BMRB Entry 5878

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PDB ID: 1ssf
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR5878
MolProbity Validation Chart

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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:

1H, 13C and 15N NMR assignment of the region 1463-1617 of mouse p53 Binding Protein 1 (53BP1)

Deposition date:

2003-07-22

Original release date:

2004-02-11

Authors:

Charier, Gaelle; Alpha-Bazin, Beatrice; Couprie, Joel; Callebaut, Isabelle; Berenguer, Frederic; Quemeneur, Eric; Gilquin, Bernard; Zinn-Justin, Sophie

Citation:

Citation: Charier, Gaelle; Alpha-Bazin, Beatrice; Couprie, Joel; Callebaut, Isabelle; Berenguer, Frederic; Quemeneur, Eric; Gilquin, Bernard; Zinn-Justin, Sophie. "Letter to the Editor: 1H, 13C and 15N resonance assignments of the region 1463-1617 of the mouse p53 Binding Protein 1 (53BP1) " J. Biomol. NMR 28, 303-304 (2004).
PubMed: 14752266

Assembly members:

Assembly members:
p53 Binding Protein 1, polymer, 155 residues, 17345 Da.

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pDEST15

Entity Sequences (FASTA):

Entity Sequences (FASTA):
p53 Binding Protein 1: DSSSSGNSFVGLRVVAKWSS NGYFYSGKITRDVGAGKYKL LFDDGYECDVLGKDILLCDP IPLDTEVTALSEDEYFSAGV VKGHRKESGELYYSIEKEGQ RKWYKRMAVILSLEQGNRLR EQYGLGPYEAVTPLTKAADI SLDNLVEGKRKRRSN

Data sets:

assigned_chemical_shifts
- shift_set_1
- shift_set_2

Data type	Count
1H chemical shifts	1023
13C chemical shifts	676
15N chemical shifts	162

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	53BP1 subunit 1	1

Entities:

Entity 1, 53BP1 subunit 1 155 residues - 17345 Da.

1

ASP

SER

GLY

ASN

SER

PHE

VAL

2

GLY

LEU

ARG

VAL

ALA

LYS

TRP

SER

3

ASN

GLY

TYR

PHE

TYR

SER

GLY

LYS

ILE

THR

4

ARG

ASP

VAL

GLY

ALA

GLY

LYS

TYR

LYS

LEU

5

LEU

PHE

ASP

GLY

TYR

GLU

CYS

ASP

VAL

6

LEU

GLY

LYS

ASP

ILE

LEU

CYS

ASP

PRO

7

ILE

PRO

LEU

ASP

THR

GLU

VAL

THR

ALA

LEU

8

SER

GLU

ASP

GLU

TYR

PHE

SER

ALA

GLY

VAL

9

VAL

LYS

GLY

HIS

ARG

LYS

GLU

SER

GLY

GLU

10

LEU

TYR

SER

ILE

GLU

LYS

GLU

GLY

GLN

11

ARG

LYS

TRP

TYR

LYS

ARG

MET

ALA

VAL

ILE

12

LEU

SER

LEU

GLU

GLN

GLY

ASN

ARG

LEU

ARG

13

GLU

GLN

TYR

GLY

LEU

GLY

PRO

TYR

GLU

ALA

14

VAL

THR

PRO

LEU

THR

LYS

ALA

ASP

ILE

15

SER

LEU

ASP

ASN

LEU

VAL

GLU

GLY

LYS

ARG

16

LYS

ARG

SER

ASN

Samples:

sample_1: p53 Binding Protein 1, [U-95% 13C; U-95% 15N], 0.8 mM; Tris-HCl 50 mM; NaCl 150 mM; D2O 100%

sample_2: p53 Binding Protein 1, [U-95% 13C; U-95% 15N], 0.8 mM; Tris-HCl 50 mM; NaCl 150 mM; H2O 90%; D2O 10%

sample_3: p53 Binding Protein 1, [U-95% 15N], 0.7 mM; Tris-HCl 50 mM; NaCl 150 mM; H2O 90%; D2O 10%

condition_1: pH: 7.1; temperature: 300 K; ionic strength: 0.2 M

condition_2: pH*: 7.0; temperature: 300 K; ionic strength: 0.2 M

Experiments:

Name	Sample	Sample state	Sample conditions
1H-15N HSQC	not available	not available	not available
HNCO	not available	not available	not available
HNCA	not available	not available	not available
HN(CO)CA	not available	not available	not available
CBCA(CO)NH	not available	not available	not available
CBCANH	not available	not available	not available
CBCACOHA	not available	not available	not available
HNHA	not available	not available	not available
(HCA)CO(CA)NH	not available	not available	not available
15N HSQC NOESY	not available	not available	not available
HBHA(CO)NH	not available	not available	not available
HCCH TOSCY	not available	not available	not available
HCCH COSY	not available	not available	not available
13C HSQC NOESY	not available	not available	not available

Software:

NMRPipe v2.0 - data processing

FELIX v2000 - data analysis

NMR spectrometers:

Bruker DRX 500 MHz
Bruker DRX 600 MHz

BMRB	18579 25347 25348
PDB	1SSF 1XNI 2G3R 2IG0 2LVM 2MWO 2MWP 3LGF 3LGL 3LH0 4CRI 4RG2
DBJ	BAC26637 BAC29383 BAE06107 BAE21103 BAG10235
EMBL	CAC94013 CAD97660
GB	AAA21596 AAC62018 AAH35206 AAH79906 AAI12162
REF	NP_001135451 NP_001135452 NP_001162434 NP_001193326 NP_001277759
SP	P70399 Q12888
AlphaFold	P70399 Q12888