BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16312

Title: Solution NMR structure of a domain from a putative phage integrase protein Nmul_A0064 from Nitrosospira multiformis, Northeast Structural Genomics Consortium Target NmR46C.

Deposition date: 2009-05-21 Original release date: 2009-06-11

Authors: Mills, Jeffrey; Eletsky, Alexander; Ghosh, Arindam; Wang, Dongyang; Lee, Hsiau-Wei; Ciccosanti, Colleen; Jiang, Mei; Nair, R.; Rost, Burkhard; Swapna, G. V. T.; Acton, Thomas; Xiao, Rong; Everett, John; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas

Citation: Mills, Jeffrey. "Solution NMR structure of a domain from a putative phage integrase protein Nmul_A0064 from Nitrosospira multiformis, Northeast Structural Genomics Consortium Target NmR46C."  Not known ., .-..

Assembly members:
NmR46C, polymer, 116 residues, 13400.581 Da.

Natural source:   Common Name: Nitrosospira multiformis   Taxonomy ID: 1231   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Nitrosospira multiformis

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

Entity Sequences (FASTA):
NmR46C: MAEKNAYTVAQLADEYFERM IAGRWKHPNIVRSRIEKDIK PAIGSLKVEDVKPRHIDDVL KAVMKRGAPSIANDTLRWLK RMFNYAIKRHIIEYNPAAAF DPGDAGGKLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts392
15N chemical shifts124
1H chemical shifts830
residual dipolar couplings72

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NmR46C1

Entities:

Entity 1, NmR46C 116 residues - 13400.581 Da.

L46 is a sequence variation; Please add a "remark 999"

1   METALAGLULYSASNALATYRTHRVALALA
2   GLNLEUALAASPGLUTYRPHEGLUARGMET
3   ILEALAGLYARGTRPLYSHISPROASNILE
4   VALARGSERARGILEGLULYSASPILELYS
5   PROALAILEGLYSERLEULYSVALGLUASP
6   VALLYSPROARGHISILEASPASPVALLEU
7   LYSALAVALMETLYSARGGLYALAPROSER
8   ILEALAASNASPTHRLEUARGTRPLEULYS
9   ARGMETPHEASNTYRALAILELYSARGHIS
10   ILEILEGLUTYRASNPROALAALAALAPHE
11   ASPPROGLYASPALAGLYGLYLYSLEUGLU
12   HISHISHISHISHISHIS

Samples:

NC: NmR46C, [U-98% 13C; U-98% 15N], 1.2 mM; D2O 10%; H2O 90%; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; protease inhibitors 1x v/v; sodium azide 0.02%

NC5: NmR46C, [U-5% 13C; U-98% 15N], 1.2 mM; D2O 10%; H2O 90%; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; protease inhibitors 1x v/v; sodium azide 0.02%

NC5ani: NmR46C, [U-5% 13C; U-98% 15N], 1.2 mM; D2O 10%; H2O 90%; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; protease inhibitors 1x v/v; sodium azide 0.02%

sample_conditions_1: ionic strength: 430 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D 1H-13C HSQCNCisotropicsample_conditions_1
2D 1H-13C HSQCNC5isotropicsample_conditions_1
3D sim 15N,13C NOESYNCisotropicsample_conditions_1
3D HNCONCisotropicsample_conditions_1
(4,3)D HNCABCANCisotropicsample_conditions_1
GFT (4,3)D CABCA(CO)NHNCisotropicsample_conditions_1
GFT (4,3)D HABCAB(CO)NHNCisotropicsample_conditions_1
GFT (4,3)D arom. HCCHNCisotropicsample_conditions_1
GFT (4,3)D aliph. HCCHNCisotropicsample_conditions_1
2D 1H-15N HSQCNC5anianisotropicsample_conditions_1
2D 1H-15N TROSYNC5anianisotropicsample_conditions_1

Software:

VNMRJ, Varian - collection

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

SPSCAN, Glaser - processing

XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, refinement, structure solution

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

Molmol, Koradi, Billeter and Wuthrich - data analysis, refinement, structure solution

AutoStruct, Huang, Tejero, Powers and Montelione - chemical shift assignment, refinement, structure solution

PSVS, Bhattacharya and Montelione - refinement

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
GB ABB73373
REF WP_011379428

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