PDB-3e1l: Crystal structure of E. coli Bacterioferritin (BFR) soaked in pho...

ID or keywords:

Entry

Database: PDB / ID: 3e1l

Title

Crystal structure of E. coli Bacterioferritin (BFR) soaked in phosphate with an alternative conformation of the unoccupied Ferroxidase centre (APO-BFR II).

Components

BACTERIOFERRITIN

Keywords

METAL BINDING PROTEIN / BACTERIOFERRITIN. RHOMBIC DODECAHEDRAL SUPERSTRUCTURE / HEME / IRON / IRON STORAGE / METAL-BINDING

Function / homology

Function and homology information

ferrous iron transmembrane transporter activity / iron ion sequestering activity / ferroxidase / : / ferroxidase activity / ferric iron binding / oxidoreductase activity / iron ion binding / heme binding / protein homodimerization activity ...
Similarity search - Function

Biological species

ESCHERICHIA COLI (E. coli)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.5 Å

Authors

Crow, A. / Lawson, T. / Lewin, A. / Moore, G.R. / Le Brun, N.

Citation

Journal: J.Am.Chem.Soc. / Year: 2009
Title: Structural basis for iron mineralization by bacterioferritin
Authors: Crow, A. / Lawson, T.L. / Lewin, A. / Moore, G.R. / Le Brun, N.E.

History

Deposition	Aug 4, 2008	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	May 5, 2009	Provider: repository / Type: Initial release
Revision 1.1	Jul 13, 2011	Group: Version format compliance
Revision 1.2	Aug 30, 2023	Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn / 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 / _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_conn.ptnr2_label_seq_id / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

Remark 650

HELIX DETERMINATION METHOD: AUTHOR

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	3e1l.cif.gz	399.8 KB	Display	PDBx/mmCIF format
PDB format	pdb3e1l.ent.gz	331.8 KB	Display	PDB format
PDBx/mmJSON format	3e1l.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Summary document	3e1l_validation.pdf.gz	2.4 MB	Display	wwPDB validaton report
Full document	3e1l_full_validation.pdf.gz	2.4 MB	Display
Data in XML	3e1l_validation.xml.gz	72 KB	Display
Data in CIF	3e1l_validation.cif.gz	93.1 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/e1/3e1l ftp://data.pdbj.org/pub/pdb/validation_reports/e1/3e1l	HTTPS FTP

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Related structure data

Related structure data	3e1jC 3e1mC 3e1nC 3e1oC 3e1pC 2qp7 PDB Unreleased entryS 3e1q C: citing same article (ref.) S: Starting model for refinement
Similar structure data	7k5e-1 6nlk-1 3is7-d 7k5h-1 3e1o-1 5zur-1 4tog-1 4toa-d 4xkt-1 5d8q-1 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	#35 - Nov 2002 Ferritin and Transferrin similarity (6) #114 - Jun 2009 Vaults similarity (1) #57 - Sep 2004 Catalase similarity (1)

Deposited unit

A: BACTERIOFERRITIN

B: BACTERIOFERRITIN

C: BACTERIOFERRITIN

D: BACTERIOFERRITIN

E: BACTERIOFERRITIN

F: BACTERIOFERRITIN

G: BACTERIOFERRITIN

H: BACTERIOFERRITIN

I: BACTERIOFERRITIN

J: BACTERIOFERRITIN

K: BACTERIOFERRITIN

L: BACTERIOFERRITIN

hetero molecules

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

1

A: BACTERIOFERRITIN

B: BACTERIOFERRITIN

C: BACTERIOFERRITIN

D: BACTERIOFERRITIN

E: BACTERIOFERRITIN

F: BACTERIOFERRITIN

G: BACTERIOFERRITIN

H: BACTERIOFERRITIN

I: BACTERIOFERRITIN

J: BACTERIOFERRITIN

K: BACTERIOFERRITIN

L: BACTERIOFERRITIN

hetero molecules

A: BACTERIOFERRITIN

B: BACTERIOFERRITIN

C: BACTERIOFERRITIN

D: BACTERIOFERRITIN

E: BACTERIOFERRITIN

F: BACTERIOFERRITIN

G: BACTERIOFERRITIN

H: BACTERIOFERRITIN

I: BACTERIOFERRITIN

J: BACTERIOFERRITIN

K: BACTERIOFERRITIN

L: BACTERIOFERRITIN

hetero molecules

defined by author&software
455 kDa, 24 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	208.082, 208.082, 143.107
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	94
Space group name H-M	P4₂2₁2

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Component-ID: 1 / Beg auth comp-ID: MET / Beg label comp-ID: MET / End auth comp-ID: SO4 / End label comp-ID: SO4 / Refine code: 1 / Auth seq-ID: 1 - 250 / Label seq-ID: 1

NCS ensembles :

ID
1
2
3
4
5
6
7
8
9
10
11
12

#1: Protein	BACTERIOFERRITIN / BFR / CYTOCHROME B-1 / CYTOCHROME B-557 Mass: 18518.016 Da / Num. of mol.: 12 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Strain: K-12 / Gene: BFR / Plasmid: PALN1 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P0ABD3
#2: Chemical	ChemComp-SO4 / SULFATE ION Mass: 96.063 Da / Num. of mol.: 16 / Source method: obtained synthetically / Formula: SO₄
#3: Chemical	ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME Mass: 616.487 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C₃₄H₃₂FeN₄O₄
#4: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 496 / Source method: isolated from a natural source / Formula: H₂O

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 3.49 Å³/Da / Density % sol: 64.71 %
Crystal grow	Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 5 Details: 1.8 M AMMOMIUM SULFATE, 0.1 M TRI- SODIUM CITRATE PH 5.0. SUBSEQUENTLY, THE CRYSTALS WERE SOAKED IN A CRYO-PROTECTANT BUFFER CONTAINING PHOSPHATE BUFFERED WITH MOPS PH 7 INSTEAD OF CITRATE. ...Details: 1.8 M AMMOMIUM SULFATE, 0.1 M TRI- SODIUM CITRATE PH 5.0. SUBSEQUENTLY, THE CRYSTALS WERE SOAKED IN A CRYO-PROTECTANT BUFFER CONTAINING PHOSPHATE BUFFERED WITH MOPS PH 7 INSTEAD OF CITRATE. SEE PAPER FOR FULL DETAILS., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K, pH 5.00

Crystal

Density Matthews: 3.49 Å³/Da / Density % sol: 64.71 %

Crystal grow

Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 5
Details: 1.8 M AMMOMIUM SULFATE, 0.1 M TRI- SODIUM CITRATE PH 5.0. SUBSEQUENTLY, THE CRYSTALS WERE SOAKED IN A CRYO-PROTECTANT BUFFER CONTAINING PHOSPHATE BUFFERED WITH MOPS PH 7 INSTEAD OF CITRATE. ...

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: SRS / Beamline: PX10.1 / Wavelength: 1.739
Detector	Detector: CCD / Date: Jan 1, 2006
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 1.739 Å / Relative weight: 1
Reflection	Resolution: 2.5→34.2 Å / Num. obs: 104275 / % possible obs: 96.4 % / Observed criterion σ(I): 1 / Redundancy: 13.9 % / R_sym value: 0.101 / Net I/σ(I): 19.6
Reflection shell	Resolution: 2.5→2.64 Å / Redundancy: 5.7 % / Mean I/σ(I) obs: 5.2 / R_sym value: 0.251 / % possible all: 80.7

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Processing

Software

Name	Version	Classification
MOLREP		phasing
REFMAC	5.2.0019	refinement
MOSFLM		data reduction
SCALA		data scaling

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 2QP7

2qp7
PDB Unreleased entry

Resolution: 2.5→34 Å / Cor.coef. F_o:F_c: 0.943 / Cor.coef. F_o:F_c free: 0.937 / SU B: 7.19 / SU ML: 0.163 / Cross valid method: THROUGHOUT / ESU R: 0.437 / ESU R Free: 0.262 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.248	5157	4.9 %	EXTENDED FROM THE VALIDATION SET USED IN 2QP7.
R_work	0.236	-	-	-
obs	0.236	99059	96.2 %	-

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK

Displacement parameters

B_iso mean: 11.67 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-0.02 Å²	0 Å²	0 Å²
2-	-	-0.02 Å²	0 Å²
3-	-	-	0.03 Å²

Refinement step

Cycle: LAST / Resolution: 2.5→34 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	15876	0	337	496	16709

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.012	0.021	16514
X-RAY DIFFRACTION	r_bond_other_d
X-RAY DIFFRACTION	r_angle_refined_deg	1.368	2.019	22351
X-RAY DIFFRACTION	r_angle_other_deg
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	4.248	5	1956
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	38.119	25.065	924
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	20.307	15	3144
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	24.406	15	120
X-RAY DIFFRACTION	r_chiral_restr	0.123	0.2	2328
X-RAY DIFFRACTION	r_gen_planes_refined	0.005	0.02	12634
X-RAY DIFFRACTION	r_gen_planes_other
X-RAY DIFFRACTION	r_nbd_refined	0.213	0.2	8123
X-RAY DIFFRACTION	r_nbd_other
X-RAY DIFFRACTION	r_nbtor_refined	0.307	0.2	11219
X-RAY DIFFRACTION	r_nbtor_other
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.165	0.2	682
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	0.224	0.2	144
X-RAY DIFFRACTION	r_symmetry_vdw_other
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.17	0.2	37
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	0.728	1.5	9867
X-RAY DIFFRACTION	r_mcbond_other
X-RAY DIFFRACTION	r_mcangle_it	1.122	2	15240
X-RAY DIFFRACTION	r_scbond_it	2.237	3	7569
X-RAY DIFFRACTION	r_scangle_it	3.493	4.5	7087
X-RAY DIFFRACTION	r_rigid_bond_restr
X-RAY DIFFRACTION	r_sphericity_free
X-RAY DIFFRACTION	r_sphericity_bonded

Refine LS restraints NCS

Number: 1328 / Refine-ID: X-RAY DIFFRACTION / Rms dev position: 0.01 Å

Ens-ID	Dom-ID	Auth asym-ID	Type	Weight position
1	1	A	tight positional	0.05
1	2	B	tight positional	0.05
1	3	C	tight positional	0.05
1	4	D	tight positional	0.05
1	5	E	tight positional	0.05
1	6	F	tight positional	0.05
1	7	G	tight positional	0.05
1	8	H	tight positional	0.05
1	9	I	tight positional	0.05
1	10	J	tight positional	0.05
1	11	K	tight positional	0.05
1	12	L	tight positional	0.05
2	1	B	tight positional	0.05
2	2	A	tight positional	0.05
2	3	C	tight positional	0.05
2	4	D	tight positional	0.05
2	5	E	tight positional	0.05
2	6	F	tight positional	0.05
2	7	G	tight positional	0.05
2	8	H	tight positional	0.05
2	9	I	tight positional	0.05
2	10	J	tight positional	0.05
2	11	K	tight positional	0.05
2	12	L	tight positional	0.05
3	1	C	tight positional	0.05
3	2	A	tight positional	0.05
3	3	B	tight positional	0.05
3	4	D	tight positional	0.05
3	5	E	tight positional	0.05
3	6	F	tight positional	0.05
3	7	G	tight positional	0.05
3	8	H	tight positional	0.05
3	9	I	tight positional	0.05
3	10	J	tight positional	0.05
3	11	K	tight positional	0.05
3	12	L	tight positional	0.05
4	1	D	tight positional	0.05
4	2	A	tight positional	0.05
4	3	B	tight positional	0.05
4	4	C	tight positional	0.05
4	5	E	tight positional	0.05
4	6	F	tight positional	0.05
4	7	G	tight positional	0.05
4	8	H	tight positional	0.05
4	9	I	tight positional	0.05
4	10	J	tight positional	0.05
4	11	K	tight positional	0.05
4	12	L	tight positional	0.05
5	1	E	tight positional	0.05
5	2	A	tight positional	0.05
5	3	B	tight positional	0.05
5	4	C	tight positional	0.05
5	5	D	tight positional	0.05
5	6	F	tight positional	0.05
5	7	G	tight positional	0.05
5	8	H	tight positional	0.05
5	9	I	tight positional	0.05
5	10	J	tight positional	0.05
5	11	K	tight positional	0.05
5	12	L	tight positional	0.05
6	1	F	tight positional	0.05
6	2	A	tight positional	0.05
6	3	B	tight positional	0.05
6	4	C	tight positional	0.05
6	5	D	tight positional	0.05
6	6	E	tight positional	0.05
6	7	G	tight positional	0.05
6	8	H	tight positional	0.05
6	9	I	tight positional	0.05
6	10	J	tight positional	0.05
6	11	K	tight positional	0.05
6	12	L	tight positional	0.05
7	1	G	tight positional	0.05
7	2	A	tight positional	0.05
7	3	B	tight positional	0.05
7	4	C	tight positional	0.05
7	5	D	tight positional	0.05
7	6	E	tight positional	0.05
7	7	F	tight positional	0.05
7	8	H	tight positional	0.05
7	9	I	tight positional	0.05
7	10	J	tight positional	0.05
7	11	K	tight positional	0.05
7	12	L	tight positional	0.05
8	1	H	tight positional	0.05
8	2	A	tight positional	0.05
8	3	B	tight positional	0.05
8	4	C	tight positional	0.05
8	5	D	tight positional	0.05
8	6	E	tight positional	0.05
8	7	F	tight positional	0.05
8	8	G	tight positional	0.05
8	9	I	tight positional	0.05
8	10	J	tight positional	0.05
8	11	K	tight positional	0.05
8	12	L	tight positional	0.05
9	1	I	tight positional	0.05
9	2	A	tight positional	0.05
9	3	B	tight positional	0.05
9	4	C	tight positional	0.05
9	5	D	tight positional	0.05
9	6	E	tight positional	0.05
9	7	F	tight positional	0.05
9	8	G	tight positional	0.05
9	9	H	tight positional	0.05
9	10	J	tight positional	0.05
9	11	K	tight positional	0.05
9	12	L	tight positional	0.05
10	1	J	tight positional	0.05
10	2	A	tight positional	0.05
10	3	B	tight positional	0.05
10	4	C	tight positional	0.05
10	5	D	tight positional	0.05
10	6	E	tight positional	0.05
10	7	F	tight positional	0.05
10	8	G	tight positional	0.05
10	9	H	tight positional	0.05
10	10	I	tight positional	0.05
10	11	K	tight positional	0.05
10	12	L	tight positional	0.05
11	1	K	tight positional	0.05
11	2	A	tight positional	0.05
11	3	B	tight positional	0.05
11	4	C	tight positional	0.05
11	5	D	tight positional	0.05
11	6	E	tight positional	0.05
11	7	F	tight positional	0.05
11	8	G	tight positional	0.05
11	9	H	tight positional	0.05
11	10	I	tight positional	0.05
11	11	J	tight positional	0.05
11	12	L	tight positional	0.05
12	1	L	tight positional	0.05
12	2	A	tight positional	0.05
12	3	B	tight positional	0.05
