BMRB Entry 17047

Title:
Backbone dynamics of Tryptophan repressor A77V mutant protein in holo-form
Deposition date:
2010-07-06
Original release date:
2010-08-09
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:
TrpR_A77V, polymer, 113 residues, Formula weight is not available
TRYPTOPHAN, non-polymer, 204.225 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

Data sets:
Data typeCount
13C chemical shifts187
15N chemical shifts88
1H chemical shifts87
heteronuclear NOE values82
order parameters79
spectral density values82
T1 relaxation values82
T2 relaxation values82

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit1
2L-Tryptophan2

Entities:

Entity 1, subunit 113 residues - Formula weight is not available

1   HISHISHISHISHISHISALAGLNGLNSER
2   PROTYRSERALAALAMETALAGLUGLNARG
3   HISGLNGLUTRPLEUARGPHEVALASPLEU
4   LEULYSASNALATYRGLNASNASPLEUHIS
5   LEUPROLEULEUASNLEUMETLEUTHRPRO
6   ASPGLUARGGLUALALEUGLYTHRARGVAL
7   ARGILEVALGLUGLULEULEUARGGLYGLU
8   METSERGLNARGGLULEULYSASNGLULEU
9   GLYVALGLYILEALATHRILETHRARGGLY
10   SERASNSERLEULYSALAALAPROVALGLU
11   LEUARGGLNTRPLEUGLUGLUVALLEULEU
12   LYSSERASP

Entity 2, L-Tryptophan - C11 H12 N2 O2 - 204.225 Da.

1   TRP

Samples:

sample_CSA: TrpR, [U-100% 13C; U-100% 15N], 1 mM; L-Tryptophan 5 mM; D2O 5%; H2O 95%; PMSF 0.1 mM; sodium azide 0.01%; sodium chloride 500 mM; sodium phosphate 50 mM; EDTA 1 mM

sample_relax: TrpR, [U-100% 13C; U-100% 15N], 1 mM; L-Tryptophan 5 mM; D2O 5%; H2O 95%; PMSF 0.1 mM; sodium azide 0.01%; sodium chloride 500 mM; sodium phosphate 50 mM; EDTA 1 mM

sample_conditions_1: ionic strength: 0.001 M; pH: 5.7; pressure: 1 atm; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_CSAanisotropicsample_conditions_1
3D HNCACBsample_CSAanisotropicsample_conditions_1
3D CBCA(CO)NHsample_CSAanisotropicsample_conditions_1
2D 15N T1sample_relaxanisotropicsample_conditions_1
2D 15N T2 interleavedsample_relaxanisotropicsample_conditions_1
2D 15N {1H} nOesample_relaxanisotropicsample_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 17012 17013 17041 17046 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

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks