BMRB Entry 15646

Title:
NMR analysis of the closed conformation of syntaxin-1
Deposition date:
2008-02-02
Original release date:
2008-02-05
Authors:
Chen, Xiaocheng; Lu, Jun; Dulubova, Irina
Citation:

Citation: Chen, Xiaocheng; Lu, Jun; Dulubova, Irina; Rizo, Josep. "NMR analysis of the closed conformation of syntaxin-1"  J. Biomol. NMR 41, 43-54 (2008).
PubMed: 18458823

Assembly members:

Assembly members:
sx23, polymer, 207 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: PGEX-KT

Data sets:
Data typeCount
13C chemical shifts605
15N chemical shifts151
1H chemical shifts811

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1sx231

Entities:

Entity 1, sx23 207 residues - Formula weight is not available

1   GLYSERARGASPARGPHEMETASPGLUPHE
2   PHEGLUGLNVALGLUGLUILEARGGLYPHE
3   ILEASPLYSILEALAGLUASNVALGLUGLU
4   VALLYSARGLYSHISSERALAILELEUALA
5   SERPROASNPROASPGLULYSTHRLYSGLU
6   GLULEUGLUGLULEUMETSERASPILELYS
7   LYSTHRALAASNLYSVALARGSERLYSLEU
8   LYSSERILEGLUGLNSERILEGLUGLNGLU
9   GLUGLYLEUASNARGSERSERALAASPLEU
10   ARGILEARGLYSTHRGLNHISSERTHRLEU
11   SERARGLYSPHEVALGLUVALMETSERGLU
12   TYRASNALATHRGLNSERASPTYRARGGLU
13   ARGCYSLYSGLYARGILEGLNARGGLNLEU
14   GLUILETHRGLYARGTHRTHRTHRSERGLU
15   GLULEUGLUASPMETLEUGLUSERGLYASN
16   PROALAILEPHEALASERGLYILEILEMET
17   ASPSERSERILESERLYSGLNALALEUSER
18   GLUILEGLUTHRARGHISSERGLUILEILE
19   LYSLEUGLUASNARGLEUARGGLULEUHIS
20   ASPMETPHEMETASPMETALAMETLEUVAL
21   GLUSERGLNGLYGLUMETILE

Samples:

sample_1: sx23, [U-99% 13C; U-99% 15N], 700 uM; sodium phosphate 20 mM

sample_2: sx23, [U-99% 15N], 700 uM; sodium phosphate 20 mM

sample_3: sx23, [U-13C; U-15N; U-2H], 700 uM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 20 mM; pH: 7.4; pressure: 1 atm; temperature: 301 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D DQF-COSYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HN(CO)CAsample_3isotropicsample_conditions_1

Software:

VNMR, Varian - collection

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 4198
PDB
DBJ BAA01231 BAA02089 BAA07151 BAA28865 BAC78519
EMBL CAG33299 CAH93304
GB AAA20940 AAA42195 AAA53519 AAB22525 AAB65500
PIR G01485
PRF 2116295A
REF NP_001028037 NP_001126944 NP_001159375 NP_004594 NP_058081
SP O35526 P32850 P32851 Q16623 Q5R4L2
AlphaFold O35526 P32850 P32851 Q16623 Q5R4L2

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