PDB-2f1m: Conformational flexibility in the multidrug efflux system protein AcrA

ID or keywords:

Entry

Database: PDB / ID: 2f1m

Title

Conformational flexibility in the multidrug efflux system protein AcrA

Components

Acriflavine resistance protein A

Keywords

TRANSPORT PROTEIN / helical hairpin / lipoyl domain / beta barrel

Function / homology

Function and homology information

alkane transmembrane transporter activity / alkane transport / xenobiotic detoxification by transmembrane export across the cell outer membrane / periplasmic side of plasma membrane / efflux pump complex / bile acid transmembrane transporter activity / xenobiotic transport / bile acid and bile salt transport / fatty acid transport / response to toxic substance ...
Similarity search - Function

Biological species

Escherichia coli (E. coli)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MAD / Resolution: 2.71 Å

Authors

Mikolosko, J. / Bobyk, K. / Zgurskaya, H.I. / Ghosh, P.

Citation

Journal: Structure / Year: 2006
Title: Conformational Flexibility in the Multidrug Efflux System Protein AcrA.
Authors: Mikolosko, J. / Bobyk, K. / Zgurskaya, H.I. / Ghosh, P.

History

Deposition	Nov 14, 2005	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Mar 21, 2006	Provider: repository / Type: Initial release
Revision 1.1	May 1, 2008	Group: Version format compliance
Revision 1.2	Jul 13, 2011	Group: Advisory / Version format compliance
Revision 1.3	Oct 18, 2017	Group: Advisory / Refinement description / Category: pdbx_unobs_or_zero_occ_atoms / software Item: _software.classification / _software.contact_author ..._software.classification / _software.contact_author / _software.contact_author_email / _software.date / _software.language / _software.location / _software.name / _software.type / _software.version
Revision 1.4	Oct 20, 2021	Group: Advisory / Database references / Derived calculations Category: database_2 / pdbx_unobs_or_zero_occ_atoms ...database_2 / pdbx_unobs_or_zero_occ_atoms / struct_conn / struct_ref_seq_dif Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _struct_ref_seq_dif.details
Revision 1.5	Nov 20, 2024	Group: Data collection / Refinement description / Structure summary Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature / struct_ncs_dom_lim Item: _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.end_auth_comp_id

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	2f1m.cif.gz	186.8 KB	Display	PDBx/mmCIF format
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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/f1/2f1m ftp://data.pdbj.org/pub/pdb/validation_reports/f1/2f1m	HTTPS FTP

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Related structure data

Similar structure data	4lc0-2 5okc-2 4lbv-2 4lbw-2 6m2l-d 2ixf-d 1h9d-d 4bla-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) Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#95 - Nov 2007 Multidrug Resistance Transporters similarity (8) #261 - Sep 2021 DNA-Sequencing Nanopores similarity (1) #22 - Oct 2001 Photosystem I similarity (1) #262 - Oct 2021 Fifty Years of Open Access to PDB Structures similarity (1) #29 - May 2002 Penicillin-binding Proteins similarity (1)

Deposited unit

A: Acriflavine resistance protein A

B: Acriflavine resistance protein A

C: Acriflavine resistance protein A

D: Acriflavine resistance protein A

121 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Acriflavine resistance protein A

B: Acriflavine resistance protein A

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

2

C: Acriflavine resistance protein A

D: Acriflavine resistance protein A

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

Unit cell

Length a, b, c (Å)	88.788, 100.031, 332.586
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	20
Space group name H-M	C222₁

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Dom-ID	Component-ID	Ens-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Refine code	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	1	THR	THR	ALA	ALA	6	A	A	54 - 62	11 - 19
2	1	1	THR	THR	ALA	ALA	6	B	B	54 - 62	11 - 19
3	1	1	THR	THR	ALA	ALA	6	C	C	54 - 62	11 - 19
4	1	1	THR	THR	ALA	ALA	6	D	D	54 - 62	11 - 19
1	1	2	ARG	ARG	ILE	ILE	3	A	A	64 - 96	21 - 53
2	1	2	ARG	ARG	ILE	ILE	3	B	B	64 - 96	21 - 53
3	1	2	ARG	ARG	ILE	ILE	3	C	C	64 - 96	21 - 53
4	1	2	ARG	ARG	ILE	ILE	3	D	D	64 - 96	21 - 53
1	1	3	ALA	ALA	LYS	LYS	5	A	A	99 - 131	56 - 88
2	1	3	ALA	ALA	LYS	LYS	5	B	B	99 - 131	56 - 88
3	1	3	ALA	ALA	LYS	LYS	5	C	C	99 - 131	56 - 88
4	1	3	ALA	ALA	LYS	LYS	5	D	D	99 - 131	56 - 88
5	2	3	GLN	GLN	LYS	LYS	4	A	A	141 - 175	98 - 132
6	2	3	GLN	GLN	LYS	LYS	4	B	B	141 - 175	98 - 132
7	2	3	GLN	GLN	LYS	LYS	4	C	C	141 - 175	98 - 132
8	2	3	GLN	GLN	LYS	LYS	4	D	D	141 - 175	98 - 132
1	1	4	VAL	VAL	GLN	GLN	3	A	A	176 - 208	133 - 165
2	1	4	VAL	VAL	GLN	GLN	3	B	B	176 - 208	133 - 165
3	1	4	VAL	VAL	GLN	GLN	3	C	C	176 - 208	133 - 165
4	1	4	VAL	VAL	GLN	GLN	3	D	D	176 - 208	133 - 165
1	1	5	LEU	LEU	GLN	GLN	5	A	A	209 - 218	166 - 175
2	1	5	LEU	LEU	GLN	GLN	5	B	B	209 - 218	166 - 175
3	1	5	LEU	LEU	GLN	GLN	5	C	C	209 - 218	166 - 175
4	1	5	LEU	LEU	GLN	GLN	5	D	D	209 - 218	166 - 175
1	1	6	ALA	ALA	ASP	ASP	5	A	A	242 - 257	199 - 214
2	1	6	ALA	ALA	ASP	ASP	5	B	B	242 - 257	199 - 214
3	1	6	GLY	GLY	ASP	ASP	5	C	C	240 - 257	197 - 214
4	1	6	GLY	GLY	ASP	ASP	5	D	D	240 - 257	197 - 214
1	1	7	THR	THR	LEU	LEU	5	A	A	275 - 297	232 - 254
2	1	7	THR	THR	LEU	LEU	5	B	B	275 - 297	232 - 254
3	1	7	THR	THR	LEU	LEU	5	C	C	275 - 297	232 - 254
4	1	7	THR	THR	LEU	LEU	5	D	D	275 - 297	232 - 254

NCS ensembles :

ID
1
2
3
4
5
6
7

Details

The current oligomerization state of AcrA is unknown.

#1: Protein	Acriflavine resistance protein A Mass: 30355.184 Da / Num. of mol.: 4 / Fragment: residues 45-312 / Mutation: F223M, L224M, L287M, L288M Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: JM109 / Gene: acrA, lir, mtcA / Plasmid: pET28b / Production host: Escherichia coli (E. coli) / Strain (production host): B834(DE3) / References: UniProt: P0AE06
#2: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 36 / 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: 3.17 Å³/Da / Density % sol: 61.2 %
Crystal grow	Temperature: 277 K / pH: 5.4 Details: 30% 2-methyl-2,4-pentadiol (MPD), 20 mM MgCl2, 100 mM citrate pH 5.4, 1 mM TCEP, VAPOR DIFFUSION, HANGING DROP, temperature 277K, pH 5.40

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Data collection

Diffraction

ID	Mean temperature (K)	Crystal-ID
1	100	1
2		1
3		1

Diffraction source

Source:

SYNCHROTRON / Site:

ALS

/ Beamline: 8.2.1 / Wavelength: 1

Detector

Type: ADSC QUANTUM 210 / Detector: CCD / Date: Nov 22, 2004

Radiation

Monochromator: DOUBLE CRYSTAL, SI(111) / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray

Radiation wavelength

Wavelength: 1 Å / Relative weight: 1

Reflection

D res low: 50 Å / % possible obs: 99.8

Redundancy (%)	ID	Number	R_merge(I) obs	Χ²	D res high (Å)
4.2	1	57352	0.139	1.032	3
4.4	2	41031	0.098	1.042	3.39
4.2	3	37276	0.185	1.049	3.5

