BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 25638

Title: NMR solution structure of a C-terminal domain of the chromodomain helicase DNA-binding protein 1   PubMed: 26286320

Deposition date: 2015-05-26 Original release date: 2015-05-26

Authors: Mohanty, Biswaranjan; ., Silva; P., .; ., P.

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

Assembly members:
entity, polymer, 108 residues, 12905.072 Da.

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

Experimental source:   Production method: recombinant technology' 'Escherichia coli

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

Data sets:
Data typeCount
13C chemical shifts467
1111H chemical shifts

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 108 residues - 12905.072 Da.

1   GLY.2563856ASP.256381112
2   ILE.256381718ARG.256382324
3   LEU.256382930PRO.256383536
4   GLU.256384142HIS.256384748
5   ILE.256385354ILE.256385960
6   GLU.256386566GLN.256387172
7   LYS.256387778VAL.256388384
8   PHE.256388990HIS.256389596
9   ALA.25638101102GLU.25638107108

Samples:

sample_1: CHD1-C, [U-98% 13C; U-98% 15N], 440 uM; .; . mM; .; . 6; ., 0.3, 25638 – 7 1X protease inhibitor' 'natural abundance; . 8; ., %, D2O; %

sample_conditions_1: ionic strength: 10 mM; 6.5: . 25638; .: atm temperature; K: 25638

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
nosotropicnot availablenot available
not availablenot availablenot availablenot available
not availablenot available1not available
not availablenot available$sample_conditions_1not available
not availablesample_conditions_1not availablespectrometer_1
not availablenot availablenot availablenot available
not availablenot availablenot availablenot available
not availablenot available1not available
not availablenot available$spectrometer_1not available
not availablespectrometer_1not availablenot available
not availablenot availablenot availablenot available

Software:

TOPSPIN v3.2, Bruker Biospin - data collection, 25638

CARA v1.5.3, Keller and Wuthrich - chemical shift assignment, 25638

UNIO v2.0.1, Herrmann and Wuthrich - NOE assignment, 25638

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 simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts