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 25994

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for designed protein E_1r26   PubMed: 27522946

Deposition date: 2016-03-12 Original release date: 2016-10-13

Authors: Zhou, Xiaoqun

Citation: Zhou, Xiaoqun; Xiong, Peng; Wang, Meng; Ma, Rongsheng; Zhang, Jiahai; Chen, Quan; Liu, Haiyan. "Proteins of well-defined structures can be designed without backbone readjustment by a statistical model."  J. Struct. Biol. 196, 350-357 (2016).

Assembly members:
E_1r26, polymer, 122 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

Entity Sequences (FASTA):
E_1r26: MARPSNVKPSPHVIKSLEEL REATASNRISVIVFTHPDSK RSKEIKEKLKKLAEEFPDVD IYLVDTSTNPEAREWYNITS VPTFVIEKGGEPLGEVKGPD IDKLRETLDELLARLEHHHH HH

Data sets:
Data typeCount
13C chemical shifts311
15N chemical shifts106
1H chemical shifts591

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 122 residues - Formula weight is not available

1   METALAARGPROSERASNVALLYSPROSER
2   PROHISVALILELYSSERLEUGLUGLULEU
3   ARGGLUALATHRALASERASNARGILESER
4   VALILEVALPHETHRHISPROASPSERLYS
5   ARGSERLYSGLUILELYSGLULYSLEULYS
6   LYSLEUALAGLUGLUPHEPROASPVALASP
7   ILETYRLEUVALASPTHRSERTHRASNPRO
8   GLUALAARGGLUTRPTYRASNILETHRSER
9   VALPROTHRPHEVALILEGLULYSGLYGLY
10   GLUPROLEUGLYGLUVALLYSGLYPROASP
11   ILEASPLYSLEUARGGLUTHRLEUASPGLU
12   LEULEUALAARGLEUGLUHISHISHISHIS
13   HISHIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], mM; sodium phosphate 0.02 mM; EDTA 0.01 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; 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 C(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker DMX 600 MHz

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