BMRB Entry 17150

Title:
Solution Structure of cellobiose-specific phosphotransferase IIB component protein from Borrelia burgdorferi. Seattle Structure Genomics Center for Infectious Disease (SSGCID).
Deposition date:
2010-08-25
Original release date:
2010-09-16
Authors:
Yang, Fan; Barnwal, Ravi; Varani, Gabriele
Citation:

Citation: Yang, Fan; Barnwal, Ravi; Varani, Gabriele. "Solution Structure of cellobiose-specific phosphotransferase IIB component protein from Borrelia burgdorferi"  .

Assembly members:

Assembly members:
phosphotransferase_IIB, polymer, 109 residues, 11981.025 Da.

Natural source:

Natural source:   Common Name: spirochetes   Taxonomy ID: 139   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Borrelia burgdorferi

Experimental source:

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts419
15N chemical shifts109
1H chemical shifts705

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1phosphotransferase_IIB1

Entities:

Entity 1, phosphotransferase_IIB 109 residues - 11981.025 Da.

1   GLYPROGLYSERMETASNILELEULEUVAL
2   CYSGLYALAGLYMETSERTHRSERMETLEU
3   VALGLNARGILEGLULYSTYRALALYSSER
4   LYSASNILEASNALATHRILEGLUALAILE
5   ALAGLUTHRARGLEUSERGLUVALVALASP
6   ARGPHEASPVALVALLEULEUALAPROGLN
7   SERARGPHEASNLYSLYSARGLEUGLUGLU
8   ILETHRLYSPROLYSGLYILEPROILEGLU
9   ILEILEASNTHRILEASPTYRGLYTHRMET
10   ASNGLYGLULYSVALLEUGLNLEUALAILE
11   ASNALAPHEASNASNLYSSERSERVAL

Samples:

sample_1: phosphotransferase_IIB, [U-95% 15N], 1.2 mM; potassium phosphate 20 mM; potassium chloride 100 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_2: phosphotransferase_IIB, [U-95% 13C; U-95% 15N], 1.2 mM; potassium phosphate 20 mM; potassium chloride 100 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_3: phosphotransferase_IIB 1.1 mM; potassium phosphate 20 mM; potassium chloride 100 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
2D 1H-1H TOCSYsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

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

Molmol, Koradi, Billeter and Wuthrich - structure display

TOPSPIN, Bruker Biospin - collection

CcpNMR, CCPN - chemical shift assignment

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

SANE, Duggan, Legge, Dyson & Wright - data analysis

NMR spectrometers:

  • Bruker AMX 500 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
GB AAC66322 AAD01257 ACK75410 ACL34270 ACM10275
REF NP_046992 WP_010258206 WP_010890589 WP_012593119 WP_012622040

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