BMRB Entry 15172

Title:
1H, 13C and 15N chemical shift assignments for hypothetical protein TA0095 from Thermoplasma acidophilum
Deposition date:
2007-03-12
Original release date:
2007-09-27
Authors:
Jimenez, M. Angeles; Leon, Esther; Santoro, Jorge; Rico, Manuel; Yee, Adelinda
Citation:

Citation: Leon, Esther; Yee, Adelinda; Ortiz, A.R.; Santoro, Jorge; Rico, Manuel; Jimenez, M. Angeles. "Solution structure of the hypothetical protein TA0095 from Thermoplasma acidophilum: A novel superfamily with a 2-layer sandwich architecture"  Protein Sci. 16, 2278-2286 (2007).
PubMed: 17766377

Assembly members:

Assembly members:
H6TA0095, polymer, 118 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Thermoplasma acidophilum   Taxonomy ID: 2303   Superkingdom: Archaea   Kingdom: not available   Genus/species: Thermoplasma acidophilum

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-11b

Data typeCount
13C chemical shifts283
15N chemical shifts109
1H chemical shifts1463

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1H6TA00951

Entities:

Entity 1, H6TA0095 118 residues - Formula weight is not available

1   METGLYTHRSERHISHISHISHISHISHIS
2   SERSERGLYARGGLUASNLEUTYRPHEGLN
3   GLYHISMETARGGLUTYRPROVALLYSLYS
4   GLYPHEPROTHRASPTYRASPSERILELYS
5   ARGLYSILESERGLULEUGLYPHEASPVAL
6   LYSSERGLUGLYASPLEUILEILEALASER
7   ILEPROGLYILESERARGILEGLUILELYS
8   PROASPLYSARGLYSILELEUVALASNTHR
9   GLYASPTYRASPSERASPALAASPLYSLEU
10   ALAVALVALARGTHRTYRASNASPPHEILE
11   GLULYSLEUTHRGLYTYRSERALALYSGLU
12   ARGLYSLYSMETMETTHRLYSASP

Samples:

sample_1: H6TA0095, [U-13C; U-15N], 0.5 mM; sodium chloride 450 mM; sodium phosphate 25 mM; DTT 10 mM; Zn chloride 10 mM; DSS0.1 – 0.5 mM

sample_2: H6TA0095, [U-100% 15N], 1 mM; DSS0.1 – 0.5 mM

sample_3: H6TA0095 1 mM; DSS0.1 – 0.5 mM

sample_4: H6TA0095 1 mM; DSS0.1 – 0.5 mM

sample_conditions_1: ionic strength: 0.5 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.0 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HACANHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
3D 1H-15N NOESYsample_2isotropicsample_conditions_2
3D HNHAsample_2isotropicsample_conditions_2
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
3D 1H-15N TOCSYsample_2isotropicsample_conditions_2
3D 1H-15N NOESYsample_2isotropicsample_conditions_2
2D 1H-1H COSYsample_3isotropicsample_conditions_2
2D 1H-1H TOCSYsample_3isotropicsample_conditions_2
2D 1H-1H NOESYsample_3isotropicsample_conditions_2
2D 1H-1H COSYsample_4isotropicsample_conditions_2
2D 1H-1H TOCSYsample_4isotropicsample_conditions_2
2D 1H-1H NOESYsample_4isotropicsample_conditions_2
2D 1H-13C HSQCsample_4isotropicsample_conditions_2

Software:

SPARKY, Goddard - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

TOPSPIN, Bruker Biospin - processing

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
EMBL CAC11243
REF WP_010900522

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