PDB-3fg6: Structure of the C-terminus of Adseverin

Basic information

• Entry: Database: PDB / ID: 3fg6
• Title: Structure of the C-terminus of Adseverin
• Components: Adseverin
• Keywords: ACTIN-BINDING PROTEIN / C-terminus of adseverin / Actin capping / Actin-binding / Cytoskeleton / Phosphoprotein

Function / homology

Function:

positive regulation of secretion / regulation of chondrocyte differentiation / 1-phosphatidylinositol binding / actin nucleation / positive regulation of actin nucleation / positive regulation of megakaryocyte differentiation / actin filament severing / calcium-ion regulated exocytosis / barbed-end actin filament capping / actin filament capping / cell projection assembly / actin polymerization or depolymerization / podosome / anchoring junction / phosphatidylserine binding / brush border / phosphatidylinositol-4,5-bisphosphate binding / central nervous system development / cell projection / actin filament binding / actin cytoskeleton / actin binding / cell cortex / positive regulation of apoptotic process / negative regulation of cell population proliferation / calcium ion binding / extracellular exosome / cytoplasm

Domain/homology:

Gelsolin-like domain superfamily / Villin/Gelsolin / Gelsolin homology domain / Severin / Severin / Gelsolin-like domain / Gelsolin repeat / ADF-H/Gelsolin-like domain superfamily / 3-Layer(aba) Sandwich / Alpha Beta

Component:

Scinderin

• Biological species: Homo sapiens (human)
• Method: X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3 Å
• Authors: Robinson, R.C.
• Citation: Journal: Proc.Natl.Acad.Sci.USA / Year: 2009; Title: The crystal structure of the C-terminus of adseverin reveals the actin-binding interface.; Authors: Chumnarnsilpa, S. / Lee, W.L. / Nag, S. / Kannan, B. / Larsson, M. / Burtnick, L.D. / Robinson, R.C.

History

Deposition	Dec 5, 2008	Deposition site: RCSB / Processing site: PDBJ
Revision 1.0	Aug 11, 2009	Provider: repository / Type: Initial release
Revision 1.1	Jul 13, 2011	Group: Advisory / Refinement description / Version format compliance
Revision 1.2	Nov 1, 2017	Group: Refinement description / Category: software
Revision 1.3	Nov 1, 2023	Group: Data collection / Database references / Derived calculations / Refinement description Category: chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _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 / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

Assembly

Deposited unit

A: Adseverin

C: Adseverin

G: Adseverin

E: Adseverin

F: Adseverin

H: Adseverin

D: Adseverin

B: Adseverin

hetero molecules

Summary:

• 336 kDa, 8 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	336,329	31
Polymers	335,407	8
Non-polymers	922	23
Water	0	0

1

A: Adseverin

hetero molecules

Summary:

• defined by author&software
• 42 kDa, 1 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	42,046	4
Polymers	41,926	1
Non-polymers	120	3
Water	0

Symmetry operations:

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

Calculated values:

Method	PISA

2

C: Adseverin

hetero molecules

Summary:

• defined by author&software
• 42 kDa, 1 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	42,046	4
Polymers	41,926	1
Non-polymers	120	3
Water	0

Symmetry operations:

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

Calculated values:

Method	PISA

3

G: Adseverin

hetero molecules

Summary:

• defined by author&software
• 42 kDa, 1 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	42,046	4
Polymers	41,926	1
Non-polymers	120	3
Water	0

Symmetry operations:

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

Calculated values:

Method	PISA

4

E: Adseverin

hetero molecules

Summary:

• defined by author&software
• 42 kDa, 1 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	42,046	4
Polymers	41,926	1
Non-polymers	120	3
Water	0

Symmetry operations:

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

Calculated values:

Method	PISA

5

F: Adseverin

hetero molecules

Summary:

• defined by author&software
• 42 kDa, 1 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	42,006	3
Polymers	41,926	1
Non-polymers	80	2
Water	0

Symmetry operations:

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

Calculated values:

Method	PISA

6

H: Adseverin

hetero molecules

Summary:

• defined by author&software
• 42 kDa, 1 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	42,046	4
Polymers	41,926	1
Non-polymers	120	3
Water	0

Symmetry operations:

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

Calculated values:

Method	PISA

7

D: Adseverin

hetero molecules

Summary:

• defined by author&software
• 42 kDa, 1 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	42,046	4
Polymers	41,926	1
Non-polymers	120	3
Water	0

Symmetry operations:

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

Calculated values:

Method	PISA

8

B: Adseverin

hetero molecules

Summary:

• defined by author&software
• 42 kDa, 1 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	42,046	4
Polymers	41,926	1
Non-polymers	120	3
Water	0

Symmetry operations:

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

Calculated values:

Method	PISA

Unit cell

Length a, b, c (Å)	67.644, 90.384, 98.839
Angle α, β, γ (deg.)	88.79, 88.26, 76.26
Int Tables number	1
Space group name H-M	P1

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	A
2	1	B
3	1	C
4	1	D
5	1	E
6	1	F
7	1	G
8	1	H
1	2	A
2	2	B
3	2	C
4	2	D
5	2	E
6	2	F
7	2	G
8	2	H
1	3	A
2	3	B
3	3	C
4	3	D
5	3	E
6	3	F
7	3	G
8	3	H
1	4	A
2	4	C
3	4	G
4	4	E
5	4	F
6	4	H
7	4	D
8	4	B
1	5	A
2	5	C
3	5	G
4	5	E
5	5	F
6	5	H
7	5	D
8	5	B
1	6	A
2	6	C
3	6	G
4	6	E
5	6	F
6	6	H
7	6	D
8	6	B
1	7	A
2	7	C
3	7	G
4	7	E
5	7	F
6	7	H
7	7	D
8	7	B
1	8	A
2	8	C
3	8	G
4	8	E
5	8	F
6	8	H
7	8	D
8	8	B
1	9	A
2	9	C
3	9	G
4	9	E
5	9	F
6	9	H
7	9	D
8	9	B
1	10	A
2	10	C
3	10	G
4	10	E
5	10	F
6	10	H
7	10	D
8	10	B
1	11	A
2	11	C
3	11	G
4	11	E
5	11	F
6	11	H
7	11	D
8	11	B
1	12	A
2	12	C
3	12	G
4	12	E
5	12	F
6	12	H
7	12	D
8	12	B

NCS domain segments:

Refine code: 1

Dom-ID	Component-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	1	VAL	VAL	ILE	ILE	A	A	398 - 400	54 - 56
2	1	1	VAL	VAL	ILE	ILE	B	H	398 - 400	54 - 56
3	1	1	VAL	VAL	ILE	ILE	C	B	398 - 400	54 - 56
4	1	1	VAL	VAL	ILE	ILE	D	G	398 - 400	54 - 56
5	1	1	VAL	VAL	ILE	ILE	E	D	398 - 400	54 - 56
6	1	1	VAL	VAL	ILE	ILE	F	E	398 - 400	54 - 56
7	1	1	VAL	VAL	ILE	ILE	G	C	398 - 400	54 - 56
8	1	1	VAL	VAL	ILE	ILE	H	F	398 - 400	54 - 56
1	2	1	GLY	GLY	ASN	ASN	A	A	422 - 444	78 - 100
2	2	1	GLY	GLY	ASN	ASN	B	H	422 - 444	78 - 100
3	2	1	GLY	GLY	ASN	ASN	C	B	422 - 444	78 - 100
4	2	1	GLY	GLY	ASN	ASN	D	G	422 - 444	78 - 100
5	2	1	GLY	GLY	ASN	ASN	E	D	422 - 444	78 - 100
6	2	1	GLY	GLY	ASN	ASN	F	E	422 - 444	78 - 100
7	2	1	GLY	GLY	ASN	ASN	G	C	422 - 444	78 - 100
8	2	1	GLY	GLY	ASN	ASN	H	F	422 - 444	78 - 100
1	3	1	GLN	GLN	GLN	GLN	A	A	467 - 475	123 - 131
2	3	1	GLN	GLN	GLN	GLN	B	H	467 - 475	123 - 131
3	3	1	GLN	GLN	GLN	GLN	C	B	467 - 475	123 - 131
4	3	1	GLN	GLN	GLN	GLN	D	G	467 - 475	123 - 131
5	3	1	GLN	GLN	GLN	GLN	E	D	467 - 475	123 - 131
6	3	1	GLN	GLN	GLN	GLN	F	E	467 - 475	123 - 131
7	3	1	GLN	GLN	GLN	GLN	G	C	467 - 475	123 - 131
8	3	1	GLN	GLN	GLN	GLN	H	F	467 - 475	123 - 131
1	1	2	ALA	ALA	GLY	GLY	A	A	445 - 466	101 - 122
2	1	2	ALA	ALA	GLY	GLY	B	H	445 - 466	101 - 122
3	1	2	ALA	ALA	GLY	GLY	C	B	445 - 466	101 - 122
4	1	2	ALA	ALA	GLY	GLY	D	G	445 - 466	101 - 122
5	1	2	ALA	ALA	GLY	GLY	E	D	445 - 466	101 - 122
6	1	2	ALA	ALA	GLY	GLY	F	E	445 - 466	101 - 122
7	1	2	ALA	ALA	GLY	GLY	G	C	445 - 466	101 - 122
8	1	2	ALA	ALA	GLY	GLY	H	F	445 - 466	101 - 122
1	1	3	GLN	GLN	GLY	GLY	A	A	410 - 421	66 - 77
2	1	3	GLN	GLN	GLY	GLY	B	H	410 - 421	66 - 77
3	1	3	GLN	GLN	GLY	GLY	C	B	410 - 421	66 - 77
4	1	3	GLN	GLN	GLY	GLY	D	G	410 - 421	66 - 77
5	1	3	GLN	GLN	GLY	GLY	E	D	410 - 421	66 - 77
6	1	3	GLN	GLN	GLY	GLY	F	E	410 - 421	66 - 77
7	1	3	GLN	GLN	GLY	GLY	G	C	410 - 421	66 - 77
8	1	3	GLN	GLN	GLY	GLY	H	F	410 - 421	66 - 77
1	1	4	ARG	ARG	LYS	LYS	A	A	615 - 622	271 - 278
2	1	4	ARG	ARG	LYS	LYS	C	B	615 - 622	271 - 278
3	1	4	ARG	ARG	LYS	LYS	G	C	615 - 622	271 - 278
4	1	4	ARG	ARG	LYS	LYS	E	D	615 - 622	271 - 278
5	1	4	ARG	ARG	LYS	LYS	F	E	615 - 622	271 - 278
6	1	4	ARG	ARG	LYS	LYS	H	F	615 - 622	271 - 278
7	1	4	ARG	ARG	LYS	LYS	D	G	615 - 622	271 - 278
8	1	4	ARG	ARG	LYS	LYS	B	H	615 - 622	271 - 278
1	2	4	ASP	ASP	LYS	LYS	A	A	643 - 660	299 - 316
2	2	4	ASP	ASP	LYS	LYS	C	B	643 - 660	299 - 316
3	2	4	ASP	ASP	LYS	LYS	G	C	643 - 660	299 - 316
4	2	4	ASP	ASP	LYS	LYS	E	D	643 - 660	299 - 316
5	2	4	ASP	ASP	LYS	LYS	F	E	643 - 660	299 - 316
6	2	4	ASP	ASP	LYS	LYS	H	F	643 - 660	299 - 316
7	2	4	ASP	ASP	LYS	LYS	D	G	643 - 660	299 - 316
8	2	4	ASP	ASP	LYS	LYS	B	H	643 - 660	299 - 316
1	3	4	PRO	PRO	GLN	GLN	A	A	690 - 696	346 - 352
2	3	4	PRO	PRO	GLN	GLN	C	B	690 - 696	346 - 352
3	3	4	PRO	PRO	GLN	GLN	G	C	690 - 696	346 - 352
4	3	4	PRO	PRO	GLN	GLN	E	D	690 - 696	346 - 352
5	3	4	PRO	PRO	GLN	GLN	F	E	690 - 696	346 - 352
6	3	4	PRO	PRO	GLN	GLN	H	F	690 - 696	346 - 352
7	3	4	PRO	PRO	GLN	GLN	D	G	690 - 696	346 - 352
8	3	4	PRO	PRO	GLN	GLN	B	H	690 - 696	346 - 352
1	1	5	THR	THR	GLY	GLY	A	A	623 - 633	279 - 289
2	1	5	THR	THR	GLY	GLY	C	B	623 - 633	279 - 289
3	1	5	THR	THR	GLY	GLY	G	C	623 - 633	279 - 289
4	1	5	THR	THR	GLY	GLY	E	D	623 - 633	279 - 289
5	1	5	THR	THR	GLY	GLY	F	E	623 - 633	279 - 289
6	1	5	THR	THR	GLY	GLY	H	F	623 - 633	279 - 289
7	1	5	THR	THR	GLY	GLY	D	G	623 - 633	279 - 289
8	1	5	THR	THR	GLY	GLY	B	H	623 - 633	279 - 289
1	1	6	GLU	GLU	GLU	GLU	A	A	634 - 642	290 - 298
2	1	6	GLU	GLU	GLU	GLU	C	B	634 - 642	290 - 298
3	1	6	GLU	GLU	GLU	GLU	G	C	634 - 642	290 - 298
4	1	6	GLU	GLU	GLU	GLU	E	D	634 - 642	290 - 298
5	1	6	GLU	GLU	GLU	GLU	F	E	634 - 642	290 - 298
6	1	6	GLU	GLU	GLU	GLU	H	F	634 - 642	290 - 298
7	1	6	GLU	GLU	GLU	GLU	D	G	634 - 642	290 - 298
8	1	6	GLU	GLU	GLU	GLU	B	H	634 - 642	290 - 298
1	1	7	ASP	ASP	LYS	LYS	A	A	661 - 667	317 - 323
2	1	7	ASP	ASP	LYS	LYS	C	B	661 - 667	317 - 323
3	1	7	ASP	ASP	LYS	LYS	G	C	661 - 667	317 - 323
4	1	7	ASP	ASP	LYS	LYS	E	D	661 - 667	317 - 323
5	1	7	ASP	ASP	LYS	LYS	F	E	661 - 667	317 - 323
6	1	7	ASP	ASP	LYS	LYS	H	F	661 - 667	317 - 323
7	1	7	ASP	ASP	LYS	LYS	D	G	661 - 667	317 - 323
8	1	7	ASP	ASP	LYS	LYS	B	H	661 - 667	317 - 323
1	1	8	GLU	GLU	TRP	TRP	A	A	699 - 706	355 - 362
2	1	8	GLU	GLU	TRP	TRP	C	B	699 - 706	355 - 362
3	1	8	GLU	GLU	TRP	TRP	G	C	699 - 706	355 - 362
4	1	8	GLU	GLU	TRP	TRP	E	D	699 - 706	355 - 362
5	1	8	GLU	GLU	TRP	TRP	F	E	699 - 706	355 - 362
6	1	8	GLU	GLU	TRP	TRP	H	F	699 - 706	355 - 362
7	1	8	GLU	GLU	TRP	TRP	D	G	699 - 706	355 - 362
8	1	8	GLU	GLU	TRP	TRP	B	H	699 - 706	355 - 362
1	1	9	ASN	ASN	TRP	TRP	A	A	536 - 553	192 - 209
2	1	9	ASN	ASN	TRP	TRP	C	B	536 - 553	192 - 209
3	1	9	ASN	ASN	TRP	TRP	G	C	536 - 553	192 - 209
4	1	9	ASN	ASN	TRP	TRP	E	D	536 - 553	192 - 209
5	1	9	ASN	ASN	TRP	TRP	F	E	536 - 553	192 - 209
6	1	9	ASN	ASN	TRP	TRP	H	F	536 - 553	192 - 209
7	1	9	ASN	ASN	TRP	TRP	D	G	536 - 553	192 - 209
8	1	9	ASN	ASN	TRP	TRP	B	H	536 - 553	192 - 209
1	2	9	LEU	LEU	ARG	ARG	A	A	573 - 579	229 - 235
2	2	9	LEU	LEU	ARG	ARG	C	B	573 - 579	229 - 235
3	2	9	LEU	LEU	ARG	ARG	G	C	573 - 579	229 - 235
4	2	9	LEU	LEU	ARG	ARG	E	D	573 - 579	229 - 235
5	2	9	LEU	LEU	ARG	ARG	F	E	573 - 579	229 - 235
6	2	9	LEU	LEU	ARG	ARG	H	F	573 - 579	229 - 235
7	2	9	LEU	LEU	ARG	ARG	D	G	573 - 579	229 - 235
8	2	9	LEU	LEU	ARG	ARG	B	H	573 - 579	229 - 235
1	3	9	PRO	PRO	ASN	ASN	A	A	509 - 518	165 - 174
2	3	9	PRO	PRO	ASN	ASN	C	B	509 - 518	165 - 174
3	3	9	PRO	PRO	ASN	ASN	G	C	509 - 518	165 - 174
4	3	9	PRO	PRO	ASN	ASN	E	D	509 - 518	165 - 174
5	3	9	PRO	PRO	ASN	ASN	F	E	509 - 518	165 - 174
6	3	9	PRO	PRO	ASN	ASN	H	F	509 - 518	165 - 174
7	3	9	PRO	PRO	ASN	ASN	D	G	509 - 518	165 - 174
8	3	9	PRO	PRO	ASN	ASN	B	H	509 - 518	165 - 174
1	1	10	VAL	VAL	VAL	VAL	A	A	554 - 572	210 - 228
2	1	10	VAL	VAL	VAL	VAL	C	B	554 - 572	210 - 228
3	1	10	VAL	VAL	VAL	VAL	G	C	554 - 572	210 - 228
4	1	10	VAL	VAL	VAL	VAL	E	D	554 - 572	210 - 228
5	1	10	VAL	VAL	VAL	VAL	F	E	554 - 572	210 - 228
6	1	10	VAL	VAL	VAL	VAL	H	F	554 - 572	210 - 228
7	1	10	VAL	VAL	VAL	VAL	D	G	554 - 572	210 - 228
8	1	10	VAL	VAL	VAL	VAL	B	H	554 - 572	210 - 228
1	1	11	ILE	ILE	LEU	LEU	A	A	525 - 535	181 - 191
2	1	11	ILE	ILE	LEU	LEU	C	B	525 - 535	181 - 191
3	1	11	ILE	ILE	LEU	LEU	G	C	525 - 535	181 - 191
4	1	11	ILE	ILE	LEU	LEU	E	D	525 - 535	181 - 191
5	1	11	ILE	ILE	LEU	LEU	F	E	525 - 535	181 - 191
6	1	11	ILE	ILE	LEU	LEU	H	F	525 - 535	181 - 191
7	1	11	ILE	ILE	LEU	LEU	D	G	525 - 535	181 - 191
8	1	11	ILE	ILE	LEU	LEU	B	H	525 - 535	181 - 191
1	1	12	ILE	ILE	LYS	LYS	A	A	580 - 596	236 - 252
2	1	12	ILE	ILE	LYS	LYS	C	B	580 - 596	236 - 252
3	1	12	ILE	ILE	LYS	LYS	G	C	580 - 596	236 - 252
4	1	12	ILE	ILE	LYS	LYS	E	D	580 - 596	236 - 252
5	1	12	ILE	ILE	LYS	LYS	F	E	580 - 596	236 - 252
6	1	12	ILE	ILE	LYS	LYS	H	F	580 - 596	236 - 252
7	1	12	ILE	ILE	LYS	LYS	D	G	580 - 596	236 - 252
8	1	12	ILE	ILE	LYS	LYS	B	H	580 - 596	236 - 252

