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HEADER HYDROLASE/HYDROLASE INHIBITOR 09-JAN-14 4OCZ
TITLE CRYSTAL STRUCTURE OF HUMAN SOLUBLE EPOXIDE HYDROLASE COMPLEXED WITH 1-
TITLE 2 (1-ISOBUTYRYLPIPERIDIN-4-YL)-3-(4-(TRIFLUOROMETHYL)PHENYL)UREA
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 GENE: EPHX2;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: ACHSEH1
KEYWDS DOMAIN-SWAPPED DIMER, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.S.S.LEE,J.LIU,K.M.WAGNER,S.PAKHOMOVA,H.DONG,C.MORRISEAU,S.H.FU,
AUTHOR 2 J.YANG,P.WANG,A.ULU,C.MATE,L.NGUYEN,H.WULLF,M.L.ELDIN,A.A.MARA,
AUTHOR 3 M.E.NEWCOMER,D.C.ZELDIN,B.D.HAMMOCK
REVDAT 1 24-SEP-14 4OCZ 0
JRNL AUTH K.S.LEE,J.Y.LIU,K.M.WAGNER,S.PAKHOMOVA,H.DONG,C.MORISSEAU,
JRNL AUTH 2 S.H.FU,J.YANG,P.WANG,A.ULU,C.A.MATE,L.V.NGUYEN,S.H.HWANG,
JRNL AUTH 3 M.L.EDIN,A.A.MARA,H.WULFF,M.E.NEWCOMER,D.C.ZELDIN,
JRNL AUTH 4 B.D.HAMMOCK
JRNL TITL OPTIMIZED INHIBITORS OF SOLUBLE EPOXIDE HYDROLASE IMPROVE IN
JRNL TITL 2 VITRO TARGET RESIDENCE TIME AND IN VIVO EFFICACY.
JRNL REF J.MED.CHEM. V. 57 7016 2014
JRNL REFN ISSN 0022-2623
JRNL PMID 25079952
JRNL DOI 10.1021/JM500694P
REMARK 2
REMARK 2 RESOLUTION. 2.94 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.94
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 12871
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 671
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) : 2.94
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.02
REMARK 3 REFLECTION IN BIN (WORKING SET) : 765
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.54
REMARK 3 BIN R VALUE (WORKING SET) : 0.3070
REMARK 3 BIN FREE R VALUE SET COUNT : 45
REMARK 3 BIN FREE R VALUE : 0.4310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4332
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 4
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 71.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 68.37
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.40000
REMARK 3 B22 (A**2) : 4.40000
REMARK 3 B33 (A**2) : -6.61000
REMARK 3 B12 (A**2) : 2.20000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : -0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.472
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.391
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 46.981
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4473 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3081 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6057 ; 1.801 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7523 ; 0.981 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 547 ; 9.423 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 193 ;38.732 ;24.197
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 780 ;18.920 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;17.659 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 664 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4906 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 895 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 68
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6420 62.7820 -7.4620
REMARK 3 T TENSOR
REMARK 3 T11: 0.2360 T22: 0.4003
REMARK 3 T33: 0.1068 T12: -0.0271
REMARK 3 T13: 0.0185 T23: -0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 0.7745 L22: 4.3448
REMARK 3 L33: 0.8919 L12: -0.8108
REMARK 3 L13: 0.8156 L23: -1.0431
REMARK 3 S TENSOR
REMARK 3 S11: -0.0899 S12: 0.0212 S13: 0.0475
REMARK 3 S21: -0.7044 S22: 0.0395 S23: 0.0801
REMARK 3 S31: -0.0616 S32: -0.0506 S33: 0.0504
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 69 A 369
REMARK 3 ORIGIN FOR THE GROUP (A): 20.6650 39.5650 5.4780
REMARK 3 T TENSOR
REMARK 3 T11: 0.0457 T22: 0.1199
REMARK 3 T33: 0.0705 T12: -0.0088
REMARK 3 T13: -0.0117 T23: -0.0623
REMARK 3 L TENSOR
REMARK 3 L11: 0.4356 L22: 1.0651
REMARK 3 L33: 1.3869 L12: 0.3209
REMARK 3 L13: -0.1367 L23: -0.7856
REMARK 3 S TENSOR
REMARK 3 S11: -0.0393 S12: 0.0838 S13: 0.0718
REMARK 3 S21: -0.0819 S22: 0.0895 S23: 0.0534
REMARK 3 S31: -0.0305 S32: -0.0221 S33: -0.0503
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 370 A 420
REMARK 3 ORIGIN FOR THE GROUP (A): 21.1570 4.8190 13.3830
REMARK 3 T TENSOR
REMARK 3 T11: 0.3728 T22: 0.4550
REMARK 3 T33: 0.3851 T12: -0.0228
REMARK 3 T13: -0.0281 T23: -0.1157
REMARK 3 L TENSOR
REMARK 3 L11: 0.3817 L22: 3.0973
REMARK 3 L33: 5.8783 L12: -0.9346
REMARK 3 L13: -0.1940 L23: -1.1434
REMARK 3 S TENSOR
REMARK 3 S11: 0.0165 S12: 0.1399 S13: -0.2751
REMARK 3 S21: -0.1300 S22: 0.2177 S23: 0.5981
REMARK 3 S31: 0.8445 S32: -1.2391 S33: -0.2342
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 421 A 548
REMARK 3 ORIGIN FOR THE GROUP (A): 14.2540 16.7790 14.6040
REMARK 3 T TENSOR
REMARK 3 T11: 0.1086 T22: 0.0895
REMARK 3 T33: 0.0886 T12: -0.0494
REMARK 3 T13: -0.0329 T23: -0.0471
REMARK 3 L TENSOR
REMARK 3 L11: 2.4637 L22: 1.3224
REMARK 3 L33: 2.1054 L12: -0.7856
REMARK 3 L13: -0.8199 L23: 0.0959
REMARK 3 S TENSOR
REMARK 3 S11: -0.0704 S12: 0.1509 S13: -0.2221
REMARK 3 S21: -0.0844 S22: -0.0093 S23: 0.1103
REMARK 3 S31: 0.2684 S32: -0.1163 S33: 0.0798
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4OCZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JAN-14.
REMARK 100 THE RCSB ID CODE IS RCSB084336.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97920
REMARK 200 MONOCHROMATOR : CRYO-COOLED DOUBLE CRYSTAL
REMARK 200 SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13582
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.940
REMARK 200 RESOLUTION RANGE LOW (A) : 75.890
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09300
REMARK 200 FOR THE DATA SET : 15.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.94
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.65600
REMARK 200 FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1S8O
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG3350, 0-10% SUCROSE, PH 7.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,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 162.24867
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 81.12433
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 121.68650
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 40.56217
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 202.81083
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 162.24867
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 81.12433
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 40.56217
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 121.68650
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 202.81083
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: 5110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 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 46.11450
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 79.87266
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 40.56217
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 PRO A 549
REMARK 465 PRO A 550
REMARK 465 VAL A 551
REMARK 465 VAL A 552
REMARK 465 SER A 553
REMARK 465 LYS A 554
REMARK 465 MET A 555
REMARK 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 MET A 1 CG SD CE
REMARK 470 LYS A 421 CG CD CE NZ
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 2.01
REMARK 500 OD1 ASP A 205 OG1 THR A 208 2.06
REMARK 500
REMARK 500 REMARK: NULL
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 PRO A 17 C - N - CD ANGL. DEV. = -16.3 DEGREES
REMARK 500 PRO A 161 C - N - CA ANGL. DEV. = 19.6 DEGREES
REMARK 500 PRO A 161 C - N - CD ANGL. DEV. = -30.7 DEGREES
REMARK 500 ASP A 185 CB - CG - OD1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ASP A 185 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 PRO A 268 C - N - CA ANGL. DEV. = 11.3 DEGREES
REMARK 500 PRO A 268 C - N - CD ANGL. DEV. = -21.7 DEGREES
REMARK 500 ARG A 440 NE - CZ - NH1 ANGL. DEV. = 3.6 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 ARG A 4 16.16 -149.27
REMARK 500 LEU A 10 -74.76 -98.48
REMARK 500 VAL A 13 -64.10 -122.54
REMARK 500 PRO A 17 92.03 37.86
REMARK 500 LEU A 23 -60.49 -18.17
REMARK 500 LYS A 79 76.76 51.69
REMARK 500 ASN A 85 48.97 -105.95
REMARK 500 ILE A 101 132.53 -36.78
REMARK 500 LYS A 115 45.47 -102.81
REMARK 500 PRO A 161 3.15 -153.20
REMARK 500 GLN A 204 -105.59 -111.74
REMARK 500 LEU A 221 -53.07 -121.44
REMARK 500 ASN A 223 -7.98 71.35
REMARK 500 THR A 224 137.50 -36.58
REMARK 500 LEU A 228 142.77 -38.58
REMARK 500 LYS A 245 146.40 167.70
REMARK 500 PRO A 268 93.07 -53.85
REMARK 500 GLU A 269 -150.68 -131.28
REMARK 500 ASP A 335 -121.43 51.28
REMARK 500 ASN A 359 -51.53 77.45
REMARK 500 ASN A 378 97.28 175.38
REMARK 500 ASP A 413 38.12 -75.62
REMARK 500 GLU A 414 -1.84 -152.54
REMARK 500 VAL A 416 41.37 -141.97
REMARK 500 LYS A 421 16.52 57.86
REMARK 500 VAL A 430 -33.54 -37.55
REMARK 500 GLU A 435 72.95 -119.96
REMARK 500 PRO A 487 127.61 -39.38
REMARK 500 LYS A 530 47.31 -140.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU A 16 PRO A 17 -116.28
REMARK 500 LYS A 160 PRO A 161 107.02
REMARK 500 PHE A 267 PRO A 268 -94.71
REMARK 500 MET A 291 ASP A 292 138.32
REMARK 500 SER A 418 MET A 419 -142.73
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 ASP A 207 21.2 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 602 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 9 OD2
REMARK 620 2 HOH A 704 O 155.1
REMARK 620 3 HOH A 703 O 91.2 106.7
REMARK 620 4 ASP A 185 OD1 71.8 89.3 94.6
