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 17022

Title: Solution NMR Structure of A3DHT5 from Clostridium thermocellum, Northeast Structural Genomics Consortium Target CmR116

Deposition date: 2010-06-25 Original release date: 2010-08-19

Authors: Mills, Jeffrey; Eletsky, Alexander; Lee, Hsiau-Wei; Janjua, Haleema; Ciccosanti, Colleen; Wang, Huang; Rost, B.; Acton, T.; Xiao, R.; Everett, J.; Prestegard, James; Montelione, G.; Szyperski, Thomas

Citation: Mills, Jeffrey; Eletsky, Alexander; Lee, Hsiau-Wei; Janjua, Haleema; Ciccosanti, Colleen; Wang, Huang; Rost, B.; Acton, T.; Xiao, R.; Everett, J.; Prestegard, James; Montelione, G.; Szyperski, Thomas. "Northeast Structural Genomics Consortium Target CmR116"  To be published ., .-..

Assembly members:
CmR116, polymer, 131 residues, 14849.378 Da.

Natural source:   Common Name: C. 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):
CmR116: MKDGTYYAEADDFDESGWKD TVTIEVKNGKIVSVDWNAIN KDGGDDKDTLSRNGGYKMVE YGGAQAEWHEQAEKVEAYLV EKQDPTDIKYKDNDGHTDAI SGATIKVKKFFDLAQKALKD AEKLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts512
15N chemical shifts131
1H chemical shifts823

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CmR1161

Entities:

Entity 1, CmR116 131 residues - 14849.378 Da.

1   METLYSASPGLYTHRTYRTYRALAGLUALA
2   ASPASPPHEASPGLUSERGLYTRPLYSASP
3   THRVALTHRILEGLUVALLYSASNGLYLYS
4   ILEVALSERVALASPTRPASNALAILEASN
5   LYSASPGLYGLYASPASPLYSASPTHRLEU
6   SERARGASNGLYGLYTYRLYSMETVALGLU
7   TYRGLYGLYALAGLNALAGLUTRPHISGLU
8   GLNALAGLULYSVALGLUALATYRLEUVAL
9   GLULYSGLNASPPROTHRASPILELYSTYR
10   LYSASPASNASPGLYHISTHRASPALAILE
11   SERGLYALATHRILELYSVALLYSLYSPHE
12   PHEASPLEUALAGLNLYSALALEULYSASP
13   ALAGLULYSLEUGLUHISHISHISHISHIS
14   HIS

Samples:

NC: CmR116, [U-100% 13C; U-100% 15N], 0.97 mM; sodium azide 0.02%; DTT 10 mM; calcium chloride 5 mM; sodium chloride 100 mM; MES 20 mM; H2O 90%; D2O 10%

NC5: CmR116, [U-5% 13C; U-100% 15N], 1.0 mM; sodium azide 0.02%; DTT 10 mM; calcium chloride 5 mM; sodium chloride 100 mM; MES 20 mM; H2O 90%; D2O 10%

NC5-RDC: CmR116, [U-5% 13C; U-100% 15N], 1.0 mM; sodium azide 0.02%; DTT 10 mM; calcium chloride 5 mM; sodium chloride 100 mM; MES 20 mM; PEG 4%; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.5; pressure: 1 .; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D 1H-13C HSQCNCisotropicsample_conditions_1
3D HNCONCisotropicsample_conditions_1
3D CBCA(CO)NHNCisotropicsample_conditions_1
3D HNCACBNCisotropicsample_conditions_1
3D HBHA(CO)NHNCisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYNCisotropicsample_conditions_1
3D HCCH-TOCSYNCisotropicsample_conditions_1
3D HCCH-COSYNCisotropicsample_conditions_1
3D HN(CA)CONCisotropicsample_conditions_1
2D 1H-15N HSQCNC5-RDCanisotropicsample_conditions_1
2D 1H-13C HSQCNC5isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement, structure solution

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement, structure solution

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis, refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis

PROSA, Guntert - processing

CARA v1.8, Keller et al. - chemical shift assignment, data analysis, peak picking

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PALES, PALES (Zweckstetter, Bax) - geometry optimization

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
EMBL CDG36832
GB ABN53514 ADU75963 EEU01223 EFB38080 EIC03805
REF WP_003513428

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts