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Biological Magnetic Resonance Data Bank


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BMRB Entry 17902

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17902
MolProbity Validation Chart

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Title: Solution structure of CCL2 in complex   PubMed: 22615566

Deposition date: 2011-08-30 Original release date: 2016-06-29

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

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, polymer, 153 residues, 16604.430 Da.
GlcNAc-beta1_4-(Fuc-alpha1_3-)GlcNAc-beta-spacer, polymer, 3 residues, Formula weight is not available

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: MGHHHHHHHHSGDSPAVTLS AGNYIIYNRVLSPRGEKLAL TYPGRQRTPVTVSPLDGSSE QAWILRSYDSNSNTWTISPV GSPNSQIGWGAGNVPVVLPP NNYVWTLTLTSGGYNIQDGK RTVSWSLNNATAGEEVSIGA DATFSGRWVIEKV
GlcNAc-beta1_4-(Fuc-alpha1_3-)GlcNAc-beta-spacer: XXX

Data sets:
Data typeCount
13C chemical shifts621
15N chemical shifts163
1H chemical shifts1012

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CCL21
2GlcNAc-beta1_4-(Fuc-alpha1_3-)GlcNAc-beta-spacer2

Entities:

Entity 1, CCL2 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

Entity 2, GlcNAc-beta1_4-(Fuc-alpha1_3-)GlcNAc-beta-spacer 3 residues - Formula weight is not available

1   NAGMAGFUC

Samples:

sample_1: CCL2, [U-100% 13C; U-100% 15N], 1 mM; GlcNAc-beta1_4-(Fuc-alpha1_3-)GlcNAc-beta-spacer 1 mM; potassium phosphate 50 mM; sodium chloride 100 mM; acetic acid, [U-100% 2H], ~41 mM; H2O 90%; D2O 10%

sample_2: CCL2, [U-100% 13C; U-100% 15N], 1 mM; GlcNAc-beta1_4-(Fuc-alpha1_3-)GlcNAc-beta-spacer 1 mM; potassium phosphate 50 mM; sodium chloride 100 mM; acetic acid, [U-100% 2H], ~41 mM; D2O 100%

sample_3: CCL2, [U-100% 15N], 1 mM; GlcNAc-beta1_4-(Fuc-alpha1_3-)GlcNAc-beta-spacer 1 mM; potassium phosphate 50 mM; sodium chloride 100 mM; acetic acid, [U-100% 2H], ~41 mM; H2O 90%; D2O 10%

sample_4: CCL2, [U-100% 15N], 1 mM; GlcNAc-beta1_4-(Fuc-alpha1_3-)GlcNAc-beta-spacer 1 mM; potassium phosphate 50 mM; sodium chloride 100 mM; acetic acid, [U-100% 2H], ~41 mM; D2O 100%

sample_5: CCL2, [U-10% 13C, U-100% 15N], 1 mM; GlcNAc-beta1_4-(Fuc-alpha1_3-)GlcNAc-beta-spacer 1 mM; potassium phosphate 50 mM; sodium chloride 100 mM; acetic acid, [U-100% 2H], ~41 mM; D2O 5%; H2O 95%

sample_conditions_1: ionic strength: 150 mM; pH: 4.7; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D NOESYsample_3isotropicsample_conditions_1
3D 15N edited NOESYsample_3isotropicsample_conditions_1
2D 15N F1-filtered,F2-filtered NOESYsample_3isotropicsample_conditions_1
2D NOESYsample_4isotropicsample_conditions_1
2D TOCSYsample_4isotropicsample_conditions_1
2D 13C-HSQCsample_4isotropicsample_conditions_1
2D 15N-HSQCsample_4isotropicsample_conditions_1
2D 13C-HSQCsample_1isotropicsample_conditions_1
3D 13C edited-NOESYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 13C-HSQCsample_2isotropicsample_conditions_1
3D HC(C)H-COSYsample_2isotropicsample_conditions_1
2D 13C F1-filtered TOCSYsample_1isotropicsample_conditions_1
2D 13C F1-filtered NOESYsample_2isotropicsample_conditions_1
2D 13C F1-filtered TOCSYsample_2isotropicsample_conditions_1
2D 13C F1-filtered F2-filtered NOESYsample_2isotropicsample_conditions_1
3D 13C F1-edited F3-filtered NOESYsample_2isotropicsample_conditions_1
2D constant-time 13C-HSQCsample_5isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, data analysis

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

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

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

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

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