PDB-6dv5: Oligomeric complex of a Hsp27 24-mer at 3.6 A resolution

ID or keywords:

Entry

Database: PDB / ID: 6dv5

Title

Oligomeric complex of a Hsp27 24-mer at 3.6 A resolution

Components

Heat shock protein beta-1

Heat shock response

Keywords

CHAPERONE /

Molecular Chaperone / Small Heat shock Protein / Alpha crystallin domain

Function / homology

Function and homology information

anterograde axonal protein transport / positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway / cornified envelope / positive regulation of endothelial cell chemotaxis / regulation of translational initiation / regulation of canonical NF-kappaB signal transduction /

protein kinase C inhibitor activity / response to unfolded protein / positive regulation of blood vessel endothelial cell migration / cellular response to vascular endothelial growth factor stimulus ...
Similarity search - Function

Biological species

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 3.58 Å

Authors

Aguda, A.H. / Brayer, G.D.

Funding support

Canada, 1items

Citation

Journal: To Be Published
Title: Structure-Guided Discovery of Ivermectin as an Inhibitor of Heat Shock Protein-27 Phosphorylation and Depolymerization.
Authors: Nappi, L. / Aguda, A.H. / Al Nakouzi, N. / Lelj Garolla, B. / Beraldi, E. / Lallous, N. / Thi, M. / Moore, S. / Battsogt, D. / Stoffeliene, S. / Ban, F. / Nguyen, N.T. / Saxena, N. / Dueva, ...

History

Deposition	Jun 22, 2018	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Jun 26, 2019	Provider: repository / Type: Initial release
Revision 1.1	Jan 8, 2020	Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.2	Oct 11, 2023	Group: Data collection / Database references / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	6dv5.cif.gz	798.9 KB	Display	PDBx/mmCIF format
PDB format	pdb6dv5.ent.gz	658.3 KB	Display	PDB format
PDBx/mmJSON format	6dv5.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/dv/6dv5 ftp://data.pdbj.org/pub/pdb/validation_reports/dv/6dv5	HTTPS FTP

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Related structure data

Related structure data	2ygdS S: Starting model for refinement
Similar structure data	2ygd-d 4dqw-1 10725 3681 3vcd-1 2591 Search similar-shape structures by Omokage search (details) Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#32 - Aug 2002 Chaperones similarity (1) #127 - Jul 2010 Crystallins similarity (5) #108 - Dec 2008 Hsp90 similarity (1)

Deposited unit

B: Heat shock protein beta-1

A: Heat shock protein beta-1

D: Heat shock protein beta-1

F: Heat shock protein beta-1

H: Heat shock protein beta-1

J: Heat shock protein beta-1

L: Heat shock protein beta-1

N: Heat shock protein beta-1

P: Heat shock protein beta-1

R: Heat shock protein beta-1

T: Heat shock protein beta-1

V: Heat shock protein beta-1

X: Heat shock protein beta-1

C: Heat shock protein beta-1

E: Heat shock protein beta-1

G: Heat shock protein beta-1

I: Heat shock protein beta-1

K: Heat shock protein beta-1

M: Heat shock protein beta-1

O: Heat shock protein beta-1

Q: Heat shock protein beta-1

S: Heat shock protein beta-1

U: Heat shock protein beta-1

W: Heat shock protein beta-1

547 kDa, 24 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

Idetical with deposited unit
defined by author
Evidence: gel filtration

Unit cell

Length a, b, c (Å)	324.700, 324.700, 198.761
Angle α, β, γ (deg.)	90.00, 90.00, 120.00
Int Tables number	146
Space group name H-M	H3

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Component-ID: 0 / Refine code: 0

Dom-ID	Ens-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	VAL	VAL	ALA	ALA	B	A	6 - 189	6 - 189
2	1	VAL	VAL	ALA	ALA	D	C	6 - 189	6 - 189
1	2	VAL	VAL	ALA	ALA	B	A	6 - 189	6 - 189
2	2	VAL	VAL	ALA	ALA	F	D	6 - 189	6 - 189
1	3	VAL	VAL	ALA	ALA	B	A	6 - 189	6 - 189
2	3	ARG	ARG	ALA	ALA	H	E	5 - 189	5 - 189
1	4	VAL	VAL	ALA	ALA	B	A	6 - 189	6 - 189
2	4	VAL	VAL	ALA	ALA	J	F	6 - 189	6 - 189
1	5	VAL	VAL	ALA	ALA	B	A	6 - 189	6 - 189
2	5	VAL	VAL	ALA	ALA	L	G	6 - 189	6 - 189
1	6	VAL	VAL	ALA	ALA	B	A	6 - 189	6 - 189
2	6	VAL	VAL	ALA	ALA	N	H	6 - 189	6 - 189
1	7	VAL	VAL	ALA	ALA	B	A	6 - 189	6 - 189
2	7	VAL	VAL	ALA	ALA	P	I	6 - 189	6 - 189
1	8	VAL	VAL	ALA	ALA	B	A	6 - 189	6 - 189
2	8	VAL	VAL	ALA	ALA	R	J	6 - 189	6 - 189
1	9	VAL	VAL	ALA	ALA	B	A	6 - 189	6 - 189
2	9	VAL	VAL	ALA	ALA	T	K	6 - 189	6 - 189
1	10	VAL	VAL	ALA	ALA	B	A	6 - 189	6 - 189
2	10	VAL	VAL	ALA	ALA	V	L	6 - 189	6 - 189
1	11	VAL	VAL	ALA	ALA	B	A	6 - 189	6 - 189
2	11	VAL	VAL	ALA	ALA	X	M	6 - 189	6 - 189
1	12	MET	MET	LEU	LEU	A	B	1 - 191	1 - 191
2	12	MET	MET	LEU	LEU	C	N	1 - 191	1 - 191
1	13	VAL	VAL	LYS	LYS	A	B	6 - 205	6 - 205
2	13	VAL	VAL	LYS	LYS	E	O	6 - 205	6 - 205
1	14	THR	THR	LYS	LYS	A	B	2 - 205	2 - 205
2	14	THR	THR	LYS	LYS	G	P	2 - 205	2 - 205
1	15	VAL	VAL	ALA	ALA	A	B	6 - 197	6 - 197
2	15	VAL	VAL	ALA	ALA	I	Q	6 - 204	6 - 204
1	16	MET	MET	LYS	LYS	A	B	1 - 205	1 - 205
2	16	MET	MET	LYS	LYS	K	R	1 - 205	1 - 205
1	17	ARG	ARG	LYS	LYS	A	B	4 - 205	4 - 205
2	17	ARG	ARG	LYS	LYS	M	S	4 - 205	4 - 205
1	18	MET	MET	LYS	LYS	A	B	1 - 205	1 - 205
2	18	MET	MET	LYS	LYS	O	T	1 - 205	1 - 205
1	19	MET	MET	ARG	ARG	A	B	1 - 188	1 - 188
2	19	MET	MET	ARG	ARG	Q	U	1 - 188	1 - 188
1	20	MET	MET	LYS	LYS	A	B	1 - 205	1 - 205
2	20	MET	MET	LYS	LYS	S	V	1 - 205	1 - 205
1	21	MET	MET	LYS	LYS	A	B	1 - 205	1 - 205
2	21	MET	MET	LYS	LYS	U	W	1 - 205	1 - 205
1	22	MET	MET	PRO	PRO	A	B	1 - 194	1 - 194
2	22	MET	MET	PRO	PRO	W	X	1 - 194	1 - 194
1	23	ARG	ARG	LYS	LYS	D	C	5 - 205	5 - 205
2	23	ARG	ARG	LYS	LYS	F	D	5 - 205	5 - 205
1	24	ARG	ARG	LEU	LEU	D	C	5 - 191	5 - 191
2	24	ARG	ARG	LEU	LEU	H	E	4 - 191	4 - 191
1	25	ARG	ARG	LYS	LYS	D	C	5 - 205	5 - 205
2	25	ARG	ARG	LYS	LYS	J	F	5 - 205	5 - 205
1	26	ARG	ARG	LYS	LYS	D	C	5 - 205	5 - 205
2	26	ARG	ARG	LYS	LYS	L	G	5 - 205	5 - 205
1	27	ARG	ARG	LYS	LYS	D	C	5 - 205	5 - 205
2	27	ARG	ARG	LYS	LYS	N	H	5 - 205	5 - 205
1	28	ARG	ARG	LYS	LYS	D	C	5 - 205	5 - 205
2	28	ARG	ARG	LYS	LYS	P	I	5 - 205	5 - 205
1	29	ARG	ARG	LYS	LYS	D	C	5 - 205	5 - 205
2	29	ARG	ARG	LYS	LYS	R	J	5 - 205	5 - 205
1	30	ARG	ARG	LYS	LYS	D	C	5 - 205	5 - 205
2	30	ARG	ARG	LYS	LYS	T	K	5 - 205	5 - 205
1	31	ARG	ARG	LYS	LYS	D	C	5 - 205	5 - 205
2	31	ARG	ARG	LYS	LYS	V	L	5 - 205	5 - 205
1	32	ARG	ARG	ALA	ALA	D	C	5 - 204	5 - 204
2	32	ARG	ARG	ALA	ALA	X	M	5 - 204	5 - 204
1	33	ARG	ARG	LEU	LEU	F	D	5 - 191	5 - 191
2	33	ARG	ARG	LEU	LEU	H	E	4 - 191	4 - 191
1	34	ARG	ARG	LYS	LYS	F	D	5 - 205	5 - 205
2	34	ARG	ARG	LYS	LYS	J	F	5 - 205	5 - 205
1	35	ARG	ARG	LYS	LYS	F	D	5 - 205	5 - 205
2	35	ARG	ARG	LYS	LYS	L	G	5 - 205	5 - 205
1	36	ARG	ARG	LYS	LYS	F	D	5 - 205	5 - 205
2	36	ARG	ARG	LYS	LYS	N	H	5 - 205	5 - 205
1	37	ARG	ARG	LYS	LYS	F	D	5 - 205	5 - 205
2	37	ARG	ARG	LYS	LYS	P	I	5 - 205	5 - 205
1	38	ARG	ARG	ALA	ALA	F	D	5 - 204	5 - 204
2	38	ARG	ARG	ALA	ALA	R	J	5 - 204	5 - 204
1	39	ARG	ARG	ALA	ALA	F	D	5 - 204	5 - 204
2	39	ARG	ARG	ALA	ALA	T	K	5 - 204	5 - 204
1	40	ARG	ARG	LYS	LYS	F	D	5 - 205	5 - 205
2	40	ARG	ARG	LYS	LYS	V	L	5 - 205	5 - 205
1	41	ARG	ARG	ALA	ALA	F	D	5 - 204	5 - 204
2	41	ARG	ARG	ALA	ALA	X	M	5 - 204	5 - 204
1	42	THR	THR	GLY	GLY	H	E	2 - 192	2 - 192
2	42	THR	THR	GLY	GLY	J	F	2 - 192	2 - 192
1	43	MET	MET	LEU	LEU	H	E	1 - 191	1 - 191
2	43	MET	MET	LEU	LEU	L	G	1 - 191	1 - 191
1	44	MET	MET	GLY	GLY	H	E	1 - 192	1 - 192
2	44	MET	MET	GLY	GLY	N	H	1 - 192	1 - 192
1	45	MET	MET	GLY	GLY	H	E	1 - 192	1 - 192
2	45	MET	MET	GLY	GLY	P	I	1 - 192	1 - 192
1	46	MET	MET	LEU	LEU	H	E	1 - 191	1 - 191
2	46	MET	MET	LEU	LEU	R	J	1 - 191	1 - 191
1	47	THR	THR	LEU	LEU	H	E	2 - 191	2 - 191
2	47	THR	THR	LEU	LEU	T	K	2 - 191	2 - 191
1	48	MET	MET	GLY	GLY	H	E	1 - 192	1 - 192
2	48	MET	MET	GLY	GLY	V	L	1 - 192	1 - 192
1	49	MET	MET	LEU	LEU	H	E	1 - 191	1 - 191
2	49	MET	MET	LEU	LEU	X	M	1 - 191	1 - 191
1	50	THR	THR	LYS	LYS	J	F	2 - 205	2 - 205
2	50	THR	THR	LYS	LYS	L	G	2 - 205	2 - 205
1	51	THR	THR	LYS	LYS	J	F	2 - 205	2 - 205
2	51	THR	THR	LYS	LYS	N	H	2 - 205	2 - 205
1	52	THR	THR	LYS	LYS	J	F	2 - 205	2 - 205
2	52	THR	THR	LYS	LYS	P	I	2 - 205	2 - 205
1	53	THR	THR	LYS	LYS	J	F	2 - 205	2 - 205
2	53	THR	THR	LYS	LYS	R	J	2 - 205	2 - 205
1	54	THR	THR	LYS	LYS	J	F	2 - 205	2 - 205
2	54	THR	THR	LYS	LYS	T	K	2 - 205	2 - 205
1	55	THR	THR	LYS	LYS	J	F	2 - 205	2 - 205
2	55	THR	THR	LYS	LYS	V	L	2 - 205	2 - 205
1	56	THR	THR	LYS	LYS	J	F	2 - 205	2 - 205
2	56	THR	THR	LYS	LYS	X	M	2 - 205	2 - 205
1	57	MET	MET	LYS	LYS	L	G	1 - 205	1 - 205
2	57	MET	MET	LYS	LYS	N	H	1 - 205	1 - 205
1	58	MET	MET	LYS	LYS	L	G	1 - 205	1 - 205
2	58	MET	MET	LYS	LYS	P	I	1 - 205	1 - 205
1	59	MET	MET	LYS	LYS	L	G	1 - 205	1 - 205
2	59	MET	MET	LYS	LYS	R	J	1 - 205	1 - 205
1	60	THR	THR	LYS	LYS	L	G	2 - 205	2 - 205
2	60	THR	THR	LYS	LYS	T	K	2 - 205	2 - 205
1	61	MET	MET	LYS	LYS	L	G	1 - 205	1 - 205
2	61	MET	MET	LYS	LYS	V	L	1 - 205	1 - 205
1	62	MET	MET	LYS	LYS	L	G	1 - 205	1 - 205
2	62	MET	MET	LYS	LYS	X	M	1 - 205	1 - 205
1	63	MET	MET	LYS	LYS	N	H	1 - 205	1 - 205
2	63	MET	MET	LYS	LYS	P	I	1 - 205	1 - 205
1	64	MET	MET	LYS	LYS	N	H	1 - 205	1 - 205
2	64	MET	MET	LYS	LYS	R	J	1 - 205	1 - 205
1	65	THR	THR	LYS	LYS	N	H	2 - 205	2 - 205
2	65	THR	THR	LYS	LYS	T	K	2 - 205	2 - 205
1	66	MET	MET	LYS	LYS	N	H	1 - 205	1 - 205
2	66	MET	MET	LYS	LYS	V	L	1 - 205	1 - 205
1	67	MET	MET	LYS	LYS	N	H	1 - 205	1 - 205
2	67	MET	MET	LYS	LYS	X	M	1 - 205	1 - 205
1	68	MET	MET	LYS	LYS	P	I	1 - 205	1 - 205
2	68	MET	MET	LYS	LYS	R	J	1 - 205	1 - 205
1	69	THR	THR	LYS	LYS	P	I	2 - 205	2 - 205
2	69	THR	THR	LYS	LYS	T	K	2 - 205	2 - 205
1	70	MET	MET	LYS	LYS	P	I	1 - 205	1 - 205
2	70	MET	MET	LYS	LYS	V	L	1 - 205	1 - 205
1	71	MET	MET	LYS	LYS	P	I	1 - 205	1 - 205
2	71	MET	MET	LYS	LYS	X	M	1 - 205	1 - 205
1	72	THR	THR	ALA	ALA	R	J	2 - 204	2 - 204
2	72	THR	THR	ALA	ALA	T	K	2 - 204	2 - 204
1	73	MET	MET	LYS	LYS	R	J	1 - 205	1 - 205
2	73	MET	MET	LYS	LYS	V	L	1 - 205	1 - 205
1	74	MET	MET	LYS	LYS	R	J	1 - 205	1 - 205
2	74	MET	MET	LYS	LYS	X	M	1 - 205	1 - 205
1	75	THR	THR	LYS	LYS	T	K	2 - 205	2 - 205
2	75	THR	THR	LYS	LYS	V	L	2 - 205	2 - 205
1	76	THR	THR	LYS	LYS	T	K	2 - 205	2 - 205
2	76	THR	THR	LYS	LYS	X	M	2 - 205	2 - 205
1	77	MET	MET	LYS	LYS	V	L	1 - 205	1 - 205
2	77	MET	MET	LYS	LYS	X	M	1 - 205	1 - 205
1	78	VAL	VAL	LEU	LEU	C	N	6 - 191	6 - 191
2	78	VAL	VAL	LEU	LEU	E	O	6 - 191	6 - 191
1	79	THR	THR	LEU	LEU	C	N	2 - 191	2 - 191
2	79	THR	THR	LEU	LEU	G	P	2 - 191	2 - 191
1	80	VAL	VAL	LEU	LEU	C	N	6 - 191	6 - 191
2	80	VAL	VAL	LEU	LEU	I	Q	6 - 191	6 - 191
1	81	MET	MET	LEU	LEU	C	N	1 - 191	1 - 191
2	81	MET	MET	LEU	LEU	K	R	1 - 191	1 - 191
1	82	ARG	ARG	LEU	LEU	C	N	4 - 191	4 - 191
2	82	ARG	ARG	LEU	LEU	M	S	4 - 191	4 - 191
1	83	MET	MET	LEU	LEU	C	N	1 - 191	1 - 191
2	83	MET	MET	LEU	LEU	O	T	1 - 191	1 - 191
1	84	MET	MET	ARG	ARG	C	N	1 - 188	1 - 188
2	84	MET	MET	ARG	ARG	Q	U	1 - 188	1 - 188
1	85	MET	MET	LEU	LEU	C	N	1 - 191	1 - 191
2	85	MET	MET	LEU	LEU	S	V	1 - 191	1 - 191
1	86	MET	MET	LEU	LEU	C	N	1 - 191	1 - 191
2	86	MET	MET	LEU	LEU	U	W	1 - 191	1 - 191
1	87	MET	MET	LEU	LEU	C	N	1 - 191	1 - 191
2	87	MET	MET	LEU	LEU	W	X	1 - 191	1 - 191
1	88	VAL	VAL	ALA	ALA	E	O	6 - 204	6 - 204
2	88	VAL	VAL	ALA	ALA	G	P	6 - 204	6 - 204
1	89	VAL	VAL	ALA	ALA	E	O	6 - 197	6 - 197
2	89	VAL	VAL	ALA	ALA	I	Q	6 - 204	6 - 204
1	90	VAL	VAL	LYS	LYS	E	O	6 - 205	6 - 205
2	90	VAL	VAL	LYS	LYS	K	R	6 - 205	6 - 205
1	91	VAL	VAL	LYS	LYS	E	O	6 - 205	6 - 205
2	91	VAL	VAL	LYS	LYS	M	S	6 - 205	6 - 205
1	92	VAL	VAL	LYS	LYS	E	O	6 - 205	6 - 205
2	92	VAL	VAL	LYS	LYS	O	T	6 - 205	6 - 205
1	93	VAL	VAL	ARG	ARG	E	O	6 - 188	6 - 188
2	93	VAL	VAL	ARG	ARG	Q	U	6 - 188	6 - 188
1	94	VAL	VAL	ALA	ALA	E	O	6 - 204	6 - 204
2	94	VAL	VAL	ALA	ALA	S	V	6 - 204	6 - 204
1	95	VAL	VAL	LYS	LYS	E	O	6 - 205	6 - 205
2	95	VAL	VAL	LYS	LYS	U	W	6 - 205	6 - 205
1	96	VAL	VAL	PRO	PRO	E	O	6 - 194	6 - 194
2	96	VAL	VAL	PRO	PRO	W	X	6 - 194	6 - 194
1	97	VAL	VAL	ALA	ALA	G	P	6 - 197	6 - 197
2	97	VAL	VAL	ALA	ALA	I	Q	6 - 204	6 - 204
1	98	THR	THR	LYS	LYS	G	P	2 - 205	2 - 205
2	98	THR	THR	LYS	LYS	K	R	2 - 205	2 - 205
1	99	ARG	ARG	ALA	ALA	G	P	4 - 204	4 - 204
2	99	ARG	ARG	ALA	ALA	M	S	4 - 204	4 - 204
1	100	THR	THR	LYS	LYS	G	P	2 - 205	2 - 205
2	100	THR	THR	LYS	LYS	O	T	2 - 205	2 - 205
1	101	THR	THR	ARG	ARG	G	P	2 - 188	2 - 188
2	101	THR	THR	ARG	ARG	Q	U	2 - 188	2 - 188
1	102	THR	THR	ALA	ALA	G	P	2 - 204	2 - 204
2	102	THR	THR	ALA	ALA	S	V	2 - 204	2 - 204
1	103	THR	THR	LYS	LYS	G	P	2 - 205	2 - 205
2	103	THR	THR	LYS	LYS	U	W	2 - 205	2 - 205
1	104	THR	THR	PRO	PRO	G	P	2 - 194	2 - 194
2	104	THR	THR	PRO	PRO	W	X	2 - 194	2 - 194
1	105	VAL	VAL	LYS	LYS	I	Q	6 - 205	6 - 205
2	105	VAL	VAL	LYS	LYS	K	R	6 - 205	6 - 205
1	106	VAL	VAL	ALA	ALA	I	Q	6 - 204	6 - 204
2	106	VAL	VAL	ALA	ALA	M	S	6 - 197	6 - 197
1	107	VAL	VAL	ALA	ALA	I	Q	6 - 204	6 - 204
2	107	VAL	VAL	ALA	ALA	O	T	6 - 197	6 - 197
1	108	VAL	VAL	ARG	ARG	I	Q	6 - 188	6 - 188
2	108	VAL	VAL	ARG	ARG	Q	U	6 - 188	6 - 188
1	109	VAL	VAL	ALA	ALA	I	Q	6 - 204	6 - 204
2	109	VAL	VAL	ALA	ALA	S	V	6 - 197	6 - 197
1	110	VAL	VAL	ALA	ALA	I	Q	6 - 204	6 - 204
2	110	VAL	VAL	ALA	ALA	U	W	6 - 204	6 - 204
1	111	VAL	VAL	PRO	PRO	I	Q	6 - 194	6 - 194
2	111	VAL	VAL	PRO	PRO	W	X	6 - 194	6 - 194
1	112	ARG	ARG	LYS	LYS	K	R	4 - 205	4 - 205
2	112	ARG	ARG	LYS	LYS	M	S	4 - 205	4 - 205
1	113	MET	MET	LYS	LYS	K	R	1 - 205	1 - 205
2	113	MET	MET	LYS	LYS	O	T	1 - 205	1 - 205
1	114	MET	MET	ARG	ARG	K	R	1 - 188	1 - 188
2	114	MET	MET	ARG	ARG	Q	U	1 - 188	1 - 188
1	115	MET	MET	LYS	LYS	K	R	1 - 205	1 - 205
2	115	MET	MET	LYS	LYS	S	V	1 - 205	1 - 205
1	116	MET	MET	LYS	LYS	K	R	1 - 205	1 - 205
2	116	MET	MET	LYS	LYS	U	W	1 - 205	1 - 205
1	117	MET	MET	ALA	ALA	K	R	1 - 197	1 - 197
2	117	MET	MET	PRO	PRO	W	X	1 - 194	1 - 194
1	118	ARG	ARG	LYS	LYS	M	S	4 - 205	4 - 205
2	118	ARG	ARG	LYS	LYS	O	T	4 - 205	4 - 205
1	119	ARG	ARG	ARG	ARG	M	S	4 - 188	4 - 188
2	119	ARG	ARG	ARG	ARG	Q	U	4 - 188	4 - 188
1	120	ARG	ARG	ALA	ALA	M	S	4 - 204	4 - 204
2	120	ARG	ARG	ALA	ALA	S	V	4 - 204	4 - 204
1	121	ARG	ARG	LYS	LYS	M	S	4 - 205	4 - 205
2	121	ARG	ARG	LYS	LYS	U	W	4 - 205	4 - 205
1	122	ARG	ARG	PRO	PRO	M	S	4 - 194	4 - 194
2	122	ARG	ARG	PRO	PRO	W	X	4 - 194	4 - 194
1	123	MET	MET	ARG	ARG	O	T	1 - 188	1 - 188
2	123	MET	MET	ARG	ARG	Q	U	1 - 188	1 - 188
1	124	MET	MET	LYS	LYS	O	T	1 - 205	1 - 205
2	124	MET	MET	LYS	LYS	S	V	1 - 205	1 - 205
1	125	MET	MET	LYS	LYS	O	T	1 - 205	1 - 205
2	125	MET	MET	LYS	LYS	U	W	1 - 205	1 - 205
1	126	MET	MET	PRO	PRO	O	T	1 - 194	1 - 194
2	126	MET	MET	PRO	PRO	W	X	1 - 194	1 - 194
1	127	MET	MET	ARG	ARG	Q	U	1 - 188	1 - 188
2	127	MET	MET	ARG	ARG	S	V	1 - 188	1 - 188
1	128	MET	MET	ARG	ARG	Q	U	1 - 188	1 - 188
2	128	MET	MET	ARG	ARG	U	W	1 - 188	1 - 188
1	129	MET	MET	ARG	ARG	Q	U	1 - 188	1 - 188
2	129	MET	MET	ARG	ARG	W	X	1 - 188	1 - 188
1	130	MET	MET	LYS	LYS	S	V	1 - 205	1 - 205
2	130	MET	MET	LYS	LYS	U	W	1 - 205	1 - 205
1	131	MET	MET	PRO	PRO	S	V	1 - 194	1 - 194
2	131	MET	MET	PRO	PRO	W	X	1 - 194	1 - 194
1	132	MET	MET	PRO	PRO	U	W	1 - 194	1 - 194
2	132	MET	MET	PRO	PRO	W	X	1 - 194	1 - 194

NCS ensembles :

#1: Protein	... Heat shock protein beta-1 / Heat shock response / HspB1 / 28 kDa heat shock protein / Estrogen-regulated 24 kDa protein / Heat shock 27 kDa protein / ...HspB1 / 28 kDa heat shock protein / Estrogen-regulated 24 kDa protein / Heat shock 27 kDa protein / HSP 27 / Stress-responsive protein 27 / SRP27 Mass: 22810.486 Da / Num. of mol.: 24 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: HSPB1, HSP27, HSP28 / Production host: Escherichia coli (E. coli) / References: UniProt: P04792

#1: Protein

...
Heat shock protein beta-1 /

Heat shock response / HspB1 / 28 kDa heat shock protein / Estrogen-regulated 24 kDa protein / Heat shock 27 kDa protein / ...

Mass: 22810.486 Da / Num. of mol.: 24
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Homo sapiens (human) / Gene: HSPB1, HSP27, HSP28 / Production host:

Escherichia coli (E. coli) / References: UniProt: P04792

-
Experiment

Experiment	Method: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

Crystal	Density Matthews: 3.68 Å³/Da / Density % sol: 66.61 %
Crystal grow	Temperature: 294.15 K / Method: vapor diffusion, sitting drop Details: 0.5 M ammonium phosphate monobasic and 40 % tert-butanol.

-
Data collection

Diffraction

Mean temperature: 100 K

Diffraction source

Source:

SYNCHROTRON / Site:

SSRL

/ Beamline: BL7-1 / Wavelength: 1.0971 Å

Detector

Type: ADSC QUANTUM 315 / Detector: CCD / Date: Apr 21, 2012

Radiation

Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray

Radiation wavelength

Wavelength: 1.0971 Å / Relative weight: 1

Reflection twin

Crystal-ID	ID	Operator	Domain-ID	Fraction
1	1	H, K, L	1	0.58
1	1	K, H, -L	2	0.057
1	1	-K, -1/3H+1/3K+4/3L, -2/3H-1/3K-1/3L	3	0.062
1	1	-1/3H+1/3K+4/3L, -K, 2/3H+1/3K+1/3L	4	0.061
1	1	1/3H-1/3K-4/3L, -H, 1/3H+2/3K-1/3L	5	0.062
1	1	-H, 1/3H-1/3K-4/3L, -1/3H-2/3K+1/3L	6	0.061
1	1	-1/3H-2/3K+4/3L, H+K, -1/3H+1/3K+1/3L	7	0.059
1	1	-2/3H-1/3K-4/3L, H+K, 1/3H-1/3K-1/3L	8	0.059

Reflection

Resolution: 3.579→93.73 Å / Num. obs: 87279 / % possible obs: 99.77 % / Redundancy: 2.5 % / Net I/σ(I): 2.7

Reflection shell

Resolution: 3.579→3.672 Å

-
Processing

Software

Name	Version	Classification
REFMAC	5.8.0107	refinement
MOSFLM		data reduction
SCALA		data scaling
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 2YGD

2ygd

Resolution: 3.58→93.73 Å / Cor.coef. F_o:F_c: 0.812 / Cor.coef. F_o:F_c free: 0.793 / SU B: 26.825 / SU ML: 0.408 / Cross valid method: THROUGHOUT / ESU R Free: 0.118 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.24157	4645	5.1 %	RANDOM
R_work	0.23753	-	-	-
obs	0.23773	87279	99.77 %	-

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å

Displacement parameters

B_iso mean: 65.079 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	0.69 Å²	0 Å²	0 Å²
2-	-	0.69 Å²	0 Å²
3-	-	-	-1.37 Å²

Refinement step

Cycle: 1 / Resolution: 3.58→93.73 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	32356	0	0	0	32356

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.013	0.019	33231
X-RAY DIFFRACTION	r_bond_other_d	0.017	0.02	30534
X-RAY DIFFRACTION	r_angle_refined_deg	1.596	1.955	45063
X-RAY DIFFRACTION	r_angle_other_deg	2.801	3	70428
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	6.789	5	3896
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	35.422	22.384	1577
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	16.421	15	5266
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	11.705	15	342
X-RAY DIFFRACTION	r_chiral_restr	0.098	0.2	4727
X-RAY DIFFRACTION	r_gen_planes_refined	0.011	0.021	36746
X-RAY DIFFRACTION	r_gen_planes_other	0.011	0.02	7836
X-RAY DIFFRACTION	r_nbd_refined
X-RAY DIFFRACTION	r_nbd_other
X-RAY DIFFRACTION	r_nbtor_refined
X-RAY DIFFRACTION	r_nbtor_other
X-RAY DIFFRACTION	r_xyhbond_nbd_refined
X-RAY DIFFRACTION	r_xyhbond_nbd_other
X-RAY DIFFRACTION	r_metal_ion_refined
X-RAY DIFFRACTION	r_metal_ion_other
X-RAY DIFFRACTION	r_symmetry_vdw_refined
X-RAY DIFFRACTION	r_symmetry_vdw_other
X-RAY DIFFRACTION	r_symmetry_hbond_refined
X-RAY DIFFRACTION	r_symmetry_hbond_other
X-RAY DIFFRACTION	r_symmetry_metal_ion_refined
X-RAY DIFFRACTION	r_symmetry_metal_ion_other
X-RAY DIFFRACTION	r_mcbond_it
X-RAY DIFFRACTION	r_mcbond_other
X-RAY DIFFRACTION	r_mcangle_it
X-RAY DIFFRACTION	r_mcangle_other
X-RAY DIFFRACTION	r_scbond_it
X-RAY DIFFRACTION	r_scbond_other
X-RAY DIFFRACTION	r_scangle_it
X-RAY DIFFRACTION	r_scangle_other
X-RAY DIFFRACTION	r_long_range_B_refined
X-RAY DIFFRACTION	r_long_range_B_other
X-RAY DIFFRACTION	r_rigid_bond_restr
X-RAY DIFFRACTION	r_sphericity_free
X-RAY DIFFRACTION	r_sphericity_bonded

Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-ID	Dom-ID	Auth asym-ID	Number	Rms dev position (Å)
1	1	B	12172	0.26
1	2	D	12172	0.26
2	1	B	12416	0.25
2	2	F	12416	0.25
3	1	B	12552	0.24
3	2	H	12552	0.24
4	1	B	12520	0.24
4	2	J	12520	0.24
5	1	B	12572	0.23
5	2	L	12572	0.23
6	1	B	11692	0.25
6	2	N	11692	0.25
7	1	B	12602	0.24
7	2	P	12602	0.24
8	1	B	12926	0.24
8	2	R	12926	0.24
9	1	B	12892	0.24
9	2	T	12892	0.24
10	1	B	12446	0.24
10	2	V	12446	0.24
11	1	B	12392	0.25
11	2	X	12392	0.25
12	1	A	12872	0.3
12	2	C	12872	0.3
13	1	A	13058	0.29
13	2	E	13058	0.29
14	1	A	13660	0.3
14	2	G	13660	0.3
15	1	A	12978	0.29
15	2	I	12978	0.29
16	1	A	13094	0.29
16	2	K	13094	0.29
17	1	A	13654	0.29
17	2	M	13654	0.29
18	1	A	13278	0.3
18	2	O	13278	0.3
19	1	A	12654	0.29
19	2	Q	12654	0.29
20	1	A	13424	0.29
20	2	S	13424	0.29
21	1	A	13188	0.3
21	2	U	13188	0.3
22	1	A	13206	0.29
22	2	W	13206	0.29
23	1	D	13594	0.26
23	2	F	13594	0.26
24	1	D	13272	0.22
24	2	H	13272	0.22
25	1	D	13886	0.24
25	2	J	13886	0.24
26	1	D	13860	0.24
26	2	L	13860	0.24
27	1	D	12712	0.26
27	2	N	12712	0.26
28	1	D	13854	0.23
28	2	P	13854	0.23
29	1	D	13974	0.23
29	2	R	13974	0.23
30	1	D	13986	0.25
30	2	T	13986	0.25
31	1	D	13546	0.24
31	2	V	13546	0.24
32	1	D	13934	0.23
32	2	X	13934	0.23
33	1	F	13724	0.23
33	2	H	13724	0.23
34	1	F	14152	0.22
34	2	J	14152	0.22
35	1	F	13922	0.23
35	2	L	13922	0.23
36	1	F	13342	0.23
36	2	N	13342	0.23
37	1	F	14056	0.24
37	2	P	14056	0.24
38	1	F	14250	0.22
38	2	R	14250	0.22
39	1	F	14306	0.22
39	2	T	14306	0.22
40	1	F	14258	0.23
40	2	V	14258	0.23
41	1	F	14240	0.23
41	2	X	14240	0.23
42	1	H	13562	0.23
42	2	J	13562	0.23
43	1	H	13884	0.2
43	2	L	13884	0.2
44	1	H	12688	0.24
44	2	N	12688	0.24
45	1	H	13846	0.21
45	2	P	13846	0.21
46	1	H	13942	0.21
46	2	R	13942	0.21
47	1	H	13754	0.22
47	2	T	13754	0.22
48	1	H	13736	0.21
48	2	V	13736	0.21
49	1	H	13696	0.22
49	2	X	13696	0.22
50	1	J	14062	0.22
50	2	L	14062	0.22
51	1	J	12990	0.24
51	2	N	12990	0.24
52	1	J	14282	0.23
52	2	P	14282	0.23
53	1	J	14392	0.22
53	2	R	14392	0.22
54	1	J	14536	0.22
54	2	T	14536	0.22
55	1	J	14248	0.21
55	2	V	14248	0.21
56	1	J	14076	0.23
56	2	X	14076	0.23
57	1	L	13394	0.24
57	2	N	13394	0.24
58	1	L	14478	0.22
58	2	P	14478	0.22
59	1	L	14820	0.2
59	2	R	14820	0.2
60	1	L	14424	0.21
60	2	T	14424	0.21
61	1	L	14352	0.21
61	2	V	14352	0.21
62	1	L	14278	0.23
62	2	X	14278	0.23
63	1	N	13536	0.24
63	2	P	13536	0.24
64	1	N	13840	0.22
64	2	R	13840	0.22
65	1	N	13836	0.23
65	2	T	13836	0.23
66	1	N	13626	0.23
66	2	V	13626	0.23
67	1	N	13434	0.24
67	2	X	13434	0.24
68	1	P	14678	0.22
68	2	R	14678	0.22
69	1	P	14676	0.22
69	2	T	14676	0.22
70	1	P	14158	0.22
70	2	V	14158	0.22
71	1	P	14460	0.23
71	2	X	14460	0.23
72	1	R	14816	0.21
72	2	T	14816	0.21
73	1	R	14930	0.2
73	2	V	14930	0.2
74	1	R	14774	0.22
74	2	X	14774	0.22
75	1	T	14532	0.22
75	2	V	14532	0.22
76	1	T	14474	0.23
76	2	X	14474	0.23
77	1	V	14364	0.23
77	2	X	14364	0.23
78	1	C	13236	0.25
78	2	E	13236	0.25
79	1	C	13858	0.26
79	2	G	13858	0.26
80	1	C	13550	0.26
80	2	I	13550	0.26
81	1	C	13674	0.26
81	2	K	13674	0.26
82	1	C	13542	0.27
82	2	M	13542	0.27
83	1	C	13184	0.25
83	2	O	13184	0.25
84	1	C	13242	0.26
84	2	Q	13242	0.26
85	1	C	13052	0.28
85	2	S	13052	0.28
86	1	C	13382	0.28
86	2	U	13382	0.28
87	1	C	13804	0.26
87	2	W	13804	0.26
88	1	E	14312	0.25
88	2	G	14312	0.25
89	1	E	13928	0.25
89	2	I	13928	0.25
90	1	E	13748	0.25
90	2	K	13748	0.25
91	1	E	14634	0.26
91	2	M	14634	0.26
92	1	E	13786	0.26
92	2	O	13786	0.26
93	1	E	12922	0.25
93	2	Q	12922	0.25
94	1	E	13592	0.27
94	2	S	13592	0.27
95	1	E	13592	0.26
95	2	U	13592	0.26
96	1	E	13802	0.24
96	2	W	13802	0.24
97	1	G	14104	0.26
97	2	I	14104	0.26
98	1	G	14098	0.26
98	2	K	14098	0.26
99	1	G	14864	0.26
99	2	M	14864	0.26
100	1	G	14192	0.26
100	2	O	14192	0.26
101	1	G	13382	0.26
101	2	Q	13382	0.26
102	1	G	14266	0.27
102	2	S	14266	0.27
103	1	G	14204	0.27
103	2	U	14204	0.27
104	1	G	14154	0.26
104	2	W	14154	0.26
105	1	I	13856	0.25
105	2	K	13856	0.25
106	1	I	14350	0.26
106	2	M	14350	0.26
107	1	I	13344	0.26
107	2	O	13344	0.26
108	1	I	13074	0.26
108	2	Q	13074	0.26
109	1	I	13770	0.26
109	2	S	13770	0.26
110	1	I	13666	0.28
110	2	U	13666	0.28
111	1	I	14230	0.25
111	2	W	14230	0.25
112	1	K	14078	0.26
112	2	M	14078	0.26
113	1	K	13740	0.25
113	2	O	13740	0.25
114	1	K	13486	0.25
114	2	Q	13486	0.25
115	1	K	13768	0.27
115	2	S	13768	0.27
116	1	K	13842	0.27
116	2	U	13842	0.27
117	1	K	14040	0.23
117	2	W	14040	0.23
118	1	M	14230	0.26
118	2	O	14230	0.26
119	1	M	13336	0.26
119	2	Q	13336	0.26
120	1	M	14240	0.27
120	2	S	14240	0.27
121	1	M	14164	0.26
121	2	U	14164	0.26
122	1	M	14226	0.25
122	2	W	14226	0.25
123	1	O	13010	0.25
123	2	Q	13010	0.25
124	1	O	13856	0.27
124	2	S	13856	0.27
125	1	O	13534	0.27
125	2	U	13534	0.27
126	1	O	13790	0.24
126	2	W	13790	0.24
127	1	Q	13094	0.27
127	2	S	13094	0.27
128	1	Q	13298	0.26
128	2	U	13298	0.26
129	1	Q	13578	0.25
129	2	W	13578	0.25
130	1	S	13544	0.28
130	2	U	13544	0.28
131	1	S	13602	0.27
131	2	W	13602	0.27
132	1	U	14162	0.26
132	2	W	14162	0.26

LS refinement shell

Resolution: 3.579→3.672 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.267	368	-
R_work	0.261	6267	-
obs	-	-	97.44 %

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