BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 16306

Title: 1H, 15N, and 13C resonance assignments of the 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 in the ferric bis-histidine state   PubMed: 19888693

Authors: Vuletich, David; Pond, Matthew; Falzone, Christopher; Lecomte, Juliette

Citation: Pond, Matthew; Vuletich, David; Falzone, Christopher; Majumdar, Ananya; Lecomte, Juliette. "(1)H, (15)N, and (13)C resonance assignments of the 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 in the ferric bis-histidine state"  Biomol. NMR Assignments 3, 211-214 (2009).

Assembly members:
GlbN, polymer, 123 residues, Formula weight is not available
HEB, non-polymer, 618.503 Da.

Natural source:   Common Name: cyanobacteria   Taxonomy ID: 32049   Superkingdom: Bacteria   Kingdom: Cyanobacteria   Genus/species: Chroococcales synechococcus

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

Entity Sequences (FASTA):
GlbN: ASLYEKLGGAAAVDLAVEKF YGKVLADERVNRFFVNTDMA KQKQHQKDFMTYAFGGTDRF PGRSMRAAHQDLVENAGLTD VHFDAIAENLVLTLQELNVS QDLIDEVVTIVGSVQHRNDV LNR

Data sets:
Data typeCount
13C chemical shifts492
15N chemical shifts138
1H chemical shifts830
heteronuclear NOE values93
T1 relaxation values100
T2 relaxation values99

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1protein1
2heme2

Entities:

Entity 1, protein 123 residues - Formula weight is not available

Met1 is cleaved

1   ALASERLEUTYRGLULYSLEUGLYGLYALA
2   ALAALAVALASPLEUALAVALGLULYSPHE
3   TYRGLYLYSVALLEUALAASPGLUARGVAL
4   ASNARGPHEPHEVALASNTHRASPMETALA
5   LYSGLNLYSGLNHISGLNLYSASPPHEMET
6   THRTYRALAPHEGLYGLYTHRASPARGPHE
7   PROGLYARGSERMETARGALAALAHISGLN
8   ASPLEUVALGLUASNALAGLYLEUTHRASP
9   VALHISPHEASPALAILEALAGLUASNLEU
10   VALLEUTHRLEUGLNGLULEUASNVALSER
11   GLNASPLEUILEASPGLUVALVALTHRILE
12   VALGLYSERVALGLNHISARGASNASPVAL
13   LEUASNARG

Entity 2, heme - C34 H34 Fe N4 O4 - 618.503 Da.

1   HEB

Samples:

sample_1: GlbN1 – 2 mM; H2O 90%; D2O 10%; phosphate buffer 20 mM

sample_2: GlbN, [U-15N], 1 – 2 mM; H2O 90%; D2O 10%; phosphate buffer 20 mM

sample_3: GlbN, [U-13C; U-15N], 0.6 – 1.4 mM; H2O 90%; D2O 10%; phosphate buffer 20 mM

sample_4: GlbN1 – 4 mM; phosphate buffer 20 mM; D2O 100%

sample_conditions_1: ionic strength: 25 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 25 mM; pH: 6.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HMQCsample_4isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D HCCH-COSYsample_3isotropicsample_conditions_1
3D HCC(CO)NHsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HN(CA)COsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D CBCANHsample_3isotropicsample_conditions_1
3D 1H-15N TOCSY-HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESY-HSQCsample_2isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HMQCsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_4isotropicsample_conditions_1
2D DQF-COSYsample_4isotropicsample_conditions_1
2D 1H-1H NOESYsample_4isotropicsample_conditions_1
2D 1H-1H TOCSYsample_4isotropicsample_conditions_1
2D 1H-1H NOESYsample_4isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
2D 1H-15N NOEsample_2isotropicsample_conditions_1
2D 15N R1sample_2isotropicsample_conditions_1
2D 15N R2sample_2isotropicsample_conditions_1

Software:

NMRPipe vv.3.0 Rev 2007.068.09.07, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY vv3.113, Goddard - chemical shift assignment

xwinnmr vv2.5, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Varian INOVA 800 MHz

Related Database Links:

BMRB 16307 17947 18422 18423 18424
PDB
GB AAL79195 ACA99611
REF WP_012307234 WP_030006991