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PDBsum entry 2if4

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Signaling protein PDB id
2if4
Jmol
Contents
Protein chain
258 a.a.
Waters ×16
HEADER    SIGNALING PROTEIN                       20-SEP-06   2IF4
TITLE     CRYSTAL STRUCTURE OF A MULTI-DOMAIN IMMUNOPHILIN FROM
TITLE    2 ARABIDOPSIS THALIANA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ATFKBP42;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: FKBP-TYPE DOMAIN AND TPR DOMAIN, RESIDUES 1-339;
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: FKBP42, TWD1, UCU2;
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, TPR-LIKE, ALPHA, SIGNALING PROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.GRANZIN,A.ECKHOFF,O.H.WEIERGRAEBER
REVDAT   3   24-FEB-09 2IF4    1       VERSN
REVDAT   2   05-DEC-06 2IF4    1       JRNL
REVDAT   1   31-OCT-06 2IF4    0
JRNL        AUTH   J.GRANZIN,A.ECKHOFF,O.H.WEIERGRABER
JRNL        TITL   CRYSTAL STRUCTURE OF A MULTI-DOMAIN IMMUNOPHILIN
JRNL        TITL 2 FROM ARABIDOPSIS THALIANA: A PARADIGM FOR
JRNL        TITL 3 REGULATION OF PLANT ABC TRANSPORTERS.
JRNL        REF    J.MOL.BIOL.                   V. 364   799 2006
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   17045295
JRNL        DOI    10.1016/J.JMB.2006.09.052
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.85 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) : 2.85
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.0
REMARK   3   NUMBER OF REFLECTIONS             : 9813
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) : 0.290
REMARK   3   FREE R VALUE                     : 0.355
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 969
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            : 2056
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 16
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 88.30
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 63.56
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) : 0.51
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) : 0.008
REMARK   3   BOND ANGLES            (DEGREES) : 1.55
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
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 2IF4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-SEP-06.
REMARK 100 THE RCSB ID CODE IS RCSB039504.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-JUL-04
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.3
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                         : 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)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9813
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.850
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0
REMARK 200  DATA REDUNDANCY                : 3.500
REMARK 200  R MERGE                    (I) : 0.05000
REMARK 200  R SYM                      (I) : 0.05900
REMARK 200   FOR THE DATA SET  : 20.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.92
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60
REMARK 200  R MERGE FOR SHELL          (I) : 0.43000
REMARK 200  R SYM FOR SHELL            (I) : 0.50200
REMARK 200   FOR SHELL         : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 53.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.3 M AMMONIUM SULFATE, 2% (V/V)
REMARK 280  PEG 400, 0.1 M HEPES, PH 7.3, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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       43.07100
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       58.93650
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       43.07100
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       58.93650
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER
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 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     GLY A    34
REMARK 465     TYR A   293
REMARK 465     ALA A   294
REMARK 465     PRO A   295
REMARK 465     ASP A   296
REMARK 465     ASP A   297
REMARK 465     LYS A   298
REMARK 465     ALA A   299
REMARK 465     ILE A   300
REMARK 465     ARG A   301
REMARK 465     ARG A   302
REMARK 465     GLU A   303
REMARK 465     LEU A   304
REMARK 465     ARG A   305
REMARK 465     ALA A   306
REMARK 465     LEU A   307
REMARK 465     ALA A   308
REMARK 465     GLU A   309
REMARK 465     GLN A   310
REMARK 465     GLU A   311
REMARK 465     LYS A   312
REMARK 465     ALA A   313
REMARK 465     LEU A   314
REMARK 465     TYR A   315
REMARK 465     GLN A   316
REMARK 465     LYS A   317
REMARK 465     GLN A   318
REMARK 465     LYS A   319
REMARK 465     GLU A   320
REMARK 465     MET A   321
REMARK 465     TYR A   322
REMARK 465     LYS A   323
REMARK 465     GLY A   324
REMARK 465     ILE A   325
REMARK 465     PHE A   326
REMARK 465     LYS A   327
REMARK 465     GLY A   328
REMARK 465     LYS A   329
REMARK 465     ASP A   330
REMARK 465     GLU A   331
REMARK 465     GLY A   332
REMARK 465     GLY A   333
REMARK 465     ALA A   334
REMARK 465     LYS A   335
REMARK 465     SER A   336
REMARK 465     LYS A   337
REMARK 465     SER A   338
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  37      105.35    -35.66
REMARK 500    LEU A  47       -9.24    -56.55
REMARK 500    ASP A  48      155.96    172.95
REMARK 500    LYS A  66      127.30    -28.20
REMARK 500    TYR A  67       -1.61     85.33
REMARK 500    GLN A  82       46.78     38.19
REMARK 500    ASP A  87       98.97   -171.03
REMARK 500    GLN A  93       93.46   -165.20
REMARK 500    GLU A 102     -156.57    -58.35
REMARK 500    LYS A 104      -72.61    -11.96
REMARK 500    ALA A 114      -29.61    -39.12
REMARK 500    ALA A 131     -156.01   -134.22
REMARK 500    TYR A 132       91.52    -68.17
REMARK 500    LYS A 134      -70.40    170.28
REMARK 500    SER A 139     -116.97   -111.05
REMARK 500    PHE A 140      -80.13     -7.10
REMARK 500    MET A 146       61.90     38.81
REMARK 500    ALA A 166      -72.51    -10.67
REMARK 500    SER A 168      100.50    -42.58
REMARK 500    ASP A 169      -16.43     63.56
REMARK 500    LEU A 189       18.02    -66.67
REMARK 500    LYS A 191      -91.48   -136.20
REMARK 500    LEU A 195      138.13    -31.00
REMARK 500    CYS A 232       -4.08    -51.46
REMARK 500    ALA A 237      -81.64    -62.86
REMARK 500    CYS A 239        2.73    -67.86
REMARK 500    LEU A 257        3.58    -63.93
REMARK 500    GLU A 260       76.20   -164.29
REMARK 500    GLU A 261        5.91    -54.49
REMARK 500    ASN A 263      111.10    -31.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2F4E   RELATED DB: PDB
REMARK 900 N-TERMINAL DOMAIN OF FKBP42 FROM ARABIDOPSIS THALIANA
DBREF  2IF4 A    1   338  UNP    Q9LDC0   FKB42_ARATH      1    338
SEQRES   1 A  338  MET ASP GLU SER LEU GLU HIS GLN THR GLN THR HIS ASP
SEQRES   2 A  338  GLN GLU SER GLU ILE VAL THR GLU GLY SER ALA VAL VAL
SEQRES   3 A  338  HIS SER GLU PRO SER GLN GLU GLY ASN VAL PRO PRO LYS
SEQRES   4 A  338  VAL ASP SER GLU ALA GLU VAL LEU ASP GLU LYS VAL SER
SEQRES   5 A  338  LYS GLN ILE ILE LYS GLU GLY HIS GLY SER LYS PRO SER
SEQRES   6 A  338  LYS TYR SER THR CYS PHE LEU HIS TYR ARG ALA TRP THR
SEQRES   7 A  338  LYS ASN SER GLN HIS LYS PHE GLU ASP THR TRP HIS GLU
SEQRES   8 A  338  GLN GLN PRO ILE GLU LEU VAL LEU GLY LYS GLU LYS LYS
SEQRES   9 A  338  GLU LEU ALA GLY LEU ALA ILE GLY VAL ALA SER MET LYS
SEQRES  10 A  338  SER GLY GLU ARG ALA LEU VAL HIS VAL GLY TRP GLU LEU
SEQRES  11 A  338  ALA TYR GLY LYS GLU GLY ASN PHE SER PHE PRO ASN VAL
SEQRES  12 A  338  PRO PRO MET ALA ASP LEU LEU TYR GLU VAL GLU VAL ILE
SEQRES  13 A  338  GLY PHE ASP GLU THR LYS GLU GLY LYS ALA ARG SER ASP
SEQRES  14 A  338  MET THR VAL GLU GLU ARG ILE GLY ALA ALA ASP ARG ARG
SEQRES  15 A  338  LYS MET ASP GLY ASN SER LEU PHE LYS GLU GLU LYS LEU
SEQRES  16 A  338  GLU GLU ALA MET GLN GLN TYR GLU MET ALA ILE ALA TYR
SEQRES  17 A  338  MET GLY ASP ASP PHE MET PHE GLN LEU TYR GLY LYS TYR
SEQRES  18 A  338  GLN ASP MET ALA LEU ALA VAL LYS ASN PRO CYS HIS LEU
SEQRES  19 A  338  ASN ILE ALA ALA CYS LEU ILE LYS LEU LYS ARG TYR ASP
SEQRES  20 A  338  GLU ALA ILE GLY HIS CYS ASN ILE VAL LEU THR GLU GLU
SEQRES  21 A  338  GLU LYS ASN PRO LYS ALA LEU PHE ARG ARG GLY LYS ALA
SEQRES  22 A  338  LYS ALA GLU LEU GLY GLN MET ASP SER ALA ARG ASP ASP
SEQRES  23 A  338  PHE ARG LYS ALA GLN LYS TYR ALA PRO ASP ASP LYS ALA
SEQRES  24 A  338  ILE ARG ARG GLU LEU ARG ALA LEU ALA GLU GLN GLU LYS
SEQRES  25 A  338  ALA LEU TYR GLN LYS GLN LYS GLU MET TYR LYS GLY ILE
SEQRES  26 A  338  PHE LYS GLY LYS ASP GLU GLY GLY ALA LYS SER LYS SER
FORMUL   2  HOH   *16(H2 O)
HELIX    1   1 THR A   88  GLN A   92  1                                   5
HELIX    2   2 LYS A  103  GLU A  105  5                                   3
HELIX    3   3 LEU A  106  MET A  116  1                                  11
HELIX    4   4 TRP A  128  ALA A  131  5                                   4
HELIX    5   5 THR A  171  LEU A  189  1                                  19
HELIX    6   6 LEU A  195  MET A  209  1                                  15
HELIX    7   7 GLY A  210  GLN A  216  1                                   7
HELIX    8   8 TYR A  218  ASN A  230  1                                  13
HELIX    9   9 ASN A  230  LYS A  242  1                                  13
HELIX   10  10 TYR A  246  GLU A  260  1                                  15
HELIX   11  11 ASN A  263  GLU A  276  1                                  14
HELIX   12  12 GLN A  279  ALA A  290  1                                  12
SHEET    1   A 6 GLU A  45  ASP A  48  0
SHEET    2   A 6 VAL A  51  LYS A  57 -1  O  VAL A  51   N  ASP A  48
SHEET    3   A 6 ARG A 121  VAL A 126 -1  O  ARG A 121   N  LYS A  57
SHEET    4   A 6 LEU A 149  ASP A 159 -1  O  VAL A 153   N  ALA A 122
SHEET    5   A 6 THR A  69  THR A  78 -1  N  THR A  69   O  ASP A 159
SHEET    6   A 6 GLU A  86  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  VAL A  51   N  ASP A  48
SHEET    3   B 6 ARG A 121  VAL A 126 -1  O  ARG A 121   N  LYS A  57
SHEET    4   B 6 LEU A 149  ASP A 159 -1  O  VAL A 153   N  ALA A 122
SHEET    5   B 6 THR A  69  THR A  78 -1  N  THR A  69   O  ASP A 159
SHEET    6   B 6 ILE A  95  VAL A  98 -1  O  LEU A  97   N  CYS A  70
CRYST1   86.142  117.873   40.112  90.00  90.00  90.00 P 21 21 2     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      0.011609  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008484  0.000000        0.00000
SCALE3      0.000000  0.000000  0.024930        0.00000
      
PROCHECK
Go to PROCHECK summary
 References