -6.80 -59.18
REMARK 500 MET A 247 -33.19 -143.16
REMARK 500 LYS A 252 -36.91 -134.37
REMARK 500 VAL A 264 -62.10 -99.34
REMARK 500 ALA A 344 116.85 -39.33
REMARK 500 ALA B 55 -4.33 -53.95
REMARK 500 VAL B 68 41.14 -69.06
REMARK 500 ARG B 69 96.55 -52.54
REMARK 500 SER B 117 -36.13 -34.28
REMARK 500 VAL B 166 -86.67 -116.31
REMARK 500 GLU B 246 67.58 -69.82
REMARK 500 MET B 247 -32.28 -140.52
REMARK 500 LYS B 252 -40.33 -140.70
REMARK 500 PRO B 292 171.31 -54.03
REMARK 500 LEU B 350 -28.27 -39.83
REMARK 500 ILE B 365 119.12 -39.35
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 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2064 DISTANCE = 6.87 ANGSTROMS
REMARK 525 HOH B2008 DISTANCE = 6.34 ANGSTROMS
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1374
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1375
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1376
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1377
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1378
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1374
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1375
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1376
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1377
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1378
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1379
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZSY RELATED DB: PDB
REMARK 900 THE STRUCTURE OF HUMAN MITOCHONDRIAL 2-ENOYL THIOESTERREDUCTASE
REMARK 900 (CGI-63)
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS CONSTRUCT DOES NOT CONTAIN MITOCHONDRIAL SIGNAL AND
REMARK 999 STARTS FROM RESIDUE ALA31.
DBREF 2VCY A 30 30 PDB 2VCY 2VCY 30 30
DBREF 2VCY A 31 373 UNP Q9BV79 MECR_HUMAN 31 373
DBREF 2VCY B 30 30 PDB 2VCY 2VCY 30 30
DBREF 2VCY B 31 373 UNP Q9BV79 MECR_HUMAN 31 373
SEQRES 1 A 344 MET ALA SER SER TYR SER ALA SER ALA GLU PRO ALA ARG
SEQRES 2 A 344 VAL ARG ALA LEU VAL TYR GLY HIS HIS GLY ASP PRO ALA
SEQRES 3 A 344 LYS VAL VAL GLU LEU LYS ASN LEU GLU LEU ALA ALA VAL
SEQRES 4 A 344 ARG GLY SER ASP VAL ARG VAL LYS MET LEU ALA ALA PRO
SEQRES 5 A 344 ILE ASN PRO SER ASP ILE ASN MET ILE GLN GLY ASN TYR
SEQRES 6 A 344 GLY LEU LEU PRO GLU LEU PRO ALA VAL GLY GLY ASN GLU
SEQRES 7 A 344 GLY VAL ALA GLN VAL VAL ALA VAL GLY SER ASN VAL THR
SEQRES 8 A 344 GLY LEU LYS PRO GLY ASP TRP VAL ILE PRO ALA ASN ALA
SEQRES 9 A 344 GLY LEU GLY THR TRP ARG THR GLU ALA VAL PHE SER GLU
SEQRES 10 A 344 GLU ALA LEU ILE GLN VAL PRO SER ASP ILE PRO LEU GLN
SEQRES 11 A 344 SER ALA ALA THR LEU GLY VAL ASN PRO CYS THR ALA TYR
SEQRES 12 A 344 ARG MET LEU MET ASP PHE GLU GLN LEU GLN PRO GLY ASP
SEQRES 13 A 344 SER VAL ILE GLN ASN ALA SER ASN SER GLY VAL GLY GLN
SEQRES 14 A 344 ALA VAL ILE GLN ILE ALA ALA ALA LEU GLY LEU ARG THR
SEQRES 15 A 344 ILE ASN VAL VAL ARG ASP ARG PRO ASP ILE GLN LYS LEU
SEQRES 16 A 344 SER ASP ARG LEU LYS SER LEU GLY ALA GLU HIS VAL ILE
SEQRES 17 A 344 THR GLU GLU GLU LEU ARG ARG PRO GLU MET LYS ASN PHE
SEQRES 18 A 344 PHE LYS ASP MET PRO GLN PRO ARG LEU ALA LEU ASN CYS
SEQRES 19 A 344 VAL GLY GLY LYS SER SER THR GLU LEU LEU ARG GLN LEU
SEQRES 20 A 344 ALA ARG GLY GLY THR MET VAL THR TYR GLY GLY MET ALA
SEQRES 21 A 344 LYS GLN PRO VAL VAL ALA SER VAL SER LEU LEU ILE PHE
SEQRES 22 A 344 LYS ASP LEU LYS LEU ARG GLY PHE TRP LEU SER GLN TRP
SEQRES 23 A 344 LYS LYS ASP HIS SER PRO ASP GLN PHE LYS GLU LEU ILE
SEQRES 24 A 344 LEU THR LEU CYS ASP LEU ILE ARG ARG GLY GLN LEU THR
SEQRES 25 A 344 ALA PRO ALA CYS SER GLN VAL PRO LEU GLN ASP TYR GLN
SEQRES 26 A 344 SER ALA LEU GLU ALA SER MET LYS PRO PHE ILE SER SER
SEQRES 27 A 344 LYS GLN ILE LEU THR MET
SEQRES 1 B 344 MET ALA SER SER TYR SER ALA SER ALA GLU PRO ALA ARG
SEQRES 2 B 344 VAL ARG ALA LEU VAL TYR GLY HIS HIS GLY ASP PRO ALA
SEQRES 3 B 344 LYS VAL VAL GLU LEU LYS ASN LEU GLU LEU ALA ALA VAL
SEQRES 4 B 344 ARG GLY SER ASP VAL ARG VAL LYS MET LEU ALA ALA PRO
SEQRES 5 B 344 ILE ASN PRO SER ASP ILE ASN MET ILE GLN GLY ASN TYR
SEQRES 6 B 344 GLY LEU LEU PRO GLU LEU PRO ALA VAL GLY GLY ASN GLU
SEQRES 7 B 344 GLY VAL ALA GLN VAL VAL ALA VAL GLY SER ASN VAL THR
SEQRES 8 B 344 GLY LEU LYS PRO GLY ASP TRP VAL ILE PRO ALA ASN ALA
SEQRES 9 B 344 GLY LEU GLY THR TRP ARG THR GLU ALA VAL PHE SER GLU
SEQRES 10 B 344 GLU ALA LEU ILE GLN VAL PRO SER ASP ILE PRO LEU GLN
SEQRES 11 B 344 SER ALA ALA THR LEU GLY VAL ASN PRO CYS THR ALA TYR
SEQRES 12 B 344 ARG MET LEU MET ASP PHE GLU GLN LEU GLN PRO GLY ASP
SEQRES 13 B 344 SER VAL ILE GLN ASN ALA SER ASN SER GLY VAL GLY GLN
SEQRES 14 B 344 ALA VAL ILE GLN ILE ALA ALA ALA LEU GLY LEU ARG THR
SEQRES 15 B 344 ILE ASN VAL VAL ARG ASP ARG PRO ASP ILE GLN LYS LEU
SEQRES 16 B 344 SER ASP ARG LEU LYS SER LEU GLY ALA GLU HIS VAL ILE
SEQRES 17 B 344 THR GLU GLU GLU LEU ARG ARG PRO GLU MET LYS ASN PHE
SEQRES 18 B 344 PHE LYS ASP MET PRO GLN PRO ARG LEU ALA LEU ASN CYS
SEQRES 19 B 344 VAL GLY GLY LYS SER SER THR GLU LEU LEU ARG GLN LEU
SEQRES 20 B 344 ALA ARG GLY GLY THR MET VAL THR TYR GLY GLY MET ALA
