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 11122

Title: The solution structure of the tetratrico peptide repeat of human Smooth muscle cell associated protein-1, isoform 2

Deposition date: 2010-03-31 Original release date: 2011-04-01

Authors: Tochio, N.; Sasagawa, A.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation: Tochio, N.; Sasagawa, A.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "The solution structure of the tetratrico peptide repeat of human Smooth muscle cell associated protein-1, isoform 2"  .

Assembly members:
TPR, Residues 8-142, polymer, 148 residues, Formula weight is not available

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P050302-63

Entity Sequences (FASTA):
TPR, Residues 8-142: GSSGSSGMTVSGPGTPEPRP ATPGASSVEQLRKEGNELFK CGDYGGALAAYTQALGLDAT PQDQAVLHRNRAACHLKLED YDKAETEASKAIEKDGGDVK ALYRRSQALEKLGRLDQAVL DLQRCVSLEPKNKVFQEALR NISGPSSG

Data sets:
Data typeCount
13C chemical shifts585
15N chemical shifts144
1H chemical shifts920

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TPR, Residues 8-1421

Entities:

Entity 1, TPR, Residues 8-142 148 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYMETTHRVAL
2   SERGLYPROGLYTHRPROGLUPROARGPRO
3   ALATHRPROGLYALASERSERVALGLUGLN
4   LEUARGLYSGLUGLYASNGLULEUPHELYS
5   CYSGLYASPTYRGLYGLYALALEUALAALA
6   TYRTHRGLNALALEUGLYLEUASPALATHR
7   PROGLNASPGLNALAVALLEUHISARGASN
8   ARGALAALACYSHISLEULYSLEUGLUASP
9   TYRASPLYSALAGLUTHRGLUALASERLYS
10   ALAILEGLULYSASPGLYGLYASPVALLYS
11   ALALEUTYRARGARGSERGLNALALEUGLU
12   LYSLEUGLYARGLEUASPGLNALAVALLEU
13   ASPLEUGLNARGCYSVALSERLEUGLUPRO
14   LYSASNLYSVALPHEGLNGLUALALEUARG
15   ASNILESERGLYPROSERSERGLY

Samples:

sample_1: TPRx3 domain, [U-13C; U-15N], 1.3 mM; d-Tris HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1isotropiccondition_1
3D 13C-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.932, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - structure solution

NMR spectrometers:

  • Bruker AVANCE 900 MHz

Related Database Links:

PDB
DBJ BAB20266 BAB20273 BAF84311 BAG54239 BAG57020
EMBL CAH91170
GB AAH06214 AAH37992 AAH45635 ABM83879 ABM87199
REF NP_001034764 NP_001127383 NP_061141 XP_003268606 XP_003807756
SP Q5RAP0 Q9H3U1
AlphaFold Q5RAP0 Q9H3U1

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