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 16339

Title: NMR structures of a designed Cyanovirin-N homolog lectin; LKAMG   PubMed: 19639634

Deposition date: 2009-06-08 Original release date: 2009-11-16

Authors: Koharudin, Leonardus; Gronenborn, Angela

Citation: Koharudin, Leonardus; Furey, William; Gronenborn, Angela. "A designed chimeric cyanovirin-N homolog lectin: structure and molecular basis of sucrose binding."  Proteins 77, 904-915 (2009).

Assembly members:
LKAMG, polymer, 107 residues, 12104.285 Da.

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

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

Entity Sequences (FASTA):
LKAMG: MSYADSSRNAVLTNGGRTLR AECRNADGNWVTSELDLDTI IGNNDGHFQWGGQNFTETAE DIRFHPKEGAAEQPILRARL RDCNGEFHDRDVNLNRIQNV NGRLVFQ

Data sets:
Data typeCount
13C chemical shifts301
15N chemical shifts121
1H chemical shifts658

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1LKAMG1

Entities:

Entity 1, LKAMG 107 residues - 12104.285 Da.

a triplet (GSH) artifact cloning is not included in the protein sequence and structure calculation.

1   METSERTYRALAASPSERSERARGASNALA
2   VALLEUTHRASNGLYGLYARGTHRLEUARG
3   ALAGLUCYSARGASNALAASPGLYASNTRP
4   VALTHRSERGLULEUASPLEUASPTHRILE
5   ILEGLYASNASNASPGLYHISPHEGLNTRP
6   GLYGLYGLNASNPHETHRGLUTHRALAGLU
7   ASPILEARGPHEHISPROLYSGLUGLYALA
8   ALAGLUGLNPROILELEUARGALAARGLEU
9   ARGASPCYSASNGLYGLUPHEHISASPARG
10   ASPVALASNLEUASNARGILEGLNASNVAL
11   ASNGLYARGLEUVALPHEGLN

Samples:

sample_1: LKAMG, [U-100% 15N], 0.5 mM; sodium phosphate 20 mM; sodium azide 0.02%

sample_2: LKAMG, [U-100% 13C; U-100% 15N], 1.2 mM; sodium phosphate 20 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 20 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 15N-1H HSQCsample_1isotropicsample_conditions_1
3D CBCANHsample_2isotropicsample_conditions_1
3D CBCA(co)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D H(c)CH-NH TOCSYsample_2isotropicsample_conditions_1
(h)CCH-NH TOCSYsample_2isotropicsample_conditions_1
3D HBHA(co)NHsample_2isotropicsample_conditions_1
3D simultaneous 15N/13C NOESY-HSQCsample_2isotropicsample_conditions_1

Software:

CNS v1.1, Brunger A. T. et.al. - refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - Automatic NOE calibration

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

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB

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