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 16382

Title: Solution NMR structure of the Rhodanese-like domain from Anabaena sp Alr3790 protein. Northeast Structural Genomics Consortium Target NsR437A

Deposition date: 2009-06-30 Original release date: 2009-09-15

Authors: Eletsky, Alexander; Belote, Rachel; Ciccosanti, Colleen; Janjua, Haleema; Nair, Rajesh; Rost, Burkhard; Swapna, G.; Acton, Thomas; Xiao, Rong; Everett, John; Lee, Hsiau-Wei; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas

Citation: Eletsky, Alexander; Belote, Rachel; Ciccosanti, Colleen; Janjua, Haleema; Nair, Rajesh; Rost, Burkhard; Swapna, G.; Acton, Thomas; Xiao, Rong; Everett, John; Lee, Hsiau-Wei; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR structure of the Rhodanese-like domain from Anabaena sp Alr3790 protein. Northeast Structural Genomics Consortium Target NsR437A"  Proteins: Struct. Funct. Genet. ., .-..

Assembly members:
Alr3790, polymer, 132 residues, 14539.188 Da.

Natural source:   Common Name: Anabaena sp.   Taxonomy ID: 1167   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Anabaena sp.

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

Entity Sequences (FASTA):
Alr3790: MEPQSDAHVLKSRLEWGEPA FTILDVRDRSTYNDGHIMGA MAMPIEDLVDRASSSLEKSR DIYVYGAGDEQTSQAVNLLR SAGFEHVSELKGGLAAWKAI GGPTEGIIESRTPAGADDYN VVSRLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts534
15N chemical shifts143
1H chemical shifts857

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Alr37901

Entities:

Entity 1, Alr3790 132 residues - 14539.188 Da.

Residues 2-124 correspond to the native residues 17-139. Residue 1 corresponds to the new start codon. Residues 125-132 represent a non-native affinity tag.

1   METGLUPROGLNSERASPALAHISVALLEU
2   LYSSERARGLEUGLUTRPGLYGLUPROALA
3   PHETHRILELEUASPVALARGASPARGSER
4   THRTYRASNASPGLYHISILEMETGLYALA
5   METALAMETPROILEGLUASPLEUVALASP
6   ARGALASERSERSERLEUGLULYSSERARG
7   ASPILETYRVALTYRGLYALAGLYASPGLU
8   GLNTHRSERGLNALAVALASNLEULEUARG
9   SERALAGLYPHEGLUHISVALSERGLULEU
10   LYSGLYGLYLEUALAALATRPLYSALAILE
11   GLYGLYPROTHRGLUGLYILEILEGLUSER
12   ARGTHRPROALAGLYALAASPASPTYRASN
13   VALVALSERARGLEUGLUHISHISHISHIS
14   HISHIS

Samples:

NC5_peg: nsr437a, [U-2% 13C; U-100% 15N], 0.7 mM; MES 16 mM; sodium chloride 160 mM; calcium chloride 4 mM; DSS 40 uM; sodium azide 0.016%; PEG 4.2%; H2O 88%; D2O 12%

NC: nsr437a, [U-100% 13C; U-100% 15N], 1 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DSS 50 uM; sodium azide 0.02%; H2O 90%; D2O 10%

NC5: nsr437a, [U-2% 13C; U-100% 15N], 1 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DSS 50 uM; sodium azide 0.02%; H2O 90%; D2O 10%

NC5_phage: nsr437a, [U-2% 13C; U-100% 15N], 0.7 mM; MES 14.4 mM; sodium chloride 144 mM; calcium chloride 3.6 mM; DSS 36 uM; sodium azide 0.014%; Pf1 phage 13.25 g/l; H2O 87%; D2O 13%

iso: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

phage: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

peg: ionic strength: 160 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1D 15N T1NCisotropiciso
1D 15N T2NCisotropiciso
2D 1H-15N HSQCNCisotropiciso
2D 1H-13C HSQC aliphaticNCisotropiciso
2D 1H-13C CT-HSQC aliphaticNCisotropiciso
2D 1H-13C CT-HSQC aromaticNCisotropiciso
3D HNCONCisotropiciso
3D HN(CA)CONCisotropiciso
3D CBCA(CO)NHNCisotropiciso
3D HNCACBNCisotropiciso
3D HBHA(CO)NHNCisotropiciso
3D (H)CCH-TOCSY aliphaticNCisotropiciso
3D (H)CCH-COSY aliphaticNCisotropiciso
3D (H)CCH-COSY aromaticNCisotropiciso
3D 1H-15N/13C NOESYNCisotropiciso
2D 1H-15N HSQC long-range (His)NC5isotropiciso
2D 1H-13C CT-HSQC methylNC5isotropiciso
2D 1H-15N HSQCNC5isotropiciso
2D 1H-15N TROSYNC5isotropiciso
2D 1H-15N HSQCNC5_phageanisotropicphage
2D 1H-15N TROSYNC5_phageanisotropicphage
2D 1H-15N HSQCNC5_peganisotropicpeg
2D 1H-15N TROSYNC5_peganisotropicpeg
2D CLEANEXNCisotropiciso

Software:

VNMRJ v2.1B, Varian - collection

PROSA v6.4, Guntert - processing

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

ANALYSIS v2.0.7, CCPN - chemical shift assignment, data analysis, peak picking

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

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

AutoStruct, Huang, Tejero, Powers and Montelione - structure solution

TALOS v2007.068.09.07, Cornilescu, Delaglio and Bax - data analysis

CNS v1.2.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

PSVS v1.3, Bhattacharya and Montelione - validation

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB

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