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 18269

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18269
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: Solution Structure of N-Terminal domain of human Conserved Dopamine Neurotrophic Factor (CDNF)   PubMed: 22528768

Deposition date: 2012-02-15 Original release date: 2012-06-13

Authors: Cristiane, Latge; Katia, Cabral; Debora, Foguel; Pires, Jose Ricardo; Almeida, Marcius

Citation: Latge, Cristiane; Cabral, Katia; Almeida, Marcius; Foguel, Debora. "(1)H-, (13)C- and (15)N-NMR assignment of the N-terminal domain of human cerebral dopamine neurotrophic factor (CDNF)"  Biomol. NMR Assign. ., .-. (2012).

Assembly members:
entity, polymer, 105 residues, 11965.022 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
entity: QEAGGRPGADCEVCKEFLNR FYKSLIDRGVNFSLDTIEKE LISFCLDTKGKENRLCYYLG ATKDAATKILSEVTRPMSVH MPAMKICEKLKKLDSQICEL KYEKT

Data sets:
Data typeCount
13C chemical shifts360
15N chemical shifts98
1H chemical shifts688

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1N-terminal domain of human CDNF1

Entities:

Entity 1, N-terminal domain of human CDNF 105 residues - 11965.022 Da.

Mature sequence of N-terminal domain.

1   GLNGLUALAGLYGLYARGPROGLYALAASP
2   CYSGLUVALCYSLYSGLUPHELEUASNARG
3   PHETYRLYSSERLEUILEASPARGGLYVAL
4   ASNPHESERLEUASPTHRILEGLULYSGLU
5   LEUILESERPHECYSLEUASPTHRLYSGLY
6   LYSGLUASNARGLEUCYSTYRTYRLEUGLY
7   ALATHRLYSASPALAALATHRLYSILELEU
8   SERGLUVALTHRARGPROMETSERVALHIS
9   METPROALAMETLYSILECYSGLULYSLEU
10   LYSLYSLEUASPSERGLNILECYSGLULEU
11   LYSTYRGLULYSTHR

Samples:

sample_1: CDNF, [U-100% 13C; U-100% 15N], 0.7 mM; D2O, [U-2H], 10%; sodium azide 5 mM; MES 20 mM; sodium chloride 150 mM; H2O 90%

sample_conditions_1: ionic strength: 175 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

ARIA, Linge, O, . - peak picking, refinement, structure solution

TOPSPIN v3, Bruker Biospin - collection, processing

CARA v1.8.4.2., Keller and Wuthrich - chemical shift assignment, data analysis

CNSSOLVE v1.1., Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

NMR spectrometers:

  • Bruker Avance III 800 MHz

Related Database Links:

BMRB 19164
PDB
DBJ BAG62825
GB AAI33043 AAI33045 AIC53868 EAW86264 EHH18900
REF NP_001025125 NP_001180755 XP_002820588 XP_003257694 XP_003806807
SP Q49AH0

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