BMRB Entry 10164

Name: Solution structure of the A1pp domain from human protein C6orf130
Published: 2009-02-23

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PDB ID: 2eee
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR10164
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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 A1pp domain from human protein C6orf130

Deposition date:

2007-12-28

Original release date:

2009-02-23

Authors:

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

Citation:

Citation: Tomizawa, T.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.. "Solution structure of the A1pp domain from human protein C6orf130" .

Assembly members:

Assembly members:
A1pp domain, 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 Vector: P060821-05

Entity Sequences (FASTA):

Entity Sequences (FASTA):
A1pp domain: GSSGSSGGSRITYVKGDLFA CPKTDSLAHCISEDCRMGAG IAVLFKKKFGGVQELLNQQK KSGEVAVLKRDGRYIYYLIT KKRASHKPTYENLQKSLEAM KSHCLKNGVTDLSMPRIGCG LDRLQWENVSAMIEEVFEAT DIKITVYTL

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	646
15N chemical shifts	146
1H chemical shifts	1029

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Uncharacterized protein C6orf130	1

Entities:

Entity 1, Uncharacterized protein C6orf130 149 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

SER

ARG

2

ILE

THR

TYR

VAL

LYS

GLY

ASP

LEU

PHE

ALA

3

CYS

PRO

LYS

THR

ASP

SER

LEU

ALA

HIS

CYS

4

ILE

SER

GLU

ASP

CYS

ARG

MET

GLY

ALA

GLY

5

ILE

ALA

VAL

LEU

PHE

LYS

PHE

GLY

6

GLY

VAL

GLN

GLU

LEU

ASN

GLN

LYS

7

LYS

SER

GLY

GLU

VAL

ALA

VAL

LEU

LYS

ARG

8

ASP

GLY

ARG

TYR

ILE

TYR

LEU

ILE

THR

9

LYS

ARG

ALA

SER

HIS

LYS

PRO

THR

TYR

10

GLU

ASN

LEU

GLN

LYS

SER

LEU

GLU

ALA

MET

11

LYS

SER

HIS

CYS

LEU

LYS

ASN

GLY

VAL

THR

12

ASP

LEU

SER

MET

PRO

ARG

ILE

GLY

CYS

GLY

13

LEU

ASP

ARG

LEU

GLN

TRP

GLU

ASN

VAL

SER

14

ALA

MET

ILE

GLU

VAL

PHE

GLU

ALA

THR

15

ASP

ILE

LYS

ILE

THR

VAL

TYR

THR

LEU

Samples:

sample_1: A1pp domain, [U-13C; U-15N], 1.22 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 13C-separated NOESY	sample_1	not available	condition_1
3D 15N-separated NOESY	sample_1	not available	condition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20060524, Delaglio, F - processing

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

Kujira v0.9823, Kobayashi, N. - data analysis

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

NMR spectrometers:

Bruker AVANCE 800 MHz

BMRB	15593 17421
PDB	2EEE 2L8R 2LGR 4J5Q 4J5R 4J5S
DBJ	BAF83628 BAG36161
GB	AAH11709 AIC53444 AIC58012 EAX04011 EAX04012
REF	NP_001181654 NP_659500 XP_001117219 XP_001117235 XP_001174030
SP	Q9Y530
AlphaFold	Q9Y530