BMRB Entry 19741

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

Experimental source:

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

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:
Data typeCount
13C chemical shifts125
15N chemical shifts42
1H chemical shifts280

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1p75-TM-C257A, 11
2p75-TM-C257A, 21

Entities:

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

1   METTHRARGGLYTHRTHRASPASNLEUILE
2   PROVALTYRALASERILELEUALAALAVAL
3   VALVALGLYLEUVALALATYRILEALAPHE
4   LYSARGTRPASNSERSERLYSGLNASNLYS
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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_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

Related Database Links:

BMRB 19673
PDB

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