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HEADER HYDROLASE 11-JUL-21 7P4K
TITLE SOLUBLE EPOXIDE HYDROLASE IN COMPLEX WITH FL217
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIFUNCTIONAL EPOXIDE HYDROLASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.3.2.10,3.1.3.76;
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 GENE: EPHX2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS COMPLEX, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.NI,J.S.KRAMER,F.LILLICH,E.PROSCHAK,A.CHAIKUAD,S.KNAPP,STRUCTURAL
AUTHOR 2 GENOMICS CONSORTIUM (SGC)
REVDAT 1 06-JUL-22 7P4K 0
JRNL AUTH F.F.LILLICH,S.WILLEMS,X.NI,W.KILU,C.BORKOWSKY,M.BRODSKY,
JRNL AUTH 2 J.S.KRAMER,S.BRUNST,V.HERNANDEZ-OLMOS,J.HEERING,S.SCHIERLE,
JRNL AUTH 3 R.I.KESTNER,F.M.MAYSER,M.HELMSTADTER,T.GOBEL,L.WEIZEL,
JRNL AUTH 4 D.NAMGALADZE,A.KAISER,D.STEINHILBER,W.PFEILSCHIFTER,
JRNL AUTH 5 A.S.KAHNT,A.PROSCHAK,A.CHAIKUAD,S.KNAPP,D.MERK,E.PROSCHAK
JRNL TITL STRUCTURE-BASED DESIGN OF DUAL PARTIAL PEROXISOME
JRNL TITL 2 PROLIFERATOR-ACTIVATED RECEPTOR GAMMA AGONISTS/SOLUBLE
JRNL TITL 3 EPOXIDE HYDROLASE INHIBITORS.
JRNL REF J.MED.CHEM. V. 64 17259 2021
JRNL REFN ISSN 0022-2623
JRNL PMID 34818007
JRNL DOI 10.1021/ACS.JMEDCHEM.1C01331
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.02
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.7
REMARK 3 NUMBER OF REFLECTIONS : 33693
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1811
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) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2527
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.60
REMARK 3 BIN R VALUE (WORKING SET) : 0.2380
REMARK 3 BIN FREE R VALUE SET COUNT : 148
REMARK 3 BIN FREE R VALUE : 0.2630
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4865
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 76
REMARK 3 SOLVENT ATOMS : 74
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.19
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.84000
REMARK 3 B22 (A**2) : -5.72000
REMARK 3 B33 (A**2) : -0.35000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.75000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.244
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.194
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.145
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.128
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5121 ; 0.013 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 4659 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6970 ; 1.169 ; 1.640
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10738 ; 1.192 ; 1.585
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 619 ; 8.465 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 251 ;30.903 ;22.112
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 816 ;15.646 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;16.605 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 629 ; 0.063 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6047 ; 0.013 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1213 ; 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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 229 547 B 229 547 10084 0.070 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
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 229 A 352
REMARK 3 ORIGIN FOR THE GROUP (A): -6.1248 -3.6325 39.8878
REMARK 3 T TENSOR
REMARK 3 T11: 0.0905 T22: 0.1313
REMARK 3 T33: 0.0539 T12: -0.0103
REMARK 3 T13: 0.0015 T23: 0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 1.2408 L22: 2.2661
REMARK 3 L33: 1.6716 L12: -0.2316
REMARK 3 L13: -0.4363 L23: 0.7801
REMARK 3 S TENSOR
REMARK 3 S11: 0.0258 S12: 0.0410 S13: 0.0281
REMARK 3 S21: 0.0304 S22: 0.0018 S23: -0.1265
REMARK 3 S31: -0.1381 S32: 0.0092 S33: -0.0276
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 353 A 547
REMARK 3 ORIGIN FOR THE GROUP (A): -1.2013 -14.8953 31.4266
REMARK 3 T TENSOR
REMARK 3 T11: 0.0420 T22: 0.1195
REMARK 3 T33: 0.0645 T12: 0.0310
REMARK 3 T13: 0.0133 T23: -0.0494
REMARK 3 L TENSOR
REMARK 3 L11: 1.5054 L22: 2.1933
REMARK 3 L33: 2.2790 L12: -0.0310
REMARK 3 L13: -0.2500 L23: 0.2245
REMARK 3 S TENSOR
REMARK 3 S11: 0.0566 S12: 0.1239 S13: -0.1904
REMARK 3 S21: -0.1901 S22: -0.0142 S23: -0.2298
REMARK 3 S31: 0.1014 S32: 0.1892 S33: -0.0424
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 : B 229 B 547
REMARK 3 ORIGIN FOR THE GROUP (A): -23.9353 11.8507 62.6433
REMARK 3 T TENSOR
REMARK 3 T11: 0.2050 T22: 0.1463
REMARK 3 T33: 0.0076 T12: 0.0065
REMARK 3 T13: -0.0128 T23: -0.0206
REMARK 3 L TENSOR
REMARK 3 L11: 0.9625 L22: 1.7417
REMARK 3 L33: 1.6656 L12: -0.0534
REMARK 3 L13: -0.4119 L23: 0.4744
REMARK 3 S TENSOR
REMARK 3 S11: -0.0491 S12: 0.0149 S13: -0.0120
REMARK 3 S21: 0.2041 S22: -0.0571 S23: 0.0270
REMARK 3 S31: -0.1185 S32: -0.1910 S33: 0.1061
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: U VALUES : WITH TLS ADDED HYDROGENS
REMARK 3 HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 4
REMARK 4 7P4K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JUL-21.
REMARK 100 THE DEPOSITION ID IS D_1292116989.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-NOV-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00004
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35542
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 44.020
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.22
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 6FR2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28 % (W/V) POLYETHYLENGLYCOL (PEG)
REMARK 280 6000, 70 MM AMMONIUM ACETAT, 200 MM MAGNESIUM ACETAT, 100 MM
REMARK 280 SODIUM CACODYLATE AT PH 6.13, VAPOR DIFFUSION, TEMPERATURE 293K
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 63.91000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.66300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 63.91000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 39.66300
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 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: 1450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 3.0 KCAL/MOL
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 219
REMARK 465 ALA A 220
REMARK 465 SER A 221
REMARK 465 LEU A 222
REMARK 465 ASN A 223
REMARK 465 THR A 224
REMARK 465 PRO A 225
REMARK 465 ALA A 226
REMARK 465 PRO A 227
REMARK 465 LEU A 228
REMARK 465 ILE A 375
REMARK 465 LYS A 376
REMARK 465 ALA A 377
REMARK 465 ASN A 378
REMARK 465 PRO A 379
REMARK 465 VAL A 380
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 LEU A 556
REMARK 465 LEU A 557
REMARK 465 GLU A 558
REMARK 465 HIS A 559
REMARK 465 HIS A 560
REMARK 465 HIS A 561
REMARK 465 HIS A 562
REMARK 465 HIS A 563
REMARK 465 HIS A 564
REMARK 465 MET B 219
REMARK 465 ALA B 220
REMARK 465 SER B 221
REMARK 465 LEU B 222
REMARK 465 ASN B 223
REMARK 465 THR B 224
REMARK 465 PRO B 225
REMARK 465 ALA B 226
REMARK 465 PRO B 227
REMARK 465 LEU B 228
REMARK 465 SER B 374
REMARK 465 ILE B 375
REMARK 465 LYS B 376
REMARK 465 ALA B 377
REMARK 465 ASN B 378
REMARK 465 PRO B 379
REMARK 465 VAL B 380
REMARK 465 PHE B 381
REMARK 465 MET B 419
REMARK 465 HIS B 420
REMARK 465 LYS B 421
REMARK 465 VAL B 422
REMARK 465 CYS B 423
REMARK 465 GLU B 424
REMARK 465 ALA B 425
REMARK 465 GLY B 426
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 465 LEU B 556
REMARK 465 LEU B 557
REMARK 465 GLU B 558
REMARK 465 HIS B 559
REMARK 465 HIS B 560
REMARK 465 HIS B 561
REMARK 465 HIS B 562
REMARK 465 HIS B 563
REMARK 465 HIS B 564
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 369 CG SD CE
REMARK 470 LEU A 372 CG CD1 CD2
REMARK 470 GLU A 373 CG CD OE1 OE2
REMARK 470 SER A 374 OG
REMARK 470 PHE A 381 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP A 382 CG OD1 OD2
REMARK 470 SER A 418 OG
REMARK 470 HIS A 420 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 421 CG CD CE NZ
REMARK 470 GLU A 424 CG CD OE1 OE2
REMARK 470 GLU A 434 CG CD OE1 OE2
REMARK 470 GLU A 435 CG CD OE1 OE2
REMARK 470 GLU A 470 CG CD OE1 OE2
REMARK 470 TRP A 510 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 510 CZ3 CH2
REMARK 470 HIS A 513 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A 547 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 247 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 368 CG OD1 ND2
REMARK 470 MET B 369 CG SD CE
REMARK 470 SER B 370 OG
REMARK 470 LEU B 372 CG CD1 CD2
REMARK 470 GLU B 373 CG CD OE1 OE2
REMARK 470 ASP B 382 CG OD1 OD2
REMARK 470 SER B 418 OG
REMARK 470 ASN B 431 CG OD1 ND2
REMARK 470 GLU B 470 CG CD OE1 OE2
REMARK 470 LEU B 480 CG CD1 CD2
REMARK 470 GLU B 533 CG CD OE1 OE2
REMARK 470 ARG B 547 CG CD NE CZ NH1 NH2
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 -145.61 -123.26
REMARK 500 ASP A 335 -125.51 64.80
REMARK 500 ASN A 359 -44.16 85.93
REMARK 500 GLU A 435 79.16 -117.10
REMARK 500 GLU B 269 -148.76 -124.22
REMARK 500 ASP B 335 -127.04 65.61
REMARK 500 ASN B 359 -45.70 83.71
REMARK 500 GLU B 435 79.67 -119.05
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 292 137.52
REMARK 500 MET B 291 ASP B 292 138.48
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7P4K A 222 555 UNP P34913 HYES_HUMAN 222 555
DBREF 7P4K B 222 555 UNP P34913 HYES_HUMAN 222 555
SEQADV 7P4K MET A 219 UNP P34913 INITIATING METHIONINE
SEQADV 7P4K ALA A 220 UNP P34913 EXPRESSION TAG
SEQADV 7P4K SER A 221 UNP P34913 EXPRESSION TAG
SEQADV 7P4K LEU A 556 UNP P34913 EXPRESSION TAG
SEQADV 7P4K LEU A 557 UNP P34913 EXPRESSION TAG
SEQADV 7P4K GLU A 558 UNP P34913 EXPRESSION TAG
SEQADV 7P4K HIS A 559 UNP P34913 EXPRESSION TAG
SEQADV 7P4K HIS A 560 UNP P34913 EXPRESSION TAG
SEQADV 7P4K HIS A 561 UNP P34913 EXPRESSION TAG
SEQADV 7P4K HIS A 562 UNP P34913 EXPRESSION TAG
SEQADV 7P4K HIS A 563 UNP P34913 EXPRESSION TAG
SEQADV 7P4K HIS A 564 UNP P34913 EXPRESSION TAG
SEQADV 7P4K MET B 219 UNP P34913 INITIATING METHIONINE
SEQADV 7P4K ALA B 220 UNP P34913 EXPRESSION TAG
SEQADV 7P4K SER B 221 UNP P34913 EXPRESSION TAG
SEQADV 7P4K LEU B 556 UNP P34913 EXPRESSION TAG
SEQADV 7P4K LEU B 557 UNP P34913 EXPRESSION TAG
SEQADV 7P4K GLU B 558 UNP P34913 EXPRESSION TAG
SEQADV 7P4K HIS B 559 UNP P34913 EXPRESSION TAG
SEQADV 7P4K HIS B 560 UNP P34913 EXPRESSION TAG
SEQADV 7P4K HIS B 561 UNP P34913 EXPRESSION TAG
SEQADV 7P4K HIS B 562 UNP P34913 EXPRESSION TAG
SEQADV 7P4K HIS B 563 UNP P34913 EXPRESSION TAG
SEQADV 7P4K HIS B 564 UNP P34913 EXPRESSION TAG
SEQRES 1 A 346 MET ALA SER LEU ASN THR PRO ALA PRO LEU PRO THR SER
SEQRES 2 A 346 CYS ASN PRO SER ASP MET SER HIS GLY TYR VAL THR VAL
SEQRES 3 A 346 LYS PRO ARG VAL ARG LEU HIS PHE VAL GLU LEU GLY SER
SEQRES 4 A 346 GLY PRO ALA VAL CYS LEU CYS HIS GLY PHE PRO GLU SER
SEQRES 5 A 346 TRP TYR SER TRP ARG TYR GLN ILE PRO ALA LEU ALA GLN
SEQRES 6 A 346 ALA GLY TYR ARG VAL LEU ALA MET ASP MET LYS GLY TYR
SEQRES 7 A 346 GLY GLU SER SER ALA PRO PRO GLU ILE GLU GLU TYR CYS
SEQRES 8 A 346 MET GLU VAL LEU CYS LYS GLU MET VAL THR PHE LEU ASP
SEQRES 9 A 346 LYS LEU GLY LEU SER GLN ALA VAL PHE ILE GLY HIS ASP
SEQRES 10 A 346 TRP GLY GLY MET LEU VAL TRP TYR MET ALA LEU PHE TYR
SEQRES 11 A 346 PRO GLU ARG VAL ARG ALA VAL ALA SER LEU ASN THR PRO
SEQRES 12 A 346 PHE ILE PRO ALA ASN PRO ASN MET SER PRO LEU GLU SER
SEQRES 13 A 346 ILE LYS ALA ASN PRO VAL PHE ASP TYR GLN LEU TYR PHE
SEQRES 14 A 346 GLN GLU PRO GLY VAL ALA GLU ALA GLU LEU GLU GLN ASN
SEQRES 15 A 346 LEU SER ARG THR PHE LYS SER LEU PHE ARG ALA SER ASP
SEQRES 16 A 346 GLU SER VAL LEU SER MET HIS LYS VAL CYS GLU ALA GLY
SEQRES 17 A 346 GLY LEU PHE VAL ASN SER PRO GLU GLU PRO SER LEU SER
SEQRES 18 A 346 ARG MET VAL THR GLU GLU GLU ILE GLN PHE TYR VAL GLN
SEQRES 19 A 346 GLN PHE LYS LYS SER GLY PHE ARG GLY PRO LEU ASN TRP
SEQRES 20 A 346 TYR ARG ASN MET GLU ARG ASN TRP LYS TRP ALA CYS LYS
SEQRES 21 A 346 SER LEU GLY ARG LYS ILE LEU ILE PRO ALA LEU MET VAL
SEQRES 22 A 346 THR ALA GLU LYS ASP PHE VAL LEU VAL PRO GLN MET SER
SEQRES 23 A 346 GLN HIS MET GLU ASP TRP ILE PRO HIS LEU LYS ARG GLY
SEQRES 24 A 346 HIS ILE GLU ASP CYS GLY HIS TRP THR GLN MET ASP LYS
SEQRES 25 A 346 PRO THR GLU VAL ASN GLN ILE LEU ILE LYS TRP LEU ASP
SEQRES 26 A 346 SER ASP ALA ARG ASN PRO PRO VAL VAL SER LYS MET LEU
SEQRES 27 A 346 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 346 MET ALA SER LEU ASN THR PRO ALA PRO LEU PRO THR SER
SEQRES 2 B 346 CYS ASN PRO SER ASP MET SER HIS GLY TYR VAL THR VAL
SEQRES 3 B 346 LYS PRO ARG VAL ARG LEU HIS PHE VAL GLU LEU GLY SER
SEQRES 4 B 346 GLY PRO ALA VAL CYS LEU CYS HIS GLY PHE PRO GLU SER
SEQRES 5 B 346 TRP TYR SER TRP ARG TYR GLN ILE PRO ALA LEU ALA GLN
SEQRES 6 B 346 ALA GLY TYR ARG VAL LEU ALA MET ASP MET LYS GLY TYR
SEQRES 7 B 346 GLY GLU SER SER ALA PRO PRO GLU ILE GLU GLU TYR CYS
SEQRES 8 B 346 MET GLU VAL LEU CYS LYS GLU MET VAL THR PHE LEU ASP
SEQRES 9 B 346 LYS LEU GLY LEU SER GLN ALA VAL PHE ILE GLY HIS ASP
SEQRES 10 B 346 TRP GLY GLY MET LEU VAL TRP TYR MET ALA LEU PHE TYR
SEQRES 11 B 346 PRO GLU ARG VAL ARG ALA VAL ALA SER LEU ASN THR PRO
SEQRES 12 B 346 PHE ILE PRO ALA ASN PRO ASN MET SER PRO LEU GLU SER
SEQRES 13 B 346 ILE LYS ALA ASN PRO VAL PHE ASP TYR GLN LEU TYR PHE
SEQRES 14 B 346 GLN GLU PRO GLY VAL ALA GLU ALA GLU LEU GLU GLN ASN
SEQRES 15 B 346 LEU SER ARG THR PHE LYS SER LEU PHE ARG ALA SER ASP
SEQRES 16 B 346 GLU SER VAL LEU SER MET HIS LYS VAL CYS GLU ALA GLY
SEQRES 17 B 346 GLY LEU PHE VAL ASN SER PRO GLU GLU PRO SER LEU SER
SEQRES 18 B 346 ARG MET VAL THR GLU GLU GLU ILE GLN PHE TYR VAL GLN
SEQRES 19 B 346 GLN PHE LYS LYS SER GLY PHE ARG GLY PRO LEU ASN TRP
SEQRES 20 B 346 TYR ARG ASN MET GLU ARG ASN TRP LYS TRP ALA CYS LYS
SEQRES 21 B 346 SER LEU GLY ARG LYS ILE LEU ILE PRO ALA LEU MET VAL
SEQRES 22 B 346 THR ALA GLU LYS ASP PHE VAL LEU VAL PRO GLN MET SER
SEQRES 23 B 346 GLN HIS MET GLU ASP TRP ILE PRO HIS LEU LYS ARG GLY
SEQRES 24 B 346 HIS ILE GLU ASP CYS GLY HIS TRP THR GLN MET ASP LYS
SEQRES 25 B 346 PRO THR GLU VAL ASN GLN ILE LEU ILE LYS TRP LEU ASP
SEQRES 26 B 346 SER ASP ALA ARG ASN PRO PRO VAL VAL SER LYS MET LEU
SEQRES 27 B 346 LEU GLU HIS HIS HIS HIS HIS HIS
HET 5IV A 601 38
HET 5IV B 601 38
HETNAM 5IV ~{N}-[[4-(CYCLOPROPYLSULFONYLAMINO)-2-
HETNAM 2 5IV (TRIFLUOROMETHYL)PHENYL]METHYL]-1-[(3-FLUOROPHENYL)
HETNAM 3 5IV METHYL]INDOLE-5-CARBOXAMIDE
FORMUL 3 5IV 2(C27 H23 F4 N3 O3 S)
FORMUL 5 HOH *74(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 ASP A 382 PHE A 387 1 6
HELIX 8 AA8 GLY A 391 ASN A 400 1 10
HELIX 9 AA9 ASN A 400 PHE A 409 1 10
HELIX 10 AB1 ALA A 411 SER A 415 5 5
HELIX 11 AB2 LYS A 421 GLY A 426 1 6
HELIX 12 AB3 THR A 443 LYS A 455 1 13
HELIX 13 AB4 PHE A 459 TRP A 465 1 7
HELIX 14 AB5 ASN A 468 LYS A 478 1 11
HELIX 15 AB6 VAL A 500 GLN A 505 5 6
HELIX 16 AB7 HIS A 506 TRP A 510 5 5
HELIX 17 AB8 TRP A 525 LYS A 530 1 6
HELIX 18 AB9 LYS A 530 ALA A 546 1 17
HELIX 19 AC1 ASN B 233 MET B 237 5 5
HELIX 20 AC2 SER B 270 ARG B 275 5 6
HELIX 21 AC3 GLN B 277 ALA B 284 1 8
HELIX 22 AC4 GLU B 304 TYR B 308 5 5
HELIX 23 AC5 CYS B 309 GLY B 325 1 17
HELIX 24 AC6 ASP B 335 TYR B 348 1 14
HELIX 25 AC7 TYR B 383 PHE B 387 1 5
HELIX 26 AC8 GLY B 391 ASN B 400 1 10
HELIX 27 AC9 ASN B 400 PHE B 409 1 10
HELIX 28 AD1 ALA B 411 SER B 415 5 5
HELIX 29 AD2 THR B 443 LYS B 455 1 13
HELIX 30 AD3 PHE B 459 TRP B 465 1 7
HELIX 31 AD4 ASN B 468 LYS B 478 1 11
HELIX 32 AD5 VAL B 500 GLN B 505 5 6
HELIX 33 AD6 HIS B 506 TRP B 510 5 5
HELIX 34 AD7 TRP B 525 LYS B 530 1 6
HELIX 35 AD8 LYS B 530 ALA B 546 1 17
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 ARG A 287 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 VAL A 242 O LEU A 250
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 VAL B 261 O ARG B 287
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 LEU B 514 ILE B 519 1 O LYS B 515 N ALA B 488
CISPEP 1 PHE A 267 PRO A 268 0 -20.00
CISPEP 2 PHE B 267 PRO B 268 0 -22.44
CRYST1 127.820 79.326 88.599 90.00 126.65 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 0.007824 0.000000 0.005821 0.00000
SCALE2 0.000000 0.012606 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014068 0.00000
TER 2463 ARG A 547
TER 4893 ARG B 547
MASTER 454 0 2 35 16 0 0 6 5015 2 76 54
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