BMRB Entry 15039

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15039
MolProbity Validation Chart

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Title:
solution structure of ta0956
Deposition date:
2006-11-20
Original release date:
2007-10-16
Authors:
Koo, Bon-Kyung; Jung, Jinwon; Jung, Hyunseob; Nam, Hyung Wook; Kim, Yu Sam; Yee, Adelinda; Arrowsmith, Cheryl; Lee, Weontae
Citation:

Citation: Koo, Bon-Kyung; Jung, Jinwon; Jung, Hyunseob; Nam, Hyung Wook; Kim, Yu Sam; Yee, Adelinda; Lee, Weontae. "Solution structure of the hypothetical novel-fold protein TA0956 from Thermoplasma acidophilum"  Proteins 69, 444-447 (2007).
PubMed: 17634985

Assembly members:

Assembly members:
ta0956, polymer, 110 residues, 12574.589 Da.

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: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ta0956: MTLCAMYNISMAGSHPTTIC VVMDRFLESFSELYDIIDEN DTDVMMDFISRFARTDEIMP EDKTVGFVVVNADKKLMSVS FSDIDENMKKVIKATAEKFK NKGFKVETDM

Data sets:
Data typeCount
13C chemical shifts303
15N chemical shifts110
1H chemical shifts695

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1TA09561

Entities:

Entity 1, TA0956 110 residues - 12574.589 Da.

1   METTHRLEUCYSALAMETTYRASNILESER
2   METALAGLYSERHISPROTHRTHRILECYS
3   VALVALMETASPARGPHELEUGLUSERPHE
4   SERGLULEUTYRASPILEILEASPGLUASN
5   ASPTHRASPVALMETMETASPPHEILESER
6   ARGPHEALAARGTHRASPGLUILEMETPRO
7   GLUASPLYSTHRVALGLYPHEVALVALVAL
8   ASNALAASPLYSLYSLEUMETSERVALSER
9   PHESERASPILEASPGLUASNMETLYSLYS
10   VALILELYSALATHRALAGLULYSPHELYS
11   ASNLYSGLYPHELYSVALGLUTHRASPMET

Samples:

sample_1: ta0956, [U-98% 13C; U-98% 15N], 1.5 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DTT 5 mM; sodium azide 0.01 w/v; DSS 0.01 w/v

sample_2: ta0956, [U-98% 13C; U-98% 15N], 1.5 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DTT 5 mM; sodium azide 0.01 w/v; DSS 0.01 w/v

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

CYANA v2.1, P.GUNTERT ET AL. - refinement

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

xwinnmr, Bruker Biospin - collection

SPARKY, Goddard - peak picking

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker AMX 800 MHz

Related Database Links:

BMRB 15688
PDB
EMBL CAC12085
REF WP_010901367

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