BMRB Entry 11303

Name: An extended conformation of the RWD domain of human Ring finger protein 25
Published: 2011-08-19

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PDB ID: 2dmf
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11303
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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:

An extended conformation of the RWD domain of human Ring finger protein 25

Deposition date:

2010-08-09

Original release date:

2011-08-19

Authors:

Yoneyama, M.; Tochio, N.; Koshiba, S.; Watabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.

Citation:

Citation: Yoneyama, M.; Tochio, N.; Koshiba, S.; Watabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.. "An extended conformation of the RWD domain of human Ring finger protein 25" .

Assembly members:

Assembly members:
RWD domain, polymer, 137 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: P051212-01

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RWD domain: GSSGSSGEEDWVLPSEVEVL ESIYLDELQVIKGNGRTSPW EIYITLHPATAEDQDSQYVC FTLVLQVPAEYPHEVPQISI RNPRGLSDEQIHTILQVLGH VAKAGLGTAMLYELIEKGKE ILTDNNIPHGQSGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	567
15N chemical shifts	129
1H chemical shifts	911

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RWD domain	1

Entities:

Entity 1, RWD domain 137 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

GLU

ASP

2

TRP

VAL

LEU

PRO

SER

GLU

VAL

GLU

VAL

LEU

3

GLU

SER

ILE

TYR

LEU

ASP

GLU

LEU

GLN

VAL

4

ILE

LYS

GLY

ASN

GLY

ARG

THR

SER

PRO

TRP

5

GLU

ILE

TYR

ILE

THR

LEU

HIS

PRO

ALA

THR

6

ALA

GLU

ASP

GLN

ASP

SER

GLN

TYR

VAL

CYS

7

PHE

THR

LEU

VAL

LEU

GLN

VAL

PRO

ALA

GLU

8

TYR

PRO

HIS

GLU

VAL

PRO

GLN

ILE

SER

ILE

9

ARG

ASN

PRO

ARG

GLY

LEU

SER

ASP

GLU

GLN

10

ILE

HIS

THR

ILE

LEU

GLN

VAL

LEU

GLY

HIS

11

VAL

ALA

LYS

ALA

GLY

LEU

GLY

THR

ALA

MET

12

LEU

TYR

GLU

LEU

ILE

GLU

LYS

GLY

LYS

GLU

13

ILE

LEU

THR

ASP

ASN

ILE

PRO

HIS

GLY

14

GLN

SER

GLY

PRO

SER

GLY

Samples:

sample_1: RWD domain, [U-13C; U-15N], 0.94 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 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 v0.9736, Kobayashi, N. - data analysis

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

NMR spectrometers:

Bruker AVANCE 800 MHz

PDB	2DMF
DBJ	BAD96245 BAF82190 BAI45678
GB	AAH15612 ADZ15417 AIC52126 EAW70645 EHH21677
REF	NP_071898 XP_002749840 XP_003818674 XP_003908009 XP_003925575
SP	Q96BH1
AlphaFold	Q96BH1