HEADER LYASE 26-AUG-02 1MJ3
TITLE CRYSTAL STRUCTURE ANALYSIS OF RAT ENOYL-COA HYDRATASE IN COMPLEX WITH
TITLE 2 HEXADIENOYL-COA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENOYL-COA HYDRATASE, MITOCHONDRIAL;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: SHORT CHAIN ENOYL-COA HYDRATASE, ENOYL-COA HYDRATASE 1,
COMPND 5 SCEH;
COMPND 6 EC: 4.2.1.17;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HOMOHEXAMER, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.F.BELL,Y.FENG,H.A.HOFSTEIN,S.PARIKH,J.WU,M.J.RUDOLPH,C.KISKER,
AUTHOR 2 P.J.TONGE
REVDAT 4 14-FEB-24 1MJ3 1 REMARK
REVDAT 3 24-FEB-09 1MJ3 1 VERSN
REVDAT 2 18-DEC-02 1MJ3 1 JRNL REMARK
REVDAT 1 24-SEP-02 1MJ3 0
JRNL AUTH A.F.BELL,Y.FENG,H.A.HOFSTEIN,S.PARIKH,J.WU,M.J.RUDOLPH,
JRNL AUTH 2 C.KISKER,A.WHITTY,P.J.TONGE
JRNL TITL STEREOSELECTIVITY OF ENOYL-COA HYDRATASE RESULTS FROM
JRNL TITL 2 PREFERENTIAL ACTIVATION OF ONE OF TWO BOUND SUBSTRATE
JRNL TITL 3 CONFORMERS
JRNL REF CHEM.BIOL. V. 9 1247 2002
JRNL REFN ISSN 1074-5521
JRNL PMID 12445775
JRNL DOI 10.1016/S1074-5521(02)00263-6
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.2
REMARK 3 NUMBER OF REFLECTIONS : 92256
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) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4801
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5820
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2220
REMARK 3 BIN FREE R VALUE SET COUNT : 322
REMARK 3 BIN FREE R VALUE : 0.3060
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11730
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 275
REMARK 3 SOLVENT ATOMS : 919
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.33000
REMARK 3 B22 (A**2) : 0.48000
REMARK 3 B33 (A**2) : -0.15000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.215
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.190
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.125
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.801
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12160 ; 0.033 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 16355 ; 2.593 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1536 ; 6.182 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1857 ; 0.182 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8882 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 5768 ; 0.246 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 908 ; 0.175 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 127 ; 0.493 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 33 ; 0.491 ; 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): 7632 ; 2.925 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12126 ; 4.588 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4528 ; 7.872 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4229 ;12.394 ; 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 : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 1MJ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-AUG-02.
REMARK 100 THE DEPOSITION ID IS D_1000016947.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAR-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X26C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : PLATINUM
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 96809
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: FFT
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, DTT, EDTA, N
REMARK 280 -OCTANOL, MES, PH 6.5, VAPOR DIFFUSION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 38.43850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 124.71450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.59900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 124.71450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.43850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.59900
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HOMOHEXAMER WHICH IS FOUND IN
REMARK 300 THE ASYMETRIC UNIT
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 39140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 53170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -236.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 LYS A 115
REMARK 465 PHE A 116
REMARK 465 LYS B 115
REMARK 465 PHE B 116
REMARK 465 LYS C 115
REMARK 465 PHE C 116
REMARK 465 LYS D 115
REMARK 465 PHE D 116
REMARK 465 LYS E 115
REMARK 465 PHE E 116
REMARK 465 LYS F 115
REMARK 465 PHE F 116
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 ASN A 32 CG OD1 ND2
REMARK 470 ASN B 32 CG OD1 ND2
REMARK 470 ASN C 32 CG OD1 ND2
REMARK 470 ASN D 32 CG OD1 ND2
REMARK 470 ASN E 32 CG OD1 ND2
REMARK 470 ASN F 32 CG OD1 ND2
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 O33 HXC C 953 O HOH C 986 0.84
REMARK 500 P3 HXC C 953 O HOH C 986 1.22
REMARK 500 N CYS D 62 O HOH D 386 1.70
REMARK 500 C ALA D 96 O HOH D 400 1.81
REMARK 500 C LEU D 61 O HOH D 386 1.85
REMARK 500 N GLY A 114 O HOH A 1109 1.91
REMARK 500 NE ARG D 272 O HOH D 347 1.93
REMARK 500 OG SER A 113 O HOH A 1109 1.97
REMARK 500 O32 HXC C 953 O HOH C 986 1.99
REMARK 500 NE ARG A 272 O HOH A 1045 2.03
REMARK 500 CB SER D 118 O HOH D 370 2.04
REMARK 500 O HOH E 1032 O HOH E 1088 2.15
REMARK 500 CB ALA D 96 O HOH D 400 2.16
REMARK 500 O ALA D 96 O HOH D 400 2.16
REMARK 500 ND2 ASN D 286 O HOH D 373 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 O GLY D 42 NZ LYS E 282 4466 1.45
REMARK 500 OE1 GLU B 227 NZ LYS F 288 3756 1.79
REMARK 500 O GLY D 42 CE LYS E 282 4466 1.86
REMARK 500 N SER D 45 NZ LYS E 282 4466 1.94
REMARK 500 OD1 ASN C 44 O LYS C 56 4576 2.19
REMARK 500 NZ LYS B 234 OD1 ASN F 44 3756 2.19
REMARK 500 NZ LYS B 288 OE1 GLU F 227 3756 2.19
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 111 CB CYS A 111 SG -0.173
REMARK 500 MET A 250 SD MET A 250 CE -0.342
REMARK 500 GLU A 254 CD GLU A 254 OE1 0.072
REMARK 500 TYR A 264 CD1 TYR A 264 CE1 0.098
REMARK 500 TYR A 264 CE2 TYR A 264 CD2 0.115
REMARK 500 ARG A 272 CZ ARG A 272 NH1 0.093
REMARK 500 VAL A 280 CB VAL A 280 CG1 0.135
REMARK 500 ARG B 272 CZ ARG B 272 NH1 0.194
REMARK 500 PHE B 287 CE1 PHE B 287 CZ 0.240
REMARK 500 LYS B 288 CE LYS B 288 NZ 0.173
REMARK 500 GLU C 68 CD GLU C 68 OE2 0.066
REMARK 500 CYS C 225 CB CYS C 225 SG 0.117
REMARK 500 ALA C 226 CA ALA C 226 CB -0.134
REMARK 500 VAL C 237 CB VAL C 237 CG1 0.131
REMARK 500 MET C 250 CB MET C 250 CG -0.202
REMARK 500 GLU C 254 CD GLU C 254 OE2 0.066
REMARK 500 ARG C 272 CZ ARG C 272 NH1 0.099
REMARK 500 SER D 46 CA SER D 46 CB -0.093
REMARK 500 ARG D 272 NE ARG D 272 CZ 0.094
REMARK 500 ARG D 272 CZ ARG D 272 NH1 0.128
REMARK 500 ALA E 95 CA ALA E 95 CB -0.130
REMARK 500 VAL E 237 CB VAL E 237 CG2 0.158
REMARK 500 ARG E 272 CZ ARG E 272 NH1 0.194
REMARK 500 LYS F 241 CD LYS F 241 CE 0.154
REMARK 500 ARG F 272 CZ ARG F 272 NH1 0.110
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 ASP A 99 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 196 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG A 197 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG A 197 NE - CZ - NH2 ANGL. DEV. = -8.5 DEGREES
REMARK 500 ASP A 271 CB - CG - OD2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG A 272 CG - CD - NE ANGL. DEV. = 17.4 DEGREES
REMARK 500 ARG A 272 CD - NE - CZ ANGL. DEV. = 9.5 DEGREES
REMARK 500 ARG A 272 NE - CZ - NH1 ANGL. DEV. = 10.0 DEGREES
REMARK 500 ARG A 272 NE - CZ - NH2 ANGL. DEV. = -9.5 DEGREES
REMARK 500 ARG B 54 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG B 197 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ASP B 271 CB - CG - OD2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ARG B 272 CG - CD - NE ANGL. DEV. = 12.9 DEGREES
REMARK 500 ARG B 272 CD - NE - CZ ANGL. DEV. = 11.5 DEGREES
REMARK 500 ARG B 272 NE - CZ - NH1 ANGL. DEV. = 12.5 DEGREES
REMARK 500 ARG B 272 NE - CZ - NH2 ANGL. DEV. = -15.4 DEGREES
REMARK 500 ARG B 283 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASP C 150 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG C 197 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 MET C 250 CG - SD - CE ANGL. DEV. = -13.2 DEGREES
REMARK 500 ASP C 271 CB - CG - OD2 ANGL. DEV. = 9.0 DEGREES
REMARK 500 ARG C 272 CG - CD - NE ANGL. DEV. = 17.1 DEGREES
REMARK 500 ARG C 272 CD - NE - CZ ANGL. DEV. = 9.9 DEGREES
REMARK 500 ARG C 272 NE - CZ - NH1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG C 272 NE - CZ - NH2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 ARG D 54 NE - CZ - NH1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 LEU D 65 CA - CB - CG ANGL. DEV. = 16.4 DEGREES
REMARK 500 ALA D 96 O - C - N ANGL. DEV. = -11.0 DEGREES
REMARK 500 GLY D 97 C - N - CA ANGL. DEV. = -15.2 DEGREES
REMARK 500 ALA D 98 N - CA - C ANGL. DEV. = -17.6 DEGREES
REMARK 500 ASP D 150 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG D 197 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 MET D 250 CG - SD - CE ANGL. DEV. = -13.5 DEGREES
REMARK 500 ASP D 270 CB - CG - OD2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 ARG D 272 CG - CD - NE ANGL. DEV. = 17.7 DEGREES
REMARK 500 ARG D 272 CD - NE - CZ ANGL. DEV. = 15.6 DEGREES
REMARK 500 ARG D 272 NE - CZ - NH1 ANGL. DEV. = 12.5 DEGREES
REMARK 500 ARG D 272 NE - CZ - NH2 ANGL. DEV. = -11.9 DEGREES
REMARK 500 ARG D 283 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 HIS E 119 CG - ND1 - CE1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP E 150 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP E 196 CB - CG - OD1 ANGL. DEV. = 8.2 DEGREES
REMARK 500 ARG E 197 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG E 197 NE - CZ - NH2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 ARG E 272 CG - CD - NE ANGL. DEV. = 17.9 DEGREES
REMARK 500 ARG E 272 CD - NE - CZ ANGL. DEV. = 14.2 DEGREES
REMARK 500 ARG E 272 NE - CZ - NH1 ANGL. DEV. = 12.8 DEGREES
REMARK 500 ARG E 272 NE - CZ - NH2 ANGL. DEV. = -17.7 DEGREES
REMARK 500 ASP E 289 CB - CG - OD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 HIS E 290 CA - C - O ANGL. DEV. = -15.2 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 61 ANGLE DEVIATIONS.
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 ALA A 95 135.53 -174.53
REMARK 500 TYR A 112 -85.02 -59.90
REMARK 500 SER A 118 -43.72 -144.96
REMARK 500 ARG B 54 57.70 -144.19
REMARK 500 LEU B 58 42.45 38.59
REMARK 500 ALA B 95 133.94 -172.74
REMARK 500 LYS C 43 114.80 -33.26
REMARK 500 ARG C 54 56.64 -141.67
REMARK 500 ALA C 95 132.46 -175.92
REMARK 500 ALA C 173 46.60 -142.34
REMARK 500 ASP C 289 33.54 76.17
REMARK 500 ARG D 54 58.30 -140.64
REMARK 500 LEU D 58 42.62 36.50
REMARK 500 LEU D 61 97.28 -69.67
REMARK 500 ALA D 95 115.55 -173.60
REMARK 500 LYS D 282 43.47 34.60
REMARK 500 ASP D 289 34.22 71.11
REMARK 500 TYR E 112 -72.93 -82.83
REMARK 500 ASP E 289 39.55 70.26
REMARK 500 ALA F 173 43.81 -141.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU C 117 SER C 118 -149.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HXC A 951
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HXC B 952
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HXC C 953
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HXC E 954
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HXC F 955
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DUB RELATED DB: PDB
REMARK 900 2-ENOYL-COA HYDRATASE, DATA COLLECTED AT 100 K, PH 6.5
REMARK 900 RELATED ID: 2DUB RELATED DB: PDB
REMARK 900 ENOYL-COA HYDRATASE COMPLEXED WITH OCTANOYL-COA
REMARK 900 RELATED ID: 1EY3 RELATED DB: PDB
REMARK 900 STRUCTURE OF ENOYL-COA HYDRATASE COMPLEXED WITH THE SUBSTRATE DAC-
REMARK 900 COA
DBREF 1MJ3 A 31 290 UNP P14604 ECHM_RAT 31 290
DBREF 1MJ3 B 31 290 UNP P14604 ECHM_RAT 31 290
DBREF 1MJ3 C 31 290 UNP P14604 ECHM_RAT 31 290
DBREF 1MJ3 D 31 290 UNP P14604 ECHM_RAT 31 290
DBREF 1MJ3 E 31 290 UNP P14604 ECHM_RAT 31 290
DBREF 1MJ3 F 31 290 UNP P14604 ECHM_RAT 31 290
SEQRES 1 A 260 ALA ASN PHE GLN TYR ILE ILE THR GLU LYS LYS GLY LYS
SEQRES 2 A 260 ASN SER SER VAL GLY LEU ILE GLN LEU ASN ARG PRO LYS
SEQRES 3 A 260 ALA LEU ASN ALA LEU CYS ASN GLY LEU ILE GLU GLU LEU
SEQRES 4 A 260 ASN GLN ALA LEU GLU THR PHE GLU GLU ASP PRO ALA VAL
SEQRES 5 A 260 GLY ALA ILE VAL LEU THR GLY GLY GLU LYS ALA PHE ALA
SEQRES 6 A 260 ALA GLY ALA ASP ILE LYS GLU MET GLN ASN ARG THR PHE
SEQRES 7 A 260 GLN ASP CYS TYR SER GLY LYS PHE LEU SER HIS TRP ASP
SEQRES 8 A 260 HIS ILE THR ARG ILE LYS LYS PRO VAL ILE ALA ALA VAL
SEQRES 9 A 260 ASN GLY TYR ALA LEU GLY GLY GLY CYS GLU LEU ALA MET
SEQRES 10 A 260 MET CYS ASP ILE ILE TYR ALA GLY GLU LYS ALA GLN PHE
SEQRES 11 A 260 GLY GLN PRO GLU ILE LEU LEU GLY THR ILE PRO GLY ALA
SEQRES 12 A 260 GLY GLY THR GLN ARG LEU THR ARG ALA VAL GLY LYS SER
SEQRES 13 A 260 LEU ALA MET GLU MET VAL LEU THR GLY ASP ARG ILE SER
SEQRES 14 A 260 ALA GLN ASP ALA LYS GLN ALA GLY LEU VAL SER LYS ILE
SEQRES 15 A 260 PHE PRO VAL GLU THR LEU VAL GLU GLU ALA ILE GLN CYS
SEQRES 16 A 260 ALA GLU LYS ILE ALA ASN ASN SER LYS ILE ILE VAL ALA
SEQRES 17 A 260 MET ALA LYS GLU SER VAL ASN ALA ALA PHE GLU MET THR
SEQRES 18 A 260 LEU THR GLU GLY ASN LYS LEU GLU LYS LYS LEU PHE TYR
SEQRES 19 A 260 SER THR PHE ALA THR ASP ASP ARG ARG GLU GLY MET SER
SEQRES 20 A 260 ALA PHE VAL GLU LYS ARG LYS ALA ASN PHE LYS ASP HIS
SEQRES 1 B 260 ALA ASN PHE GLN TYR ILE ILE THR GLU LYS LYS GLY LYS
SEQRES 2 B 260 ASN SER SER VAL GLY LEU ILE GLN LEU ASN ARG PRO LYS
SEQRES 3 B 260 ALA LEU ASN ALA LEU CYS ASN GLY LEU ILE GLU GLU LEU
SEQRES 4 B 260 ASN GLN ALA LEU GLU THR PHE GLU GLU ASP PRO ALA VAL
SEQRES 5 B 260 GLY ALA ILE VAL LEU THR GLY GLY GLU LYS ALA PHE ALA
SEQRES 6 B 260 ALA GLY ALA ASP ILE LYS GLU MET GLN ASN ARG THR PHE
SEQRES 7 B 260 GLN ASP CYS TYR SER GLY LYS PHE LEU SER HIS TRP ASP
SEQRES 8 B 260 HIS ILE THR ARG ILE LYS LYS PRO VAL ILE ALA ALA VAL
SEQRES 9 B 260 ASN GLY TYR ALA LEU GLY GLY GLY CYS GLU LEU ALA MET
SEQRES 10 B 260 MET CYS ASP ILE ILE TYR ALA GLY GLU LYS ALA GLN PHE
SEQRES 11 B 260 GLY GLN PRO GLU ILE LEU LEU GLY THR ILE PRO GLY ALA
SEQRES 12 B 260 GLY GLY THR GLN ARG LEU THR ARG ALA VAL GLY LYS SER
SEQRES 13 B 260 LEU ALA MET GLU MET VAL LEU THR GLY ASP ARG ILE SER
SEQRES 14 B 260 ALA GLN ASP ALA LYS GLN ALA GLY LEU VAL SER LYS ILE
SEQRES 15 B 260 PHE PRO VAL GLU THR LEU VAL GLU GLU ALA ILE GLN CYS
SEQRES 16 B 260 ALA GLU LYS ILE ALA ASN ASN SER LYS ILE ILE VAL ALA
SEQRES 17 B 260 MET ALA LYS GLU SER VAL ASN ALA ALA PHE GLU MET THR
SEQRES 18 B 260 LEU THR GLU GLY ASN LYS LEU GLU LYS LYS LEU PHE TYR
SEQRES 19 B 260 SER THR PHE ALA THR ASP ASP ARG ARG GLU GLY MET SER
SEQRES 20 B 260 ALA PHE VAL GLU LYS ARG LYS ALA ASN PHE LYS ASP HIS
SEQRES 1 C 260 ALA ASN PHE GLN TYR ILE ILE THR GLU LYS LYS GLY LYS
SEQRES 2 C 260 ASN SER SER VAL GLY LEU ILE GLN LEU ASN ARG PRO LYS
SEQRES 3 C 260 ALA LEU ASN ALA LEU CYS ASN GLY LEU ILE GLU GLU LEU
SEQRES 4 C 260 ASN GLN ALA LEU GLU THR PHE GLU GLU ASP PRO ALA VAL
SEQRES 5 C 260 GLY ALA ILE VAL LEU THR GLY GLY GLU LYS ALA PHE ALA
SEQRES 6 C 260 ALA GLY ALA ASP ILE LYS GLU MET GLN ASN ARG THR PHE
SEQRES 7 C 260 GLN ASP CYS TYR SER GLY LYS PHE LEU SER HIS TRP ASP
SEQRES 8 C 260 HIS ILE THR ARG ILE LYS LYS PRO VAL ILE ALA ALA VAL
SEQRES 9 C 260 ASN GLY TYR ALA LEU GLY GLY GLY CYS GLU LEU ALA MET
SEQRES 10 C 260 MET CYS ASP ILE ILE TYR ALA GLY GLU LYS ALA GLN PHE
SEQRES 11 C 260 GLY GLN PRO GLU ILE LEU LEU GLY THR ILE PRO GLY ALA
SEQRES 12 C 260 GLY GLY THR GLN ARG LEU THR ARG ALA VAL GLY LYS SER
SEQRES 13 C 260 LEU ALA MET GLU MET VAL LEU THR GLY ASP ARG ILE SER
SEQRES 14 C 260 ALA GLN ASP ALA LYS GLN ALA GLY LEU VAL SER LYS ILE
SEQRES 15 C 260 PHE PRO VAL GLU THR LEU VAL GLU GLU ALA ILE GLN CYS
SEQRES 16 C 260 ALA GLU LYS ILE ALA ASN ASN SER LYS ILE ILE VAL ALA
SEQRES 17 C 260 MET ALA LYS GLU SER VAL ASN ALA ALA PHE GLU MET THR
SEQRES 18 C 260 LEU THR GLU GLY ASN LYS LEU GLU LYS LYS LEU PHE TYR
SEQRES 19 C 260 SER THR PHE ALA THR ASP ASP ARG ARG GLU GLY MET SER
SEQRES 20 C 260 ALA PHE VAL GLU LYS ARG LYS ALA ASN PHE LYS ASP HIS
SEQRES 1 D 260 ALA ASN PHE GLN TYR ILE ILE THR GLU LYS LYS GLY LYS
SEQRES 2 D 260 ASN SER SER VAL GLY LEU ILE GLN LEU ASN ARG PRO LYS
SEQRES 3 D 260 ALA LEU ASN ALA LEU CYS ASN GLY LEU ILE GLU GLU LEU
SEQRES 4 D 260 ASN GLN ALA LEU GLU THR PHE GLU GLU ASP PRO ALA VAL
SEQRES 5 D 260 GLY ALA ILE VAL LEU THR GLY GLY GLU LYS ALA PHE ALA
SEQRES 6 D 260 ALA GLY ALA ASP ILE LYS GLU MET GLN ASN ARG THR PHE
SEQRES 7 D 260 GLN ASP CYS TYR SER GLY LYS PHE LEU SER HIS TRP ASP
SEQRES 8 D 260 HIS ILE THR ARG ILE LYS LYS PRO VAL ILE ALA ALA VAL
SEQRES 9 D 260 ASN GLY TYR ALA LEU GLY GLY GLY CYS GLU LEU ALA MET
SEQRES 10 D 260 MET CYS ASP ILE ILE TYR ALA GLY GLU LYS ALA GLN PHE
SEQRES 11 D 260 GLY GLN PRO GLU ILE LEU LEU GLY THR ILE PRO GLY ALA
SEQRES 12 D 260 GLY GLY THR GLN ARG LEU THR ARG ALA VAL GLY LYS SER
SEQRES 13 D 260 LEU ALA MET GLU MET VAL LEU THR GLY ASP ARG ILE SER
SEQRES 14 D 260 ALA GLN ASP ALA LYS GLN ALA GLY LEU VAL SER LYS ILE
SEQRES 15 D 260 PHE PRO VAL GLU THR LEU VAL GLU GLU ALA ILE GLN CYS
SEQRES 16 D 260 ALA GLU LYS ILE ALA ASN ASN SER LYS ILE ILE VAL ALA
SEQRES 17 D 260 MET ALA LYS GLU SER VAL ASN ALA ALA PHE GLU MET THR
SEQRES 18 D 260 LEU THR GLU GLY ASN LYS LEU GLU LYS LYS LEU PHE TYR
SEQRES 19 D 260 SER THR PHE ALA THR ASP ASP ARG ARG GLU GLY MET SER
SEQRES 20 D 260 ALA PHE VAL GLU LYS ARG LYS ALA ASN PHE LYS ASP HIS
SEQRES 1 E 260 ALA ASN PHE GLN TYR ILE ILE THR GLU LYS LYS GLY LYS
SEQRES 2 E 260 ASN SER SER VAL GLY LEU ILE GLN LEU ASN ARG PRO LYS
SEQRES 3 E 260 ALA LEU ASN ALA LEU CYS ASN GLY LEU ILE GLU GLU LEU
SEQRES 4 E 260 ASN GLN ALA LEU GLU THR PHE GLU GLU ASP PRO ALA VAL
SEQRES 5 E 260 GLY ALA ILE VAL LEU THR GLY GLY GLU LYS ALA PHE ALA
SEQRES 6 E 260 ALA GLY ALA ASP ILE LYS GLU MET GLN ASN ARG THR PHE
SEQRES 7 E 260 GLN ASP CYS TYR SER GLY LYS PHE LEU SER HIS TRP ASP
SEQRES 8 E 260 HIS ILE THR ARG ILE LYS LYS PRO VAL ILE ALA ALA VAL
SEQRES 9 E 260 ASN GLY TYR ALA LEU GLY GLY GLY CYS GLU LEU ALA MET
SEQRES 10 E 260 MET CYS ASP ILE ILE TYR ALA GLY GLU LYS ALA GLN PHE
SEQRES 11 E 260 GLY GLN PRO GLU ILE LEU LEU GLY THR ILE PRO GLY ALA
SEQRES 12 E 260 GLY GLY THR GLN ARG LEU THR ARG ALA VAL GLY LYS SER
SEQRES 13 E 260 LEU ALA MET GLU MET VAL LEU THR GLY ASP ARG ILE SER
SEQRES 14 E 260 ALA GLN ASP ALA LYS GLN ALA GLY LEU VAL SER LYS ILE
SEQRES 15 E 260 PHE PRO VAL GLU THR LEU VAL GLU GLU ALA ILE GLN CYS
SEQRES 16 E 260 ALA GLU LYS ILE ALA ASN ASN SER LYS ILE ILE VAL ALA
SEQRES 17 E 260 MET ALA LYS GLU SER VAL ASN ALA ALA PHE GLU MET THR
SEQRES 18 E 260 LEU THR GLU GLY ASN LYS LEU GLU LYS LYS LEU PHE TYR
SEQRES 19 E 260 SER THR PHE ALA THR ASP ASP ARG ARG GLU GLY MET SER
SEQRES 20 E 260 ALA PHE VAL GLU LYS ARG LYS ALA ASN PHE LYS ASP HIS
SEQRES 1 F 260 ALA ASN PHE GLN TYR ILE ILE THR GLU LYS LYS GLY LYS
SEQRES 2 F 260 ASN SER SER VAL GLY LEU ILE GLN LEU ASN ARG PRO LYS
SEQRES 3 F 260 ALA LEU ASN ALA LEU CYS ASN GLY LEU ILE GLU GLU LEU
SEQRES 4 F 260 ASN GLN ALA LEU GLU THR PHE GLU GLU ASP PRO ALA VAL
SEQRES 5 F 260 GLY ALA ILE VAL LEU THR GLY GLY GLU LYS ALA PHE ALA
SEQRES 6 F 260 ALA GLY ALA ASP ILE LYS GLU MET GLN ASN ARG THR PHE
SEQRES 7 F 260 GLN ASP CYS TYR SER GLY LYS PHE LEU SER HIS TRP ASP
SEQRES 8 F 260 HIS ILE THR ARG ILE LYS LYS PRO VAL ILE ALA ALA VAL
SEQRES 9 F 260 ASN GLY TYR ALA LEU GLY GLY GLY CYS GLU LEU ALA MET
SEQRES 10 F 260 MET CYS ASP ILE ILE TYR ALA GLY GLU LYS ALA GLN PHE
SEQRES 11 F 260 GLY GLN PRO GLU ILE LEU LEU GLY THR ILE PRO GLY ALA
SEQRES 12 F 260 GLY GLY THR GLN ARG LEU THR ARG ALA VAL GLY LYS SER
SEQRES 13 F 260 LEU ALA MET GLU MET VAL LEU THR GLY ASP ARG ILE SER
SEQRES 14 F 260 ALA GLN ASP ALA LYS GLN ALA GLY LEU VAL SER LYS ILE
SEQRES 15 F 260 PHE PRO VAL GLU THR LEU VAL GLU GLU ALA ILE GLN CYS
SEQRES 16 F 260 ALA GLU LYS ILE ALA ASN ASN SER LYS ILE ILE VAL ALA
SEQRES 17 F 260 MET ALA LYS GLU SER VAL ASN ALA ALA PHE GLU MET THR
SEQRES 18 F 260 LEU THR GLU GLY ASN LYS LEU GLU LYS LYS LEU PHE TYR
SEQRES 19 F 260 SER THR PHE ALA THR ASP ASP ARG ARG GLU GLY MET SER
SEQRES 20 F 260 ALA PHE VAL GLU LYS ARG LYS ALA ASN PHE LYS ASP HIS
HET HXC A 951 55
HET HXC B 952 55
HET HXC C 953 55
HET HXC E 954 55
HET HXC F 955 55
HETNAM HXC HEXANOYL-COENZYME A
FORMUL 7 HXC 5(C27 H46 N7 O17 P3 S)
FORMUL 12 HOH *919(H2 O)
HELIX 1 1 GLY A 42 SER A 45 5 4
HELIX 2 2 ARG A 54 LEU A 58 5 5
HELIX 3 3 CYS A 62 ASP A 79 1 18
HELIX 4 4 ASP A 99 GLN A 104 1 6
HELIX 5 5 THR A 107 GLY A 114 1 8
HELIX 6 6 SER A 118 ILE A 126 5 9
HELIX 7 7 GLY A 140 CYS A 149 1 10
HELIX 8 8 GLN A 162 GLY A 168 5 7
HELIX 9 9 GLN A 177 GLY A 184 1 8
HELIX 10 10 GLY A 184 GLY A 195 1 12
HELIX 11 11 ALA A 200 ALA A 206 1 7
HELIX 12 12 THR A 217 ASN A 232 1 16
HELIX 13 13 SER A 233 ALA A 246 1 14
HELIX 14 14 ALA A 247 GLU A 249 5 3
HELIX 15 15 THR A 251 THR A 266 1 16
HELIX 16 16 THR A 269 GLU A 281 1 13
HELIX 17 17 GLY B 42 SER B 45 5 4
HELIX 18 18 ARG B 54 LEU B 58 5 5
HELIX 19 19 CYS B 62 ASP B 79 1 18
HELIX 20 20 ASP B 99 GLN B 104 1 6
HELIX 21 21 THR B 107 GLY B 114 1 8
HELIX 22 22 SER B 118 ILE B 126 5 9
HELIX 23 23 GLY B 140 CYS B 149 1 10
HELIX 24 24 GLN B 162 GLY B 168 5 7
HELIX 25 25 GLN B 177 GLY B 184 1 8
HELIX 26 26 GLY B 184 GLY B 195 1 12
HELIX 27 27 ALA B 200 ALA B 206 1 7
HELIX 28 28 THR B 217 ASN B 232 1 16
HELIX 29 29 SER B 233 ALA B 247 1 15
HELIX 30 30 THR B 251 PHE B 267 1 17
HELIX 31 31 THR B 269 GLU B 281 1 13
HELIX 32 32 GLY C 42 SER C 45 5 4
HELIX 33 33 ARG C 54 LEU C 58 5 5
HELIX 34 34 CYS C 62 ASP C 79 1 18
HELIX 35 35 ASP C 99 GLN C 104 1 6
HELIX 36 36 THR C 107 GLY C 114 1 8
HELIX 37 37 ASP C 121 ILE C 126 5 6
HELIX 38 38 GLY C 140 CYS C 149 1 10
HELIX 39 39 GLN C 162 GLY C 168 5 7
HELIX 40 40 GLN C 177 GLY C 184 1 8
HELIX 41 41 GLY C 184 GLY C 195 1 12
HELIX 42 42 ALA C 200 ALA C 206 1 7
HELIX 43 43 THR C 217 ASN C 231 1 15
HELIX 44 44 SER C 233 ALA C 246 1 14
HELIX 45 45 ALA C 247 GLU C 249 5 3
HELIX 46 46 THR C 251 PHE C 267 1 17
HELIX 47 47 THR C 269 GLU C 281 1 13
HELIX 48 48 GLY D 42 SER D 45 5 4
HELIX 49 49 ARG D 54 LEU D 58 5 5
HELIX 50 50 CYS D 62 ASP D 79 1 18
HELIX 51 51 ILE D 100 ASN D 105 1 6
HELIX 52 52 THR D 107 GLY D 114 1 8
HELIX 53 53 LEU D 117 ILE D 126 5 10
HELIX 54 54 GLY D 140 CYS D 149 1 10
HELIX 55 55 GLN D 162 GLY D 168 5 7
HELIX 56 56 GLN D 177 GLY D 184 1 8
HELIX 57 57 GLY D 184 GLY D 195 1 12
HELIX 58 58 ALA D 200 ALA D 206 1 7
HELIX 59 59 PRO D 214 GLU D 216 5 3
HELIX 60 60 THR D 217 ASN D 232 1 16
HELIX 61 61 SER D 233 ALA D 247 1 15
HELIX 62 62 THR D 251 THR D 266 1 16
HELIX 63 63 THR D 269 GLU D 281 1 13
HELIX 64 64 GLY E 42 SER E 45 5 4
HELIX 65 65 ARG E 54 LEU E 58 5 5
HELIX 66 66 CYS E 62 ASP E 79 1 18
HELIX 67 67 ASP E 99 GLN E 104 1 6
HELIX 68 68 THR E 107 GLY E 114 1 8
HELIX 69 69 SER E 118 ILE E 126 5 9
HELIX 70 70 GLY E 140 CYS E 149 1 10
HELIX 71 71 GLN E 162 GLY E 168 5 7
HELIX 72 72 GLN E 177 GLY E 184 1 8
HELIX 73 73 GLY E 184 GLY E 195 1 12
HELIX 74 74 ALA E 200 ALA E 206 1 7
HELIX 75 75 THR E 217 ASN E 232 1 16
HELIX 76 76 SER E 233 ALA E 246 1 14
HELIX 77 77 ALA E 247 GLU E 249 5 3
HELIX 78 78 THR E 251 PHE E 267 1 17
HELIX 79 79 THR E 269 GLU E 281 1 13
HELIX 80 80 GLY F 42 SER F 45 5 4
HELIX 81 81 ARG F 54 LEU F 58 5 5
HELIX 82 82 CYS F 62 ASP F 79 1 18
HELIX 83 83 ASP F 99 GLN F 104 1 6
HELIX 84 84 THR F 107 GLY F 114 1 8
HELIX 85 85 LEU F 117 ILE F 126 5 10
HELIX 86 86 GLY F 140 CYS F 149 1 10
HELIX 87 87 GLN F 162 GLY F 168 5 7
HELIX 88 88 GLN F 177 GLY F 184 1 8
HELIX 89 89 GLY F 184 GLY F 195 1 12
HELIX 90 90 ALA F 200 ALA F 206 1 7
HELIX 91 91 THR F 217 ASN F 231 1 15
HELIX 92 92 SER F 233 ALA F 247 1 15
HELIX 93 93 THR F 251 PHE F 267 1 17
HELIX 94 94 THR F 269 GLU F 281 1 13
SHEET 1 A 6 ILE A 36 LYS A 41 0
SHEET 2 A 6 VAL A 47 LEU A 52 -1 O GLN A 51 N ILE A 37
SHEET 3 A 6 ALA A 84 THR A 88 1 O VAL A 86 N GLY A 48
SHEET 4 A 6 VAL A 130 VAL A 134 1 O ILE A 131 N ILE A 85
SHEET 5 A 6 ILE A 151 GLY A 155 1 O GLY A 155 N VAL A 134
SHEET 6 A 6 LYS A 211 PHE A 213 1 O LYS A 211 N ALA A 154
SHEET 1 B 4 ALA A 93 ALA A 95 0
SHEET 2 B 4 TYR A 137 LEU A 139 1 O LEU A 139 N ALA A 95
SHEET 3 B 4 GLN A 159 GLY A 161 1 O GLN A 159 N ALA A 138
SHEET 4 B 4 ILE A 198 SER A 199 -1 O ILE A 198 N PHE A 160
SHEET 1 C 6 ILE B 36 LYS B 41 0
SHEET 2 C 6 VAL B 47 LEU B 52 -1 O GLN B 51 N ILE B 37
SHEET 3 C 6 ALA B 84 THR B 88 1 O VAL B 86 N GLY B 48
SHEET 4 C 6 VAL B 130 VAL B 134 1 O ILE B 131 N ILE B 85
SHEET 5 C 6 ILE B 151 GLY B 155 1 O GLY B 155 N VAL B 134
SHEET 6 C 6 LYS B 211 PHE B 213 1 O LYS B 211 N ALA B 154
SHEET 1 D 4 ALA B 93 ALA B 95 0
SHEET 2 D 4 TYR B 137 LEU B 139 1 O LEU B 139 N ALA B 95
SHEET 3 D 4 GLN B 159 GLY B 161 1 O GLN B 159 N ALA B 138
SHEET 4 D 4 ILE B 198 SER B 199 -1 O ILE B 198 N PHE B 160
SHEET 1 E 6 ILE C 36 LYS C 41 0
SHEET 2 E 6 VAL C 47 LEU C 52 -1 O VAL C 47 N LYS C 41
SHEET 3 E 6 ALA C 84 THR C 88 1 O VAL C 86 N ILE C 50
SHEET 4 E 6 VAL C 130 VAL C 134 1 O ILE C 131 N LEU C 87
SHEET 5 E 6 ILE C 151 GLY C 155 1 O GLY C 155 N VAL C 134
SHEET 6 E 6 LYS C 211 PHE C 213 1 O LYS C 211 N ALA C 154
SHEET 1 F 4 ALA C 93 ALA C 95 0
SHEET 2 F 4 TYR C 137 LEU C 139 1 O TYR C 137 N ALA C 95
SHEET 3 F 4 GLN C 159 GLY C 161 1 O GLN C 159 N ALA C 138
SHEET 4 F 4 ILE C 198 SER C 199 -1 O ILE C 198 N PHE C 160
SHEET 1 G 6 ILE D 36 LYS D 41 0
SHEET 2 G 6 VAL D 47 LEU D 52 -1 O VAL D 47 N LYS D 41
SHEET 3 G 6 ALA D 84 THR D 88 1 O VAL D 86 N ILE D 50
SHEET 4 G 6 VAL D 130 VAL D 134 1 O ILE D 131 N LEU D 87
SHEET 5 G 6 ILE D 151 GLY D 155 1 O GLY D 155 N VAL D 134
SHEET 6 G 6 LYS D 211 PHE D 213 1 O LYS D 211 N ALA D 154
SHEET 1 H 4 ALA D 93 ALA D 95 0
SHEET 2 H 4 TYR D 137 LEU D 139 1 O TYR D 137 N ALA D 95
SHEET 3 H 4 GLN D 159 GLY D 161 1 O GLN D 159 N ALA D 138
SHEET 4 H 4 ILE D 198 SER D 199 -1 O ILE D 198 N PHE D 160
SHEET 1 I 6 ILE E 36 LYS E 41 0
SHEET 2 I 6 VAL E 47 LEU E 52 -1 O LEU E 49 N GLU E 39
SHEET 3 I 6 ALA E 84 THR E 88 1 O VAL E 86 N ILE E 50
SHEET 4 I 6 VAL E 130 VAL E 134 1 O ILE E 131 N ILE E 85
SHEET 5 I 6 ILE E 151 GLY E 155 1 O GLY E 155 N VAL E 134
SHEET 6 I 6 LYS E 211 PHE E 213 1 O LYS E 211 N ALA E 154
SHEET 1 J 4 ALA E 93 ALA E 95 0
SHEET 2 J 4 TYR E 137 LEU E 139 1 O LEU E 139 N ALA E 95
SHEET 3 J 4 GLN E 159 GLY E 161 1 O GLN E 159 N ALA E 138
SHEET 4 J 4 ILE E 198 SER E 199 -1 O ILE E 198 N PHE E 160
SHEET 1 K 6 ILE F 36 LYS F 41 0
SHEET 2 K 6 VAL F 47 LEU F 52 -1 O VAL F 47 N LYS F 41
SHEET 3 K 6 ALA F 84 THR F 88 1 O VAL F 86 N ILE F 50
SHEET 4 K 6 VAL F 130 VAL F 134 1 O ALA F 133 N LEU F 87
SHEET 5 K 6 ILE F 151 GLY F 155 1 O GLY F 155 N VAL F 134
SHEET 6 K 6 LYS F 211 PHE F 213 1 O LYS F 211 N ALA F 154
SHEET 1 L 4 ALA F 93 ALA F 95 0
SHEET 2 L 4 TYR F 137 LEU F 139 1 O LEU F 139 N ALA F 95
SHEET 3 L 4 GLN F 159 GLY F 161 1 O GLN F 159 N ALA F 138
SHEET 4 L 4 ILE F 198 SER F 199 -1 O ILE F 198 N PHE F 160
SITE 1 AC1 26 LYS A 56 ALA A 57 LEU A 58 ALA A 60
SITE 2 AC1 26 ALA A 96 GLY A 97 ALA A 98 ASP A 99
SITE 3 AC1 26 ILE A 100 LYS A 101 LEU A 117 LEU A 139
SITE 4 AC1 26 GLY A 141 PRO A 163 GLU A 164 LEU A 167
SITE 5 AC1 26 GLY A 172 HOH A 960 HOH A 990 HOH A1020
SITE 6 AC1 26 HOH A1048 HOH A1060 HOH A1069 PHE B 279
SITE 7 AC1 26 LYS B 282 LYS F 282
SITE 1 AC2 21 LYS B 56 ALA B 57 ALA B 60 ALA B 96
SITE 2 AC2 21 GLY B 97 ALA B 98 ASP B 99 ILE B 100
SITE 3 AC2 21 LYS B 101 LEU B 139 GLY B 140 GLY B 141
SITE 4 AC2 21 PRO B 163 LEU B 167 GLY B 172 HOH B 995
SITE 5 AC2 21 HOH B1078 HOH B1087 HOH B1089 PHE C 279
SITE 6 AC2 21 LYS C 282
SITE 1 AC3 26 PHE A 279 LYS A 282 LYS C 43 ASN C 44
SITE 2 AC3 26 ALA C 57 LEU C 58 ALA C 60 LYS C 92
SITE 3 AC3 26 ALA C 96 GLY C 97 ALA C 98 ASP C 99
SITE 4 AC3 26 ILE C 100 LYS C 101 LEU C 139 GLY C 140
SITE 5 AC3 26 GLY C 141 PRO C 163 GLU C 164 LEU C 167
SITE 6 AC3 26 GLY C 172 HOH C 986 HOH C 994 HOH C1018
SITE 7 AC3 26 HOH C1041 HOH C1076
SITE 1 AC4 28 HOH A1048 LYS B 282 LYS E 56 ALA E 57
SITE 2 AC4 28 LEU E 58 ALA E 60 LYS E 92 ALA E 96
SITE 3 AC4 28 GLY E 97 ALA E 98 ASP E 99 ILE E 100
SITE 4 AC4 28 LYS E 101 LEU E 117 LEU E 139 GLY E 141
SITE 5 AC4 28 PRO E 163 LEU E 167 GLY E 172 ARG E 197
SITE 6 AC4 28 HOH E 987 HOH E 992 HOH E1001 HOH E1015
SITE 7 AC4 28 HOH E1102 PHE F 279 LYS F 282 HOH F 991
SITE 1 AC5 20 PHE D 279 LYS D 282 LYS F 56 ALA F 57
SITE 2 AC5 20 ALA F 60 ALA F 96 GLY F 97 ALA F 98
SITE 3 AC5 20 ASP F 99 ILE F 100 LYS F 101 MET F 103
SITE 4 AC5 20 LEU F 117 GLY F 140 GLY F 141 PRO F 163
SITE 5 AC5 20 LEU F 167 ARG F 197 HOH F1083 HOH F1095
CRYST1 76.877 95.198 249.429 90.00 90.00 90.00 P 21 21 21 24
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 0.013008 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010504 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004009 0.00000
(ATOM LINES ARE NOT SHOWN.)
END