longtext: 6ap6-pdb

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HEADER    PLANT PROTEIN                           17-AUG-17   6AP6
TITLE     CRYSTAL STRUCTURE OF DAD2 IN COMPLEX WITH TOLFENAMIC ACID
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROBABLE STRIGOLACTONE ESTERASE DAD2;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: PROTEIN DECREASED APICAL DOMINANCE 2;
COMPND   5 ENGINEERED: YES;
COMPND   6 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: PETUNIA HYBRIDA;
SOURCE   3 ORGANISM_COMMON: PETUNIA;
SOURCE   4 ORGANISM_TAXID: 4102;
SOURCE   5 GENE: DAD2;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA GAMI 2;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PDEST566
KEYWDS    ALPHA/BETA HYDROLASE, PLANT PROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    C.HAMIAUX
REVDAT   1   21-MAR-18 6AP6    0
JRNL        AUTH   C.HAMIAUX,R.S.M.DRUMMOND,Z.LUO,H.W.LEE,P.SHARMA,B.J.JANSSEN,
JRNL        AUTH 2 N.B.PERRY,W.A.DENNY,K.C.SNOWDEN
JRNL        TITL   INHIBITION OF STRIGOLACTONE RECEPTORS BY N-PHENYLANTHRANILIC
JRNL        TITL 2 ACID DERIVATIVES: STRUCTURAL AND FUNCTIONAL INSIGHTS
JRNL        REF    J.BIOL.CHEM.                               2018
JRNL        REFN                   ESSN 1083-351X
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   C.HAMIAUX,R.S.DRUMMOND,B.J.JANSSEN,S.E.LEDGER,J.M.COONEY,
REMARK   1  AUTH 2 R.D.NEWCOMB,K.C.SNOWDEN
REMARK   1  TITL   DAD2 IS AN ALPHA/BETA HYDROLASE LIKELY TO BE INVOLVED IN THE
REMARK   1  TITL 2 PERCEPTION OF THE PLANT BRANCHING HORMONE, STRIGOLACTONE.
REMARK   1  REF    CURR. BIOL.                   V.  22  2032 2012
REMARK   1  REFN                   ISSN 1879-0445
REMARK   1  PMID   22959345
REMARK   1  DOI    10.1016/J.CUB.2012.08.007
REMARK   2
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.42
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.2
REMARK   3   NUMBER OF REFLECTIONS             : 53834
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) : 0.170
REMARK   3   R VALUE            (WORKING SET) : 0.168
REMARK   3   FREE R VALUE                     : 0.200
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 2868
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4154
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 36
REMARK   3   SOLVENT ATOMS            : 485
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 16.30
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.89
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.45000
REMARK   3    B22 (A**2) : -0.97000
REMARK   3    B33 (A**2) : 0.92000
REMARK   3    B12 (A**2) : -0.33000
REMARK   3    B13 (A**2) : 0.15000
REMARK   3    B23 (A**2) : -0.18000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.107
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.080
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.764
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL
REMARK   3
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
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 6AP6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1000229524.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 24-FEB-15
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON
REMARK 200  BEAMLINE                       : MX1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210R
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.4
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56704
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.670
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.2
REMARK 200  DATA REDUNDANCY                : 3.900
REMARK 200  R MERGE                    (I) : 0.08600
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.68
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80
REMARK 200  R MERGE FOR SHELL          (I) : 0.86800
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 2.5.7
REMARK 200 STARTING MODEL: 4DNP
REMARK 200
REMARK 200 REMARK: ROD
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 45.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS/ACETATE 0.1M, MGCL2 0.2M, PEG
REMARK 280  8000 24%, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,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
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     GLY A    -1
REMARK 465     GLY A     0
REMARK 465     MET A     1
REMARK 465     GLY A     2
REMARK 465     ARG A   267
REMARK 465     GLY B    -1
REMARK 465     GLY B     0
REMARK 465     MET B     1
REMARK 465     GLY B     2
REMARK 465     ARG B   267
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (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,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ARG A  66   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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    ASP A  30     -166.59   -126.44
REMARK 500    SER A  96     -123.23     58.74
REMARK 500    ARG A 124      115.22   -167.32
REMARK 500    ALA A 252       58.37   -142.21
REMARK 500    SER B  96     -124.36     56.69
REMARK 500    ARG B 124      114.89   -167.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 649        DISTANCE =  5.83 ANGSTROMS
REMARK 525    HOH B 636        DISTANCE =  5.86 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TLF A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TLF B 300
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4DNP   RELATED DB: PDB
REMARK 900 4DNP IS THE APO PROTEIN
DBREF  6AP6 A    1   267  UNP    J9U5U9   DAD2_PETHY       1    267
DBREF  6AP6 B    1   267  UNP    J9U5U9   DAD2_PETHY       1    267
SEQADV 6AP6 GLY A   -1  UNP  J9U5U9              EXPRESSION TAG
SEQADV 6AP6 GLY A    0  UNP  J9U5U9              EXPRESSION TAG
SEQADV 6AP6 GLN A   89  UNP  J9U5U9    CYS    89 ENGINEERED MUTATION
SEQADV 6AP6 GLY B   -1  UNP  J9U5U9              EXPRESSION TAG
SEQADV 6AP6 GLY B    0  UNP  J9U5U9              EXPRESSION TAG
SEQADV 6AP6 GLN B   89  UNP  J9U5U9    CYS    89 ENGINEERED MUTATION
SEQRES   1 A  269  GLY GLY MET GLY GLN THR LEU LEU ASP ALA LEU ASN VAL
SEQRES   2 A  269  ARG VAL VAL GLY SER GLY GLU ARG VAL LEU VAL LEU ALA
SEQRES   3 A  269  HIS GLY PHE GLY THR ASP GLN SER ALA TRP ASN ARG ILE
SEQRES   4 A  269  LEU PRO PHE PHE LEU ARG ASP TYR ARG VAL VAL LEU TYR
SEQRES   5 A  269  ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP PHE PHE
SEQRES   6 A  269  ASP PHE ARG ARG TYR THR THR LEU ASP PRO TYR VAL ASP
SEQRES   7 A  269  ASP LEU LEU HIS ILE LEU ASP ALA LEU GLY ILE ASP GLN
SEQRES   8 A  269  CYS ALA TYR VAL GLY HIS SER VAL SER ALA MET ILE GLY
SEQRES   9 A  269  ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS
SEQRES  10 A  269  LEU ILE LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP
SEQRES  11 A  269  GLU ASP TYR HIS GLY GLY PHE GLU GLN GLY GLU ILE GLU
SEQRES  12 A  269  LYS VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP
SEQRES  13 A  269  VAL ASN GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL
SEQRES  14 A  269  PRO ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN
SEQRES  15 A  269  MET ARG PRO ASP ILE THR LEU PHE VAL SER ARG THR VAL
SEQRES  16 A  269  PHE ASN SER ASP MET ARG GLY VAL LEU GLY LEU VAL LYS
SEQRES  17 A  269  VAL PRO CYS HIS ILE PHE GLN THR ALA ARG ASP HIS SER
SEQRES  18 A  269  VAL PRO ALA SER VAL ALA THR TYR LEU LYS ASN HIS LEU
SEQRES  19 A  269  GLY GLY LYS ASN THR VAL HIS TRP LEU ASN ILE GLU GLY
SEQRES  20 A  269  HIS LEU PRO HIS LEU SER ALA PRO THR LEU LEU ALA GLN
SEQRES  21 A  269  GLU LEU ARG ARG ALA LEU SER HIS ARG
SEQRES   1 B  269  GLY GLY MET GLY GLN THR LEU LEU ASP ALA LEU ASN VAL
SEQRES   2 B  269  ARG VAL VAL GLY SER GLY GLU ARG VAL LEU VAL LEU ALA
SEQRES   3 B  269  HIS GLY PHE GLY THR ASP GLN SER ALA TRP ASN ARG ILE
SEQRES   4 B  269  LEU PRO PHE PHE LEU ARG ASP TYR ARG VAL VAL LEU TYR
SEQRES   5 B  269  ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP PHE PHE
SEQRES   6 B  269  ASP PHE ARG ARG TYR THR THR LEU ASP PRO TYR VAL ASP
SEQRES   7 B  269  ASP LEU LEU HIS ILE LEU ASP ALA LEU GLY ILE ASP GLN
SEQRES   8 B  269  CYS ALA TYR VAL GLY HIS SER VAL SER ALA MET ILE GLY
SEQRES   9 B  269  ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS
SEQRES  10 B  269  LEU ILE LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP
SEQRES  11 B  269  GLU ASP TYR HIS GLY GLY PHE GLU GLN GLY GLU ILE GLU
SEQRES  12 B  269  LYS VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP
SEQRES  13 B  269  VAL ASN GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL
SEQRES  14 B  269  PRO ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN
SEQRES  15 B  269  MET ARG PRO ASP ILE THR LEU PHE VAL SER ARG THR VAL
SEQRES  16 B  269  PHE ASN SER ASP MET ARG GLY VAL LEU GLY LEU VAL LYS
SEQRES  17 B  269  VAL PRO CYS HIS ILE PHE GLN THR ALA ARG ASP HIS SER
SEQRES  18 B  269  VAL PRO ALA SER VAL ALA THR TYR LEU LYS ASN HIS LEU
SEQRES  19 B  269  GLY GLY LYS ASN THR VAL HIS TRP LEU ASN ILE GLU GLY
SEQRES  20 B  269  HIS LEU PRO HIS LEU SER ALA PRO THR LEU LEU ALA GLN
SEQRES  21 B  269  GLU LEU ARG ARG ALA LEU SER HIS ARG
HET    TLF  A 300      18
HET    TLF  B 300      18
HETNAM     TLF 2-[(3-CHLORO-2-METHYLPHENYL)AMINO]BENZOIC ACID
HETSYN     TLF TOLFENAMIC ACID
FORMUL   3  TLF    2(C14 H12 CL N O2)
FORMUL   5  HOH   *485(H2 O)
HELIX    1 AA1 GLN A    3  LEU A    9  1                                   7
HELIX    2 AA2 ASP A   30  ASN A   35  5                                   6
HELIX    3 AA3 ILE A   37  PHE A   41  5                                   5
HELIX    4 AA4 ASN A   59  PHE A   63  5                                   5
HELIX    5 AA5 LEU A   71  LEU A   85  1                                  15
HELIX    6 AA6 SER A   96  ARG A  109  1                                  14
HELIX    7 AA7 GLU A  136  ASN A  150  1                                  15
HELIX    8 AA8 ASN A  150  GLY A  164  1                                  15
HELIX    9 AA9 VAL A  167  MET A  181  1                                  15
HELIX   10 AB1 ARG A  182  SER A  196  1                                  15
HELIX   11 AB2 MET A  198  VAL A  205  5                                   8
HELIX   12 AB3 PRO A  221  LEU A  232  1                                  12
HELIX   13 AB4 LEU A  247  ALA A  252  1                                   6
HELIX   14 AB5 ALA A  252  HIS A  266  1                                  15
HELIX   15 AB6 THR B    4  LEU B    9  1                                   6
HELIX   16 AB7 ASP B   30  ASN B   35  5                                   6
HELIX   17 AB8 ILE B   37  PHE B   41  5                                   5
HELIX   18 AB9 ASN B   59  PHE B   63  5                                   5
HELIX   19 AC1 LEU B   71  LEU B   85  1                                  15
HELIX   20 AC2 SER B   96  ARG B  109  1                                  14
HELIX   21 AC3 GLU B  136  ASN B  150  1                                  15
HELIX   22 AC4 ASN B  150  GLY B  164  1                                  15
HELIX   23 AC5 VAL B  167  MET B  181  1                                  15
HELIX   24 AC6 ARG B  182  SER B  196  1                                  15
HELIX   25 AC7 MET B  198  VAL B  205  5                                   8
HELIX   26 AC8 PRO B  221  LEU B  232  1                                  12
HELIX   27 AC9 LEU B  247  ALA B  252  1                                   6
HELIX   28 AD1 ALA B  252  HIS B  266  1                                  15
SHEET    1 AA1 7 ARG A  12  VAL A  14  0
SHEET    2 AA1 7 TYR A  45  TYR A  50 -1  O  VAL A  47   N  VAL A  14
SHEET    3 AA1 7 ARG A  19  ALA A  24  1  N  LEU A  21   O  VAL A  48
SHEET    4 AA1 7 CYS A  90  HIS A  95  1  O  VAL A  93   N  VAL A  22
SHEET    5 AA1 7 PHE A 113  ILE A 119  1  O  ILE A 117   N  TYR A  92
SHEET    6 AA1 7 CYS A 209  ALA A 215  1  O  PHE A 212   N  LEU A 118
SHEET    7 AA1 7 ASN A 236  GLU A 244  1  O  THR A 237   N  ILE A 211
SHEET    1 AA2 7 ARG B  12  VAL B  14  0
SHEET    2 AA2 7 ARG B  46  TYR B  50 -1  O  VAL B  47   N  VAL B  14
SHEET    3 AA2 7 VAL B  20  ALA B  24  1  N  LEU B  21   O  VAL B  48
SHEET    4 AA2 7 CYS B  90  HIS B  95  1  O  VAL B  93   N  ALA B  24
SHEET    5 AA2 7 PHE B 113  ILE B 119  1  O  ILE B 117   N  TYR B  92
SHEET    6 AA2 7 CYS B 209  ALA B 215  1  O  PHE B 212   N  LEU B 118
SHEET    7 AA2 7 ASN B 236  GLU B 244  1  O  THR B 237   N  ILE B 211
SITE     1 AC1 12 PHE A  27  SER A  96  PHE A 125  ILE A 140
SITE     2 AC1 12 PHE A 158  SER A 190  VAL A 193  PHE A 194
SITE     3 AC1 12 SER A 219  HIS A 246  HOH A 545  HOH A 572
SITE     1 AC2 11 PHE B  27  SER B  96  PHE B 125  PHE B 135
SITE     2 AC2 11 PHE B 158  SER B 190  VAL B 193  SER B 219
SITE     3 AC2 11 HIS B 246  HOH B 536  HOH B 537
CRYST1   36.860   55.830   69.230  95.76  95.13 108.46 P 1           2
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      0.027130  0.009056  0.003704        0.00000
SCALE2      0.000000  0.018883  0.002596        0.00000
SCALE3      0.000000  0.000000  0.014639        0.00000
TER    2098      HIS A 266
TER    4218      HIS B 266
MASTER      284    0    2   28   14    0    6    6 4675    2   36   42
END