BMRB Entry 19302

Name: Solution Structure of ERCC4 domain of human FAAP24
Published: 2013-09-16

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PDB ID: 2m9m
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19302
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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 ERCC4 domain of human FAAP24

Deposition date:

2013-06-18

Original release date:

2013-09-16

Authors:

Wu, Fangming; Han, Xiao; Shi, Chaowei; Gong, Weimin; Tian, Changlin

Citation:

Citation: Wang, Yucai; Han, Xiao; Wu, Fangming; Leung, Justin; Lowery, Megan; Do, Huong; Chen, Junjie; Shi, Chaowei; Tian, Changlin; Li, Lei; Gong, Weimin. "Structure analysis of FAAP24 reveals single-stranded DNA-binding activity and domain functions in DNA damage response." Cell Res. 23, 1215-1228 (2013).
PubMed: 23999858

Assembly members:

Assembly members:
FAAP24-ERCC4, polymer, 147 residues, 15680.295 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: pET-22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FAAP24-ERCC4: MEKNPPDDTGPVHVPLGHIV ANEKWRGSQLAQEMQGKIKL IFEDGLTPDFYLSNRCCILY VTEADLVAGNGYRKRLVRVR NSNNLKGIVVVEKTRMSEQY FPALQKFTVLDLGMVLLPVA SQMEASCLVIQLVQEQTKEL EHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	542
15N chemical shifts	131
1H chemical shifts	867

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ERCC4 domain of human FAAP24	1

Entities:

Entity 1, ERCC4 domain of human FAAP24 147 residues - 15680.295 Da.

1

MET

GLU

LYS

ASN

PRO

ASP

THR

GLY

2

PRO

VAL

HIS

VAL

PRO

LEU

GLY

HIS

ILE

VAL

3

ALA

ASN

GLU

LYS

TRP

ARG

GLY

SER

GLN

LEU

4

ALA

GLN

GLU

MET

GLN

GLY

LYS

ILE

LYS

LEU

5

ILE

PHE

GLU

ASP

GLY

LEU

THR

PRO

ASP

PHE

6

TYR

LEU

SER

ASN

ARG

CYS

ILE

LEU

TYR

7

VAL

THR

GLU

ALA

ASP

LEU

VAL

ALA

GLY

ASN

8

GLY

TYR

ARG

LYS

ARG

LEU

VAL

ARG

VAL

ARG

9

ASN

SER

ASN

LEU

LYS

GLY

ILE

VAL

10

VAL

GLU

LYS

THR

ARG

MET

SER

GLU

GLN

TYR

11

PHE

PRO

ALA

LEU

GLN

LYS

PHE

THR

VAL

LEU

12

ASP

LEU

GLY

MET

VAL

LEU

PRO

VAL

ALA

13

SER

GLN

MET

GLU

ALA

SER

CYS

LEU

VAL

ILE

14

GLN

LEU

VAL

GLN

GLU

GLN

THR

LYS

GLU

LEU

15

GLU

HIS

Samples:

sample_1: FAAP24-ERCC4, [U-100% 13C; U-100% 15N], 0.5 – 0.8 mM; potassium phosphate 50 mM; sodium chloride 50 mM; beta-mercaptoethanol 1 mM; EDTA 0.5 mM; H2O 90%; D2O 10%

sample_2: FAAP24-ERCC4, [U-100% 13C; U-100% 15N], 0.5 – 0.8 mM; potassium phosphate 50 mM; sodium chloride 50 mM; beta-mercaptoethanol 1 mM; EDTA 0.5 mM; D2O 100%

sample_conditions_1: ionic strength: 0.35 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HCCH-COSY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

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

TALOS, Cornilescu, Delaglio and Bax - data analysis

SPARKY, Goddard - chemical shift assignment

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

Bruker Avance 850 MHz
Varian INOVA 700 MHz

UNP	Q9BTP7
PDB	2M9M 4BXO 4M6W
DBJ	BAG54708
GB	AAH03535 AAH10170 AAH20247 ADQ32151 AIC52732
REF	NP_689479 XP_003780763 XP_003915337 XP_004093270 XP_005259450
SP	Q9BTP7
AlphaFold	Q96FX6 Q9BTP7