BMRB Entry 16996

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for human Rad51D from 1 to 83
Published: 2011-06-01

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PDB ID: 2kz3
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16996
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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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for human Rad51D from 1 to 83

Deposition date:

2010-06-11

Original release date:

2011-06-01

Authors:

Choi, Byong-Seok; Kim, Young Mee

Citation:

Citation: Kim, Young Mee; Choi, Byong-Seok. "Structural and functional characterization of the N-terminal domain of human Rad51D." Int. J. Biochem. Cell Biol. 43, 416-422 (2011).
PubMed: 21111057

Assembly members:

Assembly members:
human_Rad51D_N, polymer, 83 residues, 9070.740 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: pET-28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
human_Rad51D_N: MGVLRVGLCPGLTEEMIQLL RSHRIKTVVDLVSADLEEVA QKCGLSYKALVALRRVLLAQ FSAFPVNGADLYEELKTSTA ILS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	333
15N chemical shifts	80
1H chemical shifts	587

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	human Rad51D N	1

Entities:

Entity 1, human Rad51D N 83 residues - 9070.740 Da.

1

MET

GLY

VAL

LEU

ARG

VAL

GLY

LEU

CYS

PRO

2

GLY

LEU

THR

GLU

MET

ILE

GLN

LEU

3

ARG

SER

HIS

ARG

ILE

LYS

THR

VAL

ASP

4

LEU

VAL

SER

ALA

ASP

LEU

GLU

VAL

ALA

5

GLN

LYS

CYS

GLY

LEU

SER

TYR

LYS

ALA

LEU

6

VAL

ALA

LEU

ARG

VAL

LEU

ALA

GLN

7

PHE

SER

ALA

PHE

PRO

VAL

ASN

GLY

ALA

ASP

8

LEU

TYR

GLU

LEU

LYS

THR

SER

THR

ALA

9

ILE

LEU

SER

Samples:

sample_1: human Rad51D_N, [U-100% 15N], 1 mM; DTT 1 mM; sodium azide 0.02%; Tris-HCl 25 mM; NaCl 100 mM; D2O 100%

sample_2: human Rad51D_N, [U-99% 13C; U-99% 15N], 1 mM; TRIS 25 mM; sodium chloride 100 mM; DTT 1 mM; sodium azide 0.02%; D2O 100%

sample_3: human Rad51D_N, [U-99% 15N], 1 mM; TRIS 25 mM; sodium chloride 100 mM; DTT 1 mM; sodium azide 0.02%; D2O 90%; H2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7.5; pressure: 1 atm; temperature: 287 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_3	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

CYANA v2.1, P.GUNTERT ET AL. - refinement

NMR spectrometers:

Varian INOVA 600 MHz
Bruker Avance 800 MHz

PDB	2KZ3
DBJ	BAA25914 BAA31747 BAA31748 BAA33779 BAA33780
EMBL	CAA75681
GB	AAC39719 AAH14422 AAT38112 ABM83244 ABM86446
REF	NP_002869 XP_001174459 XP_003818041 XP_004041973 XP_008969520
SP	O75771
AlphaFold	O75771