BMRB Entry 25638

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25638
MolProbity Validation Chart

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Title:
NMR solution structure of a C-terminal domain of the chromodomain helicase DNA-binding protein 1
Deposition date:
2015-05-26
Original release date:
2016-05-31
Authors:
Mohanty, Biswaranjan; Silva, Ana; Mackay, Joel; Ryan, Daniel
Citation:

Citation: Mohanty, Biswaranjan; Silva, Ana; Mackay, Joel; Ryan, Daniel. "1H, 13C and 15N resonance assignments of a C-terminal domain of human CHD1"  Biomol. NMR Assign. 10, 31-34 (2016).
PubMed: 26286320

Assembly members:

Assembly members:
entity, polymer, 108 residues, 12905.072 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: pGEX-6P

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GPLGSLDQKTFSICKERMRP VKAALKQLDRPEKGLSEREQ LEHTRQCLIKIGDHITECLK EYTNPEQIKQWRKNLWIFVS KFTEFDARKLHKLYKHAIKK RQESQQNS

Data sets:
Data typeCount
13C chemical shifts467
15N chemical shifts111
1H chemical shifts747

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 108 residues - 12905.072 Da.

1   GLYPROLEUGLYSERLEUASPGLNLYSTHR
2   PHESERILECYSLYSGLUARGMETARGPRO
3   VALLYSALAALALEULYSGLNLEUASPARG
4   PROGLULYSGLYLEUSERGLUARGGLUGLN
5   LEUGLUHISTHRARGGLNCYSLEUILELYS
6   ILEGLYASPHISILETHRGLUCYSLEULYS
7   GLUTYRTHRASNPROGLUGLNILELYSGLN
8   TRPARGLYSASNLEUTRPILEPHEVALSER
9   LYSPHETHRGLUPHEASPALAARGLYSLEU
10   HISLYSLEUTYRLYSHISALAILELYSLYS
11   ARGGLNGLUSERGLNGLNASNSER

Samples:

sample_1: CHD1-C, [U-98% 13C; U-98% 15N], 440 uM; Sodium phosphate 20 mM; NaCl 10 mM; DTT 1 mM; Sodium Azide 0.3%; DSS 0.3%; 1X protease inhibitor 0.1%; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 10 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - data collection, processing

CARA v1.5.3, Keller and Wuthrich - chemical shift assignment, peak picking

UNIO v2.0.1, Herrmann and Wuthrich - NOE assignment, structure solution

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure calculation

OPALp v1.2, Koradi,Billeter and Guntert - Water refinement

NMR spectrometers:

  • Bruker Avance 800 MHz

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