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HEADER HYDROLASE 28-AUG-20 7A7G
TITLE SOLUBLE EPOXIDE HYDROLASE IN COMPLEX WITH TK90
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,T.KIRCHNER,E.PROSCHAK,A.CHAIKUAD,S.KNAPP,STRUCTURAL
AUTHOR 2 GENOMICS CONSORTIUM (SGC)
REVDAT 1 04-AUG-21 7A7G 0
JRNL AUTH M.HARTMANN,S.I.BIBLI,D.TEWS,X.NI,T.KIRCHER,J.S.KRAMER,
JRNL AUTH 2 W.KILU,J.HEERING,V.HERNANDEZ-OLMOS,L.WEIZEL,G.K.E.SCRIBA,
JRNL AUTH 3 S.KRAIT,S.KNAPP,A.CHAIKUAD,D.MERK,I.FLEMING,
JRNL AUTH 4 P.FISCHER-POSOVSZKY,E.PROSCHAK
JRNL TITL COMBINED CARDIOPROTECTIVE AND ADIPOCYTE BROWNING EFFECTS
JRNL TITL 2 PROMOTED BY THE EUTOMER OF DUAL SEH/PPAR GAMMA MODULATOR.
JRNL REF J.MED.CHEM. V. 64 2815 2021
JRNL REFN ISSN 0022-2623
JRNL PMID 33620196
JRNL DOI 10.1021/ACS.JMEDCHEM.0C02063
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0258
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 84.0
REMARK 3 NUMBER OF REFLECTIONS : 23195
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) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1213
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1652
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.38
REMARK 3 BIN R VALUE (WORKING SET) : 0.2770
REMARK 3 BIN FREE R VALUE SET COUNT : 97
REMARK 3 BIN FREE R VALUE : 0.2520
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4931
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 33
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.33
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.21000
REMARK 3 B22 (A**2) : -1.13000
REMARK 3 B33 (A**2) : 0.85000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.68000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.676
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.296
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.242
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.151
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.914
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5166 ; 0.012 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 4571 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7034 ; 1.108 ; 1.640
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10567 ; 1.117 ; 1.579
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 637 ; 9.364 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 251 ;31.669 ;21.673
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 783 ;16.864 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;17.505 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 644 ; 0.052 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5979 ; 0.013 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1151 ; 0.005 ; 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 10273 0.060 0.050
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 229 A 368
REMARK 3 ORIGIN FOR THE GROUP (A): 6.3580 4.0087 22.9487
REMARK 3 T TENSOR
REMARK 3 T11: 0.3454 T22: 0.0092
REMARK 3 T33: 0.1020 T12: -0.0260
REMARK 3 T13: 0.0487 T23: -0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 1.8156 L22: 1.9702
REMARK 3 L33: 1.6529 L12: -0.7568
REMARK 3 L13: -0.5169 L23: 1.1086
REMARK 3 S TENSOR
REMARK 3 S11: -0.0752 S12: 0.0093 S13: -0.0984
REMARK 3 S21: 0.1529 S22: -0.0396 S23: 0.0076
REMARK 3 S31: 0.0878 S32: -0.1047 S33: 0.1148
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 547
REMARK 3 ORIGIN FOR THE GROUP (A): -1.3048 15.3087 27.9497
REMARK 3 T TENSOR
REMARK 3 T11: 0.4273 T22: 0.0761
REMARK 3 T33: 0.1016 T12: 0.0334
REMARK 3 T13: 0.0687 T23: -0.0723
REMARK 3 L TENSOR
REMARK 3 L11: 1.6658 L22: 2.4337
REMARK 3 L33: 1.4041 L12: -0.1688
REMARK 3 L13: -1.0890 L23: 0.4156
REMARK 3 S TENSOR
REMARK 3 S11: -0.0302 S12: 0.0054 S13: 0.1012
REMARK 3 S21: 0.2464 S22: -0.0722 S23: 0.1639
REMARK 3 S31: -0.2374 S32: -0.2185 S33: 0.1024
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 368
REMARK 3 ORIGIN FOR THE GROUP (A): 23.7236 -4.5046 3.2493
REMARK 3 T TENSOR
REMARK 3 T11: 0.3051 T22: 0.0085
REMARK 3 T33: 0.1388 T12: 0.0007
REMARK 3 T13: 0.0475 T23: 0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 1.7274 L22: 1.5815
REMARK 3 L33: 2.0223 L12: -0.5372
REMARK 3 L13: -0.7629 L23: 1.3524
REMARK 3 S TENSOR
REMARK 3 S11: 0.0942 S12: 0.0628 S13: 0.0925
REMARK 3 S21: -0.0404 S22: -0.0132 S23: -0.1614
REMARK 3 S31: -0.1895 S32: 0.0451 S33: -0.0810
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 369 B 547
REMARK 3 ORIGIN FOR THE GROUP (A): 27.0981 -15.8017 -5.3969
REMARK 3 T TENSOR
REMARK 3 T11: 0.2597 T22: 0.0299
REMARK 3 T33: 0.1326 T12: 0.0332
REMARK 3 T13: 0.0991 T23: -0.0228
REMARK 3 L TENSOR
REMARK 3 L11: 2.0253 L22: 1.9355
REMARK 3 L33: 2.6935 L12: -0.0678
REMARK 3 L13: -1.2311 L23: 0.1652
REMARK 3 S TENSOR
REMARK 3 S11: 0.0402 S12: 0.2011 S13: -0.2501
REMARK 3 S21: -0.1314 S22: -0.0551 S23: -0.2117
REMARK 3 S31: 0.1704 S32: -0.0014 S33: 0.0149
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 7A7G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE.
REMARK 100 THE DEPOSITION ID IS D_1292110991.
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 : 6.13
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 0.7.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24408
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 39.660
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.7
REMARK 200 DATA REDUNDANCY : 2.100
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.24900
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: PHASER
REMARK 200 STARTING MODEL: 6FR2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG6000, 70 MM AMMONIUMACETAT, 200
REMARK 280 MM MAGNESIUM ACETAT TETRAHYDRATE, PH 6.13, VAPOR DIFFUSION,
REMARK 280 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 68.90400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.62450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 68.90400
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 39.62450
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 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 LYS A 376
REMARK 465 ALA A 377
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 ASN B 378
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 LYS A 315 CG CD CE NZ
REMARK 470 ASN A 366 CG OD1 ND2
REMARK 470 ASN A 368 CG OD1 ND2
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 ILE A 375 CG1 CG2 CD1
REMARK 470 ASN A 378 CG OD1 ND2
REMARK 470 VAL A 380 CG1 CG2
REMARK 470 HIS A 420 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 421 CG CD CE NZ
REMARK 470 CYS A 423 SG
REMARK 470 GLU A 424 CG CD OE1 OE2
REMARK 470 ASN A 431 CG OD1 ND2
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 LYS A 478 CG CD CE NZ
REMARK 470 LEU A 480 CG CD1 CD2
REMARK 470 GLN A 502 CG CD OE1 NE2
REMARK 470 TRP A 510 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 510 CZ3 CH2
REMARK 470 ARG A 547 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 283 CG CD OE1 NE2
REMARK 470 LYS B 315 CG CD CE NZ
REMARK 470 ASN B 366 CG OD1 ND2
REMARK 470 ASN B 368 CG OD1 ND2
REMARK 470 MET B 369 CG SD CE
REMARK 470 LEU B 372 CG CD1 CD2
REMARK 470 GLU B 373 CG CD OE1 OE2
REMARK 470 SER B 374 OG
REMARK 470 ILE B 375 CG1 CG2 CD1
REMARK 470 LYS B 376 CG CD CE NZ
REMARK 470 ASP B 382 CG OD1 OD2
REMARK 470 GLU B 389 CG CD OE1 OE2
REMARK 470 GLN B 399 CG CD OE1 NE2
REMARK 470 LYS B 421 CG CD CE NZ
REMARK 470 CYS B 423 SG
REMARK 470 GLU B 424 CG CD OE1 OE2
REMARK 470 GLU B 434 CG CD OE1 OE2
REMARK 470 GLU B 470 CG CD OE1 OE2
REMARK 470 LYS B 474 CG CD CE NZ
REMARK 470 LYS B 478 CG CD CE NZ
REMARK 470 LEU B 480 CG CD1 CD2
REMARK 470 LEU B 485 CG CD1 CD2
REMARK 470 GLN B 502 CG CD OE1 NE2
REMARK 470 TRP B 510 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 510 CZ3 CH2
REMARK 470 LYS B 515 CG CD CE NZ
REMARK 470 LYS B 540 CG CD CE NZ
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 SER A 231 -168.22 -102.12
REMARK 500 LYS A 245 158.96 176.48
REMARK 500 GLU A 269 -137.14 -115.33
REMARK 500 ASP A 335 -125.46 69.39
REMARK 500 ASN A 359 -47.01 78.42
REMARK 500 PRO A 379 -6.99 -55.39
REMARK 500 GLU A 435 71.21 -113.37
REMARK 500 VAL A 498 -60.86 -104.62
REMARK 500 LYS A 530 58.58 -141.60
REMARK 500 ALA A 546 -37.06 -132.61
REMARK 500 SER B 231 -166.14 -101.03
REMARK 500 LYS B 245 163.85 179.77
REMARK 500 GLU B 269 -138.05 -116.02
REMARK 500 ASP B 335 -126.30 68.83
REMARK 500 ASN B 359 -46.56 76.64
REMARK 500 ILE B 375 -70.10 -71.31
REMARK 500 LYS B 376 38.08 -86.20
REMARK 500 GLU B 435 75.32 -113.04
REMARK 500 LEU B 480 130.55 -38.42
REMARK 500 VAL B 498 -61.23 -105.41
REMARK 500 HIS B 513 33.99 -96.38
REMARK 500 LYS B 530 58.00 -142.58
REMARK 500 ALA B 546 -35.26 -131.21
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 292 136.03
REMARK 500 MET B 291 ASP B 292 135.70
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 TK9 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TK9 B 601
DBREF 7A7G A 222 555 UNP P34913 HYES_HUMAN 222 555
DBREF 7A7G B 222 555 UNP P34913 HYES_HUMAN 222 555
SEQADV 7A7G MET A 219 UNP P34913 INITIATING METHIONINE
SEQADV 7A7G ALA A 220 UNP P34913 EXPRESSION TAG
SEQADV 7A7G SER A 221 UNP P34913 EXPRESSION TAG
SEQADV 7A7G LEU A 556 UNP P34913 EXPRESSION TAG
SEQADV 7A7G LEU A 557 UNP P34913 EXPRESSION TAG
SEQADV 7A7G GLU A 558 UNP P34913 EXPRESSION TAG
SEQADV 7A7G HIS A 559 UNP P34913 EXPRESSION TAG
SEQADV 7A7G HIS A 560 UNP P34913 EXPRESSION TAG
SEQADV 7A7G HIS A 561 UNP P34913 EXPRESSION TAG
SEQADV 7A7G HIS A 562 UNP P34913 EXPRESSION TAG
SEQADV 7A7G HIS A 563 UNP P34913 EXPRESSION TAG
SEQADV 7A7G HIS A 564 UNP P34913 EXPRESSION TAG
SEQADV 7A7G MET B 219 UNP P34913 INITIATING METHIONINE
SEQADV 7A7G ALA B 220 UNP P34913 EXPRESSION TAG
SEQADV 7A7G SER B 221 UNP P34913 EXPRESSION TAG
SEQADV 7A7G LEU B 556 UNP P34913 EXPRESSION TAG
SEQADV 7A7G LEU B 557 UNP P34913 EXPRESSION TAG
SEQADV 7A7G GLU B 558 UNP P34913 EXPRESSION TAG
SEQADV 7A7G HIS B 559 UNP P34913 EXPRESSION TAG
SEQADV 7A7G HIS B 560 UNP P34913 EXPRESSION TAG
SEQADV 7A7G HIS B 561 UNP P34913 EXPRESSION TAG
SEQADV 7A7G HIS B 562 UNP P34913 EXPRESSION TAG
SEQADV 7A7G HIS B 563 UNP P34913 EXPRESSION TAG
SEQADV 7A7G 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 TK9 A 601 29
HET TK9 B 601 29
HETNAM TK9 (2~{R})-2-[[4-[[4-METHOXY-2-(TRIFLUOROMETHYL)
HETNAM 2 TK9 PHENYL]METHYLCARBAMOYL]PHENYL]METHYL]BUTANOIC ACID
FORMUL 3 TK9 2(C21 H22 F3 N O4)
FORMUL 5 HOH *33(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 LEU A 324 1 16
HELIX 6 AA6 ASP A 335 TYR A 348 1 14
HELIX 7 AA7 SER A 370 ILE A 375 1 6
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 LYS A 455 1 13
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 TRP A 525 LYS A 530 1 6
HELIX 19 AC1 LYS A 530 ALA A 546 1 17
HELIX 20 AC2 ASN B 233 MET B 237 5 5
HELIX 21 AC3 SER B 270 ARG B 275 5 6
HELIX 22 AC4 GLN B 277 ALA B 284 1 8
HELIX 23 AC5 GLU B 304 TYR B 308 5 5
HELIX 24 AC6 CYS B 309 LEU B 324 1 16
HELIX 25 AC7 ASP B 335 TYR B 348 1 14
HELIX 26 AC8 SER B 370 LYS B 376 1 7
HELIX 27 AC9 PRO B 379 PHE B 381 5 3
HELIX 28 AD1 ASP B 382 PHE B 387 1 6
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 LYS B 421 GLY B 426 1 6
HELIX 33 AD6 THR B 443 LYS B 455 1 13
HELIX 34 AD7 PHE B 459 TRP B 465 1 7
HELIX 35 AD8 ASN B 468 LYS B 478 1 11
HELIX 36 AD9 VAL B 500 GLN B 505 5 6
HELIX 37 AE1 HIS B 506 ILE B 511 1 6
HELIX 38 AE2 TRP B 525 LYS B 530 1 6
HELIX 39 AE3 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 ASP A 292 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 LEU B 250 N VAL B 242
SHEET 11 AA116 ARG B 287 ASP B 292 -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 LEU B 514 ILE B 519 1 O LYS B 515 N ALA B 488
CISPEP 1 PHE A 267 PRO A 268 0 -22.23
CISPEP 2 PHE B 267 PRO B 268 0 -19.42
SITE 1 AC1 12 PHE A 267 PRO A 268 ASP A 335 MET A 339
SITE 2 AC1 12 TYR A 383 GLN A 384 LEU A 408 MET A 419
SITE 3 AC1 12 TYR A 466 VAL A 498 MET A 503 HIS A 524
SITE 1 AC2 13 PHE B 267 PRO B 268 ASP B 335 TRP B 336
SITE 2 AC2 13 MET B 339 TYR B 383 GLN B 384 LEU B 408
SITE 3 AC2 13 MET B 419 TYR B 466 VAL B 498 MET B 503
SITE 4 AC2 13 HIS B 524
CRYST1 137.808 79.249 90.443 90.00 130.62 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 0.007256 0.000000 0.006225 0.00000
SCALE2 0.000000 0.012618 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014567 0.00000
TER 2472 ARG A 547
TER 4958 ARG B 547
MASTER 498 0 2 39 16 0 7 6 5022 2 58 54
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