PDB-2qr0: Structure of VEGF complexed to a Fab containing TYR and SER in th...

ID or keywords:

Entry

Database: PDB / ID: 2qr0

Title

Structure of VEGF complexed to a Fab containing TYR and SER in the CDRs

Components

Fab-Fragment Heavy Chain
Fab-Fragment Light Chain
Vascular endothelial growth factor A

Keywords

IMMUNE SYSTEM / VEGF / Antibody Recognition / Specificity / Phage Display

Function / homology

Function and homology information

basophil chemotaxis / positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway / VEGF-A complex / Signaling by VEGF / cellular stress response to acid chemical / positive regulation of lymphangiogenesis / negative regulation of adherens junction organization / vascular endothelial growth factor receptor 1 binding / negative regulation of establishment of endothelial barrier / vascular endothelial growth factor receptor binding ...basophil chemotaxis / positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway / VEGF-A complex / Signaling by VEGF / cellular stress response to acid chemical / positive regulation of lymphangiogenesis / negative regulation of adherens junction organization / vascular endothelial growth factor receptor 1 binding / negative regulation of establishment of endothelial barrier / vascular endothelial growth factor receptor binding / VEGF ligand-receptor interactions / post-embryonic camera-type eye development / positive regulation of mast cell chemotaxis / lymph vessel morphogenesis / primitive erythrocyte differentiation / negative regulation of blood-brain barrier permeability / positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway / VEGF-activated neuropilin signaling pathway / bone trabecula formation / coronary vein morphogenesis / lung vasculature development / cardiac vascular smooth muscle cell development / lymphangiogenesis / endothelial cell chemotaxis / positive regulation of trophoblast cell migration / vascular endothelial growth factor receptor-2 signaling pathway / positive regulation of epithelial tube formation / VEGF binds to VEGFR leading to receptor dimerization / motor neuron migration / regulation of nitric oxide mediated signal transduction / positive regulation of protein localization to early endosome / eye photoreceptor cell development / positive regulation of axon extension involved in axon guidance / vascular wound healing / regulation of hematopoietic progenitor cell differentiation / positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis / camera-type eye morphogenesis / positive regulation of branching involved in ureteric bud morphogenesis / neuropilin binding / coronary artery morphogenesis / induction of positive chemotaxis / transmembrane receptor protein tyrosine kinase activator activity / negative regulation of cell-cell adhesion mediated by cadherin / vascular endothelial growth factor receptor 2 binding / commissural neuron axon guidance / dopaminergic neuron differentiation / tube formation / positive regulation of vascular endothelial growth factor signaling pathway / positive regulation of vascular permeability / positive regulation of blood vessel branching / platelet-derived growth factor receptor binding / surfactant homeostasis / endothelial cell proliferation / extracellular matrix binding / cell migration involved in sprouting angiogenesis / epithelial cell maturation / positive regulation of leukocyte migration / positive regulation of positive chemotaxis / cardiac muscle cell development / sprouting angiogenesis / Regulation of gene expression by Hypoxia-inducible Factor / positive regulation of endothelial cell chemotaxis / vascular endothelial growth factor signaling pathway / artery morphogenesis / negative regulation of epithelial to mesenchymal transition / positive regulation of cell migration involved in sprouting angiogenesis / positive regulation of peptidyl-tyrosine phosphorylation / positive regulation of DNA biosynthetic process / retinal ganglion cell axon guidance / branching involved in blood vessel morphogenesis / positive regulation of neuroblast proliferation / negative regulation of fat cell differentiation / positive chemotaxis / positive regulation of sprouting angiogenesis / chemoattractant activity / mesoderm development / outflow tract morphogenesis / positive regulation of protein autophosphorylation / monocyte differentiation / macrophage differentiation / fibronectin binding / positive regulation of cell division / positive regulation of receptor internalization / mammary gland alveolus development / neuroblast proliferation / cellular response to vascular endothelial growth factor stimulus / positive regulation of focal adhesion assembly / positive regulation of blood vessel endothelial cell migration / vascular endothelial growth factor receptor signaling pathway / positive regulation of osteoblast differentiation / vasculogenesis / heart morphogenesis / cell maturation / ovarian follicle development / homeostasis of number of cells within a tissue / positive regulation of endothelial cell proliferation / lactation / TFAP2 (AP-2) family regulates transcription of growth factors and their receptors / epithelial cell differentiation / positive regulation of endothelial cell migration
Similarity search - Function

Biological species

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT /

molecular replacement / Resolution: 3.5 Å

Authors

Wiesmann, C.

Citation

Journal: J.Mol.Biol. / Year: 2007
Title: High-throughput generation of synthetic antibodies from highly functional minimalist phage-displayed libraries
Authors: Fellouse, F.A. / Esaki, K. / Birtalan, S. / Raptis, D. / Cancasci, V.J. / Koide, A. / Jhurani, P. / Vasser, M. / Wiesmann, C. / Kossiakoff, A.A. / Koide, S. / Sidhu, S.S.

History

Deposition	Jul 27, 2007	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Aug 14, 2007	Provider: repository / Type: Initial release
Revision 1.1	Jul 13, 2011	Group: Advisory / Version format compliance
Revision 1.2	Oct 25, 2017	Group: Refinement description / Category: software Item: _software.classification / _software.contact_author ..._software.classification / _software.contact_author / _software.contact_author_email / _software.date / _software.language / _software.location / _software.name / _software.type / _software.version
Revision 1.3	Oct 16, 2024	Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / 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.end_auth_comp_id

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	2qr0.cif.gz	783.9 KB	Display	PDBx/mmCIF format
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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/qr/2qr0 ftp://data.pdbj.org/pub/pdb/validation_reports/qr/2qr0	HTTPS FTP

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Related structure data

Similar structure data	1tzh-d 5ue8-2 6r0x-d 1tzi-1 5ue8-1 5szo-d 6bx7-1 6meq-1 2gjz-6 1v7m-d 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

Similar structure data

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#267 - Mar 2022 Vascular Endothelial Growth Factor (VegF similarity (17) #21 - Sep 2001 Antibodies similarity (1) #256 - Apr 2021 SARS-CoV-2 Spike and Antibodies similarity (1) #68 - Aug 2005 Neurotrophins similarity (1) #122 - Feb 2010 Enhanceosome similarity (1) #240 - Dec 2019 Hypoxia-Inducible Factors similarity (1) #126 - Jun 2010 Epidermal Growth Factor similarity (1) #148 - Apr 2012 Ras Protein similarity (1) #45 - Sep 2003 Estrogen Receptor similarity (1) #44 - Aug 2003 Calmodulin similarity (1) #195 - Mar 2016 RAF Protein Kinases similarity (1) #196 - Apr 2016 Lead Poisoning similarity (1) #28 - Apr 2002 Anthrax Toxin similarity (1) #43 - Jul 2003 Src Tyrosine Kinase similarity (1) #60 - Dec 2004 Ubiquitin similarity (1)

PDB pages

PDBj /

wwPDB /

NCBI

Related items in Molecule of the Month

#267 - Mar 2022
Vascular Endothelial Growth Factor (VegF
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#68 - Aug 2005
Neurotrophins
similarity (1)
#122 - Feb 2010
Enhanceosome
similarity (1)
#240 - Dec 2019
Hypoxia-Inducible Factors
similarity (1)
#126 - Jun 2010
Epidermal Growth Factor
similarity (1)
#148 - Apr 2012
Ras Protein
similarity (1)
#45 - Sep 2003
Estrogen Receptor
similarity (1)
#44 - Aug 2003
Calmodulin
similarity (1)
#195 - Mar 2016
RAF Protein Kinases
similarity (1)
#196 - Apr 2016
Lead Poisoning
similarity (1)
#28 - Apr 2002
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Ubiquitin
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Deposited unit

A: Fab-Fragment Light Chain

B: Fab-Fragment Heavy Chain

C: Vascular endothelial growth factor A

D: Vascular endothelial growth factor A

E: Fab-Fragment Light Chain

F: Fab-Fragment Heavy Chain

G: Fab-Fragment Light Chain

H: Fab-Fragment Heavy Chain

I: Vascular endothelial growth factor A

J: Vascular endothelial growth factor A

K: Fab-Fragment Light Chain

L: Fab-Fragment Heavy Chain

M: Fab-Fragment Light Chain

N: Fab-Fragment Heavy Chain

O: Vascular endothelial growth factor A

P: Vascular endothelial growth factor A

Q: Fab-Fragment Light Chain

R: Fab-Fragment Heavy Chain

S: Fab-Fragment Light Chain

T: Fab-Fragment Heavy Chain

U: Vascular endothelial growth factor A

V: Vascular endothelial growth factor A

W: Fab-Fragment Light Chain

X: Fab-Fragment Heavy Chain

466 kDa, 24 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Fab-Fragment Light Chain

B: Fab-Fragment Heavy Chain

C: Vascular endothelial growth factor A

D: Vascular endothelial growth factor A

E: Fab-Fragment Light Chain

F: Fab-Fragment Heavy Chain

defined by author
116 kDa, 6 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

G: Fab-Fragment Light Chain

H: Fab-Fragment Heavy Chain

I: Vascular endothelial growth factor A

J: Vascular endothelial growth factor A

K: Fab-Fragment Light Chain

L: Fab-Fragment Heavy Chain

defined by author
116 kDa, 6 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

M: Fab-Fragment Light Chain

N: Fab-Fragment Heavy Chain

O: Vascular endothelial growth factor A

P: Vascular endothelial growth factor A

Q: Fab-Fragment Light Chain

R: Fab-Fragment Heavy Chain

defined by author
116 kDa, 6 polymers
Search similar-shape structures of this assembly by Omokage search (details)

4

S: Fab-Fragment Light Chain

T: Fab-Fragment Heavy Chain

U: Vascular endothelial growth factor A

V: Vascular endothelial growth factor A

W: Fab-Fragment Light Chain

X: Fab-Fragment Heavy Chain

defined by author
116 kDa, 6 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	154.453, 90.218, 205.558
Angle α, β, γ (deg.)	90.000, 90.850, 90.000
Int Tables number	4
Space group name H-M	P12₁1

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Refine code: 1

Dom-ID	Component-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	1	ASP	ASP	GLN	GLN	A	A	1 - 90	1 - 90
2	1	1	ASP	ASP	GLN	GLN	E	E	1 - 90	1 - 90
3	1	1	ASP	ASP	GLN	GLN	G	G	1 - 90	1 - 90
4	1	1	ASP	ASP	GLN	GLN	K	K	1 - 90	1 - 90
5	1	1	ASP	ASP	GLN	GLN	M	M	1 - 90	1 - 90
6	1	1	ASP	ASP	GLN	GLN	Q	Q	1 - 90	1 - 90
7	1	1	ASP	ASP	GLN	GLN	S	S	1 - 90	1 - 90
8	1	1	ASP	ASP	GLN	GLN	W	W	1 - 90	1 - 90
9	2	1	ILE	ILE	ARG	ARG	A	A	106 - 211	108 - 213
10	2	1	ILE	ILE	ARG	ARG	E	E	106 - 211	108 - 213
11	2	1	ILE	ILE	ARG	ARG	G	G	106 - 211	108 - 213
12	2	1	ILE	ILE	ARG	ARG	K	K	106 - 211	108 - 213
13	2	1	ILE	ILE	ARG	ARG	M	M	106 - 211	108 - 213
14	2	1	ILE	ILE	ARG	ARG	Q	Q	106 - 211	108 - 213
15	2	1	ILE	ILE	ARG	ARG	S	S	106 - 211	108 - 213
16	2	1	ILE	ILE	ARG	ARG	W	W	106 - 211	108 - 213
1	1	2	GLU	GLU	SER	SER	B	B	1 - 113	1 - 118
2	1	2	GLU	GLU	SER	SER	F	F	1 - 113	1 - 118
3	1	2	GLU	GLU	SER	SER	H	H	1 - 113	1 - 118
4	1	2	GLU	GLU	SER	SER	L	L	1 - 113	1 - 118
5	1	2	GLU	GLU	SER	SER	N	N	1 - 113	1 - 118
6	1	2	GLU	GLU	SER	SER	R	R	1 - 113	1 - 118
7	1	2	GLU	GLU	SER	SER	T	T	1 - 113	1 - 118
8	1	2	GLU	GLU	SER	SER	X	X	1 - 113	1 - 118
9	2	2	ALA	ALA	CYS	CYS	B	B	114 - 216	119 - 221
10	2	2	ALA	ALA	CYS	CYS	F	F	114 - 216	119 - 221
11	2	2	ALA	ALA	CYS	CYS	H	H	114 - 216	119 - 221
12	2	2	ALA	ALA	CYS	CYS	L	L	114 - 216	119 - 221
13	2	2	ALA	ALA	CYS	CYS	N	N	114 - 216	119 - 221
14	2	2	ALA	ALA	CYS	CYS	R	R	114 - 216	119 - 221
15	2	2	ALA	ALA	CYS	CYS	T	T	114 - 216	119 - 221
16	2	2	ALA	ALA	CYS	CYS	X	X	114 - 216	119 - 221
1	1	3	GLU	GLU	LYS	LYS	C	C	13 - 107	1 - 95
2	1	3	GLU	GLU	ASP	ASP	D	D	13 - 109	1 - 97
3	1	3	GLU	GLU	LYS	LYS	I	I	13 - 107	1 - 95
4	1	3	GLU	GLU	ASP	ASP	J	J	13 - 109	1 - 97
5	1	3	GLU	GLU	LYS	LYS	O	O	13 - 107	1 - 95
6	1	3	GLU	GLU	ASP	ASP	P	P	13 - 109	1 - 97
7	1	3	GLU	GLU	LYS	LYS	U	U	13 - 107	1 - 95
8	1	3	GLU	GLU	ASP	ASP	V	V	13 - 109	1 - 97

NCS ensembles :

ID
1
2
3

#1: Antibody	Fab-Fragment Light Chain Mass: 23497.047 Da / Num. of mol.: 8 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)
#2: Antibody	Fab-Fragment Heavy Chain Mass: 23362.049 Da / Num. of mol.: 8 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)
#3: Protein	Vascular endothelial growth factor A / VEGF-A / Vascular permeability factor / VPF Mass: 11373.103 Da / Num. of mol.: 8 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P15692
Has protein modification	Y

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 3.07 Å³/Da / Density % sol: 59.96 %

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Data collection

Diffraction source

Source:

SYNCHROTRON / Site:

ALS

/ Beamline: 5.0.2 / Wavelength: 1 Å

Radiation

Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray

Radiation wavelength

Wavelength: 1 Å / Relative weight: 1

Reflection

Resolution: 3.5→50 Å / Num. obs: 71940 / % possible obs: 96.1 % / Redundancy: 3.3 % / R_merge(I) obs: 0.097 / Χ²: 1.1 / Net I/σ(I): 10.7

Reflection shell

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Num. unique all	Χ²	Diffraction-ID	% possible all
3.5-3.63	2.9	0.444	6873	0.947	1	93.4
3.63-3.77	3.1	0.369	6994	0.967	1	93.6
3.77-3.94	3.1	0.278	7029	1.061	1	94.5
3.94-4.15	3.2	0.192	7054	1.102	1	94.5
4.15-4.41	3.2	0.126	7060	1.196	1	95.3
4.41-4.75	3.2	0.092	7180	1.214	1	96.1
4.75-5.23	3.3	0.083	7294	1.21	1	97.4
5.23-5.98	3.4	0.083	7348	1.14	1	97.8
5.98-7.53	3.4	0.064	7426	1.126	1	98.3
7.53-50	3.6	0.037	7682	1.001	1	99.4

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Phasing

Phasing	Method: molecular replacement

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Processing

Software

Name	Version	Classification
DENZO		data reduction
SCALEPACK		data scaling
PHASER		phasing
REFMAC		refinement
PDB_EXTRACT	3	data extraction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 3.5→20 Å / Cor.coef. F_o:F_c: 0.84 / Cor.coef. F_o:F_c free: 0.821 / SU B: 95.462 / SU ML: 0.675 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.793 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.312	3496	5.1 %	RANDOM
R_work	0.291	-	-	-
all	0.292	-	-	-
obs	0.292	68755	96.13 %	-

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: 65.484 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	4.8 Å²	0 Å²	-3.56 Å²
2-	-	0.36 Å²	0 Å²
3-	-	-	-5.27 Å²

Refinement step

Cycle: LAST / Resolution: 3.5→20 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	32356	0	0	0	32356

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.007	0.022	33204
X-RAY DIFFRACTION	r_bond_other_d	0.001	0.02	28664
X-RAY DIFFRACTION	r_angle_refined_deg	1.037	1.955	45152
X-RAY DIFFRACTION	r_angle_other_deg	0.712	3	67260
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.494	5	4168
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	35.478	24.218	1356
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	18.479	15	5340
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	12.205	15	128
X-RAY DIFFRACTION	r_chiral_restr	0.058	0.2	4976
X-RAY DIFFRACTION	r_gen_planes_refined	0.002	0.02	36912
X-RAY DIFFRACTION	r_gen_planes_other	0.001	0.02	6608
X-RAY DIFFRACTION	r_nbd_refined	0.193	0.2	5177
X-RAY DIFFRACTION	r_nbd_other	0.181	0.2	27180
X-RAY DIFFRACTION	r_nbtor_refined	0.177	0.2	15655
X-RAY DIFFRACTION	r_nbtor_other	0.082	0.2	19536
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.149	0.2	644
X-RAY DIFFRACTION	r_xyhbond_nbd_other	0.005	0.2	3
X-RAY DIFFRACTION	r_symmetry_vdw_refined	0.337	0.2	93
X-RAY DIFFRACTION	r_symmetry_vdw_other	0.38	0.2	177
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.277	0.2	10
X-RAY DIFFRACTION	r_mcbond_it	2.959	2.5	26696
X-RAY DIFFRACTION	r_mcbond_other	0.105	2.5	8488
X-RAY DIFFRACTION	r_mcangle_it	3.626	5	33936
X-RAY DIFFRACTION	r_scbond_it	1.602	2.5	14698
X-RAY DIFFRACTION	r_scangle_it	2.611	5	11216

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	2839	TIGHT POSITIONAL	0.01	0.05
1	2	E	2839	TIGHT POSITIONAL	0.01	0.05
1	3	G	2839	TIGHT POSITIONAL	0.01	0.05
1	4	K	2839	TIGHT POSITIONAL	0.01	0.05
1	5	M	2839	TIGHT POSITIONAL	0.01	0.05
1	6	Q	2839	TIGHT POSITIONAL	0.01	0.05
1	7	S	2839	TIGHT POSITIONAL	0.01	0.05
1	8	W	2839	TIGHT POSITIONAL	0.01	0.05
1	1	A	2839	TIGHT THERMAL	0.02	0.5
1	2	E	2839	TIGHT THERMAL	0.02	0.5
1	3	G	2839	TIGHT THERMAL	0.03	0.5
1	4	K	2839	TIGHT THERMAL	0.02	0.5
1	5	M	2839	TIGHT THERMAL	0.02	0.5
1	6	Q	2839	TIGHT THERMAL	0.03	0.5
1	7	S	2839	TIGHT THERMAL	0.03	0.5
1	8	W	2839	TIGHT THERMAL	0.03	0.5
2	1	B	3047	TIGHT POSITIONAL	0.01	0.05
2	2	F	3047	TIGHT POSITIONAL	0.01	0.05
2	3	H	3047	TIGHT POSITIONAL	0.02	0.05
2	4	L	3047	TIGHT POSITIONAL	0.01	0.05
2	5	N	3047	TIGHT POSITIONAL	0.01	0.05
2	6	R	3047	TIGHT POSITIONAL	0.02	0.05
2	7	T	3047	TIGHT POSITIONAL	0.01	0.05
2	8	X	3047	TIGHT POSITIONAL	0.01	0.05
2	1	B	3047	TIGHT THERMAL	0.02	0.5
2	2	F	3047	TIGHT THERMAL	0.02	0.5
2	3	H	3047	TIGHT THERMAL	0.03	0.5
2	4	L	3047	TIGHT THERMAL	0.02	0.5
2	5	N	3047	TIGHT THERMAL	0.02	0.5
2	6	R	3047	TIGHT THERMAL	0.03	0.5
2	7	T	3047	TIGHT THERMAL	0.03	0.5
2	8	X	3047	TIGHT THERMAL	0.03	0.5
3	1	C	1457	TIGHT POSITIONAL	0.01	0.05
3	2	D	1457	TIGHT POSITIONAL	0.01	0.05
3	3	I	1457	TIGHT POSITIONAL	0.01	0.05
3	4	J	1457	TIGHT POSITIONAL	0.01	0.05
3	5	O	1457	TIGHT POSITIONAL	0.01	0.05
3	6	P	1457	TIGHT POSITIONAL	0.01	0.05
3	7	U	1457	TIGHT POSITIONAL	0.01	0.05
3	8	V	1457	TIGHT POSITIONAL	0.01	0.05
3	1	C	1457	TIGHT THERMAL	0.02	0.5
3	2	D	1457	TIGHT THERMAL	0.02	0.5
3	3	I	1457	TIGHT THERMAL	0.02	0.5
3	4	J	1457	TIGHT THERMAL	0.02	0.5
3	5	O	1457	TIGHT THERMAL	0.02	0.5
3	6	P	1457	TIGHT THERMAL	0.02	0.5
3	7	U	1457	TIGHT THERMAL	0.02	0.5
3	8	V	1457	TIGHT THERMAL	0.02	0.5

LS refinement shell

Resolution: 3.5→3.57 Å / Total num. of bins used: 25

	R_factor	Num. reflection	% reflection
R_free	0.341	187	-
R_work	0.341	3622	-
all	-	3809	-
obs	-	-	93.47 %

Refinement TLS params.

Method: refined / Origin x: -38.4554 Å / Origin y: 60.4287 Å / Origin z: 19.4604 Å

	11	12	13	21	22	23	31	32	33
T	0 Å²	0 Å²	0 Å²	-	0 Å²	0 Å²	-	-	0 Å²
L	0.0632 °²	0.0204 °²	0.0135 °²	-	0.0679 °²	0.0836 °²	-	-	0.1053 °²
S	0.0196 Å °	-0.0349 Å °	-0.0028 Å °	0.0537 Å °	-0.0021 Å °	0.0118 Å °	0.053 Å °	-0.0138 Å °	-0.0175 Å °

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	X-RAY DIFFRACTION	1	A	A	1 - 105	1 - 107
2	X-RAY DIFFRACTION	1	A	A	106 - 211	108 - 213
3	X-RAY DIFFRACTION	1	B	B	1 - 113	1 - 118
4	X-RAY DIFFRACTION	1	B	B	114 - 216	119 - 221
5	X-RAY DIFFRACTION	1	C	C	13 - 107	1 - 95
6	X-RAY DIFFRACTION	1	D	D	13 - 107	1 - 95
7	X-RAY DIFFRACTION	1	E	E	1 - 105	1 - 107
8	X-RAY DIFFRACTION	1	E	E	106 - 211	108 - 213
9	X-RAY DIFFRACTION	1	F	F	1 - 113	1 - 118
10	X-RAY DIFFRACTION	1	F	F	114 - 216	119 - 221
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