BMRB Entry 26821

Name: apoTrpR
Published: 2016-07-20

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PDB ID: 5tm0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26821
MolProbity Validation Chart

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

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Title:

apoTrpR

Deposition date:

2016-06-20

Original release date:

2016-07-20

Authors:

Gurla, Swapna; Montelione, Gaetano; Balasubramanian, Harish; Carey, Jannette; Kornhaber, Gregory; NESG, NE Struct. Genomics Consortium

Citation:

Citation: Harish, Balasubramanian; Swapna, G.; Kornhaber, Gregory; Montelione, Gaetano; Carey, Jannette. "Multiple helical conformations of the helix-turn-helix region revealed by NOE-restrained MD simulations of tryptophan aporepressor, TrpR" Proteins 85, 731-740 (2017).
PubMed: 28120439

Assembly members:

Assembly members:
apo_TrpR, polymer, 108 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15 T7

Entity Sequences (FASTA):

Entity Sequences (FASTA):
apo_TrpR: MAQQSPYSAAMAEQRHQEWL RFVDLLKNAYQNDLHLPLLN LMLTPDEREALGTRVRIVEE LLRGEMSQRELKNELGAGIA TITRGSNSLKAAPVELRQWL EEVLLKSD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	218
15N chemical shifts	90
1H chemical shifts	417

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TrpR, sununit 1	1

Entities:

Entity 1, TrpR, sununit 1 108 residues - Formula weight is not available

1

MET

ALA

GLN

SER

PRO

TYR

SER

ALA

2

MET

ALA

GLU

GLN

ARG

HIS

GLN

GLU

TRP

LEU

3

ARG

PHE

VAL

ASP

LEU

LYS

ASN

ALA

TYR

4

GLN

ASN

ASP

LEU

HIS

LEU

PRO

LEU

ASN

5

LEU

MET

LEU

THR

PRO

ASP

GLU

ARG

GLU

ALA

6

LEU

GLY

THR

ARG

VAL

ARG

ILE

VAL

GLU

7

LEU

ARG

GLY

GLU

MET

SER

GLN

ARG

GLU

8

LEU

LYS

ASN

GLU

LEU

GLY

ALA

GLY

ILE

ALA

9

THR

ILE

THR

ARG

GLY

SER

ASN

SER

LEU

LYS

10

ALA

PRO

VAL

GLU

LEU

ARG

GLN

TRP

LEU

11

GLU

VAL

LEU

LYS

SER

ASP

Samples:

sample_1: apo TrpR, [U-100% 13C; U-100% 15N], 0.5 mM; Tris-HCl buffer 10 mM; NaCl 100 mM; DTT 5 mM; NaN3 0.02%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 5.7; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

AutoAssign v2.1.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

TOPSPIN v2.3, Bruker Biospin - collection

NMRPipe v2.1, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.0, Goddard - data analysis, peak picking

NMR spectrometers:

Bruker Avance 800 MHz

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