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 17199

Title: Solution structure of Rap1-Taz1 fusion protein   PubMed: 21217703

Deposition date: 2010-09-19 Original release date: 2011-03-30

Authors: Zhou, Zi-ren; Wang, Feng; Chen, Yong; Lei, Ming; Hu, Hong-yu

Citation: Chen, Yong; Rai, Rekha; Zhou, Zi-Ren; Kanoh, Junko; Ribeyre, Cyril; Yang, Yuting; Zheng, Hong; Damay, Pascal; Wang, Feng; Tsujii, Hisayo; Hiraoka, Yasushi; Shore, David; Hu, Hong-Yu; Chang, Sandy; Lei, Ming. "A conserved motif within RAP1 has diversified roles in telomere protection and regulation in different organisms."  Nat. Struct. Mol. Biol. 18, 213-221 (2011).

Assembly members:
spRT6, polymer, 104 residues, 11117.421 Da.

Natural source:   Common Name: fission   Taxonomy ID: 4896   Superkingdom: not available   Kingdom: Eukaryota   Genus/species: Fungi Schizosaccharomyces

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

Entity Sequences (FASTA):
spRT6: SVSILRSSVNHREVDEAIDN ILRYTNSTEQQFLEAMESTG GRVRIAIAKLLSKQTSGGSG GSKLGGSGGSRKDLSVKGML YDSDSQQILNRLRERVSGST AQSA

Data sets:
Data typeCount
13C chemical shifts380
15N chemical shifts88
1H chemical shifts535

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1spRT61

Entities:

Entity 1, spRT6 104 residues - 11117.421 Da.

1   SERVALSERILELEUARGSERSERVALASN
2   HISARGGLUVALASPGLUALAILEASPASN
3   ILELEUARGTYRTHRASNSERTHRGLUGLN
4   GLNPHELEUGLUALAMETGLUSERTHRGLY
5   GLYARGVALARGILEALAILEALALYSLEU
6   LEUSERLYSGLNTHRSERGLYGLYSERGLY
7   GLYSERLYSLEUGLYGLYSERGLYGLYSER
8   ARGLYSASPLEUSERVALLYSGLYMETLEU
9   TYRASPSERASPSERGLNGLNILELEUASN
10   ARGLEUARGGLUARGVALSERGLYSERTHR
11   ALAGLNSERALA

Samples:

sample_1: spRT6, [U-99% 13C; U-99% 15N], 1.1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_2: spRT6, [U-99% 15N], 0.6 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 0.07 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
2D 1H-15N IPAP HSQCsample_2isotropicsample_conditions_1
3D CCH-COSYsample_1isotropicsample_conditions_1

Software:

AMBER v9, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAB70735
EMBL CAC39280
GB AAK57740
PIR T39684
REF NP_596285
SP Q96TL7

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