BMRB Entry 7381

Name: Calcium binding protein in the free form
Published: 2015-10-27

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PDB ID: 2p0p
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR7381
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:

Calcium binding protein in the free form

Deposition date:

2007-03-21

Original release date:

2015-10-27

Authors:

Zhang, X.; Hu, Y.; Jin, C.

Citation:

Citation: Zhang, X.; Hu, Y.; Xia, B.; Jin, C.. "Solution Structures of Ccbp from Anabaena Reveals a New Fold and Novel Calcium Binding Sites" To be Published ., .-..

Assembly members:

Assembly members:
Alr1010_protein, polymer, 126 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Anabaena sp. Taxonomy ID: 1167 Superkingdom: Bacteria Kingdom: not available Genus/species: Anabaena sp.

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Alr1010_protein: MASVERDETREHRIETEIIV DAEDKEERAMGWYYYLDDTL EFPFMGKWKKKSRKTSTIEE KTVEVLGMAPDDECLKDMYV EVADIGGKDDDVYTAKLSDI EAIDVDDDTQEAIADWLYWL ARGYKF

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	532
15N chemical shifts	127
1H chemical shifts	805

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Alr1010_protein	1

Entities:

Entity 1, Alr1010_protein 126 residues - Formula weight is not available

1

MET

ALA

SER

VAL

GLU

ARG

ASP

GLU

THR

ARG

2

GLU

HIS

ARG

ILE

GLU

THR

GLU

ILE

VAL

3

ASP

ALA

GLU

ASP

LYS

GLU

ARG

ALA

MET

4

GLY

TRP

TYR

LEU

ASP

THR

LEU

5

GLU

PHE

PRO

PHE

MET

GLY

LYS

TRP

LYS

6

LYS

SER

ARG

LYS

THR

SER

THR

ILE

GLU

7

LYS

THR

VAL

GLU

VAL

LEU

GLY

MET

ALA

PRO

8

ASP

GLU

CYS

LEU

LYS

ASP

MET

TYR

VAL

9

GLU

VAL

ALA

ASP

ILE

GLY

LYS

ASP

10

ASP

VAL

TYR

THR

ALA

LYS

LEU

SER

ASP

ILE

11

GLU

ALA

ILE

ASP

VAL

ASP

THR

GLN

12

GLU

ALA

ILE

ALA

ASP

TRP

LEU

TYR

TRP

LEU

13

ALA

ARG

GLY

TYR

LYS

PHE

Samples:

sample: Alr1010_protein, [U-13C; U-15N], 1 mM; Tris 20 mM; NaCl 220 mM; CaCl2 40 mM; DTT 10 mM; D2O 10%; H2O 90%

sample_conditions_1: pH: 7.5; pressure: 1 .; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D_13C-separated_NOESY	sample	isotropic	sample_conditions_1
3D_15N-separated_NOESY	sample	isotropic	sample_conditions_1
HNCACB,CBCA(CO)NH	sample	isotropic	sample_conditions_1
HNCO,HN(CA)CO	sample	isotropic	sample_conditions_1
HC(C)H-COSY	sample	isotropic	sample_conditions_1
HC(C)H-TOCSY	sample	isotropic	sample_conditions_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v2.1, F.Delaglio, S.Grzesiek, G.W.Vuister, G.Zhu, J.Pfeifer, A.Bax - processing

NMRView v5, B.A.Johnson, R.A.Blevins - data analysis

DYANA vcyana2.0, P.Guntert, C.Mumenthaler, W thrich, K.W.Thrich - structure solution

AMBER v7.0, D.A.Case - refinement

NMR spectrometers:

Bruker AVANCE 800 MHz
Bruker AVANCE 500 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks