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Biological Magnetic Resonance Data Bank


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BMRB Entry 16388

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16388
MolProbity Validation Chart

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Title: NMR Solution structure of a diflavin flavoprotein A3 from Nostoc sp. PCC 7120, Northeast Structural Genomics Consortium Target NsR431C

Deposition date: 2009-06-30 Original release date: 2009-08-06

Authors: Swapna, G.V.T.; Ciccosanti, Colleen; Wang, Dongyan; Jiang, Mei; Xiao, Rong; Acton, Thomas; Everett, John; Nair, R.; Montelione, Gaetano

Citation: Swapna, G.V.T.; Ciccosanti, Colleen; Wang, Dongyan; Jiang, Mei; Xiao, Rong; Acton, Thomas; Everett, John; Nair, R.; Montelione, Gaetano. "NMR Solution structure of a diflavin flavoprotein A3 from Nostoc sp. PCC 7120, Northeast Structural Genomics Consortium Target NsR431C"  To be Published ., .-..

Assembly members:
NsR431C, polymer, 154 residues, 16475.629 Da.

Natural source:   Common Name: Nostoc sp. PCC 7120   Taxonomy ID: 103690   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Nostoc sp. PCC 7120

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: BL21

Entity Sequences (FASTA):
NsR431C: SIGVFYVSEYGYSDRLAQAI INGITKTGVGVDVVDLGAAV DLQELRELVGRCTGLVIGMS PAASAASIQGALSTILGSVN EKQAVGIFETGGGDDEPIDP LLSKFRNLGLTTAFPAIRIK QTPTENTYKLCEEAGTDLGQ WVTRDRLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts612
15N chemical shifts154
1H chemical shifts1014

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NsR431C1

Entities:

Entity 1, NsR431C 154 residues - 16475.629 Da.

1   SERILEGLYVALPHETYRVALSERGLUTYR
2   GLYTYRSERASPARGLEUALAGLNALAILE
3   ILEASNGLYILETHRLYSTHRGLYVALGLY
4   VALASPVALVALASPLEUGLYALAALAVAL
5   ASPLEUGLNGLULEUARGGLULEUVALGLY
6   ARGCYSTHRGLYLEUVALILEGLYMETSER
7   PROALAALASERALAALASERILEGLNGLY
8   ALALEUSERTHRILELEUGLYSERVALASN
9   GLULYSGLNALAVALGLYILEPHEGLUTHR
10   GLYGLYGLYASPASPGLUPROILEASPPRO
11   LEULEUSERLYSPHEARGASNLEUGLYLEU
12   THRTHRALAPHEPROALAILEARGILELYS
13   GLNTHRPROTHRGLUASNTHRTYRLYSLEU
14   CYSGLUGLUALAGLYTHRASPLEUGLYGLN
15   TRPVALTHRARGASPARGLEUGLUHISHIS
16   HISHISHISHIS

Samples:

sample_1: NsR431C, [U-100% 13C; U-100% 15N], 1.18 ± 0.2 mM; DTT 10 mM; DSS 50 uM; NaN3 0.02%; NaCl 200 mM; CaCl2 5 mM; MES 20 mM; H2O 90%; D2O 10%

sample_2: NsR431C, [U-100% 13C; U-100% 15N], 1.18 ± 0.2 mM; DTT 10 mM; DSS 50 uM; NaN3 0.02%; NaCl 200 mM; CaCl2 5 mM; MES 20 mM; D2O 100%

sample_3: NsR431C, [U-10% 13C; U-100% 15N], 1.18 ± 0.2 mM; DTT 10 mM; DSS 50 uM; NaN3 0.02%; NaCl 200 mM; CaCl2 5 mM; MES 20 mM; D2O 100%

sample_conditions_1: ionic strength: 205 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

AutoAssign v2.2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, structure solution

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - chemical shift assignment, structure solution

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - geometry optimization, structure solution

CNS v2.0.6, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAB75594
REF WP_010998036
SP Q8YQD8
AlphaFold Q8YQD8

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