BMRB Entry 26994

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for HSP27
Published: 2017-05-09

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26994

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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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for HSP27

Deposition date:

2017-01-12

Original release date:

2017-05-09

Authors:

Alderson, Thomas; Benesch, Justin; Baldwin, Andrew

Citation:

Citation: Alderson, T Reid; Benesch, Justin; Baldwin, Andrew. "Proline isomerization in the C-terminal region of HSP27" Cell Stress Chaperones 22, 639-651 (2017).
PubMed: 28547731

Assembly members:

Assembly members:
HSP27, polymer, 205 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HSP27: MTERRVPFSLLRGPSWDPFR DWYPHSRLFDQAFGLPRLPE EWSQWLGGSSWPGYVRPLPP AAIESPAVAAPAYSRALSRQ LSSGVSEIRHTADRWRVSLD VNHFAPDELTVKTKDGVVEI TGKHEERQDEHGYISRCFTR KYTLPPGVDPTQVSSSLSPE GTLTVEAPMPKLATQSNEIT IPVTFESRAQLGGPEAAKSD ETAAK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	102
15N chemical shifts	31
1H chemical shifts	31

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HSP27 trans, chain 1	1
2	HSP27 trans, chain 2	1
3	HSP27 cis, chain 1	1
4	HSP27 cis, chain 2	1

Entities:

Entity 1, HSP27 trans, chain 1 205 residues - Formula weight is not available

1

MET

THR

GLU

ARG

VAL

PRO

PHE

SER

LEU

2

LEU

ARG

GLY

PRO

SER

TRP

ASP

PRO

PHE

ARG

3

ASP

TRP

TYR

PRO

HIS

SER

ARG

LEU

PHE

ASP

4

GLN

ALA

PHE

GLY

LEU

PRO

ARG

LEU

PRO

GLU

5

GLU

TRP

SER

GLN

TRP

LEU

GLY

SER

6

TRP

PRO

GLY

TYR

VAL

ARG

PRO

LEU

PRO

7

ALA

ILE

GLU

SER

PRO

ALA

VAL

ALA

8

PRO

ALA

TYR

SER

ARG

ALA

LEU

SER

ARG

GLN

9

LEU

SER

GLY

VAL

SER

GLU

ILE

ARG

HIS

10

THR

ALA

ASP

ARG

TRP

ARG

VAL

SER

LEU

ASP

11

VAL

ASN

HIS

PHE

ALA

PRO

ASP

GLU

LEU

THR

12

VAL

LYS

THR

LYS

ASP

GLY

VAL

GLU

ILE

13

THR

GLY

LYS

HIS

GLU

ARG

GLN

ASP

GLU

14

HIS

GLY

TYR

ILE

SER

ARG

CYS

PHE

THR

ARG

15

LYS

TYR

THR

LEU

PRO

GLY

VAL

ASP

PRO

16

THR

GLN

VAL

SER

LEU

SER

PRO

GLU

17

GLY

THR

LEU

THR

VAL

GLU

ALA

PRO

MET

PRO

18

LYS

LEU

ALA

THR

GLN

SER

ASN

GLU

ILE

THR

19

ILE

PRO

VAL

THR

PHE

GLU

SER

ARG

ALA

GLN

20

LEU

GLY

PRO

GLU

ALA

LYS

SER

ASP

21

GLU

THR

ALA

LYS

Samples:

sample_1: HSP27, [U-13C; U-15N], 2 mM; NaH2PO4 30 mM; EDTA 2 mM; NaCl 100 mM; NaN3 2 mM

sample_conditions_1: ionic strength: 130 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Goddard - chemical shift assignment, processing

NMR spectrometers:

Varian INOVA 600 MHz

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