BMRB Entry 4282

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4282

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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, and 13C Resonance Assignments for the N-terminal 20 kDa Domain of the DNA Single-Strand Break Repair Protein XRCC1

Deposition date:

1998-12-10

Original release date:

2000-05-03

Authors:

Marintchev, Assen; Maciejewski, Mark; Mullen, Gregory

Citation:

Citation: Marintchev, Assen; Maciejewski, Mark; Mullen, Gregory. "1H, 15N, and 13C Resonance Assignments for the N-terminal 20 kDa Domain of the DNA Single-Strand Break Repair Protein XRCC1" J. Biomol. NMR 13, 393-394 (1999).

Assembly members:

Assembly members:
XRCC1 NTD, polymer, 183 residues, 20217 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
XRCC1 NTD: MPEIRLRHVVSCSSQDSTHC AENLLKADTYRKWRAAKAGE KTISVVLQLEKEEQIHSVDI GNDGSAFVEVLVGSSAGGAG EQDYEVLLVTSSFMSPSESR SGSNPNRVRMFGPDKLVRAA AEKRWDRVKIVCSQPYSKDS PFGLSFVRFHSPPDKDEAEA PSQKVTVTKLGQFRVKEEEE SAN

Data sets:

assigned_chemical_shifts
- shift_set_1

Data type	Count
1H chemical shifts	1201
13C chemical shifts	766
15N chemical shifts	187

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	XRCC1 NTD	1

Entities:

Entity 1, XRCC1 NTD 183 residues - 20217 Da.

1

MET

PRO

GLU

ILE

ARG

LEU

ARG

HIS

VAL

2

SER

CYS

SER

GLN

ASP

SER

THR

HIS

CYS

3

ALA

GLU

ASN

LEU

LYS

ALA

ASP

THR

TYR

4

ARG

LYS

TRP

ARG

ALA

LYS

ALA

GLY

GLU

5

LYS

THR

ILE

SER

VAL

LEU

GLN

LEU

GLU

6

LYS

GLU

GLN

ILE

HIS

SER

VAL

ASP

ILE

7

GLY

ASN

ASP

GLY

SER

ALA

PHE

VAL

GLU

VAL

8

LEU

VAL

GLY

SER

ALA

GLY

ALA

GLY

9

GLU

GLN

ASP

TYR

GLU

VAL

LEU

VAL

THR

10

SER

PHE

MET

SER

PRO

SER

GLU

SER

ARG

11

SER

GLY

SER

ASN

PRO

ASN

ARG

VAL

ARG

MET

12

PHE

GLY

PRO

ASP

LYS

LEU

VAL

ARG

ALA

13

ALA

GLU

LYS

ARG

TRP

ASP

ARG

VAL

LYS

ILE

14

VAL

CYS

SER

GLN

PRO

TYR

SER

LYS

ASP

SER

15

PRO

PHE

GLY

LEU

SER

PHE

VAL

ARG

PHE

HIS

16

SER

PRO

ASP

LYS

ASP

GLU

ALA

GLU

ALA

17

PRO

SER

GLN

LYS

VAL

THR

VAL

THR

LYS

LEU

18

GLY

GLN

PHE

ARG

VAL

LYS

GLU

19

SER

ALA

ASN

Samples:

sample_1: XRCC1 NTD, [U-15N; U-13C], 2 – 4 mM; DTT 5 mM

Ex-cond: pH: 6.8; temperature: 298 K; ionic strength: 0.4 M

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	not available	not available	not available
2D 1H-1H TOCSY	not available	not available	not available
2D 1H-13C HSQC	not available	not available	not available
2D 1H-15N HSQC	not available	not available	not available
2D (HB)CB(CGCD)HD	not available	not available	not available
3D 1H-1H-15N NOESY	not available	not available	not available
3D 13C-1H-1H NOESY	not available	not available	not available
3D 1H-1H-15N TOCSY	not available	not available	not available
3D 1H-13C-1H HCCH-TOCSY	not available	not available	not available
3D CBCA(CO)NH	not available	not available	not available
3D HNCACB	not available	not available	not available
3D HNCA	not available	not available	not available
3D HNCO	not available	not available	not available
3D HN(CO)CA	not available	not available	not available
3D HCC(CO)NH	not available	not available	not available
3D CC(CO)NH	not available	not available	not available

Software:

FELIX v97 - data processing

XEASY v1.3.13 - data analysis

NMR spectrometers:

Varian INOVA 600 MHz

PDB	1XNA 1XNT 3K75 3K77 3LQC
DBJ	BAD92018 BAG10574 BAG37732 BAG57023
EMBL	CAG33009
GB	AAA63270 AAH23593 AAM34791 EAW57201 EAW57202
REF	NP_006288 XP_001100256 XP_002829368 XP_003281242 XP_003799533
SP	P18887
AlphaFold	P18887