BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 30514

Title: Human Obscurin Ig57 Domain   PubMed: 30289063

Deposition date: 2018-09-13 Original release date: 2019-02-01

Authors: Wright, N.; Whitley, J.

Citation: Letourneau, Allyn; Wright, Nathan. "Structural Insights on the Obscurin-Binding Domains in Titin."  Protein Pept. Lett. 25, 973-979 (2018).

Assembly members:
entity_1, polymer, 102 residues, 11098.264 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 BL21

Entity Sequences (FASTA):
entity_1: MAPEVTILEPLQDVQLSEGQ DASFQCRLSRASGQEARWAL GGVPLQANEMNDITVEQGTL HLLTLHKVTLEDAGTVSFHV GTCSSEAQLKVTAGLEHHHH HH

Data sets:
Data typeCount
13C chemical shifts315
1H chemical shifts534

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 102 residues - 11098.264 Da.

1   METALAPROGLUVALTHRILELEUGLUPRO
2   LEUGLNASPVALGLNLEUSERGLUGLYGLN
3   ASPALASERPHEGLNCYSARGLEUSERARG
4   ALASERGLYGLNGLUALAARGTRPALALEU
5   GLYGLYVALPROLEUGLNALAASNGLUMET
6   ASNASPILETHRVALGLUGLNGLYTHRLEU
7   HISLEULEUTHRLEUHISLYSVALTHRLEU
8   GLUASPALAGLYTHRVALSERPHEHISVAL
9   GLYTHRCYSSERSERGLUALAGLNLEULYS
10   VALTHRALAGLYLEUGLUHISHISHISHIS
11   HISHIS

Samples:

sample_1: entity_1 mM; TRIS 20 mM; DTT 1 mM; sodium chloride 50 mM

sample_2: entity_1 mM; TRIS 20 mM; DTT 1 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.2; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - peak picking

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

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMR spectrometers:

  • Bruker Avance 600 MHz