BMRB Entry 17314

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17314
MolProbity Validation Chart

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Title:
Solution Structure of a Nonphosphorylated Peptide Recognizing Domain
Deposition date:
2010-11-22
Original release date:
2012-07-25
Authors:
Dai, Kun; Liao, Shanhui; Zhang, Jiahai; Zhang, Xuecheng; Tu, Xiaoming
Citation:

Citation: Dai, Kun; Liao, Shanhui; Zhang, Jiahai; Zhang, Xuecheng; Tu, Xiaoming. "Solution Structure of a Nonphosphorylated Peptide Recognizing Domain"  .

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET22

Entity Sequences (FASTA):

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
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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
AlphaFold Q63HR2 Q8CGB6

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks