BMRB Entry 26517

Name: TAM DOMAIN OF TIP5_BAZ2A
Published: 2015-04-28

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PDB ID: 5agq
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26517
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:

TAM DOMAIN OF TIP5_BAZ2A

Deposition date:

2015-02-23

Original release date:

2015-04-28

Authors:

Anosova, I.; Melnik, S.; Tripsianes, Kostas; Kateb, F.; Grummt, I.; Sattler, M.

Citation:

Citation: Anosova, I.; Melnik, S.; Tripsianes, Kostas; Kateb, F.; Grummt, I.; Sattler, M.. "A novel RNA binding surface of the TAM domain of TIP5/BAZ2A mediates epigenetic regulation of rRNA genes" Nucleic Acids Res. ., .-. (2015).

Assembly members:

Assembly members:
entity_1, polymer, 109 residues, 13011.8499 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: RRRIATPEEVRLPLQHGWRR EVRIKKGSHRWQGETWYYGP CGKRMKQFPEVIKYLSRNVV HSVRREHFSFSPRMPVGDFF EERDTPEGLQWVQLSAEEIP SRIQAITGS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list

Data type	Count
13C chemical shifts	392
15N chemical shifts	107
1H chemical shifts	788

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TAM DOMAIN OF TIP5_BAZ2A	1

Entities:

Entity 1, TAM DOMAIN OF TIP5_BAZ2A 109 residues - 13011.8499 Da.

1

ARG

ILE

ALA

THR

PRO

GLU

VAL

2

ARG

LEU

PRO

LEU

GLN

HIS

GLY

TRP

ARG

3

GLU

VAL

ARG

ILE

LYS

GLY

SER

HIS

ARG

4

TRP

GLN

GLY

GLU

THR

TRP

TYR

GLY

PRO

5

CYS

GLY

LYS

ARG

MET

LYS

GLN

PHE

PRO

GLU

6

VAL

ILE

LYS

TYR

LEU

SER

ARG

ASN

VAL

7

HIS

SER

VAL

ARG

GLU

HIS

PHE

SER

PHE

8

SER

PRO

ARG

MET

PRO

VAL

GLY

ASP

PHE

9

GLU

ARG

ASP

THR

PRO

GLU

GLY

LEU

GLN

10

TRP

VAL

GLN

LEU

SER

ALA

GLU

ILE

PRO

11

SER

ARG

ILE

GLN

ALA

ILE

THR

GLY

SER

Samples:

sample_new_1: TAM, [U-13C; U-15N], 0.6 mM; sodium phosphate 20 mM; NACL 50 mM; DTT 1 mM

sample_conditions_new_1: ionic strength: 100.000 mM; pH: 7.000; pressure: 1.000 atm; temperature: 293.000 K

Experiments:

Name	Sample	Sample state	Sample conditions
15N-HSQC	sample_new_1	solution	sample_conditions_new_1
13C-HSQC	sample_new_1	solution	sample_conditions_new_1
HNCACB	sample_new_1	solution	sample_conditions_new_1
HN(CO)CACB	sample_new_1	solution	sample_conditions_new_1
CC(CO)NH-TOCSY	sample_new_1	solution	sample_conditions_new_1
HCCH-TOCSY	sample_new_1	solution	sample_conditions_new_1
15N-EDITED 3D NOESY	sample_new_1	solution	sample_conditions_new_1
13C-EDITED 3D NOESY (ALIPHATICS)	sample_new_1	solution	sample_conditions_new_1
13C-EDITED 3D NOESY (AROMATICS)	sample_new_1	solution	sample_conditions_new_1

Software:

AutoDep v4.3, PDBe - chemical shift assignment

CNS vany, Brunger, Adams, Clore, Gros, Nilges and Read - chemical shift assignment

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - chemical shift assignment

CcpNmr_Analysis v2.3, CCPN - chemical shift assignment, data analysis

SPARKY vany, Goddard - chemical shift assignment

NMR spectrometers:

BRUKER AVANCE 900 MHz

UNP	BAZ2A_HUMAN
PDB	5AGQ
DBJ	BAA20773 BAA89211 BAC31656 BAE21532 BAE33307
EMBL	CAC69992 CAH18232
GB	AAB60864 AAH20083 AAH38012 AAH48415 AAI48496
REF	NP_001100628 NP_001180159 NP_001287834 NP_038477 NP_473419
SP	Q91YE5 Q9UIF9
TPG	DAA29585
AlphaFold	Q96H26 Q91YE5 Q9UIF9