BMRB Entry 16737

Name: 1H,13C and 15N chemical shift assignment for NMB1343 apoprotein
Published: 2011-05-20

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PDB ID: 2kxi
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16737
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: 1H,13C and 15N chemical shift assignment for NMB1343 apoprotein PubMed: 21367854

Deposition date: 2010-02-19 Original release date: 2011-05-20

Authors: Koehler, Christian; Carlier, Ludovic; Veggi, Daniele; Soriani, Marco; Pizza, Mariagrazia; Boelens, Rolf; Bonvin, Alexandre

Citation: Koehler, Christian; Carlier, Ludovic; Veggi, Daniele; Balducci, Enrico; Di Marcello, Federica; Ferrer-Navarro, Mario; Pizza, Mariagrazia; Daura, Xavier; Soriani, Marco; Boelens, Rolf; Bonvin, Alexandre M J J. "Structural and Biochemical Characterization of NarE, an Iron-containing ADP-ribosyltransferase from Neisseria meningitidis." J. Biol. Chem. 286, 14842-14851 (2011).

Assembly members:
NMB1343, polymer, 153 residues, Formula weight is not available

Natural source: Common Name: Neisseria meningitidis Taxonomy ID: 487 Superkingdom: Bacteria Kingdom: not available Genus/species: Neisseria meningitidis

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

Entity Sequences (FASTA):
NMB1343: MGNFLYRGISCQQDEQNNGQ LKPKGNKAEVAIRYDGKFKY DGKATHGPSVKNAVYAHQIE TGLYDGCYISTTTDKEIAKK FATSSGIENGYIYVLNRDLF GQYSIFEYEVEHPENPNEKE VTIRAEDCGCIPEEVIIAKE LIEINLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
heteronucl_NOEs
- heteronuclear_noe_list_1
heteronucl_T1_relaxation
- heteronuclear_T1_list_1
heteronucl_T2_relaxation
- heteronuclear_T2_list_1

Data type	Count
13C chemical shifts	590
15N chemical shifts	157
1H chemical shifts	1020
heteronuclear NOE values	103

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HN(CA)CO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_3	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC T1 edited	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC T2 edited	sample_1	isotropic	sample_conditions_1
2D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

PDB	2KXI
EMBL	CCI72935
GB	AAF41718 ADO31780 ADY97402 ADZ03753 AJC62209
REF	NP_274362 WP_002219146 WP_016687434 WP_029670159 WP_039637683

Biological Magnetic Resonance Data Bank

BMRB Entry 16737

Title: 1H,13C and 15N chemical shift assignment for NMB1343 apoprotein PubMed: 21367854

Additional metadata:

Assembly:

Entities:

Samples:

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Software:

NMR spectrometers:

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