BMRB Entry 17947

Name: Partial backbone 1H assignments of the 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 in the ferrous bis-histidine state
Published: 2012-05-02

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17947

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Partial backbone 1H assignments of the 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 in the ferrous bis-histidine state

Deposition date:

2011-09-19

Original release date:

2012-05-02

Authors:

Lecomte, Juliette; Preimesberger, Matthew; Pond, Matthew; Majumdar, Ananya

Citation:

Citation: Preimesberger, Matthew; Pond, Matthew; Majumdar, Ananya; Lecomte, Juliette. "Electron self-exchange and self-amplified posttranslational modification in the hemoglobins from Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002" J. Biol. Inorg. Chem. 17, 599-609 (2012).
PubMed: 22349976

Assembly members:

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

Natural source:

Natural source: Common Name: cyanobacteria synechococcus Taxonomy ID: 269084 Superkingdom: Eukaryota Kingdom: Cyanobacteria Genus/species: Synechococcus Synechococcus elongatus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET3c

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
15N chemical shifts	115
1H chemical shifts	249
heteronuclear NOE values	91
T1 relaxation values	92
T2 relaxation values	93

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	GlbN	1
2	HEB	2

Entities:

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

1

ALA

SER

LEU

TYR

GLU

LYS

LEU

GLY

ALA

2

ALA

VAL

ASP

LEU

ALA

VAL

GLU

LYS

PHE

3

TYR

GLY

LYS

VAL

LEU

ALA

ASP

GLU

ARG

VAL

4

ASN

ARG

PHE

VAL

ASN

THR

ASP

MET

ALA

5

LYS

GLN

LYS

GLN

HIS

GLN

LYS

ASP

PHE

MET

6

THR

TYR

ALA

PHE

GLY

THR

ASP

ARG

PHE

7

PRO

GLY

ARG

SER

MET

ARG

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

THR

ILE

12

VAL

GLY

SER

VAL

GLN

HIS

ARG

ASN

ASP

VAL

13

LEU

ASN

ARG

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

1

HEB

Samples:

sample_1: GlbN, [U-15N], 1.6 mM; HEB 1.6 mM; potassium phosphate 100 mM; glucose 0.1%; glucose oxidase 0.2-0.5 mg/mL; catalase 0.05-0.2 mg/mL; dithionite 8 mM

sample_2: GlbN, [U-100% 13C; U-100% 15N], .76 mM; HEB .76 mM; potassium phosphate 250 mM; glucose 0.1%; glucose oxidase 0.2-0.5 mg/mL; catalase 0.05-0.2 mg/mL; dithionite 4 mM

sample_3: GlbN, [U-100% 15N], 1.6 mM; HEB 1.6 mM; potassium phosphate 100 mM; glucose 8 mM; glucose oxidase 0.8 uM; catalase 0.05 uM

sample_conditions_1: ionic strength: 0.3 M; pH: 7.15; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.75 M; pH: 7.15; pressure: 1 atm; temperature: 298 K

sample_conditions_3: ionic strength: 0.3 M; pH: 7.20; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_2
3D HNCACB	sample_2	isotropic	sample_conditions_2
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_2
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D DQF-COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N NOE	sample_3	isotropic	sample_conditions_3
2D 15N R1	sample_3	isotropic	sample_conditions_3
2D 15N R2	sample_3	isotropic	sample_conditions_3
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_3

Software:

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

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz
Bruker DRX 600 MHz

BMRB	16306 16307 18422 18423 18424
PDB	2KSC 4L2M 4MAX
GB	AAL79195 ACA99611
REF	WP_012307234 WP_030006991