PDB-7nmm: Complex of rice blast (Magnaporthe oryzae) effector protein APikL...

ID or keywords:

Entry

Database: PDB / ID: 7nmm

Title

Complex of rice blast (Magnaporthe oryzae) effector protein APikL2F with the host target sHMA94 from Setaria italica

Components

APikL2F
sHMAx

Keywords

PLANT PROTEIN /

Complex / fungal effector / host target / heavy-metal associated domain / MAX effector

Function / homology

DI(HYDROXYETHYL)ETHER / Uncharacterized protein

Function and homology information

Biological species

Setaria italica (foxtail millet)

Pyricularia oryzae B157 (fungus)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.3 Å

Authors

Bentham, A.R. / Banfield, M.J.

Funding support

United Kingdom, 2items

Citation

Journal: Plos Pathog. / Year: 2021
Title: A single amino acid polymorphism in a conserved effector of the multihost blast fungus pathogen expands host-target binding spectrum.
Authors: Bentham, A.R. / Petit-Houdenot, Y. / Win, J. / Chuma, I. / Terauchi, R. / Banfield, M.J. / Kamoun, S. / Langner, T.

History

Deposition	Feb 23, 2021	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Mar 24, 2021	Provider: repository / Type: Initial release
Revision 1.1	Nov 24, 2021	Group: Data collection / Database references / Structure summary Category: citation / citation_author ...citation / citation_author / database_2 / diffrn_source / pdbx_database_proc / struct Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _diffrn_source.pdbx_synchrotron_site / _struct.pdbx_center_of_mass_x / _struct.pdbx_center_of_mass_y / _struct.pdbx_center_of_mass_z
Revision 1.2	Jan 31, 2024	Group: Data collection / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / diffrn_source / pdbx_initial_refinement_model / struct_ncs_dom_lim Item: _diffrn_source.pdbx_synchrotron_site / _struct_ncs_dom_lim.beg_auth_comp_id ..._diffrn_source.pdbx_synchrotron_site / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	7nmm.cif.gz	546.1 KB	Display	PDBx/mmCIF format
PDB format	pdb7nmm.ent.gz	454.3 KB	Display	PDB format
PDBx/mmJSON format	7nmm.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/nm/7nmm ftp://data.pdbj.org/pub/pdb/validation_reports/nm/7nmm	HTTPS FTP

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Related structure data

Related structure data	7nljSC S: Starting model for refinement C: citing same article (ref.)
Similar structure data	6gx6-d 4tkg-4 4fhr-1 6anr-d 3r8j-1 5wa7-d 5ldj-1 4u9b-d 4pnr-1 5wa6-d 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) 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) Search similar-shape structures by Omokage search (details) Similarity search - Function & homologyF&H Search Similarity search - HomologyF&H Search

Related structure data

7nljSC

S: Starting model for refinement

C: citing same article (ref.)

Similar structure data

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Links

PDB pages	PDBj / wwPDB / NCBI

Deposited unit

A: sHMAx

B: sHMAx

C: sHMAx

D: sHMAx

E: sHMAx

F: sHMAx

G: sHMAx

H: sHMAx

I: APikL2F

J: APikL2F

K: APikL2F

L: APikL2F

M: APikL2F

N: APikL2F

O: APikL2F

P: APikL2F

hetero molecules

158 kDa, 16 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: sHMAx

I: APikL2F

hetero molecules

defined by software
Evidence: isothermal titration calorimetry
19.6 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: sHMAx

J: APikL2F

hetero molecules

defined by software
19.6 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

C: sHMAx

K: APikL2F

hetero molecules

defined by software
19.7 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

4

D: sHMAx

L: APikL2F

hetero molecules

defined by software
19.9 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

5

E: sHMAx

M: APikL2F

hetero molecules

defined by software
19.7 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

6

F: sHMAx

N: APikL2F

hetero molecules

defined by software
19.6 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

7

G: sHMAx

O: APikL2F

hetero molecules

defined by software
19.6 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

8

H: sHMAx

P: APikL2F

hetero molecules

defined by software
19.8 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	125.444, 222.479, 102.015
Angle α, β, γ (deg.)	90.000, 90.000, 90.000
Int Tables number	20
Space group name H-M	C222₁

Components on special symmetry positions

ID	Model	Components
1	1	M-202- CL
2	1	P-318- HOH

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Component-ID: 0 / Refine code: 0

Dom-ID	Ens-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	MET	MET	ASP	ASP	A	A	2 - 79	1 - 78
2	1	MET	MET	ASP	ASP	B	B	2 - 79	1 - 78
1	2	MET	MET	ALA	ALA	A	A	2 - 77	1 - 76
2	2	MET	MET	ALA	ALA	C	C	2 - 77	1 - 76
1	3	MET	MET	ASP	ASP	A	A	2 - 79	1 - 78
2	3	MET	MET	ASP	ASP	D	D	2 - 79	1 - 78
1	4	MET	MET	ASP	ASP	A	A	2 - 79	1 - 78
2	4	MET	MET	ASP	ASP	E	E	2 - 79	1 - 78
1	5	MET	MET	ASP	ASP	A	A	2 - 79	1 - 78
2	5	MET	MET	ASP	ASP	F	F	2 - 79	1 - 78
1	6	MET	MET	ASP	ASP	A	A	2 - 79	1 - 78
2	6	MET	MET	ASP	ASP	G	G	2 - 79	1 - 78
1	7	MET	MET	ASP	ASP	A	A	2 - 79	1 - 78
2	7	MET	MET	ASP	ASP	H	H	2 - 79	1 - 78
1	8	MET	MET	ALA	ALA	B	B	2 - 77	1 - 76
2	8	MET	MET	ALA	ALA	C	C	2 - 77	1 - 76
1	9	MET	MET	ASP	ASP	B	B	2 - 79	1 - 78
2	9	MET	MET	ASP	ASP	D	D	2 - 79	1 - 78
1	10	MET	MET	ASP	ASP	B	B	2 - 79	1 - 78
2	10	MET	MET	ASP	ASP	E	E	2 - 79	1 - 78
1	11	MET	MET	ASP	ASP	B	B	2 - 79	1 - 78
2	11	MET	MET	ASP	ASP	F	F	2 - 79	1 - 78
1	12	MET	MET	ASP	ASP	B	B	2 - 79	1 - 78
2	12	MET	MET	ASP	ASP	G	G	2 - 79	1 - 78
1	13	MET	MET	ASP	ASP	B	B	2 - 79	1 - 78
2	13	MET	MET	ASP	ASP	H	H	2 - 79	1 - 78
1	14	MET	MET	ALA	ALA	C	C	2 - 77	1 - 76
2	14	MET	MET	ALA	ALA	D	D	2 - 77	1 - 76
1	15	MET	MET	ALA	ALA	C	C	2 - 77	1 - 76
2	15	MET	MET	ALA	ALA	E	E	2 - 77	1 - 76
1	16	MET	MET	ALA	ALA	C	C	2 - 77	1 - 76
2	16	MET	MET	ALA	ALA	F	F	2 - 77	1 - 76
1	17	MET	MET	ALA	ALA	C	C	2 - 77	1 - 76
2	17	MET	MET	ALA	ALA	G	G	2 - 77	1 - 76
1	18	MET	MET	ALA	ALA	C	C	2 - 77	1 - 76
2	18	MET	MET	ALA	ALA	H	H	2 - 77	1 - 76
1	19	MET	MET	ASP	ASP	D	D	2 - 79	1 - 78
2	19	MET	MET	ASP	ASP	E	E	2 - 79	1 - 78
1	20	MET	MET	ASP	ASP	D	D	2 - 79	1 - 78
2	20	MET	MET	ASP	ASP	F	F	2 - 79	1 - 78
1	21	MET	MET	ASP	ASP	D	D	2 - 79	1 - 78
2	21	MET	MET	ASP	ASP	G	G	2 - 79	1 - 78
1	22	MET	MET	ASP	ASP	D	D	2 - 79	1 - 78
2	22	MET	MET	ASP	ASP	H	H	2 - 79	1 - 78
1	23	MET	MET	ASP	ASP	E	E	2 - 79	1 - 78
2	23	MET	MET	ASP	ASP	F	F	2 - 79	1 - 78
1	24	MET	MET	ASP	ASP	E	E	2 - 79	1 - 78
2	24	MET	MET	ASP	ASP	G	G	2 - 79	1 - 78
1	25	MET	MET	ASP	ASP	E	E	2 - 79	1 - 78
2	25	MET	MET	ASP	ASP	H	H	2 - 79	1 - 78
1	26	MET	MET	ASP	ASP	F	F	2 - 79	1 - 78
2	26	MET	MET	ASP	ASP	G	G	2 - 79	1 - 78
1	27	MET	MET	ASP	ASP	F	F	2 - 79	1 - 78
2	27	MET	MET	ASP	ASP	H	H	2 - 79	1 - 78
1	28	MET	MET	ASP	ASP	G	G	2 - 79	1 - 78
2	28	MET	MET	ASP	ASP	H	H	2 - 79	1 - 78
1	29	ASN	ASN	PHE	PHE	I	I	23 - 113	5 - 95
2	29	ASN	ASN	PHE	PHE	J	J	23 - 113	5 - 95
1	30	ASN	ASN	PHE	PHE	I	I	23 - 113	5 - 95
2	30	ASN	ASN	PHE	PHE	K	K	23 - 113	5 - 95
1	31	GLU	GLU	GLY	GLY	I	I	24 - 112	6 - 94
2	31	GLU	GLU	GLY	GLY	L	L	24 - 112	6 - 94
1	32	ASN	ASN	PHE	PHE	I	I	23 - 113	5 - 95
2	32	ASN	ASN	PHE	PHE	M	M	23 - 113	5 - 95
1	33	ASN	ASN	PHE	PHE	I	I	23 - 113	5 - 95
2	33	ASN	ASN	PHE	PHE	N	N	23 - 113	5 - 95
1	34	ASN	ASN	PHE	PHE	I	I	23 - 113	5 - 95
2	34	ASN	ASN	PHE	PHE	O	O	23 - 113	5 - 95
1	35	ASN	ASN	PHE	PHE	I	I	23 - 113	5 - 95
2	35	ASN	ASN	PHE	PHE	P	P	23 - 113	5 - 95
1	36	ASN	ASN	PHE	PHE	J	J	23 - 113	5 - 95
2	36	ASN	ASN	PHE	PHE	K	K	23 - 113	5 - 95
1	37	GLU	GLU	GLY	GLY	J	J	24 - 112	6 - 94
2	37	GLU	GLU	GLY	GLY	L	L	24 - 112	6 - 94
1	38	ASN	ASN	PHE	PHE	J	J	23 - 113	5 - 95
2	38	ASN	ASN	PHE	PHE	M	M	23 - 113	5 - 95
1	39	ASN	ASN	PHE	PHE	J	J	23 - 113	5 - 95
2	39	ASN	ASN	PHE	PHE	N	N	23 - 113	5 - 95
1	40	ASN	ASN	PHE	PHE	J	J	23 - 113	5 - 95
2	40	ASN	ASN	PHE	PHE	O	O	23 - 113	5 - 95
1	41	ASN	ASN	PHE	PHE	J	J	23 - 113	5 - 95
2	41	ASN	ASN	PHE	PHE	P	P	23 - 113	5 - 95
1	42	GLU	GLU	GLY	GLY	K	K	24 - 112	6 - 94
2	42	GLU	GLU	GLY	GLY	L	L	24 - 112	6 - 94
1	43	ASN	ASN	PHE	PHE	K	K	23 - 113	5 - 95
2	43	ASN	ASN	PHE	PHE	M	M	23 - 113	5 - 95
1	44	ASN	ASN	PHE	PHE	K	K	23 - 113	5 - 95
2	44	ASN	ASN	PHE	PHE	N	N	23 - 113	5 - 95
1	45	ASN	ASN	PHE	PHE	K	K	23 - 113	5 - 95
2	45	ASN	ASN	PHE	PHE	O	O	23 - 113	5 - 95
1	46	ASN	ASN	PHE	PHE	K	K	23 - 113	5 - 95
2	46	ASN	ASN	PHE	PHE	P	P	23 - 113	5 - 95
1	47	GLU	GLU	GLY	GLY	L	L	24 - 112	6 - 94
2	47	GLU	GLU	GLY	GLY	M	M	24 - 112	6 - 94
1	48	GLU	GLU	GLY	GLY	L	L	24 - 112	6 - 94
2	48	GLU	GLU	GLY	GLY	N	N	24 - 112	6 - 94
1	49	GLU	GLU	GLY	GLY	L	L	24 - 112	6 - 94
2	49	GLU	GLU	GLY	GLY	O	O	24 - 112	6 - 94
1	50	GLU	GLU	GLY	GLY	L	L	24 - 112	6 - 94
2	50	GLU	GLU	GLY	GLY	P	P	24 - 112	6 - 94
1	51	ASN	ASN	PHE	PHE	M	M	23 - 113	5 - 95
2	51	ASN	ASN	PHE	PHE	N	N	23 - 113	5 - 95
1	52	ASN	ASN	PHE	PHE	M	M	23 - 113	5 - 95
2	52	ASN	ASN	PHE	PHE	O	O	23 - 113	5 - 95
1	53	ASN	ASN	PHE	PHE	M	M	23 - 113	5 - 95
2	53	ASN	ASN	PHE	PHE	P	P	23 - 113	5 - 95
1	54	ASN	ASN	PHE	PHE	N	N	23 - 113	5 - 95
2	54	ASN	ASN	PHE	PHE	O	O	23 - 113	5 - 95
1	55	ASN	ASN	PHE	PHE	N	N	23 - 113	5 - 95
2	55	ASN	ASN	PHE	PHE	P	P	23 - 113	5 - 95
1	56	ASN	ASN	PHE	PHE	O	O	23 - 113	5 - 95
2	56	ASN	ASN	PHE	PHE	P	P	23 - 113	5 - 95

NCS ensembles :

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Protein , 2 types, 16 molecules ABCDEFGHIJKLMNOP

#1: Protein	sHMAx Mass: 8614.323 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Setaria italica (foxtail millet) / Gene: SETIT_7G131600v2 / Production host: Escherichia coli (E. coli) / Strain (production host): SHuffle / References: UniProt: K3YDQ6
#2: Protein	APikL2F Mass: 10902.430 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pyricularia oryzae B157 (fungus) / Production host: Escherichia coli (E. coli) / Strain (production host): SHuffle

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Non-polymers , 5 types, 203 molecules

#3: Chemical	ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol Mass: 62.068 Da / Num. of mol.: 13 / Source method: obtained synthetically / Formula: C₂H₆O₂
#4: Chemical	ChemComp-1PE / PENTAETHYLENE GLYCOL / PEG400 / Polyethylene glycol Mass: 238.278 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₁₀H₂₂O₆ / Comment: precipitant*YM
#5: Chemical	ChemComp-CL / CHLORIDE ION / Chloride Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#6: Chemical	ChemComp-PEG / DI(HYDROXYETHYL)ETHER / Diethylene glycol Mass: 106.120 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₄H₁₀O₃
#7: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 186 / Source method: isolated from a natural source / Formula: H₂O

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Details

Has ligand of interest	N

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.35 Å³/Da / Density % sol: 47.62 %
Crystal grow	Temperature: 293.15 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 0.2 M lithium sulfate, 0.1 M BIS-TRIS pH 6.5, 25 % PEG3350

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Data collection

Diffraction	Mean temperature: 100 K / Serial crystal experiment: N
Diffraction source	Source: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.91188 Å
Detector	Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Oct 6, 2019
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.91188 Å / Relative weight: 1
Reflection	Resolution: 2.3→109.51 Å / Num. obs: 63610 / % possible obs: 99.9 % / Redundancy: 6.6 % / CC_1/2: 0.999 / R_rim(I) all: 0.087 / Net I/σ(I): 10.6
Reflection shell	Resolution: 2.3→2.36 Å / Num. unique obs: 4432 / CC_1/2: 0.756 / % possible all: 99.8

