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 19229

Title: PHD Domain from Human SHPRH   PubMed: 23907177

Deposition date: 2013-05-07 Original release date: 2013-08-12

Authors: Machado, Luciana; Pustovalova, Yulia; Pozhidaeva, Alexandra; Almeida, Fabio; Bezsonova, Irina; Korzhnev, Dmitry

Citation: Machado, Luciana; Pustovalova, Yulia; Kile, Andrew; Pozhidaeva, Alexandra; Cimprich, Karlene; Almeida, Fabio; Bezsonova, Irina; Korzhnev, Dmitry. "PHD domain from human SHPRH."  J. Biomol. NMR 56, 393-399 (2013).

Assembly members:
SHPRH, polymer, 73 residues, 7776.120 Da.
ZINC ION, non-polymer, 65.409 Da.

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

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

Entity Sequences (FASTA):
SHPRH: GSPNSRVDFNTSDYRFECIC GELDQIDRKPRVQCLKCHLW QHAKCVNYDEKNLKIKPFYC PHCLVAMEPVSTR

Data sets:
Data typeCount
13C chemical shifts285
15N chemical shifts68
1H chemical shifts467

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SHPRH1
2ZINC ION_12
3ZINC ION_22

Entities:

Entity 1, SHPRH 73 residues - 7776.120 Da.

1   GLYSERPROASNSERARGVALASPPHEASN
2   THRSERASPTYRARGPHEGLUCYSILECYS
3   GLYGLULEUASPGLNILEASPARGLYSPRO
4   ARGVALGLNCYSLEULYSCYSHISLEUTRP
5   GLNHISALALYSCYSVALASNTYRASPGLU
6   LYSASNLEULYSILELYSPROPHETYRCYS
7   PROHISCYSLEUVALALAMETGLUPROVAL
8   SERTHRARG

Entity 2, ZINC ION_1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: HEPES, [U-100% 13C; U-100% 15N], 50 mM; sodium chloride 150 mM; ZINC ION 0.05 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1

Software:

CARA v1.8, Keller and Wuthrich - chemical shift assignment, peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TALOS v2.2, Cornilescu, Delaglio and Bax - prediction of backbone torsion angles

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

ABACUS v2.5, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization

Molmol v2K.2, Koradi, Billeter and Wuthrich - data analysis

CNS v2.5, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization

NMR spectrometers:

  • Varian Avance 500 MHz
  • Varian Avance 800 MHz

Related Database Links:

PDB
REF XP_002747128 XP_010335830 XP_010335831 XP_012308223 XP_012308230

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