NCS ensembles :

ID
1
2
3
4
5
6
7
8
9
10
11
12

Components

#1: Protein

A C G E F H D B
Adseverin / Scinderin

Details:

Mass: 41925.914 Da / Num. of mol.: 8 / Fragment: C-terminal domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SCIN, KIAA1905 / Plasmid: pSY5 (modified pET21d) / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 Codonplus (DE3)-RIL / References: UniProt: Q9Y6U3

#2: Chemical

A-2001 A-2002 A-2003 C-2001 C-2002 C-2003 G-2001 G-2002 G-2003 E-2001 E-2002 E-2003 F-2002 F-2003 H-2001 H-2002 H-2003 D-2001 D-2002 D-2003 ...
ChemComp-CA / CALCIUM ION

Details:

Mass: 40.078 Da / Num. of mol.: 23 / Source method: obtained synthetically / Formula: Ca

Experimental details

Experiment

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

Sample preparation

• Crystal: Density Matthews: 1.749113 ų/Da / Density % sol: 29.678656 % / Mosaicity: 0.829 °
• Crystal grow: Temperature: 289 K / Method: vapor diffusion, sitting drop; Details: 20% PEG 4000, 200mM sodium isothiocyanate, VAPOR DIFFUSION, SITTING DROP, temperature 289K

Data collection

• Diffraction: Mean temperature: 105 K
• Diffraction source: Source: SYNCHROTRON / Site: NSRRC / Beamline: BL13B1 / Wavelength: 1 Å
• Detector: Type: ADSC QUANTUM 315 / Detector: CCD / Date: Mar 20, 2007
• Radiation: Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
• Radiation wavelength: Wavelength: 1 Å / Relative weight: 1
• Reflection: Redundancy: 1.9 % / Av σ(I) over netI: 16.78 / Number: 79198 / R_merge(I) obs: 0.04 / Χ²: 0.91 / D res high: 3 Å / D res low: 30 Å / Num. obs: 41218 / % possible obs: 90.3

Diffraction reflection shell

Highest resolution (Å)	Lowest resolution (Å)	% possible obs (%)	ID	Rmerge(I) obs	Chi squared	Redundancy
6.44	30	88.3	1	0.026	0.681	1.9
5.12	6.44	90.4	1	0.031	0.874	1.9
4.48	5.12	89.2	1	0.028	0.771	1.9
4.07	4.48	89.5	1	0.031	0.818	1.9
3.78	4.07	90.4	1	0.039	0.926	2
3.56	3.78	92.3	1	0.051	1.01	1.9
3.38	3.56	93.5	1	0.066	0.976	1.9
3.23	3.38	93.6	1	0.087	0.916	1.9
3.11	3.23	91.1	1	0.105	0.959	1.9
3	3.11	85	1	0.142	1.182	1.8

• Reflection: Resolution: 3→30 Å / Num. obs: 41218 / % possible obs: 90.3 % / Redundancy: 1.9 % / R_merge(I) obs: 0.04 / Χ²: 0.908 / Net I/σ(I): 16.784
• Reflection shell: Resolution: 3→3.11 Å / Redundancy: 1.8 % / R_merge(I) obs: 0.142 / Num. unique all: 3909 / Χ²: 1.182 / % possible all: 85

Phasing

• Phasing: Method: molecular replacement

Phasing MR

Model details: Phaser MODE: MR_AUTO

	Highest resolution	Lowest resolution
Rotation	2.99 Å	29.92 Å
Translation	2.99 Å	29.92 Å

Processing

Software

Name	Version	Classification	NB
DENZO		data reduction
SCALEPACK		data scaling
PHASER		phasing
REFMAC		refinement
PDB_EXTRACT	3.006	data extraction

Refinement

Method to determine structure: MOLECULAR REPLACEMENT
Starting model: 1P8X

1p8x

Resolution: 3→29.92 Å / Cor.coef. F_o:F_c: 0.895 / Cor.coef. F_o:F_c free: 0.842 / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.783 / SU B: 61.231 / SU ML: 0.517 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.651 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	Rfactor	Num. reflection	% reflection	Selection details
Rfree	0.295	2084	5.1 %	RANDOM
Rwork	0.244	39127	-	-
obs	0.247	41211	90.23 %	-

• Solvent computation: Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK

Displacement parameters

B_iso max: 71.73 Ų / B_iso mean: 38.605 Ų / B_iso min: 7.72 Ų

	Baniso -1	Baniso -2	Baniso -3
1-	0.05 Å2	0.05 Å2	0.08 Å2
2-	-	-0.05 Å2	-0.04 Å2
3-	-	-	-0.03 Å2

Refinement step

Cycle: LAST / Resolution: 3→29.92 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	19089	0	23	0	19112

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.007	0.022	19516
X-RAY DIFFRACTION	r_angle_refined_deg	1.002	1.951	26432
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.354	5	2350
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	36.442	24.865	962
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	18.974	15	3389
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	18.151	15	109
X-RAY DIFFRACTION	r_chiral_restr	0.067	0.2	2845
X-RAY DIFFRACTION	r_gen_planes_refined	0.003	0.02	14855
X-RAY DIFFRACTION	r_nbd_refined	0.203	0.2	8005
X-RAY DIFFRACTION	r_nbtor_refined	0.31	0.2	12808
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.128	0.2	638
X-RAY DIFFRACTION	r_metal_ion_refined	0.106	0.2	29
X-RAY DIFFRACTION	r_symmetry_vdw_refined	0.301	0.2	326
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.245	0.2	28
X-RAY DIFFRACTION	r_mcbond_it	0.168	1.5	12037
X-RAY DIFFRACTION	r_mcangle_it	0.298	2	18999
X-RAY DIFFRACTION	r_scbond_it	0.306	3	8623
X-RAY DIFFRACTION	r_scangle_it	0.495	4.5	7433

Refine LS restraints NCS

Dom-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Ens-ID	Auth asym-ID	Number	Type	Rms dev position (Å)	Weight position
1	A	252	TIGHT POSITIONAL	0.02	0.05
1	B	252	TIGHT POSITIONAL	0.02	0.05
1	C	252	TIGHT POSITIONAL	0.02	0.05
1	D	252	TIGHT POSITIONAL	0.03	0.05
1	E	252	TIGHT POSITIONAL	0.03	0.05
1	F	252	TIGHT POSITIONAL	0.02	0.05
1	G	252	TIGHT POSITIONAL	0.02	0.05
1	H	252	TIGHT POSITIONAL	0.02	0.05
1	A	252	TIGHT THERMAL	0.03	0.5
1	B	252	TIGHT THERMAL	0.03	0.5
1	C	252	TIGHT THERMAL	0.03	0.5
1	D	252	TIGHT THERMAL	0.04	0.5
1	E	252	TIGHT THERMAL	0.03	0.5
1	F	252	TIGHT THERMAL	0.03	0.5
1	G	252	TIGHT THERMAL	0.03	0.5
1	H	252	TIGHT THERMAL	0.04	0.5
2	A	164	TIGHT POSITIONAL	0.02	0.05
2	B	164	TIGHT POSITIONAL	0.02	0.05
2	C	164	TIGHT POSITIONAL	0.02	0.05
2	D	164	TIGHT POSITIONAL	0.02	0.05
2	E	164	TIGHT POSITIONAL	0.02	0.05
2	F	164	TIGHT POSITIONAL	0.02	0.05
2	G	164	TIGHT POSITIONAL	0.02	0.05
2	H	164	TIGHT POSITIONAL	0.02	0.05
2	A	164	TIGHT THERMAL	0.03	0.5
2	B	164	TIGHT THERMAL	0.02	0.5
2	C	164	TIGHT THERMAL	0.03	0.5
2	D	164	TIGHT THERMAL	0.03	0.5
2	E	164	TIGHT THERMAL	0.02	0.5
2	F	164	TIGHT THERMAL	0.02	0.5
2	G	164	TIGHT THERMAL	0.03	0.5
2	H	164	TIGHT THERMAL	0.03	0.5
3	A	99	TIGHT POSITIONAL	0.02	0.05
3	B	99	TIGHT POSITIONAL	0.02	0.05
3	C	99	TIGHT POSITIONAL	0.02	0.05
3	D	99	TIGHT POSITIONAL	0.02	0.05
3	E	99	TIGHT POSITIONAL	0.02	0.05
3	F	99	TIGHT POSITIONAL	0.02	0.05
3	G	99	TIGHT POSITIONAL	0.02	0.05
3	H	99	TIGHT POSITIONAL	0.02	0.05
3	A	99	TIGHT THERMAL	0.03	0.5
3	B	99	TIGHT THERMAL	0.02	0.5
3	C	99	TIGHT THERMAL	0.03	0.5
3	D	99	TIGHT THERMAL	0.03	0.5
3	E	99	TIGHT THERMAL	0.03	0.5
3	F	99	TIGHT THERMAL	0.03	0.5
3	G	99	TIGHT THERMAL	0.03	0.5
3	H	99	TIGHT THERMAL	0.03	0.5
4	A	274	TIGHT POSITIONAL	0.02	0.05
4	C	274	TIGHT POSITIONAL	0.02	0.05
4	G	274	TIGHT POSITIONAL	0.02	0.05
4	E	274	TIGHT POSITIONAL	0.02	0.05
4	F	274	TIGHT POSITIONAL	0.02	0.05
4	H	274	TIGHT POSITIONAL	0.02	0.05
4	D	274	TIGHT POSITIONAL	0.02	0.05
4	B	274	TIGHT POSITIONAL	0.02	0.05
4	A	274	TIGHT THERMAL	0.03	0.5
4	C	274	TIGHT THERMAL	0.03	0.5
4	G	274	TIGHT THERMAL	0.02	0.5
4	E	274	TIGHT THERMAL	0.02	0.5
4	F	274	TIGHT THERMAL	0.03	0.5
4	H	274	TIGHT THERMAL	0.04	0.5
4	D	274	TIGHT THERMAL	0.03	0.5
4	B	274	TIGHT THERMAL	0.03	0.5
5	A	85	TIGHT POSITIONAL	0.02	0.05
5	C	85	TIGHT POSITIONAL	0.02	0.05
5	G	85	TIGHT POSITIONAL	0.01	0.05
5	E	85	TIGHT POSITIONAL	0.02	0.05
5	F	85	TIGHT POSITIONAL	0.01	0.05
5	H	85	TIGHT POSITIONAL	0.02	0.05
5	D	85	TIGHT POSITIONAL	0.02	0.05
5	B	85	TIGHT POSITIONAL	0.02	0.05
5	A	85	TIGHT THERMAL	0.03	0.5
5	C	85	TIGHT THERMAL	0.02	0.5
5	G	85	TIGHT THERMAL	0.03	0.5
5	E	85	TIGHT THERMAL	0.02	0.5
5	F	85	TIGHT THERMAL	0.02	0.5
5	H	85	TIGHT THERMAL	0.03	0.5
5	D	85	TIGHT THERMAL	0.02	0.5
5	B	85	TIGHT THERMAL	0.02	0.5
6	A	74	TIGHT POSITIONAL	0.02	0.05
6	C	74	TIGHT POSITIONAL	0.01	0.05
6	G	74	TIGHT POSITIONAL	0.02	0.05
6	E	74	TIGHT POSITIONAL	0.02	0.05
6	F	74	TIGHT POSITIONAL	0.02	0.05
6	H	74	TIGHT POSITIONAL	0.02	0.05
6	D	74	TIGHT POSITIONAL	0.02	0.05
6	B	74	TIGHT POSITIONAL	0.02	0.05
6	A	74	TIGHT THERMAL	0.02	0.5
6	C	74	TIGHT THERMAL	0.02	0.5
6	G	74	TIGHT THERMAL	0.02	0.5
6	E	74	TIGHT THERMAL	0.02	0.5
6	F	74	TIGHT THERMAL	0.03	0.5
6	H	74	TIGHT THERMAL	0.02	0.5
6	D	74	TIGHT THERMAL	0.02	0.5
6	B	74	TIGHT THERMAL	0.02	0.5
7	A	55	TIGHT POSITIONAL	0.01	0.05
7	C	55	TIGHT POSITIONAL	0.02	0.05
7	G	55	TIGHT POSITIONAL	0.02	0.05
7	E	55	TIGHT POSITIONAL	0.01	0.05
7	F	55	TIGHT POSITIONAL	0.02	0.05
7	H	55	TIGHT POSITIONAL	0.02	0.05
7	D	55	TIGHT POSITIONAL	0.03	0.05
7	B	55	TIGHT POSITIONAL	0.02	0.05
7	A	55	TIGHT THERMAL	0.03	0.5
7	C	55	TIGHT THERMAL	0.03	0.5
7	G	55	TIGHT THERMAL	0.02	0.5
7	E	55	TIGHT THERMAL	0.03	0.5
7	F	55	TIGHT THERMAL	0.03	0.5
7	H	55	TIGHT THERMAL	0.04	0.5
7	D	55	TIGHT THERMAL	0.03	0.5
7	B	55	TIGHT THERMAL	0.03	0.5
8	A	66	TIGHT POSITIONAL	0.01	0.05
8	C	66	TIGHT POSITIONAL	0.02	0.05
8	G	66	TIGHT POSITIONAL	0.02	0.05
8	E	66	TIGHT POSITIONAL	0.02	0.05
8	F	66	TIGHT POSITIONAL	0.01	0.05
8	H	66	TIGHT POSITIONAL	0.02	0.05
8	D	66	TIGHT POSITIONAL	0.02	0.05
8	B	66	TIGHT POSITIONAL	0.02	0.05
8	A	66	TIGHT THERMAL	0.02	0.5
8	C	66	TIGHT THERMAL	0.04	0.5
8	G	66	TIGHT THERMAL	0.03	0.5
8	E	66	TIGHT THERMAL	0.03	0.5
8	F	66	TIGHT THERMAL	0.02	0.5
8	H	66	TIGHT THERMAL	0.03	0.5
8	D	66	TIGHT THERMAL	0.02	0.5
8	B	66	TIGHT THERMAL	0.03	0.5
9	A	296	TIGHT POSITIONAL	0.02	0.05
9	C	296	TIGHT POSITIONAL	0.02	0.05
9	G	296	TIGHT POSITIONAL	0.01	0.05
9	E	296	TIGHT POSITIONAL	0.02	0.05
9	F	296	TIGHT POSITIONAL	0.02	0.05
9	H	296	TIGHT POSITIONAL	0.02	0.05
9	D	296	TIGHT POSITIONAL	0.02	0.05
9	B	296	TIGHT POSITIONAL	0.02	0.05
9	A	296	TIGHT THERMAL	0.04	0.5
9	C	296	TIGHT THERMAL	0.03	0.5
9	G	296	TIGHT THERMAL	0.03	0.5
9	E	296	TIGHT THERMAL	0.03	0.5
9	F	296	TIGHT THERMAL	0.03	0.5
9	H	296	TIGHT THERMAL	0.04	0.5
9	D	296	TIGHT THERMAL	0.03	0.5
9	B	296	TIGHT THERMAL	0.03	0.5
10	A	135	TIGHT POSITIONAL	0.02	0.05
10	C	135	TIGHT POSITIONAL	0.02	0.05
10	G	135	TIGHT POSITIONAL	0.02	0.05
10	E	135	TIGHT POSITIONAL	0.02	0.05
10	F	135	TIGHT POSITIONAL	0.02	0.05
10	H	135	TIGHT POSITIONAL	0.02	0.05
10	D	135	TIGHT POSITIONAL	0.02	0.05
10	B	135	TIGHT POSITIONAL	0.02	0.05
10	A	135	TIGHT THERMAL	0.04	0.5
10	C	135	TIGHT THERMAL	0.04	0.5
10	G	135	TIGHT THERMAL	0.03	0.5
10	E	135	TIGHT THERMAL	0.04	0.5
10	F	135	TIGHT THERMAL	0.03	0.5
10	H	135	TIGHT THERMAL	0.04	0.5
10	D	135	TIGHT THERMAL	0.03	0.5
10	B	135	TIGHT THERMAL	0.03	0.5
11	A	81	TIGHT POSITIONAL	0.02	0.05
11	C	81	TIGHT POSITIONAL	0.02	0.05
11	G	81	TIGHT POSITIONAL	0.01	0.05
11	E	81	TIGHT POSITIONAL	0.03	0.05
11	F	81	TIGHT POSITIONAL	0.02	0.05
11	H	81	TIGHT POSITIONAL	0.02	0.05
11	D	81	TIGHT POSITIONAL	0.02	0.05
11	B	81	TIGHT POSITIONAL	0.02	0.05
11	A	81	TIGHT THERMAL	0.04	0.5
11	C	81	TIGHT THERMAL	0.04	0.5
11	G	81	TIGHT THERMAL	0.03	0.5
11	E	81	TIGHT THERMAL	0.04	0.5
11	F	81	TIGHT THERMAL	0.03	0.5
11	H	81	TIGHT THERMAL	0.05	0.5
11	D	81	TIGHT THERMAL	0.03	0.5
11	B	81	TIGHT THERMAL	0.03	0.5
12	A	137	TIGHT POSITIONAL	0.02	0.05
12	C	137	TIGHT POSITIONAL	0.02	0.05
12	G	137	TIGHT POSITIONAL	0.01	0.05
12	E	137	TIGHT POSITIONAL	0.02	0.05
12	F	137	TIGHT POSITIONAL	0.02	0.05
12	H	137	TIGHT POSITIONAL	0.02	0.05
12	D	137	TIGHT POSITIONAL	0.01	0.05
12	B	137	TIGHT POSITIONAL	0.02	0.05
12	A	137	TIGHT THERMAL	0.03	0.5
12	C	137	TIGHT THERMAL	0.03	0.5
12	G	137	TIGHT THERMAL	0.02	0.5
12	E	137	TIGHT THERMAL	0.04	0.5
12	F	137	TIGHT THERMAL	0.02	0.5
12	H	137	TIGHT THERMAL	0.03	0.5
12	D	137	TIGHT THERMAL	0.02	0.5
12	B	137	TIGHT THERMAL	0.02	0.5

LS refinement shell

Resolution: 2.995→3.072 Å / Total num. of bins used: 20

	Rfactor	Num. reflection	% reflection
Rfree	0.402	133	-
Rwork	0.349	2647	-
all	-	2780	-
obs	-	-	83.01 %

Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

ID	L11 (°2)	L12 (°2)	L13 (°2)	L22 (°2)	L23 (°2)	L33 (°2)	S11 (Å °)	S12 (Å °)	S13 (Å °)	S21 (Å °)	S22 (Å °)	S23 (Å °)	S31 (Å °)	S32 (Å °)	S33 (Å °)	T11 (Å2)	T12 (Å2)	T13 (Å2)	T22 (Å2)	T23 (Å2)	T33 (Å2)	Origin x (Å)	Origin y (Å)	Origin z (Å)
1	4.2721	-1.0834	-0.3464	5.2599	-0.7527	17.0284	0.2226	0.1344	0.3326	-0.2123	-0.2177	0.4536	-0.0201	-0.2219	-0.005	-0.3687	-0.0036	-0.0552	-0.3246	-0.1517	-0.2174	29.5813	-45.8517	-30.562
2	3.3569	-2.1655	0.0406	10.8756	0.7804	11.0351	0.3524	0.4621	0.1546	-0.6442	-0.3797	-0.2232	0.1102	-0.0071	0.0273	-0.5338	-0.0356	0.0246	-0.2384	0.0415	-0.3188	32.7849	-49.23	-57.6537
3	4.5406	-5.3692	3.7281	18.6282	-7.1785	10.3674	0.7973	0.4503	-0.198	-1.2064	-0.9037	0.1345	1.9113	0.7877	0.1064	0.1364	0.2795	0.2422	-0.0836	0.1119	-0.1426	38.4473	-70.8589	-44.6171
4	3.5297	-3.5093	-1.4056	15.6266	1.1668	4.2942	-0.2041	-0.6388	0.0171	0.4301	0.1828	-0.1294	-0.3351	-0.0207	0.0212	-0.1796	0.0111	-0.0258	-0.2089	-0.0726	-0.3178	32.6412	8.4602	-78.7288
5	5.8878	-0.863	-0.3588	7.8191	2.3609	13.6058	0.2897	0.3639	-0.2944	-0.198	-0.207	-0.1327	0.5663	0.229	-0.0827	-0.3342	0.0621	-0.0875	-0.3441	0.0449	-0.2808	41.5965	-17.3239	-82.7858
6	1.9474	-3.3961	1.6941	6.4282	-0.8648	16.1556	-0.0996	-0.1265	0.1412	0.2298	0.1617	-0.2698	-0.2395	0.4494	-0.0621	-0.1039	-0.174	-0.0487	-0.3037	-0.0349	-0.2325	39.0903	-4.1077	-104.7253
7	11.1388	-5.591	-1.4353	13.9615	2.6012	2.2788	-0.0416	0.6829	0.1891	-0.363	0.3377	-0.021	-0.3503	-0.4213	-0.2961	-0.2711	-0.1725	0.0538	-0.2339	0.0953	-0.3158	18.3169	-24.2384	-3.3747
8	5.8586	-1.4029	0.1834	7.1161	-1.2595	11.2504	-0.3194	-0.0073	-0.2822	0.504	0.1147	-0.3155	0.5897	0.1843	0.2047	-0.2802	-0.0277	-0.0469	-0.4496	-0.1004	-0.3413	35.4475	-45.8089	-0.0097
9	6.3209	-2.0555	-2.7719	9.1545	2.3322	11.131	-0.0971	0.1018	0.1242	-0.4645	0.1023	0.6481	0.1077	-0.3328	-0.0052	-0.3363	-0.1036	-0.1236	-0.1641	-0.0587	-0.2856	23.4807	-39.8954	23.0362
10	5.9623	0.1622	1.6803	3.4221	1.0949	13.7302	0.1297	0.0284	-0.3315	-0.0386	-0.075	0.0071	0.4687	0.3273	-0.0547	-0.4926	-0.0142	0.0536	-0.3809	-0.0155	-0.3098	19.8739	32.3391	-54.6523
11	7.3589	-3.5769	0.69	11.1111	-0.9389	6.2157	0.5983	0.5901	-0.3198	-1.3207	-0.3743	0.5762	-0.1161	0.0849	-0.224	0.0363	0.3392	-0.0792	-0.1695	-0.1201	-0.4185	13.6819	33.1214	-81.5265
12	3.83	-4.143	-0.795	9.536	5.7872	9.5115	0.0884	-0.238	-0.1361	-0.2784	-0.0429	-0.3362	0.3856	1.1239	-0.0454	-0.1669	0.1219	-0.0109	-0.15	0.0318	-0.2486	9.7605	56.1738	-69.7381
13	11.1162	-9.8027	-2.0277	15.6254	-0.662	3.2496	-0.0057	0.6626	0.1417	-0.0746	0.0638	0.0652	-0.251	-0.1512	-0.0581	-0.1374	-0.0553	0.0511	-0.2179	-0.0073	-0.3289	31.6968	11.6294	-28.2461
14	7.0944	-3.3136	-1.8407	12.1418	0.6669	11.9739	-0.1423	-0.3073	0.3627	0.8408	0.158	-0.123	-0.097	-0.3925	-0.0157	-0.3523	-0.0064	-0.0063	-0.3954	0.0426	-0.2861	16.7392	34.1317	-23.9714
15	6.1453	-4.1695	5.8819	6.0081	-6.0417	15.232	-0.1939	-0.0722	0.2034	0.1866	-0.0024	-0.2133	-1.562	-0.1042	0.1963	0.2579	0.0842	0.1003	-0.1361	-0.0254	-0.366	27.6803	25.076	-1.9468
16	4.9809	1.5943	1.6161	1.2738	3.4362	26.9117	0.0953	0.2897	-0.096	-0.4438	-0.1153	0.0191	-0.051	0.4352	0.02	-0.0697	0.0741	0.0831	-0.2296	0.0408	-0.0896	5.7372	-0.715	-26.424
17	10.5603	-2.5563	1.1817	12.7858	2.4105	9.6804	-0.5397	-0.8876	0.3917	0.8177	0.3553	0.2106	-0.6718	-0.6243	0.1844	-0.0973	0.1366	0.1128	-0.2507	0.1631	-0.3623	7.0415	4.9801	0.222
18	6.9183	-5.2681	1.4676	13.3866	-2.3309	5.4932	-0.2221	-0.3066	-0.6259	0.6018	0.1493	0.6032	0.781	-0.3645	0.0728	-0.1257	-0.1099	-0.0571	-0.2856	-0.0232	-0.1855	-8.4719	21.6894	-11.7732
19	7.2374	-2.1302	-0.2546	13.198	-2.6279	6.0228	0.0374	-0.1835	-0.1883	0.4092	0.263	0.297	-0.0208	-0.2499	-0.3004	-0.386	-0.0052	-0.0249	-0.2567	-0.023	-0.3073	16.0057	-23.0567	-53.7569
20	7.2364	0.2063	-0.3822	6.2678	-3.3001	15.7802	0.4444	-0.2291	0.8905	0.2032	0.0101	0.1521	-2.1958	-0.4745	-0.4546	0.458	0.3944	0.5073	-0.2762	-0.0665	-0.0727	8.5147	3.3354	-57.4518
21	1.2315	-2.6646	-0.2457	7.551	3.5068	13.9888	-0.1851	-0.2223	-0.349	0.5078	0.3	0.0609	-0.2137	-0.8982	-0.1149	-0.0361	0.0491	0.2882	-0.1146	0.2235	-0.167	7.4889	-10.5965	-79.1561
22	4.7001	-1.5504	-1.2541	2.633	-2.0007	14.1031	0.0081	-0.0187	0.3877	-0.3306	-0.3279	-0.0968	-0.5957	-0.1908	0.3198	-0.4069	-0.0839	-0.0383	-0.4037	-0.0409	-0.1557	44.612	-12.43	-52.1215
23	4.6397	-2.5666	2.3403	8.9626	-0.5611	9.6218	-0.3872	-0.3956	0.1718	0.5819	0.4706	-0.1305	0.019	-0.013	-0.0833	-0.3717	-0.0952	-0.0052	-0.3996	-0.0916	-0.3635	42.1426	-17.8311	-24.9741
24	3.7541	-3.6863	-1.9081	8.1186	3.2814	9.3589	-0.3922	0.1292	0.2718	0.1612	0.3255	-0.4823	-0.8154	0.2853	0.0667	-0.3073	-0.0804	-0.0023	-0.4085	-0.0184	-0.1911	59.062	-34.2836	-36.5193

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	396 - 494
2	X-RAY DIFFRACTION	2	A	509 - 609
3	X-RAY DIFFRACTION	3	A	610 - 715
4	X-RAY DIFFRACTION	4	B	396 - 494
5	X-RAY DIFFRACTION	5	B	509 - 609
6	X-RAY DIFFRACTION	6	B	610 - 715
7	X-RAY DIFFRACTION	7	C	396 - 494
8	X-RAY DIFFRACTION	8	C	509 - 609
9	X-RAY DIFFRACTION	9	C	610 - 712
10	X-RAY DIFFRACTION	10	D	396 - 494
11	X-RAY DIFFRACTION	11	D	509 - 609
12	X-RAY DIFFRACTION	12	D	610 - 712
13	X-RAY DIFFRACTION	13	E	396 - 494
14	X-RAY DIFFRACTION	14	E	509 - 603
15	X-RAY DIFFRACTION	15	E	613 - 715
16	X-RAY DIFFRACTION	16	F	396 - 494
17	X-RAY DIFFRACTION	17	F	509 - 609
18	X-RAY DIFFRACTION	18	F	610 - 715
19	X-RAY DIFFRACTION	19	G	396 - 494
20	X-RAY DIFFRACTION	20	G	509 - 609
21	X-RAY DIFFRACTION	21	G	610 - 715
22	X-RAY DIFFRACTION	22	H	396 - 494
23	X-RAY DIFFRACTION	23	H	509 - 609
24	X-RAY DIFFRACTION	24	H	610 - 715