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Biological Magnetic Resonance Data Bank


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BMRB Entry 16560

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16560
MolProbity Validation Chart

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Title: Solution NMR Structure of uncharacterized protein from gene locus NE0665 of Nitrosomonas europaea. Northeast Structural Genomics Target NeR103A

Deposition date: 2009-10-16 Original release date: 2010-01-07

Authors: Rossi, Paolo; Belote, Rachel; Jiang, Mei; Xiao, Rong; Ciccosanti, Colleen; Acton, Thomas; Everett, John; Rost, Burkhard; Montelione, Gaetano

Citation: Rossi, Paolo; Xiao, Rong; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano. "Solution NMR Structure of uncharacterized protein from gene locus NE0665 of Nitrosomonas europaea. Northeast Structural Genomics Target NeR103A"  Not known ., .-..

Assembly members:
protein from gene locus NE0665, polymer, 105 residues, 11939.455 Da.

Natural source:   Common Name: N. europaea   Taxonomy ID: 915   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Nitrosomonas europaea

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

Entity Sequences (FASTA):
protein from gene locus NE0665: MDQKSSSPQPAAQAPETKQA FPRKFVLAALEQSSDDAGWA NLGNFGNYLNKLQPDFDSRL YGYKKLSDLVKARTDLFVTE ERQVPGSTQKALYLRAKLEH HHHHH

Data typeCount
13C chemical shifts405
15N chemical shifts98
1H chemical shifts632

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1protein from gene locus NE06651

Entities:

Entity 1, protein from gene locus NE0665 105 residues - 11939.455 Da.

1   METASPGLNLYSSERSERSERPROGLNPRO
2   ALAALAGLNALAPROGLUTHRLYSGLNALA
3   PHEPROARGLYSPHEVALLEUALAALALEU
4   GLUGLNSERSERASPASPALAGLYTRPALA
5   ASNLEUGLYASNPHEGLYASNTYRLEUASN
6   LYSLEUGLNPROASPPHEASPSERARGLEU
7   TYRGLYTYRLYSLYSLEUSERASPLEUVAL
8   LYSALAARGTHRASPLEUPHEVALTHRGLU
9   GLUARGGLNVALPROGLYSERTHRGLNLYS
10   ALALEUTYRLEUARGALALYSLEUGLUHIS
11   HISHISHISHISHIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.957 mM; sodium chloride 200 mM; MES 20 mM; DTT 10 mM; sodium azide 0.02%; Calcium Chloride 5 mM; DSS 50 uM; D2O 10%; H2O 90%

sample_2: entity, [U-5% 13C; U-100% 15N], 0.9 mM; sodium chloride 200 mM; MES 20 mM; DTT 10 mM; sodium azide 0.02%; Calcium Chloride 5 mM; DSS 50 uM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
het-NOEsample_2isotropicsample_conditions_1
T1-pseudo2Dsample_2isotropicsample_conditions_1
T2CPMG-pseudo2Dsample_2isotropicsample_conditions_1
high-resC13-HSQCsample_2isotropicsample_conditions_1
1D presat referencingsample_1isotropicsample_conditions_1
1D presat referencingsample_1isotropicsample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.112, Goddard - data analysis

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

TALOS v+, Shen,Cornilescu, Delaglio and Bax - geometry optimization

PSVS v1.3, Bhattacharya and Montelione - validation

TOPSPIN v2.1, Bruker Biospin - collection

PyMol v1.2, delano scientific - visualization

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
EMBL CAD84576
REF WP_011111286

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