PDB-5tj4: Gasdermin-B C-terminal domain containing the polymorphism residue...

ID or keywords:

Entry

Database: PDB / ID: 5tj4

Title

Gasdermin-B C-terminal domain containing the polymorphism residues Gly299:Pro306 fused to maltose binding protein

Components

Sugar ABC transporter substrate-binding protein,Gasdermin-B fusion protein

Keywords

LIGAND BINDING PROTEIN / alpha helices / fusion protein / C-terminal domain / 1 SNP

Function / homology

Function and homology information

cytotoxic T cell pyroptotic cell death / wide pore channel activity / killing by host of symbiont cells / cardiolipin binding / phosphatidylinositol-4-phosphate binding / phosphatidylserine binding / pyroptotic inflammatory response / phosphatidylinositol-4,5-bisphosphate binding / phospholipid binding / defense response to Gram-negative bacterium ...
Similarity search - Function

Biological species

Escherichia coli (E. coli)

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT /

molecular replacement / Resolution: 3.5 Å

Authors

Chao, L.K. / Herzberg, O.

Funding support

United States, 1items

Citation

Journal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2017
Title: Gene polymorphism linked to increased asthma and IBD risk alters gasdermin-B structure, a sulfatide and phosphoinositide binding protein.
Authors: Chao, K.L. / Kulakova, L. / Herzberg, O.

History

Deposition	Oct 3, 2016	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Feb 1, 2017	Provider: repository / Type: Initial release
Revision 1.1	Sep 20, 2017	Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.2	May 16, 2018	Group: Data collection / Database references / Category: citation / citation_author Item: _citation.journal_abbrev / _citation.journal_volume ..._citation.journal_abbrev / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.name
Revision 1.3	Dec 25, 2019	Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 2.0	Jul 29, 2020	Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Non-polymer description / Structure summary Category: atom_site / chem_comp ...atom_site / chem_comp / entity / entity_name_com / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_molecule_features / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / struct_asym / struct_conn / struct_conn_type / struct_site / struct_site_gen Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _struct_asym.entity_id Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1	Oct 4, 2023	Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _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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Download

PDBx/mmCIF format	5tj4.cif.gz	991 KB	Display	PDBx/mmCIF format
PDB format	pdb5tj4.ent.gz	807.7 KB	Display	PDB format
PDBx/mmJSON format	5tj4.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Summary document	5tj4_validation.pdf.gz	3.6 MB	Display	wwPDB validaton report
Full document	5tj4_full_validation.pdf.gz	3.7 MB	Display
Data in XML	5tj4_validation.xml.gz	179.9 KB	Display
Data in CIF	5tj4_validation.cif.gz	244.7 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/tj/5tj4 ftp://data.pdbj.org/pub/pdb/validation_reports/tj/5tj4	HTTPS FTP

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Related structure data

Related structure data	5tibS 5tj2 S: Starting model for refinement
Similar structure data	5tj2-3 4emz-2 5tib-1 5l6w-d 5jj4-1 1gwb-d 4yz5-2 3n95-7 6zpv-d 6d1u-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) Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search

Related structure data

5tibS

5tj2

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	#100 - Apr 2008 Adrenergic Receptors similarity (1) #138 - Jun 2011 Glucansucrase similarity (1) #205 - Jan 2017 Nuclear Pore Complex similarity (1) #208 - Apr 2017 Glucose Transporters similarity (1) #221 - May 2018 Human Papillomavirus and Vaccines similarity (1) #74 - Feb 2006 alpha-Amylase similarity (1)

Deposited unit

A: Sugar ABC transporter substrate-binding protein,Gasdermin-B fusion protein

B: Sugar ABC transporter substrate-binding protein,Gasdermin-B fusion protein

C: Sugar ABC transporter substrate-binding protein,Gasdermin-B fusion protein

D: Sugar ABC transporter substrate-binding protein,Gasdermin-B fusion protein

E: Sugar ABC transporter substrate-binding protein,Gasdermin-B fusion protein

F: Sugar ABC transporter substrate-binding protein,Gasdermin-B fusion protein

G: Sugar ABC transporter substrate-binding protein,Gasdermin-B fusion protein

H: Sugar ABC transporter substrate-binding protein,Gasdermin-B fusion protein

I: Sugar ABC transporter substrate-binding protein,Gasdermin-B fusion protein

J: Sugar ABC transporter substrate-binding protein,Gasdermin-B fusion protein

hetero molecules

617 kDa, 10 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Sugar ABC transporter substrate-binding protein,Gasdermin-B fusion protein

hetero molecules

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

2

B: Sugar ABC transporter substrate-binding protein,Gasdermin-B fusion protein

hetero molecules

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

3

C: Sugar ABC transporter substrate-binding protein,Gasdermin-B fusion protein

hetero molecules

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

4

D: Sugar ABC transporter substrate-binding protein,Gasdermin-B fusion protein

hetero molecules

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

5

E: Sugar ABC transporter substrate-binding protein,Gasdermin-B fusion protein

hetero molecules

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

6

F: Sugar ABC transporter substrate-binding protein,Gasdermin-B fusion protein

hetero molecules

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

7

G: Sugar ABC transporter substrate-binding protein,Gasdermin-B fusion protein

hetero molecules

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

8

H: Sugar ABC transporter substrate-binding protein,Gasdermin-B fusion protein

hetero molecules

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

9

I: Sugar ABC transporter substrate-binding protein,Gasdermin-B fusion protein

hetero molecules

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

10

J: Sugar ABC transporter substrate-binding protein,Gasdermin-B fusion protein

hetero molecules

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

Unit cell

Length a, b, c (Å)	89.599, 274.569, 174.019
Angle α, β, γ (deg.)	90.000, 96.090, 90.000
Int Tables number	4
Space group name H-M	P12₁1

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Component-ID: _ / Beg auth comp-ID: LYS / Beg label comp-ID: LYS / Refine code: _

Dom-ID	Ens-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	A	A	1 - 1405	1 - 556
2	1	GLY	GLY	B	B	1 - 1405	1 - 556
1	2	GLY	GLY	A	A	1 - 1405	1 - 556
2	2	GLY	GLY	C	C	1 - 1405	1 - 556
1	3	ALA	ALA	A	A	1 - 1403	1 - 554
2	3	ALA	ALA	D	D	1 - 1403	1 - 554
1	4	GLY	GLY	A	A	1 - 1405	1 - 556
2	4	GLY	GLY	E	E	1 - 1405	1 - 556
1	5	GLY	GLY	A	A	1 - 1405	1 - 556
2	5	GLY	GLY	F	F	1 - 1405	1 - 556
1	6	GLY	GLY	A	A	1 - 1405	1 - 556
2	6	GLY	GLY	G	G	1 - 1405	1 - 556
1	7	GLY	GLY	A	A	1 - 1405	1 - 556
2	7	GLY	GLY	H	H	1 - 1405	1 - 556
1	8	ALA	ALA	A	A	1 - 1403	1 - 554
2	8	ALA	ALA	I	I	1 - 1403	1 - 554
1	9	GLY	GLY	A	A	1 - 1405	1 - 556
2	9	GLY	GLY	J	J	1 - 1405	1 - 556
1	10	THR	THR	B	B	1 - 1407	1 - 558
2	10	THR	THR	C	C	1 - 1407	1 - 558
1	11	ALA	ALA	B	B	1 - 1403	1 - 554
2	11	ALA	ALA	D	D	1 - 1403	1 - 554
1	12	VAL	VAL	B	B	1 - 1409	1 - 560
2	12	VAL	VAL	E	E	1 - 1409	1 - 560
1	13	GLY	GLY	B	B	1 - 1405	1 - 556
2	13	GLY	GLY	F	F	1 - 1405	1 - 556
1	14	THR	THR	B	B	1 - 1407	1 - 558
2	14	THR	THR	G	G	1 - 1407	1 - 558
1	15	VAL	VAL	B	B	1 - 1409	1 - 560
2	15	VAL	VAL	H	H	1 - 1409	1 - 560
1	16	ALA	ALA	B	B	1 - 1403	1 - 554
2	16	ALA	ALA	I	I	1 - 1403	1 - 554
1	17	SER	SER	B	B	1 - 1408	1 - 559
2	17	SER	SER	J	J	1 - 1408	1 - 559
1	18	ALA	ALA	C	C	1 - 1403	1 - 554
2	18	ALA	ALA	D	D	1 - 1403	1 - 554
1	19	THR	THR	C	C	1 - 1407	1 - 558
2	19	THR	THR	E	E	1 - 1407	1 - 558
1	20	GLY	GLY	C	C	1 - 1405	1 - 556
2	20	GLY	GLY	F	F	1 - 1405	1 - 556
1	21	THR	THR	C	C	1 - 1407	1 - 558
2	21	THR	THR	G	G	1 - 1407	1 - 558
1	22	THR	THR	C	C	1 - 1407	1 - 558
2	22	THR	THR	H	H	1 - 1407	1 - 558
1	23	ALA	ALA	C	C	1 - 1403	1 - 554
2	23	ALA	ALA	I	I	1 - 1403	1 - 554
1	24	THR	THR	C	C	1 - 1407	1 - 558
2	24	THR	THR	J	J	1 - 1407	1 - 558
1	25	ALA	ALA	D	D	1 - 1403	1 - 554
2	25	ALA	ALA	E	E	1 - 1403	1 - 554
1	26	ALA	ALA	D	D	1 - 1403	1 - 554
2	26	ALA	ALA	F	F	1 - 1403	1 - 554
1	27	LEU	LEU	D	D	1 - 1402	1 - 553
2	27	LEU	LEU	G	G	1 - 1402	1 - 553
1	28	ALA	ALA	D	D	1 - 1403	1 - 554
2	28	ALA	ALA	H	H	1 - 1403	1 - 554
1	29	ALA	ALA	D	D	1 - 1403	1 - 554
2	29	ALA	ALA	I	I	1 - 1403	1 - 554
1	30	ALA	ALA	D	D	1 - 1403	1 - 554
2	30	ALA	ALA	J	J	1 - 1403	1 - 554
1	31	GLY	GLY	E	E	1 - 1405	1 - 556
2	31	GLY	GLY	F	F	1 - 1405	1 - 556
1	32	THR	THR	E	E	1 - 1407	1 - 558
2	32	THR	THR	G	G	1 - 1407	1 - 558
1	33	VAL	VAL	E	E	1 - 1409	1 - 560
2	33	VAL	VAL	H	H	1 - 1409	1 - 560
1	34	ALA	ALA	E	E	1 - 1403	1 - 554
2	34	ALA	ALA	I	I	1 - 1403	1 - 554
1	35	SER	SER	E	E	1 - 1408	1 - 559
2	35	SER	SER	J	J	1 - 1408	1 - 559
1	36	GLY	GLY	F	F	1 - 1405	1 - 556
2	36	GLY	GLY	G	G	1 - 1405	1 - 556
1	37	GLY	GLY	F	F	1 - 1405	1 - 556
2	37	GLY	GLY	H	H	1 - 1405	1 - 556
1	38	ALA	ALA	F	F	1 - 1403	1 - 554
2	38	ALA	ALA	I	I	1 - 1403	1 - 554
1	39	GLY	GLY	F	F	1 - 1405	1 - 556
2	39	GLY	GLY	J	J	1 - 1405	1 - 556
1	40	THR	THR	G	G	1 - 1407	1 - 558
2	40	THR	THR	H	H	1 - 1407	1 - 558
1	41	ALA	ALA	G	G	1 - 1403	1 - 554
2	41	ALA	ALA	I	I	1 - 1403	1 - 554
1	42	THR	THR	G	G	1 - 1407	1 - 558
2	42	THR	THR	J	J	1 - 1407	1 - 558
1	43	ALA	ALA	H	H	1 - 1403	1 - 554
2	43	ALA	ALA	I	I	1 - 1403	1 - 554
1	44	SER	SER	H	H	1 - 1408	1 - 559
2	44	SER	SER	J	J	1 - 1408	1 - 559
1	45	ALA	ALA	I	I	1 - 1403	1 - 554
2	45	ALA	ALA	J	J	1 - 1403	1 - 554

NCS ensembles :

#1: Protein

Sugar ABC transporter substrate-binding protein,Gasdermin-B fusion protein / Gasdermin-like protein

Mass: 61370.527 Da / Num. of mol.: 10
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli, Homo sapiens / Gene: malE, OO96_18925, GSDMB, GSDML, PP4052, PRO2521 / Plasmid: pMALX(E) / Production host:

Escherichia coli (E. coli) / References: UniProt: A0A178SBV6, UniProt: Q8TAX9

#2: Polysaccharide

alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-maltose

Type: oligosaccharide, Oligosaccharide / Class: Nutrient / Mass: 342.297 Da / Num. of mol.: 10
Source method: isolated from a genetically manipulated source
Details: oligosaccharide / References: alpha-maltose

#3: Chemical

ChemComp-NA / SODIUM ION

Mass: 22.990 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Na

Sequence details

The sequence of this entry corresponds to a common polymorphism present in half of the population.

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 3.47 Å³/Da / Density % sol: 64.53 %
Crystal grow	Temperature: 295 K / Method: vapor diffusion / pH: 6 / Details: 2.1 M sodium malonate / Temp details: room temperature

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Data collection

Diffraction	Mean temperature: 80 K / Ambient temp details: liquid nitrogen
Diffraction source	Source: SYNCHROTRON / Site: APS / Beamline: 23-ID-B / Wavelength: 1.0332 Å
Detector	Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Nov 14, 2015
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 1.0332 Å / Relative weight: 1
Reflection	Resolution: 3.5→173.04 Å / Num. obs: 99563 / % possible obs: 99.7 % / Redundancy: 2.6 % / R_merge(I) obs: 0.094 / Net I/σ(I): 8.5

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Phasing

Phasing	Method: molecular replacement

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Processing

Software

Name	Version	Classification
MOSFLM		data reduction
Aimless		data scaling
PHASER		phasing
REFMAC	5.8.0135	refinement
PDB_EXTRACT	3.2	data extraction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 5TIB

5tib

Resolution: 3.5→173.04 Å / Cor.coef. F_o:F_c: 0.917 / Cor.coef. F_o:F_c free: 0.893 / SU B: 33.775 / SU ML: 0.504 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.56
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.2485	5198	5 %	RANDOM
R_work	0.213	-	-	-
obs	0.2148	99563	99.74 %	-

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å

Displacement parameters

B_iso max: 229.18 Å² / B_iso mean: 89.428 Å² / B_iso min: 20 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	2.01 Å²	0 Å²	2.94 Å²
2-	-	1.25 Å²	-0 Å²
3-	-	-	-3.8 Å²

Refinement step

Cycle: final / Resolution: 3.5→173.04 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	39606	0	232	0	39838
B_iso mean	-	-	65.07	-	-
Num. residues	-	-	-	-	5462

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.012	0.019	40675
X-RAY DIFFRACTION	r_bond_other_d	0.01	0.02	37264
X-RAY DIFFRACTION	r_angle_refined_deg	1.678	1.97	55644
X-RAY DIFFRACTION	r_angle_other_deg	1.988	3	85230
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.823	5	5431
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	34.587	25.51	1548
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	17.56	15	5708
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	21.913	15	100
X-RAY DIFFRACTION	r_chiral_restr	0.097	0.2	6559
X-RAY DIFFRACTION	r_gen_planes_refined	0.007	0.021	47165
X-RAY DIFFRACTION	r_gen_planes_other	0.006	0.02	8657
X-RAY DIFFRACTION	r_mcbond_it	6.012	9.343	21817
X-RAY DIFFRACTION	r_mcbond_other	6.012	9.342	21816
X-RAY DIFFRACTION	r_mcangle_it	9.732	14.007	27217

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	58032	0.09
1	2	B	58032	0.09
2	1	A	58504	0.1
2	2	C	58504	0.1
3	1	A	57624	0.1
3	2	D	57624	0.1
4	1	A	58160	0.1
4	2	E	58160	0.1
5	1	A	56784	0.1
5	2	F	56784	0.1
6	1	A	55524	0.1
6	2	G	55524	0.1
7	1	A	54378	0.1
7	2	H	54378	0.1
8	1	A	53018	0.1
8	2	I	53018	0.1
9	1	A	54252	0.1
9	2	J	54252	0.1
10	1	B	56824	0.1
10	2	C	56824	0.1
11	1	B	58068	0.09
11	2	D	58068	0.09
12	1	B	59298	0.09
12	2	E	59298	0.09
13	1	B	57496	0.09
13	2	F	57496	0.09
14	1	B	56762	0.09
14	2	G	56762	0.09
15	1	B	55342	0.09
15	2	H	55342	0.09
16	1	B	53632	0.09
16	2	I	53632	0.09
17	1	B	55552	0.09
17	2	J	55552	0.09
18	1	C	57292	0.09
18	2	D	57292	0.09
19	1	C	57844	0.1
19	2	E	57844	0.1
20	1	C	56976	0.1
20	2	F	56976	0.1
21	1	C	55048	0.1
21	2	G	55048	0.1
22	1	C	53830	0.1
22	2	H	53830	0.1
23	1	C	52768	0.1
23	2	I	52768	0.1
24	1	C	54252	0.1
24	2	J	54252	0.1
25	1	D	58018	0.08
25	2	E	58018	0.08
26	1	D	57506	0.09
26	2	F	57506	0.09
27	1	D	56088	0.08
27	2	G	56088	0.08
28	1	D	54406	0.09
28	2	H	54406	0.09
29	1	D	53754	0.1
29	2	I	53754	0.1
30	1	D	54450	0.08
30	2	J	54450	0.08
31	1	E	57382	0.09
31	2	F	57382	0.09
32	1	E	56526	0.09
32	2	G	56526	0.09
33	1	E	54940	0.09
33	2	H	54940	0.09
34	1	E	53476	0.1
34	2	I	53476	0.1
35	1	E	55888	0.09
35	2	J	55888	0.09
36	1	F	55648	0.09
36	2	G	55648	0.09
37	1	F	54182	0.09
37	2	H	54182	0.09
38	1	F	53156	0.1
38	2	I	53156	0.1
39	1	F	53754	0.09
39	2	J	53754	0.09
40	1	G	53882	0.09
40	2	H	53882	0.09
41	1	G	52574	0.1
41	2	I	52574	0.1
42	1	G	54292	0.08
42	2	J	54292	0.08
43	1	H	52002	0.1
43	2	I	52002	0.1
44	1	H	52710	0.1
44	2	J	52710	0.1
45	1	I	51380	0.09
45	2	J	51380	0.09

LS refinement shell

Resolution: 3.5→3.591 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.317	415	-
R_work	0.299	7384	-
all	-	7799	-
obs	-	-	99.97 %

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