BMRB Entry 19741

Name: NMR structure of p75 transmembrane domain C257A mutant in DPC micelles
Published: 2015-01-26

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PDB ID: 2mjo
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19741
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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:

NMR structure of p75 transmembrane domain C257A mutant in DPC micelles

Deposition date:

2014-01-20

Original release date:

2015-01-26

Authors:

Nadezhdin, Kirill; Arseniev, Alexander; Goncharuk, Sergey; Mineev, Konstantin

Citation:

Citation: Nadezhdin, Kirill; Arseniev, Alexander; Goncharuk, Sergey; Mineev, Konstantin; Vilar, Mar al; Garc a-Carpio, Irmina; Fernandez, Eva. "Structure of dimeric p75 neurotrophin receptor transmembrane domain provides insight on neurotrophin signaling" .

Assembly members:

Assembly members:
entity, polymer, 41 residues, 4530.318 Da.

Natural source:

Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus

Experimental source:

Experimental source: Production method: cell free synthesis Host organism: E. coli - cell free Vector: pGEMEX-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MTRGTTDNLIPVYASILAAV VVGLVAYIAFKRWNSSKQNK Q

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	125
15N chemical shifts	42
1H chemical shifts	280

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	p75-TM-C257A, 1	1
2	p75-TM-C257A, 2	1

Entities:

Entity 1, p75-TM-C257A, 1 41 residues - 4530.318 Da.

1

MET

THR

ARG

GLY

THR

ASP

ASN

LEU

ILE

2

PRO

VAL

TYR

ALA

SER

ILE

LEU

ALA

VAL

3

VAL

GLY

LEU

VAL

ALA

TYR

ILE

ALA

PHE

4

LYS

ARG

TRP

ASN

SER

LYS

GLN

ASN

LYS

5

GLN

Samples:

sample_1: p75-TM-C257A, [U-100% 13C; U-100% 15N], 1.5 mM; DPC, [U-98% 2H], 30 mM; sodium phosphate 20 mM

sample_conditions_1: pH: 5.9; pressure: 1 atm; temperature: 318 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 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, data analysis, processing

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

TALOS-N, Yang Shen, and Ad Bax - angles constrains prediction

CARA, Keller, R - chemical shift assignment, data analysis, peak picking

Molmol, Koradi, Billeter and Wuthrich - structure visualization

qMDD, Mayzel M, Orekhov V. - processing

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 600 MHz