PDB-5akd: MutS in complex with the N-terminal domain of MutL - crystal form 3

ID or keywords:

Entry

Database: PDB / ID: 5akd

Title

MutS in complex with the N-terminal domain of MutL - crystal form 3

Components

DNA MISMATCH REPAIR PROTEIN MUTL
DNA MISMATCH REPAIR PROTEIN MUTS

Keywords

DNA BINDING PROTEIN / DNA MISMATCH REPAIR / COMPLEX / SLIDING CLAMP / CROSSLINKING

Function / homology

Function and homology information

single-stranded DNA-dependent ATP-dependent DNA helicase complex / mismatch repair involved in maintenance of fidelity involved in DNA-dependent DNA replication / adenine/cytosine mispair binding / MutS complex / mismatch repair complex / regulation of DNA recombination / nucleotide-excision repair, DNA duplex unwinding / mismatched DNA binding / DNA binding, bending / ATP-dependent DNA damage sensor activity ...
Similarity search - Function

DNA mismatch repair protein, MutL / MutL, C-terminal domain, regulatory subdomain / MutL C terminal dimerisation domain / DNA mismatch repair protein MutS / MutL, C-terminal, dimerisation / MutL, C-terminal domain superfamily / MutL, C-terminal domain, dimerisation subdomain / MutL C terminal dimerisation domain / DNA mismatch repair protein family, N-terminal / DNA mismatch repair protein, S5 domain 2-like ...
Similarity search - Domain/homology

Biological species

ESCHERICHIA COLI (E. coli)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 7.6 Å

Authors

Groothuizen, F.S. / Winkler, I. / Cristovao, M. / Fish, A. / Winterwerp, H.H.K. / Reumer, A. / Marx, A.D. / Hermans, N. / Nicholls, R.A. / Murshudov, G.N. ...

Citation

Journal: Elife / Year: 2015
Title: MutS/MutL crystal structure reveals that the MutS sliding clamp loads MutL onto DNA.
Authors: Groothuizen, F.S. / Winkler, I. / Cristovao, M. / Fish, A. / Winterwerp, H.H. / Reumer, A. / Marx, A.D. / Hermans, N. / Nicholls, R.A. / Murshudov, G.N. / Lebbink, J.H. / Friedhoff, P. / Sixma, T.K.

History

Deposition	Mar 3, 2015	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Jul 22, 2015	Provider: repository / Type: Initial release
Revision 1.1	Feb 27, 2019	Group: Data collection / Database references / Other Category: citation / citation_author ...citation / citation_author / database_PDB_rev / database_PDB_rev_record / pdbx_database_proc / pdbx_database_status Item: _citation.page_first / _citation.page_last ..._citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.title / _citation_author.name / _pdbx_database_status.recvd_author_approval
Revision 1.2	Jan 10, 2024	Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / struct_ncs_dom_lim / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _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

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	5akd.cif.gz	2.3 MB	Display	PDBx/mmCIF format
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Validation report

Summary document	5akd_validation.pdf.gz	1.7 MB	Display	wwPDB validaton report
Full document	5akd_full_validation.pdf.gz	1.9 MB	Display
Data in XML	5akd_validation.xml.gz	198.8 KB	Display
Data in CIF	5akd_validation.cif.gz	261 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/ak/5akd ftp://data.pdbj.org/pub/pdb/validation_reports/ak/5akd	HTTPS FTP

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Related structure data

Related structure data	5akbC 5akcC 1bknS 1w7aS C: citing same article (ref.) S: Starting model for refinement
Similar structure data	5akc-2 5akc-3 5akc-1 5akb-1 6wpa-d 0901 11579 4gx5-1 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

Related structure data

C: citing same article (ref.)

S: Starting model for refinement

Similar structure data

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#150 - Jun 2012 Sliding Clamps similarity (1) #108 - Dec 2008 Hsp90 similarity (1) #168 - Dec 2013 DNA Helicase similarity (1) #182 - Feb 2015 Insulin receptor similarity (1) #214 - Oct 2017 Chimeric Antigen Receptors similarity (1) #238 - Oct 2019 Ribonucleotide Reductase similarity (1) #43 - Jul 2003 Src Tyrosine Kinase similarity (1) #50 - Feb 2004 Glycolytic Enzymes similarity (1) #60 - Dec 2004 Ubiquitin similarity (1) #73 - Jan 2006 Topoisomerase similarity (1) #80 - Aug 2006 AAA+ Proteases similarity (1) #95 - Nov 2007 Multidrug Resistance Transporters similarity (1)

PDB pages

PDBj /

wwPDB /

NCBI

Related items in Molecule of the Month

#150 - Jun 2012
Sliding Clamps
similarity (1)
#108 - Dec 2008
Hsp90
similarity (1)
#168 - Dec 2013
DNA Helicase
similarity (1)
#182 - Feb 2015
Insulin receptor
similarity (1)
#214 - Oct 2017
Chimeric Antigen Receptors
similarity (1)
#238 - Oct 2019
Ribonucleotide Reductase
similarity (1)
#43 - Jul 2003
Src Tyrosine Kinase
similarity (1)
#50 - Feb 2004
Glycolytic Enzymes
similarity (1)
#60 - Dec 2004
Ubiquitin
similarity (1)
#73 - Jan 2006
Topoisomerase
similarity (1)
#80 - Aug 2006
AAA+ Proteases
similarity (1)
#95 - Nov 2007
Multidrug Resistance Transporters
similarity (1)

Deposited unit

A: DNA MISMATCH REPAIR PROTEIN MUTS

B: DNA MISMATCH REPAIR PROTEIN MUTS

C: DNA MISMATCH REPAIR PROTEIN MUTL

D: DNA MISMATCH REPAIR PROTEIN MUTL

E: DNA MISMATCH REPAIR PROTEIN MUTS

F: DNA MISMATCH REPAIR PROTEIN MUTS

G: DNA MISMATCH REPAIR PROTEIN MUTL

H: DNA MISMATCH REPAIR PROTEIN MUTL

I: DNA MISMATCH REPAIR PROTEIN MUTS

J: DNA MISMATCH REPAIR PROTEIN MUTS

K: DNA MISMATCH REPAIR PROTEIN MUTL

L: DNA MISMATCH REPAIR PROTEIN MUTL

hetero molecules

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

1

A: DNA MISMATCH REPAIR PROTEIN MUTS

B: DNA MISMATCH REPAIR PROTEIN MUTS

C: DNA MISMATCH REPAIR PROTEIN MUTL

D: DNA MISMATCH REPAIR PROTEIN MUTL

hetero molecules

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

2

E: DNA MISMATCH REPAIR PROTEIN MUTS

F: DNA MISMATCH REPAIR PROTEIN MUTS

G: DNA MISMATCH REPAIR PROTEIN MUTL

H: DNA MISMATCH REPAIR PROTEIN MUTL

hetero molecules

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

3

I: DNA MISMATCH REPAIR PROTEIN MUTS

J: DNA MISMATCH REPAIR PROTEIN MUTS

K: DNA MISMATCH REPAIR PROTEIN MUTL

L: DNA MISMATCH REPAIR PROTEIN MUTL

hetero molecules

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

Unit cell

Length a, b, c (Å)	193.020, 109.762, 275.841
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	4
Space group name H-M	P12₁1

Noncrystallographic symmetry (NCS)

NCS domain:
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	ARG	ARG	SER	SER	A	A	128 - 800	128 - 800
2	1	ARG	ARG	SER	SER	B	B	128 - 800	128 - 800
1	2	ARG	ARG	SER	SER	A	A	128 - 800	128 - 800
2	2	ARG	ARG	SER	SER	E	E	128 - 800	128 - 800
1	3	ARG	ARG	SER	SER	A	A	128 - 800	128 - 800
2	3	ARG	ARG	SER	SER	F	F	128 - 800	128 - 800
1	4	ARG	ARG	SER	SER	A	A	128 - 800	128 - 800
2	4	ARG	ARG	SER	SER	I	I	128 - 800	128 - 800
1	5	ARG	ARG	SER	SER	A	A	128 - 800	128 - 800
2	5	ARG	ARG	SER	SER	J	J	128 - 800	128 - 800
1	6	ARG	ARG	SER	SER	B	B	128 - 800	128 - 800
2	6	ARG	ARG	SER	SER	E	E	128 - 800	128 - 800
1	7	ARG	ARG	SER	SER	B	B	128 - 800	128 - 800
2	7	ARG	ARG	SER	SER	F	F	128 - 800	128 - 800
1	8	ARG	ARG	SER	SER	B	B	128 - 800	128 - 800
2	8	ARG	ARG	SER	SER	I	I	128 - 800	128 - 800
1	9	ARG	ARG	SER	SER	B	B	128 - 800	128 - 800
2	9	ARG	ARG	SER	SER	J	J	128 - 800	128 - 800
1	10	VAL	VAL	GLN	GLN	C	C	20 - 331	40 - 351
2	10	VAL	VAL	GLN	GLN	D	D	20 - 331	40 - 351
1	11	VAL	VAL	GLN	GLN	C	C	20 - 331	40 - 351
2	11	VAL	VAL	GLN	GLN	G	G	20 - 331	40 - 351
1	12	VAL	VAL	GLN	GLN	C	C	20 - 331	40 - 351
2	12	VAL	VAL	GLN	GLN	H	H	20 - 331	40 - 351
1	13	VAL	VAL	GLN	GLN	C	C	20 - 331	40 - 351
2	13	VAL	VAL	GLN	GLN	K	K	20 - 331	40 - 351
1	14	VAL	VAL	GLN	GLN	C	C	20 - 331	40 - 351
2	14	VAL	VAL	GLN	GLN	L	L	20 - 331	40 - 351
1	15	VAL	VAL	GLN	GLN	D	D	20 - 331	40 - 351
2	15	VAL	VAL	GLN	GLN	G	G	20 - 331	40 - 351
1	16	VAL	VAL	GLN	GLN	D	D	20 - 331	40 - 351
2	16	VAL	VAL	GLN	GLN	H	H	20 - 331	40 - 351
1	17	VAL	VAL	GLN	GLN	D	D	20 - 331	40 - 351
2	17	VAL	VAL	GLN	GLN	K	K	20 - 331	40 - 351
1	18	VAL	VAL	GLN	GLN	D	D	20 - 331	40 - 351
2	18	VAL	VAL	GLN	GLN	L	L	20 - 331	40 - 351
1	19	ARG	ARG	SER	SER	E	E	128 - 800	128 - 800
2	19	ARG	ARG	SER	SER	F	F	128 - 800	128 - 800
1	20	ARG	ARG	SER	SER	E	E	128 - 800	128 - 800
2	20	ARG	ARG	SER	SER	I	I	128 - 800	128 - 800
1	21	ARG	ARG	SER	SER	E	E	128 - 800	128 - 800
2	21	ARG	ARG	SER	SER	J	J	128 - 800	128 - 800
1	22	ARG	ARG	SER	SER	F	F	128 - 800	128 - 800
2	22	ARG	ARG	SER	SER	I	I	128 - 800	128 - 800
1	23	ARG	ARG	SER	SER	F	F	128 - 800	128 - 800
2	23	ARG	ARG	SER	SER	J	J	128 - 800	128 - 800
1	24	VAL	VAL	GLN	GLN	G	G	20 - 331	40 - 351
2	24	VAL	VAL	GLN	GLN	H	H	20 - 331	40 - 351
1	25	VAL	VAL	GLN	GLN	G	G	20 - 331	40 - 351
2	25	VAL	VAL	GLN	GLN	K	K	20 - 331	40 - 351
1	26	VAL	VAL	GLN	GLN	G	G	20 - 331	40 - 351
2	26	VAL	VAL	GLN	GLN	L	L	20 - 331	40 - 351
1	27	VAL	VAL	GLN	GLN	H	H	20 - 331	40 - 351
2	27	VAL	VAL	GLN	GLN	K	K	20 - 331	40 - 351
1	28	VAL	VAL	GLN	GLN	H	H	20 - 331	40 - 351
2	28	VAL	VAL	GLN	GLN	L	L	20 - 331	40 - 351
1	29	ARG	ARG	SER	SER	I	I	128 - 800	128 - 800
2	29	ARG	ARG	SER	SER	J	J	128 - 800	128 - 800
1	30	VAL	VAL	GLN	GLN	K	K	20 - 331	40 - 351
2	30	VAL	VAL	GLN	GLN	L	L	20 - 331	40 - 351

NCS ensembles :

Details

IN THIS STRUCTURE SINGLE CYSTEINES IN MUTS AND THE LN40 DOMAIN OF MUTL HAVE BEEN PLACED SUCH THAT CROSSLINKING OCCURS ONLY IN THE PRESENCE OF A DNA MISMATCH AND A NUCLEOTIDE (SEE WINKLER ET AL 2011, JBC). TO OBTAIN HOMOGENEOUS MATERIAL BOTH MUTS SUBUNITS HAVE BEEN CROSSLINKED TO A MUTL(LN40), WHEREAS FOR BIOLOGICAL FUNCTION ONLY ONE MUTL PER MUTS DIMER IS REQUIRED.

#1: Protein	DNA MISMATCH REPAIR PROTEIN MUTS Mass: 89476.086 Da / Num. of mol.: 6 / Mutation: YES Source method: isolated from a genetically manipulated source Details: BM(PEO)3 (THIOETHER) CROSSLINK BETWEEN A 246 AND D 131, B 246 AND C 131, E 246 AND H 131, F 246 AND G 131, I 246 AND L 131, J 246 AND K 131 Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Strain: K-12 / Production host: ESCHERICHIA COLI B (bacteria) / Strain (production host): B834(DE3) / Variant (production host): PLYSS / References: UniProt: P23909
#2: Protein	DNA MISMATCH REPAIR PROTEIN MUTL Mass: 41275.738 Da / Num. of mol.: 6 / Fragment: N-TERMINAL DOMAIN, RESIDUES 1-349 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Strain: K-12 / Production host: ESCHERICHIA COLI BL21(DE3) (bacteria) / References: UniProt: P23367
#3: Chemical	ChemComp-ANP / PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER Mass: 506.196 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C₁₀H₁₇N₆O₁₂P₃ / Comment: AMP-PNP, energy-carrying molecule analogue*YM
Sequence details	NATIVE CYSTEINES REPLACED AND ONE CYSTEINE INTRODUCED N-TERMINAL HIS-TAG. NATIVE CYSTEINES REPLACED ...NATIVE CYSTEINES REPLACED AND ONE CYSTEINE INTRODUCED N-TERMINAL HIS-TAG. NATIVE CYSTEINES REPLACED AND ONE CYSTEINE INTRODUCED

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 3.72 Å³/Da / Density % sol: 68 % / Description: NONE
Crystal grow	Details: 9-12% PEG8000, 100 MM TRIS PH 7.0, 200 MM MGCL2, 80-450 MM SODIUM MALONATE

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 0.97796
Detector	Type: DECTRIS PILATUS 2MF / Detector: PIXEL / Date: Oct 12, 2013
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.97796 Å / Relative weight: 1
Reflection	Resolution: 7.6→49.3 Å / Num. obs: 11763 / % possible obs: 81.3 % / Observed criterion σ(I): 1 / Redundancy: 2.3 % / R_merge(I) obs: 0.17 / Net I/σ(I): 4.3
Reflection shell	Resolution: 7.6→8.5 Å / Redundancy: 2.2 % / R_merge(I) obs: 0.92 / Mean I/σ(I) obs: 1 / % possible all: 82.5

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Processing

Software

Name	Version	Classification
REFMAC	5.8.0107	refinement
XDS		data reduction
Aimless		data scaling
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB ENTRIES 1W7A, 1BKN

1w7a

1bkn

Resolution: 7.6→275.84 Å / Cor.coef. F_o:F_c: 0.844 / Cor.coef. F_o:F_c free: 0.814 / SU ML: 5.398 / Cross valid method: THROUGHOUT / ESU R Free: 5.118 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: U VALUES WITH TLS ADDED. RESIDUES ABEFIJ1-127, ABEFIJ660-669, CDGHKLF1-19, CDGHKLF74-79, CDGHKLF126-131, CDGHKL300-314, CDGHKL332- -349 ARE DISORDERED. CROSSLINKER BMPEO3 IS DISORDERED. IN ...

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.30604	585	5 %	RANDOM
R_work	0.26378	-	-	-
obs	0.26591	11165	80.11 %	-

Solvent computation

Ion probe radii: 0.7 Å / Shrinkage radii: 0.7 Å / VDW probe radii: 1.3 Å / Solvent model: MASK

Displacement parameters

B_iso mean: 231.338 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	14.07 Å²	0 Å²	-6.53 Å²
2-	-	6.19 Å²	0 Å²
3-	-	-	-20.26 Å²

Refinement step

Cycle: LAST / Resolution: 7.6→275.84 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	44868	0	186	0	45054

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.014	0.019	45792
X-RAY DIFFRACTION	r_bond_other_d
X-RAY DIFFRACTION	r_angle_refined_deg	1.441	1.976	62016
X-RAY DIFFRACTION	r_angle_other_deg
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.409	5	5652
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	34.102	23.288	2190
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	16.108	15	8070
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	14.214	15	486
X-RAY DIFFRACTION	r_chiral_restr	0.088	0.2	7080
X-RAY DIFFRACTION	r_gen_planes_refined	0.007	0.021	34494
X-RAY DIFFRACTION	r_gen_planes_other
X-RAY DIFFRACTION	r_nbd_refined
X-RAY DIFFRACTION	r_nbd_other
X-RAY DIFFRACTION	r_nbtor_refined
X-RAY DIFFRACTION	r_nbtor_other
X-RAY DIFFRACTION	r_xyhbond_nbd_refined
X-RAY DIFFRACTION	r_xyhbond_nbd_other
X-RAY DIFFRACTION	r_metal_ion_refined
X-RAY DIFFRACTION	r_metal_ion_other
X-RAY DIFFRACTION	r_symmetry_vdw_refined
X-RAY DIFFRACTION	r_symmetry_vdw_other
X-RAY DIFFRACTION	r_symmetry_hbond_refined
X-RAY DIFFRACTION	r_symmetry_hbond_other
X-RAY DIFFRACTION	r_symmetry_metal_ion_refined
X-RAY DIFFRACTION	r_symmetry_metal_ion_other
X-RAY DIFFRACTION	r_mcbond_it
X-RAY DIFFRACTION	r_mcbond_other
X-RAY DIFFRACTION	r_mcangle_it
X-RAY DIFFRACTION	r_mcangle_other
X-RAY DIFFRACTION	r_scbond_it
X-RAY DIFFRACTION	r_scbond_other
X-RAY DIFFRACTION	r_scangle_it
X-RAY DIFFRACTION	r_scangle_other
X-RAY DIFFRACTION	r_long_range_B_refined
X-RAY DIFFRACTION	r_long_range_B_other
X-RAY DIFFRACTION	r_rigid_bond_restr
X-RAY DIFFRACTION	r_sphericity_free
X-RAY DIFFRACTION	r_sphericity_bonded

Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-ID	Dom-ID	Auth asym-ID	Number	Rms dev position (Å)
1	1	A	1786	0.03
1	2	B	1786	0.03
2	1	A	1782	0.05
2	2	E	1782	0.05
3	1	A	1786	0.05
3	2	F	1786	0.05
4	1	A	1794	0.03
4	2	I	1794	0.03
5	1	A	1786	0.05
5	2	J	1786	0.05
6	1	B	1788	0.04
6	2	E	1788	0.04
7	1	B	1794	0.04
7	2	F	1794	0.04
8	1	B	1794	0.02
8	2	I	1794	0.02
9	1	B	1782	0.04
9	2	J	1782	0.04
10	1	C	742	0.02
10	2	D	742	0.02
11	1	C	760	0.06
11	2	G	760	0.06
12	1	C	752	0.06
12	2	H	752	0.06
13	1	C	774	0.03
13	2	K	774	0.03
14	1	C	766	0.01
14	2	L	766	0.01
15	1	D	736	0.05
15	2	G	736	0.05
16	1	D	736	0.05
16	2	H	736	0.05
17	1	D	744	0.01
17	2	K	744	0.01
18	1	D	740	0.01
18	2	L	740	0.01
19	1	E	1802	0.03
19	2	F	1802	0.03
20	1	E	1784	0.03
20	2	I	1784	0.03
21	1	E	1796	0.02
21	2	J	1796	0.02
22	1	F	1798	0.03
22	2	I	1798	0.03
23	1	F	1794	0.01
23	2	J	1794	0.01
24	1	G	760	0.01
24	2	H	760	0.01
25	1	G	766	0.06
25	2	K	766	0.06
26	1	G	762	0.06
26	2	L	762	0.06
27	1	H	760	0.06
27	2	K	760	0.06
28	1	H	758	0.06
28	2	L	758	0.06
29	1	I	1784	0.03
29	2	J	1784	0.03
30	1	K	776	0.01
30	2	L	776	0.01

LS refinement shell

Resolution: 7.601→7.798 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.372	36	-
R_work	0.342	850	-
obs	-	-	82.73 %

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	6.1589	-0.6871	-1.0543	3.3522	2.271	3.9883	0.4273	0.4109	0.0614	-0.1733	-0.2445	0.1955	-0.4879	0.0793	-0.1828	0.6835	0.5368	0.9153	1.5214	0.2682	1.5855	-33.7981	38.9187	-90.6614
2	3.4613	-0.5336	1.3211	2.5232	0.7682	4.5231	-0.1643	-0.603	-0.4981	0.7076	0.4306	0.0985	0.9767	0.4261	-0.2663	0.9875	0.3365	0.9842	1.7116	0.0023	1.6191	-37.9697	12.5097	-78.5962
3	5.6166	-2.0394	-1.3066	8.5703	0.1791	3.2323	0.1789	0.0154	0.1769	-0.1423	-0.1026	0.5491	0.0707	0.2106	-0.0764	2.2542	0.0777	-0.1254	2.1355	-0.5636	1.5659	-22.0091	60.6161	-53.7386
4	3.4378	1.4842	1.6763	6.3172	-1.3524	4.1763	0.5984	0.3316	-0.3406	0.4266	-0.2249	0.9215	0.8718	0.0678	-0.3736	2.169	0.2849	0.0863	2.2419	-0.5404	1.5498	-35.2306	-11.3869	-115.2499
5	5.3713	-0.3412	2.9351	5.0401	-2.9162	4.7653	0.8754	0.5485	0.475	-0.7503	-0.3361	0.4356	1.3231	1.2273	-0.5393	0.982	0.3139	0.9391	2.8989	0.0435	1.943	-46.9263	11.3821	-182.3373
6	2.3112	-0.5673	1.6365	2.1933	-1.8235	5.446	0.0644	-0.3745	-0.0211	0.8282	0.4266	-0.103	-0.564	-0.6885	-0.4911	0.5798	0.0832	0.5654	2.0867	0.0869	1.6953	-67.312	28.1908	-170.0587
7	7.204	2.0849	1.0168	2.1611	0.7212	1.8693	0.2787	0.4126	0.6137	0.4646	0.0722	-0.4697	0.6391	-0.1988	-0.3509	2.5567	0.0977	-0.0565	2.3363	0.113	2.1093	-33.6126	-9.7729	-145.6677
8	10.4126	4.1225	-4.014	6.0502	-3.7588	7.1261	-0.0637	0.1134	-0.3204	0.4221	-0.1746	0.0962	0.0646	-0.942	0.2383	1.2532	0.0766	-0.2014	2.7749	0.7044	1.1773	-89.4866	38.4637	-206.6772
9	2.031	0.4753	0.0941	2.5279	0.1671	3.7304	-0.0147	-0.07	-0.5765	0.809	0.5457	-0.4596	0.4822	0.7033	-0.531	2.2782	0.2823	0.6247	2.0337	-0.4353	2.0369	-40.424	45.4377	-261.9058
10	1.6222	-1.053	0.4884	6.6132	-0.6944	3.8752	0.5819	-0.2374	0.0286	-0.5826	-0.2582	0.247	0.6771	-0.4089	-0.3237	2.369	-0.0303	0.0591	2.1802	-0.0197	1.2739	-65.8281	36.8086	-274.0381
11	6.9673	-1.6618	0.4695	7.8743	-0.9171	1.9754	0.3143	-0.6574	-1.1199	0.134	-0.4309	-0.0115	-1.6041	0.6637	0.1166	2.5216	0.1577	0.2125	2.388	-0.2783	1.4087	-20.2504	59.3752	-299.0967
12	3.4751	1.5633	-0.652	5.7962	0.4796	1.4855	-0.4053	0.1806	-0.1573	-0.1594	0.4667	-0.021	-0.1482	-0.4059	-0.0614	2.4952	0.003	0.0034	2.9511	0.4413	1.7919	-89.9353	37.1556	-236.7281

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	128 - 1802
2	X-RAY DIFFRACTION	2	B	128 - 1802
3	X-RAY DIFFRACTION	3	C	20 - 331
4	X-RAY DIFFRACTION	4	D	20 - 331
5	X-RAY DIFFRACTION	5	E	128 - 1802
6	X-RAY DIFFRACTION	6	F	128 - 1802
7	X-RAY DIFFRACTION	7	G	20 - 331
8	X-RAY DIFFRACTION	8	H	20 - 331
9	X-RAY DIFFRACTION	9	I	128 - 1802
10	X-RAY DIFFRACTION	10	J	128 - 1802
11	X-RAY DIFFRACTION	11	K	20 - 331
12	X-RAY DIFFRACTION	12	L	20 - 331

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