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Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 30494

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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/BMR30494
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Title: NMR Data for Solution NMR Structures of Protein PF2048.1

Deposition date: 2018-07-17 Original release date: 2018-08-10

Authors: Daigham, N.; Liu, G.; Swapna, G.; Cole, C.; Valafar, H.; Montelione, G.

Citation: Cole, C.; Daigham, N.; Liu, G.; Montelione, G.; Valafar, H.. "REDCRAFT: A Computational Platform Using Residual Dipolar Coupling NMR Data for Determining Structures of Perdeuterated Proteins Without NOEs"  . ., .-..

Assembly members:
entity_1, polymer, 80 residues, 9310.680 Da.

Natural source:   Common Name: Pyrococcus furiosus   Taxonomy ID: 1185654   Superkingdom: Archaea   Kingdom: not available   Genus/species: Pyrococcus furiosus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21 (DE3)

Entity Sequences (FASTA):
entity_1: MAHHHHHHGSVVKEKLEKAL IEVRPYVEYYNELKALVSKI SSSVNDLEEAIVVLREEEKK ASEPFKTDIRILLDFLESKP

Data sets:
Data typeCount
13C chemical shifts263
15N chemical shifts70
1H chemical shifts548

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 80 residues - 9310.680 Da.

1   METALAHISHISHISHISHISHISGLYSER
2   VALVALLYSGLULYSLEUGLULYSALALEU
3   ILEGLUVALARGPROTYRVALGLUTYRTYR
4   ASNGLULEULYSALALEUVALSERLYSILE
5   SERSERSERVALASNASPLEUGLUGLUALA
6   ILEVALVALLEUARGGLUGLUGLULYSLYS
7   ALASERGLUPROPHELYSTHRASPILEARG
8   ILELEULEUASPPHELEUGLUSERLYSPRO

Samples:

sample_1: PF2048.1, [U-100% 13C; U-100% 15N], 0.8 mM; MES 20 mM; sodium chloride 100 mM; Calcium chloride 5 na; sodium azide 0.02%; DSS 10%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D CCH-TOSCYsample_1isotropicsample_conditions_1
3D N15-TOCSYsample_1isotropicsample_conditions_1
3D simultaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

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

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

SPARKY, Goddard - data analysis

TOPSPIN, Bruker Biospin - collection

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

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

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

AVS, Moseley and Montelione - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

PSVS, Bhattacharya and Montelione - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

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