BMRB Entry 17012

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17012

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Title:
Backbone Amide relaxation parameters for mutant L75F Tryptophan Repressor
Deposition date:
2010-06-21
Original release date:
2010-07-09
Authors:
Goel, Anupam
Citation:

Citation: Goel, Anupam; Tripet, Brian; Tyler, Robert; Nebert, Lucas; Copie, Valerie. "Backbone Amide Dynamics Studies of Apo-L75F-TrpR, a Temperature-Sensitive Mutant of the Tryptophan Repressor Protein (TrpR): Comparison with the (15)N NMR Relaxation Profiles of Wild-Type and A77V Mutant Apo-TrpR Repressors."  Biochemistry 49, 8006-8019 (2010).
PubMed: 20718459

Assembly members:

Assembly members:
apo-L75F-TrpR, polymer, 108 residues, 12389.1 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pJPR2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
apo-L75F-TrpR: MAQQSPYSAAMAEQRHQEWL RFVDLLKNAYQNDLHLPLLN LMLTPDEREALGTRVRIVEE LLRGEMSQRELKNEFGAGIA TITRGSNSLKAAPVELRQWL EEVLLKSD

Data sets:
Data typeCount
heteronuclear NOE values92
order parameters88
spectral density values92
T1 relaxation values92
T2 relaxation values92

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Tryptophan apo-repressor, chain 11
2Tryptophan apo-repressor, chain 21

Entities:

Entity 1, Tryptophan apo-repressor, chain 1 108 residues - 12389.1 Da.

sample studied as a homodimer. sequence provided is for one protomer.

1   METALAGLNGLNSERPROTYRSERALAALA
2   METALAGLUGLNARGHISGLNGLUTRPLEU
3   ARGPHEVALASPLEULEULYSASNALATYR
4   GLNASNASPLEUHISLEUPROLEULEUASN
5   LEUMETLEUTHRPROASPGLUARGGLUALA
6   LEUGLYTHRARGVALARGILEVALGLUGLU
7   LEULEUARGGLYGLUMETSERGLNARGGLU
8   LEULYSASNGLUPHEGLYALAGLYILEALA
9   THRILETHRARGGLYSERASNSERLEULYS
10   ALAALAPROVALGLULEUARGGLNTRPLEU
11   GLUGLUVALLEULEULYSSERASP

Samples:

sample_1: H2O 95%; D2O, [U-100% 2H], 5%; PMSF 0.1 mM; sodium phosphate 50 mM; sodium azide 0.01%; sodium chloride 500 mM; EDTA 1 mM; apo-L75F-TrpR, [U-100% 13C; U-100% 15N], 1 mM

sample_conditions_1: ionic strength: 1 M; pH: 5.7; pressure: 1 atm; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1anisotropicsample_conditions_1
2D 15N T1sample_1anisotropicsample_conditions_1
2D 15N T2 interleavedsample_1anisotropicsample_conditions_1
2D 15N {1H} nOesample_1anisotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis, processing

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

ModelFree, Palmer - data analysis, geometry optimization, refinement

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

BMRB 17010 17013 17041 17046 17047 2040 2042 2043 2074 2173 2209 2764 441 442
PDB
DBJ BAB38774 BAE78382 BAG80193 BAI28718 BAI33927
EMBL CAP78881 CAQ34751 CAQ91905 CAR01357 CAR06215
GB AAA72140 AAA97289 AAC77346 AAG59573 AAN45839
REF NP_313378 NP_418810 NP_710132 WP_000068670 WP_000068671
SP A1AJW2 A7ZVT5 A8A8C2 B1IS26 B1LEK0
AlphaFold A1AJW2 A7ZVT5 A8A8C2 B1IS26 B1LEK0