longtext: 5zhr-pdb

content
HEADER    HYDROLASE                               13-MAR-18   5ZHR
TITLE     CRYSTAL STRUCTURE OF OSD14 IN COMPLEX WITH COVALENTLY BOUND KK094
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: STRIGOLACTONE ESTERASE D14;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: PROTEIN DWARF 14,PROTEIN DWARF 88,PROTEIN HIGH-TILLERING
COMPND   5 DWARF 2;
COMPND   6 EC: 3.1.-.-;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ORYZA SATIVA SUBSP. JAPONICA;
SOURCE   3 ORGANISM_COMMON: RICE;
SOURCE   4 ORGANISM_TAXID: 39947;
SOURCE   5 GENE: D14, D88, HTD2, OS03G0203200, LOC_OS03G10620;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    PLANT HORMONES, PLANT SIGNALLING, STRIGOLACTONES, RECEPTOR, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.HIRABAYASHI,T.MIYAKAWA,M.TANOKURA
REVDAT   1   21-NOV-18 5ZHR    0
JRNL        AUTH   H.NAKAMURA,K.HIRABAYASHI,T.MIYAKAWA,K.KIKUZATO,W.HU,Y.XU,
JRNL        AUTH 2 K.JIANG,I.TAKAHASHI,R.NIIYAMA,N.DOHMAE,M.TANOKURA,T.ASAMI
JRNL        TITL   TRIAZOLE UREAS COVALENTLY BIND TO STRIGOLACTONE RECEPTOR AND
JRNL        TITL 2 ANTAGONIZE STRIGOLACTONE RESPONSES.
JRNL        REF    MOL PLANT                                  2018
JRNL        REFN                   ESSN 1752-9867
JRNL        PMID   30391752
JRNL        DOI    10.1016/J.MOLP.2018.10.006
REMARK   2
REMARK   2 RESOLUTION.    1.45 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX 1.9_1692
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) : 1.45
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.51
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7
REMARK   3   NUMBER OF REFLECTIONS             : 173170
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.167
REMARK   3   R VALUE            (WORKING SET) : 0.166
REMARK   3   FREE R VALUE                     : 0.199
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.200
REMARK   3   FREE R VALUE TEST SET COUNT      : 3809
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 49.5396 -  4.3490    1.00     6328   141  0.1547 0.1783
REMARK   3     2  4.3490 -  3.4522    1.00     6353   142  0.1492 0.2026
REMARK   3     3  3.4522 -  3.0159    1.00     6354   143  0.1636 0.1873
REMARK   3     4  3.0159 -  2.7402    1.00     6349   143  0.1700 0.1827
REMARK   3     5  2.7402 -  2.5438    1.00     6367   145  0.1669 0.1896
REMARK   3     6  2.5438 -  2.3938    1.00     6335   136  0.1673 0.2006
REMARK   3     7  2.3938 -  2.2739    1.00     6370   149  0.1636 0.1966
REMARK   3     8  2.2739 -  2.1749    1.00     6372   139  0.1668 0.2230
REMARK   3     9  2.1749 -  2.0912    1.00     6347   147  0.1636 0.1870
REMARK   3    10  2.0912 -  2.0190    1.00     6319   137  0.1659 0.2062
REMARK   3    11  2.0190 -  1.9559    1.00     6370   140  0.1654 0.2085
REMARK   3    12  1.9559 -  1.9000    1.00     6386   147  0.1666 0.1937
REMARK   3    13  1.9000 -  1.8500    1.00     6317   144  0.1687 0.2187
REMARK   3    14  1.8500 -  1.8048    1.00     6336   142  0.1713 0.1950
REMARK   3    15  1.8048 -  1.7638    1.00     6414   149  0.1754 0.2067
REMARK   3    16  1.7638 -  1.7263    1.00     6305   144  0.1734 0.2213
REMARK   3    17  1.7263 -  1.6917    1.00     6387   143  0.1684 0.2106
REMARK   3    18  1.6917 -  1.6598    1.00     6304   143  0.1689 0.2138
REMARK   3    19  1.6598 -  1.6302    1.00     6385   141  0.1731 0.2180
REMARK   3    20  1.6302 -  1.6025    1.00     6314   146  0.1675 0.1682
REMARK   3    21  1.6025 -  1.5767    1.00     6414   146  0.1697 0.2145
REMARK   3    22  1.5767 -  1.5524    1.00     6250   143  0.1755 0.2309
REMARK   3    23  1.5524 -  1.5296    1.00     6402   142  0.1825 0.1897
REMARK   3    24  1.5296 -  1.5080    1.00     6324   139  0.1905 0.2160
REMARK   3    25  1.5080 -  1.4877    0.98     6267   142  0.1965 0.2287
REMARK   3    26  1.4877 -  1.4683    0.88     5609   127  0.2157 0.2221
REMARK   3    27  1.4683 -  1.4500    0.80     5083   109  0.2280 0.2750
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)     : 0.130
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.220
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
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      :  0.009           4218
REMARK   3   ANGLE     :  1.215           5748
REMARK   3   CHIRALITY :  0.051            662
REMARK   3   PLANARITY :  0.007            744
REMARK   3   DIHEDRAL  : 11.996           1508
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
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 5ZHR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-MAR-18.
REMARK 100 THE DEPOSITION ID IS D_1300007101.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 23-JUN-16
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY
REMARK 200  BEAMLINE                       : BL-1A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1
REMARK 200  MONOCHROMATOR                  : CRYO-COOLED CHANNEL-CUT SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : PIXEL
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 4M
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XDS
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 173170
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.450
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.511
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0
REMARK 200  DATA REDUNDANCY                : 9.300
REMARK 200  R MERGE                    (I) : 0.04700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 26.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.54
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.80
REMARK 200  R MERGE FOR SHELL          (I) : 0.27400
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 5.900
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: 3VXK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 20000, MES, PH 6.5, VAPOR
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
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       24.12500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       59.69000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.32000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       59.69000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.12500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.32000
REMARK 290   SMTRY3   4  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 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 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    45
REMARK 465     PRO A    46
REMARK 465     GLY A    47
REMARK 465     TYR A    48
REMARK 465     GLN A    49
REMARK 465     ASP A    50
REMARK 465     PRO A    51
REMARK 465     ASN A    52
REMARK 465     SER A    53
REMARK 465     GLY B    45
REMARK 465     PRO B    46
REMARK 465     GLY B    47
REMARK 465     TYR B    48
REMARK 465     GLN B    49
REMARK 465     ASP B    50
REMARK 465     PRO B    51
REMARK 465     ASN B    52
REMARK 465     SER B    53
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 147     -119.63     58.33
REMARK 500    ARG A 175      121.40   -170.86
REMARK 500    ASN A 201       78.97   -162.73
REMARK 500    GLN A 293       31.82    -88.02
REMARK 500    ALA A 303       55.79   -145.72
REMARK 500    ASP B  81     -167.83   -126.77
REMARK 500    SER B 147     -118.92     57.56
REMARK 500    ARG B 175      120.98   -171.57
REMARK 500    ASP B 181       -8.01     61.50
REMARK 500    ASN B 201       85.26   -154.24
REMARK 500    ALA B 303       57.21   -141.75
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 883        DISTANCE =  6.11 ANGSTROMS
REMARK 525    HOH B 843        DISTANCE =  6.63 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KOK A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide KOK B 500 and SER B
REMARK 800  147
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5YZ7   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH DIFFERENT LIGAND
REMARK 900 RELATED ID: 3VXK   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN (LIGAND-FREE STRUCTURE)
REMARK 900 RELATED ID: 3WIO   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH DIFFERENT LIGAND
DBREF  5ZHR A   54   318  UNP    Q10QA5   D14_ORYSJ       54    318
DBREF  5ZHR B   54   318  UNP    Q10QA5   D14_ORYSJ       54    318
SEQADV 5ZHR GLY A   45  UNP  Q10QA5              EXPRESSION TAG
SEQADV 5ZHR PRO A   46  UNP  Q10QA5              EXPRESSION TAG
SEQADV 5ZHR GLY A   47  UNP  Q10QA5              EXPRESSION TAG
SEQADV 5ZHR TYR A   48  UNP  Q10QA5              EXPRESSION TAG
SEQADV 5ZHR GLN A   49  UNP  Q10QA5              EXPRESSION TAG
SEQADV 5ZHR ASP A   50  UNP  Q10QA5              EXPRESSION TAG
SEQADV 5ZHR PRO A   51  UNP  Q10QA5              EXPRESSION TAG
SEQADV 5ZHR ASN A   52  UNP  Q10QA5              EXPRESSION TAG
SEQADV 5ZHR SER A   53  UNP  Q10QA5              EXPRESSION TAG
SEQADV 5ZHR GLY B   45  UNP  Q10QA5              EXPRESSION TAG
SEQADV 5ZHR PRO B   46  UNP  Q10QA5              EXPRESSION TAG
SEQADV 5ZHR GLY B   47  UNP  Q10QA5              EXPRESSION TAG
SEQADV 5ZHR TYR B   48  UNP  Q10QA5              EXPRESSION TAG
SEQADV 5ZHR GLN B   49  UNP  Q10QA5              EXPRESSION TAG
SEQADV 5ZHR ASP B   50  UNP  Q10QA5              EXPRESSION TAG
SEQADV 5ZHR PRO B   51  UNP  Q10QA5              EXPRESSION TAG
SEQADV 5ZHR ASN B   52  UNP  Q10QA5              EXPRESSION TAG
SEQADV 5ZHR SER B   53  UNP  Q10QA5              EXPRESSION TAG
SEQRES   1 A  274  GLY PRO GLY TYR GLN ASP PRO ASN SER ALA LYS LEU LEU
SEQRES   2 A  274  GLN ILE LEU ASN VAL ARG VAL VAL GLY SER GLY GLU ARG
SEQRES   3 A  274  VAL VAL VAL LEU SER HIS GLY PHE GLY THR ASP GLN SER
SEQRES   4 A  274  ALA TRP SER ARG VAL LEU PRO TYR LEU THR ARG ASP HIS
SEQRES   5 A  274  ARG VAL VAL LEU TYR ASP LEU VAL CYS ALA GLY SER VAL
SEQRES   6 A  274  ASN PRO ASP HIS PHE ASP PHE ARG ARG TYR ASP ASN LEU
SEQRES   7 A  274  ASP ALA TYR VAL ASP ASP LEU LEU ALA ILE LEU ASP ALA
SEQRES   8 A  274  LEU ARG ILE PRO ARG CYS ALA PHE VAL GLY HIS SER VAL
SEQRES   9 A  274  SER ALA MET ILE GLY ILE LEU ALA SER ILE ARG ARG PRO
SEQRES  10 A  274  ASP LEU PHE ALA LYS LEU VAL LEU ILE GLY ALA SER PRO
SEQRES  11 A  274  ARG PHE LEU ASN ASP SER ASP TYR HIS GLY GLY PHE GLU
SEQRES  12 A  274  LEU GLU GLU ILE GLN GLN VAL PHE ASP ALA MET GLY ALA
SEQRES  13 A  274  ASN TYR SER ALA TRP ALA THR GLY TYR ALA PRO LEU ALA
SEQRES  14 A  274  VAL GLY ALA ASP VAL PRO ALA ALA VAL GLN GLU PHE SER
SEQRES  15 A  274  ARG THR LEU PHE ASN MET ARG PRO ASP ILE SER LEU HIS
SEQRES  16 A  274  VAL CYS GLN THR VAL PHE LYS THR ASP LEU ARG GLY VAL
SEQRES  17 A  274  LEU GLY MET VAL ARG ALA PRO CYS VAL VAL VAL GLN THR
SEQRES  18 A  274  THR ARG ASP VAL SER VAL PRO ALA SER VAL ALA ALA TYR
SEQRES  19 A  274  LEU LYS ALA HIS LEU GLY GLY ARG THR THR VAL GLU PHE
SEQRES  20 A  274  LEU GLN THR GLU GLY HIS LEU PRO HIS LEU SER ALA PRO
SEQRES  21 A  274  SER LEU LEU ALA GLN VAL LEU ARG ARG ALA LEU ALA ARG
SEQRES  22 A  274  TYR
SEQRES   1 B  274  GLY PRO GLY TYR GLN ASP PRO ASN SER ALA LYS LEU LEU
SEQRES   2 B  274  GLN ILE LEU ASN VAL ARG VAL VAL GLY SER GLY GLU ARG
SEQRES   3 B  274  VAL VAL VAL LEU SER HIS GLY PHE GLY THR ASP GLN SER
SEQRES   4 B  274  ALA TRP SER ARG VAL LEU PRO TYR LEU THR ARG ASP HIS
SEQRES   5 B  274  ARG VAL VAL LEU TYR ASP LEU VAL CYS ALA GLY SER VAL
SEQRES   6 B  274  ASN PRO ASP HIS PHE ASP PHE ARG ARG TYR ASP ASN LEU
SEQRES   7 B  274  ASP ALA TYR VAL ASP ASP LEU LEU ALA ILE LEU ASP ALA
SEQRES   8 B  274  LEU ARG ILE PRO ARG CYS ALA PHE VAL GLY HIS SER VAL
SEQRES   9 B  274  SER ALA MET ILE GLY ILE LEU ALA SER ILE ARG ARG PRO
SEQRES  10 B  274  ASP LEU PHE ALA LYS LEU VAL LEU ILE GLY ALA SER PRO
SEQRES  11 B  274  ARG PHE LEU ASN ASP SER ASP TYR HIS GLY GLY PHE GLU
SEQRES  12 B  274  LEU GLU GLU ILE GLN GLN VAL PHE ASP ALA MET GLY ALA
SEQRES  13 B  274  ASN TYR SER ALA TRP ALA THR GLY TYR ALA PRO LEU ALA
SEQRES  14 B  274  VAL GLY ALA ASP VAL PRO ALA ALA VAL GLN GLU PHE SER
SEQRES  15 B  274  ARG THR LEU PHE ASN MET ARG PRO ASP ILE SER LEU HIS
SEQRES  16 B  274  VAL CYS GLN THR VAL PHE LYS THR ASP LEU ARG GLY VAL
SEQRES  17 B  274  LEU GLY MET VAL ARG ALA PRO CYS VAL VAL VAL GLN THR
SEQRES  18 B  274  THR ARG ASP VAL SER VAL PRO ALA SER VAL ALA ALA TYR
SEQRES  19 B  274  LEU LYS ALA HIS LEU GLY GLY ARG THR THR VAL GLU PHE
SEQRES  20 B  274  LEU GLN THR GLU GLY HIS LEU PRO HIS LEU SER ALA PRO
SEQRES  21 B  274  SER LEU LEU ALA GLN VAL LEU ARG ARG ALA LEU ALA ARG
SEQRES  22 B  274  TYR
HET    KOK  A 500      11
HET    KOK  B 500      11
HETNAM     KOK (2,3-DIHYDRO-1H-INDOL-1-YL)(1H-1,2,3-TRIAZOL-1-YL)
HETNAM   2 KOK  METHANONE
FORMUL   3  KOK    2(C11 H10 N4 O)
FORMUL   5  HOH   *526(H2 O)
HELIX    1 AA1 ALA A   54  LEU A   60  1                                   7
HELIX    2 AA2 ASP A   81  SER A   86  5                                   6
HELIX    3 AA3 VAL A   88  LEU A   92  5                                   5
HELIX    4 AA4 ASN A  110  PHE A  114  5                                   5
HELIX    5 AA5 ARG A  117  ASP A  120  5                                   4
HELIX    6 AA6 ASN A  121  LEU A  136  1                                  16
HELIX    7 AA7 SER A  147  ARG A  160  1                                  14
HELIX    8 AA8 GLU A  187  ASN A  201  1                                  15
HELIX    9 AA9 ASN A  201  GLY A  215  1                                  15
HELIX   10 AB1 VAL A  218  MET A  232  1                                  15
HELIX   11 AB2 ARG A  233  THR A  247  1                                  15
HELIX   12 AB3 LEU A  249  VAL A  256  5                                   8
HELIX   13 AB4 SER A  274  LEU A  283  1                                  10
HELIX   14 AB5 LEU A  298  ALA A  303  1                                   6
HELIX   15 AB6 ALA A  303  LEU A  315  1                                  13
HELIX   16 AB7 LYS B   55  LEU B   60  1                                   6
HELIX   17 AB8 ASP B   81  SER B   86  5                                   6
HELIX   18 AB9 VAL B   88  LEU B   92  5                                   5
HELIX   19 AC1 ASN B  110  PHE B  114  5                                   5
HELIX   20 AC2 ARG B  117  ASP B  120  5                                   4
HELIX   21 AC3 ASN B  121  LEU B  136  1                                  16
HELIX   22 AC4 SER B  147  ARG B  160  1                                  14
HELIX   23 AC5 GLU B  187  ASN B  201  1                                  15
HELIX   24 AC6 ASN B  201  GLY B  215  1                                  15
HELIX   25 AC7 VAL B  218  MET B  232  1                                  15
HELIX   26 AC8 ARG B  233  LYS B  246  1                                  14
HELIX   27 AC9 LEU B  249  VAL B  256  5                                   8
HELIX   28 AD1 ALA B  273  LEU B  283  1                                  11
HELIX   29 AD2 LEU B  298  ALA B  303  1                                   6
HELIX   30 AD3 ALA B  303  LEU B  315  1                                  13
SHEET    1 AA1 7 ARG A  63  GLY A  66  0
SHEET    2 AA1 7 ARG A  97  LEU A 100 -1  O  VAL A  98   N  VAL A  65
SHEET    3 AA1 7 VAL A  71  SER A  75  1  N  VAL A  72   O  ARG A  97
SHEET    4 AA1 7 CYS A 141  HIS A 146  1  O  VAL A 144   N  VAL A  73
SHEET    5 AA1 7 PHE A 164  ILE A 170  1  O  ALA A 165   N  CYS A 141
SHEET    6 AA1 7 CYS A 260  GLN A 264  1  O  VAL A 261   N  LEU A 169
SHEET    7 AA1 7 THR A 287  PHE A 291  1  O  THR A 288   N  VAL A 262
SHEET    1 AA2 7 ARG B  63  GLY B  66  0
SHEET    2 AA2 7 ARG B  97  LEU B 100 -1  O  VAL B  98   N  VAL B  65
SHEET    3 AA2 7 VAL B  71  SER B  75  1  N  VAL B  72   O  VAL B  99
SHEET    4 AA2 7 CYS B 141  HIS B 146  1  O  VAL B 144   N  VAL B  73
SHEET    5 AA2 7 PHE B 164  ILE B 170  1  O  ALA B 165   N  CYS B 141
SHEET    6 AA2 7 CYS B 260  GLN B 264  1  O  VAL B 263   N  LEU B 169
SHEET    7 AA2 7 THR B 287  PHE B 291  1  O  GLU B 290   N  GLN B 264
LINK         OG  SER A 147                 CAA KOK A 500     1555   1555  1.40
LINK         OG  SER B 147                 CAA KOK B 500     1555   1555  1.37
SITE     1 AC1  8 PHE A  78  SER A 147  VAL A 148  PHE A 176
SITE     2 AC1  8 VAL A 244  PHE A 245  SER A 270  HOH A 723
SITE     1 AC2 15 PHE B  78  HIS B 146  VAL B 148  SER B 149
SITE     2 AC2 15 ALA B 150  MET B 151  ILE B 170  GLY B 171
SITE     3 AC2 15 PHE B 176  VAL B 244  PHE B 245  SER B 270
SITE     4 AC2 15 HIS B 297  HOH B 689  HOH B 738
CRYST1   48.250   88.640  119.380  90.00  90.00  90.00 P 21 21 21    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      0.020725  0.000000  0.000000        0.00000
SCALE2      0.000000  0.011282  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008377        0.00000
TER    2052      TYR A 318
TER    4104      TYR B 318
MASTER      305    0    2   30   14    0    6    6 4650    2   24   44
END