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 27651

Title: Conformational Changes in the Cytoplasmic Region of KIR3DL1 upon Interaction with SHP-2   PubMed: 30773397

Deposition date: 2018-10-15 Original release date: 2019-02-22

Authors: Cheng, Hong; Schwell, Vered; Curtis, Brett; Fazlieva, Ruzaliya; Roder, Heinrich; Campbell, Kerry

Citation: Cheng, Hong; Schwell, Vered; Curtis, Brett; Fazlieva, Ruzaliya; Roder, Heinrich; Campbell, Kerry. "Conformational Changes in the Cytoplasmic Region of KIR3DL1 upon Interaction with SHP-2"  Structure 27, 639-650 (2019).

Assembly members:
KIR3DL1-cyto, polymer, 117 residues, Formula weight is not available

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET32b

Entity Sequences (FASTA):
KIR3DL1-cyto: GSGMKETAAAKFERQDMDSP DLGTDDDDKAMEFHLWCSNK KNAAVMDQEPAGNRTANSED SDEQDPEEVTYAQLDHCVFT QRKITRPSQRPKTPPTDTIL YTELPNAKPRSKVVSCP

Data sets:
Data typeCount
13C chemical shifts392
15N chemical shifts99

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1KIR3DL1-cyto1

Entities:

Entity 1, KIR3DL1-cyto 117 residues - Formula weight is not available

1   GLYSERGLYMETLYSGLUTHRALAALAALA
2   LYSPHEGLUARGGLNASPMETASPSERPRO
3   ASPLEUGLYTHRASPASPASPASPLYSALA
4   METGLUPHEHISLEUTRPCYSSERASNLYS
5   LYSASNALAALAVALMETASPGLNGLUPRO
6   ALAGLYASNARGTHRALAASNSERGLUASP
7   SERASPGLUGLNASPPROGLUGLUVALTHR
8   TYRALAGLNLEUASPHISCYSVALPHETHR
9   GLNARGLYSILETHRARGPROSERGLNARG
10   PROLYSTHRPROPROTHRASPTHRILELEU
11   TYRTHRGLULEUPROASNALALYSPROARG
12   SERLYSVALVALSERCYSPRO

Samples:

sample_1: KIR3DL1-cyto, [U-100% 13C; U-100% 15N], 1 mM; HEPES 20 mM; sodium chloride 20 mM; EDTA 3 mM; DTT 3 mM

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
CONsample_1isotropicsample_conditions_1
CANCOsample_1isotropicsample_conditions_1
CANCOisample_1isotropicsample_conditions_1
CBCACOsample_1isotropicsample_conditions_1
CBCANCOsample_1isotropicsample_conditions_1
CCCONsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

SPARKY v3.134, Goddard - chemical shift assignment

Felix v2007, Accelrys Software Inc. - processing

NMR spectrometers:

  • Bruker Avance 600 MHz