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

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

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BMRB Entry 26821

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: