BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 4282

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: 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:
XRCC1 NTD, polymer, 183 residues, 20217 Da.

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology

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

Data sets:
Data typeCount
1H chemical shifts1201
13C chemical shifts766
15N chemical shifts187

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1XRCC1 NTD1

Entities:

Entity 1, XRCC1 NTD 183 residues - 20217 Da.

1   METPROGLUILEARGLEUARGHISVALVAL
2   SERCYSSERSERGLNASPSERTHRHISCYS
3   ALAGLUASNLEULEULYSALAASPTHRTYR
4   ARGLYSTRPARGALAALALYSALAGLYGLU
5   LYSTHRILESERVALVALLEUGLNLEUGLU
6   LYSGLUGLUGLNILEHISSERVALASPILE
7   GLYASNASPGLYSERALAPHEVALGLUVAL
8   LEUVALGLYSERSERALAGLYGLYALAGLY
9   GLUGLNASPTYRGLUVALLEULEUVALTHR
10   SERSERPHEMETSERPROSERGLUSERARG
11   SERGLYSERASNPROASNARGVALARGMET
12   PHEGLYPROASPLYSLEUVALARGALAALA
13   ALAGLULYSARGTRPASPARGVALLYSILE
14   VALCYSSERGLNPROTYRSERLYSASPSER
15   PROPHEGLYLEUSERPHEVALARGPHEHIS
16   SERPROPROASPLYSASPGLUALAGLUALA
17   PROSERGLNLYSVALTHRVALTHRLYSLEU
18   GLYGLNPHEARGVALLYSGLUGLUGLUGLU
19   SERALAASN

Samples:

sample_1: XRCC1 NTD' '[U-15N; U-13C] 2; .

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYnot availablenot availablenot available
2D 1H-1H TOCSYnot availablenot availablenot available
2D 1H-13C HSQCnot availablenot availablenot available
2D 1H-15N HSQCnot availablenot availablenot available
2D (HB)CB(CGCD)HDnot availablenot availablenot available
3D 1H-1H-15N NOESYnot availablenot availablenot available
3D 13C-1H-1H NOESYnot availablenot availablenot available
3D 1H-1H-15N TOCSYnot availablenot availablenot available
3D 1H-13C-1H HCCH-TOCSYnot availablenot availablenot available
3D CBCA(CO)NHnot availablenot availablenot available
3D HNCACBnot availablenot availablenot available
3D HNCAnot availablenot availablenot available
3D HNCOnot availablenot availablenot available
3D HN(CO)CAnot availablenot availablenot available
3D HCC(CO)NHnot availablenot availablenot available
3D CC(CO)NHnot availablenot availablenot available

Software:

FELIX v97 - data processing

XEASY v1.3.13 - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
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

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts