PDB-2x2y: Cellulomonas fimi endo-beta-1,4-mannanase double mutant

ID or keywords:

Entry

Database: PDB / ID: 2x2y

Title

Cellulomonas fimi endo-beta-1,4-mannanase double mutant

Components

MAN26A

Keywords

HYDROLASE / CLAN GH-A / FAMILY 26 /

GLYCOSIDE HYDROLASE

Function / homology

Function and homology information

substituted mannan metabolic process /

mannan endo-1,4-beta-mannosidase activity /

cellulase activity / cellulose catabolic process /

metal ion binding
Similarity search - Function

Biological species

CELLULOMONAS FIMI (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.35 Å

Authors

Hekmat, O. / Lo Leggio, L. / Rosengren, A. / Kamarauskaite, J. / Kolenova, K. / Staalbrand, H.

Citation

Journal: Biochemistry / Year: 2010
Title: Rational Engineering of Mannosyl Binding in the Distal Glycone Subsites of Cellulomonas Fimi Endo-Beta-1,4-Mannanase: Mannosyl Binding Promoted at Subsite -2 and Demoted at Subsite -3 .
Authors: Hekmat, O. / Lo Leggio, L. / Rosengren, A. / Kamarauskaite, J. / Kolenova, K. / Stalbrand, H.

History

Deposition	Jan 18, 2010	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Jun 23, 2010	Provider: repository / Type: Initial release
Revision 1.1	May 7, 2011	Group: Version format compliance
Revision 1.2	Jul 13, 2011	Group: Version format compliance
Revision 1.3	Jan 17, 2018	Group: Data collection / Category: diffrn_source / Item: _diffrn_source.pdbx_synchrotron_site
Revision 1.4	Mar 6, 2019	Group: Data collection / Experimental preparation / Category: exptl_crystal_grow / Item: _exptl_crystal_grow.method
Revision 1.5	Dec 20, 2023	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 / pdbx_struct_conn_angle / 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 / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _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_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.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	2x2y.cif.gz	196.7 KB	Display	PDBx/mmCIF format
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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/x2/2x2y ftp://data.pdbj.org/pub/pdb/validation_reports/x2/2x2y	HTTPS FTP

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Related structure data

Related structure data	2bvyS 2bvt S: Starting model for refinement
Similar structure data	6obg-1 2bvt-1 4qfu-2 4ffj-1 4qfu-10 4u72-1 2bvy-d 4b6z-2 4r0v-2 4qfu-4 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

Deposited unit

A: MAN26A

B: MAN26A

hetero molecules

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

1

A: MAN26A

hetero molecules

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

2

B: MAN26A

hetero molecules

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

Unit cell

Length a, b, c (Å)	73.093, 99.555, 132.970
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: 1

Dom-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	VAL	VAL	GLY	GLY	1	A	A	447 - 456	447 - 456
2	1	VAL	VAL	GLY	GLY	1	B	B	447 - 456	447 - 456
1	2	GLU	GLU	GLU	GLU	1	A	A	4	4
2	2	GLU	GLU	GLU	GLU	1	B	B	4	4
1	3	HIS	HIS	LEU	LEU	1	A	A	141 - 231	141 - 231
2	3	HIS	HIS	LEU	LEU	1	B	B	141 - 231	141 - 231
1	4	GLU	GLU	GLU	GLU	3	A	A	30	30
2	4	GLU	GLU	GLU	GLU	3	B	B	30	30
1	5	ARG	ARG	ARG	ARG	3	A	A	79	79
2	5	ARG	ARG	ARG	ARG	3	B	B	79	79
1	6	ARG	ARG	ARG	ARG	3	A	A	232	232
2	6	ARG	ARG	ARG	ARG	3	B	B	232	232
1	7	LEU	LEU	LEU	LEU	3	A	A	245	245
2	7	LEU	LEU	LEU	LEU	3	B	B	245	245
1	8	GLN	GLN	GLN	GLN	1	A	A	329	329
2	8	GLN	GLN	GLN	GLN	1	B	B	329	329
1	9	GLU	GLU	GLU	GLU	3	A	A	341	341
2	9	GLU	GLU	GLU	GLU	3	B	B	341	341
1	10	GLN	GLN	GLN	GLN	3	A	A	372	372
2	10	GLN	GLN	GLN	GLN	3	B	B	372	372
1	11	THR	THR	THR	THR	3	A	A	391	391
2	11	THR	THR	THR	THR	3	B	B	391	391
1	12	GLN	GLN	GLN	GLN	3	A	A	403	403
2	12	GLN	GLN	GLN	GLN	3	B	B	403	403
1	13	ASP	ASP	ASP	ASP	3	A	A	420	420
2	13	ASP	ASP	ASP	ASP	3	B	B	420	420
1	14	THR	THR	THR	THR	3	A	A	446	446
2	14	THR	THR	THR	THR	3	B	B	446	446
1	15	THR	THR	ALA	ALA	1	A	A	5 - 11	5 - 11
2	15	THR	THR	ALA	ALA	1	B	B	5 - 11	5 - 11
1	16	ALA	ALA	GLY	GLY	1	A	A	13 - 29	13 - 29
2	16	ALA	ALA	GLY	GLY	1	B	B	13 - 29	13 - 29
1	17	GLY	GLY	GLU	GLU	1	A	A	31 - 78	31 - 78
2	17	GLY	GLY	GLU	GLU	1	B	B	31 - 78	31 - 78
1	18	PRO	PRO	ALA	ALA	1	A	A	80 - 83	80 - 83
2	18	PRO	PRO	ALA	ALA	1	B	B	80 - 83	80 - 83
1	19	THR	THR	GLY	GLY	1	A	A	233 - 244	233 - 244
2	19	THR	THR	GLY	GLY	1	B	B	233 - 244	233 - 244
1	20	ASP	ASP	GLY	GLY	1	A	A	246 - 328	246 - 328
2	20	ASP	ASP	GLY	GLY	1	B	B	246 - 328	246 - 328
1	21	HIS	HIS	LEU	LEU	1	A	A	330 - 340	330 - 340
2	21	HIS	HIS	LEU	LEU	1	B	B	330 - 340	330 - 340
1	22	ASP	ASP	ALA	ALA	1	A	A	342 - 371	342 - 371
2	22	ASP	ASP	ALA	ALA	1	B	B	342 - 371	342 - 371
1	23	PRO	PRO	PRO	PRO	1	A	A	373 - 390	373 - 390
2	23	PRO	PRO	PRO	PRO	1	B	B	373 - 390	373 - 390
1	24	THR	THR	VAL	VAL	1	A	A	392 - 402	392 - 402
2	24	THR	THR	VAL	VAL	1	B	B	392 - 402	392 - 402
1	25	SER	SER	LEU	LEU	1	A	A	404 - 419	404 - 419
2	25	SER	SER	LEU	LEU	1	B	B	404 - 419	404 - 419
1	26	LEU	LEU	TYR	TYR	1	A	A	421 - 445	421 - 445
2	26	LEU	LEU	TYR	TYR	1	B	B	421 - 445	421 - 445
1	27	GLU	GLU	GLU	GLU	3	A	A	84	84
2	27	GLU	GLU	GLU	GLU	3	B	B	84	84
1	28	ASN	ASN	SER	SER	1	A	A	85 - 139	85 - 139
2	28	ASN	ASN	SER	SER	1	B	B	85 - 139	85 - 139
1	29	THR	THR	THR	THR	3	A	A	457	457
2	29	THR	THR	THR	THR	3	B	B	457	457
1	30	LEU	LEU	ALA	ALA	1	A	A	458 - 465	458 - 465
2	30	LEU	LEU	ALA	ALA	1	B	B	458 - 465	458 - 465
1	31	HIS	HIS	HIS	HIS	3	A	A	140	140
2	31	HIS	HIS	HIS	HIS	3	B	B	140	140

NCS ensembles :
NCS oper: (Code: given
Matrix: (1, 0.00526, -0.001397), (0.005272, -0.9999, 0.009144), (-0.001349, -0.009151, -1)
Vector: -36.46, -33.48, -56.34)

#1: Protein	MAN26A / BETA-1 / 4-MANNANASE Mass: 50466.121 Da / Num. of mol.: 2 / Fragment: CATALYTIC AND IGG-LIKE DOMAIN, RESIDUES 52-514 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) CELLULOMONAS FIMI (bacteria) / Plasmid: PET28B / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) References: UniProt: Q9XCV5, mannan endo-1,4-beta-mannosidase
#2: Chemical	ChemComp-MG / MAGNESIUM ION Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#3: Chemical	ChemComp-FMT / FORMIC ACID / Formic acid Mass: 46.025 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: CH₂O₂
#4: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 625 / Source method: isolated from a natural source / Formula: H₂O
Compound details	ENGINEERED RESIDUE IN CHAIN A, ALA 373 TO ARG ENGINEERED RESIDUE IN CHAIN A, PHE 375 TO ALA ...ENGINEERED RESIDUE IN CHAIN A, ALA 373 TO ARG ENGINEERED RESIDUE IN CHAIN A, PHE 375 TO ALA ENGINEERED RESIDUE IN CHAIN B, ALA 373 TO ARG ENGINEERED RESIDUE IN CHAIN B, PHE 375 TO ALA

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.4 Å³/Da / Density % sol: 49 % / Description: NONE
Crystal grow	Method: vapor diffusion / pH: 5.9 Details: VAPOR DIFFUSION. PROTEIN SOLUTION (8.4 MG/ML) IN 50 MM SODIUM CITRATE BUFFER, PH 6.0. RESERVOIR CONDITIONS: 0.2 M MAGNESIUM FORMATE, PH 5.9, 20% PEG 3350

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: MAX II / Beamline: I911-2 / Wavelength: 1.0379
Detector	Type: MARRESEARCH SX-165 / Detector: CCD / Date: Oct 30, 2008 / Details: MULTILAYER MIRROR
Radiation	Monochromator: BENT SI (111) CRYSTAL, HORIZONTALLY FOCUSING / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 1.0379 Å / Relative weight: 1
Reflection	Resolution: 2.35→19.43 Å / Num. obs: 41120 / % possible obs: 99.8 % / Observed criterion σ(I): 0 / Redundancy: 6 % / B_iso Wilson estimate: 27.9 Å² / R_merge(I) obs: 0.11 / Net I/σ(I): 6.6
Reflection shell	Resolution: 2.35→2.48 Å / Redundancy: 5.6 % / R_merge(I) obs: 0.38 / Mean I/σ(I) obs: 2.1 / % possible all: 99.9

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Processing

Software

Name	Version	Classification
REFMAC	5.2.0019	refinement
MOSFLM	VERSION 7.0.1	data reduction
SCALA	3.2.5	data scaling
MOLREP		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2BVY

2bvy

Resolution: 2.35→19.43 Å / Cor.coef. F_o:F_c: 0.962 / Cor.coef. F_o:F_c free: 0.941 / SU B: 5.498 / SU ML: 0.132 / Cross valid method: THROUGHOUT / ESU R: 0.348 / ESU R Free: 0.21 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.19935	2065	5 %	RANDOM
R_work	0.1579	-	-	-
obs	0.15997	38998	99.75 %	-

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: 19.604 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	0.33 Å²	0 Å²	0 Å²
2-	-	-0.4 Å²	0 Å²
3-	-	-	0.07 Å²

Refinement step

Cycle: LAST / Resolution: 2.35→19.43 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	6776	0	28	625	7429

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.009	0.022	7070
X-RAY DIFFRACTION	r_bond_other_d
X-RAY DIFFRACTION	r_angle_refined_deg	1.096	1.93	9684
X-RAY DIFFRACTION	r_angle_other_deg
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.38	5	922
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	34.076	23.939	330
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	13.761	15	954
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	22.331	15	43
X-RAY DIFFRACTION	r_chiral_restr	0.074	0.2	1083
X-RAY DIFFRACTION	r_gen_planes_refined	0.003	0.02	5587
X-RAY DIFFRACTION	r_gen_planes_other
X-RAY DIFFRACTION	r_nbd_refined	0.18	0.2	3167
X-RAY DIFFRACTION	r_nbd_other
X-RAY DIFFRACTION	r_nbtor_refined	0.301	0.2	4815
X-RAY DIFFRACTION	r_nbtor_other
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.172	0.2	554
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	0.204	0.2	39
X-RAY DIFFRACTION	r_symmetry_vdw_other
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.194	0.2	21
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	0.469	1.5	4611
X-RAY DIFFRACTION	r_mcbond_other
X-RAY DIFFRACTION	r_mcangle_it	0.821	2	7199
X-RAY DIFFRACTION	r_mcangle_other
X-RAY DIFFRACTION	r_scbond_it	1.033	3	2855
X-RAY DIFFRACTION	r_scbond_other
X-RAY DIFFRACTION	r_scangle_it	1.635	4.5	2474
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

Ens-ID	Dom-ID	Auth asym-ID	Number	Type	Rms dev position (Å)	Weight position
1	1	A	59	tight positional	0.02	0.05
1	2	B	59	tight positional	0.02	0.05
2	1	A	9	tight positional	0	0.05
2	2	B	9	tight positional	0	0.05
32	32	A	736	tight positional	0.02	0.05
32	32	B	736	tight positional	0.02	0.05
4	1	A	5	tight positional	0	0.05
4	2	B	5	tight positional	0	0.05
5	1	A	5	tight positional	0.01	0.05
5	2	B	5	tight positional	0.01	0.05
6	1	A	3	tight positional	0.01	0.05
6	2	B	3	tight positional	0.01	0.05
7	1	A	4	tight positional	0.01	0.05
7	2	B	4	tight positional	0.01	0.05
8	1	A	9	tight positional	0.01	0.05
8	2	B	9	tight positional	0.01	0.05
9	1	A	8	tight positional	0	0.05
9	2	B	8	tight positional	0	0.05
10	1	A	3	tight positional	0	0.05
10	2	B	3	tight positional	0	0.05
11	1	A	4	tight positional	0.02	0.05
11	2	B	4	tight positional	0.02	0.05
12	1	A	3	tight positional	0.02	0.05
12	2	B	3	tight positional	0.02	0.05
13	1	A	5	tight positional	0	0.05
14	1	A	4	tight positional	0.01	0.05
15	1	A	48	tight positional	0.02	0.05
15	2	B	48	tight positional	0.02	0.05
16	1	A	126	tight positional	0.02	0.05
16	2	B	126	tight positional	0.02	0.05
17	1	A	357	tight positional	0.02	0.05
17	2	B	357	tight positional	0.02	0.05
18	1	A	24	tight positional	0.02	0.05
18	2	B	24	tight positional	0.02	0.05
19	1	A	88	tight positional	0.02	0.05
19	2	B	88	tight positional	0.02	0.05
20	1	A	608	tight positional	0.02	0.05
20	2	B	608	tight positional	0.02	0.05
21	1	A	82	tight positional	0.02	0.05
21	2	B	82	tight positional	0.02	0.05
22	1	A	221	tight positional	0.02	0.05
23	1	A	104	tight positional	0.02	0.05
24	1	A	80	tight positional	0.02	0.05
24	2	B	80	tight positional	0.02	0.05
25	1	A	101	tight positional	0.02	0.05
25	2	B	101	tight positional	0.02	0.05
26	1	A	136	tight positional	0.02	0.05
26	2	B	136	tight positional	0.02	0.05
27	1	A	3	tight positional	0.01	0.05
27	2	B	3	tight positional	0.01	0.05
28	1	A	406	tight positional	0.02	0.05
28	2	B	406	tight positional	0.02	0.05
29	1	A	4	tight positional	0.02	0.05
29	2	B	4	tight positional	0.02	0.05
30	1	A	59	tight positional	0.02	0.05
30	2	B	59	tight positional	0.02	0.05
31	1	A	4	tight positional	0.01	0.05
31	2	B	4	tight positional	0.01	0.05
4	1	A	10	loose positional	0.14	5
4	2	B	10	loose positional	0.14	5
5	1	A	14	loose positional	1.45	5
5	2	B	14	loose positional	1.45	5
7	1	A	4	loose positional	0.93	5
7	2	B	4	loose positional	0.93	5
9	1	A	10	loose positional	0.16	5
9	2	B	10	loose positional	0.16	5
11	1	A	3	loose positional	1.05	5
11	2	B	3	loose positional	1.05	5
13	1	A	8	loose positional	0.26	5
14	1	A	3	loose positional	0.74	5
29	1	A	3	loose positional	0.1	5
29	2	B	3	loose positional	0.1	5
31	1	A	6	loose positional	0.74	5
31	2	B	6	loose positional	0.74	5
1	1	A	59	tight thermal	0.07	0.5
1	2	B	59	tight thermal	0.07	0.5
2	1	A	9	tight thermal	0.04	0.5
2	2	B	9	tight thermal	0.04	0.5
32	32	A	736	tight thermal	0.06	0.5
32	32	B	736	tight thermal	0.06	0.5
4	1	A	5	tight thermal	0.04	0.5
4	2	B	5	tight thermal	0.04	0.5
5	1	A	5	tight thermal	0.05	0.5
5	2	B	5	tight thermal	0.05	0.5
6	1	A	3	tight thermal	0.05	0.5
6	2	B	3	tight thermal	0.05	0.5
7	1	A	4	tight thermal	0.05	0.5
7	2	B	4	tight thermal	0.05	0.5
8	1	A	9	tight thermal	0.07	0.5
8	2	B	9	tight thermal	0.07	0.5
9	1	A	8	tight thermal	0.04	0.5
9	2	B	8	tight thermal	0.04	0.5
10	1	A	3	tight thermal	0.15	0.5
10	2	B	3	tight thermal	0.15	0.5
11	1	A	4	tight thermal	0.21	0.5
11	2	B	4	tight thermal	0.21	0.5
12	1	A	3	tight thermal	0.06	0.5
12	2	B	3	tight thermal	0.06	0.5
13	1	A	5	tight thermal	0.06	0.5
14	1	A	4	tight thermal	0.04	0.5
15	1	A	48	tight thermal	0.06	0.5
15	2	B	48	tight thermal	0.06	0.5
16	1	A	126	tight thermal	0.07	0.5
16	2	B	126	tight thermal	0.07	0.5
17	1	A	357	tight thermal	0.06	0.5
17	2	B	357	tight thermal	0.06	0.5
18	1	A	24	tight thermal	0.03	0.5
18	2	B	24	tight thermal	0.03	0.5
19	1	A	88	tight thermal	0.07	0.5
19	2	B	88	tight thermal	0.07	0.5
20	1	A	608	tight thermal	0.06	0.5
20	2	B	608	tight thermal	0.06	0.5
21	1	A	82	tight thermal	0.06	0.5
21	2	B	82	tight thermal	0.06	0.5
22	1	A	221	tight thermal	0.07	0.5
23	1	A	104	tight thermal	0.07	0.5
24	1	A	80	tight thermal	0.07	0.5
24	2	B	80	tight thermal	0.07	0.5
25	1	A	101	tight thermal	0.03	0.5
25	2	B	101	tight thermal	0.03	0.5
26	1	A	136	tight thermal	0.07	0.5
26	2	B	136	tight thermal	0.07	0.5
27	1	A	3	tight thermal	0.13	0.5
27	2	B	3	tight thermal	0.13	0.5
28	1	A	406	tight thermal	0.06	0.5
28	2	B	406	tight thermal	0.06	0.5
29	1	A	4	tight thermal	0.09	0.5
29	2	B	4	tight thermal	0.09	0.5
30	1	A	59	tight thermal	0.07	0.5
30	2	B	59	tight thermal	0.07	0.5
31	1	A	4	tight thermal	0.09	0.5
31	2	B	4	tight thermal	0.09	0.5
4	1	A	10	loose thermal	0.32	10
4	2	B	10	loose thermal	0.32	10
5	1	A	14	loose thermal	1.22	10
5	2	B	14	loose thermal	1.22	10
7	1	A	4	loose thermal	0.65	10
7	2	B	4	loose thermal	0.65	10
9	1	A	10	loose thermal	0.16	10
9	2	B	10	loose thermal	0.16	10
11	1	A	3	loose thermal	1.04	10
11	2	B	3	loose thermal	1.04	10
13	1	A	8	loose thermal	0.32	10
14	1	A	3	loose thermal	0.15	10
29	1	A	3	loose thermal	0.39	10
29	2	B	3	loose thermal	0.39	10
31	1	A	6	loose thermal	1.13	10
31	2	B	6	loose thermal	1.13	10

LS refinement shell

Resolution: 2.35→2.411 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.237	142	-
R_work	0.201	2855	-
obs	-	-	99.83 %

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