BMRB Entry 11090

Click here to enlarge.

PDB ID: 2ys4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11090
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 N-terminal PapD-like domain of HYDIN protein from human

Deposition date:

2010-01-18

Original release date:

2011-01-19

Authors:

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

Citation:

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

Assembly members:

Assembly members:
PapD-like, UNP residues 182-296, polymer, 122 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: P060327-16

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PapD-like, UNP residues 182-296: GSSGSSGTEREKFIVPIKAR GARAILDFPDKLNFSTCPVK YSTQKILLVRNIGNKNAVFH IKTCRPFSIEPAIGTLNVGE SMQLEVEFEPQSVGDHSGRL IVCYDTGEKVFVSLYGAAID MN

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	521
15N chemical shifts	119
1H chemical shifts	842

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PapD-like, UNP residues 182-296	1

Entities:

Entity 1, PapD-like, UNP residues 182-296 122 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

THR

GLU

ARG

2

GLU

LYS

PHE

ILE

VAL

PRO

ILE

LYS

ALA

ARG

3

GLY

ALA

ARG

ALA

ILE

LEU

ASP

PHE

PRO

ASP

4

LYS

LEU

ASN

PHE

SER

THR

CYS

PRO

VAL

LYS

5

TYR

SER

THR

GLN

LYS

ILE

LEU

VAL

ARG

6

ASN

ILE

GLY

ASN

LYS

ASN

ALA

VAL

PHE

HIS

7

ILE

LYS

THR

CYS

ARG

PRO

PHE

SER

ILE

GLU

8

PRO

ALA

ILE

GLY

THR

LEU

ASN

VAL

GLY

GLU

9

SER

MET

GLN

LEU

GLU

VAL

GLU

PHE

GLU

PRO

10

GLN

SER

VAL

GLY

ASP

HIS

SER

GLY

ARG

LEU

11

ILE

VAL

CYS

TYR

ASP

THR

GLY

GLU

LYS

VAL

12

PHE

VAL

SER

LEU

TYR

GLY

ALA

ILE

ASP

13

MET

ASN

Samples:

sample_1: PapD-like, UNP residues 182-296, [U-13C; U-15N], 1.19 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 v20031121, Delaglio, F. - processing

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

Kujira v0.9820, Kobayashi, N. - data analysis

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

NMR spectrometers:

Bruker AVANCE 900 MHz

PDB	2YS4
DBJ	BAB14314 BAG61096 BAG61346
EMBL	CAD38687
GB	AAH28351 AIC60203
REF	NP_001185471 NP_001185472 NP_001257903 NP_060028 XP_004057985
SP	Q4G0P3
AlphaFold	Q4G0P3