PDB-1ob1: Crystal structure of a Fab complex whith Plasmodium falciparum MSP1-19

ID or keywords:

Entry

Database: PDB / ID: 1ob1

Title

Crystal structure of a Fab complex whith Plasmodium falciparum MSP1-19

Components

ANTIBODY, HEAVY CHAIN
ANTIBODY, LIGHT CHAIN
MAJOR MEROZOITE SURFACE PROTEIN

Keywords

IMMUNE SYSTEM / IMMUNOGLOBULIN-COMPLEX / IMMUNOGLOBULIN / ANTIBODY FAB FRAGMENT / MSP1-19 / EGF-LIKE DOMAIN / SURFACE ANTIGEN / MALARIA VACCINE COMPONENT

Function / homology

Function and homology information

vacuolar membrane / immunoglobulin receptor binding / side of membrane / extracellular region / plasma membrane
Similarity search - Function

Biological species

PLASMODIUM FALCIPARUM (malaria parasite P. falciparum)

MUS MUSCULUS (house mouse)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.9 Å

Authors

Pizarro, J.C. / Chitarra, V. / Verger, D. / Holm, I. / Petres, S. / Dartville, S. / Nato, F. / Longacre, S. / Bentley, G.A.

Citation

Journal: J.Mol.Biol. / Year: 2003
Title: Crystal Structure of a Fab Complex Formed with Pfmsp1-19, the C-Terminal Fragment of Merozoite Surface Protein 1 from Plasmodium Falciparum: A Malaria Vaccine Candidate
Authors: Pizarro, J.C. / Chitarra, V. / Verger, D. / Holm, I. / Petres, S. / Dartville, S. / Nato, F. / Longacre, S. / Bentley, G.A.

History

Deposition	Jan 22, 2003	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	May 1, 2003	Provider: repository / Type: Initial release
Revision 1.1	Jul 13, 2011	Group: Advisory / Version format compliance
Revision 1.2	Apr 3, 2019	Group: Advisory / Data collection ...Advisory / Data collection / Other / Source and taxonomy Category: entity_src_gen / pdbx_database_proc ...entity_src_gen / pdbx_database_proc / pdbx_database_status / pdbx_unobs_or_zero_occ_atoms Item: _entity_src_gen.pdbx_host_org_cell_line / _pdbx_database_status.recvd_author_approval
Revision 1.3	Dec 13, 2023	Group: Advisory / Data collection ...Advisory / Data collection / Database references / 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_unobs_or_zero_occ_atoms / struct_ncs_dom_lim 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_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
Revision 1.4	Oct 23, 2024	Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

Remark 700

SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ...

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	1ob1.cif.gz	206.9 KB	Display	PDBx/mmCIF format
PDB format	pdb1ob1.ent.gz	164 KB	Display	PDB format
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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/ob/1ob1 ftp://data.pdbj.org/pub/pdb/validation_reports/ob/1ob1	HTTPS FTP

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Related structure data

Related structure data	1a3rS 1b9wS 2igfS S: Starting model for refinement
Similar structure data	3s36-d 5fcu-d 7lsf-d 6mvl-d 7lsg-d 7lse-d 6plk-1 6ute-1 6k7o-2 6w0d-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) 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
Related items in Molecule of the Month	#21 - Sep 2001 Antibodies similarity (2) #161 - May 2013 Ricin similarity (1) #62 - Feb 2005 Major Histocompatibility Complex similarity (1) #256 - Apr 2021 SARS-CoV-2 Spike and Antibodies similarity (1) #133 - Jan 2011 Nitric Oxide Synthase similarity (1) #203 - Nov 2016 Aminopeptidase 1 and Autophagy similarity (1) #75 - Mar 2006 Tissue Factor similarity (1) #90 - Jun 2007 Fatty Acid Synthase similarity (1)

PDB pages

PDBj /

wwPDB /

NCBI

Related items in Molecule of the Month

#21 - Sep 2001
Antibodies
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#161 - May 2013
Ricin
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#62 - Feb 2005
Major Histocompatibility Complex
similarity (1)
#256 - Apr 2021
SARS-CoV-2 Spike and Antibodies
similarity (1)
#133 - Jan 2011
Nitric Oxide Synthase
similarity (1)
#203 - Nov 2016
Aminopeptidase 1 and Autophagy
similarity (1)
#75 - Mar 2006
Tissue Factor
similarity (1)
#90 - Jun 2007
Fatty Acid Synthase
similarity (1)

Deposited unit

A: ANTIBODY, HEAVY CHAIN

B: ANTIBODY, LIGHT CHAIN

C: MAJOR MEROZOITE SURFACE PROTEIN

D: ANTIBODY, HEAVY CHAIN

E: ANTIBODY, LIGHT CHAIN

F: MAJOR MEROZOITE SURFACE PROTEIN

hetero molecules

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

1

A: ANTIBODY, HEAVY CHAIN

B: ANTIBODY, LIGHT CHAIN

C: MAJOR MEROZOITE SURFACE PROTEIN

hetero molecules

defined by author&software
58.6 kDa, 3 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

D: ANTIBODY, HEAVY CHAIN

E: ANTIBODY, LIGHT CHAIN

F: MAJOR MEROZOITE SURFACE PROTEIN

hetero molecules

defined by author&software
58.6 kDa, 3 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	51.750, 213.460, 59.890
Angle α, β, γ (deg.)	90.00, 100.95, 90.00
Int Tables number	4
Space group name H-M	P12₁1

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	A
2	1	D
1	2	B
2	2	E
1	3	A
2	3	D
1	4	B
2	4	E
1	5	C
2	5	F

NCS domain segments:

Refine code: 3

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	ILE	ILE	GLN	GLN	A	A	10 - 38	10 - 39
2	1	1	ILE	ILE	GLN	GLN	D	D	10 - 38	10 - 39
1	2	1	PRO	PRO	ILE	ILE	A	A	44 - 75	45 - 76
2	2	1	PRO	PRO	ILE	ILE	D	D	44 - 75	45 - 76
1	3	1	ASP	ASP	ARG	ARG	A	A	82 - 107	83 - 109
2	3	1	ASP	ASP	ARG	ARG	D	D	82 - 107	83 - 109
1	1	2	GLU	GLU	VAL	VAL	B	B	1 - 37	1 - 37
2	1	2	GLU	GLU	VAL	VAL	E	E	1 - 37	1 - 37
1	2	2	ASP	ASP	ASP	ASP	B	B	44 - 101	44 - 108
2	2	2	ASP	ASP	ASP	ASP	E	E	44 - 101	44 - 108
1	3	2	TRP	TRP	ALA	ALA	B	B	103 - 118	110 - 125
2	3	2	TRP	TRP	ALA	ALA	E	E	103 - 118	110 - 125
1	1	3	THR	THR	PHE	PHE	A	A	113 - 138	115 - 140
2	1	3	THR	THR	PHE	PHE	D	D	113 - 138	115 - 140
1	2	3	ILE	ILE	ASN	ASN	A	A	149 - 211	151 - 213
2	2	3	ILE	ILE	ASN	ASN	D	D	149 - 211	151 - 213
1	1	4	LEU	LEU	THR	THR	B	B	124 - 131	131 - 138
2	1	4	LEU	LEU	THR	THR	E	E	124 - 131	131 - 138
1	2	4	LEU	LEU	PRO	PRO	B	B	141 - 212	148 - 219
2	2	4	LEU	LEU	PRO	PRO	E	E	141 - 212	148 - 219
1	1	5	GLN	GLN	THR	THR	C	C	6 - 63	6 - 63
2	1	5	GLN	GLN	THR	THR	F	F	6 - 63	6 - 63
1	2	5	ILE	ILE	SER	SER	C	C	74 - 93	74 - 93
2	2	5	ILE	ILE	SER	SER	F	F	74 - 93	74 - 93

NCS ensembles :

ID
1
2
3
4
5

Details

ONE TRIMER IS MADE UP OF HEAVY CHAIN A LIGHT CHAIN BAND MEROZOITE SURFACE PROTEIN 1 CHAIN C. THE OTHER TRIMER IS MADE UP OF HEAVY CHAIN D LIGHTCHAIN E AND MEROZOITE SURFACE PROTEIN 1 CHAIN FTHE CHAIN IN THE COMPLEX A, B, C IS 1691.4 ANGSTROM**2THE CHAIN IN THE COMPLEX D, E, F IS 1666.6 ANGSTROM**2

#1: Antibody	ANTIBODY, HEAVY CHAIN Mass: 23659.107 Da / Num. of mol.: 2 / Fragment: FAB FRAGMENT / Source method: isolated from a natural source / Source: (natural) MUS MUSCULUS (house mouse) / Cell: B-LYMPHOCYTE / Cell line: G17-12 MURINE HYBRIDOMA / Strain: BALB/C / References: UniProt: A0A5E3*PLUS
#2: Antibody	ANTIBODY, LIGHT CHAIN Mass: 23650.516 Da / Num. of mol.: 2 / Fragment: FAB FRAGMENT / Source method: isolated from a natural source / Source: (natural) MUS MUSCULUS (house mouse) / Cell: B-LYMPHOCYTE / Cell line: G17-12 MURINE HYBRIDOMA / Strain: BALB/C / References: UniProt: P01863*PLUS
#3: Protein	MAJOR MEROZOITE SURFACE PROTEIN Mass: 11185.328 Da / Num. of mol.: 2 / Fragment: MSP1-19, RESIDUES 8-100 Source method: isolated from a genetically manipulated source Source: (gene. exp.) PLASMODIUM FALCIPARUM (malaria parasite P. falciparum) Strain: UGANDA PALO ALTO / Description: SYNTHETIC GENE / Cell: MEROZOITE STAGE / Cell line (production host): High Five / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: Q25976
#4: Chemical	ChemComp-CAC / CACODYLATE ION / dimethylarsinate Mass: 136.989 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C₂H₆AsO₂
Has protein modification	Y
Sequence details	ANTIBODY RESIDUE NUMBERING FOLLOWS THE KABAT CONVENTION (E.A.KABAT,T.T.WU, M.REID-MILLER, H.M. ...ANTIBODY RESIDUE NUMBERING FOLLOWS THE KABAT CONVENTION (E.A.KABAT,T.T.WU, M.REID-MILLER, H.M.PERRY, A K.S.GOTTESMAN (1991) SEQUENCES OF PROTEINS OF IMMUNOLOGIC INTEREST, 5TH ED., NATIONAL INSTITUTES OF HEALTH BETHESDA) CHAINS A AND C HAVE A C-TERMINAL SIX RESIDUE HIS TAG

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Experiment

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

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Sample preparation

Crystal

Density Matthews: 2.8 Å³/Da / Density % sol: 56 %

Crystal grow

pH: 6.5
Details: 0.075M SODIUM ACETATE 0.038M SODIUM CACODYLATE, 11.3% PEG8000, 3% DIOXANE, pH 6.50

Crystal grow

*PLUS

Temperature: 291 K / pH: 7.4 / Method: vapor diffusion
Details: Pizarro, J.C., (2001) Acta Crystallogr.,Sect.D, D58, 1246.

Components of the solutions

*PLUS

ID	Conc.	Common name	Crystal-ID	Sol-ID	Details
1	11 mg/ml	protein	1	drop
2	10 mM	Tris	1	drop	pH7.4
3	0.075 M	sodium acetate	1	reservoir
4	0.038 M	sodium cacodylate	1	reservoir
5	11.3 %	PEG8000	1	reservoir
6	3 %	dioxane	1	reservoir	pH6.5

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Data collection

Diffraction	Mean temperature: 110 K
Diffraction source	Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.934
Detector	Type: MARRESEARCH / Detector: CCD / Date: Apr 15, 2001
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.934 Å / Relative weight: 1
Reflection	Resolution: 2.9→30 Å / Num. obs: 27530 / % possible obs: 96.8 % / Redundancy: 3.39 % / R_merge(I) obs: 0.071 / Net I/σ(I): 16.5
Reflection shell	Resolution: 2.9→3 Å / R_merge(I) obs: 0.578 / Mean I/σ(I) obs: 2.6 / % possible all: 87.6
Reflection	PLUS Lowest resolution: 30 Å / Redundancy*: 3.34 %
Reflection shell	PLUS % possible obs*: 87.6 %

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Processing

Software

Name	Version	Classification
REFMAC	5	refinement
DENZO		data reduction
SCALEPACK		data scaling
AMoRE		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB ENTRIES 2IGF, 1A3R, 1B9W

2igf

1a3r

1b9w

Resolution: 2.9→105.41 Å / Cor.coef. F_o:F_c: 0.892 / Cor.coef. F_o:F_c free: 0.854 / SU B: 21.27 / SU ML: 0.416 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R Free: 0.482 / Stereochemistry target values: MAXIMUM LIKELIHOOD

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.288	1368	5 %	RANDOM
R_work	0.257	-	-	-
obs	0.258	25850	96.6 %	-

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK

Displacement parameters

B_iso mean: 11.51 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	1.63 Å²	0 Å²	1.44 Å²
2-	-	3.19 Å²	0 Å²
3-	-	-	-4.27 Å²

Refinement step

Cycle: LAST / Resolution: 2.9→105.41 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	8132	0	10	0	8142

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.008	0.021	8362
X-RAY DIFFRACTION	r_bond_other_d
X-RAY DIFFRACTION	r_angle_refined_deg
X-RAY DIFFRACTION	r_angle_other_deg	1.267	1.937	11376
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	3.529	3	1053
X-RAY DIFFRACTION	r_dihedral_angle_2_deg
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	19.478	15	1450
X-RAY DIFFRACTION	r_dihedral_angle_4_deg
X-RAY DIFFRACTION	r_chiral_restr	0.088	0.2	1250
X-RAY DIFFRACTION	r_gen_planes_refined	0.005	0.02	6355
X-RAY DIFFRACTION	r_gen_planes_other
X-RAY DIFFRACTION	r_nbd_refined	0.292	0.3	3900
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	0.188	0.5	761
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	0.363	0.3	41
X-RAY DIFFRACTION	r_symmetry_vdw_other
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.311	0.5	3
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	0.187	1.5	5276
X-RAY DIFFRACTION	r_mcbond_other
X-RAY DIFFRACTION	r_mcangle_it	0.355	2	8549
X-RAY DIFFRACTION	r_mcangle_other
X-RAY DIFFRACTION	r_scbond_it	0.673	3	3086
X-RAY DIFFRACTION	r_scbond_other
X-RAY DIFFRACTION	r_scangle_it	1.083	4.5	2827
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	418	tight positional	0.03	0.05
1	2	D	418	tight positional	0.03	0.05
2	1	B	1294	tight positional	0.04	0.05
2	2	E	1294	tight positional	0.04	0.05
3	1	A	1981	tight positional	0.02	0.05
3	2	D	1981	tight positional	0.02	0.05
4	1	B	2567	tight positional	0.01	0.05
4	2	E	2567	tight positional	0.01	0.05
5	1	C	3167	tight positional	0.01	0.05
5	2	F	3167	tight positional	0.01	0.05
1	1	A	252	loose positional	0.23	5
1	2	D	252	loose positional	0.23	5
2	1	B	252	loose positional	0.03	5
2	2	E	252	loose positional	0.03	5
3	1	A	252	loose positional	0.01	5
3	2	D	252	loose positional	0.01	5
4	1	B	252	loose positional	0.01	5
4	2	E	252	loose positional	0.01	5
5	1	C	252	loose positional	0.01	5
5	2	F	252	loose positional	0.01	5
1	1	A	418	tight thermal	0.07	0.5
1	2	D	418	tight thermal	0.07	0.5
2	1	B	1294	tight thermal	0.57	0.5
2	2	E	1294	tight thermal	0.57	0.5
3	1	A	1981	tight thermal	1.34	0.5
3	2	D	1981	tight thermal	1.34	0.5
4	1	B	2567	tight thermal	1.8	0.5
4	2	E	2567	tight thermal	1.8	0.5
5	1	C	3167	tight thermal	1.88	0.5
5	2	F	3167	tight thermal	1.88	0.5
1	1	A	252	loose thermal	0.8	10
1	2	D	252	loose thermal	0.8	10
2	1	B	252	loose thermal	4.44	10
2	2	E	252	loose thermal	4.44	10
3	1	A	252	loose thermal	10.47	10
3	2	D	252	loose thermal	10.47	10
4	1	B	252	loose thermal	16.1	10
4	2	E	252	loose thermal	16.1	10
5	1	C	252	loose thermal	19.96	10
5	2	F	252	loose thermal	19.96	10

LS refinement shell

Resolution: 2.9→2.98 Å / Total num. of bins used: 20 /

	R_factor	Num. reflection
R_free	0.384	89
R_work	0.33	1731

Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

ID	L11 (°²)	L12 (°²)	L13 (°²)	L22 (°²)	L23 (°²)	L33 (°²)	S11 (Å °)	S12 (Å °)	S13 (Å °)	S21 (Å °)	S22 (Å °)	S23 (Å °)	S31 (Å °)	S32 (Å °)	S33 (Å °)	T11 (Å²)	T12 (Å²)	T13 (Å²)	T22 (Å²)	T23 (Å²)	T33 (Å²)	Origin x (Å)	Origin y (Å)	Origin z (Å)
1	5.0057	0.3025	-0.2121	3.3009	1.6664	8.404	0.0077	0.309	-0.2376	-0.1216	-0.4483	0.4766	-0.2873	-0.8088	0.4406	0.0152	0.0624	-0.0629	0.3982	-0.1476	0.3464	0.3711	8.2554	10.5924
2	8.2447	1.46	0.6827	8.7224	2.5406	6.5914	0.3876	-0.6468	-1.8213	0.999	-0.2619	0.5993	1.81	-0.261	-0.1256	0.8984	-0.0277	-0.0571	0.3816	0.1962	0.6951	7.3157	-8.4296	23.7657
3	4.4674	-0.9736	-1.4963	5.5659	3.7117	10.3324	0.0133	-0.0866	0.7714	-0.8458	-0.2558	0.3867	-2.5565	-0.9028	0.2425	0.9171	0.1429	0.0166	0.3222	-0.1208	0.5038	10.6731	35.7045	23.6276
4	7.607	-0.2463	0.5109	10.5547	2.7275	7.8089	0.4265	-0.0527	1.9867	-1.1807	0.5583	-1.4343	-3.032	1.5647	-0.9848	1.5334	-0.747	0.5924	0.8241	-0.3307	0.976	31.0396	39.7716	15.4681
5	4.747	-0.7634	3.0213	9.8563	6.3285	10.4088	0.1643	-0.0439	0.0992	0.5931	0.2966	-0.7457	-0.2425	1.21	-0.4609	0.5654	-0.1636	-0.0456	0.7528	-0.0231	0.26	19.7025	16.8633	38.2882
6	5.0269	-0.7103	1.2059	10.9989	7.0146	9.846	-0.1574	0.2323	-0.3723	-0.0147	0.715	-0.396	-0.376	0.4992	-0.5576	0.238	-0.2124	0.1489	0.5717	-0.0947	0.2516	23.8311	11.737	2.1529
7	9.5969	5.4551	-0.6316	20.0774	-1.9622	6.1167	-1.0786	1.4617	-1.7848	-1.512	1.6648	1.2137	1.7103	-1.2764	-0.5862	0.8079	-0.4269	-0.141	1.587	-0.5537	1.3164	-17.163	-17.4107	-9.3258
8	12.7836	7.0558	-0.1429	26.5103	-6.8357	18.4233	-0.0172	2.0836	-5.053	-1.2832	-0.3395	-4.768	2.8027	1.2759	0.3567	0.9331	0.1237	0.2174	1.0957	-1.0326	3.276	-2.7904	-23.5546	-6.1193
9	46.5244	46.5358	-13.4463	67.51	-15.3783	6.5247	5.1344	0.7984	10.5178	7.9676	-0.4722	9.1753	-3.6638	-0.1382	-4.6622	3.6691	0.3424	1.292	0.694	-0.352	3.3954	14.2133	68.8091	40.5997
10	28.4184	6.7547	0.002	14.8233	-5.405	8.4909	1.6163	-3.3451	0.5791	2.4507	0.1289	-2.7167	-2.7913	1.2965	-1.7452	2.8553	-0.1859	-0.689	0.9111	-0.5426	2.3322	28.5872	61.371	41.7156

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	1 - 110
2	X-RAY DIFFRACTION	2	B	1 - 120
3	X-RAY DIFFRACTION	3	D	1 - 110
4	X-RAY DIFFRACTION	4	E	1 - 120
5	X-RAY DIFFRACTION	5	C	1 - 95
6	X-RAY DIFFRACTION	5	C	1096
7	X-RAY DIFFRACTION	6	F	1 - 96
8	X-RAY DIFFRACTION	6	F	1097
9	X-RAY DIFFRACTION	7	A	111 - 215
10	X-RAY DIFFRACTION	8	B	121 - 219
11	X-RAY DIFFRACTION	9	D	111 - 215
12	X-RAY DIFFRACTION	10	E	121 - 219

Refinement

*PLUS

Lowest resolution: 20 Å / % reflection R_free: 5 % / R_factor obs: 0.258 / R_factor R_free: 0.288 / R_factor R_work: 0.256

Solvent computation

*PLUS

Displacement parameters

*PLUS

Refine LS restraints

*PLUS

Refine-ID	Type	Dev ideal
X-RAY DIFFRACTION	r_bond_d	0.008
X-RAY DIFFRACTION	r_angle_d
X-RAY DIFFRACTION	r_angle_deg	1.3
X-RAY DIFFRACTION	r_plane_restr	0.005

LS refinement shell

*PLUS

Highest resolution: 2.9 Å / Lowest resolution: 2.98 Å / R_factor R_work: 0.33

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