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PDBsum entry 2f4e

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Top Page protein Protein-protein interface(s) links
Signaling protein PDB id
2f4e
Jmol
Contents
Protein chains
131 a.a.
Waters ×46
HEADER    SIGNALING PROTEIN                       23-NOV-05   2F4E
TITLE     N-TERMINAL DOMAIN OF FKBP42 FROM ARABIDOPSIS THALIANA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ATFKBP42;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: N-TERMINAL FKBP-TYPE DOMAIN, RESIDUES 1-180;
COMPND   5 SYNONYM: TWD1 (TWISTED DWARF 1);
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE   3 ORGANISM_COMMON: THALE CRESS;
SOURCE   4 ORGANISM_TAXID: 3702;
SOURCE   5 STRAIN: ECOTYPE COLUMBIA;
SOURCE   6 GENE: TWD1;
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS    FKBP-LIKE, ALPHA-BETA, SIGNALING PROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    O.H.WEIERGRABER,A.ECKHOFF,J.GRANZIN
REVDAT   2   24-FEB-09 2F4E    1       VERSN
REVDAT   1   10-JAN-06 2F4E    0
JRNL        AUTH   O.H.WEIERGRABER,A.ECKHOFF,J.GRANZIN
JRNL        TITL   CRYSTAL STRUCTURE OF A PLANT IMMUNOPHILIN DOMAIN
JRNL        TITL 2 INVOLVED IN REGULATION OF MDR-TYPE ABC
JRNL        TITL 3 TRANSPORTERS.
JRNL        REF    FEBS LETT.                    V. 580   251 2006
JRNL        REFN                   ISSN 0014-5793
JRNL        PMID   16364310
JRNL        DOI    10.1016/J.FEBSLET.2005.12.007
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.32 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS
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) : 2.32
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.28
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
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             : 11907
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : SHELLS
REMARK   3   R VALUE            (WORKING SET) : 0.246
REMARK   3   FREE R VALUE                     : 0.283
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 589
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            : 2029
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 46
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 46.70
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.22
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) : 0.35
REMARK   3   ESD FROM SIGMAA              (A) : NULL
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) : 0.40
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.008
REMARK   3   BOND ANGLES            (DEGREES) : 1.50
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.70
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.97
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC
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 2F4E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-DEC-05.
REMARK 100 THE RCSB ID CODE IS RCSB035438.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 05-OCT-02
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               : ESRF
REMARK 200  BEAMLINE                       : ID14-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934
REMARK 200  MONOCHROMATOR                  : DIAMOND, GERMANIUM
REMARK 200  OPTICS                         : MONOCHROMATORS, MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA, TRUNCATE)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11953
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.320
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.280
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.1
REMARK 200  DATA REDUNDANCY                : 6.200
REMARK 200  R MERGE                    (I) : 0.05500
REMARK 200  R SYM                      (I) : 0.05500
REMARK 200   FOR THE DATA SET  : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.32
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.45
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.19800
REMARK 200  R SYM FOR SHELL            (I) : 0.19800
REMARK 200   FOR SHELL         : 3.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1FKF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 26.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.5 M AMMONIUM SULFATE, 0.1 M
REMARK 280  SODIUM CHLORIDE, 0.1 M TRIS-HCL, PH 8.0, VAPOR DIFFUSION,
REMARK 280  HANGING DROP, TEMPERATURE 290K
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       17.49000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.38900
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.38350
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       61.38900
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       17.49000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       31.38350
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     MET A     1
REMARK 465     ASP A     2
REMARK 465     GLU A     3
REMARK 465     SER A     4
REMARK 465     LEU A     5
REMARK 465     GLU A     6
REMARK 465     HIS A     7
REMARK 465     GLN A     8
REMARK 465     THR A     9
REMARK 465     GLN A    10
REMARK 465     THR A    11
REMARK 465     HIS A    12
REMARK 465     ASP A    13
REMARK 465     GLN A    14
REMARK 465     GLU A    15
REMARK 465     SER A    16
REMARK 465     GLU A    17
REMARK 465     ILE A    18
REMARK 465     VAL A    19
REMARK 465     THR A    20
REMARK 465     GLU A    21
REMARK 465     GLY A    22
REMARK 465     SER A    23
REMARK 465     ALA A    24
REMARK 465     VAL A    25
REMARK 465     VAL A    26
REMARK 465     HIS A    27
REMARK 465     SER A    28
REMARK 465     GLU A    29
REMARK 465     PRO A    30
REMARK 465     SER A    31
REMARK 465     GLN A    32
REMARK 465     GLU A    33
REMARK 465     LYS A   165
REMARK 465     ALA A   166
REMARK 465     ARG A   167
REMARK 465     SER A   168
REMARK 465     ASP A   169
REMARK 465     MET A   170
REMARK 465     THR A   171
REMARK 465     VAL A   172
REMARK 465     GLU A   173
REMARK 465     GLU A   174
REMARK 465     ARG A   175
REMARK 465     ILE A   176
REMARK 465     GLY A   177
REMARK 465     ALA A   178
REMARK 465     ALA A   179
REMARK 465     ASP A   180
REMARK 465     MET B     1
REMARK 465     ASP B     2
REMARK 465     GLU B     3
REMARK 465     SER B     4
REMARK 465     LEU B     5
REMARK 465     GLU B     6
REMARK 465     HIS B     7
REMARK 465     GLN B     8
REMARK 465     THR B     9
REMARK 465     GLN B    10
REMARK 465     THR B    11
REMARK 465     HIS B    12
REMARK 465     ASP B    13
REMARK 465     GLN B    14
REMARK 465     GLU B    15
REMARK 465     SER B    16
REMARK 465     GLU B    17
REMARK 465     ILE B    18
REMARK 465     VAL B    19
REMARK 465     THR B    20
REMARK 465     GLU B    21
REMARK 465     GLY B    22
REMARK 465     SER B    23
REMARK 465     ALA B    24
REMARK 465     VAL B    25
REMARK 465     VAL B    26
REMARK 465     HIS B    27
REMARK 465     SER B    28
REMARK 465     GLU B    29
REMARK 465     PRO B    30
REMARK 465     SER B    31
REMARK 465     GLN B    32
REMARK 465     GLU B    33
REMARK 465     THR B   161
REMARK 465     LYS B   162
REMARK 465     GLU B   163
REMARK 465     GLY B   164
REMARK 465     LYS B   165
REMARK 465     ALA B   166
REMARK 465     ARG B   167
REMARK 465     SER B   168
REMARK 465     ASP B   169
REMARK 465     MET B   170
REMARK 465     THR B   171
REMARK 465     VAL B   172
REMARK 465     GLU B   173
REMARK 465     GLU B   174
REMARK 465     ARG B   175
REMARK 465     ILE B   176
REMARK 465     GLY B   177
REMARK 465     ALA B   178
REMARK 465     ALA B   179
REMARK 465     ASP B   180
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     LYS A  39    CG   CD   CE   NZ
REMARK 470     LYS B  39    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (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,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    SER B  42   N   -  CA  -  C   ANGL. DEV. =  19.2 DEGREES
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    ASN A  35      -16.80   -176.86
REMARK 500    SER A  42      136.60    -31.43
REMARK 500    ASP A  87       88.92   -161.06
REMARK 500    ALA A 131     -116.75   -119.04
REMARK 500    PRO B  37     -176.73    -55.91
REMARK 500    ASP B  41      -78.27    -58.33
REMARK 500    SER B  42     -163.90   -169.78
REMARK 500    GLU B  43       80.78     91.03
REMARK 500    LYS B  66      151.17    -45.68
REMARK 500    GLN B  82       64.34     67.71
REMARK 500    ALA B 114      -19.40    -49.71
REMARK 500    ALA B 131     -124.22   -133.20
REMARK 500    PHE B 140       67.13     33.47
REMARK 500    MET B 146       55.65     38.17
REMARK 500
REMARK 500 REMARK: NULL
DBREF  2F4E A    1   180  GB     30686321 NP_188801        1    180
DBREF  2F4E B    1   180  GB     30686321 NP_188801        1    180
SEQRES   1 A  180  MET ASP GLU SER LEU GLU HIS GLN THR GLN THR HIS ASP
SEQRES   2 A  180  GLN GLU SER GLU ILE VAL THR GLU GLY SER ALA VAL VAL
SEQRES   3 A  180  HIS SER GLU PRO SER GLN GLU GLY ASN VAL PRO PRO LYS
SEQRES   4 A  180  VAL ASP SER GLU ALA GLU VAL LEU ASP GLU LYS VAL SER
SEQRES   5 A  180  LYS GLN ILE ILE LYS GLU GLY HIS GLY SER LYS PRO SER
SEQRES   6 A  180  LYS TYR SER THR CYS PHE LEU HIS TYR ARG ALA TRP THR
SEQRES   7 A  180  LYS ASN SER GLN HIS LYS PHE GLU ASP THR TRP HIS GLU
SEQRES   8 A  180  GLN GLN PRO ILE GLU LEU VAL LEU GLY LYS GLU LYS LYS
SEQRES   9 A  180  GLU LEU ALA GLY LEU ALA ILE GLY VAL ALA SER MET LYS
SEQRES  10 A  180  SER GLY GLU ARG ALA LEU VAL HIS VAL GLY TRP GLU LEU
SEQRES  11 A  180  ALA TYR GLY LYS GLU GLY ASN PHE SER PHE PRO ASN VAL
SEQRES  12 A  180  PRO PRO MET ALA ASP LEU LEU TYR GLU VAL GLU VAL ILE
SEQRES  13 A  180  GLY PHE ASP GLU THR LYS GLU GLY LYS ALA ARG SER ASP
SEQRES  14 A  180  MET THR VAL GLU GLU ARG ILE GLY ALA ALA ASP
SEQRES   1 B  180  MET ASP GLU SER LEU GLU HIS GLN THR GLN THR HIS ASP
SEQRES   2 B  180  GLN GLU SER GLU ILE VAL THR GLU GLY SER ALA VAL VAL
SEQRES   3 B  180  HIS SER GLU PRO SER GLN GLU GLY ASN VAL PRO PRO LYS
SEQRES   4 B  180  VAL ASP SER GLU ALA GLU VAL LEU ASP GLU LYS VAL SER
SEQRES   5 B  180  LYS GLN ILE ILE LYS GLU GLY HIS GLY SER LYS PRO SER
SEQRES   6 B  180  LYS TYR SER THR CYS PHE LEU HIS TYR ARG ALA TRP THR
SEQRES   7 B  180  LYS ASN SER GLN HIS LYS PHE GLU ASP THR TRP HIS GLU
SEQRES   8 B  180  GLN GLN PRO ILE GLU LEU VAL LEU GLY LYS GLU LYS LYS
SEQRES   9 B  180  GLU LEU ALA GLY LEU ALA ILE GLY VAL ALA SER MET LYS
SEQRES  10 B  180  SER GLY GLU ARG ALA LEU VAL HIS VAL GLY TRP GLU LEU
SEQRES  11 B  180  ALA TYR GLY LYS GLU GLY ASN PHE SER PHE PRO ASN VAL
SEQRES  12 B  180  PRO PRO MET ALA ASP LEU LEU TYR GLU VAL GLU VAL ILE
SEQRES  13 B  180  GLY PHE ASP GLU THR LYS GLU GLY LYS ALA ARG SER ASP
SEQRES  14 B  180  MET THR VAL GLU GLU ARG ILE GLY ALA ALA ASP
FORMUL   3  HOH   *46(H2 O)
HELIX    1   1 LYS A  103  GLU A  105  5                                   3
HELIX    2   2 LEU A  106  ALA A  114  1                                   9
HELIX    3   3 TRP A  128  ALA A  131  5                                   4
HELIX    4   4 LYS B  103  GLU B  105  5                                   3
HELIX    5   5 LEU B  106  ALA B  114  1                                   9
HELIX    6   6 TRP B  128  ALA B  131  5                                   4
SHEET    1   A 6 GLU A  45  ASP A  48  0
SHEET    2   A 6 VAL A  51  LYS A  57 -1  O  LYS A  53   N  GLU A  45
SHEET    3   A 6 ARG A 121  VAL A 126 -1  O  ARG A 121   N  ILE A  56
SHEET    4   A 6 LEU A 149  PHE A 158 -1  O  TYR A 151   N  VAL A 124
SHEET    5   A 6 THR A  69  THR A  78 -1  N  PHE A  71   O  GLY A 157
SHEET    6   A 6 LYS A  84  ASP A  87 -1  O  GLU A  86   N  ALA A  76
SHEET    1   B 6 GLU A  45  ASP A  48  0
SHEET    2   B 6 VAL A  51  LYS A  57 -1  O  LYS A  53   N  GLU A  45
SHEET    3   B 6 ARG A 121  VAL A 126 -1  O  ARG A 121   N  ILE A  56
SHEET    4   B 6 LEU A 149  PHE A 158 -1  O  TYR A 151   N  VAL A 124
SHEET    5   B 6 THR A  69  THR A  78 -1  N  PHE A  71   O  GLY A 157
SHEET    6   B 6 ILE A  95  VAL A  98 -1  O  LEU A  97   N  CYS A  70
SHEET    1   C 6 GLU B  45  ASP B  48  0
SHEET    2   C 6 VAL B  51  LYS B  57 -1  O  LYS B  53   N  GLU B  45
SHEET    3   C 6 ARG B 121  VAL B 126 -1  O  ARG B 121   N  ILE B  56
SHEET    4   C 6 LEU B 149  ASP B 159 -1  O  LEU B 149   N  VAL B 126
SHEET    5   C 6 THR B  69  THR B  78 -1  N  PHE B  71   O  GLY B 157
SHEET    6   C 6 LYS B  84  ASP B  87 -1  O  GLU B  86   N  ALA B  76
SHEET    1   D 6 GLU B  45  ASP B  48  0
SHEET    2   D 6 VAL B  51  LYS B  57 -1  O  LYS B  53   N  GLU B  45
SHEET    3   D 6 ARG B 121  VAL B 126 -1  O  ARG B 121   N  ILE B  56
SHEET    4   D 6 LEU B 149  ASP B 159 -1  O  LEU B 149   N  VAL B 126
SHEET    5   D 6 THR B  69  THR B  78 -1  N  PHE B  71   O  GLY B 157
SHEET    6   D 6 ILE B  95  VAL B  98 -1  O  LEU B  97   N  CYS B  70
CISPEP   1 PHE A  140    PRO A  141          0         0.50
CISPEP   2 PHE B  140    PRO B  141          0         0.93
CRYST1   34.980   62.767  122.778  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      0.028590  0.000000  0.000000        0.00000
SCALE2      0.000000  0.015930  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008140        0.00000
      
PROCHECK
Go to PROCHECK summary
 References