BMRB Entry 11280

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PDB ID: 2dzj
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11280
MolProbity Validation Chart

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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:

2DZJ/Solution Structure of the N-terminal Ubiquitin-like Domain in Human Synaptic Glycoprotein SC2

Deposition date:

2010-08-09

Original release date:

2011-08-18

Authors:

Zhao, C.; Yoneyama, M.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.

Citation:

Citation: Zhao, C.; Yoneyama, M.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.. "2DZJ/Solution Structure of the N-terminal Ubiquitin-like Domain in Human Synaptic Glycoprotein SC2" .

Assembly members:

Assembly members:
ubiquitin-like domain, polymer, 88 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: P060522-14

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ubiquitin-like domain: GSSGSSGMKHYEVEILDAKT REKLCFLDKVEPHATIAEIK NLFTKTHPQWYPARQSLRLD PKGKSLKDEDVLQKLPVGTT ATLYFRDL

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	393
15N chemical shifts	82
1H chemical shifts	602

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ubiquitin-like domain	1

Entities:

Entity 1, ubiquitin-like domain 88 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

MET

LYS

HIS

2

TYR

GLU

VAL

GLU

ILE

LEU

ASP

ALA

LYS

THR

3

ARG

GLU

LYS

LEU

CYS

PHE

LEU

ASP

LYS

VAL

4

GLU

PRO

HIS

ALA

THR

ILE

ALA

GLU

ILE

LYS

5

ASN

LEU

PHE

THR

LYS

THR

HIS

PRO

GLN

TRP

6

TYR

PRO

ALA

ARG

GLN

SER

LEU

ARG

LEU

ASP

7

PRO

LYS

GLY

LYS

SER

LEU

LYS

ASP

GLU

ASP

8

VAL

LEU

GLN

LYS

LEU

PRO

VAL

GLY

THR

9

ALA

THR

LEU

TYR

PHE

ARG

ASP

LEU

Samples:

sample_1: ubiquitin-like domain, [U-13C; U-15N], 1.10 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: 296.0 K

Experiments:

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

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

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

Kujira v0.9748, Kobayashi, N. - data analysis

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

NMR spectrometers:

Bruker AVANCE 800 MHz

PDB	2DZJ
DBJ	BAE88553 BAE90144 BAG37802 BAG50909 BAI47191
EMBL	CAG33173
GB	AAF32373 AAH00174 AAH02425 AAH05952 AAH07801
REF	NP_001029920 NP_001231519 NP_001270331 NP_612510 XP_001498421
SP	Q3ZCD7 Q9NZ01
TPG	DAA28092
AlphaFold	Q3ZCD7 Q9NZ01