BMRB Entry 17047

Name: Backbone dynamics of Tryptophan repressor A77V mutant protein in holo-form
Published: 2010-08-09

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17047

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TrpR_A77V: HHHHHHAQQSPYSAAMAEQR HQEWLRFVDLLKNAYQNDLH LPLLNLMLTPDEREALGTRV RIVEELLRGEMSQRELKNEL GVGIATITRGSNSLKAAPVE LRQWLEEVLLKSD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
heteronucl_NOEs
- heteronuclear_noe_list_1
heteronucl_T1_relaxation
- heteronuclear_T1_list_1
heteronucl_T2_relaxation
- heteronuclear_T2_list_1
order_parameters
- order_parameter_list_1
spectral_density_values
- spectral_density_list_1

Data type	Count
13C chemical shifts	187
15N chemical shifts	88
1H chemical shifts	87
heteronuclear NOE values	82
order parameters	79
spectral density values	82
T1 relaxation values	82
T2 relaxation values	82

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	subunit	1
2	L-Tryptophan	2

Entities:

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

1

HIS

ALA

GLN

SER

2

PRO

TYR

SER

ALA

MET

ALA

GLU

GLN

ARG

3

HIS

GLN

GLU

TRP

LEU

ARG

PHE

VAL

ASP

LEU

4

LEU

LYS

ASN

ALA

TYR

GLN

ASN

ASP

LEU

HIS

5

LEU

PRO

LEU

ASN

LEU

MET

LEU

THR

PRO

6

ASP

GLU

ARG

GLU

ALA

LEU

GLY

THR

ARG

VAL

7

ARG

ILE

VAL

GLU

LEU

ARG

GLY

GLU

8

MET

SER

GLN

ARG

GLU

LEU

LYS

ASN

GLU

LEU

9

GLY

VAL

GLY

ILE

ALA

THR

ILE

THR

ARG

GLY

10

SER

ASN

SER

LEU

LYS

ALA

PRO

VAL

GLU

11

LEU

ARG

GLN

TRP

LEU

GLU

VAL

LEU

12

LYS

SER

ASP

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_CSA	anisotropic	sample_conditions_1
3D HNCACB	sample_CSA	anisotropic	sample_conditions_1
3D CBCA(CO)NH	sample_CSA	anisotropic	sample_conditions_1
2D 15N T1	sample_relax	anisotropic	sample_conditions_1
2D 15N T2 interleaved	sample_relax	anisotropic	sample_conditions_1
2D 15N {1H} nOe	sample_relax	anisotropic	sample_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

BMRB	17010 17012 17013 17041 17046 2040 2042 2043 2074 2173 2209 2764 441 442
PDB	1CO0 1JHG 1MI7 1RCS 1TRO 1TRR 1WRP 1WRS 1WRT 1ZT9 2OZ9 2XDI 3SSW 3SSX 3WRP
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