BMRB Entry 17866

Name: 1H,15N and 13C backbone and side chain chemical shifts of human halo S100P
Published: 2012-03-09

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17866

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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:

1H,15N and 13C backbone and side chain chemical shifts of human halo S100P

Deposition date:

2011-08-17

Original release date:

2012-03-09

Authors:

Rao, Penumutchu; Yu, Chin

Citation:

Citation: Gupta, Arun; Mohan, Sepuru; Chin, Yu. "1H, 13C and 15N backbone and side chain resonance assignments of human halo S100A1." Biomol. NMR Assignments 6, 213-215 (2012).
PubMed: 22311340

Assembly members:

Assembly members:
S100P, polymer, 95 residues, 10399.873 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9616 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET(20b)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
S100P: MTELETAMGMIIDVFSRYSG SEGSTQTLTKGELKVLMEKE LPGFLQSGKDKDAVDKLLKD LDANGDAQVDFSEFIVFVAA ITSACHKYFEKAGLK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	327
15N chemical shifts	85
1H chemical shifts	536

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	S100P	1

Entities:

Entity 1, S100P 95 residues - 10399.873 Da.

1

MET

THR

GLU

LEU

GLU

THR

ALA

MET

GLY

MET

2

ILE

ASP

VAL

PHE

SER

ARG

TYR

SER

GLY

3

SER

GLU

GLY

SER

THR

GLN

THR

LEU

THR

LYS

4

GLY

GLU

LEU

LYS

VAL

LEU

MET

GLU

LYS

GLU

5

LEU

PRO

GLY

PHE

LEU

GLN

SER

GLY

LYS

ASP

6

LYS

ASP

ALA

VAL

ASP

LYS

LEU

LYS

ASP

7

LEU

ASP

ALA

ASN

GLY

ASP

ALA

GLN

VAL

ASP

8

PHE

SER

GLU

PHE

ILE

VAL

PHE

VAL

ALA

9

ILE

THR

SER

ALA

CYS

HIS

LYS

TYR

PHE

GLU

10

LYS

ALA

GLY

LEU

LYS

Samples:

sample_1: S100P, [U-100% 13C; U-100% 15N], 1.0 mM; TRIS 20 mM; potassium chloride 100 mM; sodium azide 0.1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.8; 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 HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	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 HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

VNMR, Varian - collection, processing

SPARKY, Goddard - chemical shift assignment, data analysis, data analysis

NMR spectrometers:

Varian VNMR 700 MHz

PDB	1J55 2MJW
DBJ	BAJ20330
EMBL	CAA46566
GB	AAB21475 AAH06819 AAO41114 AAP35953 AAS00487
REF	NP_005971 XP_001091876 XP_002814597 XP_003310290 XP_003816512
SP	P25815
AlphaFold	P25815