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HEADER HYDROLASE 14-APR-05 1ZD2
TITLE HUMAN SOLUBLE EPOXIDE HYDROLASE 4-(3-CYCLOHEXYLURIEDO)-
TITLE 2 ETHANOIC ACID COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPOXIDE HYDROLASE 2, CYTOPLASMIC;
COMPND 3 CHAIN: P;
COMPND 4 EC: 3.3.2.3;
COMPND 5 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: SF9;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: ACHSEH1
KEYWDS DOMAIN-SWAPPED DIMER
EXPDTA X-RAY DIFFRACTION
AUTHOR G.A.GOMEZ,C.MORISSEAU,B.D.HAMMOCK,D.W.CHRISTIANSON
REVDAT 1 07-MAR-06 1ZD2 0
JRNL AUTH G.A.GOMEZ,C.MORISSEAU,B.D.HAMMOCK,D.W.CHRISTIANSON
JRNL TITL HUMAN SOLUBLE EPOXIDE HYDROLASE: STRUCTURAL BASIS
JRNL TITL 2 OF INHIBITION BY 4-(3-CYCLOHEXYLUREIDO)-CARBOXYLIC
JRNL TITL 3 ACIDS
JRNL REF PROTEIN SCI. V. 15 58 2006
JRNL REFN ASTM PRCIEI US ISSN 0961-8368
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
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) (%) : 95.1
REMARK 3 NUMBER OF REFLECTIONS : 12377
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) : 0.233
REMARK 3 FREE R VALUE : 0.283
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 892
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4331
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 18
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
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) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.40
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.00
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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: NULL
REMARK 4
REMARK 4 1ZD2 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-APR-2005.
REMARK 100 THE RCSB ID CODE IS RCSB032587.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-DEC-2004
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 : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : SINGLE CRYSTAL, CYLINDRICALLY
REMARK 200 BENT, ASYMMETRICALLY CUT
REMARK 200 SI(220) CRYSTAL
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 : 12983
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 9.200
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.30
REMARK 200 R MERGE FOR SHELL (I) : 0.46000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.000
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 1S8O
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, TRIS, N-HEXADECYL-B-D-
REMARK 280 MALTOSIDE, PH 8.4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 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 162.24000
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 81.12000
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 121.68000
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 40.56000
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 202.80000
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 162.24000
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 81.12000
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 40.56000
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 121.68000
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 202.80000
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: P
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 -92.24000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 121.68000
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 P 1
REMARK 465 PRO P 548
REMARK 465 PRO P 549
REMARK 465 VAL P 550
REMARK 465 VAL P 551
REMARK 465 SER P 552
REMARK 465 LYS P 553
REMARK 465 MET P 554
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 OE1 GLU P 252 OE1 GLU P 252 11455 2.01
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 P 105 SD MET P 105 CE -0.057
REMARK 500 MET P 111 SD MET P 111 CE 0.072
REMARK 500 MET P 145 SD MET P 145 CE 0.112
REMARK 500 ASP P 380 CB ASP P 380 CG -0.058
REMARK 500 TYR P 381 CD1 TYR P 381 CE1 0.081
REMARK 500 TYR P 381 CE2 TYR P 381 CD2 0.054
REMARK 500 VAL P 415 CA VAL P 415 CB 0.061
REMARK 500 MET P 418 SD MET P 418 CE 0.086
REMARK 500 MET P 468 SD MET P 468 CE 0.068
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 THR P 118 N - CA - C ANGL. DEV. = -9.5 DEGREES
REMARK 500 PRO P 161 C - N - CA ANGL. DEV. = 55.9 DEGREES
REMARK 500 LEU P 183 CA - CB - CG ANGL. DEV. = 10.5 DEGREES
REMARK 500 ASP P 290 N - CA - C ANGL. DEV. =-16.1 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 P 357 -53.05 73.46
REMARK 500 VAL P 415 6.97 114.61
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: 1ZD3 RELATED DB: PDB
REMARK 900 HUMAN SOLUBLE EPOXIDE HYDROLASE 4-(3-CYCLOHEXYLURIEDO)-
REMARK 900 BUTYRIC ACID COMPLEX
REMARK 900 RELATED ID: 1ZD4 RELATED DB: PDB
REMARK 900 HUMAN SOLUBLE EPOXIDE HYDROLASE 4-(3-CYCLOHEXYLURIEDO)-
REMARK 900 HEXANOIC ACID COMPLEX
REMARK 900 RELATED ID: 1ZD5 RELATED DB: PDB
REMARK 900 HUMAN SOLUBLE EPOXIDE HYDROLASE 4-(3-CYCLOHEXYLURIEDO)-
REMARK 900 HEPTANOIC ACID COMPLEX
DBREF 1ZD2 P 1 554 GB 30582609 AAP35531 1 555
SEQRES 1 P 555 MET THR LEU ARG ALA ALA VAL PHE ASP LEU ASP GLY VAL
SEQRES 2 P 555 LEU ALA LEU PRO ALA VAL PHE GLY VAL LEU GLY ARG THR
SEQRES 3 P 555 GLU GLU ALA LEU ALA LEU PRO ARG GLY LEU LEU ASN ASP
SEQRES 4 P 555 ALA PHE GLN LYS GLY GLY PRO GLU GLY ALA THR THR ARG
SEQRES 5 P 555 LEU MET LYS GLY GLU ILE THR LEU SER GLN TRP ILE PRO
SEQRES 6 P 555 LEU MET GLU GLU ASN CYS ARG LYS CYS SER GLU THR ALA
SEQRES 7 P 555 LYS VAL CYS LEU PRO LYS ASN PHE SER ILE LYS GLU ILE
SEQRES 8 P 555 PHE ASP LYS ALA ILE SER ALA ARG LYS ILE ASN ARG PRO
SEQRES 9 P 555 MET LEU GLN ALA ALA LEU MET LEU ARG LYS LYS GLY PHE
SEQRES 10 P 555 THR THR ALA ILE LEU THR ASN THR TRP LEU ASP ASP ARG
SEQRES 11 P 555 ALA GLU ARG ASP GLY LEU ALA GLN LEU MET CYS GLU LEU
SEQRES 12 P 555 LYS MET HIS PHE ASP PHE LEU ILE GLU SER CYS GLN VAL
SEQRES 13 P 555 GLY MET VAL LYS PRO GLU PRO GLN ILE TYR LYS PHE LEU
SEQRES 14 P 555 LEU ASP THR LEU LYS ALA SER PRO SER GLU VAL VAL PHE
SEQRES 15 P 555 LEU ASP ASP ILE GLY ALA ASN LEU LYS PRO ALA ARG ASP
SEQRES 16 P 555 LEU GLY MET VAL THR ILE LEU VAL GLN ASP THR ASP THR
SEQRES 17 P 555 ALA LEU LYS GLU LEU GLU LYS VAL THR GLY ILE GLN LEU
SEQRES 18 P 555 LEU ASN THR PRO ALA PRO LEU PRO THR SER CYS ASN PRO
SEQRES 19 P 555 SER ASP MET SER HIS GLY TYR VAL THR VAL LYS PRO ARG
SEQRES 20 P 555 VAL ARG LEU HIS PHE VAL GLU LEU GLY SER GLY PRO ALA
SEQRES 21 P 555 VAL CYS LEU CYS HIS GLY PHE PRO GLU SER TRP TYR SER
SEQRES 22 P 555 TRP ARG TYR GLN ILE PRO ALA LEU ALA GLN ALA GLY TYR
SEQRES 23 P 555 ARG VAL LEU ALA MET ASP MET LYS GLY TYR GLY GLU SER
SEQRES 24 P 555 SER ALA PRO PRO GLU ILE GLU GLU TYR CYS MET GLU VAL
SEQRES 25 P 555 LEU CYS LYS GLU MET VAL THR PHE LEU ASP LYS LEU GLY
SEQRES 26 P 555 LEU SER GLN ALA VAL PHE ILE GLY HIS ASP TRP GLY GLY
SEQRES 27 P 555 MET LEU VAL TRP TYR MET ALA LEU PHE TYR PRO GLU ARG
SEQRES 28 P 555 VAL ARG ALA VAL ALA SER LEU ASN THR PRO PHE ILE PRO
SEQRES 29 P 555 ALA ASN PRO ASN MET SER PRO LEU GLU SER ILE LYS ALA
SEQRES 30 P 555 ASN PRO VAL PHE ASP TYR GLN LEU TYR PHE GLN GLU PRO
SEQRES 31 P 555 GLY VAL ALA GLU ALA GLU LEU GLU GLN ASN LEU SER ARG
SEQRES 32 P 555 THR PHE LYS SER LEU PHE ARG ALA SER ASP GLU SER VAL
SEQRES 33 P 555 LEU SER MET HIS LYS VAL CYS GLU ALA GLY GLY LEU PHE
SEQRES 34 P 555 VAL ASN SER PRO GLU GLU PRO SER LEU SER ARG MET VAL
SEQRES 35 P 555 THR GLU GLU GLU ILE GLN PHE TYR VAL GLN GLN PHE LYS
SEQRES 36 P 555 LYS SER GLY PHE ARG GLY PRO LEU ASN TRP TYR ARG ASN
SEQRES 37 P 555 MET GLU ARG ASN TRP LYS TRP ALA CYS LYS SER LEU GLY
SEQRES 38 P 555 ARG LYS ILE LEU ILE PRO ALA LEU MET VAL THR ALA GLU
SEQRES 39 P 555 LYS ASP PHE VAL LEU VAL PRO GLN MET SER GLN HIS MET
SEQRES 40 P 555 GLU ASP TRP ILE PRO HIS LEU LYS ARG GLY HIS ILE GLU
SEQRES 41 P 555 ASP CYS GLY HIS TRP THR GLN MET ASP LYS PRO THR GLU
SEQRES 42 P 555 VAL ASN GLN ILE LEU ILE LYS TRP LEU ASP SER ASP ALA
SEQRES 43 P 555 ARG ASN PRO PRO VAL VAL SER LYS MET
HET MG 800 1
HET PO4 900 5
HET NC3 700 14
HETNAM MG MAGNESIUM ION
HETNAM PO4 PHOSPHATE ION
HETNAM NC3 N-[(CYCLOHEXYLAMINO)CARBONYL]GLYCINE
HETSYN NC3 4-(3-CYCLOHEXYLURIEDO)-ETHANOIC ACID
FORMUL 2 MG MG1 2+
FORMUL 3 PO4 O4 P1 3-
FORMUL 4 NC3 C9 H16 N2 O3
FORMUL 5 HOH *18(H2 O1)
HELIX 1 1 GLY P 21 LEU P 30 1 10
HELIX 2 2 GLY P 35 GLN P 42 1 8
HELIX 3 3 GLY P 44 GLU P 47 5 4
HELIX 4 4 GLY P 48 LYS P 55 1 8
HELIX 5 5 THR P 59 ALA P 78 1 20
HELIX 6 6 SER P 87 ARG P 99 1 13
HELIX 7 7 ASN P 102 LYS P 115 1 14
HELIX 8 8 ARG P 133 LYS P 144 1 12
HELIX 9 9 MET P 145 PHE P 147 5 3
HELIX 10 10 SER P 153 GLY P 157 1 5
HELIX 11 11 GLU P 162 LYS P 174 1 13
HELIX 12 12 SER P 176 SER P 178 5 3
HELIX 13 13 LEU P 190 LEU P 196 1 7
HELIX 14 14 ASP P 205 GLY P 218 1 14
HELIX 15 15 ASN P 231 MET P 235 5 5
HELIX 16 16 SER P 268 ARG P 273 5 6
HELIX 17 17 TYR P 274 ALA P 282 1 9
HELIX 18 18 ILE P 303 TYR P 306 5 4
HELIX 19 19 CYS P 307 GLY P 323 1 17
HELIX 20 20 ASP P 333 TYR P 346 1 14
HELIX 21 21 PRO P 347 VAL P 350 5 4
HELIX 22 22 SER P 368 ALA P 375 1 8
HELIX 23 23 ASN P 376 VAL P 378 5 3
HELIX 24 24 PHE P 379 TYR P 384 1 6
HELIX 25 25 GLY P 389 ASN P 398 1 10
HELIX 26 26 ASN P 398 PHE P 407 1 10
HELIX 27 27 LYS P 420 GLY P 425 1 6
HELIX 28 28 THR P 442 GLY P 457 1 16
HELIX 29 29 PHE P 458 ASN P 463 1 6
HELIX 30 30 TRP P 464 ARG P 466 5 3
HELIX 31 31 ASN P 467 CYS P 476 1 10
HELIX 32 32 LYS P 477 LEU P 479 5 3
HELIX 33 33 VAL P 499 GLN P 504 5 6
HELIX 34 34 HIS P 505 TRP P 509 5 5
HELIX 35 35 TRP P 524 LYS P 529 1 6
HELIX 36 36 LYS P 529 ALA P 545 1 17
SHEET 1 A 5 PHE P 149 GLU P 152 0
SHEET 2 A 5 THR P 118 THR P 123 1 N THR P 123 O ILE P 151
SHEET 3 A 5 ALA P 5 PHE P 8 1 N PHE P 8 O ALA P 120
SHEET 4 A 5 VAL P 180 ASP P 184 1 O VAL P 181 N ALA P 5
SHEET 5 A 5 VAL P 199 LEU P 202 1 O VAL P 199 N PHE P 182
SHEET 1 B 2 ALA P 15 LEU P 16 0
SHEET 2 B 2 LYS P 100 ILE P 101 -1 O LYS P 100 N LEU P 16
SHEET 1 C 8 SER P 236 LYS P 243 0
SHEET 2 C 8 VAL P 246 GLY P 254 -1 O PHE P 250 N GLY P 238
SHEET 3 C 8 ARG P 285 ASP P 290 -1 O ALA P 288 N VAL P 251
SHEET 4 C 8 ALA P 258 CYS P 262 1 N VAL P 259 O LEU P 287
SHEET 5 C 8 VAL P 328 HIS P 332 1 O VAL P 328 N CYS P 260
SHEET 6 C 8 ALA P 352 LEU P 356 1 O ALA P 354 N GLY P 331
SHEET 7 C 8 ALA P 487 ALA P 492 1 O VAL P 490 N SER P 355
SHEET 8 C 8 LYS P 514 ILE P 518 1 O GLY P 516 N THR P 491
CISPEP 1 LEU P 16 PRO P 17 0 2.55
CISPEP 2 PHE P 265 PRO P 266 0 -0.02
CRYST1 92.240 92.240 243.360 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 0.010841 0.006259 0.000000 0.00000
SCALE2 0.000000 0.012518 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004109 0.00000
TER 4332 ASN P 547
MASTER 350 0 3 36 15 0 0 6 4369 1 19 43
END |