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HEADER HYDROLASE 09-SEP-13 4C4X
TITLE CRYSTAL STRUCTURE OF HUMAN BIFUNCTIONAL EPOXIDE HYDROXYLASE 2
TITLE 2 COMPLEXED WITH C9
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIFUNCTIONAL EPOXIDE HYDROLASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: EPOXIDE HYDROXYLASE DOMAIN RESIDUES 230-555;
COMPND 5 SYNONYM: BIFUNCTIONAL EPOXIDE HYDROXYLASE 2, CYTOSOLIC EPOXIDE
COMPND 6 HYDROLASE 2, CEH, EPOXIDE HYDRATASE, SOLUBLE EPOXIDE HYDROLASE,
COMPND 7 SEH, LIPID-PHOSPHATE PHOSPHATASE;
COMPND 8 EC: 3.3.2.10, 3.1.3.76;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET16B
KEYWDS HYDROLASE, DRUG DESIGN, MULTIPLE BINDING MODES
EXPDTA X-RAY DIFFRACTION
AUTHOR J.PILGER,A.MAZUR,P.MONECKE,H.SCHREUDER,B.ELSHORST,T.LANGER,
AUTHOR 2 A.SCHIFFER,I.KRIMM,M.WEGSTROTH,D.LEE,G.HESSLER,K.-U.WENDT,S.BECKER,
AUTHOR 3 C.GRIESINGER
REVDAT 1 01-OCT-14 4C4X 0
JRNL AUTH J.PILGER,A.MAZUR,P.MONECKE,H.SCHREUDER,B.ELSHORST,T.LANGER,
JRNL AUTH 2 A.SCHIFFER,I.KRIMM,M.WEGSTROTH,D.LEE,G.HESSLER,K.-U.WENDT,
JRNL AUTH 3 S.BECKER,C.GRIESINGER
JRNL TITL A COMBINATION OF SPIN DIFFUSION METHODS FOR THE
JRNL TITL 2 DETERMINATION OF PROTEIN-LIGAND COMPLEX STRUCTURAL
JRNL TITL 3 ENSEMBLES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.17 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,WOMACK;
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.17
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.63
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.80
REMARK 3 NUMBER OF REFLECTIONS : 34823
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) : 0.2133
REMARK 3 R VALUE (WORKING SET) : 0.2111
REMARK 3 FREE R VALUE : 0.2418
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.21
REMARK 3 FREE R VALUE TEST SET COUNT : 2512
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 17
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.17
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.24
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.80
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2990
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2383
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2774
REMARK 3 BIN R VALUE (WORKING SET) : 0.2364
REMARK 3 BIN FREE R VALUE : 0.2635
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.22
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 216
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5061
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 445
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.12
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.9696
REMARK 3 B22 (A**2) : 11.5946
REMARK 3 B33 (A**2) : -8.6250
REMARK 3 B12 (A**2) : 0.0000
REMARK 3 B13 (A**2) : 1.4659
REMARK 3 B23 (A**2) : 0.0000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.287
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.319
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.211
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.304
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.210
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.9089
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.8790
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 5267 ; 2.00 ; HARMONIC
REMARK 3 BOND ANGLES : 7141 ; 2.00 ; HARMONIC
REMARK 3 TORSION ANGLES : 1797 ; 2.00 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 122 ; 2.00 ; HARMONIC
REMARK 3 GENERAL PLANES : 755 ; 5.00 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 5267 ; 20.00 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 629 ; 5.00 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : 2 ; 1.00 ; HARMONIC
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 6357 ; 4.00 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 0.94
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.13
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.31
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP.
REMARK 3 ALL ATOMS HAVE CCP4 ATOM TYPE FROM LIBRARY.
REMARK 3 THE INHIBITOR HAS BEEN MODELED IN TWO ORIENTATIONS
REMARK 4
REMARK 4 4C4X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-SEP-13.
REMARK 100 THE PDBE ID CODE IS EBI-58281.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-NOV-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL (PILATUS)
REMARK 200 DETECTOR MANUFACTURER : DECTRIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35085
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.17
REMARK 200 RESOLUTION RANGE LOW (A) : 44.31
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 3.3
REMARK 200 R MERGE (I) : 0.09
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.90
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.17
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.3
REMARK 200 R MERGE FOR SHELL (I) : 0.41
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.40
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: PDB ENTRY 3OTQ
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.6
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROP. 1 UL PROTEIN
REMARK 280 SOLUTION (8 MG/ML SEH IN 100 MM NAPO2, PH 7.4, 5 MM DTT
REMARK 280 AND 15% GLYCEROL) WAS MIXED WITH 1 UL RESERVOIR SOLUTION
REMARK 280 (100 MM TRIS-HCL, PH 8.3, 26% PEG4000 AND 200 MM LI2SO4
REMARK 280 AND EQUILIBRATED AT 20C. CRYSTALS APPEARED IN ABOUT 2 WEEKS
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 39.93500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 THR A 230
REMARK 465 SER A 231
REMARK 465 CYS A 232
REMARK 465 ASN A 233
REMARK 465 PRO A 234
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 THR B 230
REMARK 465 SER B 231
REMARK 465 CYS B 232
REMARK 465 ASN B 233
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 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 PRO B 234 CG CD
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 -155.87 -105.31
REMARK 500 ASP A 335 -118.00 59.52
REMARK 500 ASN A 359 -40.95 72.89
REMARK 500 SER A 418 61.98 -112.37
REMARK 500 CYS A 423 132.65 69.42
REMARK 500 GLU A 424 124.51 -8.05
REMARK 500 ALA A 425 -47.61 4.68
REMARK 500 LEU A 480 106.89 38.59
REMARK 500 LEU A 499 67.87 -105.24
REMARK 500 HIS A 513 38.40 -99.22
REMARK 500 PRO B 268 75.58 -100.53
REMARK 500 GLU B 269 -156.83 -99.78
REMARK 500 ASP B 335 -118.98 58.44
REMARK 500 ASN B 359 -45.83 69.92
REMARK 500 PHE B 381 31.36 -92.64
REMARK 500 VAL B 422 63.37 -108.88
REMARK 500 CYS B 423 -44.84 -153.32
REMARK 500 PHE B 429 59.91 -104.75
REMARK 500 LEU B 480 117.25 -10.76
REMARK 500 HIS B 513 32.35 -97.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 GLU A 269 24.8 L L OUTSIDE RANGE
REMARK 500 VAL A 341 24.9 L L OUTSIDE RANGE
REMARK 500 GLU A 424 23.0 L L OUTSIDE RANGE
REMARK 500 GLU B 269 24.9 L L OUTSIDE RANGE
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 W9M A1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE W9M B1548
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4C4Y RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN BIFUNCTIONAL EPOXIDE
REMARK 900 HYDROXYLASE 2 COMPLEXED WITH A4
REMARK 900 RELATED ID: 4C4Z RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN BIFUNCTIONAL EPOXIDE
REMARK 900 HYDROXYLASE 2 COMPLEXED WITH A8
DBREF 4C4X A 230 555 UNP P34913 HYES_HUMAN 230 555
DBREF 4C4X B 230 555 UNP P34913 HYES_HUMAN 230 555
SEQRES 1 A 326 THR SER CYS ASN PRO SER ASP MET SER HIS GLY TYR VAL
SEQRES 2 A 326 THR VAL LYS PRO ARG VAL ARG LEU HIS PHE VAL GLU LEU
SEQRES 3 A 326 GLY SER GLY PRO ALA VAL CYS LEU CYS HIS GLY PHE PRO
SEQRES 4 A 326 GLU SER TRP TYR SER TRP ARG TYR GLN ILE PRO ALA LEU
SEQRES 5 A 326 ALA GLN ALA GLY TYR ARG VAL LEU ALA MET ASP MET LYS
SEQRES 6 A 326 GLY TYR GLY GLU SER SER ALA PRO PRO GLU ILE GLU GLU
SEQRES 7 A 326 TYR CYS MET GLU VAL LEU CYS LYS GLU MET VAL THR PHE
SEQRES 8 A 326 LEU ASP LYS LEU GLY LEU SER GLN ALA VAL PHE ILE GLY
SEQRES 9 A 326 HIS ASP TRP GLY GLY MET LEU VAL TRP TYR MET ALA LEU
SEQRES 10 A 326 PHE TYR PRO GLU ARG VAL ARG ALA VAL ALA SER LEU ASN
SEQRES 11 A 326 THR PRO PHE ILE PRO ALA ASN PRO ASN MET SER PRO LEU
SEQRES 12 A 326 GLU SER ILE LYS ALA ASN PRO VAL PHE ASP TYR GLN LEU
SEQRES 13 A 326 TYR PHE GLN GLU PRO GLY VAL ALA GLU ALA GLU LEU GLU
SEQRES 14 A 326 GLN ASN LEU SER ARG THR PHE LYS SER LEU PHE ARG ALA
SEQRES 15 A 326 SER ASP GLU SER VAL LEU SER MET HIS LYS VAL CYS GLU
SEQRES 16 A 326 ALA GLY GLY LEU PHE VAL ASN SER PRO GLU GLU PRO SER
SEQRES 17 A 326 LEU SER ARG MET VAL THR GLU GLU GLU ILE GLN PHE TYR
SEQRES 18 A 326 VAL GLN GLN PHE LYS LYS SER GLY PHE ARG GLY PRO LEU
SEQRES 19 A 326 ASN TRP TYR ARG ASN MET GLU ARG ASN TRP LYS TRP ALA
SEQRES 20 A 326 CYS LYS SER LEU GLY ARG LYS ILE LEU ILE PRO ALA LEU
SEQRES 21 A 326 MET VAL THR ALA GLU LYS ASP PHE VAL LEU VAL PRO GLN
SEQRES 22 A 326 MET SER GLN HIS MET GLU ASP TRP ILE PRO HIS LEU LYS
SEQRES 23 A 326 ARG GLY HIS ILE GLU ASP CYS GLY HIS TRP THR GLN MET
SEQRES 24 A 326 ASP LYS PRO THR GLU VAL ASN GLN ILE LEU ILE LYS TRP
SEQRES 25 A 326 LEU ASP SER ASP ALA ARG ASN PRO PRO VAL VAL SER LYS
SEQRES 26 A 326 MET
SEQRES 1 B 326 THR SER CYS ASN PRO SER ASP MET SER HIS GLY TYR VAL
SEQRES 2 B 326 THR VAL LYS PRO ARG VAL ARG LEU HIS PHE VAL GLU LEU
SEQRES 3 B 326 GLY SER GLY PRO ALA VAL CYS LEU CYS HIS GLY PHE PRO
SEQRES 4 B 326 GLU SER TRP TYR SER TRP ARG TYR GLN ILE PRO ALA LEU
SEQRES 5 B 326 ALA GLN ALA GLY TYR ARG VAL LEU ALA MET ASP MET LYS
SEQRES 6 B 326 GLY TYR GLY GLU SER SER ALA PRO PRO GLU ILE GLU GLU
SEQRES 7 B 326 TYR CYS MET GLU VAL LEU CYS LYS GLU MET VAL THR PHE
SEQRES 8 B 326 LEU ASP LYS LEU GLY LEU SER GLN ALA VAL PHE ILE GLY
SEQRES 9 B 326 HIS ASP TRP GLY GLY MET LEU VAL TRP TYR MET ALA LEU
SEQRES 10 B 326 PHE TYR PRO GLU ARG VAL ARG ALA VAL ALA SER LEU ASN
SEQRES 11 B 326 THR PRO PHE ILE PRO ALA ASN PRO ASN MET SER PRO LEU
SEQRES 12 B 326 GLU SER ILE LYS ALA ASN PRO VAL PHE ASP TYR GLN LEU
SEQRES 13 B 326 TYR PHE GLN GLU PRO GLY VAL ALA GLU ALA GLU LEU GLU
SEQRES 14 B 326 GLN ASN LEU SER ARG THR PHE LYS SER LEU PHE ARG ALA
SEQRES 15 B 326 SER ASP GLU SER VAL LEU SER MET HIS LYS VAL CYS GLU
SEQRES 16 B 326 ALA GLY GLY LEU PHE VAL ASN SER PRO GLU GLU PRO SER
SEQRES 17 B 326 LEU SER ARG MET VAL THR GLU GLU GLU ILE GLN PHE TYR
SEQRES 18 B 326 VAL GLN GLN PHE LYS LYS SER GLY PHE ARG GLY PRO LEU
SEQRES 19 B 326 ASN TRP TYR ARG ASN MET GLU ARG ASN TRP LYS TRP ALA
SEQRES 20 B 326 CYS LYS SER LEU GLY ARG LYS ILE LEU ILE PRO ALA LEU
SEQRES 21 B 326 MET VAL THR ALA GLU LYS ASP PHE VAL LEU VAL PRO GLN
SEQRES 22 B 326 MET SER GLN HIS MET GLU ASP TRP ILE PRO HIS LEU LYS
