BMRB Entry 16306
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR16306
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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
Deposition date: 2009-05-19 Original release date: 2009-07-22
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
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 492 |
| 15N chemical shifts | 138 |
| 1H chemical shifts | 830 |
| heteronuclear NOE values | 93 |
| T1 relaxation values | 100 |
| T2 relaxation values | 99 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | protein | 1 |
| 2 | heme | 2 |
Entities:
Entity 1, protein 123 residues - Formula weight is not available
Met1 is cleaved
| 1 | ALA | SER | LEU | TYR | GLU | LYS | LEU | GLY | GLY | ALA | ||||
| 2 | ALA | ALA | VAL | ASP | LEU | ALA | VAL | GLU | LYS | PHE | ||||
| 3 | TYR | GLY | LYS | VAL | LEU | ALA | ASP | GLU | ARG | VAL | ||||
| 4 | ASN | ARG | PHE | PHE | VAL | ASN | THR | ASP | MET | ALA | ||||
| 5 | LYS | GLN | LYS | GLN | HIS | GLN | LYS | ASP | PHE | MET | ||||
| 6 | THR | TYR | ALA | PHE | GLY | GLY | THR | ASP | ARG | PHE | ||||
| 7 | PRO | GLY | ARG | SER | MET | ARG | ALA | ALA | HIS | GLN | ||||
| 8 | ASP | LEU | VAL | GLU | ASN | ALA | GLY | LEU | THR | ASP | ||||
| 9 | VAL | HIS | PHE | ASP | ALA | ILE | ALA | GLU | ASN | LEU | ||||
| 10 | VAL | LEU | THR | LEU | GLN | GLU | LEU | ASN | VAL | SER | ||||
| 11 | GLN | ASP | LEU | ILE | ASP | GLU | VAL | VAL | THR | ILE | ||||
| 12 | VAL | GLY | SER | VAL | GLN | HIS | ARG | ASN | ASP | VAL | ||||
| 13 | LEU | ASN | ARG |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HMQC | sample_4 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_3 | isotropic | sample_conditions_1 |
| 3D HCC(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_3 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_3 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 3D CBCANH | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY-HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY-HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HMQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_4 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_2 |
| 2D 1H-15N NOE | sample_2 | isotropic | sample_conditions_1 |
| 2D 15N R1 | sample_2 | isotropic | sample_conditions_1 |
| 2D 15N R2 | sample_2 | isotropic | sample_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 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts