| content |
HEADER HYDROLASE 11-FEB-15 5AI0
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: SOLUBLE EPOXIDE HYDROLASE, SEH;
COMPND 5 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 5AI0 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. 1.75 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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.67
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.91
REMARK 3 NUMBER OF REFLECTIONS : 63714
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) : 0.2021
REMARK 3 FREE R VALUE : 0.2321
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.09
REMARK 3 FREE R VALUE TEST SET COUNT : 3240
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 : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.79
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.91
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4376
REMARK 3 BIN R VALUE (WORKING SET) : 0.4137
REMARK 3 BIN FREE R VALUE : 0.3853
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.24
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 242
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 : 4324
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 518
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.01
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.6690
REMARK 3 B22 (A**2) : 0.6690
REMARK 3 B33 (A**2) : -1.3380
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 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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 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 5AI0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-FEB-15.
REMARK 100 THE PDBE ID CODE IS EBI-63021.
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) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63827
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.75
REMARK 200 RESOLUTION RANGE LOW (A) : 50.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.8
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 10.5
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 23.10
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.9
REMARK 200 R MERGE FOR SHELL (I) : 1.32
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.80
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 (%): 48.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
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 163.51533
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 81.75767
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 122.63650
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 40.87883
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 204.39417
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 163.51533
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 81.75767
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 40.87883
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 122.63650
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 204.39417
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: 7840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.2 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 45.86900
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 79.44744
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 40.87883
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASN A 548 CA C O CB CG OD1 ND2
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 O HOH A 2060 O HOH A 2188 2.06
REMARK 500 O HOH A 2206 O HOH A 2468 2.14
REMARK 500
REMARK 500 REMARK: NULL
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 O ARG A 34 O HOH A 2229 12564 2.05
REMARK 500 OD1 ASP A 39 NE ARG A 194 12564 2.07
REMARK 500 CB GLU A 68 NH1 ARG A 72 8675 2.16
REMARK 500 CG GLU A 68 NH2 ARG A 72 8675 1.98
REMARK 500 OD1 ASP A 236 NZ LYS A 323 10665 2.11
REMARK 500 N HIS A 239 O TYR A 241 10665 1.92
REMARK 500 O HIS A 239 N TYR A 241 10665 1.71
REMARK 500 N THR A 243 O HOH A 2266 10665 1.76
REMARK 500 N GLY A 256 O LEU A 324 10665 1.98
REMARK 500 O LYS A 323 O HOH A 2268 10665 1.82
REMARK 500 N SER A 327 O HOH A 2291 10665 2.13
REMARK 500 OE2 GLU A 350 O HOH A 2152 10665 1.97
REMARK 500 O LYS A 483 O HOH A 2140 10665 1.64
REMARK 500 O LEU A 485 O HOH A 2139 10665 2.16
REMARK 500 O HOH A 2047 O HOH A 2347 10665 2.12
REMARK 500 O HOH A 2048 O HOH A 2442 10665 1.76
REMARK 500 O HOH A 2097 O HOH A 2348 10665 1.85
REMARK 500 O HOH A 2164 O HOH A 2361 10665 2.05
REMARK 500 O HOH A 2192 O HOH A 2483 8665 2.03
REMARK 500 O HOH A 2197 O HOH A 2486 8665 1.90
REMARK 500 O HOH A 2290 O HOH A 2349 10665 2.14
REMARK 500 O HOH A 2292 O HOH A 2293 10665 1.27
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 -70.12 -91.22
REMARK 500 VAL A 13 -70.70 -121.03
REMARK 500 GLN A 204 -78.73 -108.73
REMARK 500 GLU A 269 -147.72 -113.28
REMARK 500 ASP A 335 -123.69 60.57
REMARK 500 ASN A 359 -45.58 74.90
REMARK 500 ASN A 431 45.57 -107.84
REMARK 500 GLU A 435 76.87 -119.31
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 LYS A 191 23.1 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 PEG A1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1549
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1551
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A1552
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A1553
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE JF6 A1554
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5AHX RELATED DB: PDB
REMARK 900 APO STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5AI4 RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5AI5 RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5AI6 RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5AI8 RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5AI9 RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5AIA RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5AIB RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
REMARK 900 RELATED ID: 5AIC RELATED DB: PDB
REMARK 900 LIGAND COMPLEX STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE
DBREF 5AI0 A 1 548 UNP P34913 HYES_HUMAN 1 548
SEQADV 5AI0 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 PEG A1548 7
HET PEG A1549 7
HET SO4 A1550 5
HET SO4 A1551 5
HET DMS A1552 4
HET DMS A1553 4
HET JF6 A1554 12
HETNAM JF6 4-PHENYL-1,2,5-OXADIAZOL-3-AMINE
HETNAM SO4 SULFATE ION
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 2 JF6 C8 H7 N3 O
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 4 DMS 2(C2 H6 O S)
FORMUL 5 PEG 2(C4 H10 O3)
FORMUL 6 HOH *518(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 GLY A 197 1 12
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 ASN A 378 1 9
HELIX 22 22 PHE A 381 PHE A 387 1 7
HELIX 23 23 GLY A 391 GLN A 399 1 9
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 456 1 14
HELIX 27 27 PHE A 459 TRP A 465 1 7
HELIX 28 28 ASN A 468 LYS A 478 1 11
HELIX 29 29 VAL A 500 GLN A 505 5 6
HELIX 30 30 HIS A 506 TRP A 510 5 5
HELIX 31 31 TRP A 525 LYS A 530 1 6
HELIX 32 32 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 ILE A 121 N ILE A 151
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 ASP A 292 -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 -8.08
CISPEP 2 LYS A 160 PRO A 161 0 9.82
CISPEP 3 PHE A 267 PRO A 268 0 -6.10
SITE 1 AC1 8 CYS A 141 LYS A 144 MET A 145 ASP A 322
SITE 2 AC1 8 LYS A 323 HOH A2345 HOH A2515 HOH A2516
SITE 1 AC2 9 LYS A 211 LEU A 222 ASN A 223 GLU A 398
SITE 2 AC2 9 GLY A 458 HOH A2248 HOH A2388 HOH A2420
SITE 3 AC2 9 HOH A2517
SITE 1 AC3 9 LEU A 228 TYR A 276 ARG A 440 MET A 441
SITE 2 AC3 9 VAL A 442 THR A 443 HOH A2307 HOH A2308
SITE 3 AC3 9 HOH A2309
SITE 1 AC4 3 ASN A 85 SER A 87 GLU A 90
SITE 1 AC5 3 LYS A 144 PHE A 147 HOH A2165
SITE 1 AC6 3 ASP A 335 TRP A 336 MET A 339
SITE 1 AC7 10 MET A 339 TYR A 343 ALA A 365 PRO A 371
SITE 2 AC7 10 MET A 469 ASN A 472 TRP A 473 ALA A 476
SITE 3 AC7 10 HOH A2369 HOH A2437
CRYST1 92.914 92.914 244.486 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 0.010763 0.006214 0.000000 0.00000
SCALE2 0.000000 0.012428 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004090 0.00000
TER 4325 ASN A 548
MASTER 399 0 7 32 15 0 14 6 4886 1 44 43
END |