BMRB

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 25387

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25387

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Title: Backbone and side-chain 1H, 15N, 13C assignment and secondary structure of BPSL1445 from Burkholderia pseudomallei   PubMed: 25893672

Deposition date: 2014-12-10 Original release date: 2015-06-04

Authors: Musco, Giovanna; Bolognesi, Martino; Berardi, Andrea; Gaudesi, Davide; Gourlay, Louise; Quilici, Giacomo

Citation: Quilici, Giacomo; Berardi, Andrea; Gaudesi, Davide; Gourlay, Louise; Bolognesi, Martino; Musco, Giovanna. "Backbone and side-chain 1H, 15N, 13C assignment and secondary structure of BPSL1445 from Burkholderia pseudomallei"  Biomol. NMR Assign. 9, 347-350 (2015).

Assembly members:
BPSL1445, polymer, 163 residues, Formula weight is not available

Natural source:   Common Name: b-proteobacteria   Taxonomy ID: 28450   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bulkholderia Pseudomallei

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

Entity Sequences (FASTA):
BPSL1445: GSATNASKRQAIDASVDATL SRLYSTVRGSRELVAKSRGV LVFPDVIQAGLIIGGQTGNG ALRVGGATVGYYNTSSLSVG LQAGAQSKAIVFLFMTQDAL DKFRNSDGWAAGADASVALV KMGANGAIDTTTATAPVEVI VLTNAGLMGDVSISGTKVTK LKI

Data sets:
Data typeCount
13C chemical shifts663
15N chemical shifts168
1H chemical shifts1083

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_21

Entities:

Entity 1, entity_1 163 residues - Formula weight is not available

1   GLYSERALATHRASNALASERLYSARGGLN
2   ALAILEASPALASERVALASPALATHRLEU
3   SERARGLEUTYRSERTHRVALARGGLYSER
4   ARGGLULEUVALALALYSSERARGGLYVAL
5   LEUVALPHEPROASPVALILEGLNALAGLY
6   LEUILEILEGLYGLYGLNTHRGLYASNGLY
7   ALALEUARGVALGLYGLYALATHRVALGLY
8   TYRTYRASNTHRSERSERLEUSERVALGLY
9   LEUGLNALAGLYALAGLNSERLYSALAILE
10   VALPHELEUPHEMETTHRGLNASPALALEU
11   ASPLYSPHEARGASNSERASPGLYTRPALA
12   ALAGLYALAASPALASERVALALALEUVAL
13   LYSMETGLYALAASNGLYALAILEASPTHR
14   THRTHRALATHRALAPROVALGLUVALILE
15   VALLEUTHRASNALAGLYLEUMETGLYASP
16   VALSERILESERGLYTHRLYSVALTHRLYS
17   LEULYSILE

Samples:

sample_1: BPSL1445 0.7 mM; BPSL1445, [U-98% 15N], 0.7 mM; BPSL1445, [U-98% 13C; U-98% 15N], 0.7 mM; H2O 90%; D2O 10%

sample_2: BPSL1445 0.7 mM; BPSL1445, [U-98% 15N], 0.7 mM; BPSL1445, [U-98% 13C; U-98% 15N], 0.7 mM; D2O 100%

sample_conditions: ionic strength: 0.15 M; pH: 6.3; pressure: 1 atm; temperature: 295 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions
2D 1H-1H TOCSYsample_2isotropicsample_conditions
2D 1H-1H NOESYsample_2isotropicsample_conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions
2D 1H-13C HSQCsample_2isotropicsample_conditions
3D HNCAsample_1isotropicsample_conditions
3D HNCACBsample_1isotropicsample_conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions
3D C(CO)NHsample_1isotropicsample_conditions
3D H(CCO)NHsample_1isotropicsample_conditions
3D HNCOsample_1isotropicsample_conditions
3D HCCH-TOCSYsample_2isotropicsample_conditions

Software:

TOPSPIN, Bruker Biospin - collection, processing

CCPNMR v2.1, CCPN - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz

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