BMRB Entry 15962

Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15962

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for the heme bound form of Truncated HasAp.
Deposition date:
2008-09-24
Original release date:
2009-01-20
Authors:
Alontaga, Aileen; Rivera, Mario; Rodriguez, Juan
Citation:

Citation: Alontaga, Aileen; Rodriguez, Juan; Schonbrunn, Ernst; Becker, Andreas; Funke, Todd; Yukl, Erik; Hayashi, Takahiro; Stobaugh, Jordan; Moenne-Loccoz, Pierre; Rivera, Mario. "Structural characterization of the hemophore HasAp from Pseudomonas aeruginosa: NMR spectroscopy reveals protein-protein interactions between Holo-HasAp and hemoglobin."  Biochemistry 48, 96-109 (2009).
PubMed: 19072037

Assembly members:

Assembly members:
HasAp_truncated_polypeptide, polymer, 184 residues, 19000 Da.
HEM, non-polymer, 616.487 Da.

Natural source:

Natural source:   Common Name: Pseudomonas aeruginosa   Taxonomy ID: 287   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Pseudomonas aeruginosa

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET 11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HasAp_truncated_polypeptide: MSISISYSTTYSGWTVADYL ADWSAYFGDVNHRPGQVVDG SNTGGFNPGPFDGSQYALKS TASDAAFIAGGDLHYTLFSN PSHTLWGKLDSIALGDTLTG GASSGGYALDSQEVSFSNLG LDSPIAQGRDGTVHKVVYGL MSGDSSALQGQIDALLKAVD PSLSINSTFDQLAAAGVAHA TPAA

Data sets:
Data typeCount
13C chemical shifts518
15N chemical shifts170
1H chemical shifts170

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1monomer1
2cofactor2

Entities:

Entity 1, monomer 184 residues - 19000 Da.

1   METSERILESERILESERTYRSERTHRTHR
2   TYRSERGLYTRPTHRVALALAASPTYRLEU
3   ALAASPTRPSERALATYRPHEGLYASPVAL
4   ASNHISARGPROGLYGLNVALVALASPGLY
5   SERASNTHRGLYGLYPHEASNPROGLYPRO
6   PHEASPGLYSERGLNTYRALALEULYSSER
7   THRALASERASPALAALAPHEILEALAGLY
8   GLYASPLEUHISTYRTHRLEUPHESERASN
9   PROSERHISTHRLEUTRPGLYLYSLEUASP
10   SERILEALALEUGLYASPTHRLEUTHRGLY
11   GLYALASERSERGLYGLYTYRALALEUASP
12   SERGLNGLUVALSERPHESERASNLEUGLY
13   LEUASPSERPROILEALAGLNGLYARGASP
14   GLYTHRVALHISLYSVALVALTYRGLYLEU
15   METSERGLYASPSERSERALALEUGLNGLY
16   GLNILEASPALALEULEULYSALAVALASP
17   PROSERLEUSERILEASNSERTHRPHEASP
18   GLNLEUALAALAALAGLYVALALAHISALA
19   THRPROALAALA

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

1   HEM

Samples:

sample_1: HasAp truncated polypeptide, [U-99% 13C; U-99% 15N], 2.80 mM; sodium phosphate 46.4 mM; D2O, [U-99% 2H], 5%; H2O 95%; PROTOPORPHYRIN IX CONTAINING FE 2.8 mM

sample_conditions_1: ionic strength: .1 M; pH: 7.0; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
(HCA)CO(CA)NHsample_1isotropicsample_conditions_1

Software:

NMRPipe v3.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.112, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

BMRB 15963 19720 19721 19722
PDB
DBJ BAK91367 BAP21966 BAP49596 BAQ38483 BAR66548
EMBL CAA76520 CAW26382 CCQ88896 CDH69922 CDH76002
GB AAG06795 AAT49927 ABJ12662 ABR84528 AEO74046
REF NP_252097 WP_003091842 WP_003115011 WP_003124283 WP_003153113

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