BMRB Entry 25508

Title:
1H, 13C, and 15N Chemical Shift Assignments and structure of Probable Fe(2+)-trafficking protein from Burkholderia pseudomallei 1710b.
Deposition date:
2015-02-26
Original release date:
2015-03-23
Authors:
Tang, Changyan; Yang, Fan; Barnwal, Ravi P; Barnwal, Gabriele
Citation:

Citation: Tang, Changyan; Yang, Fan; Barnwal, Ravi P; Barnwal, Gabriele. "1H, 13C, and 15N Chemical Shift Assignments and structure of Probable Fe(2+)-trafficking protein from Burkholderia pseudomallei 1710b."  To be Published ., .-..

Assembly members:

Assembly members:
entity, polymer, 91 residues, 10388.955 Da.

Natural source:

Natural source:   Common Name: b-proteobacteria   Taxonomy ID: 320372   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Burkholderia pseudomallei

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28-AVA

Experimental source:

Natural source:   Common Name: b-proteobacteria   Taxonomy ID: 320372   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Burkholderia pseudomallei

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28-AVA

Data sets:
Data typeCount
1H chemical shifts492
13C chemical shifts361
15N chemical shifts93

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 91 residues - 10388.955 Da.

1   METALAARGMETILEHISCYSALALYSLEU
2   GLYLYSGLUALAGLUGLYLEUASPPHEPRO
3   PROLEUPROGLYGLULEUGLYLYSARGLEU
4   TYRGLUSERVALSERLYSGLNALATRPGLN
5   ASPTRPLEULYSGLNGLNTHRMETLEUILE
6   ASNGLUASNARGLEUASNMETALAASPPRO
7   ARGALAARGGLNTYRLEUMETLYSGLNTHR
8   GLULYSTYRPHEPHEGLYGLUGLYALAASP
9   GLNALASERGLYTYRVALPROPROALAGLN
10   GLY

Samples:

sample_1: Probable Fe(2+)-trafficking protein, [U-95% 13C; U-95% 15N], 1 mM; H2O 90%; H2O 10%

sample_conditions_1: temperature: 298 K; pH: 6.5; pressure: 1 atm

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 HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

CCPNMR, CCPN - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution, refinement

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

  • Bruker AMX 500 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
EMBL CAH36329 CDU28980 CFB53393 CFD92754 CFD97247
GB AAU48201 ABA48438 ABC36777 ABM51451 ABN02014
REF WP_004193961 WP_004539654 WP_009890128 YP_103370 YP_108922
SP A1V5R9 A2SAN1 A3MLE3 A3NBE8 A3NX81
AlphaFold A3NBE8

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