BMRB Entry 4706

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4706
MolProbity Validation Chart

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Title:
Structure and Binding Specificity of the Second N-Terminal Cellulose-Binding Domain from Cellulomonas fimi Endoglucanase C
Deposition date:
2000-03-31
Original release date:
2000-05-26
Authors:
Brun, E.; Johnson, P.; Creagh, L.; Haynes, C.; Tomme, P.; Webster, P.; McIntosh, L.
Citation:

Citation: Brun, E.; Johnson, P.; Creagh, A.; Haynes, C.; Tomme, P.; Webster, P.; McIntosh, L.. "Structure and Binding Specificity of the Second N-Terminal Cellulose-Binding Domain from Cellulomonas fimi Endoglucanase C"  Biochemistry 39, 2445-2458 (2000).

Assembly members:

Assembly members:
ENDOGLUCANASE C CELLULOE BINDING DOMAIN N2, polymer, 153 residues, 15868 Da.

Natural source:

Natural source:   Common Name: Bacteria   Taxonomy ID: 1708   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Cellulomonas fimi

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ENDOGLUCANASE C CELLULOE BINDING DOMAIN N2: ASLDSEVELLPHTSFAESLG PWSLYGTSEPVFADGRMCVD LPGGQGNPWDAGLVYNGVPV GEGESYVLSFTASATPDMPV RVLVGEGGGAYRTAFEQGSA PLTGEPATREYAFTSNLTFP PDGDAPGQVAFHLGKAGAYE FCISQVSLTTSAT

Data sets:
Data typeCount
13C chemical shifts484
15N chemical shifts155
1H chemical shifts970

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1CBDN21

Entities:

Entity 1, CBDN2 153 residues - 15868 Da.

1   ALASERLEUASPSERGLUVALGLULEULEU
2   PROHISTHRSERPHEALAGLUSERLEUGLY
3   PROTRPSERLEUTYRGLYTHRSERGLUPRO
4   VALPHEALAASPGLYARGMETCYSVALASP
5   LEUPROGLYGLYGLNGLYASNPROTRPASP
6   ALAGLYLEUVALTYRASNGLYVALPROVAL
7   GLYGLUGLYGLUSERTYRVALLEUSERPHE
8   THRALASERALATHRPROASPMETPROVAL
9   ARGVALLEUVALGLYGLUGLYGLYGLYALA
10   TYRARGTHRALAPHEGLUGLNGLYSERALA
11   PROLEUTHRGLYGLUPROALATHRARGGLU
12   TYRALAPHETHRSERASNLEUTHRPHEPRO
13   PROASPGLYASPALAPROGLYGLNVALALA
14   PHEHISLEUGLYLYSALAGLYALATYRGLU
15   PHECYSILESERGLNVALSERLEUTHRTHR
16   SERALATHR

Samples:

sample_1: ENDOGLUCANASE C CELLULOE BINDING DOMAIN N2, [U-99% 15N; U-99% 13C], 1.5 – 2 mM; Cellopentaose 44 mM; NaCl 50 mM; PHOSPHATE BUFFER 50 mM

sample_2: ENDOGLUCANASE C CELLULOE BINDING DOMAIN N2, [U-99% 15N], 1.5 – 2 mM; Cellopentaose 44 mM; NaCl 50 mM; PHOSPHATE BUFFER 50 mM

sample_3: ENDOGLUCANASE C CELLULOE BINDING DOMAIN N21.5 – 2 mM; Cellopentaose 44 mM; NaCl 50 mM; PHOSPHATE BUFFER 50 mM

sample_4: ENDOGLUCANASE C CELLULOE BINDING DOMAIN N2, non-random 10% 13C, 1.5 – 2 mM

sample_cond_1: ionic strength: 50 mM; pH: 6; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
3D 13C-SEPARATED_NOESYnot availablenot availablesample_cond_1
3D 15N-SEPARATED_NOESYnot availablenot availablesample_cond_1
2D NOESYnot availablenot availablesample_cond_1
4D 13C/15N-SEPARATED_NOESYnot availablenot availablesample_cond_1
HNHAnot availablenot availablesample_cond_1

Software:

VNMR v6.1A - COLLECTION

FELIX v230 - PROCESSING, DATA ANALYSIS

X-PLOR v3.8 - STRUCTURE CALCULATION, REFINEMENT

NMR spectrometers:

  • VARIAN UNITY 500 MHz

Related Database Links:

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