| content |
HEADER HYDROLASE/HYDROLASE INHIBITOR 22-OCT-10 3PDC
TITLE CRYSTAL STRUCTURE OF HYDROLASE DOMAIN OF HUMAN SOLUBLE EPOXIDE
TITLE 2 HYDROLASE COMPLEXED WITH A BENZOXAZOLE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPOXIDE HYDROLASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: HYDROLASE DOMAIN (UNP RESIDUES 226 TO 548);
COMPND 5 SYNONYM: CYTOSOLIC EPOXIDE HYDROLASE, CEH, EPOXIDE HYDRATASE, SOLUBLE
COMPND 6 EPOXIDE HYDROLASE, SEH;
COMPND 7 EC: 3.3.2.10;
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: EPHX2;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS EPOXIDE HYDROLASE, HYDROLASE, HYPERTENSION, BETA BARREL, ALPHA/BETA
KEYWDS 2 HYDROLASE FOLD; EPOXIDE HYDROLASE FOLD, ACTS ON EPOXIDES (ALKENE
KEYWDS 3 OXIDES, OXIRANES) AND ARENE OXIDES. PLAYS A ROLE IN XENOBIOTIC
KEYWDS 4 METABOLISM BY DEGRADING POTENTIALLY TOXIC EPOXIDES. ALSO DETERMINES
KEYWDS 5 STEADY-STATE LEVELS OF PHYSIOLOGICAL MEDIATORS. HAS LOW PHOSPHATASE
KEYWDS 6 ACTIVITY, BINDS MG2+, ACETYLATION OF LYSINE, CYTOPLASM; PEROXISOME,
KEYWDS 7 HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.G.KURUMBAIL,J.M.WILLIAMS
REVDAT 1 06-APR-11 3PDC 0
JRNL AUTH L.XING,J.J.MCDONALD,S.A.KOLODZIEJ,R.G.KURUMBAIL,
JRNL AUTH 2 J.M.WILLIAMS,C.J.WARREN,J.M.O'NEAL,J.E.SKEPNER,S.L.ROBERDS
JRNL TITL DISCOVERY OF POTENT INHIBITORS OF SOLUBLE EPOXIDE HYDROLASE
JRNL TITL 2 BY COMBINATORIAL LIBRARY DESIGN AND STRUCTURE-BASED VIRTUAL
JRNL TITL 3 SCREENING.
JRNL REF J.MED.CHEM. V. 54 1211 2011
JRNL REFN ISSN 0022-2623
JRNL PMID 21302953
JRNL DOI 10.1021/JM101382T
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.0
REMARK 3 NUMBER OF REFLECTIONS : 18003
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 SELECTION OF 5% OF
REMARK 3 REFLECTIONS
REMARK 3 R VALUE (WORKING SET) : 0.279
REMARK 3 FREE R VALUE : 0.333
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 897
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 (A) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.72
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3720
REMARK 3 BIN FREE R VALUE : 0.4340
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 104
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 : 5196
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 191
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.99
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) : 0.43
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : 10.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.55
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : 22.80
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ISOTROPIC B FACTOR REFINEMENT
REMARK 4
REMARK 4 3PDC COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-OCT-10.
REMARK 100 THE RCSB ID CODE IS RCSB062239.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUN-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MIRROR
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 130 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18410
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.0
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : 0.12000
REMARK 200 FOR THE DATA SET : 6.8000
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 (%) : 80.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.38100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1S80
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26-30% PEG6K, 0.1M SODIUM CACODYLATE,
REMARK 280 0.07M AMMONIUM ACETATE, 0.1M MAGNESIUM ACETATE, PH 7.4, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 39.95100
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 ASYMMETRIC UNIT CONTAINS TWO COPIES OF THE BIOLOGICAL
REMARK 300 UNIT(UNIT 1)
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 203
REMARK 465 GLY A 204
REMARK 465 SER A 205
REMARK 465 SER A 206
REMARK 465 HIS A 207
REMARK 465 HIS A 208
REMARK 465 HIS A 209
REMARK 465 HIS A 210
REMARK 465 HIS A 211
REMARK 465 HIS A 212
REMARK 465 SER A 213
REMARK 465 SER A 214
REMARK 465 GLY A 215
REMARK 465 LEU A 216
REMARK 465 VAL A 217
REMARK 465 PRO A 218
REMARK 465 ARG A 219
REMARK 465 GLY A 220
REMARK 465 SER A 221
REMARK 465 HIS A 222
REMARK 465 MET A 223
REMARK 465 MET B 203
REMARK 465 GLY B 204
REMARK 465 SER B 205
REMARK 465 SER B 206
REMARK 465 HIS B 207
REMARK 465 HIS B 208
REMARK 465 HIS B 209
REMARK 465 HIS B 210
REMARK 465 HIS B 211
REMARK 465 HIS B 212
REMARK 465 SER B 213
REMARK 465 SER B 214
REMARK 465 GLY B 215
REMARK 465 LEU B 216
REMARK 465 VAL B 217
REMARK 465 PRO B 218
REMARK 465 ARG B 219
REMARK 465 GLY B 220
REMARK 465 SER B 221
REMARK 465 HIS B 222
REMARK 465 MET B 223
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 ARG A 408 CD - NE - CZ ANGL. DEV. = 10.0 DEGREES
REMARK 500 ARG A 408 NE - CZ - NH1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG A 408 NE - CZ - NH2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 LEU A 488 CA - CB - CG ANGL. DEV. = 14.0 DEGREES
REMARK 500 ARG B 408 CD - NE - CZ ANGL. DEV. = 9.4 DEGREES
REMARK 500 ARG B 408 NE - CZ - NH1 ANGL. DEV. = -7.2 DEGREES
REMARK 500 ARG B 408 NE - CZ - NH2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 LEU B 488 CA - CB - CG ANGL. DEV. = 13.9 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 SER A 229 -164.11 -104.83
REMARK 500 PRO A 266 76.91 -113.67
REMARK 500 GLU A 267 -142.66 -91.68
REMARK 500 SER A 268 -178.82 -176.53
REMARK 500 ASP A 290 51.31 -106.26
REMARK 500 MET A 291 135.45 -7.37
REMARK 500 PRO A 301 -18.72 -49.09
REMARK 500 ASP A 333 -119.71 61.18
REMARK 500 ASN A 357 -47.16 70.47
REMARK 500 PHE A 407 88.92 -64.94
REMARK 500 SER A 413 178.60 -47.18
REMARK 500 VAL A 415 -30.69 -166.59
REMARK 500 HIS A 419 -70.24 -118.48
REMARK 500 ASN A 430 58.83 -105.34
REMARK 500 LYS A 455 -87.37 -94.96
REMARK 500 SER A 478 -22.46 -178.12
REMARK 500 LEU A 479 -102.44 21.65
REMARK 500 LEU A 498 71.92 -112.79
REMARK 500 HIS A 512 50.69 -115.06
REMARK 500 TRP A 524 49.47 -78.40
REMARK 500 THR A 525 -46.02 -25.02
REMARK 500 ARG A 546 -31.94 -34.50
REMARK 500 SER B 229 -163.58 -105.53
REMARK 500 HIS B 263 -168.54 -76.65
REMARK 500 PRO B 266 77.89 -113.47
REMARK 500 GLU B 267 -142.77 -91.47
REMARK 500 SER B 268 -178.15 -176.21
REMARK 500 ARG B 273 -22.85 -39.64
REMARK 500 ASP B 290 51.81 -104.78
REMARK 500 MET B 291 134.92 -7.23
REMARK 500 PRO B 301 -18.63 -48.83
REMARK 500 ASP B 333 -119.64 61.42
REMARK 500 ASN B 357 -48.05 71.15
REMARK 500 PHE B 407 89.64 -65.90
REMARK 500 SER B 413 178.49 -47.87
REMARK 500 VAL B 415 -30.39 -166.23
REMARK 500 ASN B 430 58.91 -104.76
REMARK 500 LYS B 455 -87.63 -94.74
REMARK 500 SER B 478 -22.54 -178.21
REMARK 500 LEU B 479 -102.28 21.35
REMARK 500 LEU B 498 71.90 -113.19
REMARK 500 HIS B 512 50.95 -114.92
REMARK 500 TRP B 524 49.30 -77.93
REMARK 500 THR B 525 -46.15 -24.80
REMARK 500 ARG B 546 -31.65 -35.20
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 B1202 DISTANCE = 5.96 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZYI A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZYI B 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1S8O RELATED DB: PDB
REMARK 900 HUMAN SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 1VJ5 RELATED DB: PDB
REMARK 900 HUMAN SOLUBLE EPOXIDE HYDROLASE- N-CYCLOHEXYL-N'-(4-
REMARK 900 IODOPHENYL)UREA COMPLEX
REMARK 900 RELATED ID: 1ZD2 RELATED DB: PDB
REMARK 900 HUMAN SOLUBLE EPOXIDE HYDROLASE 4-(3-CYCLOHEXYLURIEDO)-
REMARK 900 ETHANOIC ACID COMPLEX
REMARK 900 RELATED ID: 3IIY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 3I28 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
DBREF 3PDC A 224 547 UNP P34913 HYES_HUMAN 226 548
DBREF 3PDC B 224 547 UNP P34913 HYES_HUMAN 226 548
SEQADV 3PDC MET A 203 UNP P34913 EXPRESSION TAG
SEQADV 3PDC GLY A 204 UNP P34913 EXPRESSION TAG
SEQADV 3PDC SER A 205 UNP P34913 EXPRESSION TAG
SEQADV 3PDC SER A 206 UNP P34913 EXPRESSION TAG
SEQADV 3PDC HIS A 207 UNP P34913 EXPRESSION TAG
SEQADV 3PDC HIS A 208 UNP P34913 EXPRESSION TAG
SEQADV 3PDC HIS A 209 UNP P34913 EXPRESSION TAG
SEQADV 3PDC HIS A 210 UNP P34913 EXPRESSION TAG
SEQADV 3PDC HIS A 211 UNP P34913 EXPRESSION TAG
SEQADV 3PDC HIS A 212 UNP P34913 EXPRESSION TAG
SEQADV 3PDC SER A 213 UNP P34913 EXPRESSION TAG
SEQADV 3PDC SER A 214 UNP P34913 EXPRESSION TAG
SEQADV 3PDC GLY A 215 UNP P34913 EXPRESSION TAG
SEQADV 3PDC LEU A 216 UNP P34913 EXPRESSION TAG
SEQADV 3PDC VAL A 217 UNP P34913 EXPRESSION TAG
SEQADV 3PDC PRO A 218 UNP P34913 EXPRESSION TAG
SEQADV 3PDC ARG A 219 UNP P34913 EXPRESSION TAG
SEQADV 3PDC GLY A 220 UNP P34913 EXPRESSION TAG
SEQADV 3PDC SER A 221 UNP P34913 EXPRESSION TAG
SEQADV 3PDC HIS A 222 UNP P34913 EXPRESSION TAG
SEQADV 3PDC MET A 223 UNP P34913 EXPRESSION TAG
SEQADV 3PDC MET B 203 UNP P34913 EXPRESSION TAG
SEQADV 3PDC GLY B 204 UNP P34913 EXPRESSION TAG
SEQADV 3PDC SER B 205 UNP P34913 EXPRESSION TAG
SEQADV 3PDC SER B 206 UNP P34913 EXPRESSION TAG
SEQADV 3PDC HIS B 207 UNP P34913 EXPRESSION TAG
SEQADV 3PDC HIS B 208 UNP P34913 EXPRESSION TAG
SEQADV 3PDC HIS B 209 UNP P34913 EXPRESSION TAG
SEQADV 3PDC HIS B 210 UNP P34913 EXPRESSION TAG
SEQADV 3PDC HIS B 211 UNP P34913 EXPRESSION TAG
SEQADV 3PDC HIS B 212 UNP P34913 EXPRESSION TAG
SEQADV 3PDC SER B 213 UNP P34913 EXPRESSION TAG
SEQADV 3PDC SER B 214 UNP P34913 EXPRESSION TAG
SEQADV 3PDC GLY B 215 UNP P34913 EXPRESSION TAG
SEQADV 3PDC LEU B 216 UNP P34913 EXPRESSION TAG
SEQADV 3PDC VAL B 217 UNP P34913 EXPRESSION TAG
SEQADV 3PDC PRO B 218 UNP P34913 EXPRESSION TAG
SEQADV 3PDC ARG B 219 UNP P34913 EXPRESSION TAG
SEQADV 3PDC GLY B 220 UNP P34913 EXPRESSION TAG
SEQADV 3PDC SER B 221 UNP P34913 EXPRESSION TAG
SEQADV 3PDC HIS B 222 UNP P34913 EXPRESSION TAG
SEQADV 3PDC MET B 223 UNP P34913 EXPRESSION TAG
SEQRES 1 A 344 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 344 LEU VAL PRO ARG GLY SER HIS MET ALA PRO LEU PRO THR
SEQRES 3 A 344 SER CYS ASN PRO SER ASP MET SER HIS GLY TYR VAL THR
SEQRES 4 A 344 VAL LYS PRO ARG VAL ARG LEU HIS PHE VAL GLU LEU GLY
SEQRES 5 A 344 SER GLY PRO ALA VAL CYS LEU CYS HIS GLY PHE PRO GLU
SEQRES 6 A 344 SER TRP TYR SER TRP ARG TYR GLN ILE PRO ALA LEU ALA
SEQRES 7 A 344 GLN ALA GLY TYR ARG VAL LEU ALA MET ASP MET LYS GLY
SEQRES 8 A 344 TYR GLY GLU SER SER ALA PRO PRO GLU ILE GLU GLU TYR
SEQRES 9 A 344 CYS MET GLU VAL LEU CYS LYS GLU MET VAL THR PHE LEU
SEQRES 10 A 344 ASP LYS LEU GLY LEU SER GLN ALA VAL PHE ILE GLY HIS
SEQRES 11 A 344 ASP TRP GLY GLY MET LEU VAL TRP TYR MET ALA LEU PHE
SEQRES 12 A 344 TYR PRO GLU ARG VAL ARG ALA VAL ALA SER LEU ASN THR
SEQRES 13 A 344 PRO PHE ILE PRO ALA ASN PRO ASN MET SER PRO LEU GLU
SEQRES 14 A 344 SER ILE LYS ALA ASN PRO VAL PHE ASP TYR GLN LEU TYR
SEQRES 15 A 344 PHE GLN GLU PRO GLY VAL ALA GLU ALA GLU LEU GLU GLN
SEQRES 16 A 344 ASN LEU SER ARG THR PHE LYS SER LEU PHE ARG ALA SER
SEQRES 17 A 344 ASP GLU SER VAL LEU SER MET HIS LYS VAL CYS GLU ALA
SEQRES 18 A 344 GLY GLY LEU PHE VAL ASN SER PRO GLU GLU PRO SER LEU
SEQRES 19 A 344 SER ARG MET VAL THR GLU GLU GLU ILE GLN PHE TYR VAL
SEQRES 20 A 344 GLN GLN PHE LYS LYS SER GLY PHE ARG GLY PRO LEU ASN
SEQRES 21 A 344 TRP TYR ARG ASN MET GLU ARG ASN TRP LYS TRP ALA CYS
SEQRES 22 A 344 LYS SER LEU GLY ARG LYS ILE LEU ILE PRO ALA LEU MET
SEQRES 23 A 344 VAL THR ALA GLU LYS ASP PHE VAL LEU VAL PRO GLN MET
SEQRES 24 A 344 SER GLN HIS MET GLU ASP TRP ILE PRO HIS LEU LYS ARG
SEQRES 25 A 344 GLY HIS ILE GLU ASP CYS GLY HIS TRP THR GLN MET ASP
SEQRES 26 A 344 LYS PRO THR GLU VAL ASN GLN ILE LEU ILE LYS TRP LEU
SEQRES 27 A 344 ASP SER ASP ALA ARG ASN
SEQRES 1 B 344 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 344 LEU VAL PRO ARG GLY SER HIS MET ALA PRO LEU PRO THR
SEQRES 3 B 344 SER CYS ASN PRO SER ASP MET SER HIS GLY TYR VAL THR
SEQRES 4 B 344 VAL LYS PRO ARG VAL ARG LEU HIS PHE VAL GLU LEU GLY
SEQRES 5 B 344 SER GLY PRO ALA VAL CYS LEU CYS HIS GLY PHE PRO GLU
SEQRES 6 B 344 SER TRP TYR SER TRP ARG TYR GLN ILE PRO ALA LEU ALA
SEQRES 7 B 344 GLN ALA GLY TYR ARG VAL LEU ALA MET ASP MET LYS GLY
SEQRES 8 B 344 TYR GLY GLU SER SER ALA PRO PRO GLU ILE GLU GLU TYR
SEQRES 9 B 344 CYS MET GLU VAL LEU CYS LYS GLU MET VAL THR PHE LEU
SEQRES 10 B 344 ASP LYS LEU GLY LEU SER GLN ALA VAL PHE ILE GLY HIS
SEQRES 11 B 344 ASP TRP GLY GLY MET LEU VAL TRP TYR MET ALA LEU PHE
SEQRES 12 B 344 TYR PRO GLU ARG VAL ARG ALA VAL ALA SER LEU ASN THR
SEQRES 13 B 344 PRO PHE ILE PRO ALA ASN PRO ASN MET SER PRO LEU GLU
SEQRES 14 B 344 SER ILE LYS ALA ASN PRO VAL PHE ASP TYR GLN LEU TYR
SEQRES 15 B 344 PHE GLN GLU PRO GLY VAL ALA GLU ALA GLU LEU GLU GLN
SEQRES 16 B 344 ASN LEU SER ARG THR PHE LYS SER LEU PHE ARG ALA SER
SEQRES 17 B 344 ASP GLU SER VAL LEU SER MET HIS LYS VAL CYS GLU ALA
SEQRES 18 B 344 GLY GLY LEU PHE VAL ASN SER PRO GLU GLU PRO SER LEU
SEQRES 19 B 344 SER ARG MET VAL THR GLU GLU GLU ILE GLN PHE TYR VAL
SEQRES 20 B 344 GLN GLN PHE LYS LYS SER GLY PHE ARG GLY PRO LEU ASN
SEQRES 21 B 344 TRP TYR ARG ASN MET GLU ARG ASN TRP LYS TRP ALA CYS
SEQRES 22 B 344 LYS SER LEU GLY ARG LYS ILE LEU ILE PRO ALA LEU MET
SEQRES 23 B 344 VAL THR ALA GLU LYS ASP PHE VAL LEU VAL PRO GLN MET
SEQRES 24 B 344 SER GLN HIS MET GLU ASP TRP ILE PRO HIS LEU LYS ARG
SEQRES 25 B 344 GLY HIS ILE GLU ASP CYS GLY HIS TRP THR GLN MET ASP
SEQRES 26 B 344 LYS PRO THR GLU VAL ASN GLN ILE LEU ILE LYS TRP LEU
SEQRES 27 B 344 ASP SER ASP ALA ARG ASN
HET ZYI A 1 19
HET ZYI B 2 19
HETNAM ZYI N-(5-CHLORO-1,3-BENZOXAZOL-2-YL)-2-CYCLOPENTYLACETAMIDE
FORMUL 3 ZYI 2(C14 H15 CL N2 O2)
FORMUL 5 HOH *191(H2 O)
HELIX 1 1 ASN A 231 MET A 235 5 5
HELIX 2 2 SER A 268 ARG A 273 5 6
HELIX 3 3 TYR A 274 ALA A 282 1 9
HELIX 4 4 GLU A 302 TYR A 306 5 5
HELIX 5 5 CYS A 307 GLY A 323 1 17
HELIX 6 6 ASP A 333 PHE A 345 1 13
