BMRB Entry 18008

Name: TBA
Published: 2011-11-02

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PDB ID: 4a4h
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18008
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:

TBA

Deposition date:

2011-10-18

Original release date:

2011-11-02

Authors:

Tripsianes, Konstantinos; Madl, T.; Machyna, M.; Fessas, D.; Englbrecht, C.; Neugebauer, U.; Sattler, M.

Citation:

Citation: Tripsianes, Konstantinos; Madl, T.; Machyna, M.; Fessas, D.; Englbrecht, C.; Fischer, U.; Neugebauer, K.; Sattler, M.. "Structural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteins" Nat. Struct. Mol. Biol. 18, 1414-1420 (2011).
PubMed: 22101937

Assembly members:

Assembly members:
A, polymer, 64 residues, 6921.46 Da.
DA2, non-polymer, 202.254 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: na

Entity Sequences (FASTA):

Entity Sequences (FASTA):
A: ASTQPTHSWKVGDKCMAVWS EDGQCYEAEIEEIDEENGTA AITFAGYGNAEVTPLLNLKP VEEG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list

Data type	Count
13C chemical shifts	200
15N chemical shifts	67
1H chemical shifts	435

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	protein	1
2	DA2	2

Entities:

Entity 1, protein 64 residues - 6921.46 Da.

1

ALA

SER

THR

GLN

PRO

THR

HIS

SER

TRP

LYS

2

VAL

GLY

ASP

LYS

CYS

MET

ALA

VAL

TRP

SER

3

GLU

ASP

GLY

GLN

CYS

TYR

GLU

ALA

GLU

ILE

4

GLU

ILE

ASP

GLU

ASN

GLY

THR

ALA

5

ALA

ILE

THR

PHE

ALA

GLY

TYR

GLY

ASN

ALA

6

GLU

VAL

THR

PRO

LEU

ASN

LEU

LYS

PRO

7

VAL

GLU

GLY

Entity 2, DA2 - C8 H18 N4 O2 - 202.254 Da.

1

DA2

Samples:

sample_new_1: SPF30, [U-13C; U-15N], 4 mM; DA2 18 mM; H2O 93%; D2O 7%; phosphate 20 mM; NaCl 50 mM

sample_conditions_new_1: ionic strength: 50.000 mM; pH: 6.5; pressure: 1.000 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
15N-EDITED 3D NOESY F1 15N/13C FILTERED	sample_new_1	solution	sample_conditions_new_1
15N-EDITED 3D NOESY	sample_new_1	solution	sample_conditions_new_1
13C-EDITED 3D NOESY (ALIPHATICSS) F1 15N/13C FILTERED	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) F1 15N/13C FILTERED	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, AutoDep - chemical shift assignment

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

CYANA vany, Guntert, Mumenthaler and Wuthrich - chemical shift assignment

ANALYSIS v2.1, CCPN - chemical shift assignment

TALOS vany, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

BRUKER AVANCE 750 MHz

UNP	SPF30_HUMAN
BMRB	18006
PDB	4A4F 4A4H
DBJ	BAC37414 BAC41064 BAG36724
EMBL	CAH93075
GB	AAC64086 AAC84148 AAH11234 AAH58779 AAH97986
REF	NP_001020571 NP_001030311 NP_001030414 NP_001126821 NP_001159781
SP	O75940 Q3T045 Q4QQU6 Q5R591 Q8BGT7
TPG	DAA14726
AlphaFold	Q5T3K6 O75940 Q3T045 Q4QQU6 Q5R591 Q8BGT7