PDB-6txc: Crystal structure of tetrameric human wt-SAMHD1 (residues 109-626...

Basic information

• Entry: Database: PDB / ID: 6txc
• Title: Crystal structure of tetrameric human wt-SAMHD1 (residues 109-626) with GTP, dATP, dCMPNPP and Mg
• Components: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1
• Keywords: HYDROLASE / triphosphohydrolase / metallo-enzyme / binuclear / HD

Function / homology

Function:

Nucleotide catabolism / Hydrolases; Acting on ester bonds; Triphosphoric-monoester hydrolases / deoxynucleoside triphosphate hydrolase activity / triphosphoric monoester hydrolase activity / dGTP binding / dATP catabolic process / dGTPase activity / tetraspanin-enriched microdomain / DNA strand resection involved in replication fork processing / deoxyribonucleotide catabolic process / dGTP catabolic process / negative regulation of type I interferon-mediated signaling pathway / regulation of innate immune response / somatic hypermutation of immunoglobulin genes / RNA nuclease activity / double-strand break repair via homologous recombination / Interferon alpha/beta signaling / site of double-strand break / single-stranded DNA binding / protein homotetramerization / defense response to virus / nucleic acid binding / immune response / innate immune response / DNA damage response / GTP binding / RNA binding / zinc ion binding / nucleoplasm / identical protein binding / nucleus / plasma membrane

Domain/homology:

HD domain profile. / HD domain / HD domain / SAM domain (Sterile alpha motif) / SAM domain profile. / Metal dependent phosphohydrolases with conserved 'HD' motif. / Sterile alpha motif. / HD/PDEase domain / Sterile alpha motif domain / Sterile alpha motif/pointed domain superfamily

Component:

Chem-0KX / 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE / : / GUANOSINE-5'-TRIPHOSPHATE / Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

• Biological species: Homo sapiens (human)
• Method: X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.84 Å
• Authors: Morris, E.R. / Kunzelmann, S. / Caswell, S.J. / Arnold, L.H. / Purkiss, A. / Kelly, G. / Taylor, I.A.

Funding support

United Kingdom, 4items

Organization	Grant number	Country
Wellcome Trust	108014/Z/15/Z	United Kingdom
Wellcome Trust	FC001178	United Kingdom
Medical Research Council (MRC, United Kingdom)	FC001178	United Kingdom
Cancer Research UK	FC001178	United Kingdom

• Citation: Journal: Nat Commun / Year: 2020; Title: Crystal structures of SAMHD1 inhibitor complexes reveal the mechanism of water-mediated dNTP hydrolysis.; Authors: Morris, E.R. / Caswell, S.J. / Kunzelmann, S. / Arnold, L.H. / Purkiss, A.G. / Kelly, G. / Taylor, I.A.

History

Deposition	Jan 14, 2020	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Jun 24, 2020	Provider: repository / Type: Initial release
Revision 1.1	Jul 8, 2020	Group: Database references / Category: citation / citation_author Item: _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2	Jan 24, 2024	Group: Data collection / Database references / Derived calculations / Other / Refinement description Category: chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _pdbx_database_status.status_code_sf / _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_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_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_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_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

Assembly

Deposited unit

A: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

B: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

C: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

D: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

E: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

F: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

G: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

H: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

I: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

J: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

K: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

L: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

M: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

N: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

O: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

P: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

hetero molecules

Summary:

• 990 kDa, 16 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	989,808	131
Polymers	963,341	16
Non-polymers	26,467	115
Water	0	0

1

A: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

B: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

C: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

D: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

hetero molecules

Summary:

• defined by author&software
• Evidence: assay for oligomerization, SEC-MALLS and AUC experiments demonstrate the HD domain crystallised here assembles into a homotetramer in the presence of GTP, dATP, dCMPNPP and Mg2+.
• 248 kDa, 4 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	247,657	36
Polymers	240,835	4
Non-polymers	6,821	32
Water	0

Symmetry operations:

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

Calculated values:

Buried area	26950 Å2
ΔGint	-170 kcal/mol
Surface area	66470 Å2
Method	PISA

2

E: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

F: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

G: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

H: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

hetero molecules

Summary:

• defined by author&software
• 247 kDa, 4 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	247,296	30
Polymers	240,835	4
Non-polymers	6,460	26
Water	0

Symmetry operations:

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

Calculated values:

Buried area	25490 Å2
ΔGint	-97 kcal/mol
Surface area	64610 Å2
Method	PISA

3

I: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

J: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

K: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

L: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

hetero molecules

Summary:

• defined by author&software
• 248 kDa, 4 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	247,536	34
Polymers	240,835	4
Non-polymers	6,701	30
Water	0

Symmetry operations:

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

Calculated values:

Buried area	26530 Å2
ΔGint	-152 kcal/mol
Surface area	65100 Å2
Method	PISA

4

M: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

N: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

O: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

P: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

hetero molecules

Summary:

• defined by author&software
• 247 kDa, 4 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	247,320	31
Polymers	240,835	4
Non-polymers	6,485	27
Water	0

Symmetry operations:

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

Calculated values:

Buried area	25250 Å2
ΔGint	-122 kcal/mol
Surface area	63760 Å2
Method	PISA

Unit cell

Length a, b, c (Å)	99.113, 175.239, 277.269
Angle α, β, γ (deg.)	90.000, 94.810, 90.000
Int Tables number	4
Space group name H-M	P1211

Noncrystallographic symmetry (NCS)

NCS domain:

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

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	THR	THR	TRP	TRP	A	A	114 - 598	8 - 492
2	1	THR	THR	TRP	TRP	B	B	114 - 598	8 - 492
1	2	THR	THR	TRP	TRP	A	A	114 - 598	8 - 492
2	2	THR	THR	TRP	TRP	C	C	114 - 598	8 - 492
1	3	THR	THR	ASN	ASN	A	A	114 - 599	8 - 493
2	3	THR	THR	ASN	ASN	D	D	114 - 599	8 - 493
1	4	THR	THR	TRP	TRP	A	A	114 - 598	8 - 492
2	4	THR	THR	TRP	TRP	E	E	114 - 598	8 - 492
1	5	THR	THR	PRO	PRO	A	A	114 - 593	8 - 487
2	5	THR	THR	PRO	PRO	F	F	114 - 593	8 - 487
1	6	MET	MET	PRO	PRO	A	A	115 - 593	9 - 487
2	6	MET	MET	PRO	PRO	G	G	115 - 593	9 - 487
1	7	THR	THR	TRP	TRP	A	A	114 - 598	8 - 492
2	7	THR	THR	TRP	TRP	H	H	114 - 598	8 - 492
1	8	MET	MET	TRP	TRP	A	A	115 - 598	9 - 492
2	8	MET	MET	TRP	TRP	I	I	115 - 598	9 - 492
1	9	ASP	ASP	GLU	GLU	A	A	113 - 597	7 - 491
2	9	ASP	ASP	GLU	GLU	J	J	113 - 597	7 - 491
1	10	ASP	ASP	TRP	TRP	A	A	113 - 598	7 - 492
2	10	ASP	ASP	TRP	TRP	K	K	113 - 598	7 - 492
1	11	LYS	LYS	GLU	GLU	A	A	116 - 597	10 - 491
2	11	LYS	LYS	GLU	GLU	L	L	116 - 597	10 - 491
1	12	MET	MET	TRP	TRP	A	A	115 - 598	9 - 492
2	12	MET	MET	TRP	TRP	M	M	115 - 598	9 - 492
1	13	MET	MET	ASN	ASN	A	A	115 - 599	9 - 493
2	13	MET	MET	ASN	ASN	N	N	115 - 599	9 - 493
1	14	MET	MET	PRO	PRO	A	A	115 - 593	9 - 487
2	14	MET	MET	PRO	PRO	O	O	115 - 593	9 - 487
1	15	THR	THR	PRO	PRO	A	A	114 - 593	8 - 487
2	15	THR	THR	PRO	PRO	P	P	114 - 593	8 - 487
1	16	THR	THR	ASN	ASN	B	B	114 - 599	8 - 493
2	16	THR	THR	ASN	ASN	C	C	114 - 599	8 - 493
1	17	THR	THR	ASN	ASN	B	B	114 - 599	8 - 493
2	17	THR	THR	ASN	ASN	D	D	114 - 599	8 - 493
1	18	THR	THR	ASN	ASN	B	B	114 - 599	8 - 493
2	18	THR	THR	ASN	ASN	E	E	114 - 599	8 - 493
1	19	THR	THR	PRO	PRO	B	B	114 - 593	8 - 487
2	19	THR	THR	PRO	PRO	F	F	114 - 593	8 - 487
1	20	MET	MET	PRO	PRO	B	B	115 - 593	9 - 487
2	20	MET	MET	PRO	PRO	G	G	115 - 593	9 - 487
1	21	THR	THR	ASN	ASN	B	B	114 - 599	8 - 493
2	21	THR	THR	ASN	ASN	H	H	114 - 599	8 - 493
1	22	MET	MET	TRP	TRP	B	B	115 - 598	9 - 492
2	22	MET	MET	TRP	TRP	I	I	115 - 598	9 - 492
1	23	THR	THR	GLU	GLU	B	B	114 - 597	8 - 491
2	23	THR	THR	GLU	GLU	J	J	114 - 597	8 - 491
1	24	THR	THR	ASN	ASN	B	B	114 - 599	8 - 493
2	24	THR	THR	ASN	ASN	K	K	114 - 599	8 - 493
1	25	LYS	LYS	GLU	GLU	B	B	116 - 597	10 - 491
2	25	LYS	LYS	GLU	GLU	L	L	116 - 597	10 - 491
1	26	MET	MET	TRP	TRP	B	B	115 - 598	9 - 492
2	26	MET	MET	TRP	TRP	M	M	115 - 598	9 - 492
1	27	MET	MET	ASN	ASN	B	B	115 - 599	9 - 493
2	27	MET	MET	ASN	ASN	N	N	115 - 599	9 - 493
1	28	MET	MET	PRO	PRO	B	B	115 - 593	9 - 487
2	28	MET	MET	PRO	PRO	O	O	115 - 593	9 - 487
1	29	THR	THR	PRO	PRO	B	B	114 - 593	8 - 487
2	29	THR	THR	PRO	PRO	P	P	114 - 593	8 - 487
1	30	THR	THR	ASN	ASN	C	C	114 - 599	8 - 493
2	30	THR	THR	ASN	ASN	D	D	114 - 599	8 - 493
1	31	THR	THR	ASN	ASN	C	C	114 - 599	8 - 493
2	31	THR	THR	ASN	ASN	E	E	114 - 599	8 - 493
1	32	THR	THR	PRO	PRO	C	C	114 - 593	8 - 487
2	32	THR	THR	PRO	PRO	F	F	114 - 593	8 - 487
1	33	MET	MET	PRO	PRO	C	C	115 - 593	9 - 487
2	33	MET	MET	PRO	PRO	G	G	115 - 593	9 - 487
1	34	THR	THR	ASN	ASN	C	C	114 - 599	8 - 493
2	34	THR	THR	ASN	ASN	H	H	114 - 599	8 - 493
1	35	MET	MET	ASN	ASN	C	C	115 - 599	9 - 493
2	35	MET	MET	ASN	ASN	I	I	115 - 599	9 - 493
1	36	THR	THR	GLU	GLU	C	C	114 - 597	8 - 491
2	36	THR	THR	GLU	GLU	J	J	114 - 597	8 - 491
1	37	THR	THR	ASN	ASN	C	C	114 - 599	8 - 493
2	37	THR	THR	ASN	ASN	K	K	114 - 599	8 - 493
1	38	LYS	LYS	GLU	GLU	C	C	116 - 597	10 - 491
2	38	LYS	LYS	GLU	GLU	L	L	116 - 597	10 - 491
1	39	MET	MET	TRP	TRP	C	C	115 - 598	9 - 492
2	39	MET	MET	TRP	TRP	M	M	115 - 598	9 - 492
1	40	MET	MET	ASN	ASN	C	C	115 - 599	9 - 493
2	40	MET	MET	ASN	ASN	N	N	115 - 599	9 - 493
1	41	MET	MET	PRO	PRO	C	C	115 - 593	9 - 487
2	41	MET	MET	PRO	PRO	O	O	115 - 593	9 - 487
1	42	THR	THR	PRO	PRO	C	C	114 - 593	8 - 487
2	42	THR	THR	PRO	PRO	P	P	114 - 593	8 - 487
1	43	THR	THR	ASN	ASN	D	D	114 - 599	8 - 493
2	43	THR	THR	ASN	ASN	E	E	114 - 599	8 - 493
1	44	THR	THR	PRO	PRO	D	D	114 - 593	8 - 487
2	44	THR	THR	PRO	PRO	F	F	114 - 593	8 - 487
1	45	MET	MET	PRO	PRO	D	D	115 - 593	9 - 487
2	45	MET	MET	PRO	PRO	G	G	115 - 593	9 - 487
1	46	THR	THR	ASN	ASN	D	D	114 - 599	8 - 493
2	46	THR	THR	ASN	ASN	H	H	114 - 599	8 - 493
1	47	MET	MET	ASN	ASN	D	D	115 - 599	9 - 493
2	47	MET	MET	ASN	ASN	I	I	115 - 599	9 - 493
1	48	THR	THR	TRP	TRP	D	D	114 - 598	8 - 492
2	48	THR	THR	TRP	TRP	J	J	114 - 598	8 - 492
1	49	THR	THR	ASN	ASN	D	D	114 - 599	8 - 493
2	49	THR	THR	ASN	ASN	K	K	114 - 599	8 - 493
1	50	LYS	LYS	TRP	TRP	D	D	116 - 598	10 - 492
2	50	LYS	LYS	TRP	TRP	L	L	116 - 598	10 - 492
1	51	MET	MET	TRP	TRP	D	D	115 - 598	9 - 492
2	51	MET	MET	TRP	TRP	M	M	115 - 598	9 - 492
1	52	MET	MET	ASN	ASN	D	D	115 - 599	9 - 493
2	52	MET	MET	ASN	ASN	N	N	115 - 599	9 - 493
1	53	MET	MET	PRO	PRO	D	D	115 - 593	9 - 487
2	53	MET	MET	PRO	PRO	O	O	115 - 593	9 - 487
1	54	THR	THR	PRO	PRO	D	D	114 - 593	8 - 487
2	54	THR	THR	PRO	PRO	P	P	114 - 593	8 - 487
1	55	THR	THR	PRO	PRO	E	E	114 - 593	8 - 487
2	55	THR	THR	PRO	PRO	F	F	114 - 593	8 - 487
1	56	MET	MET	PRO	PRO	E	E	115 - 593	9 - 487
2	56	MET	MET	PRO	PRO	G	G	115 - 593	9 - 487
1	57	THR	THR	ASN	ASN	E	E	114 - 599	8 - 493
2	57	THR	THR	ASN	ASN	H	H	114 - 599	8 - 493
1	58	MET	MET	TRP	TRP	E	E	115 - 598	9 - 492
2	58	MET	MET	TRP	TRP	I	I	115 - 598	9 - 492
1	59	THR	THR	GLU	GLU	E	E	114 - 597	8 - 491
2	59	THR	THR	GLU	GLU	J	J	114 - 597	8 - 491
1	60	THR	THR	ASN	ASN	E	E	114 - 599	8 - 493
2	60	THR	THR	ASN	ASN	K	K	114 - 599	8 - 493
1	61	LYS	LYS	GLU	GLU	E	E	116 - 597	10 - 491
2	61	LYS	LYS	GLU	GLU	L	L	116 - 597	10 - 491
1	62	MET	MET	TRP	TRP	E	E	115 - 598	9 - 492
2	62	MET	MET	TRP	TRP	M	M	115 - 598	9 - 492
1	63	MET	MET	ASN	ASN	E	E	115 - 599	9 - 493
2	63	MET	MET	ASN	ASN	N	N	115 - 599	9 - 493
1	64	MET	MET	PRO	PRO	E	E	115 - 593	9 - 487
2	64	MET	MET	PRO	PRO	O	O	115 - 593	9 - 487
1	65	THR	THR	PRO	PRO	E	E	114 - 593	8 - 487
2	65	THR	THR	PRO	PRO	P	P	114 - 593	8 - 487
1	66	MET	MET	PRO	PRO	F	F	115 - 593	9 - 487
2	66	MET	MET	PRO	PRO	G	G	115 - 593	9 - 487
1	67	THR	THR	PRO	PRO	F	F	114 - 593	8 - 487
2	67	THR	THR	PRO	PRO	H	H	114 - 593	8 - 487
1	68	MET	MET	PRO	PRO	F	F	115 - 593	9 - 487
2	68	MET	MET	PRO	PRO	I	I	115 - 593	9 - 487
1	69	THR	THR	PRO	PRO	F	F	114 - 593	8 - 487
2	69	THR	THR	PRO	PRO	J	J	114 - 593	8 - 487
1	70	THR	THR	PRO	PRO	F	F	114 - 593	8 - 487
2	70	THR	THR	PRO	PRO	K	K	114 - 593	8 - 487
1	71	LYS	LYS	PRO	PRO	F	F	116 - 593	10 - 487
2	71	LYS	LYS	PRO	PRO	L	L	116 - 593	10 - 487
1	72	MET	MET	PRO	PRO	F	F	115 - 593	9 - 487
2	72	MET	MET	PRO	PRO	M	M	115 - 593	9 - 487
1	73	MET	MET	PRO	PRO	F	F	115 - 593	9 - 487
2	73	MET	MET	PRO	PRO	N	N	115 - 593	9 - 487
1	74	MET	MET	PRO	PRO	F	F	115 - 593	9 - 487
2	74	MET	MET	PRO	PRO	O	O	115 - 593	9 - 487
1	75	THR	THR	PRO	PRO	F	F	114 - 593	8 - 487
2	75	THR	THR	PRO	PRO	P	P	114 - 593	8 - 487
1	76	MET	MET	PRO	PRO	G	G	115 - 593	9 - 487
2	76	MET	MET	PRO	PRO	H	H	115 - 593	9 - 487
1	77	MET	MET	PRO	PRO	G	G	115 - 593	9 - 487
2	77	MET	MET	PRO	PRO	I	I	115 - 593	9 - 487
1	78	MET	MET	PRO	PRO	G	G	115 - 593	9 - 487
2	78	MET	MET	PRO	PRO	J	J	115 - 593	9 - 487
1	79	MET	MET	PRO	PRO	G	G	115 - 593	9 - 487
2	79	MET	MET	PRO	PRO	K	K	115 - 593	9 - 487
1	80	LYS	LYS	PRO	PRO	G	G	116 - 593	10 - 487
2	80	LYS	LYS	PRO	PRO	L	L	116 - 593	10 - 487
1	81	MET	MET	PRO	PRO	G	G	115 - 593	9 - 487
2	81	MET	MET	PRO	PRO	M	M	115 - 593	9 - 487
1	82	MET	MET	PRO	PRO	G	G	115 - 593	9 - 487
2	82	MET	MET	PRO	PRO	N	N	115 - 593	9 - 487
1	83	MET	MET	PRO	PRO	G	G	115 - 593	9 - 487
2	83	MET	MET	PRO	PRO	O	O	115 - 593	9 - 487
1	84	MET	MET	PRO	PRO	G	G	115 - 593	9 - 487
2	84	MET	MET	PRO	PRO	P	P	115 - 593	9 - 487
1	85	MET	MET	TRP	TRP	H	H	115 - 598	9 - 492
2	85	MET	MET	TRP	TRP	I	I	115 - 598	9 - 492
1	86	THR	THR	GLU	GLU	H	H	114 - 597	8 - 491
2	86	THR	THR	GLU	GLU	J	J	114 - 597	8 - 491
1	87	THR	THR	ASN	ASN	H	H	114 - 599	8 - 493
2	87	THR	THR	ASN	ASN	K	K	114 - 599	8 - 493
1	88	LYS	LYS	GLU	GLU	H	H	116 - 597	10 - 491
2	88	LYS	LYS	GLU	GLU	L	L	116 - 597	10 - 491
1	89	MET	MET	TRP	TRP	H	H	115 - 598	9 - 492
2	89	MET	MET	TRP	TRP	M	M	115 - 598	9 - 492
1	90	MET	MET	ASN	ASN	H	H	115 - 599	9 - 493
2	90	MET	MET	ASN	ASN	N	N	115 - 599	9 - 493
1	91	MET	MET	PRO	PRO	H	H	115 - 593	9 - 487
2	91	MET	MET	PRO	PRO	O	O	115 - 593	9 - 487
1	92	THR	THR	PRO	PRO	H	H	114 - 593	8 - 487
2	92	THR	THR	PRO	PRO	P	P	114 - 593	8 - 487
1	93	MET	MET	GLU	GLU	I	I	115 - 597	9 - 491
2	93	MET	MET	GLU	GLU	J	J	115 - 597	9 - 491
1	94	MET	MET	TRP	TRP	I	I	115 - 598	9 - 492
2	94	MET	MET	TRP	TRP	K	K	115 - 598	9 - 492
1	95	LYS	LYS	GLU	GLU	I	I	116 - 597	10 - 491
2	95	LYS	LYS	GLU	GLU	L	L	116 - 597	10 - 491
1	96	MET	MET	TRP	TRP	I	I	115 - 598	9 - 492
2	96	MET	MET	TRP	TRP	M	M	115 - 598	9 - 492
1	97	MET	MET	ASN	ASN	I	I	115 - 599	9 - 493
2	97	MET	MET	ASN	ASN	N	N	115 - 599	9 - 493
1	98	MET	MET	PRO	PRO	I	I	115 - 593	9 - 487
2	98	MET	MET	PRO	PRO	O	O	115 - 593	9 - 487
1	99	MET	MET	PRO	PRO	I	I	115 - 593	9 - 487
2	99	MET	MET	PRO	PRO	P	P	115 - 593	9 - 487
1	100	ASP	ASP	GLU	GLU	J	J	113 - 597	7 - 491
2	100	ASP	ASP	GLU	GLU	K	K	113 - 597	7 - 491
1	101	LYS	LYS	GLU	GLU	J	J	116 - 597	10 - 491
2	101	LYS	LYS	GLU	GLU	L	L	116 - 597	10 - 491
1	102	MET	MET	TRP	TRP	J	J	115 - 598	9 - 492
2	102	MET	MET	TRP	TRP	M	M	115 - 598	9 - 492
1	103	MET	MET	TRP	TRP	J	J	115 - 598	9 - 492
2	103	MET	MET	TRP	TRP	N	N	115 - 598	9 - 492
1	104	MET	MET	PRO	PRO	J	J	115 - 593	9 - 487
2	104	MET	MET	PRO	PRO	O	O	115 - 593	9 - 487
1	105	THR	THR	PRO	PRO	J	J	114 - 593	8 - 487
2	105	THR	THR	PRO	PRO	P	P	114 - 593	8 - 487
1	106	LYS	LYS	GLU	GLU	K	K	116 - 597	10 - 491
2	106	LYS	LYS	GLU	GLU	L	L	116 - 597	10 - 491
1	107	MET	MET	TRP	TRP	K	K	115 - 598	9 - 492
2	107	MET	MET	TRP	TRP	M	M	115 - 598	9 - 492
1	108	MET	MET	ASN	ASN	K	K	115 - 599	9 - 493
2	108	MET	MET	ASN	ASN	N	N	115 - 599	9 - 493
1	109	MET	MET	PRO	PRO	K	K	115 - 593	9 - 487
2	109	MET	MET	PRO	PRO	O	O	115 - 593	9 - 487
1	110	THR	THR	PRO	PRO	K	K	114 - 593	8 - 487
2	110	THR	THR	PRO	PRO	P	P	114 - 593	8 - 487
1	111	LYS	LYS	TRP	TRP	L	L	116 - 598	10 - 492
2	111	LYS	LYS	TRP	TRP	M	M	116 - 598	10 - 492
1	112	LYS	LYS	TRP	TRP	L	L	116 - 598	10 - 492
2	112	LYS	LYS	TRP	TRP	N	N	116 - 598	10 - 492
1	113	LYS	LYS	PRO	PRO	L	L	116 - 593	10 - 487
2	113	LYS	LYS	PRO	PRO	O	O	116 - 593	10 - 487
1	114	LYS	LYS	PRO	PRO	L	L	116 - 593	10 - 487
2	114	LYS	LYS	PRO	PRO	P	P	116 - 593	10 - 487
1	115	MET	MET	TRP	TRP	M	M	115 - 598	9 - 492
2	115	MET	MET	TRP	TRP	N	N	115 - 598	9 - 492
1	116	MET	MET	PRO	PRO	M	M	115 - 593	9 - 487
2	116	MET	MET	PRO	PRO	O	O	115 - 593	9 - 487
1	117	MET	MET	PRO	PRO	M	M	115 - 593	9 - 487
2	117	MET	MET	PRO	PRO	P	P	115 - 593	9 - 487
1	118	MET	MET	PRO	PRO	N	N	115 - 593	9 - 487
2	118	MET	MET	PRO	PRO	O	O	115 - 593	9 - 487
1	119	MET	MET	PRO	PRO	N	N	115 - 593	9 - 487
2	119	MET	MET	PRO	PRO	P	P	115 - 593	9 - 487
1	120	MET	MET	PRO	PRO	O	O	115 - 593	9 - 487
2	120	MET	MET	PRO	PRO	P	P	115 - 593	9 - 487

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

Components

Protein , 1 types, 16 molecules A B C D E F G H I J K L M N O P

#1: Protein

A B C D E F G H I J K L M N O P
Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 / dNTPase / Dendritic cell-derived IFNG-induced protein / DCIP / Monocyte protein 5 / MOP-5 / SAM domain and HD domain-containing protein 1 / hSAMHD1

Details:

Mass: 60208.809 Da / Num. of mol.: 16
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SAMHD1, MOP5 / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Rosetta2
References: UniProt: Q9Y3Z3, Hydrolases; Acting on ester bonds; Triphosphoric-monoester hydrolases

Non-polymers , 6 types, 115 molecules

#2: Chemical

A-701 B-701 C-702 D-702 E-701 F-701 G-702 H-702 I-701 J-701 K-702 L-702 M-701 N-701 O-702 P-702
ChemComp-FE / FE (III) ION

Details:

Mass: 55.845 Da / Num. of mol.: 16 / Source method: obtained synthetically / Formula: Fe / Feature type: SUBJECT OF INVESTIGATION

#3: Chemical

A-702 A-703 A-704 B-702 B-703 B-704 C-703 C-704 C-705 D-703 D-704 D-705 E-702 E-703 F-702 F-703 G-703 G-704 G-705 H-703 ...
ChemComp-MG / MAGNESIUM ION

Details:

Mass: 24.305 Da / Num. of mol.: 42 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION

#4: Chemical

A-705 B-705 C-706 D-706 E-704 F-704 G-706 H-705 I-705 J-704 K-706 L-706 M-705 N-704 O-705 P-706
ChemComp-0KX / 2'-deoxy-5'-O-[(R)-hydroxy{[(R)-hydroxy(phosphonooxy)phosphoryl]amino}phosphoryl]cytidine

Details:

Mass: 466.172 Da / Num. of mol.: 16 / Source method: obtained synthetically / Formula: C₉H₁₇N₄O₁₂P₃ / Feature type: SUBJECT OF INVESTIGATION

#5: Chemical

A-706 B-706 C-707 D-707 E-705 F-705 G-707 H-706 I-706 J-705 K-707 L-707 M-706 N-705 O-706 O-707
ChemComp-GTP / GUANOSINE-5'-TRIPHOSPHATE

Details:

Mass: 523.180 Da / Num. of mol.: 16 / Source method: obtained synthetically / Formula: C₁₀H₁₆N₅O₁₄P₃ / Feature type: SUBJECT OF INVESTIGATION / Comment: GTP, energy-carrying molecule*YM

#6: Chemical

A-707 B-707 C-708 D-708 H-707 I-707 J-706 L-708 M-707
ChemComp-SO4 / SULFATE ION

Details:

Mass: 96.063 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: SO₄

#7: Chemical

A-708 B-708 C-701 D-701 E-706 F-706 G-701 H-701 I-708 J-707 K-701 L-701 M-708 N-706 O-701 P-701
ChemComp-DTP / 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE

Details:

Mass: 491.182 Da / Num. of mol.: 16 / Source method: obtained synthetically / Formula: C₁₀H₁₆N₅O₁₂P₃ / Feature type: SUBJECT OF INVESTIGATION

Details

• Has ligand of interest: Y

Experimental details

Experiment

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

Sample preparation

• Crystal: Density Matthews: 2.49 ų/Da / Density % sol: 50.72 %
• Crystal grow: Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6 ; Details: 0.1 M Bistris methane-HCL pH 6, 17% (w/v) PEG 3350, 0.15 M Li2SO4.

