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 17314

Title: Solution Structure of a Nonphosphorylated Peptide Recognizing Domain

Authors: Dai, Kun; Liao, Shanhui; Zhang, Jiahai; Zhang, Xuecheng; Tu, Xiaoming

Citation: Dai, Kun; Liao, Shanhui; Zhang, Jiahai; Zhang, Xuecheng; Tu, Xiaoming. "Solution Structure of a Nonphosphorylated Peptide Recognizing Domain"  Not known ., .-..

Assembly members:
Protein_Domain, polymer, 123 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: not available   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
Protein_Domain: MDTSKFWYKPHLSRDQAIAL LKDKDPGAFLIRDSHSFQGA YGLALKVATPPPSAQPWKGD PVEQLVRHFLIETGPKGVKI KGCPSEPYFGSLSALVSQHS ISPISLPCCLRIPSKLEHHH HHH

Data sets:
Data typeCount
13C chemical shifts388
15N chemical shifts97
1H chemical shifts678

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Nonphosphorylated Peptide Recognizing Domain1

Entities:

Entity 1, Nonphosphorylated Peptide Recognizing Domain 123 residues - Formula weight is not available

1   METASPTHRSERLYSPHETRPTYRLYSPRO
2   HISLEUSERARGASPGLNALAILEALALEU
3   LEULYSASPLYSASPPROGLYALAPHELEU
4   ILEARGASPSERHISSERPHEGLNGLYALA
5   TYRGLYLEUALALEULYSVALALATHRPRO
6   PROPROSERALAGLNPROTRPLYSGLYASP
7   PROVALGLUGLNLEUVALARGHISPHELEU
8   ILEGLUTHRGLYPROLYSGLYVALLYSILE
9   LYSGLYCYSPROSERGLUPROTYRPHEGLY
10   SERLEUSERALALEUVALSERGLNHISSER
11   ILESERPROILESERLEUPROCYSCYSLEU
12   ARGILEPROSERLYSLEUGLUHISHISHIS
13   HISHISHIS

Samples:

sample: Protein Domain, [U-99% 13C; U-99% 15N], 0.6 mM; sodium chloride 150 mM; sodium phosphate 20 mM; EDTA 2 mM; Arginine 50 mM; glutamine 50 mM; H2O 90%; D2O 10%

sample_conditions: ionic strength: 150 mM; pH: 6.8; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsampleisotropicsample_conditions
3D CBCA(CO)NHsampleisotropicsample_conditions
3D HNCACBsampleisotropicsample_conditions
3D C(CO)NHsampleisotropicsample_conditions
3D HBHA(CO)NHsampleisotropicsample_conditions
3D H(CCO)NHsampleisotropicsample_conditions
3D HN(CO)CAsampleisotropicsample_conditions
3D 1H-15N NOESYsampleisotropicsample_conditions
3D 1H-13C NOESYsampleisotropicsample_conditions
3D HCCH-COSYsampleisotropicsample_conditions

Software:

CYANA, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Guntert, Mumenthaler and Wuthrich - data analysis, processing, structure solution

NMR spectrometers:

  • Bruker DMX 500 MHz

Related Database Links:

BMRB 16472
PDB
DBJ BAA83027 BAG09960
EMBL CAB70815 CAH56176
GB AAH25818 AAH42190 AAH54099 AAI10855 AAI29829
REF NP_056134 NP_705761 NP_736610 NP_938072 XP_001102202
SP Q63HR2 Q8CGB6