PDB-2xf8: Structure of the D-Erythrose-4-Phosphate Dehydrogenase from E. co...

ID or keywords:

Entry

Database: PDB / ID: 2xf8

Title

Structure of the D-Erythrose-4-Phosphate Dehydrogenase from E. coli in complex with a NAD cofactor analog (3-Chloroacetyl adenine pyridine dinucleotide) and sulfate anion

Components

D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

Keywords

OXIDOREDUCTASE / ALDEHYDE DEHYDROGENASE / HYDRIDE TRANSFER / COFACTOR ANALOG / PYRIDOXAL PHOPHATE BIOSYNTHESIS

Function / homology

Function and homology information

erythrose-4-phosphate dehydrogenase / erythrose-4-phosphate dehydrogenase activity / pyridoxal phosphate biosynthetic process / pyridoxine biosynthetic process / glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity / glucose metabolic process / NAD binding / cytosol
Similarity search - Function

Biological species

ESCHERICHIA COLI (E. coli)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.95 Å

Authors

Moniot, S. / Didierjean, C. / Boschi-Muller, S. / Branlant, G. / Corbier, C.

Citation

Journal: To be Published
Title: Structural Characterization of Erythrose-4- Phosphate Dehydrogenase from Escherichia Coli: Peculiar Features When Compared to Phosphorylating Gapdhs
Authors: Moniot, S. / Didierjean, C. / Boschi-Muller, S. / Branlant, G. / Corbier, C.

History

Deposition	May 20, 2010	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Jun 8, 2011	Provider: repository / Type: Initial release
Revision 1.1	Jun 9, 2011	Group: Version format compliance
Revision 1.2	Jul 13, 2011	Group: Version format compliance
Revision 1.3	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 / struct_conn / 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 / _struct_conn.pdbx_leaving_atom_flag / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4	Nov 20, 2024	Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	2xf8.cif.gz	960.4 KB	Display	PDBx/mmCIF format
PDB format	pdb2xf8.ent.gz	793.6 KB	Display	PDB format
PDBx/mmJSON format	2xf8.json.gz		Tree view	PDBx/mmJSON format
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Validation report

Summary document	2xf8_validation.pdf.gz	2.3 MB	Display	wwPDB validaton report
Full document	2xf8_full_validation.pdf.gz	2.5 MB	Display
Data in XML	2xf8_validation.xml.gz	185.1 KB	Display
Data in CIF	2xf8_validation.cif.gz	239.4 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/xf/2xf8 ftp://data.pdbj.org/pub/pdb/validation_reports/xf/2xf8	HTTPS FTP

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Related structure data

Related structure data	2x5jSC 2x5kC S: Starting model for refinement C: citing same article (ref.)
Similar structure data	2x5j-d 2x5k-d 2duu-2 5v8y-1 4wnc-2 4dib-2 2hki-1 1rpx-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) Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search

Related structure data

2x5jSC

2x5kC

S: Starting model for refinement

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	#50 - Feb 2004 Glycolytic Enzymes similarity (8)

Deposited unit

A: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

B: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

C: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

D: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

E: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

F: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

G: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

H: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

I: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

J: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

K: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

L: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

M: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

N: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

O: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

P: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

hetero molecules

603 kDa, 16 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

E: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

F: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

G: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

H: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

hetero molecules

defined by author&software
151 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

A: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

B: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

C: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

D: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

hetero molecules

defined by author&software
151 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

M: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

N: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

O: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

P: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

hetero molecules

defined by author&software
151 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

4

I: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

J: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

K: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

L: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE

hetero molecules

defined by author&software
151 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	96.180, 111.660, 135.470
Angle α, β, γ (deg.)	91.30, 96.11, 88.44
Int Tables number	1
Space group name H-M	P1

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Dom-ID	Component-ID	Ens-ID	Refine code	Auth asym-ID	Auth seq-ID
1	1	1	2	A	1 - 21
2	1	1	2	B	1 - 21
3	1	1	2	C	1 - 21
4	1	1	2	D	1 - 21
5	1	1	2	E	1 - 21
6	1	1	2	F	1 - 21
7	1	1	2	G	1 - 21
8	1	1	2	H	1 - 21
9	1	1	2	I	1 - 21
10	1	1	2	J	1 - 21
11	1	1	2	K	1 - 21
12	1	1	2	L	1 - 21
13	1	1	2	M	1 - 21
14	1	1	2	N	1 - 21
15	1	1	2	O	1 - 21
16	1	1	2	P	1 - 21
1	2	1	2	A	27 - 30
2	2	1	2	B	27 - 30
3	2	1	2	C	27 - 30
4	2	1	2	D	27 - 30
5	2	1	2	E	27 - 30
6	2	1	2	F	27 - 30
7	2	1	2	G	27 - 30
8	2	1	2	H	27 - 30
9	2	1	2	I	27 - 30
10	2	1	2	J	27 - 30
11	2	1	2	K	27 - 30
12	2	1	2	L	27 - 30
13	2	1	2	M	27 - 30
14	2	1	2	N	27 - 30
15	2	1	2	O	27 - 30
16	2	1	2	P	27 - 30
1	3	1	2	A	41 - 46
2	3	1	2	B	41 - 46
3	3	1	2	C	41 - 46
4	3	1	2	D	41 - 46
5	3	1	2	E	41 - 46
6	3	1	2	F	41 - 46
7	3	1	2	G	41 - 46
8	3	1	2	H	41 - 46
9	3	1	2	I	41 - 46
10	3	1	2	J	41 - 46
11	3	1	2	K	41 - 46
12	3	1	2	L	41 - 46
13	3	1	2	M	41 - 46
14	3	1	2	N	41 - 46
15	3	1	2	O	41 - 46
16	3	1	2	P	41 - 46
1	4	1	2	A	52 - 57
2	4	1	2	B	52 - 57
3	4	1	2	C	52 - 57
4	4	1	2	D	52 - 57
5	4	1	2	E	52 - 57
6	4	1	2	F	52 - 57
7	4	1	2	G	52 - 57
8	4	1	2	H	52 - 57
9	4	1	2	I	52 - 57
10	4	1	2	J	52 - 57
11	4	1	2	K	52 - 57
12	4	1	2	L	52 - 57
13	4	1	2	M	52 - 57
14	4	1	2	N	52 - 57
15	4	1	2	O	52 - 57
16	4	1	2	P	52 - 57
1	5	1	2	A	73 - 75
2	5	1	2	B	73 - 75
3	5	1	2	C	73 - 75
4	5	1	2	D	73 - 75
5	5	1	2	E	73 - 75
6	5	1	2	F	73 - 75
7	5	1	2	G	73 - 75
8	5	1	2	H	73 - 75
9	5	1	2	I	73 - 75
10	5	1	2	J	73 - 75
11	5	1	2	K	73 - 75
12	5	1	2	L	73 - 75
13	5	1	2	M	73 - 75
14	5	1	2	N	73 - 75
15	5	1	2	O	73 - 75
16	5	1	2	P	73 - 75
1	6	1	2	A	81 - 100
2	6	1	2	B	81 - 100
3	6	1	2	C	81 - 100
4	6	1	2	D	81 - 100
5	6	1	2	E	81 - 100
6	6	1	2	F	81 - 100
7	6	1	2	G	81 - 100
8	6	1	2	H	81 - 100
9	6	1	2	I	81 - 100
10	6	1	2	J	81 - 100
11	6	1	2	K	81 - 100
12	6	1	2	L	81 - 100
13	6	1	2	M	81 - 100
14	6	1	2	N	81 - 100
15	6	1	2	O	81 - 100
16	6	1	2	P	81 - 100
1	7	1	2	A	103 - 120
2	7	1	2	B	103 - 120
3	7	1	2	C	103 - 120
4	7	1	2	D	103 - 120
5	7	1	2	E	103 - 120
6	7	1	2	F	103 - 120
7	7	1	2	G	103 - 120
8	7	1	2	H	103 - 120
9	7	1	2	I	103 - 120
10	7	1	2	J	103 - 120
11	7	1	2	K	103 - 120
12	7	1	2	L	103 - 120
13	7	1	2	M	103 - 120
14	7	1	2	N	103 - 120
15	7	1	2	O	103 - 120
16	7	1	2	P	103 - 120
1	8	1	2	A	128 - 136
2	8	1	2	B	128 - 136
3	8	1	2	C	128 - 136
4	8	1	2	D	128 - 136
5	8	1	2	E	128 - 136
6	8	1	2	F	128 - 136
7	8	1	2	G	128 - 136
8	8	1	2	H	128 - 136
9	8	1	2	I	128 - 136
10	8	1	2	J	128 - 136
11	8	1	2	K	128 - 136
12	8	1	2	L	128 - 136
13	8	1	2	M	128 - 136
14	8	1	2	N	128 - 136
15	8	1	2	O	128 - 136
16	8	1	2	P	128 - 136
1	9	1	2	A	142 - 182
2	9	1	2	B	142 - 182
3	9	1	2	C	142 - 182
4	9	1	2	D	142 - 182
5	9	1	2	E	142 - 182
6	9	1	2	F	142 - 182
7	9	1	2	G	142 - 182
8	9	1	2	H	142 - 182
9	9	1	2	I	142 - 182
10	9	1	2	J	142 - 182
11	9	1	2	K	142 - 182
12	9	1	2	L	142 - 182
13	9	1	2	M	142 - 182
14	9	1	2	N	142 - 182
15	9	1	2	O	142 - 182
16	9	1	2	P	142 - 182
1	10	1	2	A	213 - 263
2	10	1	2	B	213 - 263
3	10	1	2	C	213 - 263
4	10	1	2	D	213 - 263
5	10	1	2	E	213 - 263
6	10	1	2	F	213 - 263
7	10	1	2	G	213 - 263
8	10	1	2	H	213 - 263
9	10	1	2	I	213 - 263
10	10	1	2	J	213 - 263
11	10	1	2	K	213 - 263
12	10	1	2	L	213 - 263
13	10	1	2	M	213 - 263
14	10	1	2	N	213 - 263
15	10	1	2	O	213 - 263
16	10	1	2	P	213 - 263
1	11	1	2	A	265 - 330
2	11	1	2	B	265 - 330
3	11	1	2	C	265 - 330
4	11	1	2	D	265 - 330
5	11	1	2	E	265 - 330
6	11	1	2	F	265 - 330
7	11	1	2	G	265 - 330
8	11	1	2	H	265 - 330
9	11	1	2	I	265 - 330
10	11	1	2	J	265 - 330
11	11	1	2	K	265 - 330
12	11	1	2	L	265 - 330
13	11	1	2	M	265 - 330
14	11	1	2	N	265 - 330
15	11	1	2	O	265 - 330
16	11	1	2	P	265 - 330

#1: Protein	D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE / E4PDH Mass: 37216.133 Da / Num. of mol.: 16 Source method: isolated from a genetically manipulated source Details: D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE IN COVALENT COMPLEX WITH A COFACTOR ANALOG THROUGH ITS CATALYTIC CYSTEINE (C149) Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Strain: K-12 / Variant: TG1 / Plasmid: PBLUESCRIPT(SK) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): K-12 / Variant (production host): HB101 References: UniProt: P0A9B6, erythrose-4-phosphate dehydrogenase
#2: Chemical	ChemComp-SO4 / SULFATE ION Mass: 96.063 Da / Num. of mol.: 16 / Source method: obtained synthetically / Formula: SO₄
#3: Chemical	ChemComp-3CD / 3-(CHLOROACETYL) PYRIDINE ADENINE DINUCLEOTIDE / 3-CAPAD Mass: 697.890 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C₂₂H₂₈ClN₆O₁₄P₂
#4: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 171 / Source method: isolated from a natural source / Formula: H₂O
Has protein modification	Y
Nonpolymer details	3-(CHLOROACETYL)PYRIDINE ADENINE DINUCLEOTIDE (3CD): COVALENTLY BOND TO THE CATALYTIC CYSTEINE C149

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.57 Å³/Da / Density % sol: 51.7 % / Description: NONE
Crystal grow	pH: 8.5 Details: 20 % (W/V) PEG 2000 MME, 100 MM TRIS-HCL BUFFER PH 8.5, 200 MM LI2SO4

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.9395
Detector	Type: ADSC CCD / Detector: CCD
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9395 Å / Relative weight: 1
Reflection	Resolution: 2.95→48.7 Å / Num. obs: 112592 / % possible obs: 95.4 % / Observed criterion σ(I): 0 / Redundancy: 2.1 % / R_merge(I) obs: 0.09 / Net I/σ(I): 10.1
Reflection shell	Resolution: 2.95→3.03 Å / Redundancy: 2 % / R_merge(I) obs: 0.49 / Mean I/σ(I) obs: 2 / % possible all: 95.8

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Processing

Software

Name	Version	Classification
REFMAC	5.5.0109	refinement
XDS		data reduction
XSCALE		data scaling
MOLREP		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2X5J

2x5j

Resolution: 2.95→48.72 Å / Cor.coef. F_o:F_c: 0.908 / Cor.coef. F_o:F_c free: 0.868 / SU B: 25.079 / SU ML: 0.452 / Cross valid method: THROUGHOUT / ESU R Free: 0.515 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY.

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.27981	5630	5 %	RANDOM
R_work	0.23688	-	-	-
obs	0.23904	106962	100 %	-

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: 38.162 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	4.95 Å²	-2.66 Å²	-2.68 Å²
2-	-	-2.48 Å²	-0.83 Å²
3-	-	-	-2.93 Å²

Refinement step

Cycle: LAST / Resolution: 2.95→48.72 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	39641	0	432	171	40244

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.013	0.021	40811
X-RAY DIFFRACTION	r_bond_other_d	0.009	0.02	26556
X-RAY DIFFRACTION	r_angle_refined_deg	1.691	1.948	55596
X-RAY DIFFRACTION	r_angle_other_deg	1.825	3	64526
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	6.109	5	5120
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	37.639	23.413	1846
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	18.744	15	6496
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	19.064	15	341
X-RAY DIFFRACTION	r_chiral_restr	0.063	0.2	6556
X-RAY DIFFRACTION	r_gen_planes_refined	0.006	0.02	45614
X-RAY DIFFRACTION	r_gen_planes_other	0.002	0.02	8427
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	0.471	1.5	25543
X-RAY DIFFRACTION	r_mcbond_other	0.059	1.5	10492
X-RAY DIFFRACTION	r_mcangle_it	0.906	2	41217
X-RAY DIFFRACTION	r_mcangle_other
X-RAY DIFFRACTION	r_scbond_it	1.087	3	15268
X-RAY DIFFRACTION	r_scbond_other
X-RAY DIFFRACTION	r_scangle_it	1.995	4.5	14379
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

Ens-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Dom-ID	Auth asym-ID	Number	Type	Rms dev position (Å)	Weight position
1	A	1422	tight positional	0.03	0.05
2	B	1422	tight positional	0.04	0.05
3	C	1422	tight positional	0.03	0.05
4	D	1422	tight positional	0.03	0.05
5	E	1422	tight positional	0.04	0.05
6	F	1422	tight positional	0.03	0.05
7	G	1422	tight positional	0.03	0.05
8	H	1422	tight positional	0.03	0.05
9	I	1422	tight positional	0.03	0.05
10	J	1422	tight positional	0.03	0.05
11	K	1422	tight positional	0.03	0.05
12	L	1422	tight positional	0.03	0.05
13	M	1422	tight positional	0.03	0.05
14	N	1422	tight positional	0.03	0.05
15	O	1422	tight positional	0.03	0.05
16	P	1422	tight positional	0.03	0.05
1	A	1645	medium positional	0.09	0.5
2	B	1645	medium positional	0.14	0.5
3	C	1645	medium positional	0.09	0.5
4	D	1645	medium positional	0.16	0.5
5	E	1645	medium positional	0.14	0.5
6	F	1645	medium positional	0.15	0.5
7	G	1645	medium positional	0.11	0.5
8	H	1645	medium positional	0.1	0.5
9	I	1645	medium positional	0.09	0.5
10	J	1645	medium positional	0.11	0.5
11	K	1645	medium positional	0.11	0.5
12	L	1645	medium positional	0.12	0.5
13	M	1645	medium positional	0.15	0.5
14	N	1645	medium positional	0.1	0.5
15	O	1645	medium positional	0.09	0.5
16	P	1645	medium positional	0.12	0.5
1	A	1422	tight thermal	0.06	0.5
2	B	1422	tight thermal	0.06	0.5
3	C	1422	tight thermal	0.06	0.5
4	D	1422	tight thermal	0.07	0.5
5	E	1422	tight thermal	0.07	0.5
6	F	1422	tight thermal	0.06	0.5
7	G	1422	tight thermal	0.06	0.5
8	H	1422	tight thermal	0.05	0.5
9	I	1422	tight thermal	0.07	0.5
10	J	1422	tight thermal	0.06	0.5
11	K	1422	tight thermal	0.07	0.5
12	L	1422	tight thermal	0.07	0.5
13	M	1422	tight thermal	0.05	0.5
14	N	1422	tight thermal	0.07	0.5
15	O	1422	tight thermal	0.09	0.5
16	P	1422	tight thermal	0.06	0.5
1	A	1645	medium thermal	0.05	2
2	B	1645	medium thermal	0.05	2
3	C	1645	medium thermal	0.05	2
4	D	1645	medium thermal	0.05	2
5	E	1645	medium thermal	0.05	2
6	F	1645	medium thermal	0.05	2
7	G	1645	medium thermal	0.05	2
8	H	1645	medium thermal	0.05	2
9	I	1645	medium thermal	0.05	2
10	J	1645	medium thermal	0.05	2
11	K	1645	medium thermal	0.05	2
12	L	1645	medium thermal	0.06	2
13	M	1645	medium thermal	0.05	2
14	N	1645	medium thermal	0.05	2
15	O	1645	medium thermal	0.06	2
16	P	1645	medium thermal	0.05	2

LS refinement shell

Resolution: 2.95→3.026 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.378	419	-
R_work	0.331	7954	-
obs	-	-	100 %

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