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HEADER HYDROLASE/HYDROLASE INHIBITOR 09-DEC-14 4X6Y
TITLE HUMAN SOLUBLE EPOXIDE HYDROLASE IN COMPLEX WITH A CYCLOPROPYL UREA
TITLE 2 DERIVATIVE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIFUNCTIONAL EPOXIDE HYDROLASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: HYDROLASE DOMAIN, UNP RESIDUES 230-555;
COMPND 5 EC: 3.3.2.10;
COMPND 6 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: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR N.CHIYO,K.TAKAI,T.ISHII
REVDAT 1 08-APR-15 4X6Y 0
JRNL AUTH K.TAKAI,N.CHIYO,T.NAKAJIMA,T.NARIAI,C.ISHIKAWA,S.NAKATANI,
JRNL AUTH 2 A.IKENO,S.YAMAMOTO,T.SONE
JRNL TITL THREE-DIMENSIONAL RATIONAL APPROACH TO THE DISCOVERY OF
JRNL TITL 2 POTENT SUBSTITUTED CYCLOPROPYL UREA SOLUBLE EPOXIDE
JRNL TITL 3 HYDROLASE INHIBITORS
JRNL REF BIOORG.MED.CHEM.LETT. 2015
JRNL REFN ESSN 1464-3405
JRNL PMID 25800114
JRNL DOI 10.1016/J.BMCL.2015.02.076
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 79.9
REMARK 3 NUMBER OF REFLECTIONS : 33454
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) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1781
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) : 2.07
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1449
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 46.69
REMARK 3 BIN R VALUE (WORKING SET) : 0.2860
REMARK 3 BIN FREE R VALUE SET COUNT : 76
REMARK 3 BIN FREE R VALUE : 0.3150
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5092
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 88
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.08000
REMARK 3 B22 (A**2) : -0.08000
REMARK 3 B33 (A**2) : -0.03000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.04000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.290
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.219
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.166
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.448
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5302 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4912 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7194 ; 1.256 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11348 ; 0.781 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 630 ; 6.149 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 244 ;33.332 ;23.934
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 884 ;14.772 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;15.468 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 738 ; 0.070 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5990 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1274 ; 0.001 ; 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): 2526 ; 1.031 ; 2.600
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2525 ; 1.031 ; 2.599
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3154 ; 1.794 ; 3.895
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 : 6
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 230 A 368
REMARK 3 ORIGIN FOR THE GROUP (A): 6.7091 -6.4235 24.4039
REMARK 3 T TENSOR
REMARK 3 T11: 0.1560 T22: 0.1551
REMARK 3 T33: 0.1050 T12: 0.0034
REMARK 3 T13: -0.0014 T23: 0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 1.4769 L22: 2.2290
REMARK 3 L33: 1.2706 L12: -0.4533
REMARK 3 L13: -0.1276 L23: 0.5494
REMARK 3 S TENSOR
REMARK 3 S11: -0.0351 S12: -0.1060 S13: -0.1127
REMARK 3 S21: 0.1976 S22: -0.0076 S23: 0.0033
REMARK 3 S31: 0.0412 S32: -0.1115 S33: 0.0427
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 369 A 430
REMARK 3 ORIGIN FOR THE GROUP (A): -10.3623 9.4191 27.8115
REMARK 3 T TENSOR
REMARK 3 T11: 0.2263 T22: 0.2540
REMARK 3 T33: 0.1997 T12: 0.1394
REMARK 3 T13: 0.0478 T23: -0.0571
REMARK 3 L TENSOR
REMARK 3 L11: 1.7932 L22: 4.6582
REMARK 3 L33: 2.3806 L12: 1.0671
REMARK 3 L13: -0.3635 L23: -0.3096
REMARK 3 S TENSOR
REMARK 3 S11: 0.1390 S12: -0.2046 S13: 0.3702
REMARK 3 S21: 0.5680 S22: -0.1226 S23: 0.5699
REMARK 3 S31: -0.2406 S32: -0.4040 S33: -0.0164
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 431 A 545
REMARK 3 ORIGIN FOR THE GROUP (A): 4.4663 3.9876 30.3573
REMARK 3 T TENSOR
REMARK 3 T11: 0.1787 T22: 0.1530
REMARK 3 T33: 0.0551 T12: 0.0416
REMARK 3 T13: -0.0078 T23: -0.0293
REMARK 3 L TENSOR
REMARK 3 L11: 2.4274 L22: 1.8716
REMARK 3 L33: 1.3886 L12: -0.1320
REMARK 3 L13: -0.2869 L23: 0.4266
REMARK 3 S TENSOR
REMARK 3 S11: -0.0204 S12: -0.3023 S13: 0.1852
REMARK 3 S21: 0.2652 S22: -0.0074 S23: -0.0265
REMARK 3 S31: -0.0515 S32: -0.0335 S33: 0.0278
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 : B 230 B 368
REMARK 3 ORIGIN FOR THE GROUP (A): 22.5594 -16.7360 3.5389
REMARK 3 T TENSOR
REMARK 3 T11: 0.0916 T22: 0.1314
REMARK 3 T33: 0.1882 T12: 0.0101
REMARK 3 T13: 0.0180 T23: -0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 1.3153 L22: 2.2996
REMARK 3 L33: 1.5379 L12: -0.0330
REMARK 3 L13: -0.4121 L23: 0.5527
REMARK 3 S TENSOR
REMARK 3 S11: 0.0001 S12: 0.1451 S13: -0.0359
REMARK 3 S21: -0.1125 S22: 0.0403 S23: -0.2180
REMARK 3 S31: -0.0135 S32: 0.0588 S33: -0.0404
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 369 B 429
REMARK 3 ORIGIN FOR THE GROUP (A): 20.7797 -31.6598 -14.4321
REMARK 3 T TENSOR
REMARK 3 T11: 0.3026 T22: 0.2116
REMARK 3 T33: 0.2094 T12: 0.0191
REMARK 3 T13: 0.1068 T23: -0.1786
REMARK 3 L TENSOR
REMARK 3 L11: 2.5113 L22: 3.4868
REMARK 3 L33: 3.5719 L12: 1.4562
REMARK 3 L13: 0.1899 L23: -1.0426
REMARK 3 S TENSOR
REMARK 3 S11: -0.0859 S12: 0.4855 S13: -0.4591
REMARK 3 S21: -0.8859 S22: 0.0262 S23: -0.3801
REMARK 3 S31: 0.4080 S32: 0.1786 S33: 0.0597
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 430 B 545
REMARK 3 ORIGIN FOR THE GROUP (A): 26.9908 -27.4426 -0.6264
REMARK 3 T TENSOR
REMARK 3 T11: 0.0922 T22: 0.0953
REMARK 3 T33: 0.2163 T12: 0.0290
REMARK 3 T13: 0.0692 T23: -0.0639
REMARK 3 L TENSOR
REMARK 3 L11: 1.7144 L22: 2.7681
REMARK 3 L33: 1.5599 L12: 0.0190
REMARK 3 L13: 0.0538 L23: 0.0330
REMARK 3 S TENSOR
REMARK 3 S11: 0.0081 S12: 0.1932 S13: -0.2768
REMARK 3 S21: -0.2348 S22: 0.0152 S23: -0.4345
REMARK 3 S31: 0.2864 S32: 0.1155 S33: -0.0233
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 U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 4X6Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-DEC-14.
REMARK 100 THE DEPOSITION ID IS D_1000204761.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43406
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 78.4
REMARK 200 DATA REDUNDANCY : 1.600
REMARK 200 R MERGE (I) : 0.04100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 55.6
REMARK 200 DATA REDUNDANCY IN SHELL : 1.30
REMARK 200 R MERGE FOR SHELL (I) : 0.19000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 3ANS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20%(W/V) PEG8000, 200MM SODIUM IODIDE,
REMARK 280 PH 7.3, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 64.61400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.36100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 64.61400
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.36100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.
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 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 220
REMARK 465 LYS A 221
REMARK 465 LYS A 222
REMARK 465 GLY A 223
REMARK 465 HIS A 224
REMARK 465 HIS A 225
REMARK 465 HIS A 226
REMARK 465 HIS A 227
REMARK 465 HIS A 228
REMARK 465 HIS A 229
REMARK 465 ALA A 546
REMARK 465 ARG A 547
REMARK 465 ASN A 548
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 465 MET B 220
REMARK 465 LYS B 221
REMARK 465 LYS B 222
REMARK 465 GLY B 223
REMARK 465 HIS B 224
REMARK 465 HIS B 225
REMARK 465 HIS B 226
REMARK 465 HIS B 227
REMARK 465 HIS B 228
REMARK 465 HIS B 229
REMARK 465 ALA B 546
REMARK 465 ARG B 547
REMARK 465 ASN B 548
REMARK 465 PRO B 549
REMARK 465 PRO B 550
REMARK 465 VAL B 551
REMARK 465 VAL B 552
REMARK 465 SER B 553
REMARK 465 LYS B 554
REMARK 465 MET B 555
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 GLU A 269 -148.10 -120.21
REMARK 500 ASP A 335 -125.81 62.96
REMARK 500 ASN A 359 -45.06 80.69
REMARK 500 PHE A 381 36.05 -87.75
REMARK 500 MET A 419 76.30 -64.76
REMARK 500 HIS A 420 -44.41 -151.69
REMARK 500 ASN A 431 34.00 -142.02
REMARK 500 SER A 544 -70.77 -104.35
REMARK 500 SER B 231 -160.89 -120.81
REMARK 500 GLU B 269 -143.27 -117.50
REMARK 500 ASP B 335 -129.97 63.32
REMARK 500 ASN B 359 -41.54 76.19
REMARK 500 MET B 419 32.58 -99.81
REMARK 500 HIS B 420 -72.27 -72.60
REMARK 500 SER B 479 14.37 -145.82
REMARK 500 SER B 544 -61.55 -94.22
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 ARG A 247 VAL A 248 -148.79
REMARK 500 MET A 291 ASP A 292 146.88
REMARK 500 MET B 291 ASP B 292 147.04
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 S94 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue S94 B 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4X6X RELATED DB: PDB
DBREF 4X6Y A 230 555 UNP P34913 HYES_HUMAN 230 555
DBREF 4X6Y B 230 555 UNP P34913 HYES_HUMAN 230 555
SEQADV 4X6Y MET A 220 UNP P34913 EXPRESSION TAG
SEQADV 4X6Y LYS A 221 UNP P34913 EXPRESSION TAG
SEQADV 4X6Y LYS A 222 UNP P34913 EXPRESSION TAG
SEQADV 4X6Y GLY A 223 UNP P34913 EXPRESSION TAG
SEQADV 4X6Y HIS A 224 UNP P34913 EXPRESSION TAG
SEQADV 4X6Y HIS A 225 UNP P34913 EXPRESSION TAG
SEQADV 4X6Y HIS A 226 UNP P34913 EXPRESSION TAG
SEQADV 4X6Y HIS A 227 UNP P34913 EXPRESSION TAG
SEQADV 4X6Y HIS A 228 UNP P34913 EXPRESSION TAG
SEQADV 4X6Y HIS A 229 UNP P34913 EXPRESSION TAG
SEQADV 4X6Y MET B 220 UNP P34913 EXPRESSION TAG
SEQADV 4X6Y LYS B 221 UNP P34913 EXPRESSION TAG
SEQADV 4X6Y LYS B 222 UNP P34913 EXPRESSION TAG
SEQADV 4X6Y GLY B 223 UNP P34913 EXPRESSION TAG
SEQADV 4X6Y HIS B 224 UNP P34913 EXPRESSION TAG
SEQADV 4X6Y HIS B 225 UNP P34913 EXPRESSION TAG
SEQADV 4X6Y HIS B 226 UNP P34913 EXPRESSION TAG
SEQADV 4X6Y HIS B 227 UNP P34913 EXPRESSION TAG
SEQADV 4X6Y HIS B 228 UNP P34913 EXPRESSION TAG
SEQADV 4X6Y HIS B 229 UNP P34913 EXPRESSION TAG
SEQRES 1 A 336 MET LYS LYS GLY HIS HIS HIS HIS HIS HIS THR SER CYS
SEQRES 2 A 336 ASN PRO SER ASP MET SER HIS GLY TYR VAL THR VAL LYS
SEQRES 3 A 336 PRO ARG VAL ARG LEU HIS PHE VAL GLU LEU GLY SER GLY
SEQRES 4 A 336 PRO ALA VAL CYS LEU CYS HIS GLY PHE PRO GLU SER TRP
SEQRES 5 A 336 TYR SER TRP ARG TYR GLN ILE PRO ALA LEU ALA GLN ALA
SEQRES 6 A 336 GLY TYR ARG VAL LEU ALA MET ASP MET LYS GLY TYR GLY
SEQRES 7 A 336 GLU SER SER ALA PRO PRO GLU ILE GLU GLU TYR CYS MET
SEQRES 8 A 336 GLU VAL LEU CYS LYS GLU MET VAL THR PHE LEU ASP LYS
SEQRES 9 A 336 LEU GLY LEU SER GLN ALA VAL PHE ILE GLY HIS ASP TRP
SEQRES 10 A 336 GLY GLY MET LEU VAL TRP TYR MET ALA LEU PHE TYR PRO
SEQRES 11 A 336 GLU ARG VAL ARG ALA VAL ALA SER LEU ASN THR PRO PHE
SEQRES 12 A 336 ILE PRO ALA ASN PRO ASN MET SER PRO LEU GLU SER ILE
SEQRES 13 A 336 LYS ALA ASN PRO VAL PHE ASP TYR GLN LEU TYR PHE GLN
SEQRES 14 A 336 GLU PRO GLY VAL ALA GLU ALA GLU LEU GLU GLN ASN LEU
SEQRES 15 A 336 SER ARG THR PHE LYS SER LEU PHE ARG ALA SER ASP GLU
SEQRES 16 A 336 SER VAL LEU SER MET HIS LYS VAL CYS GLU ALA GLY GLY
SEQRES 17 A 336 LEU PHE VAL ASN SER PRO GLU GLU PRO SER LEU SER ARG
SEQRES 18 A 336 MET VAL THR GLU GLU GLU ILE GLN PHE TYR VAL GLN GLN
SEQRES 19 A 336 PHE LYS LYS SER GLY PHE ARG GLY PRO LEU ASN TRP TYR
SEQRES 20 A 336 ARG ASN MET GLU ARG ASN TRP LYS TRP ALA CYS LYS SER
SEQRES 21 A 336 LEU GLY ARG LYS ILE LEU ILE PRO ALA LEU MET VAL THR
SEQRES 22 A 336 ALA GLU LYS ASP PHE VAL LEU VAL PRO GLN MET SER GLN
SEQRES 23 A 336 HIS MET GLU ASP TRP ILE PRO HIS LEU LYS ARG GLY HIS
SEQRES 24 A 336 ILE GLU ASP CYS GLY HIS TRP THR GLN MET ASP LYS PRO
SEQRES 25 A 336 THR GLU VAL ASN GLN ILE LEU ILE LYS TRP LEU ASP SER
SEQRES 26 A 336 ASP ALA ARG ASN PRO PRO VAL VAL SER LYS MET
SEQRES 1 B 336 MET LYS LYS GLY HIS HIS HIS HIS HIS HIS THR SER CYS
SEQRES 2 B 336 ASN PRO SER ASP MET SER HIS GLY TYR VAL THR VAL LYS
SEQRES 3 B 336 PRO ARG VAL ARG LEU HIS PHE VAL GLU LEU GLY SER GLY
SEQRES 4 B 336 PRO ALA VAL CYS LEU CYS HIS GLY PHE PRO GLU SER TRP
SEQRES 5 B 336 TYR SER TRP ARG TYR GLN ILE PRO ALA LEU ALA GLN ALA
SEQRES 6 B 336 GLY TYR ARG VAL LEU ALA MET ASP MET LYS GLY TYR GLY
SEQRES 7 B 336 GLU SER SER ALA PRO PRO GLU ILE GLU GLU TYR CYS MET
SEQRES 8 B 336 GLU VAL LEU CYS LYS GLU MET VAL THR PHE LEU ASP LYS
SEQRES 9 B 336 LEU GLY LEU SER GLN ALA VAL PHE ILE GLY HIS ASP TRP
SEQRES 10 B 336 GLY GLY MET LEU VAL TRP TYR MET ALA LEU PHE TYR PRO
SEQRES 11 B 336 GLU ARG VAL ARG ALA VAL ALA SER LEU ASN THR PRO PHE
SEQRES 12 B 336 ILE PRO ALA ASN PRO ASN MET SER PRO LEU GLU SER ILE
SEQRES 13 B 336 LYS ALA ASN PRO VAL PHE ASP TYR GLN LEU TYR PHE GLN
SEQRES 14 B 336 GLU PRO GLY VAL ALA GLU ALA GLU LEU GLU GLN ASN LEU
SEQRES 15 B 336 SER ARG THR PHE LYS SER LEU PHE ARG ALA SER ASP GLU
SEQRES 16 B 336 SER VAL LEU SER MET HIS LYS VAL CYS GLU ALA GLY GLY
SEQRES 17 B 336 LEU PHE VAL ASN SER PRO GLU GLU PRO SER LEU SER ARG
SEQRES 18 B 336 MET VAL THR GLU GLU GLU ILE GLN PHE TYR VAL GLN GLN
SEQRES 19 B 336 PHE LYS LYS SER GLY PHE ARG GLY PRO LEU ASN TRP TYR
SEQRES 20 B 336 ARG ASN MET GLU ARG ASN TRP LYS TRP ALA CYS LYS SER
SEQRES 21 B 336 LEU GLY ARG LYS ILE LEU ILE PRO ALA LEU MET VAL THR
SEQRES 22 B 336 ALA GLU LYS ASP PHE VAL LEU VAL PRO GLN MET SER GLN
SEQRES 23 B 336 HIS MET GLU ASP TRP ILE PRO HIS LEU LYS ARG GLY HIS
SEQRES 24 B 336 ILE GLU ASP CYS GLY HIS TRP THR GLN MET ASP LYS PRO
SEQRES 25 B 336 THR GLU VAL ASN GLN ILE LEU ILE LYS TRP LEU ASP SER
SEQRES 26 B 336 ASP ALA ARG ASN PRO PRO VAL VAL SER LYS MET
HET S94 A 601 25
HET S94 B 601 25
HETNAM S94 4-PHENOXY-N-[(1S,2R)-2-PHENYLCYCLOPROPYL]PIPERIDINE-1-
HETNAM 2 S94 CARBOXAMIDE
FORMUL 3 S94 2(C21 H24 N2 O2)
FORMUL 5 HOH *88(H2 O)
HELIX 1 AA1 ASN A 233 MET A 237 5 5
HELIX 2 AA2 SER A 270 ARG A 275 5 6
HELIX 3 AA3 GLN A 277 ALA A 284 1 8
HELIX 4 AA4 GLU A 304 TYR A 308 5 5
HELIX 5 AA5 CYS A 309 GLY A 325 1 17
HELIX 6 AA6 ASP A 335 TYR A 348 1 14
HELIX 7 AA7 PRO A 371 ALA A 377 1 7
HELIX 8 AA8 ASN A 378 VAL A 380 5 3
HELIX 9 AA9 PHE A 381 PHE A 387 1 7
HELIX 10 AB1 GLY A 391 ASN A 400 1 10
HELIX 11 AB2 ASN A 400 PHE A 409 1 10
HELIX 12 AB3 ALA A 411 SER A 415 5 5
HELIX 13 AB4 LYS A 421 GLY A 426 1 6
HELIX 14 AB5 THR A 443 LYS A 455 1 13
HELIX 15 AB6 PHE A 459 TRP A 465 1 7
HELIX 16 AB7 ASN A 468 CYS A 477 1 10
HELIX 17 AB8 LYS A 478 LEU A 480 5 3
HELIX 18 AB9 VAL A 500 GLN A 505 5 6
HELIX 19 AC1 HIS A 506 ILE A 511 5 6
HELIX 20 AC2 TRP A 525 LYS A 530 1 6
HELIX 21 AC3 LYS A 530 ASP A 545 1 16
HELIX 22 AC4 ASN B 233 MET B 237 5 5
HELIX 23 AC5 SER B 270 ARG B 275 5 6
HELIX 24 AC6 GLN B 277 ALA B 284 1 8
HELIX 25 AC7 GLU B 304 TYR B 308 5 5
HELIX 26 AC8 CYS B 309 GLY B 325 1 17
HELIX 27 AC9 ASP B 335 TYR B 348 1 14
HELIX 28 AD1 SER B 370 LYS B 376 1 7
HELIX 29 AD2 ALA B 377 VAL B 380 5 4
HELIX 30 AD3 PHE B 381 PHE B 387 1 7
HELIX 31 AD4 GLY B 391 ASN B 400 1 10
HELIX 32 AD5 ASN B 400 PHE B 409 1 10
HELIX 33 AD6 ALA B 411 SER B 415 5 5
HELIX 34 AD7 LYS B 421 GLY B 426 1 6
HELIX 35 AD8 THR B 443 GLY B 458 1 16
HELIX 36 AD9 PHE B 459 TRP B 465 1 7
HELIX 37 AE1 ASN B 468 CYS B 477 1 10
HELIX 38 AE2 VAL B 500 GLN B 505 5 6
HELIX 39 AE3 HIS B 506 TRP B 510 5 5
HELIX 40 AE4 TRP B 525 LYS B 530 1 6
HELIX 41 AE5 LYS B 530 ASP B 545 1 16
SHEET 1 AA116 LYS A 515 ILE A 519 0
SHEET 2 AA116 ALA A 488 ALA A 493 1 N THR A 492 O ILE A 519
SHEET 3 AA116 VAL A 352 LEU A 358 1 N SER A 357 O VAL A 491
SHEET 4 AA116 ALA A 329 HIS A 334 1 N GLY A 333 O LEU A 358
SHEET 5 AA116 ALA A 260 CYS A 264 1 N CYS A 262 O VAL A 330
SHEET 6 AA116 ARG A 287 MET A 291 1 O LEU A 289 N VAL A 261
SHEET 7 AA116 VAL A 248 LEU A 255 -1 N LEU A 255 O VAL A 288
SHEET 8 AA116 SER A 238 LYS A 245 -1 N GLY A 240 O PHE A 252
SHEET 9 AA116 SER B 238 LYS B 245 -1 O HIS B 239 N TYR A 241
SHEET 10 AA116 VAL B 248 LEU B 255 -1 O PHE B 252 N GLY B 240
SHEET 11 AA116 ARG B 287 MET B 291 -1 O VAL B 288 N LEU B 255
SHEET 12 AA116 ALA B 260 CYS B 264 1 N LEU B 263 O LEU B 289
SHEET 13 AA116 ALA B 329 HIS B 334 1 O VAL B 330 N CYS B 262
SHEET 14 AA116 VAL B 352 LEU B 358 1 O LEU B 358 N GLY B 333
SHEET 15 AA116 ALA B 488 ALA B 493 1 O LEU B 489 N SER B 357
SHEET 16 AA116 LYS B 515 ILE B 519 1 O LYS B 515 N ALA B 488
CISPEP 1 PHE A 267 PRO A 268 0 -11.57
CISPEP 2 PHE B 267 PRO B 268 0 -13.48
SITE 1 AC1 9 PHE A 267 ASP A 335 MET A 339 TYR A 383
SITE 2 AC1 9 GLN A 384 LEU A 408 TYR A 466 LEU A 499
SITE 3 AC1 9 HIS A 524
SITE 1 AC2 8 PHE B 267 ASP B 335 TRP B 336 MET B 339
SITE 2 AC2 8 TYR B 383 LEU B 408 TYR B 466 HIS B 524
CRYST1 129.228 80.722 87.326 90.00 126.22 90.00 C 1 2 1 8
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 0.007738 0.000000 0.005668 0.00000
SCALE2 0.000000 0.012388 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014194 0.00000
TER 2547 ASP A 545
TER 5094 ASP B 545
MASTER 448 0 2 41 16 0 5 6 5230 2 50 52
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