SEQRES 21 B 344 LYS GLN PRO VAL VAL ALA SER VAL SER LEU LEU ILE PHE
SEQRES 22 B 344 LYS ASP LEU LYS LEU ARG GLY PHE TRP LEU SER GLN TRP
SEQRES 23 B 344 LYS LYS ASP HIS SER PRO ASP GLN PHE LYS GLU LEU ILE
SEQRES 24 B 344 LEU THR LEU CYS ASP LEU ILE ARG ARG GLY GLN LEU THR
SEQRES 25 B 344 ALA PRO ALA CYS SER GLN VAL PRO LEU GLN ASP TYR GLN
SEQRES 26 B 344 SER ALA LEU GLU ALA SER MET LYS PRO PHE ILE SER SER
SEQRES 27 B 344 LYS GLN ILE LEU THR MET
HET SO4 A1374 5
HET SO4 A1375 5
HET SO4 A1376 5
HET SO4 A1377 5
HET SO4 A1378 5
HET SO4 B1374 5
HET SO4 B1375 5
HET SO4 B1376 5
HET SO4 B1377 5
HET SO4 B1378 5
HET SO4 B1379 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 11(O4 S 2-)
FORMUL 14 HOH *290(H2 O)
HELIX 1 1 ASP A 53 VAL A 58 1 6
HELIX 2 2 ASN A 83 GLY A 92 1 10
HELIX 3 3 PRO A 157 GLY A 165 1 9
HELIX 4 4 VAL A 166 ASP A 177 1 12
HELIX 5 5 SER A 194 ALA A 206 1 13
HELIX 6 6 ASP A 220 SER A 230 1 11
HELIX 7 7 GLU A 239 ARG A 243 1 5
HELIX 8 8 GLY A 265 LEU A 276 1 12
HELIX 9 9 SER A 296 LYS A 303 1 8
HELIX 10 10 TRP A 311 HIS A 319 1 9
HELIX 11 11 SER A 320 ARG A 337 1 18
HELIX 12 12 ASP A 352 LYS A 362 1 11
HELIX 13 13 ASP B 53 VAL B 57 1 5
HELIX 14 14 ASN B 83 GLY B 92 1 10
HELIX 15 15 PRO B 157 ALA B 162 1 6
HELIX 16 16 VAL B 166 PHE B 178 1 13
HELIX 17 17 SER B 194 LEU B 207 1 14
HELIX 18 18 ASP B 220 LEU B 231 1 12
HELIX 19 19 GLU B 239 ARG B 243 1 5
HELIX 20 20 GLY B 265 LEU B 276 1 12
HELIX 21 21 SER B 296 LYS B 303 1 8
HELIX 22 22 TRP B 311 ASP B 318 1 8
HELIX 23 23 SER B 320 ARG B 337 1 18
HELIX 24 24 ASP B 352 MET B 361 1 10
SHEET 1 AA 3 GLU A 59 LEU A 63 0
SHEET 2 AA 3 VAL A 43 TYR A 48 -1 O VAL A 43 N LEU A 63
SHEET 3 AA 3 ALA A 102 VAL A 103 -1 O ALA A 102 N TYR A 48
SHEET 1 AB 5 GLU A 141 SER A 145 0
SHEET 2 AB 5 ASP A 72 PRO A 81 -1 O VAL A 73 N PHE A 144
SHEET 3 AB 5 VAL A 109 VAL A 115 -1 O VAL A 109 N LEU A 78
SHEET 4 AB 5 TRP A 127 PRO A 130 -1 O VAL A 128 N ALA A 110
SHEET 5 AB 5 LEU A 149 VAL A 152 -1 O ILE A 150 N ILE A 129
SHEET 1 AC 4 GLU A 141 SER A 145 0
SHEET 2 AC 4 ASP A 72 PRO A 81 -1 O VAL A 73 N PHE A 144
SHEET 3 AC 4 LYS A 368 THR A 372 -1 O LEU A 371 N ALA A 80
SHEET 4 AC 4 CYS A 345 PRO A 349 1 O SER A 346 N ILE A 370
SHEET 1 AD 6 HIS A 235 THR A 238 0
SHEET 2 AD 6 ARG A 210 VAL A 215 1 O THR A 211 N HIS A 235
SHEET 3 AD 6 SER A 186 GLN A 189 1 O VAL A 187 N ILE A 212
SHEET 4 AD 6 LEU A 259 ASN A 262 1 O LEU A 259 N ILE A 188
SHEET 5 AD 6 THR A 281 THR A 284 1 O THR A 281 N ALA A 260
