2NAN

NMR structure of human DCL-1 (CD302) extracellular domain

> Summary

Summary for 2NAN

DescriptorCD302 antigen
Functional Keywordsc-type lectin like receptor, immune system
Biological sourceHomo sapiens (human)
Cellular locationMembrane ; Single-pass type I membrane protein  Q8IX05
Total number of polymer chains1
Total molecular weight16228.08
Authors
Pospisilova, E.,Kukacka, Z.,Kavan, D.,Novak, P.,Chmelik, J. (deposition date: 2016-01-06, release date: 2017-01-11)
Primary citation
Pospisilova, E.,Kukacka, Z.,Kavan, D.,Novak, P.,Chmelik, J.
NMR structure of human DCL-1 (CD302) extracellular domain
To be Published,
Experimental method
SOLUTION NMR
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Structure validation

ClashscoreRamachandran outliersSidechain outliers241.1%12.5%MetricValuePercentile RanksWorseBetterPercentile relative to all structuresPercentile relative to all NMR structures

More Asymmetric unit images

Molmil generated image of 2nan
no rotation
Molmil generated image of 2nan
rotated about x axis by 90°
Molmil generated image of 2nan
rotated about y axis by 90°

> Structural details

Entity

Chain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
ACD302 antigenpolymer14016228.11
UniProt (Q8IX05)
Pfam (PF00059)
Homo sapiens (human)C-type lectin BIMLEC, C-type lectin domain family 13 member A, DEC205-associated C-type lectin 1, Type I transmembrane C-type lectin receptor DCL-1

Sequence viewer

Contents of the asymmetric unit

PolymersNumber of chains1
Total molecular weight16228.1
Non-Polymers*Number of molecules0
Total molecular weight0.0
All*Total molecular weight16228.1
*Water molecules are not included.

> Experimental details

Spectrometer

Experimental method:SOLUTION NMR

Spectrometer IDSpectrometer makerSpectrometer modelSpectrometer typeSpectrometer field strength
1BrukerAvance IIIBruker Avance III600

Experiment

experiment idconditions idsolution idExperiment type
1112D 1H-15N HSQC
2113D HNCO
3113D HN(CA)CO
4113D HNCA
5113D HN(CO)CA
6113D HNCACB
7113D CBCA(CO)NH
8112D 1H-13C HSQC aliphatic
9112D 1H-13C HSQC aromatic
10113D 1H-15N NOESY
11113D 1H-13C NOESY aliphatic
12113D 1H-13C NOESY aromatic
13113D 1H-15N TOCSY
14113D H(CC)(CO)NH
15113D (H)CC(CO)NH
16112D (HB)CB(CGCD)HD
17113D HCCH-TOCSY
18113D HCCH-TOCSY aromatic

NMR Sample

conditions idNMR sample pHNMR sample pressureNMR sample temperature
16.51303.15

Conformers

Conformers Calculated Total Number500
Conformers Submitted Total Number10

> Functional details

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Functional Information from GO Data

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Functional Information from PDB Data

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Functional Information from PDB atom coordinates for the "HETATM" binding sites

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Functional Information from PROSITE/UniProt

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Functional Information from SwissProt/UniProt

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Catalytic Information from CSA

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> Sequence Neighbor

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