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 19879

Title: NMR solution structure of a computational designed protein based on structure template 1cy5

Deposition date: 2014-03-28 Original release date: 2014-10-27

Authors: Xiong, Peng; Wang, Meng; Zhang, Jiahai; Chen, Quan; Liu, Haiyan

Citation: Xiong, Peng; Wang, Meng; Zhou, Xiaoqun; Zhang, Tongchuan; Zhang, Jiahai; Chen, Quan; Liu, Haiyan. "Boost computational protein design with a comprehensive statistical energy function and an in vivo experimental approach"  Nat. Struct. Biol. ., .-..

Assembly members:
entity, polymer, 94 residues, 10745.617 Da.

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):
entity: MTPEQREFLPEILAEIIANL DPTKILEELLRRGLLTPAEL QEVLDLKTPEEQAKKLIDFI LKLSPADVQARINVLRAHGY QALADKLNKYLTLE

Data sets:
Data typeCount
13C chemical shifts214
15N chemical shifts57
1H chemical shifts442

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 94 residues - 10745.617 Da.

1   METTHRPROGLUGLNARGGLUPHELEUPRO
2   GLUILELEUALAGLUILEILEALAASNLEU
3   ASPPROTHRLYSILELEUGLUGLULEULEU
4   ARGARGGLYLEULEUTHRPROALAGLULEU
5   GLNGLUVALLEUASPLEULYSTHRPROGLU
6   GLUGLNALALYSLYSLEUILEASPPHEILE
7   LEULYSLEUSERPROALAASPVALGLNALA
8   ARGILEASNVALLEUARGALAHISGLYTYR
9   GLNALALEUALAASPLYSLEUASNLYSTYR
10   LEUTHRLEUGLU

Samples:

sample_1: protein, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; phosphate buffer 25 mM; sodium chloride 100 mM; EDTA 2 mM

sample_2: protein, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; phosphate buffer 25 mM; sodium chloride 100 mM; EDTA 2 mM

sample_conditions_1: ionic strength: 125 mM; 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 HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

NMR spectrometers:

  • Bruker DMX 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