BMRB Entry 17673

Name: Not Available
Published: 2012-05-09

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PDB ID: 2ldm
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17673
MolProbity Validation Chart

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

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Title:

Not Available

Deposition date:

2011-05-30

Original release date:

2012-05-09

Authors:

Cui, Gaofeng; Botuyan, Maria; Mer, Georges

Citation:

Citation: Cui, Gaofeng; Park, Sungman; Badeaux, Aimee; Kim, Donghwa; Lee, Joseph; Thompson, James; Yan, Fei; Kaneko, Satoshi; Yuan, Zengqiang; Botuyan, Maria; Bedford, Mark; Cheng, Jin; Mer, Georges. "PHF20 is an effector protein of p53 double lysine methylation that stabilizes and activates p53" Nat. Struct. Mol. Biol. 19, 916-924 (2012).
PubMed: 22864287

Assembly members:

Assembly members:
entity, polymer, 81 residues, 8743.901 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: pTEV

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GHMSSEFQINEQVLASWSDS RFYPAKVTAVNKDGTYTVKF YDGVVQTVKHIHVKAFSKDQ NIVGNARGSRAHSSHLXSKK G

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	306
15N chemical shifts	78
1H chemical shifts	519

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TDRD7	1

Entities:

Entity 1, TDRD7 81 residues - 8743.901 Da.

X=M2L

1

GLY

HIS

MET

SER

GLU

PHE

GLN

ILE

ASN

2

GLU

GLN

VAL

LEU

ALA

SER

TRP

SER

ASP

SER

3

ARG

PHE

TYR

PRO

ALA

LYS

VAL

THR

ALA

VAL

4

ASN

LYS

ASP

GLY

THR

TYR

THR

VAL

LYS

PHE

5

TYR

ASP

GLY

VAL

GLN

THR

VAL

LYS

HIS

6

ILE

HIS

VAL

LYS

ALA

PHE

SER

LYS

ASP

GLN

7

ASN

ILE

VAL

GLY

ASN

ALA

ARG

GLY

SER

ARG

8

ALA

HIS

SER

HIS

LEU

M2L

SER

LYS

9

GLY

Samples:

sample_1: entity, [U-100% 15N], 1 mM; sodium phosphate 25 mM; DSS 0.3 mM; H2O 90%; D2O 10%

sample_2: entity, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 25 mM; DSS 0.3 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.025 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HN(CA)CO	sample_2	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_2	isotropic	sample_conditions_1
2D (HB)CB(CGCD)HD	sample_2	isotropic	sample_conditions_1
2D (HB)CB(CGCDCE)HE	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - peak picking, processing

SANE, Duggan, Legge, Dyson & Wright - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER v8, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMR spectrometers:

Bruker Avance 700 MHz