Data collection

• Diffraction: Mean temperature: 100 K / Serial crystal experiment: N
• Diffraction source: Source: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.97625 Å
• Detector: Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Feb 15, 2017
• Radiation: Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
• Radiation wavelength: Wavelength: 0.97625 Å / Relative weight: 1
• Reflection: Resolution: 2.84→276.291 Å / Num. obs: 161935 / % possible obs: 93.7 % / Redundancy: 3.9 % / B_iso Wilson estimate: 46.2 Ų / CC_1/2: 0.991 / R_merge(I) obs: 0.169 / R_pim(I) all: 0.097 / R_rim(I) all: 0.195 / Net I/σ(I): 7.1

Reflection shell

Diffraction-ID: 1

Resolution (Å)	Redundancy (%)	Rmerge(I) obs	Mean I/σ(I) obs	Num. unique obs	CC1/2	Rpim(I) all	Rrim(I) all	% possible all
2.84-3.1	4.1	0.885	1.5	8099	0.595	0.494	1.016	53.8
8.612-276.291	3.7	0.035	23.9	8097	0.998	0.021	0.041	99.1

Phasing

• Phasing: Method: molecular replacement

Phasing MR

Model details: Phaser MODE: MR_AUTO

	Highest resolution	Lowest resolution
Rotation	9.57 Å	274.75 Å
Translation	9.57 Å	274.75 Å

Processing

Software

Name	Version	Classification
REFMAC	5.8.0158	refinement
XDS		data reduction
Aimless	0.7.4	data scaling
STARANISO		data scaling
PHASER	2.7.17	phasing
PDB_EXTRACT	3.25	data extraction

Refinement

Method to determine structure: MOLECULAR REPLACEMENT
Starting model: 6TXA

6txa

Resolution: 2.84→276.291 Å / Cor.coef. F_o:F_c: 0.852 / Cor.coef. F_o:F_c free: 0.752 / SU B: 55.441 / SU ML: 0.415 / SU R Cruickshank DPI: 0.5141 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.508
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED

	Rfactor	Num. reflection	% reflection	Selection details
Rfree	0.2489	8049	5 %	RANDOM
Rwork	0.228	-	-	-
obs	0.229	153495	72.74 %	-

• Solvent computation: Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å

Displacement parameters

B_iso max: 150.88 Ų / B_iso mean: 52.052 Ų / B_iso min: 13 Ų

	Baniso -1	Baniso -2	Baniso -3
1-	-1.92 Å2	0 Å2	-1.44 Å2
2-	-	0.47 Å2	-0 Å2
3-	-	-	1.67 Å2

Refinement step

Cycle: final / Resolution: 2.84→276.291 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	60407	0	1543	0	61950
Biso mean	-	-	37.35	-	-
Num. residues	-	-	-	-	7585

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.013	0.019	63430
X-RAY DIFFRACTION	r_bond_other_d	0.002	0.02	56514
X-RAY DIFFRACTION	r_angle_refined_deg	1.702	1.971	86369
X-RAY DIFFRACTION	r_angle_other_deg	0.993	2.996	130797
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.581	5	7549
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	35.955	23.982	3061
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	15.57	15	10215
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	15.357	15	388
X-RAY DIFFRACTION	r_chiral_restr	0.087	0.2	9303
X-RAY DIFFRACTION	r_gen_planes_refined	0.007	0.021	69930
X-RAY DIFFRACTION	r_gen_planes_other	0.002	0.02	13186

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	A	31646	0.04
1	2	B	31646	0.04
2	1	A	31722	0.04
2	2	C	31722	0.04
3	1	A	31664	0.04
3	2	D	31664	0.04
4	1	A	31424	0.04
4	2	E	31424	0.04
5	1	A	30762	0.03
5	2	F	30762	0.03
6	1	A	30786	0.03
6	2	G	30786	0.03
7	1	A	31656	0.04
7	2	H	31656	0.04
8	1	A	31554	0.04
8	2	I	31554	0.04
9	1	A	31530	0.04
9	2	J	31530	0.04
10	1	A	31744	0.03
10	2	K	31744	0.03
11	1	A	31126	0.04
11	2	L	31126	0.04
12	1	A	30826	0.04
12	2	M	30826	0.04
13	1	A	31340	0.04
13	2	N	31340	0.04
14	1	A	30354	0.05
14	2	O	30354	0.05
15	1	A	30376	0.03
15	2	P	30376	0.03
16	1	B	31742	0.04
16	2	C	31742	0.04
17	1	B	31548	0.04
17	2	D	31548	0.04
18	1	B	31592	0.04
18	2	E	31592	0.04
19	1	B	30682	0.04
19	2	F	30682	0.04
20	1	B	30694	0.03
20	2	G	30694	0.03
21	1	B	31672	0.04
21	2	H	31672	0.04
22	1	B	31500	0.04
22	2	I	31500	0.04
23	1	B	31474	0.04
23	2	J	31474	0.04
24	1	B	31584	0.04
24	2	K	31584	0.04
25	1	B	31058	0.04
25	2	L	31058	0.04
26	1	B	30746	0.04
26	2	M	30746	0.04
27	1	B	31246	0.03
27	2	N	31246	0.03
28	1	B	30370	0.04
28	2	O	30370	0.04
29	1	B	30276	0.03
29	2	P	30276	0.03
30	1	C	31846	0.04
30	2	D	31846	0.04
31	1	C	31612	0.04
31	2	E	31612	0.04
32	1	C	30690	0.04
32	2	F	30690	0.04
33	1	C	30666	0.04
33	2	G	30666	0.04
34	1	C	31862	0.03
34	2	H	31862	0.03
35	1	C	31736	0.04
35	2	I	31736	0.04
36	1	C	31558	0.04
36	2	J	31558	0.04
37	1	C	31860	0.03
37	2	K	31860	0.03
38	1	C	31190	0.04
38	2	L	31190	0.04
39	1	C	30902	0.03
39	2	M	30902	0.03
40	1	C	31316	0.03
40	2	N	31316	0.03
41	1	C	30426	0.04
41	2	O	30426	0.04
42	1	C	30230	0.04
42	2	P	30230	0.04
43	1	D	31478	0.04
43	2	E	31478	0.04
44	1	D	30638	0.04
44	2	F	30638	0.04
45	1	D	30710	0.03
45	2	G	30710	0.03
46	1	D	31754	0.03
46	2	H	31754	0.03
47	1	D	31718	0.03
47	2	I	31718	0.03
48	1	D	31862	0.02
48	2	J	31862	0.02
49	1	D	31666	0.04
49	2	K	31666	0.04
50	1	D	31384	0.03
50	2	L	31384	0.03
51	1	D	30844	0.04
51	2	M	30844	0.04
52	1	D	31246	0.03
52	2	N	31246	0.03
53	1	D	30352	0.05
53	2	O	30352	0.05
54	1	D	30168	0.04
54	2	P	30168	0.04
55	1	E	30584	0.04
55	2	F	30584	0.04
56	1	E	30590	0.04
56	2	G	30590	0.04
57	1	E	31580	0.03
57	2	H	31580	0.03
58	1	E	31408	0.03
58	2	I	31408	0.03
59	1	E	31384	0.04
59	2	J	31384	0.04
60	1	E	31486	0.04
60	2	K	31486	0.04
61	1	E	31112	0.04
61	2	L	31112	0.04
62	1	E	30794	0.04
62	2	M	30794	0.04
63	1	E	31230	0.03
63	2	N	31230	0.03
64	1	E	30480	0.03
64	2	O	30480	0.03
65	1	E	30234	0.04
65	2	P	30234	0.04
66	1	F	30520	0.04
66	2	G	30520	0.04
67	1	F	30620	0.04
67	2	H	30620	0.04
68	1	F	30588	0.04
68	2	I	30588	0.04
69	1	F	30694	0.04
69	2	J	30694	0.04
70	1	F	30748	0.03
70	2	K	30748	0.03
71	1	F	30484	0.04
71	2	L	30484	0.04
72	1	F	29978	0.04
72	2	M	29978	0.04
73	1	F	30336	0.04
73	2	N	30336	0.04
74	1	F	30188	0.05
74	2	O	30188	0.05
75	1	F	30216	0.03
75	2	P	30216	0.03
76	1	G	30674	0.04
76	2	H	30674	0.04
77	1	G	30802	0.03
77	2	I	30802	0.03
78	1	G	30678	0.03
78	2	J	30678	0.03
79	1	G	30560	0.04
79	2	K	30560	0.04
80	1	G	30634	0.03
80	2	L	30634	0.03
81	1	G	30180	0.03
81	2	M	30180	0.03
82	1	G	30494	0.04
82	2	N	30494	0.04
83	1	G	30208	0.04
83	2	O	30208	0.04
84	1	G	30150	0.03
84	2	P	30150	0.03
85	1	H	31650	0.03
85	2	I	31650	0.03
86	1	H	31536	0.03
86	2	J	31536	0.03
87	1	H	31686	0.04
87	2	K	31686	0.04
88	1	H	31222	0.04
88	2	L	31222	0.04
89	1	H	30788	0.04
89	2	M	30788	0.04
90	1	H	31432	0.03
90	2	N	31432	0.03
91	1	H	30372	0.04
91	2	O	30372	0.04
92	1	H	30258	0.04
92	2	P	30258	0.04
93	1	I	31478	0.03
93	2	J	31478	0.03
94	1	I	31518	0.05
94	2	K	31518	0.05
95	1	I	31356	0.03
95	2	L	31356	0.03
96	1	I	30850	0.04
96	2	M	30850	0.04
97	1	I	31308	0.03
97	2	N	31308	0.03
98	1	I	30458	0.04
98	2	O	30458	0.04
99	1	I	30194	0.03
99	2	P	30194	0.03
100	1	J	31530	0.04
100	2	K	31530	0.04
101	1	J	31204	0.04
101	2	L	31204	0.04
102	1	J	30932	0.03
102	2	M	30932	0.03
103	1	J	31248	0.03
103	2	N	31248	0.03
104	1	J	30428	0.04
104	2	O	30428	0.04
105	1	J	30304	0.03
105	2	P	30304	0.03
106	1	K	31094	0.04
106	2	L	31094	0.04
107	1	K	30958	0.03
107	2	M	30958	0.03
108	1	K	31212	0.04
108	2	N	31212	0.04
109	1	K	30384	0.05
109	2	O	30384	0.05
110	1	K	30276	0.04
110	2	P	30276	0.04
111	1	L	30756	0.04
111	2	M	30756	0.04
112	1	L	31190	0.03
112	2	N	31190	0.03
113	1	L	30364	0.04
113	2	O	30364	0.04
114	1	L	30110	0.04
114	2	P	30110	0.04
115	1	M	30658	0.04
115	2	N	30658	0.04
116	1	M	29782	0.04
116	2	O	29782	0.04
117	1	M	29696	0.03
117	2	P	29696	0.03
118	1	N	30174	0.04
118	2	O	30174	0.04
119	1	N	30032	0.03
119	2	P	30032	0.03
120	1	O	30066	0.04
120	2	P	30066	0.04

LS refinement shell

Resolution: 2.84→2.914 Å / R_factor R_free error: 0 / Total num. of bins used: 20

	Rfactor	Num. reflection	% reflection
Rfree	0.297	20	-
Rwork	0.35	398	-
all	-	418	-
obs	-	-	2.55 %

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	0.8305	0.0505	-0.2674	1.3488	0.1626	1.3247	-0.0111	-0.1058	-0.1339	0.1829	0.0428	-0.2493	0.4045	0.1434	-0.0317	0.1882	0.1127	0.0231	0.156	0.1164	0.1665	86.5285	40.2576	-58.7524
2	1.5594	-0.3973	0.2217	1.0421	-0.2065	1.4065	-0.0563	0.005	0.3327	0.0029	0.0192	-0.2206	-0.2623	0.1895	0.0371	0.1052	0.0281	0.0753	0.105	0.0883	0.2075	89.9243	70.7597	-76.4195
3	0.8834	-0.0611	0.0544	1.0413	-0.4552	1.8165	0.0622	-0.0589	0.1526	0.1262	-0.0149	0.0678	-0.3151	-0.1643	-0.0473	0.1372	0.0545	0.1016	0.0869	0.0176	0.115	52.7667	75.7034	-64.4946
4	0.7754	-0.0479	-0.0768	1.1077	-0.2007	0.9532	-0.0326	0.0374	-0.1982	0.0022	-0.0315	0.1308	0.2943	-0.1649	0.0641	0.1629	-0.0173	0.0921	0.1162	0.0089	0.1255	50.2613	41.3837	-73.5379
5	1.3505	0.2364	-0.8754	1.7143	-0.3109	1.6168	-0.2114	-0.2866	-0.1911	0.2044	-0.0517	-0.334	0.5249	0.5574	0.2632	0.6518	0.2032	0.2714	0.3424	0.1536	0.2605	46.7704	12.19	0.4154
6	1.5381	-0.5288	-0.5257	1.4091	0.1984	1.9028	-0.2165	0.0374	-0.3027	0.1066	-0.0749	0.3014	0.6246	-0.3341	0.2914	0.7633	-0.0925	0.369	0.2682	0.0338	0.2643	13.4695	7.2189	10.2648
7	1.258	0.2251	-0.2404	1.6381	0.2836	1.639	-0.0221	0.3217	0.1035	0.0132	-0.0461	0.5195	0.0967	-0.6607	0.0682	0.3588	-0.016	0.1618	0.5012	0.085	0.2664	8.1638	37.4004	-15.0558
8	1.1946	0.35	-0.9846	0.7983	-0.1556	1.9994	0.1691	-0.1969	0.2221	0.1946	-0.039	-0.0343	-0.222	0.2388	-0.1302	0.3963	-0.0021	0.1791	0.2252	0.0222	0.1619	36.0513	49.9313	2.3058
9	1.086	0.1028	-0.2372	1.393	-0.3944	1.5442	0.05	-0.1436	0.0376	0.2131	-0.0722	-0.2491	-0.3437	0.3482	0.0222	0.3553	-0.1524	-0.0079	0.1529	-0.0552	0.1094	94.3139	28.1269	-127.1902
10	0.8653	0.0333	-0.1207	1.2573	0.2437	1.3001	0.0063	-0.0604	-0.0222	0.156	0.0108	0.2947	-0.1354	-0.3623	-0.0172	0.2401	-0.0063	0.1148	0.1354	0.0037	0.1158	62.3513	17.1817	-137.7759
11	0.9941	0.1438	0.4363	0.8203	0.2452	1.5464	0.102	-0.1585	-0.3252	0.1959	0.0056	-0.0475	0.3351	-0.0596	-0.1075	0.2833	-0.056	0.0412	0.0671	0.0842	0.2324	78.9219	-18.0941	-134.4247
12	1.1154	0.0472	0.1847	1.1745	-0.1172	1.2125	0.0924	-0.0048	-0.1417	0.0495	-0.0698	-0.4878	0.0392	0.5369	-0.0226	0.1599	-0.0302	0.0485	0.2752	0.0036	0.3207	106.299	-1.4716	-149.5287
13	1.173	0.1012	-0.5374	0.9867	-0.4995	1.4812	0.1872	-0.2614	0.1512	0.2214	-0.0587	-0.1732	-0.5294	0.5912	-0.1285	0.8914	-0.0615	0.2852	0.4451	-0.0387	0.2543	32.6543	-13.6587	-59.402
14	1.1622	0.2602	-0.5851	0.6068	-0.1655	1.6128	0.1449	0.204	0.1717	0.071	0.075	0.2916	-0.4107	-0.4501	-0.2199	0.7221	0.2595	0.2994	0.3217	0.1117	0.3351	-0.856	-17.7096	-68.9913
15	1.4445	-0.1353	-1.0261	1.117	0.1097	2.4771	-0.1407	0.0669	-0.225	0.0254	0.0011	0.272	0.4999	-0.3562	0.1396	0.6731	0.0581	0.3127	0.2132	0.0751	0.2447	8.4358	-55.3969	-63.2841
16	0.8667	0.0773	-0.2212	1.5382	-0.1753	2.1305	-0.0434	-0.1547	-0.0457	0.0721	-0.0219	-0.234	0.1201	0.5345	0.0654	0.5464	0.1617	0.2732	0.2987	0.0699	0.1863	36.6187	-45.3586	-81.8539

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	112 - 901
2	X-RAY DIFFRACTION	2	B	114 - 901
3	X-RAY DIFFRACTION	3	C	114 - 901
4	X-RAY DIFFRACTION	4	D	114 - 901
5	X-RAY DIFFRACTION	5	E	114 - 803
6	X-RAY DIFFRACTION	6	F	114 - 803
7	X-RAY DIFFRACTION	7	G	115 - 803
8	X-RAY DIFFRACTION	8	H	114 - 901
9	X-RAY DIFFRACTION	9	I	115 - 901
10	X-RAY DIFFRACTION	10	J	113 - 901
11	X-RAY DIFFRACTION	11	K	113 - 803
12	X-RAY DIFFRACTION	12	L	116 - 901
13	X-RAY DIFFRACTION	13	M	115 - 901
14	X-RAY DIFFRACTION	14	N	115 - 803
15	X-RAY DIFFRACTION	15	O	115 - 803
16	X-RAY DIFFRACTION	16	P	114 - 803