BMRB Entry 17144

Title:
1H, 13C, and 15N backbone, side-chain, and heme chemical shift assignments for the oxidized form of the monoheme c-type cytochrome ApcA isolated from the acidophilic metal-reducing bacterium Acidiphilium cryptum
Deposition date:
2010-08-24
Original release date:
2010-10-04
Authors:
Cort, John; Swenson, Michael; Magnuson, Timothy
Citation:

Citation: Cort, John; Swenson, Michael; Magnuson, Timothy. "(1)H, (13)C, and (15)N backbone, side-chain, and heme chemical shift assignments for oxidized and reduced forms of the monoheme c-type cytochrome ApcA isolated from the acidophilic metal-reducing bacterium Acidiphilium cryptum."  Biomol. NMR Assignments 5, 89-92 (2011).
PubMed: 21197590

Assembly members:

Assembly members:
ApcA, polymer, 102 residues, Formula weight is not available
HEM, non-polymer, 616.487 Da.

Natural source:

Natural source:   Common Name: a-proteobacteria   Taxonomy ID: 524   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Acidiphilium cryptum

Experimental source:

Experimental source:   Production method: purified from the natural source   Host organism: Acidiphilium cryptum

Data sets:
Data typeCount
13C chemical shifts419
15N chemical shifts108
1H chemical shifts663

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ApcA1
2heme2

Entities:

Entity 1, ApcA 102 residues - Formula weight is not available

An N-terminal 21 amino acid signal sequence is not present and presumably was cleaved by the host organism.

1   ALAASNVALALAHISGLYLYSALALEUPHE
2   GLNALAGLNCYSALAALACYSHISSERVAL
3   SERPROGLYGLNASNGLYILEGLYPROSER
4   LEUALAGLYVALTYRGLYALALYSALAALA
5   ALATHRPROGLYPHEGLNPHESERPROALA
6   LEULYSLYSSERGLYILEVALTRPASNALA
7   SERTHRLEUASPLYSPHELEUALAASNPRO
8   GLNALAASPVALPROGLYTHRLYSMETPRO
9   TYRMETGLYMETALAASNALATHRASPARG
10   ALAASPVALVALALATYRLEUGLNTHRLEU
11   GLYLYS

Entity 2, heme - C34 H32 Fe N4 O4 - 616.487 Da.

1   HEM

Samples:

sample_1: ApcA, [U-100% 13C; U-100% 15N], 0.5 mM; sodium acetate 25 mM; sodium chloride 100 mM

sample_2: ApcA 0.5 mM; sodium acetate 25 mM; sodium chloride 100 mM

sample_3: ApcA, [U-100% 13C; U-100% 15N], 0.5 mM; sodium acetate 25 mM; sodium chloride 100 mM

sample_4: ApcA, [7%-biosynthetically directed 13C; 50%-U-15N], 0.5 mM; sodium acetate 25 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 125 mM; pH: 5.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_4isotropicsample_conditions_1
4D 1H-13C HMQC-NOESY-HMQCsample_3isotropicsample_conditions_1
2D HBCBCGCDHD-AROsample_1isotropicsample_conditions_1
2D HBCBCGCDCEHE-AROsample_1isotropicsample_conditions_1
3D CBCA(COCA)HAsample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

FELIX, Accelrys Software Inc. - processing

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz
  • Varian UnityPlus 500 MHz

Related Database Links:

NCBI YP_001235217.1
UNP A5G0B6
BMRB 17146
DBJ BAJ81692 GAN75771
GB ABQ31298 EGO93894 KDM67854
REF WP_007424422
AlphaFold A5G0B6

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