BMRB Entry 18471

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for PWWP domain from Trypanosoma brucei
Published: 2012-08-29

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PDB ID: 2nas
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18471
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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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for PWWP domain from Trypanosoma brucei

Deposition date:

2012-05-17

Original release date:

2012-08-29

Authors:

Dai, Kun; Liao, Shanhui; Zhang, Jiahai; Tu, Xiaoming

Citation:

Citation: Zhang, Jiahai; Dai, Kun; Liao, Shanhui; Tu, Xiaoming. "H, C and N resonance assignments of TbTFIIS2-2 PWWP domain from Trypanosoma brucei." Biomol. NMR Assignments 7, 207-209 (2013).
PubMed: 22836947

Assembly members:

Assembly members:
PWWP_domain, polymer, 118 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Kinetoplastids Taxonomy ID: 5691 Superkingdom: Eukaryota Kingdom: not available Genus/species: Trypanosoma brucei

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: Pet22(b)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PWWP_domain: MIPSFAPGTLVWLKQDRFPW WPGFVMDPDEVRDITLPEGS DVWVCCLPRDSLTLSAANSE DEGQIRYFLPDRDEGMMEEG KLDASCAVAIEEAIQLYEEQ LKAQAGGTNELEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	298
15N chemical shifts	101
1H chemical shifts	645

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PWWP_domain	1

Entities:

Entity 1, PWWP_domain 118 residues - Formula weight is not available

1

MET

ILE

PRO

SER

PHE

ALA

PRO

GLY

THR

LEU

2

VAL

TRP

LEU

LYS

GLN

ASP

ARG

PHE

PRO

TRP

3

TRP

PRO

GLY

PHE

VAL

MET

ASP

PRO

ASP

GLU

4

VAL

ARG

ASP

ILE

THR

LEU

PRO

GLU

GLY

SER

5

ASP

VAL

TRP

VAL

CYS

LEU

PRO

ARG

ASP

6

SER

LEU

THR

LEU

SER

ALA

ASN

SER

GLU

7

ASP

GLU

GLY

GLN

ILE

ARG

TYR

PHE

LEU

PRO

8

ASP

ARG

ASP

GLU

GLY

MET

GLU

GLY

9

LYS

LEU

ASP

ALA

SER

CYS

ALA

VAL

ALA

ILE

10

GLU

ALA

ILE

GLN

LEU

TYR

GLU

GLN

11

LEU

LYS

ALA

GLN

ALA

GLY

THR

ASN

GLU

12

LEU

GLU

HIS

Samples:

sample_1: PWWP_domain, [U-99% 13C; U-99% 15N], 0.6 mM; sodium phosphate 25 mM; sodium chloride 100 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 125 mM; pH: 6.8; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker DMX 600 MHz

EMBL	CBH09455
GB	AAQ15805 AAX79611
REF	XP_011771760 XP_951596