BMRB Entry 25232

Name: Solution structure of the F231L mutant ERCC1-XPF dimerization region
Published: 2015-06-22

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PDB ID: 2mut
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25232
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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:

Solution structure of the F231L mutant ERCC1-XPF dimerization region

Deposition date:

2014-09-17

Original release date:

2015-06-22

Authors:

Faridounnia, Maryam; Wienk, Hans; Kovacic, Lidija; Folkers, Gert; Jaspers, Nicolaas; Kaptein, Robert; Hoeijmakers, Jan; Boelens, Rolf

Citation:

Citation: Faridounnia, Maryam; Wienk, Hans; Kovacic, Lidija; Folkers, Gert; Jaspers, Nicolaas; Boelens, Rolf. "The Cerebro-Oculo-Facio-Skeletal (COFS) Syndrome point mutation F231L in the ERCC1 DNA repair protein causes dissociation of the ERCC1-XPF complex" J. Biol. Chem. ., .-. (2015).
PubMed: 26085086

Assembly members:

Assembly members:
entity_1, polymer, 96 residues, 10985.764 Da.
entity_2, polymer, 84 residues, 9230.592 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: pET28B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: RIRRRYNMADLLMEKLEQDL VSRVTECLTTVKSVNKTDSQ TLLTTFGSLEQLIAASREDL ALCPGLGPQKARRLFDVLHE PFLKVPGGLEHHHHHH
entity_2: MDSETLPESEKYNPGPQDFL LKMPGVNAKNCRSLMHHVKN IAELAALSQDELTSILGNAA NAKQLYDFIHTSFAEVVSKG KGKK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	695
15N chemical shifts	172
1H chemical shifts	1173

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2

Entities:

Entity 1, entity_1 96 residues - 10985.764 Da.

1

ARG

ILE

ARG

TYR

ASN

MET

ALA

ASP

2

LEU

MET

GLU

LYS

LEU

GLU

GLN

ASP

LEU

3

VAL

SER

ARG

VAL

THR

GLU

CYS

LEU

THR

4

VAL

LYS

SER

VAL

ASN

LYS

THR

ASP

SER

GLN

5

THR

LEU

THR

PHE

GLY

SER

LEU

GLU

6

GLN

LEU

ILE

ALA

SER

ARG

GLU

ASP

LEU

7

ALA

LEU

CYS

PRO

GLY

LEU

GLY

PRO

GLN

LYS

8

ALA

ARG

LEU

PHE

ASP

VAL

LEU

HIS

GLU

9

PRO

PHE

LEU

LYS

VAL

PRO

GLY

LEU

GLU

10

HIS

Entity 2, entity_2 84 residues - 9230.592 Da.

1

MET

ASP

SER

GLU

THR

LEU

PRO

GLU

SER

GLU

2

LYS

TYR

ASN

PRO

GLY

PRO

GLN

ASP

PHE

LEU

3

LEU

LYS

MET

PRO

GLY

VAL

ASN

ALA

LYS

ASN

4

CYS

ARG

SER

LEU

MET

HIS

VAL

LYS

ASN

5

ILE

ALA

GLU

LEU

ALA

LEU

SER

GLN

ASP

6

GLU

LEU

THR

SER

ILE

LEU

GLY

ASN

ALA

7

ASN

ALA

LYS

GLN

LEU

TYR

ASP

PHE

ILE

HIS

8

THR

SER

PHE

ALA

GLU

VAL

SER

LYS

GLY

9

LYS

GLY

LYS

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.4 mM; entity_2, [U-100% 13C; U-100% 15N], 0.4 mM; D2O 8%; H2O 92%; sodium phosphate 50 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 250 mM; pH: 7.0; pressure: 1 atm; temperature: 290 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D HSQC	sample_1	isotropic	sample_conditions_1
triple resonance	sample_1	isotropic	sample_conditions_1
NOESY	sample_1	isotropic	sample_conditions_1
2D HSQC	sample_1	isotropic	sample_conditions_1
2D HSQC	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

SPARKY, Goddard - chemical shift assignment, data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

CING, Doreleijers et al - validation

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 600 MHz
Bruker Avance 750 MHz
Bruker Avance 900 MHz

PDB	1Z00 2A1J 2MUT
DBJ	BAG37398 BAG52472
GB	AAA35810 AAA52394 AAC16253 AAH08930 AAM34796
PRF	1403276A
REF	NP_001181860 NP_001974 XP_003817569 XP_003915760 XP_003915761
SP	P07992
AlphaFold	P07992 Q8TD83