BMRB Entry 16891

Name: Backbone 1H, 13C and 15N Chemical Shift Assignments for the free alpha chain of human haemoglobin
Published: 2010-04-26

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16891

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Backbone 1H, 13C and 15N Chemical Shift Assignments for the free alpha chain of human haemoglobin

Deposition date:

2010-04-22

Original release date:

2010-04-26

Authors:

Gell, David

Citation:

Citation: Dickson, Claire; KrishnaKumar, Kaavya; Mackay, Joel; Gell, david. "Assigned chemical shifts for the free alpha chain of haemoglobin" .

Assembly members:

Assembly members:
HBA1, polymer, 141 residues, Formula weight is not available
HEM, non-polymer, 616.487 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pHE7

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HBA1: VLSPADKTNVKAAWGKVGAH AGEYGAEALERMFLSFPTTK TYFPHFDLSHGSAQVKGHGK KVADALTNAVAHVDDMPNAL SALSDLHAHKLRVDPVNFKL LSHCLLVTLAAHLPAEFTPA VHASLDKFLASVSTVLTSKY R

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	219
15N chemical shifts	113
1H chemical shifts	113

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	alpha globin polypeptide, 1	1
2	alpha globin polypeptide, 2	1
3	haem, 1	2
4	haem, 2	2

Entities:

Entity 1, alpha globin polypeptide, 1 141 residues - Formula weight is not available

1

VAL

LEU

SER

PRO

ALA

ASP

LYS

THR

ASN

VAL

2

LYS

ALA

TRP

GLY

LYS

VAL

GLY

ALA

HIS

3

ALA

GLY

GLU

TYR

GLY

ALA

GLU

ALA

LEU

GLU

4

ARG

MET

PHE

LEU

SER

PHE

PRO

THR

LYS

5

THR

TYR

PHE

PRO

HIS

PHE

ASP

LEU

SER

HIS

6

GLY

SER

ALA

GLN

VAL

LYS

GLY

HIS

GLY

LYS

7

LYS

VAL

ALA

ASP

ALA

LEU

THR

ASN

ALA

VAL

8

ALA

HIS

VAL

ASP

MET

PRO

ASN

ALA

LEU

9

SER

ALA

LEU

SER

ASP

LEU

HIS

ALA

HIS

LYS

10

LEU

ARG

VAL

ASP

PRO

VAL

ASN

PHE

LYS

LEU

11

LEU

SER

HIS

CYS

LEU

VAL

THR

LEU

ALA

12

ALA

HIS

LEU

PRO

ALA

GLU

PHE

THR

PRO

ALA

13

VAL

HIS

ALA

SER

LEU

ASP

LYS

PHE

LEU

ALA

14

SER

VAL

SER

THR

VAL

LEU

THR

SER

LYS

TYR

15

ARG

Entity 2, haem, 1 - C34 H32 Fe N4 O4 - 616.487 Da.

1

HEM

Samples:

sample_1: HBA1, [U-98% 13C; U-98% 15N], 0.6 – 0.9 mM; haem0.6 – 0.9 mM; DSS 40 uM

sample_conditions_1: ionic strength: 20 mM; pH: 7.0; pressure: 1 atm; temperature: 288 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin, Goddard - chemical shift assignment, collection

NMR spectrometers:

Bruker Avance 600 MHz

Related Database Links:

BMRB	1101 16898 25 2707 2709 2868 3442
PDB	1A00 1A01 1A0U 1A0Z 1A3N 1A3O 1A9W 1ABW 1ABY 1AJ9 1B86 1BAB 1BBB 1BIJ 1BUW 1BZ0 1BZ1 1BZZ 1C7B 1C7C 1C7D 1CLS 1CMY 1COH 1DKE 1DXT 1DXU 1DXV 1FDH 1FN3 1G9V 1GBU 1GBV 1GLI 1GZX 1HAB 1HAC 1HBA 1HBB 1HBS 1HCO 1HDB 1HGA 1HGB 1HGC 1HHO 1IRD 1J3Y 1J3Z 1J40 1J41 1J7S 1J7W 1J7Y 1JY7 1K0Y 1K1K 1KD2 1LFL 1LFQ 1LFT 1LFV 1LFY 1LFZ 1LJW 1M9P 1MKO 1NEJ 1NIH 1NQP 1O1I 1O1J 1O1K 1O1L 1O1M 1O1N 1O1O 1O1P 1QI8 1QSH 1QSI 1QXD 1QXE 1R1X 1R1Y 1RPS 1RQ3 1RQ4 1RQA 1RVW 1SDK 1SDL 1SHR 1SI4 1THB 1UIW 1VWT 1XXT 1XY0 1XYE 1XZ2 1XZ4 1XZ5 1XZ7 1XZU 1XZV 1Y01 1Y09 1Y0A 1Y0C 1Y0D 1Y0T 1Y0W 1Y22 1Y2Z 1Y31 1Y35 1Y45 1Y46 1Y4B 1Y4F 1Y4G 1Y4P 1Y4Q 1Y4R 1Y4V 1Y5F 1Y5J 1Y5K 1Y7C 1Y7D 1Y7G 1Y7Z 1Y83 1Y85 1Y8W 1YDZ 1YE0 1YE1 1YE2 1YEN 1YEO 1YEQ 1YEU 1YEV 1YFF 1YG5 1YGD 1YGF 1YH9 1YHE 1YHR 1YIE 1YIH 1YVQ 1YVT 1YZI 1Z8U 2D5Z 2D60 2DN1 2DN2 2DN3 2DXM 2H35 2HBC 2HBD 2HBE 2HBF 2HBS 2HCO 2HHB 2HHD 2HHE 2M6Z 2W6V 2W72 2YRS 3B75 3D17 3D7O 3DUT 3HHB 3HXN 3IA3 3IC0 3IC2 3KMF 3NL7 3NMM 3ODQ 3ONZ 3OO4 3OO5 3OVU 3P5Q 3QJB 3QJC 3QJD 3QJE 3R5I 3S48 3S65 3S66 3SZK 3WCP 3WHM 4FC3 4HHB 4IJ2 4L7Y 4M4A 4M4B 4MQC 4MQG 4MQH 4MQI 4MQJ 4MQK 4N7N 4N7O 4N7P 4N8T 4NI0 4NI1 4ROL 4ROM 4WJG 4X0I 4X0L 4XS0 5E29 5EE4 6HBW
DBJ	BAD97112 BAJ20323
EMBL	CAA23748 CAA23750 CAA23751 CAA23752 CAA23774
GB	AAA52632 AAA66030 AAA66031 AAB59407 AAB59408
PRF	0404170A 0907233A 1004272B 1509322A 610524A
REF	NP_000508 NP_000549 NP_001036091 NP_001036092 NP_001125901
SP	P01923 P01924 P06635 P18972 P21766
AlphaFold	P01923 P01924 P06635 P18972 P21766

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