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PDBsum entry 2dzp

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Lyase PDB id
2dzp
Jmol
Contents
Protein chains
244 a.a.
Waters ×360
HEADER    LYASE                                   30-SEP-06   2DZP
TITLE     STRUCTURE OF MUTANT TRYPTOPHAN SYNTHASE ALPHA-SUBUNIT
TITLE    2 (D17N) FROM A HYPERTHERMOPHILE, PYROCOCCUS FURIOSUS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TRYPTOPHAN SYNTHASE ALPHA CHAIN;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: TRYPTOPHAN SYNTHASE ALPHA-SUBUNIT;
COMPND   5 EC: 4.2.1.20;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS;
SOURCE   3 ORGANISM_TAXID: 2261;
SOURCE   4 GENE: TRPA;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PA1974
KEYWDS    TRYPTOPHAN SYNTHASE ALPHA-SUBUNIT, HYPERTHERMOPHILE,
KEYWDS   2 PYROCOCCUS FURIOSUS, X-RAY ANALYSIS, STABILITY, CALORIMETRY,
KEYWDS   3 LYASE, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON
KEYWDS   4 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN
KEYWDS   5 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.OGASAHARA,Y.YAMAGATA,K.YUTANI,RIKEN STRUCTURAL
AUTHOR   2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT   3   24-FEB-09 2DZP    1       VERSN
REVDAT   2   16-OCT-07 2DZP    1       AUTHOR KEYWDS REMARK
REVDAT   1   28-AUG-07 2DZP    0
JRNL        AUTH   K.OGASAHARA,Y.YAMAGATA,K.YUTANI
JRNL        TITL   STRUCTURES OF MUTANT TRYPTOPHAN SYNTHASE
JRNL        TITL 2 ALPHA-SUBUNITS FROM A HYPERTHERMOPHILE, PYROCOCCUS
JRNL        TITL 3 FURIOSUS
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   Y.YAMAGATA,K.OGASAHARA,Y.HIOKI,S.J.LEE,A.NAKAGAWA,
REMARK   1  AUTH 2 H.NAKAMURA,M.ISHIDA,S.KURAMITSU,K.YUTANI
REMARK   1  TITL   ENTROPIC STABILIZATION OF THE TRYPTOPHAN SYNTHASE
REMARK   1  TITL 2 ALPHA-SUBUNIT FROM A HYPERTHERMOPHILE, PYROCOCCUS
REMARK   1  TITL 3 FURIOSUS. X-RAY ANALYSIS AND CALORIMETRY
REMARK   1  REF    J.BIOL.CHEM.                  V. 276 11062 2001
REMARK   1  REFN                   ISSN 0021-9258
REMARK   1  PMID   11118452
REMARK   1  DOI    10.1074/JBC.M009987200
REMARK   2
REMARK   2 RESOLUTION.    2.40 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 : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.98
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2421910.490
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.2
REMARK   3   NUMBER OF REFLECTIONS             : 18134
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 SET) : 0.218
REMARK   3   FREE R VALUE                     : 0.279
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800
REMARK   3   FREE R VALUE TEST SET COUNT      : 869
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.009
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.55
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.10
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2886
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2400
REMARK   3   BIN FREE R VALUE                    : 0.3180
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.60
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 139
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.027
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3837
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 360
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 32.80
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.40
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -5.54000
REMARK   3    B22 (A**2) : 6.57000
REMARK   3    B33 (A**2) : -1.03000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.28
REMARK   3   ESD FROM SIGMAA              (A) : 0.19
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.37
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.29
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.005
REMARK   3   BOND ANGLES            (DEGREES) : 1.20
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.50
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.70
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.410 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.200 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.940 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.720 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.31
REMARK   3   BSOL        : 43.79
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  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2DZP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-OCT-06.
REMARK 100 THE RCSB ID CODE IS RCSB026043.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-OCT-01
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               : SPRING-8
REMARK 200  BEAMLINE                       : BL40B2
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                  : SI
REMARK 200  OPTICS                         : MIRROR
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          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23451
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.210
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.4
REMARK 200  DATA REDUNDANCY                : 4.500
REMARK 200  R MERGE                    (I) : 0.04900
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 36.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.21
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.2
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.12600
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 18.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1GEQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 41.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES-NAOH, 10-15% PEG 20000, PH
REMARK 280  6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 283K
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       82.93450
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       82.93450
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       37.13400
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       37.88850
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       37.13400
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       37.88850
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       82.93450
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       37.13400
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       37.88850
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       82.93450
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       37.13400
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       37.88850
REMARK 290   SMTRY3   8  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     THR A   169
REMARK 465     GLY A   170
REMARK 465     ALA A   171
REMARK 465     ARG A   172
REMARK 465     GLY B   170
REMARK 465     ALA B   171
REMARK 465     ARG B   172
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    ASN A  61       11.86    -66.18
REMARK 500    LEU A  65      -29.37    -39.78
REMARK 500    ARG A  77       -5.77    -55.66
REMARK 500    PHE A 159      162.49    179.01
REMARK 500    SER A 164      115.54   -161.50
REMARK 500    TYR A 166      -57.53    -29.07
REMARK 500    SER A 201       10.90   -160.62
REMARK 500    GLU A 233       22.11    -78.61
REMARK 500    THR A 235      -71.46    -28.31
REMARK 500    PHE B 159      158.21    179.82
REMARK 500    SER B 201       -0.26   -148.59
REMARK 500    THR B 235      -73.40    -24.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GEQ   RELATED DB: PDB
REMARK 900 WILD-TYPE
REMARK 900 RELATED ID: 2DZS   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, E103A MUTANT
REMARK 900 RELATED ID: 2DZT   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, D110A MUTANT
REMARK 900 RELATED ID: 2DZU   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, D110N MUTANT
REMARK 900 RELATED ID: 2DZV   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, D146A MUTANT
REMARK 900 RELATED ID: 2DZW   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, E244A MUTANT
REMARK 900 RELATED ID: 2DZX   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, E131A,E132A MUTANT
REMARK 900 RELATED ID: MY_001000046.2   RELATED DB: TARGETDB
DBREF  2DZP A    1   248  UNP    Q8U094   TRPA_PYRFU       1    248
DBREF  2DZP B    1   248  UNP    Q8U094   TRPA_PYRFU       1    248
SEQADV 2DZP ASN A   17  UNP  Q8U094    ASP    17 ENGINEERED
SEQADV 2DZP ASN B   17  UNP  Q8U094    ASP    17 ENGINEERED
SEQRES   1 A  248  MET PHE LYS ASP GLY SER LEU ILE PRO TYR LEU THR ALA
SEQRES   2 A  248  GLY ASP PRO ASN LYS GLN SER THR LEU ASN PHE LEU LEU
SEQRES   3 A  248  ALA LEU ASP GLU TYR ALA GLY ALA ILE GLU LEU GLY ILE
SEQRES   4 A  248  PRO PHE SER ASP PRO ILE ALA ASP GLY LYS THR ILE GLN
SEQRES   5 A  248  GLU SER HIS TYR ARG ALA LEU LYS ASN GLY PHE LYS LEU
SEQRES   6 A  248  ARG GLU ALA PHE TRP ILE VAL LYS GLU PHE ARG ARG HIS
SEQRES   7 A  248  SER SER THR PRO ILE VAL LEU MET THR TYR TYR ASN PRO
SEQRES   8 A  248  ILE TYR ARG ALA GLY VAL ARG ASN PHE LEU ALA GLU ALA
SEQRES   9 A  248  LYS ALA SER GLY VAL ASP GLY ILE LEU VAL VAL ASP LEU
SEQRES  10 A  248  PRO VAL PHE HIS ALA LYS GLU PHE THR GLU ILE ALA ARG
SEQRES  11 A  248  GLU GLU GLY ILE LYS THR VAL PHE LEU ALA ALA PRO ASN
SEQRES  12 A  248  THR PRO ASP GLU ARG LEU LYS VAL ILE ASP ASP MET THR
SEQRES  13 A  248  THR GLY PHE VAL TYR LEU VAL SER LEU TYR GLY THR THR
SEQRES  14 A  248  GLY ALA ARG GLU GLU ILE PRO LYS THR ALA TYR ASP LEU
SEQRES  15 A  248  LEU ARG ARG ALA LYS ARG ILE CYS ARG ASN LYS VAL ALA
SEQRES  16 A  248  VAL GLY PHE GLY VAL SER LYS ARG GLU HIS VAL VAL SER
SEQRES  17 A  248  LEU LEU LYS GLU GLY ALA ASN GLY VAL VAL VAL GLY SER
SEQRES  18 A  248  ALA LEU VAL LYS ILE ILE GLY GLU LYS GLY ARG GLU ALA
SEQRES  19 A  248  THR GLU PHE LEU LYS LYS LYS VAL GLU GLU LEU LEU GLY
SEQRES  20 A  248  ILE
SEQRES   1 B  248  MET PHE LYS ASP GLY SER LEU ILE PRO TYR LEU THR ALA
SEQRES   2 B  248  GLY ASP PRO ASN LYS GLN SER THR LEU ASN PHE LEU LEU
SEQRES   3 B  248  ALA LEU ASP GLU TYR ALA GLY ALA ILE GLU LEU GLY ILE
SEQRES   4 B  248  PRO PHE SER ASP PRO ILE ALA ASP GLY LYS THR ILE GLN
SEQRES   5 B  248  GLU SER HIS TYR ARG ALA LEU LYS ASN GLY PHE LYS LEU
SEQRES   6 B  248  ARG GLU ALA PHE TRP ILE VAL LYS GLU PHE ARG ARG HIS
SEQRES   7 B  248  SER SER THR PRO ILE VAL LEU MET THR TYR TYR ASN PRO
SEQRES   8 B  248  ILE TYR ARG ALA GLY VAL ARG ASN PHE LEU ALA GLU ALA
SEQRES   9 B  248  LYS ALA SER GLY VAL ASP GLY ILE LEU VAL VAL ASP LEU
SEQRES  10 B  248  PRO VAL PHE HIS ALA LYS GLU PHE THR GLU ILE ALA ARG
SEQRES  11 B  248  GLU GLU GLY ILE LYS THR VAL PHE LEU ALA ALA PRO ASN
SEQRES  12 B  248  THR PRO ASP GLU ARG LEU LYS VAL ILE ASP ASP MET THR
SEQRES  13 B  248  THR GLY PHE VAL TYR LEU VAL SER LEU TYR GLY THR THR
SEQRES  14 B  248  GLY ALA ARG GLU GLU ILE PRO LYS THR ALA TYR ASP LEU
SEQRES  15 B  248  LEU ARG ARG ALA LYS ARG ILE CYS ARG ASN LYS VAL ALA
SEQRES  16 B  248  VAL GLY PHE GLY VAL SER LYS ARG GLU HIS VAL VAL SER
SEQRES  17 B  248  LEU LEU LYS GLU GLY ALA ASN GLY VAL VAL VAL GLY SER
SEQRES  18 B  248  ALA LEU VAL LYS ILE ILE GLY GLU LYS GLY ARG GLU ALA
SEQRES  19 B  248  THR GLU PHE LEU LYS LYS LYS VAL GLU GLU LEU LEU GLY
SEQRES  20 B  248  ILE
FORMUL   3  HOH   *360(H2 O)
HELIX    1   1 ASN A   17  ASP A   29  1                                  13
HELIX    2   2 GLU A   30  ALA A   32  5                                   3
HELIX    3   3 GLY A   48  ASN A   61  1                                  14
HELIX    4   4 ARG A   66  ARG A   77  1                                  12
HELIX    5   5 TYR A   88  GLY A   96  1                                   9
HELIX    6   6 GLY A   96  GLY A  108  1                                  13
HELIX    7   7 PRO A  118  GLU A  132  1                                  15
HELIX    8   8 PRO A  145  THR A  156  1                                  12
HELIX    9   9 PRO A  176  ARG A  188  1                                  13
HELIX   10  10 LYS A  202  GLU A  212  1                                  11
HELIX   11  11 GLY A  220  GLY A  231  1                                  12
HELIX   12  12 ALA A  234  GLY A  247  1                                  14
HELIX   13  13 ASN B   17  ASP B   29  1                                  13
HELIX   14  14 GLU B   30  ALA B   32  5                                   3
HELIX   15  15 GLY B   48  ASN B   61  1                                  14
HELIX   16  16 ARG B   66  ARG B   77  1                                  12
HELIX   17  17 TYR B   88  GLY B   96  1                                   9
HELIX   18  18 GLY B   96  GLY B  108  1                                  13
HELIX   19  19 PRO B  118  PHE B  120  5                                   3
HELIX   20  20 HIS B  121  GLY B  133  1                                  13
HELIX   21  21 PRO B  145  THR B  156  1                                  12
HELIX   22  22 PRO B  176  ARG B  188  1                                  13
HELIX   23  23 LYS B  202  GLU B  212  1                                  11
HELIX   24  24 GLY B  220  GLY B  231  1                                  12
HELIX   25  25 ALA B  234  GLY B  247  1                                  14
SHEET    1   A 9 SER A   6  THR A  12  0
SHEET    2   A 9 ILE A  35  GLY A  38  1  O  GLY A  38   N  LEU A  11
SHEET    3   A 9 ILE A  83  THR A  87  1  O  MET A  86   N  LEU A  37
SHEET    4   A 9 GLY A 111  VAL A 114  1  O  LEU A 113   N  LEU A  85
SHEET    5   A 9 LYS A 135  ALA A 140  1  O  LYS A 135   N  ILE A 112
SHEET    6   A 9 PHE A 159  VAL A 163  1  O  TYR A 161   N  PHE A 138
SHEET    7   A 9 VAL A 194  GLY A 197  1  O  GLY A 197   N  LEU A 162
SHEET    8   A 9 GLY A 216  VAL A 219  1  O  VAL A 218   N  VAL A 196
SHEET    9   A 9 SER A   6  THR A  12  1  N  ILE A   8   O  VAL A 217
SHEET    1   B 9 SER B   6  THR B  12  0
SHEET    2   B 9 ILE B  35  GLY B  38  1  O  GLY B  38   N  LEU B  11
SHEET    3   B 9 ILE B  83  THR B  87  1  O  VAL B  84   N  ILE B  35
SHEET    4   B 9 GLY B 111  VAL B 114  1  O  GLY B 111   N  LEU B  85
SHEET    5   B 9 LYS B 135  ALA B 140  1  O  LYS B 135   N  ILE B 112
SHEET    6   B 9 PHE B 159  VAL B 163  1  O  VAL B 163   N  ALA B 140
SHEET    7   B 9 VAL B 194  GLY B 197  1  O  GLY B 197   N  LEU B 162
SHEET    8   B 9 GLY B 216  VAL B 219  1  O  VAL B 218   N  VAL B 196
SHEET    9   B 9 SER B   6  THR B  12  1  N  ILE B   8   O  VAL B 217
CISPEP   1 ASP A   15    PRO A   16          0         0.18
CISPEP   2 ASP B   15    PRO B   16          0        -0.38
CRYST1   74.268   75.777  165.869  90.00  90.00  90.00 C 2 2 21     16
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      0.013465  0.000000  0.000000        0.00000
SCALE2      0.000000  0.013197  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006029        0.00000
      
PROCHECK
Go to PROCHECK summary
 References