BMRB Entry 15512

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PDB ID: 2lqr
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15512
MolProbity Validation Chart

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Title:
1H, 13C, and 15N NMR chemical shift assignments of the palladin Ig3 domain
Deposition date:
2007-10-08
Original release date:
2008-03-31
Authors:
Dixon, Richard; Rachlin, Andrew; Otey, Carol; Campbell, Sharon
Citation:

Citation: Dixon, Richard; Campbell, Sharon. "1H, 15N, and 13C NMR chemical shift assignments for the Ig3 domain of palladin"  Biomol. NMR Assignments 2, 51-53 (2008).
PubMed: 19636923

Assembly members:

Assembly members:
Palladin_Ig3_domain, polymer, 108 residues, 11975 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pMAL-c2x

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Palladin_Ig3_domain: GGSNATAPFFEMKLKHYKIF EGMPVTFTCRVAGNPKPKIY WFKDGKQISPKSDHYTIQRD LDGTCSLHTTASTLDDDGNY TIMAANPQGRVSCTGRLMVQ AVNQRGRS

Data sets:
Data typeCount
13C chemical shifts455
15N chemical shifts112
1H chemical shifts701

Additional metadata:

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Assembly:

Entity Assembly IDEntity NameEntity ID
1molecule 11

Entities:

Entity 1, molecule 1 108 residues - 11975 Da.

Residues 1-3 are non-native amino acids resulting from the cloning and purification strategy

1   GLYGLYSERASNALATHRALAPROPHEPHE
2   GLUMETLYSLEULYSHISTYRLYSILEPHE
3   GLUGLYMETPROVALTHRPHETHRCYSARG
4   VALALAGLYASNPROLYSPROLYSILETYR
5   TRPPHELYSASPGLYLYSGLNILESERPRO
6   LYSSERASPHISTYRTHRILEGLNARGASP
7   LEUASPGLYTHRCYSSERLEUHISTHRTHR
8   ALASERTHRLEUASPASPASPGLYASNTYR
9   THRILEMETALAALAASNPROGLNGLYARG
10   VALSERCYSTHRGLYARGLEUMETVALGLN
11   ALAVALASNGLNARGGLYARGSER

Related Database Links:

PDB 2DM2 2LQR
GB EDL28653 EDL28654

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