BMRB Entry 17298

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17298
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:
Resonance assignments of protein SSO1118 from hyperthermophilic archaeon Sulfolobus solfataricus P2
Deposition date:
2010-11-15
Original release date:
2011-01-18
Authors:
Feng, Yingang
Citation:

Citation: Xuan, Jinsong; Song, Xiaxia; Wang, Jinfeng; Feng, Yingang. "Resonance assignments of a putative PilT N-terminus domain protein SSO1118 from hyperthermophilic archaeon Sulfolobus solfataricus P2."  Biomol. NMR Assignments 5, 161-164 (2011).
PubMed: 21229398

Assembly members:

Assembly members:
sso1118, polymer, 119 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: crenarchaeotes   Taxonomy ID: 273057   Superkingdom: Archaea   Kingdom: not available   Genus/species: Sulfolobus Sulfolobus solfataricus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET30a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
sso1118: MFAVISPSAFGKLKEILGSN KNYKFVITTLGVSFAIKSGI DIDSALDRGVIVRAFSHKPP KVGNLPQYESEAIMVAFELN ALLIAEDKDVINKAKELGVN AIPIEELLASSLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts510
15N chemical shifts113
1H chemical shifts826

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1sso11181

Entities:

Entity 1, sso1118 119 residues - Formula weight is not available

1   METPHEALAVALILESERPROSERALAPHE
2   GLYLYSLEULYSGLUILELEUGLYSERASN
3   LYSASNTYRLYSPHEVALILETHRTHRLEU
4   GLYVALSERPHEALAILELYSSERGLYILE
5   ASPILEASPSERALALEUASPARGGLYVAL
6   ILEVALARGALAPHESERHISLYSPROPRO
7   LYSVALGLYASNLEUPROGLNTYRGLUSER
8   GLUALAILEMETVALALAPHEGLULEUASN
9   ALALEULEUILEALAGLUASPLYSASPVAL
10   ILEASNLYSALALYSGLULEUGLYVALASN
11   ALAILEPROILEGLUGLULEULEUALASER
12   SERLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: sso1118 0.8 ± 0.1 mM; potassium phosphate 50 mM; DSS 0.02%; sodium azide 0.02%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CBCA)(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CBCA)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESY-HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESY-HSQC for aliphatic regionsample_1isotropicsample_conditions_1
3D 1H-13C NOESY-HSQC for aromatic regionsample_1isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

FELIX, Accelrys Software Inc. - chemical shift assignment, processing

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

PDB
GB AAK41375 ACX92298 AKA74318 AKA77014 AKA79706
REF WP_009989751

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