BMRB Entry 50121

Name: 1H, 15N assignments of single-stranded DNA binding domains from the 70 kDa subunit of Human Replication Protein A bound to ssDNA
Published: 2019-12-20

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50121

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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, 15N assignments of single-stranded DNA binding domains from the 70 kDa subunit of Human Replication Protein A bound to ssDNA

Deposition date:

2019-12-10

Original release date:

2019-12-20

Authors:

Arunkumar, Alphonse

Citation:

Citation: Arunkumar, Alphonse; Stauffer, Melissa; Bochkareva, Elena; Bochkarev, Alexey; Chazin, Walter. "Independent and Coordinated Functions of Replication Protein A Tandem High Affinity Single-stranded DNA Binding Domains" J. Biol. Chem. 278, 41077-41082 (2003).
PubMed: 12881520

Assembly members:

Assembly members:
entity_1, polymer, 242 residues, 27071 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: pSV281

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: QSKVVPIASLTPYQSKWTIC ARVTNKSQIRTWSNSRGEGK LFSLELVDESGEIRATAFNE QVDKFFPLIEVNKVYYFSKG TLKIANKQFTAVKNDYEMTF NNETSVMPCEDDHHLPTVQF DFTGIDDLENKSKDSLVDII GICKSYEDATKITVRSNNAE VAKRNIYLMDTSGKVVTATL WGEDADKFDGSRQPVLAIKG ARVSDFGGRSLSVLSSSTII ANPDIPEAYKLRGYFDAEGG AL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	191
1H chemical shifts	191

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RPA70AB	1

Entities:

Entity 1, RPA70AB 242 residues - 27071 Da.

1

GLN

SER

LYS

VAL

PRO

ILE

ALA

SER

LEU

2

THR

PRO

TYR

GLN

SER

LYS

TRP

THR

ILE

CYS

3

ALA

ARG

VAL

THR

ASN

LYS

SER

GLN

ILE

ARG

4

THR

TRP

SER

ASN

SER

ARG

GLY

GLU

GLY

LYS

5

LEU

PHE

SER

LEU

GLU

LEU

VAL

ASP

GLU

SER

6

GLY

GLU

ILE

ARG

ALA

THR

ALA

PHE

ASN

GLU

7

GLN

VAL

ASP

LYS

PHE

PRO

LEU

ILE

GLU

8

VAL

ASN

LYS

VAL

TYR

PHE

SER

LYS

GLY

9

THR

LEU

LYS

ILE

ALA

ASN

LYS

GLN

PHE

THR

10

ALA

VAL

LYS

ASN

ASP

TYR

GLU

MET

THR

PHE

11

ASN

GLU

THR

SER

VAL

MET

PRO

CYS

GLU

12

ASP

HIS

LEU

PRO

THR

VAL

GLN

PHE

13

ASP

PHE

THR

GLY

ILE

ASP

LEU

GLU

ASN

14

LYS

SER

LYS

ASP

SER

LEU

VAL

ASP

ILE

15

GLY

ILE

CYS

LYS

SER

TYR

GLU

ASP

ALA

THR

16

LYS

ILE

THR

VAL

ARG

SER

ASN

ALA

GLU

17

VAL

ALA

LYS

ARG

ASN

ILE

TYR

LEU

MET

ASP

18

THR

SER

GLY

LYS

VAL

THR

ALA

THR

LEU

19

TRP

GLY

GLU

ASP

ALA

ASP

LYS

PHE

ASP

GLY

20

SER

ARG

GLN

PRO

VAL

LEU

ALA

ILE

LYS

GLY

21

ALA

ARG

VAL

SER

ASP

PHE

GLY

ARG

SER

22

LEU

SER

VAL

LEU

SER

THR

ILE

23

ALA

ASN

PRO

ASP

ILE

PRO

GLU

ALA

TYR

LYS

24

LEU

ARG

GLY

TYR

PHE

ASP

ALA

GLU

GLY

25

ALA

LEU

Samples:

sample_1: entity_1, [U-15N], 50 uM; TRIS 20 ± 1 mM; potassium chloride 150 ± 2 mM; glycerol 10 ± 1 % w/v; DTT 1 ± 0.1 mM

sample_conditions_1: ionic strength: 170 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz