BMRB Entry 18328

Title:
Solution structure of CHCHD7
Deposition date:
2012-03-14
Original release date:
2012-09-14
Authors:
Winkelmann, Julia; Ciofi-Baffoni, Simone; Banci, Lucia; Bertini, Ivano
Citation:

Citation: Banci, Lucia; Bertini, Ivano; Ciofi-Baffoni, Simone; Jaiswal, Deepa; Neri, Sara; Peruzzini, Riccardo; Winkelmann, Julia. "Structural characterization of CHCHD5 and CHCHD7: two atypical human twin CX9C proteins."  J. Struct. Biol. 180, 190-200 (2012).
PubMed: 22842048

Assembly members:

Assembly members:
entity, polymer, 85 residues, 8598.808 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET16b

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts273
15N chemical shifts74
1H chemical shifts433

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CHCHD71

Entities:

Entity 1, CHCHD7 85 residues - 8598.808 Da.

The first 13 residues are removed from the coordinate file as they are disordered. Two disulfide bonds are present between Cys16 and Cys47, and between Cys26 and Cys37

1   METPROSERVALTHRGLNARGLEUARGASP
2   PROASPILEASNPROCYSLEUSERGLUSER
3   ASPALASERTHRARGCYSLEUASPGLUASN
4   ASNTYRASPARGGLUARGCYSSERTHRTYR
5   PHELEUARGTYRLYSASNCYSARGARGPHE
6   TRPASNSERILEVALMETGLNARGARGLYS
7   ASNGLYVALLYSPROPHEMETPROTHRALA
8   ALAGLUARGASPGLUILELEUARGALAVAL
9   GLYASNMETPROTYR

Samples:

sample_1: CHCHD7, [U-100% 15N], 0.5 – 1 mM; potassium phosphate 50 mM; H2O 90%; D2O 10%

sample_2: CHCHD7, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; potassium phosphate 50 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - data analysis

PECAN, Eghbalnia, Wang, Bahrami, Assadi, and Markley - data analysis

TALOS, Cornilescu, Delaglio and Bax - data analysis

ATNOS, Herrmann, Guntert and Wuthrich - peak picking

CANDID, Herrmann, Guntert and Wuthrich - NOEs assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

XEASY, Bartels et al. - data analysis

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

ProcheckNMR, Laskowski and MacArthur - Structure validation

PSVS, Bhattacharya and Montelione - Structure validation

WhatIF, Vriend - Structure validation

Molmol, Koradi, Billeter and Wuthrich - data analysis

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 500 MHz
  • Bruker Avance 700 MHz

Related Database Links:

PDB
DBJ BAF82777
GB AAH02546 AIC52242 EAW86776 EAW86778 EAW86779
REF NP_001011668 NP_001011671 NP_077276 XP_001151645 XP_002819143
SP Q9BUK0
AlphaFold Q9BUK0

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