REMARK 620 5 PO4 A 601 O1 120.1 82.8 70.2 159.8
REMARK 620 6 ASP A 11 O 78.3 86.1 166.3 90.5 107.3
REMARK 620 7 ASP A 9 OD1 50.8 146.1 84.1 122.5 70.5 82.4
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2RU A 603
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4OD0 RELATED DB: PDB
DBREF 4OCZ A 1 555 UNP P34913 HYES_HUMAN 1 555
SEQRES 1 A 555 MET THR LEU ARG ALA ALA VAL PHE ASP LEU ASP GLY VAL
SEQRES 2 A 555 LEU ALA LEU PRO ALA VAL PHE GLY VAL LEU GLY ARG THR
SEQRES 3 A 555 GLU GLU ALA LEU ALA LEU PRO ARG GLY LEU LEU ASN ASP
SEQRES 4 A 555 ALA PHE GLN LYS GLY GLY PRO GLU GLY ALA THR THR ARG
SEQRES 5 A 555 LEU MET LYS GLY GLU ILE THR LEU SER GLN TRP ILE PRO
SEQRES 6 A 555 LEU MET GLU GLU ASN CYS ARG LYS CYS SER GLU THR ALA
SEQRES 7 A 555 LYS VAL CYS LEU PRO LYS ASN PHE SER ILE LYS GLU ILE
SEQRES 8 A 555 PHE ASP LYS ALA ILE SER ALA ARG LYS ILE ASN ARG PRO
SEQRES 9 A 555 MET LEU GLN ALA ALA LEU MET LEU ARG LYS LYS GLY PHE
SEQRES 10 A 555 THR THR ALA ILE LEU THR ASN THR TRP LEU ASP ASP ARG
SEQRES 11 A 555 ALA GLU ARG ASP GLY LEU ALA GLN LEU MET CYS GLU LEU
SEQRES 12 A 555 LYS MET HIS PHE ASP PHE LEU ILE GLU SER CYS GLN VAL
SEQRES 13 A 555 GLY MET VAL LYS PRO GLU PRO GLN ILE TYR LYS PHE LEU
SEQRES 14 A 555 LEU ASP THR LEU LYS ALA SER PRO SER GLU VAL VAL PHE
SEQRES 15 A 555 LEU ASP ASP ILE GLY ALA ASN LEU LYS PRO ALA ARG ASP
SEQRES 16 A 555 LEU GLY MET VAL THR ILE LEU VAL GLN ASP THR ASP THR
SEQRES 17 A 555 ALA LEU LYS GLU LEU GLU LYS VAL THR GLY ILE GLN LEU
SEQRES 18 A 555 LEU ASN THR PRO ALA PRO LEU PRO THR SER CYS ASN PRO
SEQRES 19 A 555 SER ASP MET SER HIS GLY TYR VAL THR VAL LYS PRO ARG
SEQRES 20 A 555 VAL ARG LEU HIS PHE VAL GLU LEU GLY SER GLY PRO ALA
SEQRES 21 A 555 VAL CYS LEU CYS HIS GLY PHE PRO GLU SER TRP TYR SER
SEQRES 22 A 555 TRP ARG TYR GLN ILE PRO ALA LEU ALA GLN ALA GLY TYR
SEQRES 23 A 555 ARG VAL LEU ALA MET ASP MET LYS GLY TYR GLY GLU SER
SEQRES 24 A 555 SER ALA PRO PRO GLU ILE GLU GLU TYR CYS MET GLU VAL
SEQRES 25 A 555 LEU CYS LYS GLU MET VAL THR PHE LEU ASP LYS LEU GLY
SEQRES 26 A 555 LEU SER GLN ALA VAL PHE ILE GLY HIS ASP TRP GLY GLY
SEQRES 27 A 555 MET LEU VAL TRP TYR MET ALA LEU PHE TYR PRO GLU ARG
SEQRES 28 A 555 VAL ARG ALA VAL ALA SER LEU ASN THR PRO PHE ILE PRO
SEQRES 29 A 555 ALA ASN PRO ASN MET SER PRO LEU GLU SER ILE LYS ALA
SEQRES 30 A 555 ASN PRO VAL PHE ASP TYR GLN LEU TYR PHE GLN GLU PRO
SEQRES 31 A 555 GLY VAL ALA GLU ALA GLU LEU GLU GLN ASN LEU SER ARG
SEQRES 32 A 555 THR PHE LYS SER LEU PHE ARG ALA SER ASP GLU SER VAL
SEQRES 33 A 555 LEU SER MET HIS LYS VAL CYS GLU ALA GLY GLY LEU PHE
SEQRES 34 A 555 VAL ASN SER PRO GLU GLU PRO SER LEU SER ARG MET VAL
SEQRES 35 A 555 THR GLU GLU GLU ILE GLN PHE TYR VAL GLN GLN PHE LYS
SEQRES 36 A 555 LYS SER GLY PHE ARG GLY PRO LEU ASN TRP TYR ARG ASN
SEQRES 37 A 555 MET GLU ARG ASN TRP LYS TRP ALA CYS LYS SER LEU GLY
SEQRES 38 A 555 ARG LYS ILE LEU ILE PRO ALA LEU MET VAL THR ALA GLU
SEQRES 39 A 555 LYS ASP PHE VAL LEU VAL PRO GLN MET SER GLN HIS MET
SEQRES 40 A 555 GLU ASP TRP ILE PRO HIS LEU LYS ARG GLY HIS ILE GLU
SEQRES 41 A 555 ASP CYS GLY HIS TRP THR GLN MET ASP LYS PRO THR GLU
SEQRES 42 A 555 VAL ASN GLN ILE LEU ILE LYS TRP LEU ASP SER ASP ALA
SEQRES 43 A 555 ARG ASN PRO PRO VAL VAL SER LYS MET
HET PO4 A 601 5
HET MG A 602 1
HET 2RU A 603 25
HETNAM PO4 PHOSPHATE ION
HETNAM MG MAGNESIUM ION
HETNAM 2RU 1-[1-(2-METHYLPROPANOYL)PIPERIDIN-4-YL]-3-[4-
HETNAM 2 2RU (TRIFLUOROMETHYL)PHENYL]UREA
FORMUL 2 PO4 O4 P 3-
FORMUL 3 MG MG 2+
FORMUL 4 2RU C17 H22 F3 N3 O2
FORMUL 5 HOH *4(H2 O)
HELIX 1 1 VAL A 19 LEU A 30 1 12
HELIX 2 2 GLY A 35 LYS A 43 1 9
HELIX 3 3 GLY A 44 GLU A 47 5 4
HELIX 4 4 GLY A 48 GLY A 56 1 9
HELIX 5 5 THR A 59 ALA A 78 1 20
HELIX 6 6 SER A 87 ARG A 99 1 13
HELIX 7 7 ASN A 102 LYS A 115 1 14
HELIX 8 8 ARG A 133 MET A 145 1 13
HELIX 9 9 SER A 153 GLY A 157 1 5
HELIX 10 10 GLU A 162 LYS A 174 1 13
HELIX 11 11 SER A 176 SER A 178 5 3
HELIX 12 12 ILE A 186 LEU A 196 1 11
HELIX 13 13 ASP A 205 GLY A 218 1 14
HELIX 14 14 ASN A 233 MET A 237 5 5
HELIX 15 15 SER A 270 ARG A 275 5 6
HELIX 16 16 TYR A 276 TYR A 286 1 11
HELIX 17 17 GLU A 304 TYR A 308 5 5
HELIX 18 18 CYS A 309 GLY A 325 1 17
HELIX 19 19 ASP A 335 TYR A 348 1 14
HELIX 20 20 SER A 370 ALA A 377 1 8
HELIX 21 21 ASN A 378 VAL A 380 5 3
HELIX 22 22 PHE A 381 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 ALA A 411 SER A 415 5 5
HELIX 26 26 LYS A 421 GLY A 426 1 6
HELIX 27 27 THR A 443 GLY A 458 1 16
HELIX 28 28 PHE A 459 TRP A 465 1 7
HELIX 29 29 ASN A 468 LYS A 478 1 11
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 A 5 PHE A 149 GLU A 152 0
SHEET 2 A 5 THR A 118 THR A 123 1 N ILE A 121 O ILE A 151
SHEET 3 A 5 ALA A 5 PHE A 8 1 N ALA A 6 O ALA A 120
SHEET 4 A 5 VAL A 180 ASP A 184 1 O VAL A 181 N VAL A 7
SHEET 5 A 5 VAL A 199 LEU A 202 1 O VAL A 199 N PHE A 182
SHEET 1 B 2 ALA A 15 LEU A 16 0
SHEET 2 B 2 LYS A 100 ILE A 101 -1 O LYS A 100 N LEU A 16
SHEET 1 C 8 SER A 238 LYS A 245 0
SHEET 2 C 8 VAL A 248 GLY A 256 -1 O PHE A 252 N GLY A 240
SHEET 3 C 8 ARG A 287 ASP A 292 -1 O ALA A 290 N VAL A 253
SHEET 4 C 8 ALA A 260 CYS A 264 1 N VAL A 261 O LEU A 289
SHEET 5 C 8 ALA A 329 HIS A 334 1 O VAL A 330 N CYS A 262
SHEET 6 C 8 VAL A 352 LEU A 358 1 O ALA A 354 N PHE A 331
SHEET 7 C 8 ALA A 488 ALA A 493 1 O VAL A 491 N SER A 357
SHEET 8 C 8 LYS A 515 ILE A 519 1 O ILE A 519 N THR A 492
LINK OD2 ASP A 9 MG MG A 602 1555 1555 1.91
LINK MG MG A 602 O HOH A 704 1555 1555 1.93
LINK MG MG A 602 O HOH A 703 1555 1555 1.93
LINK OD1 ASP A 185 MG MG A 602 1555 1555 1.94
LINK O1 PO4 A 601 MG MG A 602 1555 1555 1.97
LINK O ASP A 11 MG MG A 602 1555 1555 2.20
LINK OD1 ASP A 9 MG MG A 602 1555 1555 2.78
SITE 1 AC1 9 ASP A 9 LEU A 10 ASP A 11 THR A 123
SITE 2 AC1 9 ASN A 124 LYS A 160 MG A 602 HOH A 703
SITE 3 AC1 9 HOH A 704
SITE 1 AC2 6 ASP A 9 ASP A 11 ASP A 185 PO4 A 601
SITE 2 AC2 6 HOH A 703 HOH A 704
SITE 1 AC3 9 PHE A 267 ASP A 335 TRP A 336 MET A 339
SITE 2 AC3 9 THR A 360 TYR A 383 PHE A 387 LEU A 408
SITE 3 AC3 9 TYR A 466
CRYST1 92.229 92.229 243.373 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 0.010843 0.006260 0.000000 0.00000
SCALE2 0.000000 0.012520 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004109 0.00000
TER 4333 ASN A 548
MASTER 517 0 3 32 15 0 8 6 4367 1 38 43
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