BMRB Entry 17365

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17365
MolProbity Validation Chart

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Title:
ASHH2 a CW domain
Deposition date:
2010-12-16
Original release date:
2011-05-02
Authors:
Kristiansen, Per Eugen; Hoppmann, Verena; Thorstensen, Tage; Aalen, Reidunn; Aasland, Rein; Finne, Kenneth; Veiseth, Silje
Citation:

Citation: Hoppmann, Verena; Thorstensen, Tage; Kristiansen, Per Eugen; Veiseth, Silje; Rahman, Mohummad; Finne, Kenneth; Aalen, Reidunn; Aasland, Rein. "The CW domain, a new histone recognition module in chromatin proteins"  EMBO J. 30, 1939-1952 (2011).
PubMed: 21522130

Assembly members:

Assembly members:
entity_1, polymer, 100 residues, 11213.283 Da.
ZN, non-polymer, 65.409 Da.

Natural source:

Natural source:   Common Name: Thale cress   Taxonomy ID: 3702   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Arabidopsis thaliana

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSRRASVGSEFMVVDVTIED SYSTESAWVRCDDCFKWRRI PASVVGSIDESSRWICMNNS DKRFADCSKSQEMSNEEINE ELGIGQDEADAYDCDAAKRG

Data sets:
Data typeCount
13C chemical shifts395
15N chemical shifts109
1H chemical shifts637

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ASHH2 a CW domain1
2ZINC ION2

Entities:

Entity 1, ASHH2 a CW domain 100 residues - 11213.283 Da.

1   GLYSERARGARGALASERVALGLYSERGLU
2   PHEMETVALVALASPVALTHRILEGLUASP
3   SERTYRSERTHRGLUSERALATRPVALARG
4   CYSASPASPCYSPHELYSTRPARGARGILE
5   PROALASERVALVALGLYSERILEASPGLU
6   SERSERARGTRPILECYSMETASNASNSER
7   ASPLYSARGPHEALAASPCYSSERLYSSER
8   GLNGLUMETSERASNGLUGLUILEASNGLU
9   GLULEUGLYILEGLYGLNASPGLUALAASP
10   ALATYRASPCYSASPALAALALYSARGGLY

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: entity_1, [U-98% 13C; U-98% 15N], 0.8 mM; ZINC ION 10 uM; DSS 0.2 mM; DTT 1.0 mM; potassium phosphate 20 mM; potassium chloride 50 mM; D2O 5%; H2O 95%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
1D 1H proton spectrum water suppresion with exitation sculptinsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Herrmann, Guntert and Wuthrich - structure solution

TALOS, Cornilescu, Delaglio and Bax - data analysis

SPARKY, Goddard - chemical shift assignment, data analysis

TOPSPIN, Bruker Biospin - Foruier transform

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
GB AAC34358 ABC69038 ABV68921 AEE35960 AEE35961
REF NP_001077836 NP_177854
SP Q2LAE1
AlphaFold Q2LAE1

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