BMRB Entry 16110

Name: Solution structure of the conserved C-terminal dimerization domain of Borealin
Published: 2009-06-25

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PDB ID: 2kdd
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16110
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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:

Solution structure of the conserved C-terminal dimerization domain of Borealin

Deposition date:

2009-01-06

Original release date:

2009-06-25

Authors:

Lingel, Andreas; Fairbrother, Wayne

Citation:

Citation: Bourhis, Eric; Lingel, Andreas; Phung, Qui; Fairbrother, Wayne; Cochran, Andrea. "Phosphorylation of a Borealin dimerization domain is required for proper chromosome segregation" Biochemistry 48, 6783-6793 (2009).
PubMed: 19530738

Assembly members:

Assembly members:
Borealin, polymer, 76 residues, Formula weight is not available

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: pET21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Borealin: GSAGERIYNISGNGSPLADS KEIFLTVPVGGGESLRLLAS DLQRHSIAQLDPEALGNIKK LSNRLAQICSSIRTHK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	225
15N chemical shifts	68
1H chemical shifts	465

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	1

Entities:

Entity 1, entity_1 76 residues - Formula weight is not available

1

GLY

SER

ALA

GLY

GLU

ARG

ILE

TYR

ASN

ILE

2

SER

GLY

ASN

GLY

SER

PRO

LEU

ALA

ASP

SER

3

LYS

GLU

ILE

PHE

LEU

THR

VAL

PRO

VAL

GLY

4

GLY

GLU

SER

LEU

ARG

LEU

ALA

SER

5

ASP

LEU

GLN

ARG

HIS

SER

ILE

ALA

GLN

LEU

6

ASP

PRO

GLU

ALA

LEU

GLY

ASN

ILE

LYS

7

LEU

SER

ASN

ARG

LEU

ALA

GLN

ILE

CYS

SER

8

SER

ILE

ARG

THR

HIS

LYS

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	15N_sample	isotropic	sample_conditions_1
3D 1H-13C NOESY	15N_13C_sample_D2O	isotropic	sample_conditions_1
3D HNHA	15N_sample	isotropic	sample_conditions_1
2D 1H-1H NOESY	unlabeled_sample	isotropic	sample_conditions_1
2D 1H-15N HSQC	15N_sample	anisotropic	sample_conditions_1
3D 1H-13C NOESY	mixed_sample	isotropic	sample_conditions_1
3D HNCA	15N_13C_sample	isotropic	sample_conditions_1
3D HNCACB	15N_13C_sample	isotropic	sample_conditions_1
3D CBCA(CO)NH	15N_13C_sample	isotropic	sample_conditions_1
3D C(CO)NH	15N_13C_sample	isotropic	sample_conditions_1
3D H(CCO)NH	15N_13C_sample	isotropic	sample_conditions_1
3D 1H-15N TOCSY	15N_13C_sample_D2O	isotropic	sample_conditions_1
2D 1H-15N HSQC	15N_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC	15N_13C_sample	isotropic	sample_conditions_1

PDB	2KDD
DBJ	BAA91629 BAB13961 BAB14125 BAD96269 BAD96288
EMBL	CAH90785
GB	AAH00703 AAH01651 AAH08079 AAH16944 AAR91699
REF	NP_001127334 NP_001233359 NP_001243804 NP_060571 XP_001115347
SP	Q53HL2 Q5RBS5
AlphaFold	Q53HL2 Q5RBS5

BMRB Entry 16110

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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