Diffraction reflection shell

Highest resolution (Å)	Lowest resolution (Å)	% possible obs (%)	ID	R_merge(I) obs	Chi squared	Redundancy
6.46	50	98.4	1	0.04	1.035	4.3
5.13	6.46	100	1	0.084	1.007	4.4
4.48	5.13	100	1	0.087	1.028	4.4
4.07	4.48	100	1	0.126	1.029	4.4
3.78	4.07	100	1	0.191	1.04	4.5
3.56	3.78	100	1	0.246	1.043	4.4
3.38	3.56	99.9	1	0.364	1.062	4.3
3.23	3.38	99.9	1	0.517	1.037	4.1
3.11	3.23	99.9	1	0.637	1.015	3.8
3	3.11	99.7	1	0.716	1.016	3.4
7.3	50	98.2	2	0.034	1.034	4.3
5.79	7.3	100	2	0.066	1.037	4.4
5.06	5.79	100	2	0.074	1.038	4.4
4.6	5.06	100	2	0.077	1.057	4.5
4.27	4.6	100	2	0.094	1.063	4.5
4.02	4.27	100	2	0.131	1.068	4.5
3.82	4.02	100	2	0.171	1.038	4.5
3.65	3.82	100	2	0.207	1.045	4.5
3.51	3.65	99.9	2	0.277	1.03	4.5
3.39	3.51	99.9	2	0.389	1.008	4.5
7.53	50	98	3	0.046	1.048	4.3
5.98	7.53	100	3	0.134	1.068	4.3
5.23	5.98	99.9	3	0.171	1.055	4.4
4.75	5.23	100	3	0.164	1.038	4.4
4.41	4.75	100	3	0.207	1.063	4.3
4.15	4.41	100	3	0.254	1.054	4.2
3.94	4.15	100	3	0.31	1.033	4.1
3.77	3.94	100	3	0.394	1.045	4.1
3.63	3.77	99.9	3	0.446	1.059	3.9
3.5	3.63	99.9	3	0.534	1.019	3.8

Reflection

Resolution: 2.7→50 Å / Num. obs: 39324 / % possible obs: 97.3 % / Observed criterion σ(I): 1 / Redundancy: 5 % / R_merge(I) obs: 0.09 / Net I/σ(I): 14.6

Reflection shell

Resolution: 2.7→2.8 Å / Redundancy: 3.9 % / R_merge(I) obs: 0.429 / Mean I/σ(I) obs: 2.3 / % possible all: 91.1

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Phasing

Phasing

Method:

MAD

Phasing MAD set site

ID	Cartn x (Å)	Cartn y (Å)	Cartn z (Å)	Atom type symbol	B iso	Occupancy
1	28.608	-49.811	216.176	SE	300	1.61
2	24.466	-42.925	215.138	SE	225.17	1.39
3	63.967	13.111	51.932	SE	81.79	1.72
4	22.301	70.879	54.6	SE	109.95	1.84
5	-1.427	26.768	185.307	SE	188.64	0.96
6	10.503	41.748	65.087	SE	139.46	2.1
7	5.877	37.101	59.211	SE	89.52	1.85
8	6.438	41.562	64.423	SE	161.01	2.11
9	-34.291	30.375	192.897	SE	132.06	1.45
10	85.589	20.694	22.854	SE	120.19	1.95
11	5.439	77.612	29.71	SE	124.27	2.05
12	-9.197	23.051	185.722	SE	203.25	0.63
13	12.744	79.664	26.125	SE	132.56	2.26
14	26.196	18.131	21.567	SE	87.58	2.16
15	21.795	15.517	28.129	SE	91.69	2.17
16	25.733	14.311	22.663	SE	136.24	2.07
17	34.408	25.932	140.401	SE	117.85	1.85
18	25.694	18.182	110.017	SE	124.08	1.95
19	26.914	-10.026	229.861	SE	263.62	1.08

Phasing dm

Method: Solvent flattening and Histogram matching / Reflection: 30180

Phasing dm shell

Resolution (Å)	Delta phi final	FOM	Reflection
11.93-100	51.3	0.891	501
9.47-11.93	40	0.937	501
8.18-9.47	46.6	0.931	565
7.31-8.18	45.3	0.925	616
6.66-7.31	47.4	0.911	690
6.16-6.66	48.2	0.896	738
5.76-6.16	52.3	0.888	815
5.43-5.76	51.9	0.899	842
5.15-5.43	53.1	0.896	861
4.91-5.15	57.6	0.918	936
4.7-4.91	58.2	0.913	981
4.51-4.7	59.4	0.913	1002
4.35-4.51	62.6	0.919	1069
4.2-4.35	67.9	0.91	1046
4.07-4.2	68.1	0.895	1147
3.95-4.07	69.6	0.898	1133
3.83-3.95	74.9	0.91	1205
3.73-3.83	74.8	0.888	1184
3.64-3.73	76.1	0.89	1313
3.55-3.64	80.8	0.89	1238
3.47-3.55	81.9	0.867	1329
3.39-3.47	84.5	0.842	1332
3.32-3.39	86.3	0.799	1396
3.25-3.32	85.3	0.791	1388
3.19-3.25	86.5	0.749	1376
3.13-3.19	88.4	0.739	1504
3.07-3.13	90.2	0.71	1449
3-3.07	88.5	0.626	2023

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Processing

Software

Name	Version	Classification
DENZO		data reduction
SCALEPACK		data scaling
SHARP		phasing
DM	5	phasing
REFMAC		refinement
PDB_EXTRACT	1.701	data extraction
HKL-2000		data reduction
SHELXD		phasing

Refinement

Method to determine structure:

MAD / Resolution: 2.71→50 Å / Cor.coef. F_o:F_c: 0.928 / Cor.coef. F_o:F_c free: 0.905 / SU B: 29.458 / SU ML: 0.302 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.563 / ESU R Free: 0.331 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.275	1972	5 %	RANDOM
R_work	0.237	-	-	-
all	0.239	40642	-	-
obs	0.239	39271	96.7 %	-

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 mean: 60.96 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-6.28 Å²	0 Å²	0 Å²
2-	-	10.54 Å²	0 Å²
3-	-	-	-4.26 Å²

Refinement step

Cycle: LAST / Resolution: 2.71→50 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	6964	0	0	36	7000

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.01	0.022	6988
X-RAY DIFFRACTION	r_bond_other_d
X-RAY DIFFRACTION	r_angle_refined_deg	1.608	1.961	9506
X-RAY DIFFRACTION	r_angle_other_deg
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.967	5	916
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	40.727	25.369	298
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	19.903	15	1145
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	19.113	15	39
X-RAY DIFFRACTION	r_chiral_restr	0.098	0.2	1143
X-RAY DIFFRACTION	r_gen_planes_refined	0.004	0.02	5251
X-RAY DIFFRACTION	r_gen_planes_other
X-RAY DIFFRACTION	r_nbd_refined	0.206	0.2	2844
X-RAY DIFFRACTION	r_nbd_other
X-RAY DIFFRACTION	r_nbtor_refined	0.298	0.2	4811
X-RAY DIFFRACTION	r_nbtor_other
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.137	0.2	271
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	0.192	0.2	102
X-RAY DIFFRACTION	r_symmetry_vdw_other
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.155	0.2	15
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	0.352	1.5	4680
X-RAY DIFFRACTION	r_mcbond_other
X-RAY DIFFRACTION	r_mcangle_it	0.616	2	7368
X-RAY DIFFRACTION	r_scbond_it	1.062	3	2538
X-RAY DIFFRACTION	r_scangle_it	1.735	4.5	2138
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

Ens-ID	Dom-ID	Auth asym-ID	Number	Type	Rms dev position (Å)	Weight position
2	1	A	132	tight positional	0.04	0.05
2	2	B	132	tight positional	0.04	0.05
2	3	C	132	tight positional	0.04	0.05
2	4	D	132	tight positional	0.03	0.05
4	1	A	132	tight positional	0.04	0.05
4	2	B	132	tight positional	0.04	0.05
4	3	C	132	tight positional	0.05	0.05
4	4	D	132	tight positional	0.04	0.05
3	1	A	386	medium positional	0.53	0.5
3	2	B	386	medium positional	0.71	0.5
3	3	C	386	medium positional	0.73	0.5
3	4	D	386	medium positional	0.4	0.5
5	1	A	40	medium positional	0.47	0.5
5	2	B	40	medium positional	0.29	0.5
5	3	C	40	medium positional	0.39	0.5
5	4	D	40	medium positional	0.31	0.5
6	1	A	64	medium positional	0.74	0.5
6	2	B	64	medium positional	0.37	0.5
6	3	C	64	medium positional	0.4	0.5
6	4	D	64	medium positional	0.38	0.5
7	1	A	92	medium positional	0.42	0.5
7	2	B	92	medium positional	0.3	0.5
7	3	C	92	medium positional	0.33	0.5
7	4	D	92	medium positional	0.24	0.5
1	1	A	64	loose positional	0.65	5
1	2	B	64	loose positional	0.93	5
1	3	C	64	loose positional	0.55	5
1	4	D	64	loose positional	0.73	5
2	1	A	119	loose positional	0.49	5
2	2	B	119	loose positional	0.54	5
2	3	C	119	loose positional	0.55	5
2	4	D	119	loose positional	0.78	5
3	1	A	113	loose positional	0.64	5
3	2	B	113	loose positional	1.03	5
3	3	C	113	loose positional	0.84	5
3	4	D	113	loose positional	0.87	5
4	1	A	94	loose positional	0.47	5
4	2	B	94	loose positional	0.55	5
4	3	C	94	loose positional	0.47	5
4	4	D	94	loose positional	0.5	5
5	1	A	41	loose positional	0.75	5
5	2	B	41	loose positional	0.62	5
5	3	C	41	loose positional	0.84	5
5	4	D	41	loose positional	0.77	5
6	1	A	48	loose positional	1.78	5
6	2	B	48	loose positional	0.85	5
6	3	C	48	loose positional	0.89	5
6	4	D	48	loose positional	0.93	5
7	1	A	87	loose positional	1.06	5
7	2	B	87	loose positional	0.94	5
7	3	C	87	loose positional	0.67	5
7	4	D	87	loose positional	0.74	5
2	1	A	132	tight thermal	1.3	5
2	2	B	132	tight thermal	1.06	5
2	3	C	132	tight thermal	1.53	5
2	4	D	132	tight thermal	1.54	5
4	1	A	132	tight thermal	1.94	5
4	2	B	132	tight thermal	1.43	5
4	3	C	132	tight thermal	1.21	5
4	4	D	132	tight thermal	1.01	5
3	1	A	386	medium thermal	1.95	10
3	2	B	386	medium thermal	2.32	10
3	3	C	386	medium thermal	1.7	10
3	4	D	386	medium thermal	2.7	10
5	1	A	40	medium thermal	3.67	10
5	2	B	40	medium thermal	4.57	10
5	3	C	40	medium thermal	1.6	10
5	4	D	40	medium thermal	1.68	10
6	1	A	64	medium thermal	3.07	10
6	2	B	64	medium thermal	1.99	10
6	3	C	64	medium thermal	1.55	10
6	4	D	64	medium thermal	2.01	10
7	1	A	92	medium thermal	1.94	10
7	2	B	92	medium thermal	1.17	10
7	3	C	92	medium thermal	2.19	10
7	4	D	92	medium thermal	2.71	10
1	1	A	64	loose thermal	4.13	20
1	2	B	64	loose thermal	5.61	20
1	3	C	64	loose thermal	3.72	20
1	4	D	64	loose thermal	1.87	20
2	1	A	119	loose thermal	2.45	20
2	2	B	119	loose thermal	2.44	20
2	3	C	119	loose thermal	2.39	20
2	4	D	119	loose thermal	2.03	20
3	1	A	113	loose thermal	2.33	20
3	2	B	113	loose thermal	3.94	20
3	3	C	113	loose thermal	2.25	20
3	4	D	113	loose thermal	3.42	20
4	1	A	94	loose thermal	2.63	20
4	2	B	94	loose thermal	2.35	20
4	3	C	94	loose thermal	1.76	20
4	4	D	94	loose thermal	1.73	20
5	1	A	41	loose thermal	4.61	20
5	2	B	41	loose thermal	5.1	20
5	3	C	41	loose thermal	2.23	20
5	4	D	41	loose thermal	2.01	20
6	1	A	48	loose thermal	3.2	20
6	2	B	48	loose thermal	2.54	20
6	3	C	48	loose thermal	1.5	20
6	4	D	48	loose thermal	2.04	20
7	1	A	87	loose thermal	2.18	20
7	2	B	87	loose thermal	1.54	20
7	3	C	87	loose thermal	2.64	20
7	4	D	87	loose thermal	3.2	20

LS refinement shell

Resolution: 2.71→2.78 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.474	129	-
R_work	0.407	2329	-
obs	-	-	81.23 %

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	2.562	2.4472	-0.4488	10.7774	-3.9902	1.8074	0.0692	-0.2006	0.1223	0.5708	-0.0665	0.4914	-0.0531	-0.217	-0.0027	0.0801	-0.0339	0.0038	-0.1324	-0.0893	-0.2005	29.011	-5.386	205.401
2	3.3908	0.9159	-2.5457	5.5654	-4.1632	8.0337	0.2037	-0.645	0.2678	0.8945	-0.0598	0.1494	-0.6553	0.538	-0.144	0.1506	-0.0478	-0.0363	-0.1486	-0.1197	-0.0751	40.067	15.894	209.701
3	8.2369	-0.1482	2.9115	1.0435	-0.1698	3.642	0.1095	0.7262	-0.1144	-0.1238	0.1272	0.1301	0.049	0.3582	-0.2367	0.2054	-0.0244	-0.0092	-0.2589	-0.0187	-0.1574	0.822	25.506	210.613
4	3.9579	-0.4601	2.3699	2.3695	1.6332	12.0963	-0.0281	0.878	0.5831	0.0738	0.046	-0.352	-0.2836	1.3961	-0.0179	0.1596	-0.0587	0.0147	0.139	-0.0323	0.0604	23.48	34.449	210.513
5	1.5482	0.4783	2.6876	1.0104	0.6056	23.9938	-0.0308	0.5691	-0.2496	-0.2016	-0.0746	-0.1132	-0.241	-0.1786	0.1054	0.1341	0.0808	-0.009	-0.0554	-0.0849	-0.121	28.09	8.651	163.242
6	8.8767	0.4247	6.8518	1.5722	0.7199	12.5337	-0.2117	0.5125	0.9439	-0.4625	-0.4137	0.3815	-0.8996	-0.9579	0.6254	0.3556	0.2167	-0.057	-0.0559	0.0252	-0.0123	22.313	23.736	170.794
7	0.3455	0.206	-0.4816	0.2359	-1.9569	25.3273	0.029	-0.227	-0.0443	0.0402	0.0247	0.0229	0.2333	-0.1202	-0.0537	0.5034	0.2547	-0.0384	-0.0043	-0.0041	-0.134	8.214	21.72	254.005
8	4.4282	1.7297	-1.7076	4.2517	-3.3985	9.7834	-0.4546	-0.8131	-1.0649	0.7601	-0.3379	-0.6308	0.758	1.0963	0.7925	0.6189	0.4499	-0.0507	0.3435	0.016	0.0711	23.686	13.834	249.3
9	11.7577	-2.5657	-0.0489	4.5456	-5.0231	11.5825	0.2024	-1.2141	-1.9379	0.6637	0.4076	0.4072	1.6458	-1.6077	-0.61	0.6105	-0.3943	-0.0761	0.3682	0.2793	0.3031	20.626	-33.158	218.393
10	4.1812	-6.3858	-2.197	16.3897	-0.8767	11.5076	-0.8284	-0.7655	-2.0257	1.9822	0.2631	1.1369	2.1159	-0.4802	0.5653	1.099	0.0662	0.3878	0.3182	0.1822	0.5569	26.81	-1.237	230.757
11	19.2049	-0.2246	5.2274	4.2542	0.2926	5.1832	0.525	3.2075	-0.4871	-0.3444	-0.3133	0.0684	0.1913	0.1008	-0.2117	0.329	0.0148	-0.0261	0.4116	-0.0753	-0.0507	-24.977	22.447	193.837
12	30.1377	-6.9716	0.966	4.7573	0.2728	7.9805	0.1796	3.4496	-0.9604	-0.306	-0.4245	1.7079	0.007	-1.8178	0.2449	0.3455	0.0366	0.0071	1.148	-0.1998	0.1674	7.769	26.021	185.817

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	X-RAY DIFFRACTION	1	A	A	53 - 100	10 - 57
2	X-RAY DIFFRACTION	2	B	B	53 - 100	10 - 57
3	X-RAY DIFFRACTION	2	B	B	170 - 210	127 - 167
4	X-RAY DIFFRACTION	3	C	C	53 - 100	10 - 57
5	X-RAY DIFFRACTION	3	C	C	170 - 210	127 - 167
6	X-RAY DIFFRACTION	4	D	D	54 - 100	11 - 57
7	X-RAY DIFFRACTION	4	D	D	170 - 210	127 - 167
8	X-RAY DIFFRACTION	5	A	A	101 - 169	58 - 126
9	X-RAY DIFFRACTION	6	B	B	101 - 169	58 - 126
10	X-RAY DIFFRACTION	7	C	C	101 - 169	58 - 126
11	X-RAY DIFFRACTION	8	D	D	101 - 169	58 - 126
12	X-RAY DIFFRACTION	9	A	A	211 - 298	168 - 255
13	X-RAY DIFFRACTION	10	B	B	211 - 297	168 - 254
14	X-RAY DIFFRACTION	11	C	C	211 - 299	168 - 256
15	X-RAY DIFFRACTION	12	D	D	211 - 297	168 - 254

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