BMRB Entry 18545

Name: Calcium saturated form of human C85M S100A1 mutant
Published: 2013-06-24

Click here to enlarge.

PDB ID: 2lux
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18545
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:

Calcium saturated form of human C85M S100A1 mutant

Deposition date:

2012-06-25

Original release date:

2013-06-24

Authors:

Ruszczynska-Bartnik, Katarzyna; Budzinska, Monika; Zdanowski, Konrad; Ejchart, Andrzej

Citation:

Citation: Ruszczynska-Bartnik, Katarzyna; Ejchart, Andrzej; Budzinska, Monika; Zdanowski, Konrad. "Solution structure of human holo-S100A1 C85M mutant" .

Assembly members:

Assembly members:
S100A1C85M, polymer, 93 residues, 10453.736 Da.
entity_CA, non-polymer, 40.078 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: pET30a+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
S100A1C85M: GSELETAMETLINVFHAHSG KEGDKYKLSKKELKELLQTE LSGFLDAQKDVDAVDKVMKE LDENGDGEVDFQEYVVLVAA LTVAMNNFFWENS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
heteronucl_NOEs
heteronucl_T1_relaxation
heteronucl_T2_relaxation

Data type	Count
13C chemical shifts	385
15N chemical shifts	94
1H chemical shifts	628
heteronuclear NOE values	209
T1 relaxation values	218
T2 relaxation values	216

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	C85M_S100A1, 1	1
2	C85M_S100A1, 2	1
3	CALCIUM ION_1	2
4	CALCIUM ION_2	2
5	CALCIUM ION_3	2
6	CALCIUM ION_4	2

Entities:

Entity 1, C85M_S100A1, 1 93 residues - 10453.736 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

GLU

LEU

GLN

THR

GLU

5

LEU

SER

GLY

PHE

LEU

ASP

ALA

GLN

LYS

ASP

6

VAL

ASP

ALA

VAL

ASP

LYS

VAL

MET

LYS

GLU

7

LEU

ASP

GLU

ASN

GLY

ASP

GLY

GLU

VAL

ASP

8

PHE

GLN

GLU

TYR

VAL

LEU

VAL

ALA

9

LEU

THR

VAL

ALA

MET

ASN

PHE

TRP

10

GLU

ASN

SER

Entity 2, CALCIUM ION_1 - Ca - 40.078 Da.

1

CA

Samples:

sample_1: S100A1C85M, [U-98% 13C; U-98% 15N], 1 mM; TRIS, [U-99% 2H], 50 mM; sodium chloride 50 mM; CALCIUM ION 10 mM; D2O, [U-99% 2H], 10%; H2O 90%

sample_2: S100A1C85M, [U-98% 13C; U-98% 15N], 1 mM; TRIS, [U-99% 2H], 50 mM; sodium chloride 50 mM; CALCIUM ION 10 mM; D2O, [U-99% 2H], 100%

sample_3: S100A1C85M, [U-99% 15N], 1 mM; TRIS, [U-2H], 50 mM; sodium chloride 50 mM; CALCIUM ION 10 mM; D2O, [U-99% 2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 0.05 M; pH: 7.0; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
1H-15N HSQC type NOE	sample_3	isotropic	sample_conditions_1
1H-15N HSQC type R1/R2	sample_3	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - data analysis, peak picking

CARA v1.8, Keller and Wuthrich - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CYANA v3.0, Peter Guntert - chemical shift assignment, data analysis, structure solution

X-PLOR NIH v2.26, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

Varian INOVA 400 MHz
Varian UnityPlus 500 MHz
Varian Varian NMR System 700 MHz

BMRB	16360 17857 18087 18088 18089 18101 18230 18231
PDB	2L0P 2LHL 2LLS 2LLT 2LLU 2LP2 2LP3 2LUX 2M3W
DBJ	BAE90380 BAG35086 BAG70130 BAG70260
EMBL	CAA41107 CAH90674
GB	AAH14392 AAI41992 AAI48020 AAP35584 AAP36328
PRF	2003367A
REF	NP_001092512 NP_001127319 NP_001270255 NP_006262 XP_001111015
SP	P02639 P23297 Q5RC36
TPG	DAA31796
AlphaFold	P02639 P23297 Q5RC36