BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15822

Title: NMR solution structure of A3DK08 protein from Clostridium thermocellum: Northeast Structural Genomics Consortium Target CmR9

Authors: Swapna, G; Huang, Wang; Jiang, Mei; Foote, Erika; Xiao, Rong; Nair, Rajesh; Everett, John; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano

Citation: Swapna, G; Huang, Wang; Jiang, Mei; Foote, Erika; Xiao, Rong; Nair, Rajesh; Everett, John; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano. "NMR Solution Structure of A3DK08 protein from Clostridium thermocellum: Northeast Structural Genomics Consortium Target CmR9"  Not known ., .-..

Assembly members:
A3DK08_Protein, polymer, 76 residues, 9053.35 Da.

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

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

Entity Sequences (FASTA):
A3DK08_Protein: MKITKDMIIADVLQMDRGTA PIFINNGMHCLGCPSSMGES IEDACAVHGIDADKLVKELN EYFEKKEVLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts305
15N chemical shifts73
1H chemical shifts503

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 76 residues - 9053.35 Da.

1   METLYSILETHRLYSASPMETILEILEALA
2   ASPVALLEUGLNMETASPARGGLYTHRALA
3   PROILEPHEILEASNASNGLYMETHISCYS
4   LEUGLYCYSPROSERSERMETGLYGLUSER
5   ILEGLUASPALACYSALAVALHISGLYILE
6   ASPALAASPLYSLEUVALLYSGLULEUASN
7   GLUTYRPHEGLULYSLYSGLUVALLEUGLU
8   HISHISHISHISHISHIS

Samples:

sample_1: A3DK08 Protein, [U-100% 13C; U-100% 15N], 0.91 ± 0.2 mM; DTT 10 mM; DSS 50 uM; NaN3 0.02%; CaCl2 2 mM; NaCl 100 mM; MES 20 mM; protease inhibitor 1x mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_2: A3DK08 Protein, [U-10% 13C; U-99% 15N], 1.05 ± 0.2 mM; DTT 10 mM; DSS 50 uM; NaN3 0.02%; CaCl2 2 mM; NaCl 100 mM; MES 20 mM; protease inhibitor 1x mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 105 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C 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 HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D simultaneous CN NOESYsample_1isotropicsample_conditions_1

Software:

CNS v2.0.6, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ GAE89622
EMBL CDG37571
GB ABN54287 ADU73722 EEU00234 EFB38242 EIC03356
REF WP_037294975 WP_038290015