BMRB Entry 16306

Name: 1H, 15N, and 13C resonance assignments of the 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 in the ferric bis-histidine state
Published: 2009-07-22

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PDB ID: 2ksc
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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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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

Deposition date:

2009-05-19

Original release date:

2009-07-22

Authors:

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

Citation:

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).
PubMed: 19888693

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 Taxonomy ID: 32049 Superkingdom: Bacteria Kingdom: Cyanobacteria Genus/species: Chroococcales synechococcus

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

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
Samples and Experiments
Software
Spectrometers
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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

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, 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

BMRB	16307 17947 18422 18423 18424
PDB	2KSC 4L2M 4MAX
GB	AAL79195 ACA99611
REF	WP_012307234 WP_030006991