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PDBsum entry 3ein

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Transferase PDB id
3ein
Jmol
Contents
Protein chain
207 a.a.
Ligands
GSH
Waters ×264
HEADER    TRANSFERASE                             17-SEP-08   3EIN
TITLE     DELTA CLASS GST
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUTATHIONE S-TRANSFERASE 1-1;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: GST CLASS-THETA;
COMPND   5 EC: 2.5.1.18;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE   3 ORGANISM_COMMON: FRUIT FLY;
SOURCE   4 ORGANISM_TAXID: 7227;
SOURCE   5 GENE: GSTD1, GST, GST1, CG10045;
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: PET30A(+)
KEYWDS    GLUTATHIONE S-TRANSFERASE, GLUTATHIONE, DELTA-CLASS GST, TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.C.FEIL
REVDAT   2   21-DEC-11 3EIN    1       HETATM HETNAM VERSN
REVDAT   1   01-SEP-09 3EIN    0
JRNL        AUTH   S.C.FEIL,W.Y.LOW,H.L.NG,J.PYKE,P.GOOLEY,M.W.PARKER,C.ROBIN,
JRNL        AUTH 2 M.MCCONVILLE,P.BATTERHAM
JRNL        TITL   PROBING INSECT DETOXIFICATION SYSTEMS
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    1.13 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.13
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.61
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5
REMARK   3   NUMBER OF REFLECTIONS             : 66014
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) : 0.141
REMARK   3   R VALUE            (WORKING SET) : 0.140
REMARK   3   FREE R VALUE                     : 0.157
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 3504
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.13
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.16
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4131
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 83.59
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2440
REMARK   3   BIN FREE R VALUE SET COUNT          : 219
REMARK   3   BIN FREE R VALUE                    : 0.3150
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1672
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 20
REMARK   3   SOLVENT ATOMS            : 258
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.94
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.22000
REMARK   3    B22 (A**2) : -0.35000
REMARK   3    B33 (A**2) : 0.09000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.03000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.033
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.032
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.018
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.803
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.978
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.975
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1823 ; 0.008 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  1253 ; 0.008 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2490 ; 1.267 ; 1.963
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3068 ; 0.950 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   231 ; 5.313 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    85 ;37.803 ;24.235
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   307 ;11.242 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;16.539 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   265 ; 0.248 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2039 ; 0.006 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   392 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   419 ; 0.216 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1282 ; 0.171 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   920 ; 0.195 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):   838 ; 0.085 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   175 ; 0.109 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    17 ; 0.192 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    51 ; 0.197 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    29 ; 0.130 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1419 ; 2.270 ; 2.000
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   426 ; 1.519 ; 2.000
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1751 ; 2.627 ; 3.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   921 ; 2.702 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   727 ; 3.400 ; 3.000
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  3966 ; 1.546 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   264 ;10.238 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  3015 ; 6.547 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3EIN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-SEP-08.
REMARK 100 THE RCSB ID CODE IS RCSB049370.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 27-FEB-07
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 14-BM-C
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : BENT CONICAL SI MIRRORS
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 69523
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.130
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2
REMARK 200  DATA REDUNDANCY                : 4.000
REMARK 200  R MERGE                    (I) : 0.04800
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.13
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.17
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.19600
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
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 38.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25%(W/V) PEG3350, 0.2M NACL, 100MM
REMARK 280  HEPES, PH8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
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        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       35.88750
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.60600
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       35.88750
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       31.60600
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.2 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 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  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     1
REMARK 465     GLU A   209
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  65      106.32     75.18
REMARK 500    TYR A  84       77.31   -157.66
REMARK 500    ALA A 149       50.16   -154.94
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 GSH A 210
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PN9   RELATED DB: PDB
REMARK 900 GST FROM ANOPHELES GAMBIAE
REMARK 900 RELATED ID: 1JLV   RELATED DB: PDB
REMARK 900 GST FROM ANOPHELES DIRUS SPECIES
REMARK 900 RELATED ID: 1R5A   RELATED DB: PDB
REMARK 900 GST FROM ANOPHELES CRACENS
DBREF  3EIN A    1   209  UNP    P20432   GSTT1_DROME      1    209
SEQRES   1 A  209  MET VAL ASP PHE TYR TYR LEU PRO GLY SER SER PRO CYS
SEQRES   2 A  209  ARG SER VAL ILE MET THR ALA LYS ALA VAL GLY VAL GLU
SEQRES   3 A  209  LEU ASN LYS LYS LEU LEU ASN LEU GLN ALA GLY GLU HIS
SEQRES   4 A  209  LEU LYS PRO GLU PHE LEU LYS ILE ASN PRO GLN HIS THR
SEQRES   5 A  209  ILE PRO THR LEU VAL ASP ASN GLY PHE ALA LEU TRP GLU
SEQRES   6 A  209  SER ARG ALA ILE GLN VAL TYR LEU VAL GLU LYS TYR GLY
SEQRES   7 A  209  LYS THR ASP SER LEU TYR PRO LYS CYS PRO LYS LYS ARG
SEQRES   8 A  209  ALA VAL ILE ASN GLN ARG LEU TYR PHE ASP MET GLY THR
SEQRES   9 A  209  LEU TYR GLN SER PHE ALA ASN TYR TYR TYR PRO GLN VAL
SEQRES  10 A  209  PHE ALA LYS ALA PRO ALA ASP PRO GLU ALA PHE LYS LYS
SEQRES  11 A  209  ILE GLU ALA ALA PHE GLU PHE LEU ASN THR PHE LEU GLU
SEQRES  12 A  209  GLY GLN ASP TYR ALA ALA GLY ASP SER LEU THR VAL ALA
SEQRES  13 A  209  ASP ILE ALA LEU VAL ALA THR VAL SER THR PHE GLU VAL
SEQRES  14 A  209  ALA LYS PHE GLU ILE SER LYS TYR ALA ASN VAL ASN ARG
SEQRES  15 A  209  TRP TYR GLU ASN ALA LYS LYS VAL THR PRO GLY TRP GLU
SEQRES  16 A  209  GLU ASN TRP ALA GLY CYS LEU GLU PHE LYS LYS TYR PHE
SEQRES  17 A  209  GLU
HET    GSH  A 210      20
HETNAM     GSH GLUTATHIONE
FORMUL   2  GSH    C10 H17 N3 O6 S
FORMUL   3  HOH   *258(H2 O)
HELIX    1   1 SER A   10  GLY A   24  1                                  15
HELIX    2   2 ASN A   33  LEU A   40  5                                   8
HELIX    3   3 LYS A   41  LYS A   46  1                                   6
HELIX    4   4 GLU A   65  GLY A   78  1                                  14
HELIX    5   5 CYS A   87  THR A  104  1                                  18
HELIX    6   6 THR A  104  LYS A  120  1                                  17
HELIX    7   7 ASP A  124  LEU A  142  1                                  19
HELIX    8   8 THR A  154  ALA A  170  1                                  17
HELIX    9   9 GLU A  173  LYS A  176  5                                   4
HELIX   10  10 TYR A  177  THR A  191  1                                  15
HELIX   11  11 GLY A  193  LYS A  205  1                                  13
HELIX   12  12 LYS A  206  PHE A  208  5                                   3
SHEET    1   A 4 ASN A  28  LEU A  31  0
SHEET    2   A 4 ASP A   3  TYR A   6  1  N  PHE A   4   O  LYS A  30
SHEET    3   A 4 THR A  55  ASP A  58 -1  O  THR A  55   N  TYR A   5
SHEET    4   A 4 PHE A  61  TRP A  64 -1  O  LEU A  63   N  LEU A  56
CISPEP   1 ILE A   53    PRO A   54          0         1.72
SITE     1 AC1 18 SER A  10  PRO A  12  HIS A  39  HIS A  51
SITE     2 AC1 18 THR A  52  ILE A  53  PRO A  54  GLU A  65
SITE     3 AC1 18 SER A  66  ARG A  67  MET A 102  HOH A 212
SITE     4 AC1 18 HOH A 220  HOH A 221  HOH A 226  HOH A 354
SITE     5 AC1 18 HOH A 365  HOH A 466
CRYST1   71.775   63.212   54.513  90.00 129.84  90.00 C 1 2 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      0.013932  0.000000  0.011623        0.00000
SCALE2      0.000000  0.015820  0.000000        0.00000
SCALE3      0.000000  0.000000  0.023890        0.00000
      
PROCHECK
Go to PROCHECK summary
 References