BMRB Entry 15952

Name: S100A13-C2A
Published: 2009-03-17

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15952

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:

S100A13-C2A

Deposition date:

2008-09-15

Original release date:

2009-03-17

Authors:

Mohan, Sepuru; Rani, Sandhya; Kumar, Sriramoju; Yu, Chin

Citation:

Citation: Mohan, Sepuru; Rani, Sandhya; Kumar, Sriramoju; Yu, Chin. "S100A13-C2A binary complex structure-a key component in the acidic fibroblast growth factor for the non-classical pathway" Biochem. Biophys. Res. Commun. 380, 514-519 (2009).
PubMed: 19284995

Assembly members:

Assembly members:
C2A domain, polymer, 128 residues, 14784.028 Da.
S100A13, polymer, 98 residues, 11490.304 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
C2A domain: EKLGKLQYSLDYDFQNNQLL VGIIQAAELPALDMGGTSDP YVKVFLLPDKKKKFETKVHR KTLNPVFNEQFTFKVPYSEL GGKTLVMAVYDFDRFSKHDI IGEFKVPMNTVDFGHVTEEW RDLQSAEK
S100A13: MAAEPLTELEESIETVVTTF FTFARQEGRKDSLSVNEFKE LVTQQLPHLLKDVGSLDEKM KSLDVNQDSELKFNEYWRLI GELAKEIRKKKDLKIRKK

Data sets:

assigned_chemical_shifts
- chemical_shift_set

Data type	Count
13C chemical shifts	529
15N chemical shifts	134
1H chemical shifts	869

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_2_1	2
3	entity_2_2	2
4	entity_1_2	1

Entities:

Entity 1, entity_1_1 128 residues - 14784.028 Da.

1

GLU

LYS

LEU

GLY

LYS

LEU

GLN

TYR

SER

LEU

2

ASP

TYR

ASP

PHE

GLN

ASN

GLN

LEU

3

VAL

GLY

ILE

GLN

ALA

GLU

LEU

PRO

4

ALA

LEU

ASP

MET

GLY

THR

SER

ASP

PRO

5

TYR

VAL

LYS

VAL

PHE

LEU

PRO

ASP

LYS

6

LYS

PHE

GLU

THR

LYS

VAL

HIS

ARG

7

LYS

THR

LEU

ASN

PRO

VAL

PHE

ASN

GLU

GLN

8

PHE

THR

PHE

LYS

VAL

PRO

TYR

SER

GLU

LEU

9

GLY

LYS

THR

LEU

VAL

MET

ALA

VAL

TYR

10

ASP

PHE

ASP

ARG

PHE

SER

LYS

HIS

ASP

ILE

11

ILE

GLY

GLU

PHE

LYS

VAL

PRO

MET

ASN

THR

12

VAL

ASP

PHE

GLY

HIS

VAL

THR

GLU

TRP

13

ARG

ASP

LEU

GLN

SER

ALA

GLU

LYS

Entity 2, entity_2_1 98 residues - 11490.304 Da.

1

MET

ALA

GLU

PRO

LEU

THR

GLU

LEU

GLU

2

GLU

SER

ILE

GLU

THR

VAL

THR

PHE

3

PHE

THR

PHE

ALA

ARG

GLN

GLU

GLY

ARG

LYS

4

ASP

SER

LEU

SER

VAL

ASN

GLU

PHE

LYS

GLU

5

LEU

VAL

THR

GLN

LEU

PRO

HIS

LEU

6

LYS

ASP

VAL

GLY

SER

LEU

ASP

GLU

LYS

MET

7

LYS

SER

LEU

ASP

VAL

ASN

GLN

ASP

SER

GLU

8

LEU

LYS

PHE

ASN

GLU

TYR

TRP

ARG

LEU

ILE

9

GLY

GLU

LEU

ALA

LYS

GLU

ILE

ARG

LYS

10

LYS

ASP

LEU

LYS

ILE

ARG

LYS

Samples:

sample_1: entity_1_1, [U-13C; U-15N], 1.4 mM; entity_2_1, [U-13C; U-15N], 1.4 mM; sodium phosphate 25 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 5.7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 13C-filterNOESY	sample_1	isotropic	sample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

ARIA v1.2 &2.2, Linge, O'Donoghue and Nilges - structure solution

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 600 MHz

BMRB	15785 17102 4039 4041 4166 4167 6531 6532
PDB	1BYN 1RSY 2K45 2K4A 2K8M 2KI6 3F00 3F01 3F04 3F05 1YUR 1YUS 1YUT 1YUU 2EGD 2H2K 2K8M 2KI4 2KI6 2KOT 2L5X 2LE9
GB	AAK15077 ELW70522 EPY85163 KFO26677 KFP32561 AAH00632 AAH68064 AAH70291 AAP35370 AAP36320
REF	XP_005976391 XP_010164835 XP_010202276 XP_010211789 NP_001019381 NP_001019382 NP_001019383 NP_001019384 NP_005970
DBJ	BAG74209
EMBL	CAA68188 CAG46946
SP	Q99584
AlphaFold	Q99584