BMRB Entry 36075

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR36075
MolProbity Validation Chart

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Title:
The PHD finger of human Kiaa1045 protein
Deposition date:
2017-04-24
Original release date:
2018-04-30
Authors:
Miyamoto, K.
Citation:

Citation: Miyamoto, Kazuhide; Yamashita, Ayumi; Saito, Kazuki. "Solution structure of the PHD finger from the human KIAA1045 protein"  Protein Sci. 27, 987-992 (2018).
PubMed: 29430827

Assembly members:

Assembly members:
PHD finger protein 24, polymer, 60 residues, 6858.710 Da.
ZINC ION, non-polymer, 65.409 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: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PHD finger protein 24: EMCDVCEVWTAESLFPCRVC TRVFHDGCLRRMGYIQGDSA AEVTEMAHTETGWSCHYCDN

Data sets:
Data typeCount
13C chemical shifts246
15N chemical shifts55
1H chemical shifts371

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_ZN_12
3entity_ZN_22

Entities:

Entity 1, entity_1 60 residues - 6858.710 Da.

1   GLUMETCYSASPVALCYSGLUVALTRPTHR
2   ALAGLUSERLEUPHEPROCYSARGVALCYS
3   THRARGVALPHEHISASPGLYCYSLEUARG
4   ARGMETGLYTYRILEGLNGLYASPSERALA
5   ALAGLUVALTHRGLUMETALAHISTHRGLU
6   THRGLYTRPSERCYSHISTYRCYSASPASN

Entity 2, entity_ZN_1 - Zn 2 - 65.409 Da.

1   ZN

Samples:

sample_1: PHD finger, [U-13C; U-15N], 1 mM; Tris-HCl 20 mM; NaCl 50 mM; dithiothreitol 1 mM; ZnCl2 50 uM; H2O 90%; D2O, U-2H, 10%

sample_conditions_1: ionic strength: 70 mM; pH: 6.9; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D NOESYsample_1isotropicsample_conditions_1

Software:

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

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment

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