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Processing

Software

Name	Version	Classification
REFMAC	5.8.0267	refinement
Aimless		data scaling
PDB_EXTRACT	3.27	data extraction
autoPROC		data reduction
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 7NLJ

7nlj

Resolution: 2.3→109.51 Å / Cor.coef. F_o:F_c: 0.957 / Cor.coef. F_o:F_c free: 0.947 / SU B: 18.161 / SU ML: 0.202 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.394 / ESU R Free: 0.242 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.2425	3170	5 %	RANDOM
R_work	0.2074	-	-	-
obs	0.2092	60412	99.88 %	-

Solvent computation

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

Displacement parameters

B_iso max: 147.86 Å² / B_iso mean: 58.393 Å² / B_iso min: 29.43 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-2.56 Å²	-0 Å²	0 Å²
2-	-	-1.52 Å²	0 Å²
3-	-	-	4.09 Å²

Refinement step

Cycle: final / Resolution: 2.3→109.51 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	10600	0	92	186	10878
B_iso mean	-	-	73.81	51.66	-
Num. residues	-	-	-	-	1350

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.013	0.013	10987
X-RAY DIFFRACTION	r_bond_other_d	0.001	0.017	10776
X-RAY DIFFRACTION	r_angle_refined_deg	1.612	1.642	14812
X-RAY DIFFRACTION	r_angle_other_deg	1.317	1.592	24874
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	7.327	5	1352
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	31.858	21.83	519
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	16.869	15	1984
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	14.795	15	72
X-RAY DIFFRACTION	r_chiral_restr	0.072	0.2	1391
X-RAY DIFFRACTION	r_gen_planes_refined	0.008	0.02	12126
X-RAY DIFFRACTION	r_gen_planes_other	0.001	0.02	2398

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	2188	0.07
1	2	B	2188	0.07
2	1	A	2139	0.07
2	2	C	2139	0.07
3	1	A	2174	0.07
3	2	D	2174	0.07
4	1	A	2165	0.09
4	2	E	2165	0.09
5	1	A	2170	0.06
5	2	F	2170	0.06
6	1	A	2179	0.06
6	2	G	2179	0.06
7	1	A	2179	0.07
7	2	H	2179	0.07
8	1	B	2148	0.08
8	2	C	2148	0.08
9	1	B	2254	0.08
9	2	D	2254	0.08
10	1	B	2243	0.08
10	2	E	2243	0.08
11	1	B	2250	0.06
11	2	F	2250	0.06
12	1	B	2255	0.06
12	2	G	2255	0.06
13	1	B	2260	0.06
13	2	H	2260	0.06
14	1	C	2110	0.09
14	2	D	2110	0.09
15	1	C	2120	0.09
15	2	E	2120	0.09
16	1	C	2126	0.06
16	2	F	2126	0.06
17	1	C	2149	0.08
17	2	G	2149	0.08
18	1	C	2123	0.08
18	2	H	2123	0.08
19	1	D	2187	0.09
19	2	E	2187	0.09
20	1	D	2197	0.07
20	2	F	2197	0.07
21	1	D	2195	0.08
21	2	G	2195	0.08
22	1	D	2224	0.07
22	2	H	2224	0.07
23	1	E	2214	0.08
23	2	F	2214	0.08
24	1	E	2234	0.08
24	2	G	2234	0.08
25	1	E	2216	0.09
25	2	H	2216	0.09
26	1	F	2195	0.06
26	2	G	2195	0.06
27	1	F	2213	0.05
27	2	H	2213	0.05
28	1	G	2199	0.07
28	2	H	2199	0.07
29	1	I	2810	0.09
29	2	J	2810	0.09
30	1	I	2898	0.06
30	2	K	2898	0.06
31	1	I	2729	0.09
31	2	L	2729	0.09
32	1	I	2836	0.09
32	2	M	2836	0.09
33	1	I	2849	0.06
33	2	N	2849	0.06
34	1	I	2856	0.07
34	2	O	2856	0.07
35	1	I	2839	0.07
35	2	P	2839	0.07
36	1	J	2798	0.09
36	2	K	2798	0.09
37	1	J	2763	0.06
37	2	L	2763	0.06
38	1	J	2821	0.09
38	2	M	2821	0.09
39	1	J	2844	0.08
39	2	N	2844	0.08
40	1	J	2839	0.08
40	2	O	2839	0.08
41	1	J	2833	0.08
41	2	P	2833	0.08
42	1	K	2734	0.08
42	2	L	2734	0.08
43	1	K	2827	0.09
43	2	M	2827	0.09
44	1	K	2839	0.07
44	2	N	2839	0.07
45	1	K	2847	0.08
45	2	O	2847	0.08
46	1	K	2828	0.08
46	2	P	2828	0.08
47	1	L	2758	0.08
47	2	M	2758	0.08
48	1	L	2768	0.07
48	2	N	2768	0.07
49	1	L	2773	0.07
49	2	O	2773	0.07
50	1	L	2783	0.07
50	2	P	2783	0.07
51	1	M	2855	0.08
51	2	N	2855	0.08
52	1	M	2858	0.09
52	2	O	2858	0.09
53	1	M	2847	0.07
53	2	P	2847	0.07
54	1	N	2863	0.07
54	2	O	2863	0.07
55	1	N	2893	0.06
55	2	P	2893	0.06
56	1	O	2868	0.07
56	2	P	2868	0.07

LS refinement shell

Resolution: 2.3→2.36 Å / R_factor R_free error: 0 / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.307	215	-
R_work	0.307	4442	-
all	-	4657	-
obs	-	-	99.66 %

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	3.9421	-0.7046	-3.624	2.9597	-1.0523	4.5663	0.1588	0.0533	0.1099	-0.046	-0.1677	-0.1168	-0.4224	0.2252	0.0089	0.4355	-0.1589	-0.0206	0.2544	0.1141	0.2877	-30.871	-33.181	-4.494
2	4.561	-0.3105	-0.8418	4.2987	3.9391	3.7158	-0.1307	-0.0727	0.1527	0.1817	0.2341	-0.112	0.0729	0.325	-0.1034	0.3817	-0.1499	-0.0834	0.3411	0.0531	0.2704	-13.187	-43.62	-8.813
3	4.5204	0.2717	2.939	3.6801	0.4407	3.9699	0.212	-0.0297	-0.3429	-0.015	-0.0523	-0.0572	0.683	-0.3809	-0.1597	0.3436	-0.0839	-0.0061	0.2454	-0.0044	0.2201	-1.618	-22.185	-5.593
4	4.4418	-0.6236	0.9502	2.7528	-3.3459	4.2721	0.0094	-0.1857	0.0116	0.1845	0.004	0.0833	0.0635	-0.103	-0.0134	0.4344	-0.1226	0.0995	0.2811	0.0058	0.2118	-19.493	-11.806	-10.128
5	2.5828	0.256	1.6247	3.1412	0.0233	5.9916	-0.0089	-0.0265	-0.2691	-0.0102	-0.0532	0.1292	0.4186	0.3655	0.0621	0.1742	0.0456	-0.0036	0.1404	0.0224	0.0587	-61.077	-21.917	-43.229
6	4.2893	0.3201	0.8346	3.7506	2.3034	4.4938	0.0185	-0.0014	-0.125	-0.2282	0.0572	-0.3455	0.0164	0.3231	-0.0756	0.2118	-0.0068	0.1028	0.1311	-0.0184	0.0755	-43.604	-11.451	-38.616
7	4.4618	0.2518	-2.1053	3.2375	0.6018	5.7379	0.0759	-0.0795	0.2208	0.0892	-0.0377	0.0175	-0.4375	-0.3673	-0.0382	0.1406	-0.0027	0.0577	0.1174	-0.0264	0.1379	-32.419	-33.552	-42.566
8	4.3723	0.1152	-0.7336	4.2411	-2.642	4.8787	-0.0226	0.189	0.0691	-0.2531	0.068	0.0964	-0.1641	-0.1938	-0.0455	0.0808	0.0042	0.037	0.0832	0.0067	0.0921	-50.096	-44.026	-38.641
9	3.5182	-0.2037	0.2406	3.5415	-0.0323	4.9421	-0.1299	-0.3122	-0.1738	0.0331	-0.0676	0.141	-0.0079	-0.3037	0.1974	0.1461	0.0386	0.0186	0.0588	0.034	0.1599	-42.409	-42.723	8.9
10	2.073	-0.9263	-0.0225	6.2678	-0.6768	4.0059	0.0917	0.2317	-0.2117	0.0022	-0.1792	0.098	0.4454	0.3233	0.0874	0.1119	-0.008	0.0252	0.2906	-0.0548	0.2031	-15.721	-59.797	-20.636
