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Biological Magnetic Resonance Data Bank


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BMRB Entry 16991

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16991
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Title: Solution NMR Structure of the N-terminal Domain of Putative ATP-dependent DNA Helicase RecG-related Protein from Nitrosomonas europaea, Northeast Structural Genomics Consortium Target NeR70A

Deposition date: 2010-06-09 Original release date: 2010-08-10

Authors: Eletsky, Alexander; Mills, Jeffrey; Lee, Hsiau-Wei; Maglaqui, Melissa; Ciccosanti, Colleen; Hamilton, Keith; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Prestegard, James; Szyperski, Thomas

Citation: Eletsky, Alexander; Mills, Jeffrey; Lee, Hsiau-Wei; Maglaqui, Melissa; Ciccosanti, Colleen; Hamilton, Keith; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Prestegard, James; Szyperski, Thomas. "Solution NMR Structure of the N-terminal Domain of Putative ATP-dependent DNA Helicase RecG-related Protein from Nitrosomonas europaea"  To be published ., .-..

Assembly members:
NeR70A, polymer, 153 residues, 16781.168 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):
NeR70A: MRSATDLLDELNAVDESARI EAKRASDMGKSVMETVIAFA NEPGLDGGYLLLGVDWAIND KGDTVYRPVGLPDPDKVQRD LASQCASMLNVALRPEMQLE QVGGKTLLVVYVPEADVTHK PIYKKATGLPGGAYRRIGSS DQRCVLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts642
15N chemical shifts153
1H chemical shifts1032
residual dipolar couplings103

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NeR70A1

Entities:

Entity 1, NeR70A 153 residues - 16781.168 Da.

Residues 1-145 correspond to the native protein. Residues 146-153 represent a non-native affinity tag.

1   METARGSERALATHRASPLEULEUASPGLU
2   LEUASNALAVALASPGLUSERALAARGILE
3   GLUALALYSARGALASERASPMETGLYLYS
4   SERVALMETGLUTHRVALILEALAPHEALA
5   ASNGLUPROGLYLEUASPGLYGLYTYRLEU
6   LEULEUGLYVALASPTRPALAILEASNASP
7   LYSGLYASPTHRVALTYRARGPROVALGLY
8   LEUPROASPPROASPLYSVALGLNARGASP
9   LEUALASERGLNCYSALASERMETLEUASN
10   VALALALEUARGPROGLUMETGLNLEUGLU
11   GLNVALGLYGLYLYSTHRLEULEUVALVAL
12   TYRVALPROGLUALAASPVALTHRHISLYS
13   PROILETYRLYSLYSALATHRGLYLEUPRO
14   GLYGLYALATYRARGARGILEGLYSERSER
15   ASPGLNARGCYSVALLEUGLUHISHISHIS
16   HISHISHIS

Samples:

NC: NeR70A, [U-100% 13C; U-100% 15N], 0.9 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02%; H2O 95%; D2O 5%

NC5: NeR70A, [U-5% 13C; U-100% 15N], 0.9 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02%; H2O 95%; D2O 5%

NC5-phage: NeR70A, [U-5% 13C; U-100% 15N], 0.6 mM; MES 13 mM; sodium chloride 66 mM; calcium chloride 3.3 mM; DTT 6.6 mM; sodium azide 0.013%; Pf1 phage 13.5 mg/ml; H2O 88%; D2O 12%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC aliphaticNCisotropicsample_conditions_1
3D HNCONCisotropicsample_conditions_1
3D CBCA(CO)NHNCisotropicsample_conditions_1
3D HNCACBNCisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticNCisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC aromaticNCisotropicsample_conditions_1
3D HN(CA)CONCisotropicsample_conditions_1
3D HBHA(CO)NHNCisotropicsample_conditions_1
3D HCCH-COSY aliphaticNCisotropicsample_conditions_1
3D HCCH-TOCSY aliphaticNCisotropicsample_conditions_1
3D HCCH-COSY aromaticNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC methylNC5isotropicsample_conditions_1
2D 1H-15N LR-HSQC (Histidine)NCisotropicsample_conditions_1
2D 1H-15N J-modulated HSQCNC5isotropicsample_conditions_1
2D 1H-15N J-modulated HSQCNC5-phageanisotropicsample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinemen, structure solution

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

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis, refinement

AutoAssign v2.3, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis

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

XEASY v1.3.13, Bartels et al. - data analysis

TOPSPIN v2.1, Bruker Biospin - collection

VNMRJ v2.1B, Varian - collection

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

TALOS+ v1.2009.0721.18, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PROSA v6.4, Guntert - processing

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
EMBL CAD86437
GB ABM43720 EPZ14923 ESQ97118
REF WP_011112980 WP_011806704 WP_021250010 WP_023446977 WP_033977893

Download simulated HSQC data in one of the following formats:
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