BMRB Entry 16701

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR16701
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for the C-terminal domain of Stt3p
Deposition date:
2010-02-02
Original release date:
2010-03-26
Authors:
Huang, Chengdong; Mohanty, Smita
Citation:

Citation: Huang, Chengdong; Mohanty, Smita. "Challenging the Limit: NMR Assignment of a 31 kDa Helical Membrane Protein"  J. Am. Chem. Soc. 132, 3662-3663 (2010).
PubMed: 20178386

Assembly members:

Assembly members:
the_C-terminal_domain_of_Stt3p, polymer, 273 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Baker's Yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-28C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
the_C-terminal_domain_of_Stt3p: MGSSHHHHHHSSGLVPRGSH STWVTRTAYSSPSVVLPSQT PDGKLALIDDFREAYYWLRM NSDEDSKVAAWWDYGYQIGG MADRTTLVDNNTWNNTHIAI VGKANASPEEKSYEILKEHD VDYVLVIFGGLIGFGGDDIN KFLWNIRISEGIWPEEIKER DFYTAEGEYRVDARASETMR NSLLYKMSYKDFPQLFNGGQ ATDRVRQQMITPLDVPPLDY FDEVFTSENWNVRIYQLKKD DAQGRTLRDVGELTRSSTKT RRSIKRPELGLRV

Data sets:
Data typeCount
13C chemical shifts714
15N chemical shifts236
1H chemical shifts237

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1the C-terminal domain of Stt3p1

Entities:

Entity 1, the C-terminal domain of Stt3p 273 residues - Formula weight is not available

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   SERTHRTRPVALTHRARGTHRALATYRSER
4   SERPROSERVALVALLEUPROSERGLNTHR
5   PROASPGLYLYSLEUALALEUILEASPASP
6   PHEARGGLUALATYRTYRTRPLEUARGMET
7   ASNSERASPGLUASPSERLYSVALALAALA
8   TRPTRPASPTYRGLYTYRGLNILEGLYGLY
9   METALAASPARGTHRTHRLEUVALASPASN
10   ASNTHRTRPASNASNTHRHISILEALAILE
11   VALGLYLYSALAASNALASERPROGLUGLU
12   LYSSERTYRGLUILELEULYSGLUHISASP
13   VALASPTYRVALLEUVALILEPHEGLYGLY
14   LEUILEGLYPHEGLYGLYASPASPILEASN
15   LYSPHELEUTRPASNILEARGILESERGLU
16   GLYILETRPPROGLUGLUILELYSGLUARG
17   ASPPHETYRTHRALAGLUGLYGLUTYRARG
18   VALASPALAARGALASERGLUTHRMETARG
19   ASNSERLEULEUTYRLYSMETSERTYRLYS
20   ASPPHEPROGLNLEUPHEASNGLYGLYGLN
21   ALATHRASPARGVALARGGLNGLNMETILE
22   THRPROLEUASPVALPROPROLEUASPTYR
23   PHEASPGLUVALPHETHRSERGLUASNTRP
24   ASNVALARGILETYRGLNLEULYSLYSASP
25   ASPALAGLNGLYARGTHRLEUARGASPVAL
26   GLYGLULEUTHRARGSERSERTHRLYSTHR
27   ARGARGSERILELYSARGPROGLULEUGLY
28   LEUARGVAL

Samples:

sample_1: the C-terminal domain of Stt3p, [U-13C; U-15N; U-2H], 600 mM; SDS, [U-2H], 100 mM

sample_conditions_1: ionic strength: 0.02 M; pH: 6.5; pressure: 1 atm; temperature: 328 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Zhengrong and Bax - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Varian INOVA 900 MHz

Related Database Links:

PDB
DBJ BAA06079 GAA23364
EMBL CAA96722 CAY79736
GB AHY79347 AJP38765 AJR76085 AJR76585 AJR77084
REF NP_011493
SP P39007
TPG DAA08076
AlphaFold P39007

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