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PDBsum entry 2fb9

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Ligase PDB id
2fb9
Jmol
Contents
Protein chain
322 a.a.
Waters ×115
HEADER    LIGASE                                  08-DEC-05   2FB9
TITLE     CRYSTAL STRUCTURE OF THE APO FORM OF D-ALANINE: D-ALANINE LIGASE (DDL)
TITLE    2 FROM THERMUS CALDOPHILUS: A BASIS FOR THE SUBSTRATE-INDUCED
TITLE    3 CONFORMATIONAL CHANGES
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: D-ALANINE:D-ALANINE LIGASE;
COMPND   3 CHAIN: A;
COMPND   4 EC: 6.3.2.4;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: THERMUS CALDOPHILUS;
SOURCE   3 ORGANISM_TAXID: 272;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PKK223-3
KEYWDS    LIGASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.H.LEE,Y.NA,S.H.EOM
REVDAT   3   13-JUL-11 2FB9    1       VERSN
REVDAT   2   24-FEB-09 2FB9    1       VERSN
REVDAT   1   29-AUG-06 2FB9    0
JRNL        AUTH   J.H.LEE,Y.NA,H.E.SONG,D.KIM,B.H.PARK,S.H.RHO,Y.J.IM,M.K.KIM,
JRNL        AUTH 2 G.B.KANG,D.S.LEE,S.H.EOM
JRNL        TITL   CRYSTAL STRUCTURE OF THE APO FORM OF D-ALANINE: D-ALANINE
JRNL        TITL 2 LIGASE (DDL) FROM THERMUS CALDOPHILUS: A BASIS FOR THE
JRNL        TITL 3 SUBSTRATE-INDUCED CONFORMATIONAL CHANGES
JRNL        REF    PROTEINS                      V.  64  1078 2006
JRNL        REFN                   ISSN 0887-3585
JRNL        PMID   16779845
JRNL        DOI    10.1002/PROT.20927
REMARK   2
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 24867
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.228
REMARK   3   FREE R VALUE                     : 0.268
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 3379
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           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
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            : 2481
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 115
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  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : 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  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2FB9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-DEC-05.
REMARK 100 THE RCSB ID CODE IS RCSB035676.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 24-NOV-04
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : 8.5
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-6B
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                  : GRAPHITE
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25640
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 85.0
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
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) : 1.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.96
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 61.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 29%(W/V) PEG MME 2000, 0.1M TRIS-HCL,
REMARK 280  0.2M SODIUM ACETATE, 0.2M KSCN, PH 8.5, VAPOR DIFFUSION, HANGING
REMARK 280  DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   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       29.66200
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       29.66200
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       57.60800
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       66.37200
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       57.60800
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       66.37200
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       29.66200
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       57.60800
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       66.37200
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       29.66200
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       57.60800
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       66.37200
REMARK 290   SMTRY3   8  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 300 REMARK: BIOLOGICAL UNIT IS DIMER
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 2740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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      230.43200
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       29.66200
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    PRO A  32       15.77    -65.78
REMARK 500    GLU A  63     -112.43    -50.39
REMARK 500    PHE A  68      -92.89     -9.17
REMARK 500    PRO A  69       90.54    -49.34
REMARK 500    TRP A  74      -45.55     58.81
REMARK 500    ASP A 150      157.35    -41.73
REMARK 500    VAL A 198      141.33     64.70
REMARK 500    VAL A 209      -56.35     67.65
REMARK 500    LYS A 231     -141.11     63.40
REMARK 500    ALA A 270      143.42   -178.07
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    PHE A  68        24.0      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
DBREF  2FB9 A    4   322  UNP    Q3T920   Q3T920_THECA     1    319
SEQADV 2FB9 MET A    1  UNP  Q3T920              CLONING ARTIFACT
SEQADV 2FB9 GLU A    2  UNP  Q3T920              CLONING ARTIFACT
SEQADV 2FB9 PHE A    3  UNP  Q3T920              CLONING ARTIFACT
SEQRES   1 A  322  MET GLU PHE MET ARG VAL LEU LEU ILE ALA GLY GLY VAL
SEQRES   2 A  322  SER PRO GLU HIS GLU VAL SER LEU LEU SER ALA GLU GLY
SEQRES   3 A  322  VAL LEU ARG HIS ILE PRO PHE PRO THR ASP LEU ALA VAL
SEQRES   4 A  322  ILE ALA GLN ASP GLY ARG TRP LEU LEU GLY GLU LYS ALA
SEQRES   5 A  322  LEU THR ALA LEU GLU ALA LYS ALA ALA PRO GLU GLY GLU
SEQRES   6 A  322  HIS PRO PHE PRO PRO PRO LEU SER TRP GLU ARG TYR ASP
SEQRES   7 A  322  VAL VAL PHE PRO LEU LEU HIS GLY ARG PHE GLY GLU ASP
SEQRES   8 A  322  GLY THR VAL GLN GLY PHE LEU GLU LEU LEU GLY LYS PRO
SEQRES   9 A  322  TYR VAL GLY ALA GLY VAL ALA ALA SER ALA LEU CYS MET
SEQRES  10 A  322  ASP LYS ASP LEU SER LYS ARG VAL LEU ALA GLN ALA GLY
SEQRES  11 A  322  VAL PRO VAL VAL PRO TRP VAL ALA VAL ARG LYS GLY GLU
SEQRES  12 A  322  PRO PRO VAL VAL PRO PHE ASP PRO PRO PHE PHE VAL LYS
SEQRES  13 A  322  PRO ALA ASN THR GLY SER SER VAL GLY ILE SER ARG VAL
SEQRES  14 A  322  GLU ARG PHE GLN ASP LEU GLU ALA ALA LEU ALA LEU ALA
SEQRES  15 A  322  PHE ARG TYR ASP GLU LYS ALA VAL VAL GLU LYS ALA LEU
SEQRES  16 A  322  SER PRO VAL ARG GLU LEU GLU VAL GLY VAL LEU GLY ASN
SEQRES  17 A  322  VAL PHE GLY GLU ALA SER PRO VAL GLY GLU VAL ARG TYR
SEQRES  18 A  322  GLU ALA PRO PHE TYR ASP TYR GLU THR LYS TYR THR PRO
SEQRES  19 A  322  GLY ARG ALA GLU LEU LEU ILE PRO ALA PRO LEU ASP PRO
SEQRES  20 A  322  GLY THR GLN GLU THR VAL GLN GLU LEU ALA LEU LYS ALA
SEQRES  21 A  322  TYR LYS VAL LEU GLY VAL ARG GLY MET ALA ARG VAL ASP
SEQRES  22 A  322  PHE PHE LEU ALA GLU GLY GLU LEU TYR LEU ASN GLU LEU
SEQRES  23 A  322  ASN THR ILE PRO GLY PHE THR PRO THR SER MET TYR PRO
SEQRES  24 A  322  ARG LEU PHE GLU ALA GLY GLY VAL ALA TYR PRO GLU LEU
SEQRES  25 A  322  LEU ARG ARG LEU VAL GLU LEU ALA LEU THR
FORMUL   2  HOH   *115(H2 O)
HELIX    1   1 GLU A   16  ILE A   31  1                                  16
HELIX    2   2 LEU A   48  LEU A   56  1                                   9
HELIX    3   3 GLY A   92  GLY A  102  1                                  11
HELIX    4   4 GLY A  109  ASP A  118  1                                  10
HELIX    5   5 ASP A  118  ALA A  129  1                                  12
HELIX    6   6 ARG A  171  PHE A  183  1                                  13
HELIX    7   7 GLY A  248  GLY A  265  1                                  18
HELIX    8   8 SER A  296  GLY A  305  1                                  10
HELIX    9   9 ALA A  308  LEU A  321  1                                  14
SHEET    1   A 4 TRP A  46  LEU A  47  0
SHEET    2   A 4 THR A  35  ILE A  40 -1  N  VAL A  39   O  LEU A  47
SHEET    3   A 4 VAL A   6  GLY A  11  1  N  LEU A   8   O  ASP A  36
SHEET    4   A 4 VAL A  79  LEU A  83  1  O  PHE A  81   N  LEU A   7
SHEET    1   B 4 TRP A 136  ARG A 140  0
SHEET    2   B 4 LYS A 188  LYS A 193 -1  O  ALA A 189   N  VAL A 139
SHEET    3   B 4 PHE A 153  PRO A 157 -1  N  PHE A 154   O  GLU A 192
SHEET    4   B 4 SER A 167  VAL A 169 -1  O  SER A 167   N  VAL A 155
SHEET    1   C 5 ARG A 236  LEU A 240  0
SHEET    2   C 5 GLU A 212  GLU A 222 -1  N  ARG A 220   O  GLU A 238
SHEET    3   C 5 ARG A 199  LEU A 206 -1  N  GLU A 202   O  GLY A 217
SHEET    4   C 5 MET A 269  ALA A 277 -1  O  PHE A 274   N  LEU A 201
SHEET    5   C 5 GLU A 280  ASN A 287 -1  O  GLU A 285   N  ASP A 273
SHEET    1   D 2 PHE A 225  ASP A 227  0
SHEET    2   D 2 LYS A 231  THR A 233 -1  O  LYS A 231   N  ASP A 227
CISPEP   1 SER A  196    PRO A  197          0         0.21
CISPEP   2 ILE A  241    PRO A  242          0        -0.06
CRYST1  115.216  132.744   59.324  90.00  90.00  90.00 C 2 2 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      0.008679  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007533  0.000000        0.00000
SCALE3      0.000000  0.000000  0.016857        0.00000
      
PROCHECK
Go to PROCHECK summary
 References