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HEADER HYDROLASE 05-MAR-15 5AKY
TITLE LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIFUNCTIONAL EPOXIDE HYDROLASE 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CYTOSOLIC EPOXIDE HYDROLASE 2, CEH, EPOXIDE HYDRATASE,
COMPND 5 SOLUBLE EPOXIDE HYDROLASE, SEH, LIPID-PHOSPHATE PHOSPHATASE;
COMPND 6 EC: 3.3.2.10, 3.1.3.76;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.OSTER,S.TAPANI,Y.XUE,H.KACK
REVDAT 1 13-MAY-15 5AKY 0
JRNL AUTH L.OSTER,S.TAPANI,Y.XUE,H.KACK
JRNL TITL SUCCESSFUL GENERATION OF STRUCTURAL INFORMATION FOR
JRNL TITL 2 FRAGMENT-BASED DRUG DISCOVERY.
JRNL REF DRUG DISCOV TODAY 2015
JRNL REFN ESSN 1878-5832
JRNL PMID 25931264
JRNL DOI 10.1016/J.DRUDIS.2015.04.005
REMARK 2
REMARK 2 RESOLUTION. 2.18 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.1
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.18
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.26
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.29
REMARK 3 NUMBER OF REFLECTIONS : 32967
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) : 0.1816
REMARK 3 R VALUE (WORKING SET) : 0.1798
REMARK 3 FREE R VALUE : 0.2156
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.11
REMARK 3 FREE R VALUE TEST SET COUNT : 1684
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 : 17
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.18
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.25
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.29
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2770
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2125
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2624
REMARK 3 BIN R VALUE (WORKING SET) : 0.2098
REMARK 3 BIN FREE R VALUE : 0.2588
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.27
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 146
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 : 4323
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 51
REMARK 3 SOLVENT ATOMS : 375
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.49
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.7964
REMARK 3 B22 (A**2) : -0.7964
REMARK 3 B33 (A**2) : 1.5928
REMARK 3 B12 (A**2) : 0.0000
REMARK 3 B13 (A**2) : 0.0000
REMARK 3 B23 (A**2) : 0.0000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.264
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.186
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.232
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.179
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.9449
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.9303
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4553 ; 2.00 ; HARMONIC
REMARK 3 BOND ANGLES : 6172 ; 2.00 ; HARMONIC
REMARK 3 TORSION ANGLES : 1570 ; 2.00 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 120 ; 2.00 ; HARMONIC
REMARK 3 GENERAL PLANES : 651 ; 5.00 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4553 ; 20.00 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 567 ; 5.00 ; SEMIHARMONI
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 5530 ; 4.00 ; SEMIHARMONI
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.15
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.20
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.91
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP.
REMARK 3 ALL ATOMS HAVE CCP4 ATOM TYPE FROM LIBRARY
REMARK 4
REMARK 4 5AKY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-MAR-15.
REMARK 100 THE PDBE ID CODE IS EBI-63216.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : FRE PLUS RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (A200-CU)
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33015
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.18
REMARK 200 RESOLUTION RANGE LOW (A) : 46.26
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 11.5
REMARK 200 R MERGE (I) : 0.16
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.18
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.6
REMARK 200 R MERGE FOR SHELL (I) : 1.15
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.40
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 5AHX
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 162.69067
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 81.34533
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 122.01800
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 40.67267
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 203.36333
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 162.69067
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 81.34533
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 40.67267
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 122.01800
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 203.36333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.9 KCAL/MOL
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 0.500000 -0.866025 0.000000 -46.26500
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 -80.13333
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 40.67267
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 GLY A 0
REMARK 465 MET A 1
REMARK 465 ASN A 548
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 OD1 ASP A 322 NH2 ARG A 351 2.05
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 LEU A 10 -69.79 -96.77
REMARK 500 VAL A 13 -71.05 -124.59
REMARK 500 GLN A 204 -89.58 -109.29
REMARK 500 GLU A 269 -145.21 -112.23
REMARK 500 ASP A 335 -119.91 57.54
REMARK 500 ASN A 359 -45.28 69.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 GLU A 269 24.8 L L OUTSIDE RANGE
REMARK 500 VAL A 312 22.1 L L OUTSIDE RANGE
REMARK 500 VAL A 380 24.7 L L OUTSIDE RANGE
REMARK 500 LEU A 480 24.9 L L OUTSIDE RANGE
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 SO4 A1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A1549
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A1551
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6NJ A1552
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6NJ A1553
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5AK3 RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5AK4 RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5AK5 RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5AK6 RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5AKE RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5AKG RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5AKH RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5AKI RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5AKJ RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5AKK RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5AKL RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5AKX RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5AKZ RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5ALD RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5ALE RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5ALF RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5ALG RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5ALH RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5ALI RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5ALJ RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5ALK RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5ALL RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5ALM RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5ALN RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5ALO RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5ALP RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5ALQ RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5ALR RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5ALS RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5ALT RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5ALU RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5ALV RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5ALW RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5ALX RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5ALY RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5ALZ RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5AM0 RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5AM1 RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5AM2 RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5AM3 RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5AM4 RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5AM5 RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
DBREF 5AKY A 1 548 UNP P34913 HYES_HUMAN 1 548
SEQADV 5AKY GLY A 0 UNP P34913 EXPRESSION TAG
SEQRES 1 A 549 GLY MET THR LEU ARG ALA ALA VAL PHE ASP LEU ASP GLY
SEQRES 2 A 549 VAL LEU ALA LEU PRO ALA VAL PHE GLY VAL LEU GLY ARG
SEQRES 3 A 549 THR GLU GLU ALA LEU ALA LEU PRO ARG GLY LEU LEU ASN
SEQRES 4 A 549 ASP ALA PHE GLN LYS GLY GLY PRO GLU GLY ALA THR THR
SEQRES 5 A 549 ARG LEU MET LYS GLY GLU ILE THR LEU SER GLN TRP ILE
SEQRES 6 A 549 PRO LEU MET GLU GLU ASN CYS ARG LYS CYS SER GLU THR
SEQRES 7 A 549 ALA LYS VAL CYS LEU PRO LYS ASN PHE SER ILE LYS GLU
SEQRES 8 A 549 ILE PHE ASP LYS ALA ILE SER ALA ARG LYS ILE ASN ARG
SEQRES 9 A 549 PRO MET LEU GLN ALA ALA LEU MET LEU ARG LYS LYS GLY
SEQRES 10 A 549 PHE THR THR ALA ILE LEU THR ASN THR TRP LEU ASP ASP
SEQRES 11 A 549 ARG ALA GLU ARG ASP GLY LEU ALA GLN LEU MET CYS GLU
SEQRES 12 A 549 LEU LYS MET HIS PHE ASP PHE LEU ILE GLU SER CYS GLN
SEQRES 13 A 549 VAL GLY MET VAL LYS PRO GLU PRO GLN ILE TYR LYS PHE
SEQRES 14 A 549 LEU LEU ASP THR LEU LYS ALA SER PRO SER GLU VAL VAL
SEQRES 15 A 549 PHE LEU ASP ASP ILE GLY ALA ASN LEU LYS PRO ALA ARG
SEQRES 16 A 549 ASP LEU GLY MET VAL THR ILE LEU VAL GLN ASP THR ASP
SEQRES 17 A 549 THR ALA LEU LYS GLU LEU GLU LYS VAL THR GLY ILE GLN
SEQRES 18 A 549 LEU LEU ASN THR PRO ALA PRO LEU PRO THR SER CYS ASN
SEQRES 19 A 549 PRO SER ASP MET SER HIS GLY TYR VAL THR VAL LYS PRO
SEQRES 20 A 549 ARG VAL ARG LEU HIS PHE VAL GLU LEU GLY SER GLY PRO
SEQRES 21 A 549 ALA VAL CYS LEU CYS HIS GLY PHE PRO GLU SER TRP TYR
SEQRES 22 A 549 SER TRP ARG TYR GLN ILE PRO ALA LEU ALA GLN ALA GLY
SEQRES 23 A 549 TYR ARG VAL LEU ALA MET ASP MET LYS GLY TYR GLY GLU
SEQRES 24 A 549 SER SER ALA PRO PRO GLU ILE GLU GLU TYR CYS MET GLU
SEQRES 25 A 549 VAL LEU CYS LYS GLU MET VAL THR PHE LEU ASP LYS LEU
SEQRES 26 A 549 GLY LEU SER GLN ALA VAL PHE ILE GLY HIS ASP TRP GLY
SEQRES 27 A 549 GLY MET LEU VAL TRP TYR MET ALA LEU PHE TYR PRO GLU
SEQRES 28 A 549 ARG VAL ARG ALA VAL ALA SER LEU ASN THR PRO PHE ILE
SEQRES 29 A 549 PRO ALA ASN PRO ASN MET SER PRO LEU GLU SER ILE LYS
SEQRES 30 A 549 ALA ASN PRO VAL PHE ASP TYR GLN LEU TYR PHE GLN GLU
SEQRES 31 A 549 PRO GLY VAL ALA GLU ALA GLU LEU GLU GLN ASN LEU SER
SEQRES 32 A 549 ARG THR PHE LYS SER LEU PHE ARG ALA SER ASP GLU SER
SEQRES 33 A 549 VAL LEU SER MET HIS LYS VAL CYS GLU ALA GLY GLY LEU
SEQRES 34 A 549 PHE VAL ASN SER PRO GLU GLU PRO SER LEU SER ARG MET
SEQRES 35 A 549 VAL THR GLU GLU GLU ILE GLN PHE TYR VAL GLN GLN PHE
SEQRES 36 A 549 LYS LYS SER GLY PHE ARG GLY PRO LEU ASN TRP TYR ARG
SEQRES 37 A 549 ASN MET GLU ARG ASN TRP LYS TRP ALA CYS LYS SER LEU
SEQRES 38 A 549 GLY ARG LYS ILE LEU ILE PRO ALA LEU MET VAL THR ALA
SEQRES 39 A 549 GLU LYS ASP PHE VAL LEU VAL PRO GLN MET SER GLN HIS
SEQRES 40 A 549 MET GLU ASP TRP ILE PRO HIS LEU LYS ARG GLY HIS ILE
SEQRES 41 A 549 GLU ASP CYS GLY HIS TRP THR GLN MET ASP LYS PRO THR
SEQRES 42 A 549 GLU VAL ASN GLN ILE LEU ILE LYS TRP LEU ASP SER ASP
SEQRES 43 A 549 ALA ARG ASN
HET SO4 A1548 5
HET DMS A1549 4
HET DMS A1550 4
HET DMS A1551 4
HET 6NJ A1552 17
HET 6NJ A1553 34
HETNAM 6NJ 3-(2-PHENYLETHYL)-1H-INDAZOLE
HETNAM SO4 SULFATE ION
HETNAM DMS DIMETHYL SULFOXIDE
FORMUL 2 6NJ 2(C15 H14 N2)
FORMUL 3 SO4 O4 S 2-
FORMUL 4 DMS 3(C2 H6 O S)
FORMUL 5 HOH *375(H2 O)
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 ARG A 133 MET A 145 1 13
HELIX 10 10 SER A 153 GLY A 157 1 5
HELIX 11 11 GLU A 162 LYS A 174 1 13
HELIX 12 12 SER A 176 SER A 178 5 3
HELIX 13 13 ILE A 186 LEU A 196 1 11
HELIX 14 14 ASP A 205 GLY A 218 1 14
HELIX 15 15 ASN A 233 MET A 237 5 5
HELIX 16 16 SER A 270 ARG A 275 5 6
HELIX 17 17 GLN A 277 ALA A 284 1 8
HELIX 18 18 GLU A 304 TYR A 308 5 5
HELIX 19 19 CYS A 309 GLY A 325 1 17
HELIX 20 20 ASP A 335 TYR A 348 1 14
HELIX 21 21 SER A 370 ALA A 377 1 8
HELIX 22 22 ASN A 378 VAL A 380 5 3
HELIX 23 23 PHE A 381 PHE A 387 1 7
HELIX 24 24 GLY A 391 GLN A 399 1 9
HELIX 25 25 ASN A 400 PHE A 409 1 10
HELIX 26 26 LYS A 421 GLY A 426 1 6
HELIX 27 27 THR A 443 LYS A 455 1 13
HELIX 28 28 PHE A 459 TRP A 465 1 7
HELIX 29 29 ASN A 468 CYS A 477 1 10
HELIX 30 30 LYS A 478 LEU A 480 5 3
HELIX 31 31 VAL A 500 GLN A 505 5 6
HELIX 32 32 HIS A 506 TRP A 510 5 5
HELIX 33 33 TRP A 525 LYS A 530 1 6
HELIX 34 34 LYS A 530 ALA A 546 1 17
SHEET 1 AA 5 PHE A 149 GLU A 152 0
SHEET 2 AA 5 THR A 118 THR A 123 1 O THR A 119 N PHE A 149
SHEET 3 AA 5 ALA A 5 PHE A 8 1 O ALA A 6 N ALA A 120
SHEET 4 AA 5 VAL A 180 ASP A 184 1 O VAL A 181 N VAL A 7
SHEET 5 AA 5 VAL A 199 LEU A 202 1 O VAL A 199 N PHE A 182
SHEET 1 AB 2 ALA A 15 LEU A 16 0
SHEET 2 AB 2 LYS A 100 ILE A 101 -1 O LYS A 100 N LEU A 16
SHEET 1 AC 8 SER A 238 LYS A 245 0
SHEET 2 AC 8 VAL A 248 LEU A 255 -1 O VAL A 248 N VAL A 244
SHEET 3 AC 8 ARG A 287 MET A 291 -1 O VAL A 288 N LEU A 255
SHEET 4 AC 8 ALA A 260 CYS A 264 1 O VAL A 261 N LEU A 289
SHEET 5 AC 8 ALA A 329 HIS A 334 1 O VAL A 330 N CYS A 262
SHEET 6 AC 8 VAL A 352 LEU A 358 1 N ARG A 353 O ALA A 329
SHEET 7 AC 8 ALA A 488 ALA A 493 1 O LEU A 489 N SER A 357
SHEET 8 AC 8 LYS A 515 ILE A 519 1 O LYS A 515 N MET A 490
CISPEP 1 LEU A 16 PRO A 17 0 -5.22
CISPEP 2 LYS A 160 PRO A 161 0 9.97
CISPEP 3 PHE A 267 PRO A 268 0 -6.11
SITE 1 AC1 8 LEU A 228 ARG A 440 MET A 441 VAL A 442
SITE 2 AC1 8 THR A 443 GLU A 446 HOH A2200 HOH A2201
SITE 1 AC2 4 LYS A 144 PHE A 147 HOH A2107 HOH A2230
SITE 1 AC3 3 LEU A 3 LYS A 115 GLY A 116
SITE 1 AC4 5 TYR A 343 TRP A 473 ALA A 476 6NJ A1553
SITE 2 AC4 5 HOH A2315
SITE 1 AC5 11 PHE A 267 ASP A 335 TYR A 383 LEU A 408
SITE 2 AC5 11 MET A 419 ASP A 496 VAL A 498 HIS A 524
SITE 3 AC5 11 TRP A 525 HOH A2193 HOH A2338
SITE 1 AC6 11 ASP A 335 TRP A 336 PRO A 371 ILE A 375
SITE 2 AC6 11 PHE A 381 TYR A 383 GLN A 384 MET A 469
SITE 3 AC6 11 DMS A1551 HOH A2247 HOH A2315
CRYST1 92.530 92.530 244.036 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 0.010807 0.006240 0.000000 0.00000
SCALE2 0.000000 0.012479 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004098 0.00000
TER 4372 ARG A 547
MASTER 426 0 6 34 15 0 12 6 4814 1 68 43
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