11	4.5932	0.467	2.1804	2.3231	0.0998	6.9799	0.1445	-0.4504	0.1092	0.1781	-0.1309	-0.3126	0.1429	0.2069	-0.0136	0.229	0.0221	-0.0055	0.1107	-0.0156	0.2222	10.505	-12.527	7.354
12	3.5305	-1.6885	-0.2225	5.2181	0.8588	3.4373	0.072	0.1067	0.3694	-0.0539	-0.1471	-0.292	-0.2771	0.1107	0.075	0.1071	-0.0739	0.0141	0.2994	0.063	0.1852	-16.298	3.519	-22.623
13	3.4697	0.234	-0.3414	3.6673	0.0731	4.7399	0.1118	0.3371	0.0157	-0.2503	-0.0969	0.4866	0.0055	-0.3395	-0.0149	0.2003	-0.0289	-0.0857	0.0726	0.0031	0.081	-73.14	-13.498	-56.715
14	2.9888	1.1099	0.4201	4.8643	-1.1229	4.1023	0.0643	-0.23	0.4424	0.2256	-0.1032	0.0488	-0.5732	0.1358	0.0389	0.218	-0.0333	0.0778	0.2053	-0.0885	0.1158	-46.556	4.621	-26.822
15	4.4497	-0.81	-0.2257	3.7734	-0.1313	5.1908	0.1201	0.4796	-0.0837	-0.0432	-0.0977	-0.3522	0.1623	0.5567	-0.0225	0.1201	-0.0115	0.0585	0.1436	-0.0306	0.0747	-20.058	-42.565	-55.719
16	3.2233	1.0611	-0.7156	4.6628	0.6539	3.8438	0.1539	-0.2376	-0.4037	0.1072	-0.173	-0.3904	0.3626	0.2199	0.019	0.0628	0.0338	-0.0086	0.0884	0.0569	0.1099	-47.577	-60.04	-26.486

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	2 - 79
2	X-RAY DIFFRACTION	2	B	2 - 79
3	X-RAY DIFFRACTION	3	C	2 - 78
4	X-RAY DIFFRACTION	3	C	101
5	X-RAY DIFFRACTION	4	D	2 - 79
6	X-RAY DIFFRACTION	5	E	2 - 79
7	X-RAY DIFFRACTION	6	F	2 - 79
8	X-RAY DIFFRACTION	7	G	2 - 79
9	X-RAY DIFFRACTION	8	H	2 - 79
10	X-RAY DIFFRACTION	9	I	23 - 113
11	X-RAY DIFFRACTION	9	I	201 - 202
12	X-RAY DIFFRACTION	10	J	23 - 113
13	X-RAY DIFFRACTION	11	K	23 - 113
14	X-RAY DIFFRACTION	12	L	24 - 113
15	X-RAY DIFFRACTION	12	L	201
16	X-RAY DIFFRACTION	13	M	23 - 113
17	X-RAY DIFFRACTION	13	M	201
18	X-RAY DIFFRACTION	14	N	23 - 113
19	X-RAY DIFFRACTION	14	N	201
20	X-RAY DIFFRACTION	15	O	23 - 113
21	X-RAY DIFFRACTION	15	O	201
22	X-RAY DIFFRACTION	16	P	23 - 113

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