| content |
HEADER HYDROLASE/HYDROLASE INHIBITOR 09-DEC-14 4X6X
TITLE HUMAN SOLUBLE EPOXIDE HYDROLASE IN COMPLEX WITH A THREE SUBSTITUTED
TITLE 2 CYCLOPROPANE 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 4X6X 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. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 3 NUMBER OF REFLECTIONS : 61023
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) : 0.199
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3261
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4005
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.2960
REMARK 3 BIN FREE R VALUE SET COUNT : 209
REMARK 3 BIN FREE R VALUE : 0.3080
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 : 72
REMARK 3 SOLVENT ATOMS : 191
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.06000
REMARK 3 B22 (A**2) : -0.12000
REMARK 3 B33 (A**2) : 0.00000
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): 0.137
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.123
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.104
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.101
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5324 ; 0.006 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4926 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7224 ; 1.173 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11380 ; 0.771 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 630 ; 5.904 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 244 ;33.905 ;23.934
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 884 ;14.109 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;12.978 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 738 ; 0.066 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6034 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1290 ; 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 ; 0.677 ; 1.853
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2525 ; 0.676 ; 1.852
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3154 ; 1.197 ; 2.775
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): 6.6945 -6.3426 24.6601
REMARK 3 T TENSOR
REMARK 3 T11: 0.1101 T22: 0.0950
REMARK 3 T33: 0.0998 T12: -0.0021
REMARK 3 T13: -0.0022 T23: -0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 0.9628 L22: 1.4485
REMARK 3 L33: 1.2982 L12: -0.2917
REMARK 3 L13: -0.2706 L23: 0.3142
REMARK 3 S TENSOR
REMARK 3 S11: -0.0207 S12: -0.0182 S13: -0.0842
REMARK 3 S21: 0.0632 S22: -0.0411 S23: 0.0012
REMARK 3 S31: 0.0288 S32: -0.1085 S33: 0.0618
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 429
REMARK 3 ORIGIN FOR THE GROUP (A): -10.1375 9.2795 28.6301
REMARK 3 T TENSOR
REMARK 3 T11: 0.1575 T22: 0.2018
REMARK 3 T33: 0.1710 T12: 0.1279
REMARK 3 T13: 0.0448 T23: -0.0650
REMARK 3 L TENSOR
REMARK 3 L11: 1.8451 L22: 3.3931
REMARK 3 L33: 1.6825 L12: 1.2003
REMARK 3 L13: -0.1659 L23: -0.8926
REMARK 3 S TENSOR
REMARK 3 S11: 0.1065 S12: -0.1097 S13: 0.2814
REMARK 3 S21: 0.3403 S22: -0.0710 S23: 0.5369
REMARK 3 S31: -0.3557 S32: -0.3685 S33: -0.0355
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 430 A 545
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2711 4.0072 30.8163
REMARK 3 T TENSOR
REMARK 3 T11: 0.1306 T22: 0.0901
REMARK 3 T33: 0.0619 T12: 0.0229
REMARK 3 T13: -0.0039 T23: -0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 1.1732 L22: 1.4944
REMARK 3 L33: 1.1432 L12: 0.0145
REMARK 3 L13: -0.2022 L23: 0.3304
REMARK 3 S TENSOR
REMARK 3 S11: 0.0035 S12: -0.1025 S13: 0.0661
REMARK 3 S21: 0.1487 S22: -0.0435 S23: 0.0052
REMARK 3 S31: -0.0917 S32: -0.0760 S33: 0.0400
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): 22.5244 -16.3095 3.6125
REMARK 3 T TENSOR
REMARK 3 T11: 0.1005 T22: 0.0955
REMARK 3 T33: 0.1198 T12: 0.0175
REMARK 3 T13: 0.0142 T23: -0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 1.1826 L22: 1.6443
REMARK 3 L33: 1.2959 L12: -0.0977
REMARK 3 L13: -0.3619 L23: 0.2826
REMARK 3 S TENSOR
REMARK 3 S11: 0.0389 S12: 0.1194 S13: 0.0049
REMARK 3 S21: -0.0575 S22: -0.0460 S23: -0.1144
REMARK 3 S31: -0.0377 S32: 0.0178 S33: 0.0071
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): 20.9705 -30.9418 -14.4436
REMARK 3 T TENSOR
REMARK 3 T11: 0.2656 T22: 0.2077
REMARK 3 T33: 0.1422 T12: 0.0260
REMARK 3 T13: 0.0386 T23: -0.1577
REMARK 3 L TENSOR
REMARK 3 L11: 2.1423 L22: 3.7322
REMARK 3 L33: 2.6579 L12: 0.9551
REMARK 3 L13: -0.3963 L23: -1.4583
REMARK 3 S TENSOR
REMARK 3 S11: -0.0936 S12: 0.4888 S13: -0.3972
REMARK 3 S21: -0.7151 S22: 0.0128 S23: -0.2832
REMARK 3 S31: 0.3913 S32: 0.0405 S33: 0.0808
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): 27.0316 -26.9419 -0.7070
REMARK 3 T TENSOR
REMARK 3 T11: 0.0808 T22: 0.0624
REMARK 3 T33: 0.1258 T12: 0.0326
REMARK 3 T13: 0.0485 T23: -0.0377
REMARK 3 L TENSOR
REMARK 3 L11: 1.3939 L22: 2.0057
REMARK 3 L33: 1.5561 L12: -0.0237
REMARK 3 L13: -0.0841 L23: 0.1759
REMARK 3 S TENSOR
REMARK 3 S11: 0.0320 S12: 0.1324 S13: -0.1931
REMARK 3 S21: -0.1397 S22: -0.0576 S23: -0.2325
REMARK 3 S31: 0.2310 S32: 0.0757 S33: 0.0256
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 4X6X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-DEC-14.
REMARK 100 THE DEPOSITION ID IS D_1000204680.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUN-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 : 64285
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
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 (%) : 94.3
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.24200
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 (%): 52.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
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 64.70300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.27200
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 64.70300
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.27200
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 SER A 231 -167.52 -120.96
REMARK 500 GLU A 269 -143.39 -122.03
REMARK 500 ASP A 335 -127.75 61.97
REMARK 500 ASN A 359 -45.33 79.01
REMARK 500 LEU A 480 -126.93 66.41
REMARK 500 VAL A 498 -60.12 -107.20
REMARK 500 SER B 231 -166.84 -127.67
REMARK 500 GLU B 269 -139.08 -119.32
REMARK 500 ASP B 335 -127.93 59.17
REMARK 500 ASN B 359 -44.63 79.98
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 MET A 291 ASP A 292 149.78
REMARK 500 MET B 291 ASP B 292 147.77
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 S74 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue S74 B 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4X6Y RELATED DB: PDB
DBREF 4X6X A 230 555 UNP P34913 HYES_HUMAN 230 555
DBREF 4X6X B 230 555 UNP P34913 HYES_HUMAN 230 555
SEQADV 4X6X MET A 220 UNP P34913 EXPRESSION TAG
SEQADV 4X6X LYS A 221 UNP P34913 EXPRESSION TAG
SEQADV 4X6X LYS A 222 UNP P34913 EXPRESSION TAG
SEQADV 4X6X GLY A 223 UNP P34913 EXPRESSION TAG
SEQADV 4X6X HIS A 224 UNP P34913 EXPRESSION TAG
SEQADV 4X6X HIS A 225 UNP P34913 EXPRESSION TAG
SEQADV 4X6X HIS A 226 UNP P34913 EXPRESSION TAG
SEQADV 4X6X HIS A 227 UNP P34913 EXPRESSION TAG
SEQADV 4X6X HIS A 228 UNP P34913 EXPRESSION TAG
SEQADV 4X6X HIS A 229 UNP P34913 EXPRESSION TAG
SEQADV 4X6X MET B 220 UNP P34913 EXPRESSION TAG
SEQADV 4X6X LYS B 221 UNP P34913 EXPRESSION TAG
SEQADV 4X6X LYS B 222 UNP P34913 EXPRESSION TAG
SEQADV 4X6X GLY B 223 UNP P34913 EXPRESSION TAG
SEQADV 4X6X HIS B 224 UNP P34913 EXPRESSION TAG
SEQADV 4X6X HIS B 225 UNP P34913 EXPRESSION TAG
SEQADV 4X6X HIS B 226 UNP P34913 EXPRESSION TAG
SEQADV 4X6X HIS B 227 UNP P34913 EXPRESSION TAG
SEQADV 4X6X HIS B 228 UNP P34913 EXPRESSION TAG
SEQADV 4X6X 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 S74 A 601 36
HET S74 B 601 36
HETNAM S74 3-{4-[(1-{[(1S,2R,3S)-2,3-
HETNAM 2 S74 DIPHENYLCYCLOPROPYL]CARBAMOYL}PIPERIDIN-4-YL)
HETNAM 3 S74 OXY]PHENYL}PROPANOIC ACID
FORMUL 3 S74 2(C30 H32 N2 O4)
FORMUL 5 HOH *191(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 TYR A 276 ALA A 284 1 9
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 SER A 370 ALA A 377 1 8
HELIX 8 AA8 ASN A 378 PHE A 381 5 4
HELIX 9 AA9 ASP A 382 PHE A 387 1 6
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 GLY A 458 1 16
HELIX 15 AB6 PHE A 459 TRP A 465 1 7
HELIX 16 AB7 ASN A 468 LYS A 478 1 11
HELIX 17 AB8 VAL A 500 GLN A 505 5 6
HELIX 18 AB9 HIS A 506 TRP A 510 5 5
HELIX 19 AC1 TRP A 525 LYS A 530 1 6
HELIX 20 AC2 LYS A 530 ASP A 545 1 16
HELIX 21 AC3 ASN B 233 MET B 237 5 5
HELIX 22 AC4 SER B 270 ARG B 275 5 6
HELIX 23 AC5 TYR B 276 ALA B 284 1 9
HELIX 24 AC6 GLU B 304 TYR B 308 5 5
HELIX 25 AC7 CYS B 309 GLY B 325 1 17
HELIX 26 AC8 ASP B 335 TYR B 348 1 14
HELIX 27 AC9 SER B 370 ASN B 378 1 9
HELIX 28 AD1 PHE B 381 PHE B 387 1 7
HELIX 29 AD2 GLY B 391 ASN B 400 1 10
HELIX 30 AD3 ASN B 400 PHE B 409 1 10
HELIX 31 AD4 ALA B 411 SER B 415 5 5
HELIX 32 AD5 THR B 443 LYS B 455 1 13
HELIX 33 AD6 PHE B 459 TRP B 465 1 7
HELIX 34 AD7 ASN B 468 LYS B 478 1 11
HELIX 35 AD8 VAL B 500 GLN B 505 5 6
HELIX 36 AD9 HIS B 506 ILE B 511 1 6
HELIX 37 AE1 TRP B 525 LYS B 530 1 6
HELIX 38 AE2 LYS B 530 ASP B 545 1 16
SHEET 1 AA116 LEU A 514 ILE A 519 0
SHEET 2 AA116 ALA A 488 ALA A 493 1 N ALA A 488 O LYS A 515
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 TYR B 241 N HIS A 239
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 VAL B 261 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 VAL B 491 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 -9.31
CISPEP 2 PHE B 267 PRO B 268 0 -7.56
SITE 1 AC1 13 PHE A 267 ASP A 335 ILE A 363 TYR A 383
SITE 2 AC1 13 GLN A 384 PHE A 387 MET A 419 TYR A 466
SITE 3 AC1 13 VAL A 498 LEU A 499 MET A 503 HIS A 524
SITE 4 AC1 13 TRP A 525
SITE 1 AC2 14 PHE B 267 ASP B 335 MET B 339 ILE B 363
SITE 2 AC2 14 TYR B 383 GLN B 384 PHE B 387 LEU B 408
SITE 3 AC2 14 MET B 419 TYR B 466 VAL B 498 MET B 503
SITE 4 AC2 14 HIS B 524 TRP B 525
CRYST1 129.406 80.544 88.253 90.00 125.70 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 0.007728 0.000000 0.005553 0.00000
SCALE2 0.000000 0.012416 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013953 0.00000
TER 2547 ASP A 545
TER 5094 ASP B 545
MASTER 441 0 2 38 16 0 8 6 5355 2 72 52
END |