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 16107

Title: Solution NMR structure of F5/8 type C-terminal domain of a putative chitobiase from Bacteroides thetaiotaomicron. Northeast Structural Genomics Consortium target BtR324B

Deposition date: 2009-01-04 Original release date: 2009-03-02

Authors: Eletsky, Alexander; Mills, Jeffrey; Lee, Hsiau-Wei; Lee, Dong Yup; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Nair, Rajesh; Everett, John; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Prestegard, James; Szyperski, Thomas

Citation: Eletsky, Alexander; Mills, Jeffrey; Lee, Hsiau-Wei; Lee, Dong Yup; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Nair, Rajesh; Everett, John; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Prestegard, James; Szyperski, Thomas. "Solution NMR structure of F5/8 type C-terminal domain of a putative chitobiase from Bacteroides thetaiotaomicron."  Proteins: Struct. Funct. Genet. ., .-..

Assembly members:
btr324b, polymer, 159 residues, 17550.711 Da.

Natural source:   Common Name: Bacteroides thetaiotaomicron   Taxonomy ID: 818   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacteroides thetaiotaomicron

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

Entity Sequences (FASTA):
btr324b: MGTTISKSGWEVLSFTTQEA SGEGAGNGLAKCLIDGDTET FWHAKWQGGSDPLPYDIVID MKQNIQIAQVELLPRGRGSN NPIKVVEFAASEDNVNWTPI GRFGFTNQDAALEYYVKSIK ARYIRLTIPDDGGNSTVAAI RELDVKGTIINLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts669
15N chemical shifts178
1H chemical shifts1129
residual dipolar couplings137

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1btr324b1

Entities:

Entity 1, btr324b 159 residues - 17550.711 Da.

Residues 2-151 correspond to the C-terminal residues 291-440 in the wild-type protein. Residue 1 is due to addition of a start codon. Residues 152-159 represent a non-native affinity tag. A K4T mutation was introduced during cloning

1   METGLYTHRTHRILESERLYSSERGLYTRP
2   GLUVALLEUSERPHETHRTHRGLNGLUALA
3   SERGLYGLUGLYALAGLYASNGLYLEUALA
4   LYSCYSLEUILEASPGLYASPTHRGLUTHR
5   PHETRPHISALALYSTRPGLNGLYGLYSER
6   ASPPROLEUPROTYRASPILEVALILEASP
7   METLYSGLNASNILEGLNILEALAGLNVAL
8   GLULEULEUPROARGGLYARGGLYSERASN
9   ASNPROILELYSVALVALGLUPHEALAALA
10   SERGLUASPASNVALASNTRPTHRPROILE
11   GLYARGPHEGLYPHETHRASNGLNASPALA
12   ALALEUGLUTYRTYRVALLYSSERILELYS
13   ALAARGTYRILEARGLEUTHRILEPROASP
14   ASPGLYGLYASNSERTHRVALALAALAILE
15   ARGGLULEUASPVALLYSGLYTHRILEILE
16   ASNLEUGLUHISHISHISHISHISHIS

Samples:

NC5_peg: btr324b, [U-5% 13C; U-100% 15N], 1.1 mM; ammonium acetate 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02 mM

NC: btr324b, [U-100% 13C; U-100% 15N], 1.1 mM; ammonium acetate 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02 mM

NC5: btr324b, [U-5% 13C; U-100% 15N], 1.1 mM; ammonium acetate 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02 mM

NC5_paag: btr324b, [U-5% 13C; U-100% 15N], 1.1 mM; ammonium acetate 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02 mM

sample_conditions_1: ionic strength: 215 mM; pH: 4.5; pressure: 1.0 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D 1H-13C HSQC aliNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC aliNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC aroNCisotropicsample_conditions_1
1D 1H-15N HSQC T1NCisotropicsample_conditions_1
1D 1H-15N HSQC T2NCisotropicsample_conditions_1
3D HNCONCisotropicsample_conditions_1
3D CBCA(CO)NHNCisotropicsample_conditions_1
3D HNCACBNCisotropicsample_conditions_1
3D HBHA(CO)NHNCisotropicsample_conditions_1
3D HN(CA)CONCisotropicsample_conditions_1
3D (H)CCH-COSY aliNCisotropicsample_conditions_1
3D (H)CCH-TOCSY aliNCisotropicsample_conditions_1
3D (H)CCH-COSY aroNCisotropicsample_conditions_1
3D (H)CCH-TOCSY aroNCisotropicsample_conditions_1
2D 1H-15N LR-HSQCNCisotropicsample_conditions_1
2D 1H-15N MEXICONCisotropicsample_conditions_1
3D 1H-15N/13Cali/13Caro NOESYNCisotropicsample_conditions_1
3D 1H-13Cali NOESYNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC methyl LVNC5isotropicsample_conditions_1
2D 1H-15N HSQCNC5isotropicsample_conditions_1
2D 1H-13C TROSYNC5isotropicsample_conditions_1
2D 1H-15N HSQCNC5_paaganisotropicsample_conditions_1
2D 1H-15N TROSYNC5_paaganisotropicsample_conditions_1
2D 1H-15N HSQCNC5_peganisotropicsample_conditions_1
2D 1H-15N TROSYNC5_peganisotropicsample_conditions_1

Software:

VNMRJ v2.1B, Varian - collection

TOPSPIN v2.1, Bruker Biospin - collection, processing

PROSA v6.0.2, Guntert - processing

CARA v1.8.4.2, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

TALOS v2007.068.09.07, Cornilescu, Delaglio and Bax - data analysis

CNS v1.2.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

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

PSVS v1.3, Bhattacharya and Montelione - structure validation

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
EMBL CDE80156 CUM72398 CUO89228 CUP77803
GB AAO75972 ALJ42041 EES70459 EOS01998
REF NP_809778 WP_008765703 WP_011107501 WP_016267553 WP_048697480

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