BMRB Entry 4899

Name: SMN Tudor Domain Structure and its Interaction with the Sm Proteins
Published: 2001-05-03

Click here to enlarge.

PDB ID: 1g5v
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4899
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

SMN Tudor Domain Structure and its Interaction with the Sm Proteins

Deposition date:

2000-11-15

Original release date:

2001-05-03

Authors:

Selenko, Philipp; Sprangers, Remco; Stier, Gunter; Buehler, Dirk; Fischer, Utz; Sattler, Michael

Citation:

Citation: Selenko, Philipp; Sprangers, Remco; Stier, Gunter; Buehler, Dirk; Fischer, Utz; Sattler, Michael. "SMN Tudor Domain Structure and its Interaction with the Sm Proteins" Nat. Struct. Biol. 8, 27-31 (2001).
PubMed: 11135666

Assembly members:

Assembly members:
Survival of Motor Neurons protein, polymer, 91 residues, 10049.0 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: pET9d

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Survival of Motor Neurons protein: GAMKKNTAASLQQWKVGDKC SAIWSEDGCIYPATIASIDF KRETCVVVYTGYGNREEQNL SDLLSPICEVANNIEQNAQE NENESQVSTDE

Data sets:

assigned_chemical_shifts
- shift_set_1

Data type	Count
13C chemical shifts	188
15N chemical shifts	61
1H chemical shifts	373

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	tudor	1

Entities:

Entity 1, tudor 91 residues - 10049.0 Da.

1

GLY

ALA

MET

LYS

ASN

THR

ALA

SER

2

LEU

GLN

TRP

LYS

VAL

GLY

ASP

LYS

CYS

3

SER

ALA

ILE

TRP

SER

GLU

ASP

GLY

CYS

ILE

4

TYR

PRO

ALA

THR

ILE

ALA

SER

ILE

ASP

PHE

5

LYS

ARG

GLU

THR

CYS

VAL

TYR

THR

6

GLY

TYR

GLY

ASN

ARG

GLU

GLN

ASN

LEU

7

SER

ASP

LEU

SER

PRO

ILE

CYS

GLU

VAL

8

ALA

ASN

ILE

GLU

GLN

ASN

ALA

GLN

GLU

9

ASN

GLU

ASN

GLU

SER

GLN

VAL

SER

THR

ASP

10

GLU

Samples:

sample_1: Survival of Motor Neurons protein, [U-100% 15N], 1.0 mM; sodium chloride 20 mM; phosphate buffer 30 mM; H2O 95%; D2O 5%

sample_2: Survival of Motor Neurons protein, [U-100% 13C; U-100% 15N], 1.0 mM; sodium chloride 20 mM; phosphate buffer 30 mM; H2O 95%; D2O 5%

sample_3: Survival of Motor Neurons protein, [U-100% 13C; U-100% 15N], 1.0 mM; sodium chloride 20 mM; phosphate buffer 30 mM; D2O 100%

Cond_sample_1: pH: 6.3; pressure: 1 atm; temperature: 295 K

Cond_sample_2: pH: 6.3; pressure: 1 atm; temperature: 295 K

Experiments:

Name	Sample	Sample state	Sample conditions
HNCA	not available	not available	not available
HN(CO)CA	not available	not available	not available
CBCANH	not available	not available	not available
CBCA(CO)NH	not available	not available	not available
H(C)CH TOCSY	not available	not available	not available
CCH TOCSY	not available	not available	not available
15N edited NOESY	not available	not available	not available
13C edited NOESY	not available	not available	not available
IPAP (dipolar couplings)	not available	not available	not available

Software:

xwinnmr v2.6 - recording experiments

NMRPipe - processing spectra

XEASY - chemical shift assignment

CNS - structure calculations

NMR spectrometers:

Bruker DRX 500 MHz
Bruker DRX 600 MHz

BMRB	18005 18007
PDB	1G5V 1MHN 4A4E 4A4G 4QQ6
DBJ	BAF82358 BAJ21116
EMBL	CAH89989
GB	AAA64505 AAA66242 AAC50473 AAC52048 AAC62262
REF	NP_000335 NP_001124942 NP_001284644 NP_059107 NP_075012
SP	Q16637 Q5RE18
AlphaFold	Q16637 Q5RE18