SHEET 6 AD 6 LYS A 306 GLY A 309 1 O LYS A 306 N MET A 282
SHEET 1 AE 2 VAL A 293 ALA A 295 0
SHEET 2 AE 2 VAL B 293 ALA B 295 -1 O VAL B 293 N ALA A 295
SHEET 1 BA 3 VAL B 58 LEU B 63 0
SHEET 2 BA 3 VAL B 43 TYR B 48 -1 O VAL B 43 N LEU B 63
SHEET 3 BA 3 ALA B 102 VAL B 103 -1 O ALA B 102 N TYR B 48
SHEET 1 BB 5 GLU B 141 SER B 145 0
SHEET 2 BB 5 ASP B 72 PRO B 81 -1 O VAL B 73 N PHE B 144
SHEET 3 BB 5 VAL B 109 VAL B 115 -1 O VAL B 109 N LEU B 78
SHEET 4 BB 5 TRP B 127 PRO B 130 -1 O VAL B 128 N ALA B 110
SHEET 5 BB 5 LEU B 149 GLN B 151 -1 O ILE B 150 N ILE B 129
SHEET 1 BC 4 GLU B 141 SER B 145 0
SHEET 2 BC 4 ASP B 72 PRO B 81 -1 O VAL B 73 N PHE B 144
SHEET 3 BC 4 LYS B 368 THR B 372 -1 O LEU B 371 N ALA B 80
SHEET 4 BC 4 CYS B 345 PRO B 349 1 O SER B 346 N ILE B 370
SHEET 1 BD 6 HIS B 235 THR B 238 0
SHEET 2 BD 6 ARG B 210 VAL B 215 1 O THR B 211 N HIS B 235
SHEET 3 BD 6 SER B 186 ASN B 190 1 O VAL B 187 N ILE B 212
SHEET 4 BD 6 LEU B 259 ASN B 262 1 O LEU B 259 N ILE B 188
SHEET 5 BD 6 THR B 281 THR B 284 1 O THR B 281 N ALA B 260
SHEET 6 BD 6 LYS B 306 GLY B 309 1 O LYS B 306 N MET B 282
CISPEP 1 LEU A 100 PRO A 101 0 -0.23
CISPEP 2 LEU B 100 PRO B 101 0 -1.31
SITE 1 AC1 4 GLN A 256 HOH A2147 HOH A2148 HOH A2149
SITE 1 AC2 3 ARG A 308 HOH A2069 HOH B2100
SITE 1 AC3 4 ARG A 139 HOH A2047 HOH A2150 HOH A2151
SITE 1 AC4 4 ASN A 167 SER A 194 GLY A 195 LYS A 368
SITE 1 AC5 6 ALA A 191 SER A 192 ASN A 193 VAL A 215
SITE 2 AC5 6 ARG A 216 ARG A 218
SITE 1 AC6 5 ARG A 69 PRO B 255 GLN B 256 HOH B2087
SITE 2 AC6 5 HOH B2133
SITE 1 AC7 5 LYS A 306 ARG B 308 HOH B2061 HOH B2134
SITE 2 AC7 5 HOH B2136
SITE 1 AC8 3 VAL B 103 ARG B 139 HOH B2043
SITE 1 AC9 3 ALA A 289 ARG B 274 SER B 296
SITE 1 BC1 6 PRO B 84 ASN B 167 SER B 194 GLY B 195
SITE 2 BC1 6 VAL B 196 LYS B 368
SITE 1 BC2 7 ALA B 191 SER B 192 ASN B 193 SER B 194
SITE 2 BC2 7 VAL B 215 ARG B 216 ARG B 218
CRYST1 104.620 104.620 146.560 90.00 90.00 90.00 P 42 21 2 16
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 0.009558 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009558 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006823 0.00000
MTRIX1 1 -0.147500 0.980190 0.132210 -53.60578 1
MTRIX2 1 0.986730 0.136660 0.087720 47.96128 1
MTRIX3 1 0.067910 0.143400 -0.987330 -12.56546 1
MTRIX1 2 -0.147500 0.986730 0.067910 -54.37840 1
MTRIX2 2 0.980190 0.136660 0.143400 47.79124 1
MTRIX3 2 0.132210 0.087720 -0.987330 -9.52591 1
(ATOM LINES ARE NOT SHOWN.)
END
