longtext: 5DJ5-pdb

content
HEADER    HYDROLASE                               01-SEP-15   5DJ5
TITLE     CRYSTAL STRUCTURE OF RICE DWARF14 IN COMPLEX WITH SYNTHETIC
TITLE    2 STRIGOLACTONE GR24
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROBABLE STRIGOLACTONE ESTERASE D14;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: ALPHA/BETA HYDROLASE RESIDUES 52-318;
COMPND   5 SYNONYM: PROTEIN DWARF-14,PROTEIN DWARF-88,PROTEIN HIGH-TILLERING
COMPND   6 DWARF 2;
COMPND   7 EC: 3.1.-.-;
COMPND   8 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: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PSUMO
KEYWDS    ALPHA/BETA, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    X.E.ZHOU,L.-H.ZHAO,W.YI,Z.-S.WU,Y.LIU,Y.KANG,L.HOU,P.W.DE WAAL,S.LI,
AUTHOR   2 Y.JIANG,K.MELCHER,H.E.XU
REVDAT   1   28-OCT-15 5DJ5    0
JRNL        AUTH   L.H.ZHAO,X.E.ZHOU,W.YI,Z.WU,Y.LIU,Y.KANG,L.HOU,P.W.DE WAAL,
JRNL        AUTH 2 S.LI,Y.JIANG,A.SCAFFIDI,G.R.FLEMATTI,S.M.SMITH,V.Q.LAM,
JRNL        AUTH 3 P.R.GRIFFIN,Y.WANG,J.LI,K.MELCHER,H.E.XU
JRNL        TITL   DESTABILIZATION OF STRIGOLACTONE RECEPTOR DWARF14 BY BINDING
JRNL        TITL 2 OF LIGAND AND E3-LIGASE SIGNALING EFFECTOR DWARF3.
JRNL        REF    CELL RES.                                  2015
JRNL        REFN                   ISSN 1001-0602
JRNL        PMID   26470846
JRNL        DOI    10.1038/CR.2015.122
REMARK   2
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 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 : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.92
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340
REMARK   3   COMPLETENESS FOR RANGE        (%) : 87.3
REMARK   3   NUMBER OF REFLECTIONS             : 17868
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.192
REMARK   3   R VALUE            (WORKING SET) : 0.190
REMARK   3   FREE R VALUE                     : 0.224
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.020
REMARK   3   FREE R VALUE TEST SET COUNT      : 1254
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 0.90
REMARK   3   SHRINKAGE RADIUS   : 0.60
REMARK   3   K_SOL              : NULL
REMARK   3   B_SOL              : NULL
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.270
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.740
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      :  0.008           4258
REMARK   3   ANGLE     :  1.147           5811
REMARK   3   CHIRALITY :  0.123            672
REMARK   3   PLANARITY :  0.006            753
REMARK   3   DIHEDRAL  : 12.713           1533
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 5DJ5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1000213301.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 09-NOV-11
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRF
REMARK 200  BEAMLINE                       : BL17U
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.21
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17932
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.202
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.7
REMARK 200  DATA REDUNDANCY                : 6.800
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.13600
REMARK 200   FOR THE DATA SET  : 14.6000
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) : 2.53
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.65400
REMARK 200  R SYM FOR SHELL            (I) : 0.65400
REMARK 200   FOR SHELL         : 1.100
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: 4IH9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, ETHYLENE GLYCOL, PH 7.5,
REMARK 280  VAPOR DIFFUSION, TEMPERATURE 298K
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       24.20000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       59.28500
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.94000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       59.28500
