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HEADER HYDROLASE 30-SEP-09 3K2I
TITLE HUMAN ACYL-COENZYME A THIOESTERASE 4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYL-COENZYME A THIOESTERASE 4;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACYL-COA THIOESTERASE 4, PEROXISOMAL ACYL COENZYME
COMPND 5 A THIOESTER HYDROLASE IB, PEROXISOMAL LONG-CHAIN ACYL-COA
COMPND 6 THIOESTERASE IB, PTE-IB, PTE-2B;
COMPND 7 EC: 3.1.2.2;
COMPND 8 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: ACOT4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) GOLD PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC-BSA4
KEYWDS ALPHA/BETA HYDROLASE FOLD SEVEN-STRANDED BETA-SANDWICH,
KEYWDS 2 STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC,
KEYWDS 3 HYDROLASE, PEROXISOME, POLYMORPHISM, SERINE ESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.I.SIPONEN,M.MOCHE,C.H.ARROWSMITH,H.BERGLUND,C.BOUNTRA,
AUTHOR 2 R.COLLINS,A.M.EDWARDS,S.FLODIN,A.FLORES,S.GRASLUND,
AUTHOR 3 M.HAMMARSTROM,A.JOHANSSON,I.JOHANSSON,A.KALLAS,T.KARLBERG,
AUTHOR 4 P.KRAULIS,T.KOTENYOVA,A.KOTZSCH,N.MARKOVA,T.K.NIELSEN,
AUTHOR 5 P.NORDLUND,T.NYMAN,C.PERSSON,A.K.ROOS,P.SCHUTZ,L.SVENSSON,
AUTHOR 6 A.G.THORSELL,L.TRESAUGUES,S.VAN DEN BERG,E.WAHLBERG,
AUTHOR 7 J.WEIGELT,M.WELIN,M.WISNIEWSKA,H.SCHULER,STRUCTURAL
AUTHOR 8 GENOMICS CONSORTIUM (SGC)
REVDAT 1 20-OCT-09 3K2I 0
JRNL AUTH M.I.SIPONEN,M.MOCHE,C.H.ARROWSMITH,H.BERGLUND,
JRNL AUTH 2 C.BOUNTRA,R.COLLINS,A.M.EDWARDS,S.FLODIN,A.FLORES,
JRNL AUTH 3 S.GRASLUND,M.HAMMARSTROM,A.JOHANSSON,I.JOHANSSON,
JRNL AUTH 4 A.KALLAS,T.KARLBERG,P.KRAULIS,T.KOTENYOVA,
JRNL AUTH 5 A.KOTZSCH,N.MARKOVA,T.K.NIELSEN,P.NORDLUND,T.NYMAN,
JRNL AUTH 6 C.PERSSON,A.K.ROOS,P.SCHUTZ,L.SVENSSON,
JRNL AUTH 7 A.G.THORSELL,L.TRESAUGUES,S.VAN DEN BERG,
JRNL AUTH 8 E.WAHLBERG,J.WEIGELT,M.WELIN,M.WISNIEWSKA,H.SCHULER
JRNL TITL HUMAN ACYL-COENZYME A THIOESTERASE 4
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 63.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 34897
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1124
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2551
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2450
REMARK 3 BIN FREE R VALUE SET COUNT : 77
REMARK 3 BIN FREE R VALUE : 0.2880
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6439
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 187
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.93
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.81000
REMARK 3 B22 (A**2) : 2.11000
REMARK 3 B33 (A**2) : -1.30000
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): 0.415
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.263
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.172
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.078
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.936
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.895
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6622 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 4635 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9013 ; 1.579 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11239 ; 0.919 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 832 ; 6.407 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 294 ;34.327 ;22.721
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1063 ;16.225 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 56 ;16.207 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 956 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7474 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1392 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 4112 ; 0.867 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1658 ; 0.176 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6613 ; 1.693 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2510 ; 2.606 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2400 ; 4.310 ; 4.500
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: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3K2I COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-OCT-09.
