BMRB Entry 11330

Name: Solution structure of the plus-3 domain of human KIAA0252 protein
Published: 2011-08-19

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PDB ID: 2db9
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11330
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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:

Solution structure of the plus-3 domain of human KIAA0252 protein

Deposition date:

2010-08-10

Original release date:

2011-08-19

Authors:

Yoneyama, M.; Kigawa, T.; Tochio, N.; Nameki, N.; Koshiba, S.; Inoue, M.; Yokoyama, S.

Citation:

Citation: Yoneyama, M.; Kigawa, T.; Tochio, N.; Nameki, N.; Koshiba, S.; Inoue, M.; Yokoyama, S.. "Solution structure of the plus-3 domain of human KIAA0252 protein" .

Assembly members:

Assembly members:
Plus-3 domain, Residues 8-143, polymer, 149 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: P050302-16

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Plus-3 domain, Residues 8-143: GSSGSSGPPKSQPVSLPEEL NRVRLSRHKLERWCHMPFFA KTVTGCFVRIGIGNHNSKPV YRVAEITGVVETAKVYQLGG TRTNKGLQLRHGNDQRVFRL EFVSNQEFTESEFMKWKEAM FSAGMQLPTLDEINKKELSI KEASGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	631
15N chemical shifts	145
1H chemical shifts	1006

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Plus-3 domain, Residues 8-143	1

Entities:

Entity 1, Plus-3 domain, Residues 8-143 149 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

PRO

LYS

2

SER

GLN

PRO

VAL

SER

LEU

PRO

GLU

LEU

3

ASN

ARG

VAL

ARG

LEU

SER

ARG

HIS

LYS

LEU

4

GLU

ARG

TRP

CYS

HIS

MET

PRO

PHE

ALA

5

LYS

THR

VAL

THR

GLY

CYS

PHE

VAL

ARG

ILE

6

GLY

ILE

GLY

ASN

HIS

ASN

SER

LYS

PRO

VAL

7

TYR

ARG

VAL

ALA

GLU

ILE

THR

GLY

VAL

8

GLU

THR

ALA

LYS

VAL

TYR

GLN

LEU

GLY

9

THR

ARG

THR

ASN

LYS

GLY

LEU

GLN

LEU

ARG

10

HIS

GLY

ASN

ASP

GLN

ARG

VAL

PHE

ARG

LEU

11

GLU

PHE

VAL

SER

ASN

GLN

GLU

PHE

THR

GLU

12

SER

GLU

PHE

MET

LYS

TRP

LYS

GLU

ALA

MET

13

PHE

SER

ALA

GLY

MET

GLN

LEU

PRO

THR

LEU

14

ASP

GLU

ILE

ASN

LYS

GLU

LEU

SER

ILE

15

LYS

GLU

ALA

SER

GLY

PRO

SER

GLY

Samples:

sample_1: plus-3 domain, [U-13C; U-15N], 0.73 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 v2.6, Bruker - collection

NMRPipe v20030801, Delaglio, F. - processing

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

Kujira v0.9318, Kobayashi, N. - data analysis

CYANA v1.0.8, Guntert, P. - refinement, structure solution

NMR spectrometers:

Bruker AVANCE 800 MHz

PDB	2BZE 2DB9 3U1U 4L1P 4L1U
DBJ	BAA13382 BAE22595 BAF84991 BAG09677
EMBL	CAG31800 CAH91275
GB	AAH15052 AAH76973 AAI17849 AAI17850 EAW92490
REF	NP_001005068 NP_001102428 NP_001179414 NP_055953 NP_084388
SP	A2AQ19 Q5RAD5 Q92541
TPG	DAA25394
AlphaFold	A2AQ19 Q5RAD5 Q92541