BMRB Entry 4328

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR4328

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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:

1H, 13C, and 15N Chemical Shift Assignments for Human Rad51(1-114)

Deposition date:

1999-04-03

Original release date:

1999-09-13

Authors:

Aihara, Hideki; Ito, Yutaka; Kurumizaka, Hitoshi; Yokoyama, Shigeyuki; Shibata, Takehiko

Citation:

Citation: Aihara, Hideki; Ito, Yutaka; Kurumizaka, Hitoshi; Yokoyama, Shigeyuki; Shibata, Takehiko. "The N-terminal Domain of the Human Rad51 Protein Binds DNA; Structure and a DNA Binding Surface as Revealed by NMR" J. Mol. Biol. 290, 495-504 (1999).

Assembly members:

Assembly members:
Human Rad51 protein(1-114), polymer, 114 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Human Rad51 protein(1-114): MAMQMQLEANADTSVEEESF GPQPISRLEQCGINANDVKK LEEAGFHTVEAVAYAPKKEL INIKGISEAKADKILAEAAK LVPMGFTTATEFHQRRSEII QITTGSKELDKLLQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_one
- assigned_chemical_shifts_two

Data type	Count
13C chemical shifts	332
15N chemical shifts	111
1H chemical shifts	628

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HsRad51(1-114)	1

Entities:

Entity 1, HsRad51(1-114) 114 residues - Formula weight is not available

1

MET

ALA

MET

GLN

MET

GLN

LEU

GLU

ALA

ASN

2

ALA

ASP

THR

SER

VAL

GLU

SER

PHE

3

GLY

PRO

GLN

PRO

ILE

SER

ARG

LEU

GLU

GLN

4

CYS

GLY

ILE

ASN

ALA

ASN

ASP

VAL

LYS

5

LEU

GLU

ALA

GLY

PHE

HIS

THR

VAL

GLU

6

ALA

VAL

ALA

TYR

ALA

PRO

LYS

GLU

LEU

7

ILE

ASN

ILE

LYS

GLY

ILE

SER

GLU

ALA

LYS

8

ALA

ASP

LYS

ILE

LEU

ALA

GLU

ALA

LYS

9

LEU

VAL

PRO

MET

GLY

PHE

THR

ALA

THR

10

GLU

PHE

HIS

GLN

ARG

SER

GLU

ILE

11

GLN

ILE

THR

GLY

SER

LYS

GLU

LEU

ASP

12

LYS

LEU

GLN

Samples:

sample_1: Human Rad51 protein(1-114), [U-95% 13C, U-95% 15N], 1.0 – 2.0 mM; Sodium_Phosphate 20.0 mM; NaCl 100 mM; DTT 2 mM; NaN3 0.02%

sample_conditions_1: pH: 6.5; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions

Software:

ANSIG -

NMR spectrometers:

Bruker DRX600 600 MHz
Bruker ARX400 400 MHz

BMRB	11046
PDB	1B22
DBJ	BAA02718 BAA02961 BAA02962 BAA03189 BAB27489
EMBL	CAA69384 CAG38796
GB	AAC28561 AAD49705 AAF61901 AAF69145 AAH27384
PRF	2102359A
REF	NP_001003043 NP_001039644 NP_001075493 NP_001102674 NP_001116653
SP	O77507 P70099 Q06609 Q08297 Q2KJ94
TPG	DAA25435
AlphaFold	O77507 P70099 Q06609 Q08297 Q2KJ94