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 19282

Title: NMR structure of the lymphocyte receptor NKR-P1A

Deposition date: 2013-05-31 Original release date: 2014-06-09

Authors: Chmelik, Josef; Rozbesky, Daniel; Pospisilova, Eliska; Novak, Petr

Citation: Rozbesky, Daniel; Pospisilova, Eliska; Novak, Petr; Chmelik, Josef. "NMR structure of the lymphocyte receptor NKR-P1A reveals a different conformation of the conserved loop compared to crystal structure"  .

Assembly members:
NKR-P1A, polymer, 139 residues, 16008.889 Da.

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-30a(+)

Entity Sequences (FASTA):
NKR-P1A: SAKLECPQDWLSHRDKCFHV SQVSNTWEEGLVDCDGKGAT LMLIQDQEELRFLLDSIKEK YNSFWIGLRYTLPDMNWKWI NGSTLNSDVLKITGDTENDS CAAISGDKVTFESCNSDNRW ICQKELYHETLSNYVGYGH

Data sets:
Data typeCount
13C chemical shifts622
15N chemical shifts157
1H chemical shifts967

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1lymphocyte receptor NKR-P1A1

Entities:

Entity 1, lymphocyte receptor NKR-P1A 139 residues - 16008.889 Da.

1   SERALALYSLEUGLUCYSPROGLNASPTRP
2   LEUSERHISARGASPLYSCYSPHEHISVAL
3   SERGLNVALSERASNTHRTRPGLUGLUGLY
4   LEUVALASPCYSASPGLYLYSGLYALATHR
5   LEUMETLEUILEGLNASPGLNGLUGLULEU
6   ARGPHELEULEUASPSERILELYSGLULYS
7   TYRASNSERPHETRPILEGLYLEUARGTYR
8   THRLEUPROASPMETASNTRPLYSTRPILE
9   ASNGLYSERTHRLEUASNSERASPVALLEU
10   LYSILETHRGLYASPTHRGLUASNASPSER
11   CYSALAALAILESERGLYASPLYSVALTHR
12   PHEGLUSERCYSASNSERASPASNARGTRP
13   ILECYSGLNLYSGLULEUTYRHISGLUTHR
14   LEUSERASNTYRVALGLYTYRGLYHIS

Samples:

sample: NKR-P1A, [U-100% 13C; U-100% 15N], 0.5 mM; PIPES 15 mM; sodium chloride 50 mM; sodium azide 1 mM; H2O 90%; D2O 10%

sample_conditions: pH: 6.8; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsampleisotropicsample_conditions
2D 1H-13C HSQC aliphaticsampleisotropicsample_conditions
3D CBCA(CO)NHsampleisotropicsample_conditions
3D HNCACBsampleisotropicsample_conditions
3D HNCAsampleisotropicsample_conditions
3D HN(CO)CAsampleisotropicsample_conditions
3D HNCOsampleisotropicsample_conditions
3D HN(CA)COsampleisotropicsample_conditions
3D H(CCO)NHsampleisotropicsample_conditions
3D (H)C(CO)NHsampleisotropicsample_conditions
3D HCCH-TOCSY aliphaticsampleisotropicsample_conditions
3D 1H-15N NOESYsampleisotropicsample_conditions
2D 1H-13C HSQC aromaticsampleisotropicsample_conditions
3D HCCH-TOCSY aromaticsampleisotropicsample_conditions
2D (HB)CB(CGCD)HDsampleisotropicsample_conditions
3D 1H-13C NOESY aliphaticsampleisotropicsample_conditions
3D 1H-13C NOESY aromaticsampleisotropicsample_conditions

Software:

TOPSPIN v2.3.6, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.113, Goddard - chemical shift assignment, data analysis, peak picking

ARIA v2.3.1, Linge, O'Donoghue and Nilges - structure solution

CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

RECOORD, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CING, (CING) Vuister, Doreleijer, da Silva - validation

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
EMBL CAA45971 CAA45976
GB AAA39366 AAA39822 AAI20708 AAI45046 AAK39101
REF NP_001153374 NP_034867
SP P27811
AlphaFold P27811

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