12	4	C	tight positional	0.05
12	5	D	tight positional	0.05
12	6	E	tight positional	0.05
12	7	F	tight positional	0.05
12	8	G	tight positional	0.05
12	9	H	tight positional	0.05
12	10	I	tight positional	0.05
12	11	J	tight positional	0.05
12	12	K	tight positional	0.05
1	1	A	tight thermal	0.5
1	2	B	tight thermal	0.5
1	3	C	tight thermal	0.5
1	4	D	tight thermal	0.5
1	5	E	tight thermal	0.5
1	6	F	tight thermal	0.5
1	7	G	tight thermal	0.5
1	8	H	tight thermal	0.5
1	9	I	tight thermal	0.5
1	10	J	tight thermal	0.5
1	11	K	tight thermal	0.5
1	12	L	tight thermal	0.5
2	1	B	tight thermal	0.5
2	2	A	tight thermal	0.5
2	3	C	tight thermal	0.5
2	4	D	tight thermal	0.5
2	5	E	tight thermal	0.5
2	6	F	tight thermal	0.5
2	7	G	tight thermal	0.5
2	8	H	tight thermal	0.5
2	9	I	tight thermal	0.5
2	10	J	tight thermal	0.5
2	11	K	tight thermal	0.5
2	12	L	tight thermal	0.5
3	1	C	tight thermal	0.5
3	2	A	tight thermal	0.5
3	3	B	tight thermal	0.5
3	4	D	tight thermal	0.5
3	5	E	tight thermal	0.5
3	6	F	tight thermal	0.5
3	7	G	tight thermal	0.5
3	8	H	tight thermal	0.5
3	9	I	tight thermal	0.5
3	10	J	tight thermal	0.5
3	11	K	tight thermal	0.5
3	12	L	tight thermal	0.5
4	1	D	tight thermal	0.5
4	2	A	tight thermal	0.5
4	3	B	tight thermal	0.5
4	4	C	tight thermal	0.5
4	5	E	tight thermal	0.5
4	6	F	tight thermal	0.5
4	7	G	tight thermal	0.5
4	8	H	tight thermal	0.5
4	9	I	tight thermal	0.5
4	10	J	tight thermal	0.5
4	11	K	tight thermal	0.5
4	12	L	tight thermal	0.5
5	1	E	tight thermal	0.5
5	2	A	tight thermal	0.5
5	3	B	tight thermal	0.5
5	4	C	tight thermal	0.5
5	5	D	tight thermal	0.5
5	6	F	tight thermal	0.5
5	7	G	tight thermal	0.5
5	8	H	tight thermal	0.5
5	9	I	tight thermal	0.5
5	10	J	tight thermal	0.5
5	11	K	tight thermal	0.5
5	12	L	tight thermal	0.5
6	1	F	tight thermal	0.5
6	2	A	tight thermal	0.5
6	3	B	tight thermal	0.5
6	4	C	tight thermal	0.5
6	5	D	tight thermal	0.5
6	6	E	tight thermal	0.5
6	7	G	tight thermal	0.5
6	8	H	tight thermal	0.5
6	9	I	tight thermal	0.5
6	10	J	tight thermal	0.5
6	11	K	tight thermal	0.5
6	12	L	tight thermal	0.5
7	1	G	tight thermal	0.5
7	2	A	tight thermal	0.5
7	3	B	tight thermal	0.5
7	4	C	tight thermal	0.5
7	5	D	tight thermal	0.5
7	6	E	tight thermal	0.5
7	7	F	tight thermal	0.5
7	8	H	tight thermal	0.5
7	9	I	tight thermal	0.5
7	10	J	tight thermal	0.5
7	11	K	tight thermal	0.5
7	12	L	tight thermal	0.5
8	1	H	tight thermal	0.5
8	2	A	tight thermal	0.5
8	3	B	tight thermal	0.5
8	4	C	tight thermal	0.5
8	5	D	tight thermal	0.5
8	6	E	tight thermal	0.5
8	7	F	tight thermal	0.5
8	8	G	tight thermal	0.5
8	9	I	tight thermal	0.5
8	10	J	tight thermal	0.5
8	11	K	tight thermal	0.5
8	12	L	tight thermal	0.5
9	1	I	tight thermal	0.5
9	2	A	tight thermal	0.5
9	3	B	tight thermal	0.5
9	4	C	tight thermal	0.5
9	5	D	tight thermal	0.5
9	6	E	tight thermal	0.5
9	7	F	tight thermal	0.5
9	8	G	tight thermal	0.5
9	9	H	tight thermal	0.5
9	10	J	tight thermal	0.5
9	11	K	tight thermal	0.5
9	12	L	tight thermal	0.5
10	1	J	tight thermal	0.5
10	2	A	tight thermal	0.5
10	3	B	tight thermal	0.5
10	4	C	tight thermal	0.5
10	5	D	tight thermal	0.5
10	6	E	tight thermal	0.5
10	7	F	tight thermal	0.5
10	8	G	tight thermal	0.5
10	9	H	tight thermal	0.5
10	10	I	tight thermal	0.5
10	11	K	tight thermal	0.5
10	12	L	tight thermal	0.5
11	1	K	tight thermal	0.5
11	2	A	tight thermal	0.5
11	3	B	tight thermal	0.5
11	4	C	tight thermal	0.5
11	5	D	tight thermal	0.5
11	6	E	tight thermal	0.5
11	7	F	tight thermal	0.5
11	8	G	tight thermal	0.5
11	9	H	tight thermal	0.5
11	10	I	tight thermal	0.5
11	11	J	tight thermal	0.5
11	12	L	tight thermal	0.5
12	1	L	tight thermal	0.5
12	2	A	tight thermal	0.5
12	3	B	tight thermal	0.5
12	4	C	tight thermal	0.5
12	5	D	tight thermal	0.5
12	6	E	tight thermal	0.5
12	7	F	tight thermal	0.5
12	8	G	tight thermal	0.5
12	9	H	tight thermal	0.5
12	10	I	tight thermal	0.5
12	11	J	tight thermal	0.5
12	12	K	tight thermal	0.5

LS refinement shell

Resolution: 2.5→2.56 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.36	273	-
R_work	0.313	5693	-
obs	-	-	75.7 %

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