BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16716

Title: Backbone chemical shifts of NI3C_Mut5 DARPin   PubMed: 20654623

Deposition date: 2010-02-10 Original release date: 2010-08-12

Authors: Wetzel, Svava; Ewald, Christina; Jurt, Simon; Zerbe, Oliver; Plueckthun, Andreas

Citation: Wetzel, Svava; Ewald, Christina; Settanni, Giovanni; Jurt, Simon; Pluckthun, Andreas; Zerbe, Oliver. "Residue-Resolved Stability of Full-Consensus Ankyrin Repeat Proteins Probed by NMR."  J. Mol. Biol. 402, 241-258 (2010).

Assembly members:
NI3C_Mut5, polymer, 169 residues, Formula weight is not available

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pSW_NI3C_Mut5

Entity Sequences (FASTA):
NI3C_Mut5: MRGSHHHHHHGSDLGKKLLE AARAGQDDEVRILMANGADV NAKDKDGYTPLHLAAREGHL EIVEVLLKAGADVNAKDKDG YTPLHLAAREGHLEIVEVLL KAGADVNAKDKDGYTPLHLA AREGHLEIVEVLLKAGADVN AQDKFGKTPFDLAIDNGNED IAEVLQKAA

Data sets:
Data typeCount
13C chemical shifts290
15N chemical shifts152
1H chemical shifts152

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NI3C_Mut5 monomer1

Entities:

Entity 1, NI3C_Mut5 monomer 169 residues - Formula weight is not available

1   METARGGLYSERHISHISHISHISHISHIS
2   GLYSERASPLEUGLYLYSLYSLEULEUGLU
3   ALAALAARGALAGLYGLNASPASPGLUVAL
4   ARGILELEUMETALAASNGLYALAASPVAL
5   ASNALALYSASPLYSASPGLYTYRTHRPRO
6   LEUHISLEUALAALAARGGLUGLYHISLEU
7   GLUILEVALGLUVALLEULEULYSALAGLY
8   ALAASPVALASNALALYSASPLYSASPGLY
9   TYRTHRPROLEUHISLEUALAALAARGGLU
10   GLYHISLEUGLUILEVALGLUVALLEULEU
11   LYSALAGLYALAASPVALASNALALYSASP
12   LYSASPGLYTYRTHRPROLEUHISLEUALA
13   ALAARGGLUGLYHISLEUGLUILEVALGLU
14   VALLEULEULYSALAGLYALAASPVALASN
15   ALAGLNASPLYSPHEGLYLYSTHRPROPHE
16   ASPLEUALAILEASPASNGLYASNGLUASP
17   ILEALAGLUVALLEUGLNLYSALAALA

Samples:

sample_1: NI3C_Mut5, [U-99% 15N], 700 uM; potassium phosphate 50 mM; sodium chloride 150 mM; H2O 90%; D2O 10%

sample_2: NI3C_Mut5, [U-100% 13C; U-100% 15N; U-80% 2H], 700 uM; potassium phosphate 50 mM; sodium chloride 150 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.2 M; pH: 7.4; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(CO)CACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D HN(COCA)NHsample_2isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CARA v1.8.3, R. Keller - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB

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