BMRB

Biological Magnetic Resonance Data Bank


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BMRB Entry 16737

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PDB ID:
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
MolProbity Validation Chart

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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:
Data typeCount
13C chemical shifts590
15N chemical shifts157
1H chemical shifts1020
heteronuclear NOE values103

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1NMB13431

Entities:

Entity 1, NMB1343 153 residues - Formula weight is not available

C terminal residues LEHHHHHH are purification tag

1   METGLYASNPHELEUTYRARGGLYILESER
2   CYSGLNGLNASPGLUGLNASNASNGLYGLN
3   LEULYSPROLYSGLYASNLYSALAGLUVAL
4   ALAILEARGTYRASPGLYLYSPHELYSTYR
5   ASPGLYLYSALATHRHISGLYPROSERVAL
6   LYSASNALAVALTYRALAHISGLNILEGLU
7   THRGLYLEUTYRASPGLYCYSTYRILESER
8   THRTHRTHRASPLYSGLUILEALALYSLYS
9   PHEALATHRSERSERGLYILEGLUASNGLY
10   TYRILETYRVALLEUASNARGASPLEUPHE
11   GLYGLNTYRSERILEPHEGLUTYRGLUVAL
12   GLUHISPROGLUASNPROASNGLULYSGLU
13   VALTHRILEARGALAGLUASPCYSGLYCYS
14   ILEPROGLUGLUVALILEILEALALYSGLU
15   LEUILEGLUILEASNLEUGLUHISHISHIS
16   HISHISHIS

Samples:

sample_1: NMB1343, [U-100% 15N], 0.3 mM; sodium chloride 75 mM; sodium phosphate 25 mM; sodium azide 0.01%; TSP 0.5 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_2: NMB1343, [U-100% 13C; U-100% 15N], 0.6 mM; sodium chloride 75 mM; sodium phosphate 25 mM; sodium azide 0.01%; TSP 0.5 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_3: NMB1343, [U-100% 13C; U-100% 15N], 0.8 mM; sodium chloride 75 mM; sodium phosphate 25 mM; sodium azide 0.01%; TSP 0.5 mM; DTT 1 mM; D2O 100%

sample_conditions_1: pH: 7.3; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
2D 1H-1H TOCSYsample_3isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-15N HSQC T1 editedsample_1isotropicsample_conditions_1
2D 1H-15N HSQC T2 editedsample_1isotropicsample_conditions_1
2D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

TALOS, Cornilescu, Delaglio and Bax - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Oxford Instruments Avance 750 MHz
  • Bruker Avance 600 MHz

Related Database Links:

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

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts