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

Basic information

• Entry: Database: PDB / ID: 6dv5
• Title: Oligomeric complex of a Hsp27 24-mer at 3.6 A resolution
• Components: Heat shock protein beta-1
• Keywords: CHAPERONE / Molecular Chaperone / Small Heat shock Protein / Alpha crystallin domain

Function / homology

Function:

anterograde axonal protein transport / cornified envelope / regulation of translational initiation / regulation of canonical NF-kappaB signal transduction / positive regulation of endothelial cell chemotaxis / protein kinase C inhibitor activity / regulation of protein phosphorylation / cellular response to vascular endothelial growth factor stimulus / positive regulation of blood vessel endothelial cell migration / response to unfolded protein / vascular endothelial growth factor receptor signaling pathway / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / : / axon cytoplasm / protein folding chaperone / proteasome complex / protein kinase C binding / ubiquitin binding / positive regulation of interleukin-1 beta production / negative regulation of protein kinase activity / AUF1 (hnRNP D0) binds and destabilizes mRNA / MAPK6/MAPK4 signaling / response to virus / spindle / Z disc / VEGFA-VEGFR2 Pathway / platelet aggregation / positive regulation of angiogenesis / positive regulation of tumor necrosis factor production / unfolded protein binding / response to heat / protein refolding / RNA polymerase II-specific DNA-binding transcription factor binding / cytoskeleton / Extra-nuclear estrogen signaling / regulation of autophagy / intracellular signal transduction / focal adhesion / negative regulation of apoptotic process / protein kinase binding / protein homodimerization activity / extracellular space / RNA binding / extracellular exosome / identical protein binding / nucleus / cytosol / cytoplasm

Domain/homology:

Heat shock protein beta-1, ACD domain / Alpha crystallin/Small heat shock protein, animal type / Immunoglobulin-like - #790 / Hsp20/alpha crystallin family / Small heat shock protein (sHSP) domain profile. / Alpha crystallin/Hsp20 domain / HSP20-like chaperone / Immunoglobulin-like / Sandwich / Mainly Beta

Component:

Heat shock protein beta-1

• 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

Organization	Grant number	Country
Canadian Institutes of Health Research (CIHR)	FRN # 111082	Canada

• 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, E. / Yamazaki, T. / Zoubeidi, A. / Cherkasov, A. / Brayer, G.D. / Gleave, M.

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 / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim Item: _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

Assembly

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

Summary:

• 547 kDa, 24 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	547,452	24
Polymers	547,452	24
Non-polymers	0	0
Water	0	0

1

Summary:

• Idetical with deposited unit
• defined by author
• Evidence: gel filtration

Symmetry operations:

Type	Name	Symmetry operation	Number
identity operation	1_555	x,y,z	1

Calculated values:

Buried area	104340 Å2
ΔGint	-432 kcal/mol
Surface area	205090 Å2

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:

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

NCS domain segments:

Component-ID: _ / Refine code: _

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 :

ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16
17
18
19
20
21
22
23
24
25
26
27
28
29
30
31
32
33
34
35
36
37
38
39
40
41
42
43
44
45
46
47
48
49
50
51
52
53
54
55
56
57
58
59
60
61
62
63
64
65
66
67
68
69
70
71
72
73
74
75
76
77
78
79
80
81
82
83
84
85
86
87
88
89
90
91
92
93
94
95
96
97
98
99
100
101
102
103
104
105
106
107
108
109
110
111
112
113
114
115
116
117
118
119
120
121
122
123
124
125
126
127
128
129
130
131
132

Components

#1: Protein

B A D F H J L N P R T V X C E G I K M ...
Heat shock protein beta-1 / HspB1 / 28 kDa heat shock protein / Estrogen-regulated 24 kDa protein / Heat shock 27 kDa protein / HSP 27 / Stress-responsive protein 27 / SRP27

Details:

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

Experimental details

Experiment

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

Sample preparation

• Crystal: Density Matthews: 3.68 ų/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

	Rfactor	Num. reflection	% reflection	Selection details
Rfree	0.24157	4645	5.1 %	RANDOM
Rwork	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 Ų

	Baniso -1	Baniso -2	Baniso -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

	Rfactor	Num. reflection	% reflection
Rfree	0.267	368	-
Rwork	0.261	6267	-
obs	-	-	97.44 %