BMRB Entry 6769

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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/BMR6769
MolProbity Validation Chart

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Title:
Complete assignments of a hypothetical protein NE2066, from Nitrosomonas_europaea. Northeast Structural Genomics Consortium Target NeT1.
Deposition date:
2005-08-10
Original release date:
2007-02-06
Authors:
Srisailam, Sampath; Yee, Adelinda; Lukin, Jonathan; Semesi, Anthony; Arrowsmith, Cheryl
Citation:

Citation: Srisailam, Sampath; Lukin, Jonathan; Yee, Adelinda; Semesi, Anthony; Arrowsmith, Cheryl. "Solution structure of acyl carrier protein from Nitrosomonas europaea."  Proteins 64, 800-803 (2006).
PubMed: 16741959

Assembly members:

Assembly members:
NE2066, polymer, 83 residues, 9169.3 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NE2066: MQHLEAVRNILGDVLNLGER KHTLTASSVLLGNIPELDSM AVVNVITALEEYFDFSVDDD EISAQTFETLGSLALFVEHK LSH

Data sets:
Data typeCount
13C chemical shifts348
15N chemical shifts83
1H chemical shifts577

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1protein1

Entities:

Entity 1, protein 83 residues - 9169.3 Da.

1   METGLNHISLEUGLUALAVALARGASNILE
2   LEUGLYASPVALLEUASNLEUGLYGLUARG
3   LYSHISTHRLEUTHRALASERSERVALLEU
4   LEUGLYASNILEPROGLULEUASPSERMET
5   ALAVALVALASNVALILETHRALALEUGLU
6   GLUTYRPHEASPPHESERVALASPASPASP
7   GLUILESERALAGLNTHRPHEGLUTHRLEU
8   GLYSERLEUALALEUPHEVALGLUHISLYS
9   LEUSERHIS

Samples:

sample_1: protein, [U-15N; U-13C], 1 ± 0.2 mM; MOPS 10 ± 0.1 mM; NaCl 450 ± 0.1 mM; DTT 10 ± 0.1 mM; Zinc Sulfate 10 ± 0.1 uM; Benzamidine 1 ± 0.1 mM; Sodium azide 0.01 ± 0.1 %; D2O 5 ± 1 %

conditions_1: ionic strength: 0.45 M; pH: 6.5; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1H15N_HSQCsample_1not availableconditions_1
HNCOsample_1not availableconditions_1
HNcaCOsample_1not availableconditions_1
CBCAcoNHsample_1not availableconditions_1
HNCAsample_1not availableconditions_1
HNcoCAsample_1not availableconditions_1
HBHAcoNHsample_1not availableconditions_1
CCTOCSY_NHsample_1not availableconditions_1
HCCTOCSY_NHsample_1not availableconditions_1
13C HSQCsample_1not availableconditions_1
HCCHCOSYsample_1not availableconditions_1
HCCH-TOCSYsample_1not availableconditions_1
15N NOESYsample_1not availableconditions_1
13C NOESYsample_1not availableconditions_1
HNCBsample_1not availableconditions_1

Software:

SPARKY v3.106 -

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 17995
PDB
EMBL CAD86074
REF NP_842167 WP_011112661

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks