PDB-3t5p: Crystal structure of a putative diacylglycerol kinase from Bacill...

ID or keywords:

Entry

Database: PDB / ID: 3t5p

Title

Crystal structure of a putative diacylglycerol kinase from Bacillus anthracis str. Sterne

Components

BmrU protein

Keywords

TRANSFERASE / structural genomics / center for structural genomics of infectious diseases / CSGID

Function / homology

Function and homology information

ATP-dependent diacylglycerol kinase activity / phospholipid biosynthetic process / ATP binding / metal ion binding / plasma membrane
Similarity search - Function

Biological species

Bacillus anthracis (anthrax bacterium)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

SAD / Resolution: 2.5 Å

Authors

Hou, J. / Zheng, H. / Chruszcz, M. / Cooper, D.R. / Onopriyenko, O. / Grimshaw, S. / Savchenko, A. / Anderson, W.F. / Minor, W. / Center for Structural Genomics of Infectious Diseases (CSGID)

Citation

Journal: To be Published
Title: Crystal structure of a putative diacylglycerol kinase from Bacillus anthracis str. Sterne
Authors: Hou, J. / Zheng, H. / Chruszcz, M. / Cooper, D.R. / Onopriyenko, O. / Grimshaw, S. / Savchenko, A. / Anderson, W.F. / Minor, W. / Center for Structural Genomics of Infectious Diseases (CSGID)

History

Deposition	Jul 27, 2011	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Sep 7, 2011	Provider: repository / Type: Initial release
Revision 1.1	Nov 8, 2017	Group: Refinement description / Category: software
Revision 1.2	Apr 13, 2022	Group: Database references / Derived calculations / Structure summary Category: audit_author / citation_author ...audit_author / citation_author / database_2 / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site Item: _audit_author.identifier_ORCID / _citation_author.identifier_ORCID ..._audit_author.identifier_ORCID / _citation_author.identifier_ORCID / _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_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.pdbx_leaving_atom_flag / _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_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.3	Nov 20, 2024	Group: Data collection / Structure summary Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	3t5p.cif.gz	1.3 MB	Display	PDBx/mmCIF format
PDB format	pdb3t5p.ent.gz	1.1 MB	Display	PDB format
PDBx/mmJSON format	3t5p.json.gz		Tree view	PDBx/mmJSON format
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Validation report

Summary document	3t5p_validation.pdf.gz	540.8 KB	Display	wwPDB validaton report
Full document	3t5p_full_validation.pdf.gz	574.7 KB	Display
Data in XML	3t5p_validation.xml.gz	115.9 KB	Display
Data in CIF	3t5p_validation.cif.gz	162.2 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/t5/3t5p ftp://data.pdbj.org/pub/pdb/validation_reports/t5/3t5p	HTTPS FTP

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Related structure data

Related structure data	4wrrC C: citing same article (ref.)
Similar structure data	4wrr-d 3s40-d 5uik-d 1cf8-2 1emc-d 3ggw-d 1bbj-d 4xd0-1 Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search
Other databases	TargetDB: IDP90228

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Links

PDB pages	PDBj / wwPDB / NCBI

Deposited unit

A: BmrU protein

B: BmrU protein

C: BmrU protein

D: BmrU protein

E: BmrU protein

F: BmrU protein

G: BmrU protein

H: BmrU protein

I: BmrU protein

J: BmrU protein

K: BmrU protein

L: BmrU protein

hetero molecules

405 kDa, 12 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: BmrU protein

F: BmrU protein

H: BmrU protein

J: BmrU protein

hetero molecules

defined by author&software
135 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: BmrU protein

D: BmrU protein

G: BmrU protein

L: BmrU protein

hetero molecules

defined by author&software
135 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

C: BmrU protein

E: BmrU protein

I: BmrU protein

K: BmrU protein

hetero molecules

defined by author&software
135 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	78.016, 115.100, 208.018
Angle α, β, γ (deg.)	90.000, 92.340, 90.000
Int Tables number	4
Space group name H-M	P12₁1

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:
NCS ensembles :

ID
1
2
3
4
5
6
7
8
9

#1: Protein	BmrU protein / putative diacylglycerol kinase Mass: 33740.840 Da / Num. of mol.: 12 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus anthracis (anthrax bacterium) / Strain: Sterne / Gene: BAS4713, BA_5075, GBAA_5075 / Plasmid: p15Tv lic / Production host: Escherichia coli (E. coli) / Strain (production host): BL21-CodonPlus(DE3)-RIL / References: UniProt: Q81KC6, UniProt: A0A6L8P1L2*PLUS
#2: Chemical	ChemComp-MG / MAGNESIUM ION Mass: 24.305 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: Mg
#3: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 505 / Source method: isolated from a natural source / Formula: H₂O
Has protein modification	Y

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.3 Å³/Da / Density % sol: 46.63 %
Crystal grow	Method: vapor diffusion / pH: 7 Details: 15%PEG 8K, 0.2M Mg Acetate, 0.1M Bis-Tris, pH 7, vapor diffusion

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Data collection

Diffraction

Mean temperature: 100 K

Diffraction source

Source:

SYNCHROTRON / Site:

APS

/ Beamline: 19-ID / Wavelength: 0.9792 Å

Detector

Type: ADSC QUANTUM 315r / Detector: CCD / Date: Mar 19, 2010 / Details: MIRRORS

Radiation

Monochromator: SI 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray

Radiation wavelength

Wavelength: 0.9792 Å / Relative weight: 1

Reflection

Redundancy: 4.3 % / Av σ(I) over netI: 22.56 / Number: 535182 / R_merge(I) obs: 0.087 / Χ²: 1.87 / D res high: 2.5 Å / D res low: 50 Å / Num. obs: 124871 / % possible obs: 98.9

Diffraction reflection shell

Highest resolution (Å)	Lowest resolution (Å)	% possible obs (%)	ID	R_merge(I) obs	Chi squared	Redundancy
6.78	50	95.4	1	0.053	6.145	4.2
5.38	6.78	99.5	1	0.068	4.284	4.2
4.7	5.38	99.5	1	0.057	2.951	4.2
4.27	4.7	99.6	1	0.057	2.615	4.3
3.97	4.27	99.5	1	0.064	2.431	4.3
3.73	3.97	99.4	1	0.07	2.233	4.4
3.55	3.73	99.2	1	0.079	1.995	4.3
3.39	3.55	99.6	1	0.089	1.649	4.4
3.26	3.39	99	1	0.102	1.423	4.4
3.15	3.26	99.3	1	0.126	1.295	4.4
3.05	3.15	99.3	1	0.152	1.215	4.4
2.96	3.05	99.2	1	0.196	1.129	4.4
2.89	2.96	99.2	1	0.229	1.045	4.3
2.82	2.89	99	1	0.273	1.019	4.3
2.75	2.82	98.8	1	0.31	1.006	4.3
2.69	2.75	98.8	1	0.381	0.967	4.3
2.64	2.69	98.6	1	0.474	1.035	4.2
2.59	2.64	98.8	1	0.551	1.024	4.2
2.54	2.59	98.7	1	0.646	1.009	4.2
2.5	2.54	98.4	1	0.718	1.033	4.2

Reflection

Resolution: 2.5→50 Å / Num. all: 126260 / Num. obs: 124871 / % possible obs: 98.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 4.3 % / R_merge(I) obs: 0.087 / R_sym value: 0.087 / Χ²: 1.873 / Net I/σ(I): 9.3

Reflection shell

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Num. unique all	Χ²	Diffraction-ID	% possible all
2.5-2.54	4.2	0.718	6176	1.033	1	98.4
2.54-2.59	4.2	0.646	6194	1.009	1	98.7
2.59-2.64	4.2	0.551	6182	1.024	1	98.8
2.64-2.69	4.2	0.474	6255	1.035	1	98.6
2.69-2.75	4.3	0.381	6138	0.967	1	98.8
2.75-2.82	4.3	0.31	6250	1.006	1	98.8
2.82-2.89	4.3	0.273	6272	1.019	1	99
2.89-2.96	4.3	0.229	6214	1.045	1	99.2
2.96-3.05	4.4	0.196	6187	1.129	1	99.2
3.05-3.15	4.4	0.152	6279	1.215	1	99.3
3.15-3.26	4.4	0.126	6254	1.295	1	99.3
3.26-3.39	4.4	0.102	6269	1.423	1	99
3.39-3.55	4.4	0.089	6238	1.649	1	99.6
3.55-3.73	4.3	0.079	6286	1.995	1	99.2
3.73-3.97	4.4	0.07	6268	2.233	1	99.4
3.97-4.27	4.3	0.064	6261	2.431	1	99.5
4.27-4.7	4.3	0.057	6273	2.615	1	99.6
4.7-5.38	4.2	0.057	6343	2.951	1	99.5
5.38-6.78	4.2	0.068	6343	4.284	1	99.5
6.78-50	4.2	0.053	6189	6.145	1	95.4

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Phasing

Phasing	Method: SAD

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Processing

Software

Name	Version	Classification
DENZO		data reduction
SCALEPACK		data scaling
SOLVE		phasing
DM		phasing
REFMAC		refinement
PDB_EXTRACT	3.1	data extraction
HKL-3000		data collection
HKL-3000		data reduction
HKL-3000		data scaling
HKL-3000		phasing

Refinement

Method to determine structure:

SAD / Resolution: 2.5→29.56 Å / Cor.coef. F_o:F_c: 0.951 / Cor.coef. F_o:F_c free: 0.929 / Occupancy max: 1 / Occupancy min: 0.5 / SU B: 22.636 / SU ML: 0.224 / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R Free: 0.291
Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES: RESIDUAL ONLY

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.2408	6264	5 %	RANDOM
R_work	0.2053	-	-	-
obs	0.207	124704	98.54 %	-

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK

Displacement parameters

B_iso max: 175.59 Å² / B_iso mean: 66.6765 Å² / B_iso min: 4.36 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	3.56 Å²	0 Å²	-0.49 Å²
2-	-	-3.45 Å²	0 Å²
3-	-	-	-0.14 Å²

Refinement step

Cycle: LAST / Resolution: 2.5→29.56 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	25805	0	12	505	26322

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.012	0.022	26343
X-RAY DIFFRACTION	r_bond_other_d	0.004	0.02	16840
X-RAY DIFFRACTION	r_angle_refined_deg	1.242	1.961	35849
X-RAY DIFFRACTION	r_angle_other_deg	0.97	3	41650
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	6.129	5	3411
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	37.286	25.787	1054
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	14.513	15	4124
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	10.912	15	26
X-RAY DIFFRACTION	r_chiral_restr	0.087	0.2	4219
X-RAY DIFFRACTION	r_gen_planes_refined	0.005	0.021	29490
X-RAY DIFFRACTION	r_gen_planes_other	0.002	0.02	4892
X-RAY DIFFRACTION	r_mcbond_it	0.483	1.5	17072
X-RAY DIFFRACTION	r_mcbond_other	0.07	1.5	7015
X-RAY DIFFRACTION	r_mcangle_it	0.947	2	27418
X-RAY DIFFRACTION	r_scbond_it	1.302	3	9271
X-RAY DIFFRACTION	r_scangle_it	2.211	4.5	8431

Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-ID	Dom-ID	Auth asym-ID	Number	Type	Rms dev position (Å)	Weight position
1	1	A	189	TIGHT POSITIONAL	0.03	0.05
1	2	B	189	TIGHT POSITIONAL	0.04	0.05
1	3	C	189	TIGHT POSITIONAL	0.03	0.05
1	4	D	189	TIGHT POSITIONAL	0.03	0.05
1	5	E	189	TIGHT POSITIONAL	0.03	0.05
1	6	F	189	TIGHT POSITIONAL	0.03	0.05
1	7	G	189	TIGHT POSITIONAL	0.05	0.05
1	8	H	189	TIGHT POSITIONAL	0.03	0.05
1	9	I	189	TIGHT POSITIONAL	0.06	0.05
1	10	J	189	TIGHT POSITIONAL	0.03	0.05
1	11	K	189	TIGHT POSITIONAL	0.05	0.05
1	12	L	189	TIGHT POSITIONAL	0.05	0.05
1	1	A	189	TIGHT THERMAL	0.08	0.5
1	2	B	189	TIGHT THERMAL	0.11	0.5
1	3	C	189	TIGHT THERMAL	0.1	0.5
1	4	D	189	TIGHT THERMAL	0.09	0.5
1	5	E	189	TIGHT THERMAL	0.09	0.5
1	6	F	189	TIGHT THERMAL	0.07	0.5
1	7	G	189	TIGHT THERMAL	0.09	0.5
1	8	H	189	TIGHT THERMAL	0.07	0.5
1	9	I	189	TIGHT THERMAL	0.11	0.5
1	10	J	189	TIGHT THERMAL	0.09	0.5
1	11	K	189	TIGHT THERMAL	0.1	0.5
1	12	L	189	TIGHT THERMAL	0.07	0.5
2	1	A	1290	TIGHT POSITIONAL	0.03	0.05
2	2	B	1290	TIGHT POSITIONAL	0.04	0.05
2	3	C	1290	TIGHT POSITIONAL	0.03	0.05
2	4	D	1290	TIGHT POSITIONAL	0.03	0.05
2	5	E	1290	TIGHT POSITIONAL	0.03	0.05
2	6	F	1290	TIGHT POSITIONAL	0.04	0.05
2	7	G	1290	TIGHT POSITIONAL	0.04	0.05
2	8	H	1290	TIGHT POSITIONAL	0.03	0.05
2	9	I	1290	TIGHT POSITIONAL	0.03	0.05
2	10	J	1290	TIGHT POSITIONAL	0.03	0.05
2	11	K	1290	TIGHT POSITIONAL	0.03	0.05
2	12	L	1290	TIGHT POSITIONAL	0.03	0.05
2	1	A	1290	TIGHT THERMAL	0.08	0.5
2	2	B	1290	TIGHT THERMAL	0.09	0.5
2	3	C	1290	TIGHT THERMAL	0.08	0.5
2	4	D	1290	TIGHT THERMAL	0.1	0.5
2	5	E	1290	TIGHT THERMAL	0.09	0.5
2	6	F	1290	TIGHT THERMAL	0.08	0.5
2	7	G	1290	TIGHT THERMAL	0.09	0.5
2	8	H	1290	TIGHT THERMAL	0.07	0.5
2	9	I	1290	TIGHT THERMAL	0.08	0.5
2	10	J	1290	TIGHT THERMAL	0.08	0.5
2	11	K	1290	TIGHT THERMAL	0.09	0.5
2	12	L	1290	TIGHT THERMAL	0.09	0.5
3	1	A	199	TIGHT POSITIONAL	0.12	0.05
3	2	B	199	TIGHT POSITIONAL	0.04	0.05
3	3	C	199	TIGHT POSITIONAL	0.03	0.05
3	4	D	199	TIGHT POSITIONAL	0.05	0.05
3	5	E	199	TIGHT POSITIONAL	0.04	0.05
3	6	F	199	TIGHT POSITIONAL	0.03	0.05
3	7	G	199	TIGHT POSITIONAL	0.05	0.05
3	8	H	199	TIGHT POSITIONAL	0.03	0.05
3	9	I	199	TIGHT POSITIONAL	0.04	0.05
3	10	J	199	TIGHT POSITIONAL	0.03	0.05
3	11	K	199	TIGHT POSITIONAL	0.12	0.05
3	12	L	199	TIGHT POSITIONAL	0.03	0.05
3	1	A	199	TIGHT THERMAL	0.06	0.5
3	2	B	199	TIGHT THERMAL	0.1	0.5
3	3	C	199	TIGHT THERMAL	0.06	0.5
3	4	D	199	TIGHT THERMAL	0.07	0.5
3	5	E	199	TIGHT THERMAL	0.06	0.5
3	6	F	199	TIGHT THERMAL	0.06	0.5
3	7	G	199	TIGHT THERMAL	0.08	0.5
3	8	H	199	TIGHT THERMAL	0.05	0.5
3	9	I	199	TIGHT THERMAL	0.06	0.5
3	10	J	199	TIGHT THERMAL	0.05	0.5
3	11	K	199	TIGHT THERMAL	0.07	0.5
3	12	L	199	TIGHT THERMAL	0.06	0.5
4	1	A	70	TIGHT POSITIONAL	0.09	0.05
4	2	B	70	TIGHT POSITIONAL	0.05	0.05
4	3	C	70	TIGHT POSITIONAL	0.03	0.05
4	4	D	70	TIGHT POSITIONAL	0.03	0.05
4	5	E	70	TIGHT POSITIONAL	0.05	0.05
4	6	F	70	TIGHT POSITIONAL	0.1	0.05
4	7	G	70	TIGHT POSITIONAL	0.02	0.05
4	8	H	70	TIGHT POSITIONAL	0.05	0.05
4	9	I	70	TIGHT POSITIONAL	0.03	0.05
4	10	J	70	TIGHT POSITIONAL	0.03	0.05
4	11	K	70	TIGHT POSITIONAL	0.03	0.05
4	12	L	70	TIGHT POSITIONAL	0.04	0.05
4	1	A	27	MEDIUM POSITIONAL	0.05	0.5
4	2	B	27	MEDIUM POSITIONAL	0.05	0.5
4	3	C	27	MEDIUM POSITIONAL	0.03	0.5
4	4	D	27	MEDIUM POSITIONAL	0.03	0.5
4	5	E	27	MEDIUM POSITIONAL	0.06	0.5
4	6	F	27	MEDIUM POSITIONAL	0.06	0.5
4	7	G	27	MEDIUM POSITIONAL	0.04	0.5
4	8	H	27	MEDIUM POSITIONAL	0.03	0.5
4	9	I	27	MEDIUM POSITIONAL	0.03	0.5
4	10	J	27	MEDIUM POSITIONAL	0.04	0.5
4	11	K	27	MEDIUM POSITIONAL	0.02	0.5
4	12	L	27	MEDIUM POSITIONAL	0.04	0.5
4	1	A	70	TIGHT THERMAL	0.06	0.5
4	2	B	70	TIGHT THERMAL	0.05	0.5
4	3	C	70	TIGHT THERMAL	0.04	0.5
4	4	D	70	TIGHT THERMAL	0.05	0.5
4	5	E	70	TIGHT THERMAL	0.05	0.5
4	6	F	70	TIGHT THERMAL	0.04	0.5
4	7	G	70	TIGHT THERMAL	0.04	0.5
4	8	H	70	TIGHT THERMAL	0.05	0.5
4	9	I	70	TIGHT THERMAL	0.05	0.5
4	10	J	70	TIGHT THERMAL	0.05	0.5
4	11	K	70	TIGHT THERMAL	0.05	0.5
4	12	L	70	TIGHT THERMAL	0.05	0.5
4	1	A	27	MEDIUM THERMAL	0.04	2
4	2	B	27	MEDIUM THERMAL	0.05	2
4	3	C	27	MEDIUM THERMAL	0.04	2
4	4	D	27	MEDIUM THERMAL	0.05	2
4	5	E	27	MEDIUM THERMAL	0.04	2
4	6	F	27	MEDIUM THERMAL	0.04	2
4	7	G	27	MEDIUM THERMAL	0.05	2
4	8	H	27	MEDIUM THERMAL	0.04	2
4	9	I	27	MEDIUM THERMAL	0.05	2
4	10	J	27	MEDIUM THERMAL	0.04	2
4	11	K	27	MEDIUM THERMAL	0.04	2
4	12	L	27	MEDIUM THERMAL	0.04	2
5	1	A	168	TIGHT POSITIONAL	0.03	0.05
5	2	B	168	TIGHT POSITIONAL	0.03	0.05
5	3	C	168	TIGHT POSITIONAL	0.02	0.05
5	4	D	168	TIGHT POSITIONAL	0.03	0.05
5	5	E	168	TIGHT POSITIONAL	0.02	0.05
5	6	F	168	TIGHT POSITIONAL	0.02	0.05
5	7	G	168	TIGHT POSITIONAL	0.03	0.05
5	8	H	168	TIGHT POSITIONAL	0.02	0.05
5	9	I	168	TIGHT POSITIONAL	0.02	0.05
5	10	J	168	TIGHT POSITIONAL	0.03	0.05
5	11	K	168	TIGHT POSITIONAL	0.02	0.05
5	12	L	168	TIGHT POSITIONAL	0.02	0.05
5	1	A	168	TIGHT THERMAL	0.05	0.5
5	2	B	168	TIGHT THERMAL	0.07	0.5
5	3	C	168	TIGHT THERMAL	0.04	0.5
5	4	D	168	TIGHT THERMAL	0.04	0.5
5	5	E	168	TIGHT THERMAL	0.03	0.5
5	6	F	168	TIGHT THERMAL	0.03	0.5
5	7	G	168	TIGHT THERMAL	0.04	0.5
5	8	H	168	TIGHT THERMAL	0.03	0.5
5	9	I	168	TIGHT THERMAL	0.03	0.5
5	10	J	168	TIGHT THERMAL	0.03	0.5
5	11	K	168	TIGHT THERMAL	0.04	0.5
5	12	L	168	TIGHT THERMAL	0.04	0.5
6	1	A	179	TIGHT POSITIONAL	0.04	0.05
6	2	B	179	TIGHT POSITIONAL	0.03	0.05
6	3	C	179	TIGHT POSITIONAL	0.02	0.05
6	4	D	179	TIGHT POSITIONAL	0.03	0.05
6	5	E	179	TIGHT POSITIONAL	0.03	0.05
6	6	F	179	TIGHT POSITIONAL	0.02	0.05
6	7	G	179	TIGHT POSITIONAL	0.03	0.05
6	8	H	179	TIGHT POSITIONAL	0.02	0.05
6	9	I	179	TIGHT POSITIONAL	0.03	0.05
6	10	J	179	TIGHT POSITIONAL	0.03	0.05
6	11	K	179	TIGHT POSITIONAL	0.02	0.05
6	12	L	179	TIGHT POSITIONAL	0.02	0.05
6	1	A	185	MEDIUM POSITIONAL	0.05	0.5
6	2	B	185	MEDIUM POSITIONAL	0.03	0.5
6	3	C	185	MEDIUM POSITIONAL	0.03	0.5
6	4	D	185	MEDIUM POSITIONAL	0.03	0.5
6	5	E	185	MEDIUM POSITIONAL	0.02	0.5
6	6	F	185	MEDIUM POSITIONAL	0.03	0.5
6	7	G	185	MEDIUM POSITIONAL	0.04	0.5
6	8	H	185	MEDIUM POSITIONAL	0.03	0.5
6	9	I	185	MEDIUM POSITIONAL	0.03	0.5
6	10	J	185	MEDIUM POSITIONAL	0.03	0.5
6	11	K	185	MEDIUM POSITIONAL	0.03	0.5
6	12	L	185	MEDIUM POSITIONAL	0.03	0.5
6	1	A	179	TIGHT THERMAL	0.07	0.5
6	2	B	179	TIGHT THERMAL	0.09	0.5
6	3	C	179	TIGHT THERMAL	0.06	0.5
6	4	D	179	TIGHT THERMAL	0.07	0.5
6	5	E	179	TIGHT THERMAL	0.07	0.5
6	6	F	179	TIGHT THERMAL	0.06	0.5
6	7	G	179	TIGHT THERMAL	0.06	0.5
6	8	H	179	TIGHT THERMAL	0.04	0.5
6	9	I	179	TIGHT THERMAL	0.06	0.5
6	10	J	179	TIGHT THERMAL	0.04	0.5
6	11	K	179	TIGHT THERMAL	0.08	0.5
6	12	L	179	TIGHT THERMAL	0.06	0.5
6	1	A	185	MEDIUM THERMAL	0.1	2
6	2	B	185	MEDIUM THERMAL	0.11	2
6	3	C	185	MEDIUM THERMAL	0.07	2
6	4	D	185	MEDIUM THERMAL	0.08	2
6	5	E	185	MEDIUM THERMAL	0.07	2
6	6	F	185	MEDIUM THERMAL	0.08	2
6	7	G	185	MEDIUM THERMAL	0.07	2
6	8	H	185	MEDIUM THERMAL	0.05	2
6	9	I	185	MEDIUM THERMAL	0.06	2
6	10	J	185	MEDIUM THERMAL	0.05	2
6	11	K	185	MEDIUM THERMAL	0.07	2
6	12	L	185	MEDIUM THERMAL	0.07	2
7	1	A	77	TIGHT POSITIONAL	0.05	0.05
7	2	B	77	TIGHT POSITIONAL	0.03	0.05
7	3	C	77	TIGHT POSITIONAL	0.02	0.05
7	4	D	77	TIGHT POSITIONAL	0.02	0.05
7	5	E	77	TIGHT POSITIONAL	0.02	0.05
7	6	F	77	TIGHT POSITIONAL	0.03	0.05
7	7	G	77	TIGHT POSITIONAL	0.02	0.05
7	8	H	77	TIGHT POSITIONAL	0.02	0.05
7	9	I	77	TIGHT POSITIONAL	0.02	0.05
7	10	J	77	TIGHT POSITIONAL	0.02	0.05
7	11	K	77	TIGHT POSITIONAL	0.02	0.05
7	12	L	77	TIGHT POSITIONAL	0.02	0.05
7	1	A	77	TIGHT THERMAL	0.22	0.5
7	2	B	77	TIGHT THERMAL	0.04	0.5
7	3	C	77	TIGHT THERMAL	0.04	0.5
7	4	D	77	TIGHT THERMAL	0.05	0.5
7	5	E	77	TIGHT THERMAL	0.03	0.5
7	6	F	77	TIGHT THERMAL	0.04	0.5
7	7	G	77	TIGHT THERMAL	0.04	0.5
7	8	H	77	TIGHT THERMAL	0.03	0.5
7	9	I	77	TIGHT THERMAL	0.05	0.5
7	10	J	77	TIGHT THERMAL	0.03	0.5
7	11	K	77	TIGHT THERMAL	0.06	0.5
7	12	L	77	TIGHT THERMAL	0.03	0.5
8	1	A	358	TIGHT POSITIONAL	0.03	0.05
8	2	B	358	TIGHT POSITIONAL	0.03	0.05
8	3	C	358	TIGHT POSITIONAL	0.02	0.05
8	4	D	358	TIGHT POSITIONAL	0.04	0.05
8	5	E	358	TIGHT POSITIONAL	0.02	0.05
8	6	F	358	TIGHT POSITIONAL	0.02	0.05
8	7	G	358	TIGHT POSITIONAL	0.04	0.05
8	8	H	358	TIGHT POSITIONAL	0.02	0.05
8	9	I	358	TIGHT POSITIONAL	0.05	0.05
8	10	J	358	TIGHT POSITIONAL	0.02	0.05
8	11	K	358	TIGHT POSITIONAL	0.02	0.05
8	12	L	358	TIGHT POSITIONAL	0.02	0.05
8	1	A	358	TIGHT THERMAL	0.05	0.5
8	2	B	358	TIGHT THERMAL	0.08	0.5
8	3	C	358	TIGHT THERMAL	0.05	0.5
8	4	D	358	TIGHT THERMAL	0.07	0.5
8	5	E	358	TIGHT THERMAL	0.05	0.5
8	6	F	358	TIGHT THERMAL	0.04	0.5
8	7	G	358	TIGHT THERMAL	0.06	0.5
8	8	H	358	TIGHT THERMAL	0.04	0.5
8	9	I	358	TIGHT THERMAL	0.04	0.5
8	10	J	358	TIGHT THERMAL	0.05	0.5
8	11	K	358	TIGHT THERMAL	0.04	0.5
8	12	L	358	TIGHT THERMAL	0.05	0.5
9	1	A	181	TIGHT POSITIONAL	0.04	0.05
9	2	B	181	TIGHT POSITIONAL	0.03	0.05
9	3	C	181	TIGHT POSITIONAL	0.04	0.05
9	4	D	181	TIGHT POSITIONAL	0.03	0.05
9	5	E	181	TIGHT POSITIONAL	0.03	0.05
9	6	F	181	TIGHT POSITIONAL	0.03	0.05
9	7	G	181	TIGHT POSITIONAL	0.04	0.05
9	8	H	181	TIGHT POSITIONAL	0.02	0.05
9	9	I	181	TIGHT POSITIONAL	0.04	0.05
9	10	J	181	TIGHT POSITIONAL	0.02	0.05
9	11	K	181	TIGHT POSITIONAL	0.04	0.05
9	12	L	181	TIGHT POSITIONAL	0.03	0.05
9	1	A	181	TIGHT THERMAL	0.08	0.5
9	2	B	181	TIGHT THERMAL	0.11	0.5
9	3	C	181	TIGHT THERMAL	0.11	0.5
9	4	D	181	TIGHT THERMAL	0.12	0.5
9	5	E	181	TIGHT THERMAL	0.08	0.5
9	6	F	181	TIGHT THERMAL	0.1	0.5
9	7	G	181	TIGHT THERMAL	0.09	0.5
9	8	H	181	TIGHT THERMAL	0.06	0.5
9	9	I	181	TIGHT THERMAL	0.09	0.5
9	10	J	181	TIGHT THERMAL	0.08	0.5
9	11	K	181	TIGHT THERMAL	0.14	0.5
9	12	L	181	TIGHT THERMAL	0.09	0.5

LS refinement shell

Resolution: 2.504→2.568 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.335	425	-
R_work	0.305	8294	-
all	-	8719	-
obs	-	-	94.07 %

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	1.324	0.0409	0.073	4.1039	1.1137	2.6298	-0.0573	-0.2755	0.0525	0.7313	0.1902	0.0874	0.2033	-0.109	-0.1328	0.161	0.1258	0.0359	0.3068	0.0606	0.0595	26.505	-3.265	14.486
2	0.8239	-0.1993	0.5445	3.6859	-1.7778	2.1195	-0.0006	-0.0121	0.0997	0.171	0.2822	0.6614	0.136	-0.5765	-0.2816	0.2426	0.0325	0.0145	0.3589	0.0966	0.1588	27.246	-30.629	16.948
3	2.0627	-0.5745	0.0652	5.9196	-0.2464	0.5426	0.0086	-0.1468	-0.1502	0.2921	0.2307	0.2864	0.1342	-0.2228	-0.2394	0.1411	0.0597	-0.0443	0.3325	0.1217	0.1172	28.233	-25.859	10.009
4	1.24	0.3429	0.2768	3.6889	-0.0698	1.8784	-0.0175	-0.0535	-0.0438	-0.3266	0.1276	0.3882	-0.0892	-0.0911	-0.11	0.0347	-0.0118	-0.0302	0.0728	0.0208	0.0541	49.628	12.543	82.911
5	0.994	0.0658	0.1	3.2959	-0.0263	1.4444	-0.0669	0.0091	0.3922	-0.3789	0.1003	0.4191	-0.2601	-0.2423	-0.0335	0.0942	0.0234	-0.0572	0.1246	0.0342	0.231	48.253	37.56	79.363
6	2.9965	-1.0273	0.3974	4.914	0.3576	2.6318	-0.1396	-0.114	0.4905	-0.3075	0.1921	0.1007	-0.2103	-0.1335	-0.0525	0.0437	-0.0013	-0.0377	0.0557	0.0359	0.1411	52.534	37.097	81.309
7	1.9612	-0.3373	-0.5127	1.9645	-0.4215	1.2941	-0.0259	0.1218	-0.0278	-0.204	0.043	0.3827	0.2693	-0.1628	-0.0171	0.2055	-0.0544	-0.0577	0.1904	0.0227	0.0898	6.864	81.095	57.108
8	1.83	-0.4813	-0.2376	2.6227	0.5509	1.222	0.0178	0.2974	-0.4979	-0.2842	-0.0473	0.3133	0.5942	-0.1283	0.0296	0.6497	-0.0655	-0.0325	0.2549	-0.0381	0.21	8.628	56.356	58.379
9	1.7866	0.3173	0.2572	2.6561	0.0149	1.3766	-0.0264	0.241	-0.4269	-0.17	0.0413	0.0974	0.8006	0.0301	-0.015	0.6185	-0.025	-0.0006	0.2278	-0.0335	0.1274	10.629	55.999	60.931
10	0.75	-0.3444	0.2997	2.79	-0.2532	2.3506	0.0217	-0.0316	-0.0005	0.2148	0.0765	-0.0944	-0.1488	0.1075	-0.0982	0.0537	0.0315	0.0191	0.136	-0.0171	0.0458	57.488	14.894	115.752
11	1.92	0.5327	0.3646	3.5539	-1.2741	2.4756	-0.1094	-0.0579	0.6824	0.4696	0.0118	-0.0659	-0.4477	0.2833	0.0976	0.1789	0.0267	-0.0177	0.1561	-0.045	0.3149	57.376	38.816	114.888
12	2.631	0.6978	-0.6937	3.5221	-1.2706	0.9518	0.0039	-0.1736	0.6239	0.6136	0.0552	0.116	-0.3222	0.063	-0.0592	0.1612	0.0298	-0.0205	0.158	-0.0611	0.2204	54.034	39.768	113.046
13	1.5392	-0.1276	-0.0549	2.9423	-0.2884	1.5602	0.0463	-0.0503	0.0375	-0.1481	-0.0295	0.3353	0.0072	-0.1469	-0.0167	0.0441	0.041	-0.0319	0.244	0.0291	0.1008	3.837	106.096	51.652
14	4.3479	0.2292	-6.3215	0.025	-0.2672	10.5973	-0.081	-0.1303	0.4016	0.0508	0.0305	0.0518	0.342	0.0007	0.0505	0.3094	0.0956	0.0822	0.3514	-0.0751	0.3261	-5.944	127.684	64.249
15	2.6284	-0.7834	-1.1852	4.1884	1.1211	3.6356	0.3435	-0.0842	0.4854	-0.4518	-0.1089	0.3549	-0.8552	0.0616	-0.2345	0.2754	0.0591	0.0102	0.2703	0.0357	0.2337	1.051	130.043	48.249
16	1.316	0.0727	0.087	3.0234	0.3673	1.4757	0.0564	-0.0337	0.4973	-0.5252	0.0605	0.3027	-0.5473	-0.2721	-0.117	0.262	0.0761	0.033	0.1625	0.0962	0.3384	17.44	31.057	-17.998
17	3.4532	-1.6308	8.4814	0.8418	-4.009	21.0953	-0.9211	0.1451	0.2189	0.5816	0.138	-0.1346	-2.8498	0.2852	0.783	1.9325	0.5169	-0.1078	0.5455	-0.0344	1.0665	15.738	50.592	-31.578
18	1.6042	0.6198	0.4936	0.4798	-0.2721	1.6359	-0.0015	-0.2636	0.6953	0.063	0.0832	0.3821	-0.6413	-0.3076	-0.0817	0.5459	0.0071	0.1831	0.2713	0.0173	0.5584	20.657	41.249	-12.487
19	1.1158	0.113	-0.059	3.8618	-0.8592	2.3515	-0.0738	-0.0392	-0.1357	-0.3558	0.2018	0.3226	0.1818	0.1322	-0.1281	0.0453	-0.0202	-0.037	0.0853	0.0131	0.164	47.374	-11.031	85.303
20	1.4132	-0.9767	-0.1159	6.7311	-0.2609	1.6726	-0.191	-0.0234	-0.1973	-0.3972	0.1661	-0.0609	0.3933	0.2669	0.0249	0.1592	0.0073	0.0497	0.1734	0.0001	0.3061	46.398	-35.934	86.614
21	2.2037	-0.7802	-0.3937	4.675	0.4758	1.8668	-0.2486	0.0213	-0.3061	-0.0056	0.1508	0.1473	0.3606	0.4017	0.0977	0.101	0.0304	0.0664	0.2332	0.0063	0.2647	44.753	-36.232	88.718
22	1.5103	-0.4147	-0.0913	4.1006	-0.6062	1.5296	-0.0092	-0.321	0.2639	0.8379	0.0994	0.1191	-0.0989	0.1263	-0.0903	0.2137	0.0808	0.0785	0.3509	-0.1082	0.2299	20.789	21.193	15.846
23	3.6989	1.2306	1.0522	5.8363	0.5865	0.8258	0.1128	0.0913	0.6506	0.902	0.0678	-0.1415	-0.3278	0.3726	-0.1805	0.5727	-0.0776	0.2581	0.4936	-0.2162	0.6597	20.248	48.024	16.29
24	2.8146	0.0218	0.1764	5.3317	1.3289	3.3605	0.2547	0.0343	0.6601	0.3215	-0.0797	0.2128	-0.5827	0.4769	-0.1749	0.2605	0.0003	0.2212	0.4911	-0.1097	0.5379	17.045	43.146	13.078
25	2.5923	0.545	-0.6354	3.0466	0.4145	1.8466	0.0353	-0.1711	0.0677	-0.0309	0.0502	-0.2708	0.3152	0.1663	-0.0854	0.1885	0.0965	0.0036	0.1334	-0.0122	0.0297	39.419	84.689	48.573
26	1.598	-0.0684	0.424	4.1339	-1.3233	2.1868	0.142	-0.2641	-0.5031	0.1752	-0.0793	-0.345	0.6406	0.184	-0.0626	0.6164	0.2182	-0.0434	0.2148	0.0971	0.1962	42.3	60.688	47.699
27	2.3019	0.6791	-0.2336	3.2711	-0.7006	0.9969	-0.0539	-0.3357	-0.4907	-0.0148	0.0668	-0.1014	0.6491	0.0349	-0.0128	0.6453	0.1804	-0.0076	0.1988	0.0925	0.1118	38.299	60.531	47.569
28	2.0897	-0.418	0.61	4.5452	-0.974	2.8751	0.0741	0.1118	-0.3458	-0.4234	0.0789	0.5009	0.2327	-0.0417	-0.1529	0.0536	-0.0338	-0.0706	0.1545	0.018	0.2259	13.994	-3.289	-17.013
29	1.0186	-1.402	0.3013	6.6089	-0.7087	1.6793	0.2579	0.098	-0.3355	-0.7892	0.0702	0.2481	0.8154	0.0256	-0.328	0.4696	-0.0716	-0.2644	0.2675	-0.0336	0.6597	12.574	-28.506	-16.944
30	0.2925	-0.8401	0.2147	4.2185	0.643	2.1056	0.2142	0.0204	-0.1891	-0.1355	0.2035	0.3497	0.6161	0.1969	-0.4176	0.3549	-0.0525	-0.267	0.3608	0.0249	0.5758	11.87	-26.467	-13.759
31	2.4182	-0.5874	0.2817	2.58	0.3962	1.5988	0.0389	0.1195	0.0646	-0.1529	0.0163	-0.2036	-0.051	0.0935	-0.0551	0.1015	-0.0038	0.0379	0.109	0.0085	0.0248	37.09	108.254	50.971
32	1.962	-0.086	-0.4483	4.5666	-0.5903	2.2336	0.0977	0.3449	0.5831	-0.2804	-0.0577	-0.2598	-0.674	-0.1245	-0.0399	0.2866	-0.0205	0.0342	0.1668	0.0818	0.2312	36.452	133.453	50.376
33	2.487	-0.4939	-0.4262	4.1034	-1.5342	3.2603	0.0043	0.339	0.5133	0.1074	0.1339	0.0687	-0.5804	-0.5549	-0.1383	0.1894	0.0454	0.0338	0.2226	0.0385	0.1312	30.555	130.983	54
34	1.2169	-0.4691	0.367	3.5193	0.6932	1.8232	-0.0264	-0.1437	-0.1873	0.2644	0.0634	0.0478	0.0245	-0.0265	-0.037	0.0365	0.0468	0.0179	0.1562	0.0428	0.0719	60.563	-8.752	116.296
35	1.7395	0.6733	-0.5398	3.3442	-0.5893	2.8383	-0.0694	-0.1574	-0.4198	0.0371	-0.0458	0.253	0.6315	-0.0934	0.1151	0.189	0.0446	0.0206	0.1651	0.0619	0.3115	61.147	-32.792	118.679
36	2.0123	-0.1336	-0.3356	3.054	-0.9484	3.3091	-0.0041	-0.0187	-0.6252	-0.1395	0.0681	0.0148	0.6657	0.0793	-0.064	0.1735	0.0846	-0.0143	0.1296	0.043	0.2713	63.496	-33.478	115.782

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	3 - 128
2	X-RAY DIFFRACTION	2	A	129 - 243
3	X-RAY DIFFRACTION	3	A	244 - 300
4	X-RAY DIFFRACTION	4	B	2 - 119
5	X-RAY DIFFRACTION	5	B	120 - 234
6	X-RAY DIFFRACTION	6	B	235 - 300
7	X-RAY DIFFRACTION	7	C	0 - 119
8	X-RAY DIFFRACTION	8	C	120 - 230
9	X-RAY DIFFRACTION	9	C	231 - 300
10	X-RAY DIFFRACTION	10	D	3 - 119
11	X-RAY DIFFRACTION	11	D	120 - 228
12	X-RAY DIFFRACTION	12	D	229 - 299
13	X-RAY DIFFRACTION	13	E	3 - 139
14	X-RAY DIFFRACTION	14	E	140 - 177
15	X-RAY DIFFRACTION	15	E	178 - 300
16	X-RAY DIFFRACTION	16	F	3 - 234
17	X-RAY DIFFRACTION	17	F	235 - 244
18	X-RAY DIFFRACTION	18	F	253 - 300
19	X-RAY DIFFRACTION	19	G	3 - 119
20	X-RAY DIFFRACTION	20	G	120 - 230
21	X-RAY DIFFRACTION	21	G	231 - 299
22	X-RAY DIFFRACTION	22	H	2 - 128
23	X-RAY DIFFRACTION	23	H	129 - 237
24	X-RAY DIFFRACTION	24	H	238 - 299
25	X-RAY DIFFRACTION	25	I	3 - 119
26	X-RAY DIFFRACTION	26	I	120 - 229
27	X-RAY DIFFRACTION	27	I	230 - 300
28	X-RAY DIFFRACTION	28	J	3 - 120
29	X-RAY DIFFRACTION	29	J	121 - 235
30	X-RAY DIFFRACTION	30	J	236 - 299
31	X-RAY DIFFRACTION	31	K	3 - 119
32	X-RAY DIFFRACTION	32	K	120 - 243
33	X-RAY DIFFRACTION	33	K	244 - 300
34	X-RAY DIFFRACTION	34	L	3 - 119
35	X-RAY DIFFRACTION	35	L	120 - 229
36	X-RAY DIFFRACTION	36	L	230 - 300

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