BMRB Entry 30042

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30042
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Murin CXCL13 solution structure featuring a folded N-terminal domain
Deposition date:
2016-03-25
Original release date:
2017-03-30
Authors:
Monneau, Y.; Lortat-Jacob, H.
Citation:

Citation: Monneau, Yoan; Luo, Lingjie; Sankaranarayanan, Nehru Viji; Nagarajan, Balaji; Vives, Romain; Baleux, Francoise; Desai, Umesh; Arenzana-Seidedos, Fernando; Lortat-Jacob, Hugues. "Solution structure of CXCL13 and heparan sulfate binding show that GAG binding site and cellular signalling rely on distinct domains"  Open Biol. 7, 170133-170133 (2017).
PubMed: 29070611

Assembly members:

Assembly members:
entity_1, polymer, 89 residues, 9938.868 Da.

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: pET17b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MILEAHYTNLKCRCSGVIST VVGLNIIDRIQVTPPGNGCP KTEVVIWTKMKKVICVNPRA KWLQRLLRHVQSKSLSSTPQ APVSKRRAA

Data sets:
Data typeCount
13C chemical shifts309
15N chemical shifts91
1H chemical shifts647

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 89 residues - 9938.868 Da.

1   METILELEUGLUALAHISTYRTHRASNLEU
2   LYSCYSARGCYSSERGLYVALILESERTHR
3   VALVALGLYLEUASNILEILEASPARGILE
4   GLNVALTHRPROPROGLYASNGLYCYSPRO
5   LYSTHRGLUVALVALILETRPTHRLYSMET
6   LYSLYSVALILECYSVALASNPROARGALA
7   LYSTRPLEUGLNARGLEULEUARGHISVAL
8   GLNSERLYSSERLEUSERSERTHRPROGLN
9   ALAPROVALSERLYSARGARGALAALA

Samples:

sample_1: CXCL13, [U-15N], 850 uM; potassium phosphate 20 mM; NaCl 100 mM

sample_2: CXCL13, [U-13C; U-15N], 280 uM; potassium phosphate 20 mM; NaCl 100 mM

sample_3: CXCL13, [U-13C; U-15N], 280 uM; potassium phosphate 20 mM; NaCl 100 mM

sample_4: CXCL13, [U-10% 13C; U-100% 15N], 280 uM; potassium phosphate 20 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 120 mM; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-edited NOESYsample_1isotropicsample_conditions_1
3D 13C-edited NOESYsample_2isotropicsample_conditions_1
3D 13C-HMQC-NOESY-13C,1H-HMQCsample_2isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HACACOsample_3isotropicsample_conditions_1
3D H(C)CH-TOCSYsample_3isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-13C CT-HSQC aliphaticsample_4isotropicsample_conditions_1
2D COSYdqfsample_4isotropicsample_conditions_1
2D TOCSYsample_4isotropicsample_conditions_1
2D CBCGCDHDsample_2isotropicsample_conditions_1
3D HNCOCAsample_3isotropicsample_conditions_1

Software:

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

NMRFAM-SPARKY, Lee et al. Bioinformatics 2015 Apr 15; 31(8):1325-7 - chemical shift assignment

cyana, Guntert, P., Mumenthaler, C., & Wuthrich, K., Herrmann, T., - structure calculation

NMR spectrometers:

  • Bruker AvanceIII 600 MHz
  • Bruker AvanceIII 700 MHz
  • Bruker AvanceIII 950 MHz
  • Bruker AvanceIII 850 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks