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 17399

Title: Structure of a novel CBM3 lacking the calcium-binding site   PubMed: 21880019

Deposition date: 2011-01-07 Original release date: 2011-12-20

Authors: Paiva, Joice; Meza, Andreia; Sforca, Mauricio; Navarro, Rodrigo; Neves, Jorge; Santos, Camila; Murakami, Mario; Zeri, Ana

Citation: Santos, Camila; Paiva, Joice; Sforca, Mauricio; Neves, Jorge; Navarro, Rodrigo; Cota, Junio; Akao, Patricia; Hoffmam, Zaira; Meza, Andreia; Smetana, Juliana; Nogueira, Maria; Polikarpov, Igor; Neto, Jose; Squina, Fabio; Ward, Richard; Ruller, Roberto; Zeri, Ana; Murakami, Mario. "Dissecting structure-function-stability relationships of a thermostable GH5-CBM3 cellulase from Bacillus subtilis 168"  Biochem. J. 441, 95-104.

Assembly members:
entity, polymer, 149 residues, 16717.734 Da.

Natural source:   Common Name: Bacillus subtilis   Taxonomy ID: 1423   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus subtilis

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

Entity Sequences (FASTA):
entity: MASISVQYRAGDGSMNSNQI RPQLQIKNNGNTTVDLKDVT ARYWYKAKNKGQNFDCDYAQ IGCGNVTHKFVTLHKPKQGA DTYLELGFKNGTLAPGASTG NIQLRLHNDDWSNYAQSGDY SFFKSNTFKTTKKITLYDQG KLIWGTEPN

Data sets:
Data typeCount
13C chemical shifts583
15N chemical shifts147
1H chemical shifts917

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CBM31

Entities:

Entity 1, CBM3 149 residues - 16717.734 Da.

1   METALASERILESERVALGLNTYRARGALA
2   GLYASPGLYSERMETASNSERASNGLNILE
3   ARGPROGLNLEUGLNILELYSASNASNGLY
4   ASNTHRTHRVALASPLEULYSASPVALTHR
5   ALAARGTYRTRPTYRLYSALALYSASNLYS
6   GLYGLNASNPHEASPCYSASPTYRALAGLN
7   ILEGLYCYSGLYASNVALTHRHISLYSPHE
8   VALTHRLEUHISLYSPROLYSGLNGLYALA
9   ASPTHRTYRLEUGLULEUGLYPHELYSASN
10   GLYTHRLEUALAPROGLYALASERTHRGLY
11   ASNILEGLNLEUARGLEUHISASNASPASP
12   TRPSERASNTYRALAGLNSERGLYASPTYR
13   SERPHEPHELYSSERASNTHRPHELYSTHR
14   THRLYSLYSILETHRLEUTYRASPGLNGLY
15   LYSLEUILETRPGLYTHRGLUPROASN

Samples:

sample_1: cbm, [U-99% 15N], 0.3 mM; H2O, relative abundance, 95%; D2O, relative abundance, 5%

sample_2: cbm, [U-100% 13C; U-100% 15N], 0.3 mM; H2O, relative abundance, 95%; D2O, relative abundance, 5%

sample_3: cbm, [U-100% 13C; U-100% 15N], 0.3 mM; D2O, relative abundance, 5%

sample_conditions_1: ionic strength: 70 mM; pH: 7.2; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

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

NMRView v5, Johnson, One Moon Scientific - chemical shift assignment, chemical shift calculation, peak picking

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

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAA00859 BAI85501 BAL46915 GAK81525
EMBL CAA28392 CAA47429 CAA82317 CAA97610 CAB13696
GB AAC02536 AAK39540 AAK94871 AAO63626 AAV34758
PRF 2106121A
REF NP_389695 WP_003231540 WP_014479947 WP_015251994 WP_015383776
SP P10475 P23549

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