BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 34005

Title: Murin CXCL13 solution structure   PubMed: 29070611

Deposition date: 2016-06-03 Original release date: 2017-06-15

Authors: Monneau, Y.; Lortat-Jacob, H.

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).

Assembly members:
entity_1, polymer, 88 residues, 9807.674 Da.

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

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

Entity Sequences (FASTA):
entity_1: ILEAHYTNLKCRCSGVISTV VGLNIIDRIQVTPPGNGCPK TEVVIWTKMKKVICVNPRAK WLQRLLRHVQSKSLSSTPQA PVSKRRAA

Data sets:
Data typeCount
13C chemical shifts313
15N chemical shifts81
1H chemical shifts602

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 88 residues - 9807.674 Da.

1   ILELEUGLUALAHISTYRTHRASNLEULYS
2   CYSARGCYSSERGLYVALILESERTHRVAL
3   VALGLYLEUASNILEILEASPARGILEGLN
4   VALTHRPROPROGLYASNGLYCYSPROLYS
5   THRGLUVALVALILETRPTHRLYSMETLYS
6   LYSVALILECYSVALASNPROARGALALYS
7   TRPLEUGLNARGLEULEUARGHISVALGLN
8   SERLYSSERLEUSERSERTHRPROGLNALA
9   PROVALSERLYSARGARGALAALA

Samples:

sample_1: CXCL13, [U-15N], 850 uM

sample_2: CXCL13, [U-15N; U-13C], 560 uM

sample_3: CXCL13, [U-15N], 250 uM

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

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D H(C)CH-TOCSYsample_2isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSY-HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESY-HSQCsample_1isotropicsample_conditions_1
2D (HB)CB(CG)(CD)HDsample_2isotropicsample_conditions_1
3D 1H-13C NOESY-HMQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESY-HSQCsample_3isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

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

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