BMRB Entry 6298

Name: NMR STRUCTURE OF HUMAN HISTONE CHAPERONE, ASF1A
Published: 2005-11-07

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PDB ID: 1tey
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6298
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR STRUCTURE OF HUMAN HISTONE CHAPERONE, ASF1A

Deposition date:

2004-08-26

Original release date:

2005-11-07

Authors:

MOUSSON, F.; LAUTRETTE, A.; THURET, J.; AGEZ, M.; AMIGUES, B.; BECKER, E.; COURBEYRETTE, R.; NEUMANN, J.; GUEROIS, R.; MANN, C.; OCHSENBEIN, F.

Citation:

Citation: Mousson, Florence; Couprie, Joel; Thuret, Jean-Yves; Neumann, Jean-Michel; Mann, Carl; Ochsenbein, Francoise. "Letter to the Editor: 1H, 13C and 15N Resonance Assignments of the Conserved Core of hAsf1 A" J. Biomol. NMR 29, 413-414 (2004).

Assembly members:

Assembly members:
ASF1 anti-silencing function 1 homolog A, polymer, 156 residues, Formula weight is not available

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: PETM30

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ASF1 anti-silencing function 1 homolog A: MAKVQVNNVVVLDNPSPFYN PFQFEITFECIEDLSEDLEW KIIYVGSAESEEYDQVLDSV LVGPVPAGRHMFVFQADAPN PGLIPDADAVGVTVVLITCT YRGQEFIRVGYYVNNEYTET ELRENPPVKPDFSKLQRNIL ASNPRVTRFHINWEDN

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1

Data type	Count
1H chemical shifts	1091
13C chemical shifts	668
15N chemical shifts	166

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Four-helix bundle model	1

Entities:

Entity 1, Four-helix bundle model 156 residues - Formula weight is not available

1

MET

ALA

LYS

VAL

GLN

VAL

ASN

VAL

2

VAL

LEU

ASP

ASN

PRO

SER

PRO

PHE

TYR

ASN

3

PRO

PHE

GLN

PHE

GLU

ILE

THR

PHE

GLU

CYS

4

ILE

GLU

ASP

LEU

SER

GLU

ASP

LEU

GLU

TRP

5

LYS

ILE

TYR

VAL

GLY

SER

ALA

GLU

SER

6

GLU

TYR

ASP

GLN

VAL

LEU

ASP

SER

VAL

7

LEU

VAL

GLY

PRO

VAL

PRO

ALA

GLY

ARG

HIS

8

MET

PHE

VAL

PHE

GLN

ALA

ASP

ALA

PRO

ASN

9

PRO

GLY

LEU

ILE

PRO

ASP

ALA

ASP

ALA

VAL

10

GLY

VAL

THR

VAL

LEU

ILE

THR

CYS

THR

11

TYR

ARG

GLY

GLN

GLU

PHE

ILE

ARG

VAL

GLY

12

TYR

VAL

ASN

GLU

TYR

THR

GLU

THR

13

GLU

LEU

ARG

GLU

ASN

PRO

VAL

LYS

PRO

14

ASP

PHE

SER

LYS

LEU

GLN

ARG

ASN

ILE

LEU

15

ALA

SER

ASN

PRO

ARG

VAL

THR

ARG

PHE

HIS

16

ILE

ASN

TRP

GLU

ASP

ASN

Samples:

sample_1: ASF1 anti-silencing function 1 homolog A, [U-15N; U-13C], 1 mM; tris-D11 20 mM; EDTA 1 mM; DSS 0.1 mM; NaN3 0.1 mM; H2O 90%; D2O 10%

sample_cond_1: pH: 7.4; temperature: 298 K; ionic strength: 20 mM; pressure: 1 atm

Experiments:

Name	Sample	Sample state	Sample conditions
3D 13C-separated NOESY	sample_1	not available	sample_cond_1
3D 15N-separated NOESY	sample_1	not available	sample_cond_1
HNHA	sample_1	not available	sample_cond_1

Software:

XWINNMR v3.1 - collection, processing

SPARKY v3.106 - data analysis

ARIA v1.1 - refinement

NMR spectrometers:

Bruker DRX 600 MHz

PDB	1TEY 2I32 2IIJ 2IO5 3AAD
DBJ	BAA96542 BAB15228 BAB25269 BAB26770 BAB28198
EMBL	CAB43363 CAG33628
GB	AAD34093 AAF29110 AAH10878 AAH27628 AAI12652
REF	NP_001038155 NP_001069961 NP_001086449 NP_001099859 NP_001159660
SP	Q2KIG1 Q3C1E9 Q69DB9 Q9CQE6 Q9Y294
TPG	DAA26326
AlphaFold	Q2KIG1 Q3C1E9 Q69DB9 Q9CQE6 Q9Y294 Q2KIG1 Q3C1E9 Q69DB9 Q9CQE6 Q9Y294