REMARK 100 THE RCSB ID CODE IS RCSB055463.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUL-09
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 : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
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 : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36079
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 66.820
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.122
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 13.200
REMARK 200 R MERGE (I) : 0.11700
REMARK 200 R SYM (I) : 0.11700
REMARK 200 FOR THE DATA SET : 21.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.53
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 13.50
REMARK 200 R MERGE FOR SHELL (I) : 0.40000
REMARK 200 R SYM FOR SHELL (I) : 0.40000
REMARK 200 FOR SHELL : 7.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3HLK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.2M NAI, 0.1M BTP, PH
REMARK 280 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 36.23500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.86000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.50000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.86000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.23500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.50000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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 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 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 PRO A 10
REMARK 465 GLY A 11
REMARK 465 ARG A 12
REMARK 465 GLY A 411
REMARK 465 GLY A 412
REMARK 465 THR A 413
REMARK 465 GLN A 414
REMARK 465 LYS A 415
REMARK 465 THR A 416
REMARK 465 ALA A 417
REMARK 465 VAL A 418
REMARK 465 PRO A 419
REMARK 465 LYS A 420
REMARK 465 LEU A 421
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 PRO B 10
REMARK 465 GLY B 11
REMARK 465 ARG B 12
REMARK 465 GLY B 411
REMARK 465 GLY B 412
REMARK 465 THR B 413
REMARK 465 GLN B 414
REMARK 465 LYS B 415
REMARK 465 THR B 416
REMARK 465 ALA B 417
REMARK 465 VAL B 418
REMARK 465 PRO B 419
REMARK 465 LYS B 420
REMARK 465 LEU B 421
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LEU B 333 N CA C O CB CG CD1
REMARK 480 LEU B 333 CD2
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 ND2 ASN B 262 O HOH B 525 1.83
REMARK 500 ND2 ASN A 262 O HOH A 486 1.98
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 B 121 CB CYS B 121 SG -0.160
REMARK 500 GLU B 387 CD GLU B 387 OE2 0.069
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 MET B 308 CG - SD - CE ANGL. DEV. = -10.3 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 ASP A 40 -163.99 -79.29
REMARK 500 ASP A 55 -169.00 -79.38
REMARK 500 PHE A 193 118.49 -160.87
REMARK 500 GLU A 194 -128.20 45.26
REMARK 500 PRO A 197 155.29 -49.80
REMARK 500 SER A 232 -130.35 70.72
REMARK 500 LYS A 268 -114.18 53.78
REMARK 500 CYS B 121 148.98 -175.82
REMARK 500 TYR B 190 -12.21 -143.87
REMARK 500 GLU B 194 -124.70 43.62
REMARK 500 ASN B 198 -45.21 -25.92
REMARK 500 MET B 200 76.79 -106.66
REMARK 500 SER B 232 -132.27 64.40
REMARK 500 LYS B 268 -111.72 49.80
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 NI A 422
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 423
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 423
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS SEQUENCE IS FROM NATURAL VARIANT.
REMARK 999 REFER TO REF. 3 IN UNP DATABASE Q8N9L9.
DBREF 3K2I A 1 421 UNP Q8N9L9 ACOT4_HUMAN 1 421
DBREF 3K2I B 1 421 UNP Q8N9L9 ACOT4_HUMAN 1 421
SEQADV 3K2I SER A 0 UNP Q8N9L9 EXPRESSION TAG
SEQADV 3K2I CYS A 57 UNP Q8N9L9 ARG 57 SEE REMARK 999
SEQADV 3K2I TRP A 135 UNP Q8N9L9 ARG 135 ENGINEERED
SEQADV 3K2I SER B 0 UNP Q8N9L9 EXPRESSION TAG
SEQADV 3K2I CYS B 57 UNP Q8N9L9 ARG 57 SEE REMARK 999
SEQADV 3K2I TRP B 135 UNP Q8N9L9 ARG 135 ENGINEERED
SEQRES 1 A 422 SER MET SER ALA THR LEU ILE LEU GLU PRO PRO GLY ARG
SEQRES 2 A 422 CYS CYS TRP ASN GLU PRO VAL ARG ILE ALA VAL ARG GLY
SEQRES 3 A 422 LEU ALA PRO GLU GLN ARG VAL THR LEU ARG ALA SER LEU
SEQRES 4 A 422 ARG ASP GLU LYS GLY ALA LEU PHE ARG ALA HIS ALA ARG
SEQRES 5 A 422 TYR CYS ALA ASP ALA CYS GLY GLU LEU ASP LEU GLU ARG
SEQRES 6 A 422 ALA PRO ALA LEU GLY GLY SER PHE ALA GLY LEU GLU PRO
SEQRES 7 A 422 MET GLY LEU LEU TRP ALA LEU GLU PRO GLU LYS PRO PHE
SEQRES 8 A 422 TRP ARG PHE LEU LYS ARG ASP VAL GLN ILE PRO PHE VAL
SEQRES 9 A 422 VAL GLU LEU GLU VAL LEU ASP GLY HIS ASP PRO GLU PRO
SEQRES 10 A 422 GLY ARG LEU LEU CYS GLN ALA GLN HIS GLU ARG HIS PHE
SEQRES 11 A 422 LEU PRO PRO GLY VAL TRP ARG GLN SER VAL ARG ALA GLY
SEQRES 12 A 422 ARG VAL ARG ALA THR LEU PHE LEU PRO PRO GLY PRO GLY
SEQRES 13 A 422 PRO PHE PRO GLY ILE ILE ASP ILE PHE GLY ILE GLY GLY
SEQRES 14 A 422 GLY LEU LEU GLU TYR ARG ALA SER LEU LEU ALA GLY HIS
SEQRES 15 A 422 GLY PHE ALA THR LEU ALA LEU ALA TYR TYR ASN PHE GLU
SEQRES 16 A 422 ASP LEU PRO ASN ASN MET ASP ASN ILE SER LEU GLU TYR
SEQRES 17 A 422 PHE GLU GLU ALA VAL CYS TYR MET LEU GLN HIS PRO GLN
SEQRES 18 A 422 VAL LYS GLY PRO GLY ILE GLY LEU LEU GLY ILE SER LEU
SEQRES 19 A 422 GLY ALA ASP ILE CYS LEU SER MET ALA SER PHE LEU LYS
SEQRES 20 A 422 ASN VAL SER ALA THR VAL SER ILE ASN GLY SER GLY ILE
SEQRES 21 A 422 SER GLY ASN THR ALA ILE ASN TYR LYS HIS SER SER ILE
SEQRES 22 A 422 PRO PRO LEU GLY TYR ASP LEU ARG ARG ILE LYS VAL ALA
SEQRES 23 A 422 PHE SER GLY LEU VAL ASP ILE VAL ASP ILE ARG ASN ALA
SEQRES 24 A 422 LEU VAL GLY GLY TYR LYS ASN PRO SER MET ILE PRO ILE
SEQRES 25 A 422 GLU LYS ALA GLN GLY PRO ILE LEU LEU ILE VAL GLY GLN
SEQRES 26 A 422 ASP ASP HIS ASN TRP ARG SER GLU LEU TYR ALA GLN THR
SEQRES 27 A 422 VAL SER GLU ARG LEU GLN ALA HIS GLY LYS GLU LYS PRO
SEQRES 28 A 422 GLN ILE ILE CYS TYR PRO GLY THR GLY HIS TYR ILE GLU
SEQRES 29 A 422 PRO PRO TYR PHE PRO LEU CYS PRO ALA SER LEU HIS ARG
SEQRES 30 A 422 LEU LEU ASN LYS HIS VAL ILE TRP GLY GLY GLU PRO ARG
SEQRES 31 A 422 ALA HIS SER LYS ALA GLN GLU ASP ALA TRP LYS GLN ILE
SEQRES 32 A 422 LEU ALA PHE PHE CYS LYS HIS LEU GLY GLY THR GLN LYS
SEQRES 33 A 422 THR ALA VAL PRO LYS LEU
SEQRES 1 B 422 SER MET SER ALA THR LEU ILE LEU GLU PRO PRO GLY ARG
SEQRES 2 B 422 CYS CYS TRP ASN GLU PRO VAL ARG ILE ALA VAL ARG GLY
SEQRES 3 B 422 LEU ALA PRO GLU GLN ARG VAL THR LEU ARG ALA SER LEU
SEQRES 4 B 422 ARG ASP GLU LYS GLY ALA LEU PHE ARG ALA HIS ALA ARG
SEQRES 5 B 422 TYR CYS ALA ASP ALA CYS GLY GLU LEU ASP LEU GLU ARG
SEQRES 6 B 422 ALA PRO ALA LEU GLY GLY SER PHE ALA GLY LEU GLU PRO
SEQRES 7 B 422 MET GLY LEU LEU TRP ALA LEU GLU PRO GLU LYS PRO PHE
SEQRES 8 B 422 TRP ARG PHE LEU LYS ARG ASP VAL GLN ILE PRO PHE VAL
SEQRES 9 B 422 VAL GLU LEU GLU VAL LEU ASP GLY HIS ASP PRO GLU PRO
SEQRES 10 B 422 GLY ARG LEU LEU CYS GLN ALA GLN HIS GLU ARG HIS PHE
SEQRES 11 B 422 LEU PRO PRO GLY VAL TRP ARG GLN SER VAL ARG ALA GLY
SEQRES 12 B 422 ARG VAL ARG ALA THR LEU PHE LEU PRO PRO GLY PRO GLY
SEQRES 13 B 422 PRO PHE PRO GLY ILE ILE ASP ILE PHE GLY ILE GLY GLY
SEQRES 14 B 422 GLY LEU LEU GLU TYR ARG ALA SER LEU LEU ALA GLY HIS
SEQRES 15 B 422 GLY PHE ALA THR LEU ALA LEU ALA TYR TYR ASN PHE GLU
SEQRES 16 B 422 ASP LEU PRO ASN ASN MET ASP ASN ILE SER LEU GLU TYR
SEQRES 17 B 422 PHE GLU GLU ALA VAL CYS TYR MET LEU GLN HIS PRO GLN
SEQRES 18 B 422 VAL LYS GLY PRO GLY ILE GLY LEU LEU GLY ILE SER LEU
SEQRES 19 B 422 GLY ALA ASP ILE CYS LEU SER MET ALA SER PHE LEU LYS
SEQRES 20 B 422 ASN VAL SER ALA THR VAL SER ILE ASN GLY SER GLY ILE
SEQRES 21 B 422 SER GLY ASN THR ALA ILE ASN TYR LYS HIS SER SER ILE
SEQRES 22 B 422 PRO PRO LEU GLY TYR ASP LEU ARG ARG ILE LYS VAL ALA
SEQRES 23 B 422 PHE SER GLY LEU VAL ASP ILE VAL ASP ILE ARG ASN ALA
SEQRES 24 B 422 LEU VAL GLY GLY TYR LYS ASN PRO SER MET ILE PRO ILE
SEQRES 25 B 422 GLU LYS ALA GLN GLY PRO ILE LEU LEU ILE VAL GLY GLN
SEQRES 26 B 422 ASP ASP HIS ASN TRP ARG SER GLU LEU TYR ALA GLN THR
SEQRES 27 B 422 VAL SER GLU ARG LEU GLN ALA HIS GLY LYS GLU LYS PRO
SEQRES 28 B 422 GLN ILE ILE CYS TYR PRO GLY THR GLY HIS TYR ILE GLU
SEQRES 29 B 422 PRO PRO TYR PHE PRO LEU CYS PRO ALA SER LEU HIS ARG
SEQRES 30 B 422 LEU LEU ASN LYS HIS VAL ILE TRP GLY GLY GLU PRO ARG
SEQRES 31 B 422 ALA HIS SER LYS ALA GLN GLU ASP ALA TRP LYS GLN ILE
SEQRES 32 B 422 LEU ALA PHE PHE CYS LYS HIS LEU GLY GLY THR GLN LYS
SEQRES 33 B 422 THR ALA VAL PRO LYS LEU
HET NI A 422 1
HET CL A 423 1
HET CL A 424 1
HET NI B 422 1
HET CL B 423 1
HETNAM NI NICKEL (II) ION
HETNAM CL CHLORIDE ION
FORMUL 3 NI 2(NI 2+)
FORMUL 4 CL 3(CL 1-)
FORMUL 8 HOH *187(H2 O)
HELIX 1 1 MET A 78 ALA A 83 1 6
HELIX 2 2 GLU A 172 GLY A 180 1 9
HELIX 3 3 LEU A 205 GLN A 217 1 13
HELIX 4 4 SER A 232 LEU A 245 1 14
HELIX 5 5 ASP A 278 ILE A 282 5 5
HELIX 6 6 GLY A 301 ASN A 305 5 5
HELIX 7 7 PRO A 310 ALA A 314 5 5
HELIX 8 8 ARG A 330 HIS A 345 1 16
HELIX 9 9 GLU A 387 LEU A 410 1 24
HELIX 10 10 MET B 78 ALA B 83 1 6
HELIX 11 11 GLU B 172 GLY B 180 1 9
HELIX 12 12 LEU B 205 HIS B 218 1 14
HELIX 13 13 SER B 232 LEU B 245 1 14
HELIX 14 14 ASP B 278 ILE B 282 5 5
HELIX 15 15 GLY B 301 ASN B 305 5 5
HELIX 16 16 PRO B 310 ALA B 314 5 5
HELIX 17 17 ARG B 330 HIS B 345 1 16
HELIX 18 18 GLU B 387 LEU B 410 1 24
SHEET 1 A 3 THR A 4 GLU A 8 0
SHEET 2 A 3 ARG A 20 ARG A 24 -1 O ALA A 22 N ILE A 6
SHEET 3 A 3 LEU A 60 ASP A 61 -1 O LEU A 60 N VAL A 23
SHEET 1 B 3 GLY A 69 GLY A 70 0
SHEET 2 B 3 LEU A 45 CYS A 53 -1 N ARG A 51 O GLY A 69
SHEET 3 B 3 GLU A 85 PRO A 86 -1 O GLU A 85 N ARG A 47
SHEET 1 C 5 GLY A 69 GLY A 70 0
SHEET 2 C 5 LEU A 45 CYS A 53 -1 N ARG A 51 O GLY A 69
SHEET 3 C 5 ARG A 31 ARG A 39 -1 N VAL A 32 O TYR A 52
SHEET 4 C 5 PHE A 102 ASP A 110 -1 O LEU A 109 N THR A 33
SHEET 5 C 5 LEU A 119 ARG A 127 -1 O HIS A 125 N VAL A 104
SHEET 1 D 8 TRP A 135 ALA A 141 0
SHEET 2 D 8 VAL A 144 LEU A 150 -1 O LEU A 148 N GLN A 137
SHEET 3 D 8 ALA A 184 ALA A 189 -1 O ALA A 187 N THR A 147
SHEET 4 D 8 GLY A 159 ILE A 163 1 N ASP A 162 O LEU A 186
SHEET 5 D 8 ILE A 226 ILE A 231 1 O GLY A 227 N GLY A 159
SHEET 6 D 8 VAL A 248 ILE A 254 1 O VAL A 252 N LEU A 228
SHEET 7 D 8 ILE A 318 GLY A 323 1 O ILE A 321 N SER A 253
SHEET 8 D 8 GLN A 351 TYR A 355 1 O TYR A 355 N VAL A 322
SHEET 1 E 3 ILE A 203 SER A 204 0
SHEET 2 E 3 ILE A 265 TYR A 267 1 O ASN A 266 N ILE A 203
