BMRB Entry 12024

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR12024

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Title:
Resonance assignments of a cellulosomal double-dockerin from Clostridium thermocellum
Deposition date:
2018-09-28
Original release date:
2018-12-11
Authors:
Chen, Chao; Yang, Hongwu; Cui, Qiu; Feng, Yingang
Citation:

Citation: Chen, Chao; Yang, Hongwu; Xuan, Jinsong; Cui, Qiu; Feng, Yingang. "Resonance assignments of a cellulosomal double-dockerin from Clostridium thermocellum."  Biomol. NMR Assign. ., .-. (2018).
PubMed: 30377946

Assembly members:

Assembly members:
dDoc_0689, polymer, 151 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Clostridium thermocellum   Taxonomy ID: 1515   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Hungateiclostridium thermocellum

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
dDoc_0689: MSVKIGDIDGNGEISSIDYA ILKSHLINSNLTFKQLAAAD VDGNGYVNSIDLAILQMYLL GKGGTSDIGKNRIYTYGDID NNGIVDENDYILICNHINGT GQLSDASLFAADADGNNVID QTDRILIEKYITGRITHLPV GNQLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts615
15N chemical shifts163
1H chemical shifts1008

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1protein1

Entities:

Entity 1, protein 151 residues - Formula weight is not available

1   METSERVALLYSILEGLYASPILEASPGLY
2   ASNGLYGLUILESERSERILEASPTYRALA
3   ILELEULYSSERHISLEUILEASNSERASN
4   LEUTHRPHELYSGLNLEUALAALAALAASP
5   VALASPGLYASNGLYTYRVALASNSERILE
6   ASPLEUALAILELEUGLNMETTYRLEULEU
7   GLYLYSGLYGLYTHRSERASPILEGLYLYS
8   ASNARGILETYRTHRTYRGLYASPILEASP
9   ASNASNGLYILEVALASPGLUASNASPTYR
10   ILELEUILECYSASNHISILEASNGLYTHR
11   GLYGLNLEUSERASPALASERLEUPHEALA
12   ALAASPALAASPGLYASNASNVALILEASP
13   GLNTHRASPARGILELEUILEGLULYSTYR
14   ILETHRGLYARGILETHRHISLEUPROVAL
15   GLYASNGLNLEUGLUHISHISHISHISHIS
16   HIS

Samples:

sample_1: dDoc_0689, [U-13C; U-15N], 0.6 ± 0.1 mM; sodium acetate 50 mM; potassium chloride 50 mM; CaCl2 10 mM; DTT 3 mM; DSS 0.02 % w/v; protease inhibitor cocktail (Roche) 0.4 tablet/100mL; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 120 mM; pH: 4.9; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D HA(CA)NHsample_1isotropicsample_conditions_1
3D HA(CA)(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

UNP A3DK52
GB ADU73768
AlphaFold A3DK52

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