BMRB Entry 27550

Title:
Shr Hemoglobin Interacting Domain 2
Deposition date:
2018-07-17
Original release date:
2018-10-08
Authors:
Macdonald, Ramsay; Cascio, Duilio; Collazo, Michael; Phillips, Martin; Clubb, Robert
Citation:

Citation: Macdonald, Ramsay; Cascio, Duilio; Collazo, Michael; Phillips, Martin; Clubb, Robert. "The Streptococcus pyogenes Shr protein captures human hemoglobin using two structurally unique binding domains"  J. Biol. Chem. 293, 18365-18377 (2018).
PubMed: 30301765

Assembly members:

Assembly members:
Shr-HID2, polymer, 132 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Streptococcus pyogenes   Taxonomy ID: 1314   Superkingdom: not available   Kingdom: not available   Genus/species: Streptococcus pyogenes

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pRAM402

Data sets:
Data typeCount
13C chemical shifts357
15N chemical shifts123
1H chemical shifts441

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Shr-HID21

Entities:

Entity 1, Shr-HID2 132 residues - Formula weight is not available

The first serine residue is a cloning artifact.

1   SERLYSTHRVALPROGLNASNGLNGLYTHR
2   GLNLYSVALVALLYSSERGLYLYSASNTHR
3   ALAASNLEUSERLEUILETHRLYSLEUSER
4   GLNGLUASPGLYALAILELEUPHEPROGLU
5   ILEASPARGTYRSERASPASNLYSGLNILE
6   LYSALALEUTHRGLNGLNILETHRLYSVAL
7   THRVALASNGLYTHRVALTYRLYSASPLEU
8   ILESERASPSERVALLYSASPTHRASNGLY
9   TRPVALSERASNMETTHRGLYLEUHISLEU
10   GLYTHRLYSALAPHELYSASPGLYGLUASN
11   THRILEVALILESERSERLYSGLYPHEGLU
12   ASPVALTHRILETHRVALTHRLYSLYSASP
13   GLYGLNILEHISPHEVALSERALALYSGLN
14   LYSGLN

Samples:

sample_1: Shr-HID2, [U-100% 13C; U-100% 15N], 1.1 mM; sodium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.01%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D CC(CO)NHsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - data analysis

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

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

CARA, Keller and Wuthrich - chemical shift assignment

TOPSPIN, Bruker Biospin - processing

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker DRX 600 MHz
  • Bruker DRX 500 MHz

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