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.20000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.94000
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 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     SER A     2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    ALA B     4     O    HOH B   301              2.18
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    SER A  97     -117.42     57.59
REMARK 500    SER B  97     -116.21     56.76
REMARK 500    THR B 244      164.69    173.81
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 B 397        DISTANCE =  6.60 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GR2 A 800
DBREF  5DJ5 A    2   268  UNP    Q10QA5   D14_ORYSJ       52    318
DBREF  5DJ5 B    2   268  UNP    Q10QA5   D14_ORYSJ       52    318
SEQRES   1 A  267  SER GLY ALA LYS LEU LEU GLN ILE LEU ASN VAL ARG VAL
SEQRES   2 A  267  VAL GLY SER GLY GLU ARG VAL VAL VAL LEU SER HIS GLY
SEQRES   3 A  267  PHE GLY THR ASP GLN SER ALA TRP SER ARG VAL LEU PRO
SEQRES   4 A  267  TYR LEU THR ARG ASP HIS ARG VAL VAL LEU TYR ASP LEU
SEQRES   5 A  267  VAL CYS ALA GLY SER VAL ASN PRO ASP HIS PHE ASP PHE
SEQRES   6 A  267  ARG ARG TYR ASP ASN LEU ASP ALA TYR VAL ASP ASP LEU
SEQRES   7 A  267  LEU ALA ILE LEU ASP ALA LEU ARG ILE PRO ARG CYS ALA
SEQRES   8 A  267  PHE VAL GLY HIS SER VAL SER ALA MET ILE GLY ILE LEU
SEQRES   9 A  267  ALA SER ILE ARG ARG PRO ASP LEU PHE ALA LYS LEU VAL
SEQRES  10 A  267  LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP SER ASP
SEQRES  11 A  267  TYR HIS GLY GLY PHE GLU LEU GLU GLU ILE GLN GLN VAL
SEQRES  12 A  267  PHE ASP ALA MET GLY ALA ASN TYR SER ALA TRP ALA THR
SEQRES  13 A  267  GLY TYR ALA PRO LEU ALA VAL GLY ALA ASP VAL PRO ALA
SEQRES  14 A  267  ALA VAL GLN GLU PHE SER ARG THR LEU PHE ASN MET ARG
SEQRES  15 A  267  PRO ASP ILE SER LEU HIS VAL CYS GLN THR VAL PHE LYS
SEQRES  16 A  267  THR ASP LEU ARG GLY VAL LEU GLY MET VAL ARG ALA PRO
SEQRES  17 A  267  CYS VAL VAL VAL GLN THR THR ARG ASP VAL SER VAL PRO
SEQRES  18 A  267  ALA SER VAL ALA ALA TYR LEU LYS ALA HIS LEU GLY GLY
SEQRES  19 A  267  ARG THR THR VAL GLU PHE LEU GLN THR GLU GLY HIS LEU
SEQRES  20 A  267  PRO HIS LEU SER ALA PRO SER LEU LEU ALA GLN VAL LEU
SEQRES  21 A  267  ARG ARG ALA LEU ALA ARG TYR
SEQRES   1 B  267  SER GLY ALA LYS LEU LEU GLN ILE LEU ASN VAL ARG VAL
SEQRES   2 B  267  VAL GLY SER GLY GLU ARG VAL VAL VAL LEU SER HIS GLY
SEQRES   3 B  267  PHE GLY THR ASP GLN SER ALA TRP SER ARG VAL LEU PRO
SEQRES   4 B  267  TYR LEU THR ARG ASP HIS ARG VAL VAL LEU TYR ASP LEU
SEQRES   5 B  267  VAL CYS ALA GLY SER VAL ASN PRO ASP HIS PHE ASP PHE
SEQRES   6 B  267  ARG ARG TYR ASP ASN LEU ASP ALA TYR VAL ASP ASP LEU
SEQRES   7 B  267  LEU ALA ILE LEU ASP ALA LEU ARG ILE PRO ARG CYS ALA
SEQRES   8 B  267  PHE VAL GLY HIS SER VAL SER ALA MET ILE GLY ILE LEU
SEQRES   9 B  267  ALA SER ILE ARG ARG PRO ASP LEU PHE ALA LYS LEU VAL
SEQRES  10 B  267  LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP SER ASP
SEQRES  11 B  267  TYR HIS GLY GLY PHE GLU LEU GLU GLU ILE GLN GLN VAL
SEQRES  12 B  267  PHE ASP ALA MET GLY ALA ASN TYR SER ALA TRP ALA THR
SEQRES  13 B  267  GLY TYR ALA PRO LEU ALA VAL GLY ALA ASP VAL PRO ALA
SEQRES  14 B  267  ALA VAL GLN GLU PHE SER ARG THR LEU PHE ASN MET ARG
SEQRES  15 B  267  PRO ASP ILE SER LEU HIS VAL CYS GLN THR VAL PHE LYS
SEQRES  16 B  267  THR ASP LEU ARG GLY VAL LEU GLY MET VAL ARG ALA PRO
SEQRES  17 B  267  CYS VAL VAL VAL GLN THR THR ARG ASP VAL SER VAL PRO
SEQRES  18 B  267  ALA SER VAL ALA ALA TYR LEU LYS ALA HIS LEU GLY GLY
SEQRES  19 B  267  ARG THR THR VAL GLU PHE LEU GLN THR GLU GLY HIS LEU
SEQRES  20 B  267  PRO HIS LEU SER ALA PRO SER LEU LEU ALA GLN VAL LEU
SEQRES  21 B  267  ARG ARG ALA LEU ALA ARG TYR
HET    GR2  A 800      22
HETNAM     GR2 (3E,3AR,8BS)-3-({[(2R)-4-METHYL-5-OXO-2,5-DIHYDROFURAN-
HETNAM   2 GR2  2-YL]OXY}METHYLIDENE)-3,3A,4,8B-TETRAHYDRO-2H-
HETNAM   3 GR2  INDENO[1,2-B]FURAN-2-ONE
FORMUL   3  GR2    C17 H14 O5
FORMUL   4  HOH   *163(H2 O)
HELIX    1 AA1 GLY A    3  LEU A   10  1                                   8
HELIX    2 AA2 ASP A   31  SER A   36  5                                   6
HELIX    3 AA3 VAL A   38  THR A   43  1                                   6
HELIX    4 AA4 ASN A   60  PHE A   64  5                                   5
HELIX    5 AA5 ARG A   67  ASN A   71  5                                   5
HELIX    6 AA6 LEU A   72  LEU A   86  1                                  15
HELIX    7 AA7 SER A   97  ARG A  110  1                                  14
HELIX    8 AA8 GLU A  137  ASN A  151  1                                  15
HELIX    9 AA9 ASN A  151  GLY A  165  1                                  15
HELIX   10 AB1 VAL A  168  ASN A  181  1                                  14
HELIX   11 AB2 ARG A  183  LYS A  196  1                                  14
HELIX   12 AB3 LEU A  199  VAL A  206  5                                   8
HELIX   13 AB4 PRO A  222  LEU A  233  1                                  12
HELIX   14 AB5 LEU A  248  ALA A  253  1                                   6
HELIX   15 AB6 ALA A  253  LEU A  265  1                                  13
HELIX   16 AB7 GLY B    3  LEU B   10  1                                   8
HELIX   17 AB8 ASP B   31  SER B   36  5                                   6
HELIX   18 AB9 VAL B   38  ARG B   44  1                                   7
HELIX   19 AC1 ASN B   60  PHE B   64  5                                   5
HELIX   20 AC2 ARG B   67  ASP B   70  5                                   4
HELIX   21 AC3 ASN B   71  LEU B   86  1                                  16
HELIX   22 AC4 SER B   97  ARG B  110  1                                  14
HELIX   23 AC5 GLU B  137  ASN B  151  1                                  15
HELIX   24 AC6 ASN B  151  GLY B  165  1                                  15
HELIX   25 AC7 VAL B  168  ASN B  181  1                                  14
HELIX   26 AC8 ARG B  183  LYS B  196  1                                  14
HELIX   27 AC9 LEU B  199  VAL B  206  5                                   8
HELIX   28 AD1 PRO B  222  LEU B  233  1                                  12
HELIX   29 AD2 LEU B  248  ALA B  253  1                                   6
HELIX   30 AD3 ALA B  253  LEU B  265  1                                  13
SHEET    1 AA1 7 ARG A  13  VAL A  15  0
SHEET    2 AA1 7 HIS A  46  LEU A  50 -1  O  VAL A  48   N  VAL A  15
SHEET    3 AA1 7 ARG A  20  SER A  25  1  N  ARG A  20   O  ARG A  47
SHEET    4 AA1 7 CYS A  91  HIS A  96  1  O  VAL A  94   N  VAL A  23
SHEET    5 AA1 7 PHE A 114  ILE A 120  1  O  ALA A 115   N  CYS A  91
SHEET    6 AA1 7 CYS A 210  GLN A 214  1  O  VAL A 213   N  LEU A 119
SHEET    7 AA1 7 THR A 237  PHE A 241  1  O  THR A 238   N  VAL A 212
SHEET    1 AA2 7 ARG B  13  GLY B  16  0
SHEET    2 AA2 7 ARG B  47  LEU B  50 -1  O  VAL B  48   N  VAL B  15
SHEET    3 AA2 7 VAL B  21  SER B  25  1  N  VAL B  22   O  VAL B  49
SHEET    4 AA2 7 CYS B  91  HIS B  96  1  O  VAL B  94   N  VAL B  23
SHEET    5 AA2 7 PHE B 114  ILE B 120  1  O  VAL B 118   N  PHE B  93
SHEET    6 AA2 7 CYS B 210  GLN B 214  1  O  VAL B 213   N  LEU B 119
SHEET    7 AA2 7 THR B 237  PHE B 241  1  O  THR B 238   N  VAL B 212
SITE     1 AC1  9 PHE A  28  SER A  97  VAL A  98  VAL A 144
SITE     2 AC1  9 TYR A 159  CYS A 191  VAL A 219  SER A 220
SITE     3 AC1  9 HIS A 247
CRYST1   48.400   87.880  118.570  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      0.020661  0.000000  0.000000        0.00000
SCALE2      0.000000  0.011379  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008434        0.00000
TER    2068      TYR A 268
TER    4139      TYR B 268
MASTER      253    0    1   30   14    0    3    6 4301    2   22   42
END