SEQRES 23 B 326 ARG GLY HIS ILE GLU ASP CYS GLY HIS TRP THR GLN MET
SEQRES 24 B 326 ASP LYS PRO THR GLU VAL ASN GLN ILE LEU ILE LYS TRP
SEQRES 25 B 326 LEU ASP SER ASP ALA ARG ASN PRO PRO VAL VAL SER LYS
SEQRES 26 B 326 MET
HET W9M A1548 28
HET W9M B1548 28
HETNAM W9M 3-(3,4-DICHLOROPHENYL)-1,1-DIMETHYL-UREA
FORMUL 3 W9M 2(C9 H10 CL2 N2 O)
FORMUL 4 HOH *445(H2 O)
HELIX 1 1 SER A 270 ARG A 275 5 6
HELIX 2 2 TYR A 276 ALA A 284 1 9
HELIX 3 3 ILE A 305 TYR A 308 5 4
HELIX 4 4 CYS A 309 LEU A 324 1 16
HELIX 5 5 ASP A 335 TYR A 348 1 14
HELIX 6 6 SER A 370 ASN A 378 1 9
HELIX 7 7 PHE A 381 PHE A 387 1 7
HELIX 8 8 GLY A 391 ASN A 400 1 10
HELIX 9 9 ASN A 400 PHE A 409 1 10
HELIX 10 10 THR A 443 LYS A 455 1 13
HELIX 11 11 PHE A 459 ASN A 464 1 6
HELIX 12 12 ASN A 468 LYS A 478 1 11
HELIX 13 13 VAL A 500 GLN A 505 5 6
HELIX 14 14 HIS A 506 TRP A 510 5 5
HELIX 15 15 TRP A 525 LYS A 530 1 6
HELIX 16 16 LYS A 530 ALA A 546 1 17
HELIX 17 17 SER B 270 ARG B 275 5 6
HELIX 18 18 TYR B 276 ALA B 284 1 9
HELIX 19 19 ILE B 305 TYR B 308 5 4
HELIX 20 20 CYS B 309 LEU B 324 1 16
HELIX 21 21 ASP B 335 TYR B 348 1 14
HELIX 22 22 SER B 370 ASN B 378 1 9
HELIX 23 23 PRO B 379 PHE B 381 5 3
HELIX 24 24 ASP B 382 PHE B 387 1 6
HELIX 25 25 GLY B 391 ASN B 400 1 10
HELIX 26 26 ASN B 400 PHE B 409 1 10
HELIX 27 27 THR B 443 LYS B 455 1 13
HELIX 28 28 PHE B 459 ASN B 464 1 6
HELIX 29 29 ASN B 468 CYS B 477 1 10
HELIX 30 30 VAL B 500 GLN B 505 5 6
HELIX 31 31 HIS B 506 TRP B 510 5 5
HELIX 32 32 TRP B 525 LYS B 530 1 6
HELIX 33 33 LYS B 530 ALA B 546 1 17
SHEET 1 AA16 LEU A 514 ILE A 519 0
SHEET 2 AA16 ALA A 488 ALA A 493 1 O ALA A 488 N LYS A 515
SHEET 3 AA16 VAL A 352 LEU A 358 1 O VAL A 355 N LEU A 489
SHEET 4 AA16 ALA A 329 HIS A 334 1 O ALA A 329 N ARG A 353
SHEET 5 AA16 ALA A 260 CYS A 264 1 O ALA A 260 N VAL A 330
SHEET 6 AA16 ARG A 287 ASP A 292 1 O ARG A 287 N VAL A 261
SHEET 7 AA16 VAL A 248 LEU A 255 -1 O HIS A 251 N ASP A 292
SHEET 8 AA16 SER A 238 LYS A 245 -1 O SER A 238 N GLU A 254
SHEET 9 AA16 SER B 238 THR B 243 -1 O HIS B 239 N TYR A 241
SHEET 10 AA16 ARG B 249 LEU B 255 -1 O LEU B 250 N VAL B 242
SHEET 11 AA16 ARG B 287 ASP B 292 -1 O VAL B 288 N LEU B 255
SHEET 12 AA16 ALA B 260 CYS B 264 1 O VAL B 261 N LEU B 289
SHEET 13 AA16 ALA B 329 HIS B 334 1 O VAL B 330 N CYS B 262
SHEET 14 AA16 VAL B 352 LEU B 358 1 N ARG B 353 O ALA B 329
SHEET 15 AA16 ALA B 488 ALA B 493 1 O LEU B 489 N SER B 357
SHEET 16 AA16 LEU B 514 ILE B 519 1 O LYS B 515 N MET B 490
CISPEP 1 PHE A 267 PRO A 268 0 -7.26
CISPEP 2 CYS A 423 GLU A 424 0 3.58
CISPEP 3 PHE B 267 PRO B 268 0 -6.44
SITE 1 AC1 8 PHE A 267 ASP A 335 TYR A 383 LEU A 408
SITE 2 AC1 8 MET A 419 TYR A 466 VAL A 498 HIS A 524
SITE 1 AC2 8 PHE B 267 ASP B 335 TYR B 383 LEU B 408
SITE 2 AC2 8 MET B 419 TYR B 466 VAL B 498 HIS B 524
CRYST1 47.690 79.870 88.610 90.00 89.95 90.00 P 1 21 1 4
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 0.020969 0.000000 -0.000018 0.00000
SCALE2 0.000000 0.012520 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011285 0.00000
TER 2529 ARG A 547
TER 5063 ARG B 547
MASTER 333 0 2 33 16 0 4 6 5562 2 56 52
END |