BMRB Entry 25143

Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25143

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Title:
Solution structure of the RING finger of the tripartite 19 from human.
Deposition date:
2014-08-12
Original release date:
2019-07-11
Authors:
Huang, Shu-Yu; Fan, Pei-Ju; Chang, Chi-Fon; Guntert, Peter; Huang, Tai-Huang
Citation:

Citation: Huang, Shu-Yu; Chang, Chi-Fon; Fang, Pei-Ju; Naik, Mandar; Guntert, Peter; Shih, Hsiu-Ming; Huang, Tai-Huang. "The RING domain of human promyelocytic leukemia protein (PML)."  J. Biomol. NMR 61, 173-180 (2015).
PubMed: 25627356

Assembly members:

Assembly members:
entity_1, polymer, 56 residues, 6113.158 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: recombinant technology   Host organism: Escherichia coli   Vector: pGEX4T-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: EEEFQFLRCQQCQAEAKCPK LLPCLHTLCSGCLEASGMQC PICQAPWPLGADTPAL

Data sets:
Data typeCount
13C chemical shifts176
15N chemical shifts57
1H chemical shifts366

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2ZINC ION_12
3ZINC ION_22

Entities:

Entity 1, entity_1 56 residues - 6113.158 Da.

1   GLUGLUGLUPHEGLNPHELEUARGCYSGLN
2   GLNCYSGLNALAGLUALALYSCYSPROLYS
3   LEULEUPROCYSLEUHISTHRLEUCYSSER
4   GLYCYSLEUGLUALASERGLYMETGLNCYS
5   PROILECYSGLNALAPROTRPPROLEUGLY
6   ALAASPTHRPROALALEU

Entity 2, ZINC ION_1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: entity_1, [U-99% 13C; U-99% 15N], 1 mM; TRIS, [U-99% 2H], 25 mM; sodium chloride 100 mM; TCEP 0.2 mM; zinc chloride 1 mM; D2O 10%; H2O 90%

sample_2: entity_1, [U-99% 13C; U-99% 15N], 1 mM; TRIS, [U-99% 2H], 25 mM; sodium chloride 100 mM; TCEP 0.2 mM; zinc chloride 1 mM; D2O 100%

sample_conditions_1: pH: 7.0; 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 HCCH-TOCSYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1

Software:

CYANA v3.9, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR_NIH v2.26, Schwieters, Kuszewski, Tjandra and Clore - refinement

SPARKY v3.114, Goddard - chemical shift assignment

Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Thornton - data analysis

TALOS v1.2009.0721.18, Cornilescu, Delaglio and Bax - Torsion angles prediction

NMR spectrometers:

  • Bruker Uniform NMR System 600 MHz
  • Bruker Uniform NMR System 800 MHz

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