BMRB Entry 15240

Name: Solution structure of the ERCC1 central domain
Published: 2007-08-28

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PDB ID: 2jpd
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15240
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution structure of the ERCC1 central domain PubMed: 17720715

Deposition date: 2007-05-07 Original release date: 2007-08-28

Authors: Tripsianes, Konstantinos; Folkers, Gert; Zheng, Chao; Das, Devashish; Grinstead, Jeffrey; Kaptein, Robert; Boelens, Rolf

Citation: Tripsianes, Konstantinos; Folkers, Gert; Zheng, Chao; Das, Devashish; Grinstead, Jeffrey; Kaptein, Robert; Boelens, Rolf. "Analysis of the XPA and ssDNA-binding surfaces on the central domain of human ERCC1 reveals evidence for subfunctionalization" Nucleic Acids Res. 35, 5789-5798 (2007).

Assembly members:
ERCC1 central, polymer, 135 residues, 14153.570 Da.

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

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):
ERCC1 central: MAKSNSIIVSPRQRGNPVLK FVRNVPWEFGDVIPDYVLGQ STCALFLSLRYHNLHPDYIH GRLQSLGKNFALRVLLVQVD VKDPQQALKELAKMCILADC TLILAWSPEEAGRYLETYKA YEQKPGGLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	443
15N chemical shifts	125
1H chemical shifts	914

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ERCC1 central	1

Entities:

Entity 1, ERCC1 central 135 residues - 14153.570 Da.

1

MET

ALA

LYS

SER

ASN

SER

ILE

VAL

SER

2

PRO

ARG

GLN

ARG

GLY

ASN

PRO

VAL

LEU

LYS

3

PHE

VAL

ARG

ASN

VAL

PRO

TRP

GLU

PHE

GLY

4

ASP

VAL

ILE

PRO

ASP

TYR

VAL

LEU

GLY

GLN

5

SER

THR

CYS

ALA

LEU

PHE

LEU

SER

LEU

ARG

6

TYR

HIS

ASN

LEU

HIS

PRO

ASP

TYR

ILE

HIS

7

GLY

ARG

LEU

GLN

SER

LEU

GLY

LYS

ASN

PHE

8

ALA

LEU

ARG

VAL

LEU

VAL

GLN

VAL

ASP

9

VAL

LYS

ASP

PRO

GLN

ALA

LEU

LYS

GLU

10

LEU

ALA

LYS

MET

CYS

ILE

LEU

ALA

ASP

CYS

11

THR

LEU

ILE

LEU

ALA

TRP

SER

PRO

GLU

12

ALA

GLY

ARG

TYR

LEU

GLU

THR

TYR

LYS

ALA

13

TYR

GLU

GLN

LYS

PRO

GLY

LEU

GLU

HIS

14

HIS

Samples:

sample_1: ERCC1 central, [U-13C; U-15N], 0.8 mM; sodium phosphate 50 mM; sodium chloride 100 mM

sample_2: ERCC1 central, [U-15N], 0.8 mM; sodium phosphate 50 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 5.5; pressure: 1 atm; temperature: 290 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D (H)CCH 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
2D NOESY 15N filtered	sample_1	isotropic	sample_conditions_1

Software:

CYANA v2.0, Guntert, Mumenthaler and Wuthrich - structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - data analysis, peak picking

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 900 MHz

PDB	2A1I 2JNW 2JPD
DBJ	BAB62810 BAG37398
GB	AAA35810 AAA52394 AAC16253 AAH08930 AAH52813
PRF	1403276A
REF	NP_001159521 NP_001181860 NP_001974 NP_973730 XP_001105868
SP	P07992

Biological Magnetic Resonance Data Bank