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Biological Magnetic Resonance Data Bank


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BMRB Entry 17890

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17890
MolProbity Validation Chart

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Title: NMR structure of the lectin CCL2 (free)   PubMed: 22615566

Deposition date: 2011-08-29 Original release date: 2012-06-04

Authors: Schubert, Mario; Walti, Martin; Egloff, Pascal; Bleuler-Martinez, Silvia; Aebi, Markus; Allain, Frederic; Kunzler, Markus

Citation: Schubert, Mario; Bleuler-Martinez, Silvia; Butschi, Alex; Walti, Martin; Egloff, Pascal; Stutz, Katrin; Yan, Shi; Wilson, Iain; Hengartner, Michael; Aebi, Markus; Allain, Frederic; Kunzler, Markus. "Plasticity of the beta-Trefoil Protein Fold in the Recognition and Control of Invertebrate Predators and Parasites by a Fungal Defence System"  PLoS Pathog. 8, e1002706-e1002706 (2012).

Assembly members:
CCL2 (free), polymer, 153 residues, 16604.430 Da.

Natural source:   Common Name: Coprinopsis cinerea   Taxonomy ID: 5346   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Coprinopsis cinerea

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

Entity Sequences (FASTA):
CCL2 (free): MGHHHHHHHHSGDSPAVTLS AGNYIIYNRVLSPRGEKLAL TYPGRQRTPVTVSPLDGSSE QAWILRSYDSNSNTWTISPV GSPNSQIGWGAGNVPVVLPP NNYVWTLTLTSGGYNIQDGK RTVSWSLNNATAGEEVSIGA DATFSGRWVIEKV

Data sets:
Data typeCount
13C chemical shifts605
15N chemical shifts161
1H chemical shifts989

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1CCL2 (free)1

Entities:

Entity 1, CCL2 (free) 153 residues - 16604.430 Da.

1   METGLYHISHISHISHISHISHISHISHIS
2   SERGLYASPSERPROALAVALTHRLEUSER
3   ALAGLYASNTYRILEILETYRASNARGVAL
4   LEUSERPROARGGLYGLULYSLEUALALEU
5   THRTYRPROGLYARGGLNARGTHRPROVAL
6   THRVALSERPROLEUASPGLYSERSERGLU
7   GLNALATRPILELEUARGSERTYRASPSER
8   ASNSERASNTHRTRPTHRILESERPROVAL
9   GLYSERPROASNSERGLNILEGLYTRPGLY
10   ALAGLYASNVALPROVALVALLEUPROPRO
11   ASNASNTYRVALTRPTHRLEUTHRLEUTHR
12   SERGLYGLYTYRASNILEGLNASPGLYLYS
13   ARGTHRVALSERTRPSERLEUASNASNALA
14   THRALAGLYGLUGLUVALSERILEGLYALA
15   ASPALATHRPHESERGLYARGTRPVALILE
16   GLULYSVAL

Samples:

sample_1: CCL2, [U-100% 13C; U-100% 15N], 1 mM; potassium phosphate 50 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_2: CCL2, [U-100% 13C; U-100% 15N], 1 mM; potassium phosphate 50 mM; sodium chloride 100 mM; D2O 100%

sample_3: CCL2, [U-100% 15N], 1 mM; potassium phosphate 50 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_4: CCL2, [U-100% 15N], 1 mM; potassium phosphate 50 mM; sodium chloride 100 mM; D2O 100%

sample_conditions_1: ionic strength: 150 mM; pH: 5.7; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CYANA, Guntert, Mumenthaler and Wuthrich, Herrmann, Guntert and Wuthrich - structure solution

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 750 MHz
  • Bruker Avance 900 MHz

Related Database Links:

BMRB 17902
PDB
GB ACD88750

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