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 34330

Title: Solution structure of TRIM28 RING domain

Deposition date: 2018-11-23 Original release date: 2019-04-24

Authors: Stevens, R.; Esposito, D.; Rittinger, K.

Citation: Stevens, R.; Esposito, D.; Rittinger, K.. "Solution structure of TRIM28 RING domain"  . ., .-..

Assembly members:
entity_1, polymer, 94 residues, 9674.865 Da.
entity_ZN, 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):
entity_1: GPGGAEALELLEHCGVCRER LRPEREPRLLPCLHSACSAC LGPAAPAAANSSGDGGAAGD GTVVDCPVCKQQCFSKDIVE NYFMRDSGSKAATD

Data sets:
Data typeCount
13C chemical shifts369
15N chemical shifts90
1H chemical shifts579

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_2, 12
3entity_2, 22

Entities:

Entity 1, entity_1 94 residues - 9674.865 Da.

1   GLYPROGLYGLYALAGLUALALEUGLULEU
2   LEUGLUHISCYSGLYVALCYSARGGLUARG
3   LEUARGPROGLUARGGLUPROARGLEULEU
4   PROCYSLEUHISSERALACYSSERALACYS
5   LEUGLYPROALAALAPROALAALAALAASN
6   SERSERGLYASPGLYGLYALAALAGLYASP
7   GLYTHRVALVALASPCYSPROVALCYSLYS
8   GLNGLNCYSPHESERLYSASPILEVALGLU
9   ASNTYRPHEMETARGASPSERGLYSERLYS
10   ALAALATHRASP

Entity 2, entity_2, 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: TRIM28 RING, [U-15N], 1 mM; MES 20 mM; NaCl 100 mM; TCEP 0.5 mM

sample_2: TRIM28 RING, [U-13C; U-15N], 1 mM; MES 20 mM; NaCl 100 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.2; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 100 mM; pH: 6.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_2isotropicsample_conditions_2
3D HN(CO)CAsample_2isotropicsample_conditions_2
3D CBCA(CO)NHsample_2isotropicsample_conditions_2
3D HNCACBsample_2isotropicsample_conditions_2
3D HNCOsample_2isotropicsample_conditions_2
3D 1H-13C NOESYsample_2isotropicsample_conditions_2
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_2
3D HN(CA)COsample_2isotropicsample_conditions_2
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_2
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_2

Software:

CcpNMR, CCPN - chemical shift assignment

ARIA, Linge, O'Donoghue and Nilges - structure calculation

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Bruker AvanceIII 700 MHz
  • Bruker AvanceIII 800 MHz
  • Bruker A 950 MHz

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