HELIX 7 7 TYR A 346 GLU A 348 5 3
HELIX 8 8 ASN A 376 VAL A 378 5 3
HELIX 9 9 PHE A 379 GLU A 387 1 9
HELIX 10 10 GLY A 389 ASN A 398 1 10
HELIX 11 11 ASN A 398 PHE A 407 1 10
HELIX 12 12 ALA A 409 SER A 413 5 5
HELIX 13 13 LYS A 420 GLY A 425 1 6
HELIX 14 14 THR A 442 PHE A 453 1 12
HELIX 15 15 PHE A 458 TRP A 464 1 7
HELIX 16 16 ASN A 467 LYS A 477 1 11
HELIX 17 17 SER A 503 ASP A 508 5 6
HELIX 18 18 TRP A 524 LYS A 529 1 6
HELIX 19 19 LYS A 529 ASP A 542 1 14
HELIX 20 20 ASN B 231 MET B 235 5 5
HELIX 21 21 SER B 268 ARG B 273 5 6
HELIX 22 22 TYR B 274 ALA B 282 1 9
HELIX 23 23 GLU B 302 TYR B 306 5 5
HELIX 24 24 CYS B 307 GLY B 323 1 17
HELIX 25 25 ASP B 333 PHE B 345 1 13
HELIX 26 26 TYR B 346 GLU B 348 5 3
HELIX 27 27 ASN B 376 VAL B 378 5 3
HELIX 28 28 PHE B 379 GLU B 387 1 9
HELIX 29 29 GLY B 389 ASN B 398 1 10
HELIX 30 30 ASN B 398 PHE B 407 1 10
HELIX 31 31 ALA B 409 SER B 413 5 5
HELIX 32 32 LYS B 420 GLY B 425 1 6
HELIX 33 33 THR B 442 PHE B 453 1 12
HELIX 34 34 PHE B 458 TRP B 464 1 7
HELIX 35 35 ASN B 467 LYS B 477 1 11
HELIX 36 36 SER B 503 ASP B 508 5 6
HELIX 37 37 TRP B 524 LYS B 529 1 6
HELIX 38 38 LYS B 529 ASP B 542 1 14
SHEET 1 A 8 HIS A 237 LYS A 243 0
SHEET 2 A 8 VAL A 246 LEU A 253 -1 O VAL A 246 N VAL A 242
SHEET 3 A 8 ARG A 285 MET A 289 -1 O ALA A 288 N VAL A 251
SHEET 4 A 8 ALA A 258 CYS A 262 1 N LEU A 261 O LEU A 287
SHEET 5 A 8 ALA A 327 HIS A 332 1 O VAL A 328 N CYS A 260
SHEET 6 A 8 VAL A 350 LEU A 356 1 O ALA A 354 N PHE A 329
SHEET 7 A 8 ALA A 487 ALA A 492 1 O VAL A 490 N SER A 355
SHEET 8 A 8 LEU A 513 ILE A 518 1 O GLY A 516 N THR A 491
SHEET 1 B 8 HIS B 237 LYS B 243 0
SHEET 2 B 8 VAL B 246 LEU B 253 -1 O VAL B 246 N VAL B 242
SHEET 3 B 8 ARG B 285 MET B 289 -1 O ALA B 288 N VAL B 251
SHEET 4 B 8 ALA B 258 CYS B 262 1 N VAL B 259 O LEU B 287
SHEET 5 B 8 ALA B 327 HIS B 332 1 O VAL B 328 N CYS B 260
SHEET 6 B 8 VAL B 350 LEU B 356 1 O ALA B 354 N PHE B 329
SHEET 7 B 8 ALA B 487 ALA B 492 1 O VAL B 490 N SER B 355
SHEET 8 B 8 LEU B 513 ILE B 518 1 O GLY B 516 N THR B 491
CISPEP 1 PHE A 265 PRO A 266 0 -0.72
CISPEP 2 PHE B 265 PRO B 266 0 -0.77
SITE 1 AC1 10 PHE A 265 ASP A 333 MET A 337 TYR A 381
SITE 2 AC1 10 GLN A 382 LEU A 406 LEU A 427 TYR A 465
SITE 3 AC1 10 HIS A 523 TRP A 524
SITE 1 AC2 11 PHE B 265 ASP B 333 TRP B 334 THR B 358
SITE 2 AC2 11 TYR B 381 GLN B 382 LEU B 406 LEU B 427
SITE 3 AC2 11 TYR B 465 HIS B 523 TRP B 524
CRYST1 46.523 79.902 89.318 90.00 90.22 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.021495 0.000000 0.000084 0.00000
SCALE2 0.000000 0.012515 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011196 0.00000
TER 2599 ASN A 547
TER 5198 ASN B 547
MASTER 379 0 2 38 16 0 6 6 5425 2 38 54
END |