BMRB Entry 18216

Title:
NMR structure of an acyl-carrier protein from Rickettsia prowazekii.(Seattle Structural Genomics Center for Infectious Disease (SSGCID))   PubMed: 21904063
Deposition date:
2012-01-25
Original release date:
2012-02-10
Authors:
Barnwal, Ravi P; Gonen, Shane; Varani, Gabriele
Citation:

Citation: Barnwal, Ravi; Van Voorhis, Wesley; Varani, G.. "NMR structure of an acyl-carrier protein from Borrelia burgdorferi."  Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67, 1137-1140 (2011).

Assembly members:

Assembly members:
acyl_carrier_protein, polymer, 81 residues, 9250.662 Da.

Natural source:

Natural source:   Common Name: Rickettsia prowazekii   Taxonomy ID: 782   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Rickettsia prowazekii

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

Experimental source:

Natural source:   Common Name: Rickettsia prowazekii   Taxonomy ID: 782   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Rickettsia prowazekii

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts350
15N chemical shifts78
1H chemical shifts513

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1acyl-carrier protein from Rickettsia prowazekii1

Entities:

Entity 1, acyl-carrier protein from Rickettsia prowazekii 81 residues - 9250.662 Da.

1   METSERTHRTHRASPLYSILEGLUGLNLYS
2   VALILEGLUMETVALALAGLULYSLEUASN
3   LYSASPLYSALAILEILETHRTHRASPSER
4   ARGPHEILEGLUASPLEULYSALAASPSER
5   LEUASPTHRVALGLULEUMETMETALAILE
6   GLUVALGLUTYRGLYILEASPILEPROASP
7   ASPGLUALATHRLYSILELYSTHRVALSER
8   ASPVALILELYSTYRILELYSGLUARGGLN
9   SER

Samples:

sample_1: acyl carrier protein, [U-98% 13C; U-98% 15N], 1.7 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 298 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 HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, 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 - refinement, structure solution

NMR spectrometers:

  • Bruker AMX 500 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAK97067
EMBL CAA15191 CDI28789 CEO16541
GB AAL03723 AAU04206 AAY62074 ABV73896 ABV76754
REF NP_221115 WP_001911850 WP_004997429 WP_010886364 WP_012151302
SP A8EZW3 A8F2Q2 B0BV67 C3PLP2 Q4UK61
AlphaFold Q4UK61

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