BMRB Entry 18318

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18318
MolProbity Validation Chart

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Title:
Solution structure of CHCH5
Deposition date:
2012-03-09
Original release date:
2012-09-14
Authors:
Peruzzini, Riccardo; 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, 113 residues, 9607.965 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: pET15

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GSHMQAALEVTARYCGRELE QYGQCVAAKPESWQRDCHYL KMSIAQCTSSHPIIRQIRQA CAQPFEAFEECLRQNEAAVG NCAEHMRRFLQCAEQVQPPR SPATVEAQPLPAS

Data sets:
Data typeCount
13C chemical shifts264
15N chemical shifts73
1H chemical shifts323

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CHCH51

Entities:

Entity 1, CHCH5 113 residues - 9607.965 Da.

no

1   GLYSERHISMETGLNALAALALEUGLUVAL
2   THRALAARGTYRCYSGLYARGGLULEUGLU
3   GLNTYRGLYGLNCYSVALALAALALYSPRO
4   GLUSERTRPGLNARGASPCYSHISTYRLEU
5   LYSMETSERILEALAGLNCYSTHRSERSER
6   HISPROILEILEARGGLNILEARGGLNALA
7   CYSALAGLNPROPHEGLUALAPHEGLUGLU
8   CYSLEUARGGLNASNGLUALAALAVALGLY
9   ASNCYSALAGLUHISMETARGARGPHELEU
10   GLNCYSALAGLUGLNVALGLNPROPROARG
11   SERPROALATHRVALGLUALAGLNPROLEU
12   PROALASER

Samples:

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

sample_2: entity, [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: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_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

CANDID, Herrmann, Guntert and Wuthrich - chemical shift assignment

ATNOS, Herrmann, Guntert and Wuthrich - peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

WhatIF, Vriend - data analysis

ProcheckNMR, Laskowski and MacArthur - data analysis

PSVS, Bhattacharya and Montelione - data analysis

Molmol, Koradi, Billeter and Wuthrich - data analysis

NMR spectrometers:

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

Related Database Links:

PDB
DBJ BAC04922 BAG35152
GB AAH04498 AAX82000 AIC52539 EAW73594 EAW73595
REF NP_001291282 NP_001291283 NP_115685 XP_002811830 XP_003277729
SP Q9BSY4
AlphaFold Q9BSY4

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