SHEET 3 E 3 SER A 270 ILE A 272 -1 O SER A 270 N TYR A 267
SHEET 1 F 2 LYS A 283 VAL A 284 0
SHEET 2 F 2 VAL A 290 ASP A 291 -1 O ASP A 291 N LYS A 283
SHEET 1 G 2 ALA A 372 HIS A 375 0
SHEET 2 G 2 LYS A 380 ILE A 383 -1 O VAL A 382 N SER A 373
SHEET 1 H 3 THR B 4 GLU B 8 0
SHEET 2 H 3 ARG B 20 ARG B 24 -1 O ARG B 24 N THR B 4
SHEET 3 H 3 LEU B 60 ASP B 61 -1 O LEU B 60 N VAL B 23
SHEET 1 I 3 GLY B 69 GLY B 70 0
SHEET 2 I 3 LEU B 45 CYS B 53 -1 N ARG B 51 O GLY B 69
SHEET 3 I 3 GLU B 85 PRO B 86 -1 O GLU B 85 N ARG B 47
SHEET 1 J 5 GLY B 69 GLY B 70 0
SHEET 2 J 5 LEU B 45 CYS B 53 -1 N ARG B 51 O GLY B 69
SHEET 3 J 5 ARG B 31 ARG B 39 -1 N LEU B 38 O PHE B 46
SHEET 4 J 5 PHE B 102 ASP B 110 -1 O LEU B 109 N THR B 33
SHEET 5 J 5 LEU B 119 ARG B 127 -1 O HIS B 125 N VAL B 104
SHEET 1 K 8 TRP B 135 ALA B 141 0
SHEET 2 K 8 VAL B 144 LEU B 150 -1 O LEU B 148 N GLN B 137
SHEET 3 K 8 ALA B 184 LEU B 188 -1 O ALA B 187 N THR B 147
SHEET 4 K 8 GLY B 159 ILE B 163 1 N ASP B 162 O LEU B 186
SHEET 5 K 8 ILE B 226 ILE B 231 1 O LEU B 229 N ILE B 161
SHEET 6 K 8 VAL B 248 ILE B 254 1 O VAL B 252 N LEU B 228
SHEET 7 K 8 ILE B 318 GLY B 323 1 O ILE B 321 N SER B 253
SHEET 8 K 8 GLN B 351 TYR B 355 1 O GLN B 351 N LEU B 320
SHEET 1 L 3 ILE B 203 SER B 204 0
SHEET 2 L 3 ILE B 265 TYR B 267 1 O ASN B 266 N ILE B 203
SHEET 3 L 3 SER B 270 ILE B 272 -1 O SER B 270 N TYR B 267
SHEET 1 M 2 LYS B 283 VAL B 284 0
SHEET 2 M 2 VAL B 290 ASP B 291 -1 O ASP B 291 N LYS B 283
SHEET 1 N 2 ALA B 372 HIS B 375 0
SHEET 2 N 2 LYS B 380 ILE B 383 -1 O VAL B 382 N SER B 373
CISPEP 1 GLU A 8 PRO A 9 0 -3.98
CISPEP 2 GLY A 155 PRO A 156 0 -10.03
CISPEP 3 GLY A 223 PRO A 224 0 10.52
CISPEP 4 GLU B 8 PRO B 9 0 -25.44
CISPEP 5 GLY B 155 PRO B 156 0 4.13
CISPEP 6 GLY B 223 PRO B 224 0 8.11
SITE 1 AC1 1 LEU B 289
SITE 1 AC2 1 HOH A 492
SITE 1 AC3 1 HOH B 526
CRYST1 72.470 93.000 133.720 90.00 90.00 90.00 P 21 21 21 8
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 0.013799 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010753 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007478 0.00000
TER 3206 LEU A 410
TER 6441 LEU B 410
MASTER 393 0 5 18 52 0 3 6 6631 2 0 66
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