BMRB Entry 11091

Name: Solution structure of the C-terminal PapD-like domain from human HYDIN protein
Published: 2011-01-19

Click here to enlarge.

PDB ID: 2e6j
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11091
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:

Solution structure of the C-terminal PapD-like domain from human HYDIN protein

Deposition date:

2010-01-18

Original release date:

2011-01-19

Authors:

Li, H.; Sato, M.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.

Citation:

Citation: Li, H.; Sato, M.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.. "Solution structure of the C-terminal PapD-like domain from human HYDIN protein" .

Assembly members:

Assembly members:
PapD domain, polymer, 112 residues, Formula weight is not available

Natural source:

Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: Cell free synthesis Host organism: E. coli - cell free Vector: P060327-17

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PapD domain: GSSGSSGPKIHFNFELLDIG KVFTGSAHCYEAILYNKGSI DALFNMTPPTSALGACFVFS PKEGIIEPSGVQAIQISFSS IILGNFEEEFLVNVNGSPEP VKLTIRGCVIGP

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	484
15N chemical shifts	107
1H chemical shifts	756

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PapD domain	1

Entities:

Entity 1, PapD domain 112 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

PRO

LYS

ILE

2

HIS

PHE

ASN

PHE

GLU

LEU

ASP

ILE

GLY

3

LYS

VAL

PHE

THR

GLY

SER

ALA

HIS

CYS

TYR

4

GLU

ALA

ILE

LEU

TYR

ASN

LYS

GLY

SER

ILE

5

ASP

ALA

LEU

PHE

ASN

MET

THR

PRO

THR

6

SER

ALA

LEU

GLY

ALA

CYS

PHE

VAL

PHE

SER

7

PRO

LYS

GLU

GLY

ILE

GLU

PRO

SER

GLY

8

VAL

GLN

ALA

ILE

GLN

ILE

SER

PHE

SER

9

ILE

LEU

GLY

ASN

PHE

GLU

PHE

10

LEU

VAL

ASN

VAL

ASN

GLY

SER

PRO

GLU

PRO

11

VAL

LYS

LEU

THR

ILE

ARG

GLY

CYS

VAL

ILE

12

GLY

PRO

Samples:

sample_1: PapD domain, [U-13C; U-15N], 1.13 mM; TRIS, [U-2H], 20 mM; sodium chloride 100 mM; DTT, [U-2H], 1 mM; sodium azide 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 15N-separated NOESY	sample_1	isotropic	condition_1
3D 13C-separated NOESY	sample_1	isotropic	condition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20030801, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.932, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - structure solution

NMR spectrometers:

Bruker AVANCE 800 MHz

PDB	2E6J
DBJ	BAB14314 BAG61096 BAG61346
EMBL	CAD38687 CAD39007
GB	AAH28351 AIC60203 EAW68881
REF	NP_001185471 NP_001185472 NP_001257903 NP_060028 XP_004057985
SP	Q4G0P3
AlphaFold	Q4G0P3