BMRB Entry 16050

Name: Ca-S100A1 interacting with TRTK12
Published: 2009-04-04

Click here to enlarge.

PDB ID: 2kbm
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16050
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Ca-S100A1 interacting with TRTK12

Deposition date:

2008-12-02

Original release date:

2009-04-04

Authors:

Wright, Nathan; Varney, Kristen; Cannon, Brian; Morgan, Michael; Weber, David

Citation:

Citation: Wright, Nathan; Cannon, Brian; Wilder, P.; Morgan, Michael; Varney, Kristen; Zimmer, D.; Weber, David. "Solution structure of S100A1 bound to the CapZ peptide (TRTK12)" J. Mol. Biol. 386, 1265-1277 (2009).
PubMed: 19452629

Assembly members:

Assembly members:
S100A1, polymer, 93 residues, 10439.711 Da.
TRTK12, polymer, 12 residues, 1477.742 Da.
CA, non-polymer, 40.078 Da.

Natural source:

Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
S100A1: GSELETAMETLINVFHAHSG KEGDKYKLSKKELKDLLQTE LSSFLDVQKDADAVDKIMKE LDENGDGEVDFQEFVVLVAA LTVACNNFFWENS
TRTK12: TRTKIDWNKILS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	369
15N chemical shifts	93
1H chemical shifts	668

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1_1	1
2	entity_1_2	1
3	entity_2_1	2
4	entity_2_2	2
5	CALCIUM ION_1	3
6	CALCIUM ION_2	3
7	CALCIUM ION_3	3

Entities:

Entity 1, entity_1_1 93 residues - 10439.711 Da.

1

GLY

SER

GLU

LEU

GLU

THR

ALA

MET

GLU

THR

2

LEU

ILE

ASN

VAL

PHE

HIS

ALA

HIS

SER

GLY

3

LYS

GLU

GLY

ASP

LYS

TYR

LYS

LEU

SER

LYS

4

LYS

GLU

LEU

LYS

ASP

LEU

GLN

THR

GLU

5

LEU

SER

PHE

LEU

ASP

VAL

GLN

LYS

ASP

6

ALA

ASP

ALA

VAL

ASP

LYS

ILE

MET

LYS

GLU

7

LEU

ASP

GLU

ASN

GLY

ASP

GLY

GLU

VAL

ASP

8

PHE

GLN

GLU

PHE

VAL

LEU

VAL

ALA

9

LEU

THR

VAL

ALA

CYS

ASN

PHE

TRP

10

GLU

ASN

SER

Entity 2, entity_2_1 12 residues - 1477.742 Da.

1

THR

ARG

THR

LYS

ILE

ASP

TRP

ASN

LYS

ILE

2

LEU

SER

Entity 3, CALCIUM ION_1 - Ca - 40.078 Da.

1

CA

Samples:

sample_1: D2O 10%; H2O 90%; CALCIUM ION 10 mM; DTT 10 mM; TRIS 10 mM; sodium chloride 25 mM; entity_1, [U-100% 13C; U-100% 15N], 500 uM; entity_2 1500 uM

sample_conditions_1: ionic strength: 0.05 M; pH: 7.2; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	anisotropic	sample_conditions_1
IPAP-HSQC	sample_1	anisotropic	sample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 600 MHz

BMRB	15296 4285
PDB	1K2H 1ZFS 2K2F 2KBM
GB	AAB20539 AAB53657 EDM00555
REF	NP_001007637 XP_006232665
SP	P35467
AlphaFold	P35467 Q3T1K5