BMRB Entry 11203

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PDB ID: 1x5m
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11203
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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 core domain of calcyclin binding protein; siah-interacting protein (SIP)

Deposition date:

2010-07-22

Original release date:

2011-07-21

Authors:

Qin, X.; Nagashima, T.; Hayashi, F.; Yokoyama, S.

Citation:

Citation: Qin, X.; Nagashima, T.; Hayashi, F.; Yokoyama, S.. "Solution structure of the core domain of calcyclin binding protein; siah-interacting protein (SIP)" .

Assembly members:

Assembly members:
CS domain, polymer, 127 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: p040329-62

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CS domain: GSSGSSGVVAPITTGYTVKI SNYGWDQSDKFVKIYITLTG VHQVPTENVQVHFTERSFDL LVKNLNGKSYSMIVNNLLKP ISVEGSSKKVKTDTVLILCR KKVENTRWDYLTQVEKECKE KSGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	565
15N chemical shifts	126
1H chemical shifts	890

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CS domain	1

Entities:

Entity 1, CS domain 127 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

VAL

ALA

2

PRO

ILE

THR

GLY

TYR

THR

VAL

LYS

ILE

3

SER

ASN

TYR

GLY

TRP

ASP

GLN

SER

ASP

LYS

4

PHE

VAL

LYS

ILE

TYR

ILE

THR

LEU

THR

GLY

5

VAL

HIS

GLN

VAL

PRO

THR

GLU

ASN

VAL

GLN

6

VAL

HIS

PHE

THR

GLU

ARG

SER

PHE

ASP

LEU

7

LEU

VAL

LYS

ASN

LEU

ASN

GLY

LYS

SER

TYR

8

SER

MET

ILE

VAL

ASN

LEU

LYS

PRO

9

ILE

SER

VAL

GLU

GLY

SER

LYS

VAL

10

LYS

THR

ASP

THR

VAL

LEU

ILE

LEU

CYS

ARG

11

LYS

VAL

GLU

ASN

THR

ARG

TRP

ASP

TYR

12

LEU

THR

GLN

VAL

GLU

LYS

GLU

CYS

LYS

GLU

13

LYS

SER

GLY

PRO

SER

GLY

Samples:

sample_1: CS domain, [U-13C; U-15N], 0.98 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: 298 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:

VNMR v6.1C, Varian - collection

NMRPipe v20031121, Delaglio, F. - processing

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

Kujira v0.9296, Kobayashi, N. - data analysis

CYANA v1.0.7, Guntert, P. - refinement, structure solution

NMR spectrometers:

Varian INOVA 800 MHz