PDB-4oyy: Humicola insolens cutinase

ID or keywords:

Entry

Database: PDB / ID: 4oyy

Title

Humicola insolens cutinase

Components

Cutinase

Keywords

HYDROLASE

Function / homology

Function and homology information

cutinase activity / cutinase / extracellular region
Similarity search - Function

Biological species

Humicola insolens (fungus)

Method

X-RAY DIFFRACTION / Resolution: 3 Å

Authors

Dauter, Z.D. / Brzozowski, A.M. / Turkenburg, J.P. / Wilson, K.S.

Citation

Journal: Protein Sci. / Year: 2014
Title: Thermodynamic and structural investigation of the specific SDS binding of humicola insolens cutinase.
Authors: Kold, D. / Dauter, Z. / Laustsen, A.K. / Brzozowski, A.M. / Turkenburg, J.P. / Nielsen, A.D. / Kolds, H. / Petersen, E. / Schitt, B. / De Maria, L. / Wilson, K.S. / Svendsen, A. / Wimmer, R.

History

Deposition	Feb 13, 2014	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Jul 30, 2014	Provider: repository / Type: Initial release
Revision 1.1	Jan 7, 2015	Group: Database references
Revision 1.2	Sep 23, 2015	Group: Data collection / Database references
Revision 1.3	Nov 22, 2017	Group: Derived calculations / Refinement description / Category: pdbx_struct_oper_list / software Item: _pdbx_struct_oper_list.symmetry_operation / _software.classification
Revision 1.4	Dec 27, 2023	Group: Data collection / Database references / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ncs_dom_lim Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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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Validation report

Summary document	4oyy_validation.pdf.gz	488.5 KB	Display	wwPDB validaton report
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Data in CIF	4oyy_validation.cif.gz	100.6 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/oy/4oyy ftp://data.pdbj.org/pub/pdb/validation_reports/oy/4oyy	HTTPS FTP

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Related structure data

Related structure data	4oylC C: citing same article (ref.)
Similar structure data	1ffa-d 4oyl-3 1ffc-d 3zwg-5 3zwj-4 5bpg-1 3zwg-13 3dd5-6 1cue-d 6k2g-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) 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 - FunctionF&H Search Similarity search - HomologyF&H Search

Related structure data

4oylC

C: citing same article (ref.)

Similar structure data

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#259 - Jul 2021 Designed Proteins and Citizen Science similarity (1)

Deposited unit

A: Cutinase

B: Cutinase

C: Cutinase

D: Cutinase

E: Cutinase

F: Cutinase

G: Cutinase

H: Cutinase

I: Cutinase

J: Cutinase

K: Cutinase

L: Cutinase

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

1

A: Cutinase

defined by author
20.3 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: Cutinase

defined by author
20.3 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

C: Cutinase

defined by author
20.3 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

4

D: Cutinase

defined by author
20.3 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

5

E: Cutinase

defined by author
20.3 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

6

F: Cutinase

defined by author
20.3 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

7

G: Cutinase

defined by author
20.3 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

8

H: Cutinase

defined by author
20.3 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

9

I: Cutinase

defined by author
20.3 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

10

J: Cutinase

defined by author
20.3 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

11

K: Cutinase

defined by author
20.3 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

12

L: Cutinase

defined by author
20.3 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	125.548, 126.999, 134.505
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	19
Space group name H-M	P2₁2₁2₁

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	GLY	GLY	ARG	ARG	A	A	3 - 193	3 - 193
2	1	GLY	GLY	ARG	ARG	B	B	3 - 193	3 - 193
1	2	GLY	GLY	ILE	ILE	A	A	3 - 192	3 - 192
2	2	GLY	GLY	ILE	ILE	C	C	3 - 192	3 - 192
1	3	GLY	GLY	ARG	ARG	A	A	3 - 193	3 - 193
2	3	GLY	GLY	ARG	ARG	D	D	3 - 193	3 - 193
1	4	GLY	GLY	ARG	ARG	A	A	3 - 193	3 - 193
2	4	GLY	GLY	ARG	ARG	E	E	3 - 193	3 - 193
1	5	GLY	GLY	ILE	ILE	A	A	3 - 192	3 - 192
2	5	GLY	GLY	ILE	ILE	F	F	3 - 192	3 - 192
1	6	GLY	GLY	ILE	ILE	A	A	3 - 192	3 - 192
2	6	GLY	GLY	ILE	ILE	G	G	3 - 192	3 - 192
1	7	GLY	GLY	ARG	ARG	A	A	3 - 193	3 - 193
2	7	GLY	GLY	ARG	ARG	H	H	3 - 193	3 - 193
1	8	GLY	GLY	ILE	ILE	A	A	3 - 192	3 - 192
2	8	GLY	GLY	ILE	ILE	I	I	3 - 192	3 - 192
1	9	GLY	GLY	ARG	ARG	A	A	3 - 193	3 - 193
2	9	GLY	GLY	ARG	ARG	J	J	3 - 193	3 - 193
1	10	GLY	GLY	ARG	ARG	A	A	3 - 193	3 - 193
2	10	GLY	GLY	ARG	ARG	K	K	3 - 193	3 - 193
1	11	GLY	GLY	ILE	ILE	A	A	3 - 192	3 - 192
2	11	GLY	GLY	ILE	ILE	L	L	3 - 192	3 - 192
1	12	GLY	GLY	ILE	ILE	B	B	3 - 192	3 - 192
2	12	GLY	GLY	ILE	ILE	C	C	3 - 192	3 - 192
1	13	GLY	GLY	ARG	ARG	B	B	3 - 193	3 - 193
2	13	GLY	GLY	ARG	ARG	D	D	3 - 193	3 - 193
1	14	GLY	GLY	ARG	ARG	B	B	3 - 193	3 - 193
2	14	GLY	GLY	ARG	ARG	E	E	3 - 193	3 - 193
1	15	GLY	GLY	ILE	ILE	B	B	3 - 192	3 - 192
2	15	GLY	GLY	ILE	ILE	F	F	3 - 192	3 - 192
1	16	GLY	GLY	ILE	ILE	B	B	3 - 192	3 - 192
2	16	GLY	GLY	ILE	ILE	G	G	3 - 192	3 - 192
1	17	GLY	GLY	ARG	ARG	B	B	3 - 193	3 - 193
2	17	GLY	GLY	ARG	ARG	H	H	3 - 193	3 - 193
1	18	GLY	GLY	ILE	ILE	B	B	3 - 192	3 - 192
2	18	GLY	GLY	ILE	ILE	I	I	3 - 192	3 - 192
1	19	GLY	GLY	ARG	ARG	B	B	3 - 193	3 - 193
2	19	GLY	GLY	ARG	ARG	J	J	3 - 193	3 - 193
1	20	GLY	GLY	ARG	ARG	B	B	3 - 193	3 - 193
2	20	GLY	GLY	ARG	ARG	K	K	3 - 193	3 - 193
1	21	GLY	GLY	ILE	ILE	B	B	3 - 192	3 - 192
2	21	GLY	GLY	ILE	ILE	L	L	3 - 192	3 - 192
1	22	GLY	GLY	ILE	ILE	C	C	3 - 192	3 - 192
2	22	GLY	GLY	ILE	ILE	D	D	3 - 192	3 - 192
1	23	GLY	GLY	ILE	ILE	C	C	3 - 192	3 - 192
2	23	GLY	GLY	ILE	ILE	E	E	3 - 192	3 - 192
1	24	GLN	GLN	ARG	ARG	C	C	1 - 193	1 - 193
2	24	GLN	GLN	ARG	ARG	F	F	1 - 193	1 - 193
1	25	GLN	GLN	ARG	ARG	C	C	1 - 193	1 - 193
2	25	GLN	GLN	ARG	ARG	G	G	1 - 193	1 - 193
1	26	GLY	GLY	ILE	ILE	C	C	3 - 192	3 - 192
2	26	GLY	GLY	ILE	ILE	H	H	3 - 192	3 - 192
1	27	GLN	GLN	ARG	ARG	C	C	1 - 193	1 - 193
2	27	GLN	GLN	ARG	ARG	I	I	1 - 193	1 - 193
1	28	GLY	GLY	ILE	ILE	C	C	3 - 192	3 - 192
2	28	GLY	GLY	ILE	ILE	J	J	3 - 192	3 - 192
1	29	GLY	GLY	ILE	ILE	C	C	3 - 192	3 - 192
2	29	GLY	GLY	ILE	ILE	K	K	3 - 192	3 - 192
1	30	LEU	LEU	ILE	ILE	C	C	2 - 192	2 - 192
2	30	LEU	LEU	ILE	ILE	L	L	2 - 192	2 - 192
1	31	GLY	GLY	ARG	ARG	D	D	3 - 193	3 - 193
2	31	GLY	GLY	ARG	ARG	E	E	3 - 193	3 - 193
1	32	GLY	GLY	ILE	ILE	D	D	3 - 192	3 - 192
2	32	GLY	GLY	ILE	ILE	F	F	3 - 192	3 - 192
1	33	GLY	GLY	ILE	ILE	D	D	3 - 192	3 - 192
2	33	GLY	GLY	ILE	ILE	G	G	3 - 192	3 - 192
1	34	GLY	GLY	ARG	ARG	D	D	3 - 193	3 - 193
2	34	GLY	GLY	ARG	ARG	H	H	3 - 193	3 - 193
1	35	GLY	GLY	ILE	ILE	D	D	3 - 192	3 - 192
2	35	GLY	GLY	ILE	ILE	I	I	3 - 192	3 - 192
1	36	GLY	GLY	ARG	ARG	D	D	3 - 193	3 - 193
2	36	GLY	GLY	ARG	ARG	J	J	3 - 193	3 - 193
1	37	GLY	GLY	ARG	ARG	D	D	3 - 193	3 - 193
2	37	GLY	GLY	ARG	ARG	K	K	3 - 193	3 - 193
1	38	GLY	GLY	ILE	ILE	D	D	3 - 192	3 - 192
2	38	GLY	GLY	ILE	ILE	L	L	3 - 192	3 - 192
1	39	GLY	GLY	ILE	ILE	E	E	3 - 192	3 - 192
2	39	GLY	GLY	ILE	ILE	F	F	3 - 192	3 - 192
1	40	GLY	GLY	ILE	ILE	E	E	3 - 192	3 - 192
2	40	GLY	GLY	ILE	ILE	G	G	3 - 192	3 - 192
1	41	GLY	GLY	ARG	ARG	E	E	3 - 193	3 - 193
2	41	GLY	GLY	ARG	ARG	H	H	3 - 193	3 - 193
1	42	GLY	GLY	ILE	ILE	E	E	3 - 192	3 - 192
2	42	GLY	GLY	ILE	ILE	I	I	3 - 192	3 - 192
1	43	GLY	GLY	ARG	ARG	E	E	3 - 193	3 - 193
2	43	GLY	GLY	ARG	ARG	J	J	3 - 193	3 - 193
1	44	GLY	GLY	ARG	ARG	E	E	3 - 193	3 - 193
2	44	GLY	GLY	ARG	ARG	K	K	3 - 193	3 - 193
1	45	GLY	GLY	ILE	ILE	E	E	3 - 192	3 - 192
2	45	GLY	GLY	ILE	ILE	L	L	3 - 192	3 - 192
1	46	GLN	GLN	ARG	ARG	F	F	1 - 193	1 - 193
2	46	GLN	GLN	ARG	ARG	G	G	1 - 193	1 - 193
1	47	GLY	GLY	ILE	ILE	F	F	3 - 192	3 - 192
2	47	GLY	GLY	ILE	ILE	H	H	3 - 192	3 - 192
1	48	GLN	GLN	ARG	ARG	F	F	1 - 193	1 - 193
2	48	GLN	GLN	ARG	ARG	I	I	1 - 193	1 - 193
1	49	GLY	GLY	ILE	ILE	F	F	3 - 192	3 - 192
2	49	GLY	GLY	ILE	ILE	J	J	3 - 192	3 - 192
1	50	GLY	GLY	ILE	ILE	F	F	3 - 192	3 - 192
2	50	GLY	GLY	ILE	ILE	K	K	3 - 192	3 - 192
1	51	LEU	LEU	ILE	ILE	F	F	2 - 192	2 - 192
2	51	LEU	LEU	ILE	ILE	L	L	2 - 192	2 - 192
1	52	GLY	GLY	ILE	ILE	G	G	3 - 192	3 - 192
2	52	GLY	GLY	ILE	ILE	H	H	3 - 192	3 - 192
1	53	GLN	GLN	ARG	ARG	G	G	1 - 193	1 - 193
2	53	GLN	GLN	ARG	ARG	I	I	1 - 193	1 - 193
1	54	GLY	GLY	ILE	ILE	G	G	3 - 192	3 - 192
2	54	GLY	GLY	ILE	ILE	J	J	3 - 192	3 - 192
1	55	GLY	GLY	ILE	ILE	G	G	3 - 192	3 - 192
2	55	GLY	GLY	ILE	ILE	K	K	3 - 192	3 - 192
1	56	LEU	LEU	ILE	ILE	G	G	2 - 192	2 - 192
2	56	LEU	LEU	ILE	ILE	L	L	2 - 192	2 - 192
1	57	GLY	GLY	ILE	ILE	H	H	3 - 192	3 - 192
2	57	GLY	GLY	ILE	ILE	I	I	3 - 192	3 - 192
1	58	GLY	GLY	ARG	ARG	H	H	3 - 193	3 - 193
2	58	GLY	GLY	ARG	ARG	J	J	3 - 193	3 - 193
1	59	GLY	GLY	ARG	ARG	H	H	3 - 193	3 - 193
2	59	GLY	GLY	ARG	ARG	K	K	3 - 193	3 - 193
1	60	GLY	GLY	ILE	ILE	H	H	3 - 192	3 - 192
2	60	GLY	GLY	ILE	ILE	L	L	3 - 192	3 - 192
1	61	GLY	GLY	ILE	ILE	I	I	3 - 192	3 - 192
2	61	GLY	GLY	ILE	ILE	J	J	3 - 192	3 - 192
1	62	GLY	GLY	ILE	ILE	I	I	3 - 192	3 - 192
2	62	GLY	GLY	ILE	ILE	K	K	3 - 192	3 - 192
1	63	LEU	LEU	ILE	ILE	I	I	2 - 192	2 - 192
2	63	LEU	LEU	ILE	ILE	L	L	2 - 192	2 - 192
1	64	GLY	GLY	ARG	ARG	J	J	3 - 193	3 - 193
2	64	GLY	GLY	ARG	ARG	K	K	3 - 193	3 - 193
1	65	GLY	GLY	ILE	ILE	J	J	3 - 192	3 - 192
2	65	GLY	GLY	ILE	ILE	L	L	3 - 192	3 - 192
1	66	GLY	GLY	ILE	ILE	K	K	3 - 192	3 - 192
2	66	GLY	GLY	ILE	ILE	L	L	3 - 192	3 - 192

NCS ensembles :

#1: Protein	Cutinase Mass: 20270.889 Da / Num. of mol.: 12 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Humicola insolens (fungus) / Production host: Aspergillus oryzae (mold) / References: UniProt: A0A075B5G4*PLUS
#2: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 98 / Source method: isolated from a natural source / Formula: H₂O

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Experiment

Experiment	Method: X-RAY DIFFRACTION

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Sample preparation

Crystal	Density Matthews: 2.2 Å³/Da / Density % sol: 44.2 %
Crystal grow	Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: HiCutinase 30 mg mL-1, 0.1 M Tris/HCl buffer pH 8.5, 50 mM lysine, 100 mg mL-1 (app. 8.6%) isopropanol, 50 mg mL-1 (app. 4.3 %) dioxane, PEG 4K 22% v/v of 50% w/v stock solutions

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Data collection

Diffraction	Mean temperature: 120 K
Diffraction source	Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.54 Å
Detector	Type: RIGAKU RAXIS II / Detector: IMAGE PLATE / Date: Jun 20, 1995
Radiation	Monochromator: mirrors / Protocol: SINGLE WAVELENGTH / Scattering type: x-ray
Radiation wavelength	Wavelength: 1.54 Å / Relative weight: 1
Reflection	Resolution: 3→30 Å / Num. obs: 43738 / % possible obs: 99.5 % / Redundancy: 4.5 % / Net I/σ(I): 5.9
Reflection shell	Resolution: 3→3.16 Å / Redundancy: 3.6 % / R_merge(I) obs: 0.324 / Mean I/σ(I) obs: 2.3 / % possible all: 97.5

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Processing

Software

Name	Version	Classification
MOSFLM		data reduction
AMoRE		phasing
REFMAC	5.8.0049	refinement

Refinement

Resolution: 3→29.7611 Å / Cor.coef. F_o:F_c: 0.957 / Cor.coef. F_o:F_c free: 0.957 / SU B: 15.789 / SU ML: 0.276 / Cross valid method: THROUGHOUT / ESU R Free: 0.378 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.19597	1338	3.1 %	RANDOM
R_work	0.1741	-	-	-
obs	0.17481	42118	99.36 %	-

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 mean: 27.819 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-1.05 Å²	0 Å²	-0 Å²
2-	-	2.39 Å²	-0 Å²
3-	-	-	-1.34 Å²

Refinement step

Cycle: 1 / Resolution: 3→29.7611 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	16877	0	0	98	16975

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.011	0.019	17189
X-RAY DIFFRACTION	r_bond_other_d	0.008	0.02	16543
X-RAY DIFFRACTION	r_angle_refined_deg	1.445	1.959	23355
X-RAY DIFFRACTION	r_angle_other_deg	1.539	3	37829
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.624	5	2289
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	36.083	23.844	731
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	16.371	15	2624
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	16.258	15	141
X-RAY DIFFRACTION	r_chiral_restr	0.084	0.2	2630
X-RAY DIFFRACTION	r_gen_planes_refined	0.008	0.021	20270
X-RAY DIFFRACTION	r_gen_planes_other	0.006	0.02	3987
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	1.757	2.617	9192
X-RAY DIFFRACTION	r_mcbond_other	1.756	2.617	9191
X-RAY DIFFRACTION	r_mcangle_it	2.917	3.924	11469
X-RAY DIFFRACTION	r_mcangle_other	2.918	3.924	11470
X-RAY DIFFRACTION	r_scbond_it	2.312	2.925	7997
X-RAY DIFFRACTION	r_scbond_other	2.312	2.926	7998
X-RAY DIFFRACTION	r_scangle_it
X-RAY DIFFRACTION	r_scangle_other	3.869	4.271	11887
X-RAY DIFFRACTION	r_long_range_B_refined	5.39	20.771	18530
X-RAY DIFFRACTION	r_long_range_B_other	5.39	20.773	18531
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	11229	0.07
1	2	B	11229	0.07
2	1	A	11032	0.07
2	2	C	11032	0.07
3	1	A	11457	0.05
3	2	D	11457	0.05
4	1	A	11074	0.07
4	2	E	11074	0.07
5	1	A	11069	0.07
5	2	F	11069	0.07
6	1	A	11234	0.06
6	2	G	11234	0.06
7	1	A	11337	0.06
7	2	H	11337	0.06
8	1	A	11051	0.06
8	2	I	11051	0.06
9	1	A	11380	0.06
9	2	J	11380	0.06
10	1	A	11244	0.06
10	2	K	11244	0.06
11	1	A	11035	0.08
11	2	L	11035	0.08
12	1	B	10906	0.08
12	2	C	10906	0.08
13	1	B	11228	0.07
13	2	D	11228	0.07
14	1	B	11103	0.08
14	2	E	11103	0.08
15	1	B	10953	0.08
15	2	F	10953	0.08
16	1	B	11015	0.08
16	2	G	11015	0.08
17	1	B	11358	0.06
17	2	H	11358	0.06
18	1	B	10892	0.07
18	2	I	10892	0.07
19	1	B	11144	0.08
19	2	J	11144	0.08
20	1	B	11276	0.06
20	2	K	11276	0.06
21	1	B	10938	0.09
21	2	L	10938	0.09
22	1	C	11018	0.07
22	2	D	11018	0.07
23	1	C	10864	0.08
23	2	E	10864	0.08
24	1	C	11392	0.06
24	2	F	11392	0.06
25	1	C	11237	0.07
25	2	G	11237	0.07
26	1	C	10955	0.08
26	2	H	10955	0.08
27	1	C	11180	0.07
27	2	I	11180	0.07
28	1	C	11039	0.07
28	2	J	11039	0.07
29	1	C	11005	0.07
29	2	K	11005	0.07
30	1	C	11165	0.08
30	2	L	11165	0.08
31	1	D	11063	0.07
31	2	E	11063	0.07
32	1	D	11086	0.06
32	2	F	11086	0.06
33	1	D	11198	0.06
33	2	G	11198	0.06
34	1	D	11294	0.06
34	2	H	11294	0.06
35	1	D	11035	0.06
35	2	I	11035	0.06
36	1	D	11337	0.07
36	2	J	11337	0.07
37	1	D	11235	0.06
37	2	K	11235	0.06
38	1	D	11017	0.08
38	2	L	11017	0.08
39	1	E	10860	0.08
39	2	F	10860	0.08
40	1	E	10944	0.07
40	2	G	10944	0.07
41	1	E	11114	0.07
41	2	H	11114	0.07
42	1	E	10782	0.08
42	2	I	10782	0.08
43	1	E	11063	0.07
43	2	J	11063	0.07
44	1	E	11106	0.07
44	2	K	11106	0.07
45	1	E	10872	0.09
45	2	L	10872	0.09
46	1	F	11233	0.07
46	2	G	11233	0.07
47	1	F	11004	0.08
47	2	H	11004	0.08
48	1	F	11286	0.06
48	2	I	11286	0.06
49	1	F	11039	0.07
49	2	J	11039	0.07
50	1	F	11025	0.07
50	2	K	11025	0.07
51	1	F	11188	0.08
51	2	L	11188	0.08
52	1	G	11094	0.07
52	2	H	11094	0.07
53	1	G	11177	0.07
53	2	I	11177	0.07
54	1	G	11210	0.05
54	2	J	11210	0.05
55	1	G	11065	0.06
55	2	K	11065	0.06
56	1	G	11107	0.08
56	2	L	11107	0.08
57	1	H	10945	0.07
57	2	I	10945	0.07
58	1	H	11261	0.07
58	2	J	11261	0.07
59	1	H	11350	0.05
59	2	K	11350	0.05
60	1	H	10971	0.09
60	2	L	10971	0.09
61	1	I	10954	0.07
61	2	J	10954	0.07
62	1	I	11121	0.05
62	2	K	11121	0.05
63	1	I	11042	0.08
63	2	L	11042	0.08
64	1	J	11196	0.07
64	2	K	11196	0.07
65	1	J	11101	0.07
65	2	L	11101	0.07
66	1	K	11032	0.08
66	2	L	11032	0.08

LS refinement shell

Resolution: 3→3.078 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.285	96	-
R_work	0.262	3010	-
obs	-	-	97.31 %

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