BMRB Entry 6106

Name: NMR structure of cross-reactive peptides from Homo sapiens
Published: 2004-04-06

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PDB ID: 1s4j
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR6106
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: NMR structure of cross-reactive peptides from Homo sapiens PubMed: 14988012

Deposition date: 2004-02-19 Original release date: 2004-04-06

Authors: Soares, M.; Bisch, P.; Campos de Carvalho, A.; Valente, A.; Almeida, F.

Citation: Soares, M.; Bisch, P.; Campos de Carvalho, A.; Valente, A.; Almeida, F.. "Correlation between conformation and antibody binding: NMR structure of cross-reactive peptides from T. cruzi, Human and L. braziliensis" FEBS Lett. 560, 134-140 (2004).

Assembly members:
60S acidic ribosomal protein P2, polymer, 13 residues, Formula weight is not available

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):
60S acidic ribosomal protein P2: EESDDDMGFGLFD

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1

Data type	Count
1H chemical shifts	61

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	60S acidic ribosomal protein P2	1

Entities:

Entity 1, 60S acidic ribosomal protein P2 13 residues - Formula weight is not available

1

GLU

SER

ASP

MET

GLY

PHE

GLY

2

LEU

PHE

ASP

Samples:

sample_1: 60S acidic ribosomal protein P2 2 mM; phosphate buffer 10 mM; H2O 90%; D2O 10%

sample_cond_1: ionic strength: 10 mM; pH: 5.5; pressure: 1 atm; temperature: 278 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D NOESY	sample_1	not available	sample_cond_1
2D TOCSY	sample_1	not available	sample_cond_1

Software:

NMRPipe v2.1 - processing

NMRView v5.03 - data analysis

CNS v1.1 - refinement, structure solution

NMR spectrometers:

Bruker DRX 400 MHz