spacer
spacer

PDBsum entry 1hxv

Go to PDB code: 
Top Page protein links
Chaperone PDB id
1hxv
Jmol
Contents
Protein chain
85 a.a. *
* Residue conservation analysis
HEADER    CHAPERONE                               17-JAN-01   1HXV
TITLE     PPIASE DOMAIN OF THE MYCOPLASMA GENITALIUM TRIGGER FACTOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TRIGGER FACTOR;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PPIASE DOMAIN (RESIDUES 150-250);
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOPLASMA GENITALIUM;
SOURCE   3 ORGANISM_TAXID: 2097;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS    FKBP FOLD, PPIASE, CHAPERONE
EXPDTA    SOLUTION NMR
NUMMDL    12
AUTHOR    M.VOGTHERR,T.N.PARAC,M.MAURER,A.PAHL,K.FIEBIG
REVDAT   3   24-FEB-09 1HXV    1       VERSN
REVDAT   2   01-APR-03 1HXV    1       JRNL
REVDAT   1   29-MAY-02 1HXV    0
JRNL        AUTH   M.VOGTHERR,D.M.JACOBS,T.N.PARAC,M.MAURER,A.PAHL,
JRNL        AUTH 2 K.SAXENA,H.RUTERJANS,C.GRIESINGER,K.M.FIEBIG
JRNL        TITL   NMR SOLUTION STRUCTURE AND DYNAMICS OF THE
JRNL        TITL 2 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE DOMAIN OF THE
JRNL        TITL 3 TRIGGER FACTOR FROM MYCOPLASMA GENITALIUM COMPARED
JRNL        TITL 4 TO FK506-BINDING PROTEIN.
JRNL        REF    J.MOL.BIOL.                   V. 318  1097 2002
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   12054805
JRNL        DOI    10.1016/S0022-2836(02)00112-2
REMARK   1
REMARK   2
REMARK   2 RESOLUTION. NOT APPLICABLE.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : DIPOCOUP 1.0
REMARK   3   AUTHORS     : MEILER
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1HXV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JAN-01.
REMARK 100 THE RCSB ID CODE IS RCSB012669.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210  EXPERIMENT TYPE                : NMR
REMARK 210  TEMPERATURE           (KELVIN) : 298
REMARK 210  PH                             : 6.5
REMARK 210  IONIC STRENGTH                 : 50 MM SODIUM PHOSPHATE
REMARK 210  PRESSURE                       : ATMOSPHERIC ATM
REMARK 210  SAMPLE CONTENTS                : 2 MM U-15N; 2 MM U-15N U-13C;
REMARK 210                                   2 MM UNLABELED
REMARK 210
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 3D_15N-SEPARATED_NOESY, HNHA,
REMARK 210                                   3D_13C-SEPARATED_NOESY, 2D
REMARK 210                                   NOESY
REMARK 210  SPECTROMETER FIELD STRENGTH    : 800 MHZ, 600 MHZ
REMARK 210  SPECTROMETER MODEL             : DRX
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER
REMARK 210
REMARK 210  STRUCTURE DETERMINATION.
REMARK 210   SOFTWARE USED                 : XWINNMR 2.6, XEASY 1.3.14,
REMARK 210                                   CNS 1.0, DIPOCOUP 1.0
REMARK 210   METHOD USED                   : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 160
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 12
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LOWEST
REMARK 210                                   ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: PARTIALLY ALIGNED SAMPLES:  4 % C12E5/N-HEXANOL, RATIO=
REMARK 210  0.96 (RUECKERT AND OTTING, JACS 122, 7793-7797 (2000))
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465   MODELS 1-12
REMARK 465     RES C SSSEQI
REMARK 465     MET A     1
REMARK 465     ARG A     2
REMARK 465     GLY A     3
REMARK 465     SER A     4
REMARK 465     HIS A     5
REMARK 465     HIS A     6
REMARK 465     HIS A     7
REMARK 465     HIS A     8
REMARK 465     HIS A     9
REMARK 465     HIS A    10
REMARK 465     GLY A    11
REMARK 465     SER A    12
REMARK 465     GLU A    13
REMARK 465     LYS A    14
REMARK 465     LEU A    15
REMARK 465     ALA A    16
REMARK 465     LYS A    17
REMARK 465     THR A    18
REMARK 465     LYS A    19
REMARK 465     SER A    20
REMARK 465     THR A    21
REMARK 465     MET A    22
REMARK 465     VAL A    23
REMARK 465     ASP A    24
REMARK 465     VAL A    25
REMARK 465     SER A    26
REMARK 465     ASP A    27
REMARK 465     LYS A    28
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  1 ASN A  32     -175.76    -49.17
REMARK 500  1 ASP A  45       76.18     53.27
REMARK 500  1 ASN A  46      -41.05     85.18
REMARK 500  1 GLN A  55     -137.87    -90.74
REMARK 500  1 ASN A  56       75.60    -59.44
REMARK 500  1 GLU A  58       86.27    -65.98
REMARK 500  1 PHE A  70      -78.45    -80.97
REMARK 500  1 LYS A  78     -157.74    -75.38
REMARK 500  1 LEU A  98       27.32    -79.97
REMARK 500  1 SER A 100       58.07   -141.30
REMARK 500  1 LEU A 109       76.13    -51.25
REMARK 500  2 ALA A  31     -168.44    -78.99
REMARK 500  2 ASN A  32     -174.76    -49.26
REMARK 500  2 ASP A  45       75.18     55.07
REMARK 500  2 ASN A  46      -34.95     86.25
REMARK 500  2 SER A  51      -80.76    -52.17
REMARK 500  2 GLN A  55     -137.55    -91.43
REMARK 500  2 ASN A  56       76.25    -59.36
REMARK 500  2 GLU A  58       85.26    -65.76
REMARK 500  2 PHE A  70      -79.89    -79.24
REMARK 500  2 LYS A  78     -162.90    -72.16
REMARK 500  2 LEU A  98       28.82    -79.85
REMARK 500  2 SER A 100       56.52   -141.35
REMARK 500  2 LEU A 109       76.43    -50.14
REMARK 500  3 ASN A  32     -174.23    -48.96
REMARK 500  3 ASP A  45       78.32     52.94
REMARK 500  3 ASN A  46      -39.56     85.70
REMARK 500  3 SER A  51      -80.95    -52.50
REMARK 500  3 GLN A  55     -135.22    -90.28
REMARK 500  3 ASN A  56       77.08    -59.51
REMARK 500  3 GLU A  58       88.57    -60.14
REMARK 500  3 PHE A  70      -75.93    -81.89
REMARK 500  3 LYS A  78     -157.40    -73.48
REMARK 500  3 SER A 100       54.91   -141.22
REMARK 500  3 LEU A 109       71.48    -51.64
REMARK 500  4 ALA A  31     -169.21    -79.65
REMARK 500  4 ASN A  32     -173.55    -49.75
REMARK 500  4 ASP A  45       76.49     54.58
REMARK 500  4 ASN A  46      -35.41     86.56
REMARK 500  4 SER A  51      -80.16    -50.10
REMARK 500  4 GLN A  55     -136.13    -93.55
REMARK 500  4 ASN A  56       76.01    -59.57
REMARK 500  4 GLU A  58       83.80    -65.72
REMARK 500  4 PHE A  70      -71.37    -80.40
REMARK 500  4 LYS A  78     -164.97    -73.85
REMARK 500  4 LEU A  98       26.25    -79.75
REMARK 500  4 LEU A 109       76.69    -47.66
REMARK 500  5 ALA A  31     -164.21    -79.87
REMARK 500  5 ASN A  32     -171.43    -51.24
REMARK 500  5 ASP A  45       77.26     53.71
REMARK 500  5 ASN A  46      -34.32     88.06
REMARK 500  5 SER A  51      -80.93    -47.10
REMARK 500  5 GLN A  55     -134.70    -93.44
REMARK 500  5 ASN A  56       75.60    -59.72
REMARK 500  5 GLU A  58       87.50    -60.67
REMARK 500  5 PHE A  70      -75.30    -79.09
REMARK 500  5 LYS A  78     -156.90    -78.74
REMARK 500  5 LEU A  98       28.31    -79.55
REMARK 500  5 SER A 100       57.37   -141.31
REMARK 500  5 LEU A 109       76.82    -50.00
REMARK 500  6 ASN A  32     -174.97    -49.45
REMARK 500  6 ASP A  45       77.13     54.27
REMARK 500  6 ASN A  46      -32.47     84.52
REMARK 500  6 SER A  51      -79.26    -47.58
REMARK 500  6 GLN A  55     -142.71    -89.53
REMARK 500  6 ASN A  56       80.39    -59.59
REMARK 500  6 GLU A  58       87.54    -60.15
REMARK 500  6 PHE A  70      -74.81    -75.62
REMARK 500  6 LYS A  78     -158.96    -78.06
REMARK 500  6 PRO A 102       91.53    -69.54
REMARK 500  6 LEU A 109       72.58    -49.16
REMARK 500  7 ALA A  31     -169.10    -78.70
REMARK 500  7 ASN A  32     -174.41    -49.36
REMARK 500  7 ASP A  45       76.55     55.16
REMARK 500  7 ASN A  46      -34.74     83.77
REMARK 500  7 SER A  51      -78.75    -55.30
REMARK 500  7 GLN A  55     -134.63    -90.94
REMARK 500  7 ASN A  56       73.30    -59.62
REMARK 500  7 PHE A  70      -71.82    -78.91
REMARK 500  7 LYS A  78     -163.41    -78.25
REMARK 500  7 SER A 100       59.41   -141.08
REMARK 500  7 LEU A 109       77.62    -48.84
REMARK 500  8 ALA A  31     -169.54    -79.78
REMARK 500  8 ASN A  32     -177.95    -48.19
REMARK 500  8 ASP A  45       77.86     54.79
REMARK 500  8 ASN A  46      -31.70     83.73
REMARK 500  8 SER A  51      -79.51    -49.92
REMARK 500  8 GLN A  55     -139.25    -91.71
REMARK 500  8 ASN A  56       76.00    -59.22
REMARK 500  8 PHE A  70      -81.35    -81.24
REMARK 500  8 LYS A  78     -158.65    -70.96
REMARK 500  8 SER A 100       56.31   -141.32
REMARK 500  8 LEU A 109       74.65    -54.35
REMARK 500  9 ASN A  32     -173.57    -50.10
REMARK 500  9 ASP A  45       78.76     52.79
REMARK 500  9 ASN A  46      -43.66     85.80
REMARK 500  9 GLN A  55     -134.18    -90.97
REMARK 500  9 ASN A  56       73.46    -60.70
REMARK 500  9 GLU A  58       88.87    -59.97
REMARK 500  9 ASN A  64       29.55     43.93
REMARK 500  9 PHE A  70      -82.11    -81.90
REMARK 500  9 LYS A  78     -163.97    -78.47
REMARK 500  9 LEU A  98       28.24    -79.56
REMARK 500  9 SER A 100       57.57   -141.18
REMARK 500  9 LEU A 109       78.68    -43.25
REMARK 500 10 ASN A  32     -176.29    -47.61
REMARK 500 10 ASP A  45       74.56     54.98
REMARK 500 10 ASN A  46      -32.80     88.56
REMARK 500 10 SER A  51      -82.12    -46.85
REMARK 500 10 GLN A  55     -137.43    -90.84
REMARK 500 10 ASN A  56       74.56    -59.57
REMARK 500 10 GLU A  58       87.98    -69.33
REMARK 500 10 PHE A  70      -73.43    -75.50
REMARK 500 10 LYS A  78     -165.13    -76.24
REMARK 500 10 SER A 100       57.26   -141.44
REMARK 500 10 LEU A 109       75.82    -49.80
REMARK 500 11 ASN A  32     -177.57    -46.86
REMARK 500 11 ASP A  45       76.11     54.35
REMARK 500 11 ASN A  46      -35.25     88.42
REMARK 500 11 SER A  51      -80.57    -46.54
REMARK 500 11 GLN A  55     -135.04    -91.66
REMARK 500 11 ASN A  56       75.18    -60.23
REMARK 500 11 GLU A  58       86.73    -59.76
REMARK 500 11 PHE A  70      -76.21    -81.68
REMARK 500 11 LYS A  78     -162.35    -68.86
REMARK 500 11 LEU A 109       77.72    -48.29
REMARK 500 12 ASN A  32     -172.24    -49.76
REMARK 500 12 ASP A  45       76.33     54.30
REMARK 500 12 ASN A  46      -34.99     87.37
REMARK 500 12 SER A  51      -78.15    -48.32
REMARK 500 12 GLN A  55     -133.80    -90.86
REMARK 500 12 ASN A  56       74.28    -60.73
REMARK 500 12 GLU A  58       85.36    -65.94
REMARK 500 12 PHE A  70      -72.31    -78.74
REMARK 500 12 LYS A  78     -155.56    -75.53
REMARK 500 12 LEU A  98       27.55    -78.77
REMARK 500 12 SER A 100       53.08   -141.38
REMARK 500 12 LEU A 109       76.60    -49.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4953   RELATED DB: BMRB
REMARK 900 4953 IS THE BMRB ENTRY CORRESPONDING TO THE NMR DATA FOR
REMARK 900 THIS PROTEIN
DBREF  1HXV A   13   113  UNP    P47480   TIG_MYCGE      150    250
SEQADV 1HXV MET A    1  UNP  P47480              EXPRESSION TAG
SEQADV 1HXV ARG A    2  UNP  P47480              EXPRESSION TAG
SEQADV 1HXV GLY A    3  UNP  P47480              EXPRESSION TAG
SEQADV 1HXV SER A    4  UNP  P47480              EXPRESSION TAG
SEQADV 1HXV HIS A    5  UNP  P47480              EXPRESSION TAG
SEQADV 1HXV HIS A    6  UNP  P47480              EXPRESSION TAG
SEQADV 1HXV HIS A    7  UNP  P47480              EXPRESSION TAG
SEQADV 1HXV HIS A    8  UNP  P47480              EXPRESSION TAG
SEQADV 1HXV HIS A    9  UNP  P47480              EXPRESSION TAG
SEQADV 1HXV HIS A   10  UNP  P47480              EXPRESSION TAG
SEQADV 1HXV GLY A   11  UNP  P47480              EXPRESSION TAG
SEQADV 1HXV SER A   12  UNP  P47480              EXPRESSION TAG
SEQRES   1 A  113  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER GLU
SEQRES   2 A  113  LYS LEU ALA LYS THR LYS SER THR MET VAL ASP VAL SER
SEQRES   3 A  113  ASP LYS LYS LEU ALA ASN GLY ASP ILE ALA ILE ILE ASP
SEQRES   4 A  113  PHE THR GLY ILE VAL ASP ASN LYS LYS LEU ALA SER ALA
SEQRES   5 A  113  SER ALA GLN ASN TYR GLU LEU THR ILE GLY SER ASN SER
SEQRES   6 A  113  PHE ILE LYS GLY PHE GLU THR GLY LEU ILE ALA MET LYS
SEQRES   7 A  113  VAL ASN GLN LYS LYS THR LEU ALA LEU THR PHE PRO SER
SEQRES   8 A  113  ASP TYR HIS VAL LYS GLU LEU GLN SER LYS PRO VAL THR
SEQRES   9 A  113  PHE GLU VAL VAL LEU LYS ALA ILE LYS
HELIX    1   1 GLY A   69  ALA A   76  1                                   8
HELIX    2   2 LYS A   96  SER A  100  5                                   5
SHEET    1   A 4 GLN A  81  LEU A  85  0
SHEET    2   A 4 THR A 104  LEU A 109 -1  N  PHE A 105   O  LEU A  85
SHEET    3   A 4 ASP A  34  VAL A  44 -1  O  ASP A  39   N  VAL A 108
SHEET    4   A 4 LYS A  47  LYS A  48 -1  O  LYS A  47   N  VAL A  44
SHEET    1   B 4 GLN A  81  LEU A  85  0
SHEET    2   B 4 THR A 104  LEU A 109 -1  N  PHE A 105   O  LEU A  85
SHEET    3   B 4 ASP A  34  VAL A  44 -1  O  ASP A  39   N  VAL A 108
SHEET    4   B 4 ASN A  56  ILE A  61 -1  O  TYR A  57   N  ILE A  38
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1
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      1.000000  0.000000  0.000000        0.00000
SCALE2      0.000000  1.000000  0.000000        0.00000
SCALE3      0.000000  0.000000  1.000000        0.00000
      
PROCHECK
Go to PROCHECK summary
 References