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HEADER HYDROLASE 06-APR-20 6YL4
TITLE SOLUBLE EPOXIDE HYDROLASE IN COMPLEX WITH 3-((R)-3-(1-HYDROXYUREIDO)
TITLE 2 BUT-1-YN-1-YL)-N-((S)-3-PHENYL-3-(4-TRIFLUOROMETHOXY)PHENYL)PROPYL)
TITLE 3 BENZAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIFUNCTIONAL EPOXIDE HYDROLASE 2;
COMPND 3 CHAIN: A;
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 INHIBITOR, COMPLEX, SEH, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.S.KRAMER,D.POGORYELOV,K.HIESINGER,E.PROSCHAK
REVDAT 1 21-OCT-20 6YL4 0
JRNL AUTH K.HIESINGER,J.S.KRAMER,S.BEYER,T.ECKES,S.BRUNST,C.FLAUAUS,
JRNL AUTH 2 S.K.WITTMANN,L.WEIZEL,A.KAISER,S.B.M.KRETSCHMER,S.GEORGE,
JRNL AUTH 3 C.ANGIONI,J.HEERING,G.GEISSLINGER,M.SCHUBERT-ZSILAVECZ,
JRNL AUTH 4 A.SCHMIDTKO,D.POGORYELOV,J.PFEILSCHIFTER,B.HOFMANN,
JRNL AUTH 5 D.STEINHILBER,S.SCHWALM,E.PROSCHAK
JRNL TITL DESIGN, SYNTHESIS, AND STRUCTURE-ACTIVITY RELATIONSHIP
JRNL TITL 2 STUDIES OF DUAL INHIBITORS OF SOLUBLE EPOXIDE HYDROLASE AND
JRNL TITL 3 5-LIPOXYGENASE.
JRNL REF J.MED.CHEM. 2020
JRNL REFN ISSN 0022-2623
JRNL PMID 33044073
JRNL DOI 10.1021/ACS.JMEDCHEM.0C00561
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.12_2829
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.12
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 26663
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.400
REMARK 3 FREE R VALUE TEST SET COUNT : 1173
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 46.1190 - 4.0017 1.00 3362 154 0.1678 0.1726
REMARK 3 2 4.0017 - 3.1765 1.00 3254 150 0.1703 0.2006
REMARK 3 3 3.1765 - 2.7750 1.00 3211 148 0.1902 0.2241
REMARK 3 4 2.7750 - 2.5213 1.00 3202 148 0.1923 0.2274
REMARK 3 5 2.5213 - 2.3406 1.00 3199 147 0.2051 0.2275
REMARK 3 6 2.3406 - 2.2026 1.00 3180 146 0.2080 0.2656
REMARK 3 7 2.2026 - 2.0923 1.00 3166 145 0.2349 0.2800
REMARK 3 8 2.0923 - 2.0012 0.92 2916 135 0.2615 0.3083
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.360
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.91
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.61
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 2732
REMARK 3 ANGLE : 0.906 3713
REMARK 3 CHIRALITY : 0.053 379
REMARK 3 PLANARITY : 0.006 480
REMARK 3 DIHEDRAL : 31.257 1006
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 229 THROUGH 370 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.0363 -13.6950 -32.9433
REMARK 3 T TENSOR
REMARK 3 T11: 0.2152 T22: 0.2407
REMARK 3 T33: 0.2796 T12: -0.0052
REMARK 3 T13: 0.0333 T23: 0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 3.6854 L22: 3.9954
REMARK 3 L33: 2.9972 L12: 1.2261
REMARK 3 L13: -0.4709 L23: 0.0143
REMARK 3 S TENSOR
REMARK 3 S11: -0.0692 S12: -0.0029 S13: -0.1366
REMARK 3 S21: -0.2344 S22: 0.0278 S23: -0.3477
REMARK 3 S31: 0.1627 S32: 0.1668 S33: 0.0311
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 371 THROUGH 424 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.1581 -27.6078 -44.6743
REMARK 3 T TENSOR
REMARK 3 T11: 0.6557 T22: 0.4811
REMARK 3 T33: 0.5217 T12: -0.1157
REMARK 3 T13: -0.0167 T23: -0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 8.9919 L22: 6.8003
REMARK 3 L33: 2.7971 L12: -3.2139
REMARK 3 L13: -3.5953 L23: 3.4155
REMARK 3 S TENSOR
REMARK 3 S11: -0.4856 S12: -0.1378 S13: -1.3713
REMARK 3 S21: -0.0617 S22: 0.1818 S23: 0.5029
REMARK 3 S31: 0.8205 S32: -0.1211 S33: 0.3435
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 425 THROUGH 547 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.0899 -20.6489 -31.7393
REMARK 3 T TENSOR
REMARK 3 T11: 0.2763 T22: 0.2317
REMARK 3 T33: 0.3135 T12: -0.0726
REMARK 3 T13: 0.0326 T23: 0.0258
REMARK 3 L TENSOR
REMARK 3 L11: 3.8793 L22: 4.3081
REMARK 3 L33: 3.5597 L12: -0.7208
REMARK 3 L13: -0.0611 L23: -0.2073
REMARK 3 S TENSOR
REMARK 3 S11: -0.0828 S12: -0.1036 S13: -0.2960
REMARK 3 S21: -0.2320 S22: 0.1256 S23: 0.0799
REMARK 3 S31: 0.3006 S32: -0.1686 S33: -0.0481
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6YL4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-APR-20.
REMARK 100 THE DEPOSITION ID IS D_1292103164.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-SEP-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0-6.55
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.072
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26716
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.001
REMARK 200 RESOLUTION RANGE LOW (A) : 46.119
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.6900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.6
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 : 1.570
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 UL PROTEIN SOLUTION (5-10 MG/ML, 50
REMARK 280 MM NACL, 50 MM SODIUM PHOSPHATE, 10% (V/V) GLYCEROL (98%), 2 MM
REMARK 280 DTT AT PH 7.4) WAS MIXED AT DIFFERNT RATIOS (2/1, 1/1, 1/2) WITH
REMARK 280 PRECIPITANT SOLUTION (23%-28% (W/V) POLYETHENGLYCOL (PEG) 6000,
REMARK 280 70 MM AMMONIUM ACETAT, 200 MM MAGNESIUM ACETAT, 100 MM SODIUM
REMARK 280 CACODYLATE AT PH 6.1-6.5), VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 39.96700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 46.11900
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 53.32300
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 39.96700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 46.11900
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 53.32300
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 39.96700
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 46.11900
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 53.32300
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 39.96700
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 46.11900
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 53.32300
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 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 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 -165.00 -104.44
REMARK 500 GLU A 269 -142.46 -120.88
REMARK 500 ASP A 335 -126.33 62.02
REMARK 500 ASN A 359 -45.05 74.96
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 OWW A 601
DBREF 6YL4 A 222 555 UNP P34913 HYES_HUMAN 222 555
SEQADV 6YL4 MET A 219 UNP P34913 INITIATING METHIONINE
SEQADV 6YL4 ALA A 220 UNP P34913 EXPRESSION TAG
SEQADV 6YL4 SER A 221 UNP P34913 EXPRESSION TAG
SEQADV 6YL4 LEU A 556 UNP P34913 EXPRESSION TAG
SEQADV 6YL4 LEU A 557 UNP P34913 EXPRESSION TAG
SEQADV 6YL4 GLU A 558 UNP P34913 EXPRESSION TAG
SEQADV 6YL4 HIS A 559 UNP P34913 EXPRESSION TAG
SEQADV 6YL4 HIS A 560 UNP P34913 EXPRESSION TAG
SEQADV 6YL4 HIS A 561 UNP P34913 EXPRESSION TAG
SEQADV 6YL4 HIS A 562 UNP P34913 EXPRESSION TAG
SEQADV 6YL4 HIS A 563 UNP P34913 EXPRESSION TAG
SEQADV 6YL4 HIS A 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
HET OWW A 601 38
HETNAM OWW 3-[(3~{R})-3-[AMINOCARBONYL(OXIDANYL)AMINO]BUT-1-YNYL]-
HETNAM 2 OWW ~{N}-[(3~{S})-3-PHENYL-3-[4-(TRIFLUOROMETHYLOXY)
HETNAM 3 OWW PHENYL]PROPYL]BENZAMIDE
FORMUL 2 OWW C28 H26 F3 N3 O4
FORMUL 3 HOH *93(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 THR A 443 GLY A 458 1 16
HELIX 14 AB5 PHE A 459 TRP A 465 1 7
HELIX 15 AB6 ASN A 468 LYS A 478 1 11
HELIX 16 AB7 VAL A 500 GLN A 505 5 6
HELIX 17 AB8 HIS A 506 TRP A 510 5 5
HELIX 18 AB9 TRP A 525 LYS A 530 1 6
HELIX 19 AC1 LYS A 530 ALA A 546 1 17
SHEET 1 AA1 8 SER A 238 LYS A 245 0
SHEET 2 AA1 8 VAL A 248 LEU A 255 -1 O LEU A 250 N VAL A 242
SHEET 3 AA1 8 ARG A 287 MET A 291 -1 O VAL A 288 N LEU A 255
SHEET 4 AA1 8 ALA A 260 CYS A 264 1 N VAL A 261 O LEU A 289
SHEET 5 AA1 8 ALA A 329 HIS A 334 1 O VAL A 330 N CYS A 262
SHEET 6 AA1 8 VAL A 352 LEU A 358 1 O LEU A 358 N GLY A 333
SHEET 7 AA1 8 ALA A 488 ALA A 493 1 O VAL A 491 N SER A 357
SHEET 8 AA1 8 LEU A 514 ILE A 519 1 O LYS A 515 N ALA A 488
CISPEP 1 PHE A 267 PRO A 268 0 -9.88
SITE 1 AC1 17 ASP A 335 TRP A 336 MET A 339 ILE A 375
SITE 2 AC1 17 TYR A 383 GLN A 384 PHE A 387 LEU A 408
SITE 3 AC1 17 MET A 419 LEU A 428 TYR A 466 MET A 469
SITE 4 AC1 17 ASP A 496 PHE A 497 VAL A 498 HIS A 524
SITE 5 AC1 17 TRP A 525
CRYST1 79.934 92.238 106.646 90.00 90.00 90.00 I 2 2 2 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 0.012510 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010842 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009377 0.00000
TER 2611 ARG A 547
MASTER 325 0 1 19 8 0 5 6 2700 1 38 27
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