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HEADER HYDROLASE 03-FEB-04 1S8O
TITLE HUMAN SOLUBLE EPOXIDE HYDROLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPOXIDE HYDROLASE 2, CYTOPLASMIC;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HSEH;
COMPND 5 EC: 3.3.2.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 GENE: EPHX2;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: ACHSEH1
KEYWDS DOMAIN-SWAPPED DIMER
EXPDTA X-RAY DIFFRACTION
AUTHOR G.A.GOMEZ,C.MORISSEAU,B.D.HAMMOCK,D.W.CHRISTIANSON
REVDAT 1 27-APR-04 1S8O 0
JRNL AUTH G.A.GOMEZ,C.MORISSEAU,B.D.HAMMOCK,D.W.CHRISTIANSON
JRNL TITL STRUCTURE OF HUMAN EPOXIDE HYDROLASE REVEALS
JRNL TITL 2 MECHANISTIC INFERENCES ON BIFUNCTIONAL CATALYSIS
JRNL TITL 3 IN EPOXIDE AND PHOSPHATE ESTER HYDROLYSIS
JRNL REF BIOCHEMISTRY V. 43 4716 2004
JRNL REFN ASTM BICHAW US ISSN 0006-2960
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.60 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.41
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 251057.730
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 19616
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) : 0.216
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1544
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2871
REMARK 3 BIN R VALUE (WORKING SET) : 0.2660
REMARK 3 BIN FREE R VALUE : 0.3190
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 231
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4316
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 19
REMARK 3 SOLVENT ATOMS : 46
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.66000
REMARK 3 B22 (A**2) : 1.66000
REMARK 3 B33 (A**2) : -3.32000
REMARK 3 B12 (A**2) : 6.59000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.31
REMARK 3 ESD FROM SIGMAA (A) : 0.29
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) : 0.41
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.39
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.40
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.85
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) : 1.290 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.160 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.080 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.150 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 26.36
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 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : SUL.PARAM
REMARK 3 PARAMETER FILE 4 : PEG.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 3 : SUL.TOP
REMARK 3 TOPOLOGY FILE 4 : PEG.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1S8O COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-FEB-2004.
REMARK 100 THE RCSB ID CODE IS RCSB021506.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JAN-2002
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.40
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : SI111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19879
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 9.900
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 30.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.36300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 11.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1CQZ
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: PEG 4000, TRIS, LITHIUM SULFATE, PH
REMARK 280 8.4, VAPOR DIFFUSION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,2/3+Z
REMARK 290 3555 -X+Y,-X,1/3+Z
REMARK 290 4555 -X,-Y,1/2+Z
REMARK 290 5555 Y,-X+Y,1/6+Z
REMARK 290 6555 X-Y,X,5/6+Z
REMARK 290 7555 Y,X,2/3-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,1/3-Z
REMARK 290 10555 -Y,-X,1/6-Z
REMARK 290 11555 -X+Y,Y,1/2-Z
REMARK 290 12555 X,X-Y,5/6-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 163.09133
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 81.54567
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 122.31850
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 40.77283
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 203.86417
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 163.09133
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 81.54567
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 40.77283
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 122.31850
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 203.86417
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
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 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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 122.31850
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH 586 LIES ON A SPECIAL POSITION.
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 THR A 2
REMARK 465 LEU A 3
REMARK 465 PRO A 549
REMARK 465 PRO A 550
REMARK 465 VAL A 551
REMARK 465 VAL A 552
REMARK 465 SER A 553
REMARK 465 LYS A 554
REMARK 465 MET A 555
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 C5 P6G 780 O16 P6G 780 11555 0.44
REMARK 500 C9 P6G 780 C12 P6G 780 11555 0.63
REMARK 500 C3 P6G 780 C18 P6G 780 11555 0.70
REMARK 500 C3 P6G 780 O19 P6G 780 11555 0.79
REMARK 500 C8 P6G 780 O13 P6G 780 11555 0.83
REMARK 500 O7 P6G 780 C14 P6G 780 11555 0.92
REMARK 500 C8 P6G 780 C14 P6G 780 11555 0.92
REMARK 500 C6 P6G 780 C15 P6G 780 11555 0.95
REMARK 500 O7 P6G 780 C15 P6G 780 11555 0.95
REMARK 500 C9 P6G 780 O13 P6G 780 11555 0.98
REMARK 500 O10 P6G 780 C11 P6G 780 11555 1.07
REMARK 500 C5 P6G 780 C17 P6G 780 11555 1.08
REMARK 500 C11 P6G 780 C11 P6G 780 11555 1.20
REMARK 500 C6 P6G 780 O16 P6G 780 11555 1.26
REMARK 500 C9 P6G 780 C11 P6G 780 11555 1.33
REMARK 500 O4 P6G 780 C17 P6G 780 11555 1.38
REMARK 500 C2 P6G 780 O19 P6G 780 11555 1.41
REMARK 500 O4 P6G 780 O16 P6G 780 11555 1.42
REMARK 500 O4 P6G 780 C18 P6G 780 11555 1.45
REMARK 500 C5 P6G 780 C15 P6G 780 11555 1.51
REMARK 500 O7 P6G 780 O13 P6G 780 11555 1.54
REMARK 500 C6 P6G 780 C14 P6G 780 11555 1.59
REMARK 500 O10 P6G 780 O10 P6G 780 11555 1.63
REMARK 500 C3 P6G 780 C17 P6G 780 11555 1.77
REMARK 500 C8 P6G 780 C12 P6G 780 11555 1.88
REMARK 500 C2 P6G 780 C18 P6G 780 11555 1.90
REMARK 500 O10 P6G 780 C12 P6G 780 11555 1.90
REMARK 500 O10 P6G 780 O13 P6G 780 11555 1.99
REMARK 500 O1 P6G 780 O19 P6G 780 11555 2.00
REMARK 500 C5 P6G 780 C18 P6G 780 11555 2.10
REMARK 500 O4 P6G 780 O19 P6G 780 11555 2.14
REMARK 500 C9 P6G 780 O10 P6G 780 11555 2.14
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET A 111 SD MET A 111 CE 0.044
REMARK 500 MET A 140 SD MET A 140 CE 0.047
REMARK 500 MET A 237 SD MET A 237 CE -0.051
REMARK 500 MET A 317 SD MET A 317 CE -0.051
REMARK 500 PRO A 462 CB PRO A 462 CG 0.042
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 9 N - CA - C ANGL. DEV. = -8.7 DEGREES
REMARK 500 ASN A 102 N - CA - C ANGL. DEV. = -9.8 DEGREES
REMARK 500 THR A 118 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 ASN A 124 N - CA - C ANGL. DEV. =-10.9 DEGREES
REMARK 500 LEU A 127 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 LEU A 183 CA - CB - CG ANGL. DEV. = 10.2 DEGREES
REMARK 500 ALA A 226 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 LEU A 228 N - CA - C ANGL. DEV. =-10.4 DEGREES
REMARK 500 SER A 238 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 PRO A 268 N - CA - C ANGL. DEV. = -8.6 DEGREES
REMARK 500 ARG A 287 N - CA - C ANGL. DEV. = -8.3 DEGREES
REMARK 500 ASP A 292 N - CA - C ANGL. DEV. =-17.7 DEGREES
REMARK 500 VAL A 330 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 LEU A 340 CA - CB - CG ANGL. DEV. = 9.7 DEGREES
REMARK 500 ASP A 496 N - CA - C ANGL. DEV. =-11.7 DEGREES
REMARK 500 GLN A 505 N - CA - C ANGL. DEV. = 11.2 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 ASN A 359 -46.35 71.19
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1VJ5 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE NUMBERING OF AMINO ACIDS WAS MODIFIED TO ADOPT THE
REMARK 999 NUMBERING EMPLOYED IN MURINE EPOXIDE HYDROLASE (PDB ENTRY
REMARK 999 1CQZ).
DBREF 1S8O A 1 555 GB 27597073 NP_001970 1 555
SEQRES 1 A 555 MET THR LEU ARG ALA ALA VAL PHE ASP LEU ASP GLY VAL
SEQRES 2 A 555 LEU ALA LEU PRO ALA VAL PHE GLY VAL LEU GLY ARG THR
SEQRES 3 A 555 GLU GLU ALA LEU ALA LEU PRO ARG GLY LEU LEU ASN ASP
SEQRES 4 A 555 ALA PHE GLN LYS GLY GLY PRO GLU GLY ALA THR THR ARG
SEQRES 5 A 555 LEU MET LYS GLY GLU ILE THR LEU SER GLN TRP ILE PRO
SEQRES 6 A 555 LEU MET GLU GLU ASN CYS ARG LYS CYS SER GLU THR ALA
SEQRES 7 A 555 LYS VAL CYS LEU PRO LYS ASN PHE SER ILE LYS GLU ILE
SEQRES 8 A 555 PHE ASP LYS ALA ILE SER ALA ARG LYS ILE ASN ARG PRO
SEQRES 9 A 555 MET LEU GLN ALA ALA LEU MET LEU ARG LYS LYS GLY PHE
SEQRES 10 A 555 THR THR ALA ILE LEU THR ASN THR TRP LEU ASP ASP ARG
SEQRES 11 A 555 ALA GLU ARG ASP GLY LEU ALA GLN LEU MET CYS GLU LEU
SEQRES 12 A 555 LYS MET HIS PHE ASP PHE LEU ILE GLU SER CYS GLN VAL
SEQRES 13 A 555 GLY MET VAL LYS PRO GLU PRO GLN ILE TYR LYS PHE LEU
SEQRES 14 A 555 LEU ASP THR LEU LYS ALA SER PRO SER GLU VAL VAL PHE
SEQRES 15 A 555 LEU ASP ASP ILE GLY ALA ASN LEU LYS PRO ALA ARG ASP
SEQRES 16 A 555 LEU GLY MET VAL THR ILE LEU VAL GLN ASP THR ASP THR
SEQRES 17 A 555 ALA LEU LYS GLU LEU GLU LYS VAL THR GLY ILE GLN LEU
SEQRES 18 A 555 LEU ASN THR PRO ALA PRO LEU PRO THR SER CYS ASN PRO
SEQRES 19 A 555 SER ASP MET SER HIS GLY TYR VAL THR VAL LYS PRO ARG
SEQRES 20 A 555 VAL ARG LEU HIS PHE VAL GLU LEU GLY SER GLY PRO ALA
SEQRES 21 A 555 VAL CYS LEU CYS HIS GLY PHE PRO GLU SER TRP TYR SER
SEQRES 22 A 555 TRP ARG TYR GLN ILE PRO ALA LEU ALA GLN ALA GLY TYR
SEQRES 23 A 555 ARG VAL LEU ALA MET ASP MET LYS GLY TYR GLY GLU SER
SEQRES 24 A 555 SER ALA PRO PRO GLU ILE GLU GLU TYR CYS MET GLU VAL
SEQRES 25 A 555 LEU CYS LYS GLU MET VAL THR PHE LEU ASP LYS LEU GLY
SEQRES 26 A 555 LEU SER GLN ALA VAL PHE ILE GLY HIS ASP TRP GLY GLY
SEQRES 27 A 555 MET LEU VAL TRP TYR MET ALA LEU PHE TYR PRO GLU ARG
SEQRES 28 A 555 VAL ARG ALA VAL ALA SER LEU ASN THR PRO PHE ILE PRO
SEQRES 29 A 555 ALA ASN PRO ASN MET SER PRO LEU GLU SER ILE LYS ALA
SEQRES 30 A 555 ASN PRO VAL PHE ASP TYR GLN LEU TYR PHE GLN GLU PRO
SEQRES 31 A 555 GLY VAL ALA GLU ALA GLU LEU GLU GLN ASN LEU SER ARG
SEQRES 32 A 555 THR PHE LYS SER LEU PHE ARG ALA SER ASP GLU SER VAL
SEQRES 33 A 555 LEU SER MET HIS LYS VAL CYS GLU ALA GLY GLY LEU PHE
SEQRES 34 A 555 VAL ASN SER PRO GLU GLU PRO SER LEU SER ARG MET VAL
SEQRES 35 A 555 THR GLU GLU GLU ILE GLN PHE TYR VAL GLN GLN PHE LYS
SEQRES 36 A 555 LYS SER GLY PHE ARG GLY PRO LEU ASN TRP TYR ARG ASN
SEQRES 37 A 555 MET GLU ARG ASN TRP LYS TRP ALA CYS LYS SER LEU GLY
SEQRES 38 A 555 ARG LYS ILE LEU ILE PRO ALA LEU MET VAL THR ALA GLU
SEQRES 39 A 555 LYS ASP PHE VAL LEU VAL PRO GLN MET SER GLN HIS MET
SEQRES 40 A 555 GLU ASP TRP ILE PRO HIS LEU LYS ARG GLY HIS ILE GLU
SEQRES 41 A 555 ASP CYS GLY HIS TRP THR GLN MET ASP LYS PRO THR GLU
SEQRES 42 A 555 VAL ASN GLN ILE LEU ILE LYS TRP LEU ASP SER ASP ALA
SEQRES 43 A 555 ARG ASN PRO PRO VAL VAL SER LYS MET
HET P6G 780 19
HETNAM P6G HEXAETHYLENE GLYCOL
HETSYN P6G POLYETHYLENE GLYCOL PEG400
FORMUL 2 P6G C12 H26 O7
FORMUL 3 HOH *46(H2 O1)
HELIX 1 1 ALA A 18 PHE A 20 5 3
HELIX 2 2 GLY A 21 LEU A 30 1 10
HELIX 3 3 GLY A 35 LYS A 43 1 9
HELIX 4 4 GLY A 44 GLU A 47 5 4
HELIX 5 5 GLY A 48 LYS A 55 1 8
HELIX 6 6 THR A 59 ALA A 78 1 20
HELIX 7 7 SER A 87 ARG A 99 1 13
HELIX 8 8 ASN A 102 LYS A 115 1 14
HELIX 9 9 GLU A 132 MET A 145 1 14
HELIX 10 10 SER A 153 GLY A 157 1 5
HELIX 11 11 GLU A 162 LEU A 173 1 12
HELIX 12 12 ILE A 186 LEU A 196 1 11
HELIX 13 13 ASP A 205 GLY A 218 1 14
HELIX 14 14 ASN A 233 MET A 237 5 5
HELIX 15 15 SER A 270 ARG A 275 5 6
HELIX 16 16 TYR A 276 ALA A 284 1 9
HELIX 17 17 GLU A 304 TYR A 308 5 5
HELIX 18 18 CYS A 309 LEU A 324 1 16
HELIX 19 19 ASP A 335 TYR A 348 1 14
HELIX 20 20 SER A 370 ALA A 377 1 8
HELIX 21 21 ASN A 378 VAL A 380 5 3
HELIX 22 22 PHE A 381 GLU A 389 1 9
HELIX 23 23 GLY A 391 ASN A 400 1 10
HELIX 24 24 ASN A 400 PHE A 409 1 10
HELIX 25 25 LYS A 421 GLY A 426 1 6
HELIX 26 26 THR A 443 LYS A 455 1 13
HELIX 27 27 PHE A 459 TRP A 465 1 7
HELIX 28 28 ASN A 468 CYS A 477 1 10
HELIX 29 29 LYS A 478 LEU A 480 5 3
HELIX 30 30 VAL A 500 GLN A 505 5 6
HELIX 31 31 HIS A 506 ILE A 511 1 6
HELIX 32 32 TRP A 525 LYS A 530 1 6
HELIX 33 33 LYS A 530 ALA A 546 1 17
SHEET 1 A 5 PHE A 149 GLU A 152 0
SHEET 2 A 5 THR A 118 THR A 123 1 N ILE A 121 O ILE A 151
SHEET 3 A 5 ALA A 5 PHE A 8 1 N PHE A 8 O ALA A 120
SHEET 4 A 5 VAL A 180 ASP A 184 1 O VAL A 181 N VAL A 7
SHEET 5 A 5 VAL A 199 LEU A 202 1 O VAL A 199 N PHE A 182
SHEET 1 B 2 ALA A 15 LEU A 16 0
SHEET 2 B 2 LYS A 100 ILE A 101 -1 O LYS A 100 N LEU A 16
SHEET 1 C 8 SER A 238 LYS A 245 0
SHEET 2 C 8 VAL A 248 LEU A 255 -1 O LEU A 250 N VAL A 242
SHEET 3 C 8 ARG A 287 ASP A 292 -1 O VAL A 288 N LEU A 255
SHEET 4 C 8 ALA A 260 CYS A 264 1 N VAL A 261 O LEU A 289
SHEET 5 C 8 ALA A 329 HIS A 334 1 O VAL A 330 N CYS A 262
SHEET 6 C 8 VAL A 352 LEU A 358 1 O ALA A 354 N PHE A 331
SHEET 7 C 8 ALA A 488 ALA A 493 1 O VAL A 491 N SER A 357
SHEET 8 C 8 LYS A 515 ILE A 519 1 O GLY A 517 N THR A 492
CISPEP 1 LEU A 16 PRO A 17 0 -0.09
CISPEP 2 LYS A 160 PRO A 161 0 0.53
CISPEP 3 PHE A 267 PRO A 268 0 -0.49
CRYST1 92.546 92.546 244.637 90.00 90.00 120.00 P 65 2 2 12
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 0.010805 0.006239 0.000000 0.00000
SCALE2 0.000000 0.012477 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004088 0.00000
TER 4317 ASN A 548
MASTER 395 0 1 33 15 0 0 6 4381 1 19 43
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