+Open data
-Basic information
Entry | Database: PDB / ID: 2m94 | ||||||
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Title | NMR structure of the lymphocyte receptor NKR-P1A | ||||||
Components | Killer cell lectin-like receptor subfamily B member 1A | ||||||
Keywords | IMMUNE SYSTEM RECEPTOR / NK cells / NK receptor / NKR-P1A / C-type lectin-like domain / IMMUNORECEPTOR | ||||||
Function / homology | Function and homology information regulation of natural killer cell mediated cytotoxicity / signaling receptor activity / carbohydrate binding / cell surface / plasma membrane Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Chmelik, J. / Rozbesky, D. / Pospisilova, E. / Novak, P. | ||||||
Citation | Journal: To be Published Title: NMR structure of the lymphocyte receptor NKR-P1A reveals a different conformation of the conserved loop compared to crystal structure Authors: Rozbesky, D. / Pospisilova, E. / Novak, P. / Chmelik, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2m94.cif.gz | 425.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2m94.ent.gz | 355.5 KB | Display | PDB format |
PDBx/mmJSON format | 2m94.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2m94_validation.pdf.gz | 534 KB | Display | wwPDB validaton report |
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Full document | 2m94_full_validation.pdf.gz | 654.3 KB | Display | |
Data in XML | 2m94_validation.xml.gz | 44.7 KB | Display | |
Data in CIF | 2m94_validation.cif.gz | 50.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/m9/2m94 ftp://data.pdbj.org/pub/pdb/validation_reports/m9/2m94 | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 16008.773 Da / Num. of mol.: 1 / Fragment: UNP residues 95-233 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Klrb1a / Plasmid: pET-30a(+) / Production host: Escherichia coli (E. coli) / References: UniProt: G5E882, UniProt: P27811*PLUS |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.5 mM [U-100% 13C; U-100% 15N] NKR-P1A, 15 mM PIPES, 50 mM sodium chloride, 1 mM sodium azide, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||
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Sample |
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Sample conditions | pH: 6.8 / Pressure: ambient / Temperature: 303 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 2466 / NOE intraresidue total count: 1124 / NOE long range total count: 641 / NOE medium range total count: 216 / NOE sequential total count: 485 / Hydrogen bond constraints total count: 60 / Protein chi angle constraints total count: 55 / Protein phi angle constraints total count: 91 / Protein psi angle constraints total count: 91 | ||||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 10 / Maximum lower distance constraint violation: 0.5 Å / Maximum torsion angle constraint violation: 5 ° / Maximum upper distance constraint violation: 0.5 Å | ||||||||||||||||||||||||||||||||||||||||
NMR ensemble rms | Distance rms dev: 0.01599454 Å / Distance rms dev error: 0.00086912 Å |