PDB-2gpv: Estrogen Related Receptor-gamma ligand binding domain complexed w...

ID or keywords:

Entry

Database: PDB / ID: 2gpv

Title

Estrogen Related Receptor-gamma ligand binding domain complexed with 4-hydroxy-tamoxifen and a SMRT peptide

Components

Estrogen-related receptor gamma
Nuclear receptor corepressor 2

Keywords

TRANSCRIPTION /

Estrogen related receptor / ERR / ERRg /

ESRRG /

Nuclear Receptor /

Steroid Receptor / SMRT /

Tamoxifen

Function / homology

Function and homology information

AF-2 domain binding / Loss of MECP2 binding ability to the NCoR/SMRT complex / negative regulation of androgen receptor signaling pathway / regulation of cellular ketone metabolic process / nuclear glucocorticoid receptor binding / Notch binding / nuclear steroid receptor activity / NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis / Notch-HLH transcription pathway / Regulation of MECP2 expression and activity ...AF-2 domain binding / Loss of MECP2 binding ability to the NCoR/SMRT complex / negative regulation of androgen receptor signaling pathway / regulation of cellular ketone metabolic process / nuclear glucocorticoid receptor binding / Notch binding / nuclear steroid receptor activity / NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis / Notch-HLH transcription pathway / Regulation of MECP2 expression and activity /

estrous cycle / retinoic acid receptor signaling pathway /

estrogen response element binding / nuclear retinoid X receptor binding / intracellular steroid hormone receptor signaling pathway / NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux / response to organonitrogen compound /

lactation / transcription repressor complex / Regulation of lipid metabolism by PPARalpha /

steroid binding / cerebellum development / SUMOylation of transcription cofactors / negative regulation of miRNA transcription / HDACs deacetylate histones / Downregulation of SMAD2/3:SMAD4 transcriptional activity / PPARA activates gene expression / Cytoprotection by HMOX1 / NOTCH1 Intracellular Domain Regulates Transcription / Constitutive Signaling by NOTCH1 PEST Domain Mutants / Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants /

nuclear matrix /

histone deacetylase binding / Transcriptional regulation of white adipocyte differentiation / HCMV Early Events / Nuclear Receptor transcription pathway / transcription corepressor activity /

nuclear receptor activity / sequence-specific double-stranded DNA binding / response to estradiol / positive regulation of cold-induced thermogenesis / DNA-binding transcription activator activity, RNA polymerase II-specific /

nuclear body / DNA-binding transcription factor activity, RNA polymerase II-specific / negative regulation of DNA-templated transcription /

chromatin binding /

chromatin / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II /

DNA binding / zinc ion binding /

nucleoplasm /

membrane / identical protein binding /

nucleus
Similarity search - Function

Biological species

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.85 Å

Authors

Wang, L. / Zuercher, W.J. / Consler, T.G. / Lambert, M.H. / Miller, A.B. / Osband-miller, L.A. / McKee, D.D. / Willson, T.M. / Nolte, R.T.

Citation

Journal: J.Biol.Chem. / Year: 2006
Title: X-ray crystal structures of the estrogen-related receptor-gamma ligand binding domain in three functional states reveal the molecular basis of small molecule regulation.
Authors: Wang, L. / Zuercher, W.J. / Consler, T.G. / Lambert, M.H. / Miller, A.B. / Orband-Miller, L.A. / McKee, D.D. / Willson, T.M. / Nolte, R.T.

History

Deposition	Apr 18, 2006	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Sep 26, 2006	Provider: repository / Type: Initial release
Revision 1.1	Oct 24, 2007	Group: Version format compliance
Revision 1.2	Jul 13, 2011	Group: Advisory / Derived calculations / Version format compliance
Revision 1.3	Oct 18, 2017	Group: Refinement description / Category: software / Item: _software.classification / _software.name
Revision 1.4	Jan 22, 2020	Group: Derived calculations Category: pdbx_struct_assembly / pdbx_struct_assembly_gen ...pdbx_struct_assembly / pdbx_struct_assembly_gen / pdbx_struct_assembly_prop / pdbx_struct_oper_list Item: _pdbx_struct_assembly.details / _pdbx_struct_assembly.method_details ..._pdbx_struct_assembly.details / _pdbx_struct_assembly.method_details / _pdbx_struct_assembly.oligomeric_count / _pdbx_struct_assembly.oligomeric_details
Revision 1.5	Aug 30, 2023	Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / 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 / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.end_auth_comp_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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PDBx/mmCIF format	2gpv.cif.gz	267.7 KB	Display	PDBx/mmCIF format
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Validation report

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

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Related structure data

Related structure data	2gp7SC 2gpoC 2gppC 2gpuC S: Starting model for refinement C: citing same article (ref.)
Similar structure data	4g0b-d 5kya-d 3ob6-d 3pwv-d 3jq1-d 4kxf-5 6cwz-d 2dbu-d 2y53-d 2fln-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) 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	#45 - Sep 2003 Estrogen Receptor similarity (2) #155 - Nov 2012 Vitamin D Receptor similarity (4) #245 - May 2020 Spliceosomes similarity (4) #122 - Feb 2010 Enhanceosome similarity (3) #44 - Aug 2003 Calmodulin similarity (1) #98 - Feb 2008 Small Interfering RNA similarity (2) #60 - Dec 2004 Ubiquitin similarity (1) #196 - Apr 2016 Lead Poisoning similarity (1) #28 - Apr 2002 Anthrax Toxin similarity (1) #258 - Jun 2021 Glucocorticoid Receptor and Dexamethasone similarity (1) #234 - Jun 2019 MDM2 and Cancer similarity (1) #241 - Jan 2020 Twenty Years of Molecules similarity (1)

PDB pages

PDBj /

wwPDB /

NCBI

Related items in Molecule of the Month

#45 - Sep 2003
Estrogen Receptor
similarity (2)
#155 - Nov 2012
Vitamin D Receptor
similarity (4)
#245 - May 2020
Spliceosomes
similarity (4)
#122 - Feb 2010
Enhanceosome
similarity (3)
#44 - Aug 2003
Calmodulin
similarity (1)
#98 - Feb 2008
Small Interfering RNA
similarity (2)
#60 - Dec 2004
Ubiquitin
similarity (1)
#196 - Apr 2016
Lead Poisoning
similarity (1)
#28 - Apr 2002
Anthrax Toxin
similarity (1)
#258 - Jun 2021
Glucocorticoid Receptor and Dexamethasone
similarity (1)
#234 - Jun 2019
MDM2 and Cancer
similarity (1)
#241 - Jan 2020
Twenty Years of Molecules
similarity (1)

Deposited unit

A: Estrogen-related receptor gamma

B: Estrogen-related receptor gamma

C: Estrogen-related receptor gamma

D: Estrogen-related receptor gamma

E: Estrogen-related receptor gamma

F: Estrogen-related receptor gamma

G: Nuclear receptor corepressor 2

H: Nuclear receptor corepressor 2

I: Nuclear receptor corepressor 2

hetero molecules

167 kDa, 9 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Estrogen-related receptor gamma

B: Estrogen-related receptor gamma

D: Estrogen-related receptor gamma

E: Estrogen-related receptor gamma

G: Nuclear receptor corepressor 2

H: Nuclear receptor corepressor 2

hetero molecules

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

2

C: Estrogen-related receptor gamma

F: Estrogen-related receptor gamma

I: Nuclear receptor corepressor 2

hetero molecules

C: Estrogen-related receptor gamma

F: Estrogen-related receptor gamma

I: Nuclear receptor corepressor 2

hetero molecules

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

Unit cell

Length a, b, c (Å)	200.22, 117.17, 90.47
Angle α, β, γ (deg.)	90, 102.36, 90
Int Tables number	5
Space group name H-M	C121

Components on special symmetry positions

ID	Model	Components
1	1	C-42- HOH

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	A
2	1	B
3	1	C
4	1	D
5	1	E
6	1	F
1	2	A
2	2	B
3	2	C
1	3	G
2	3	H
3	3	I

NCS domain segments:

Component-ID: 1 / Refine code: 5

Dom-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	LYS	LYS	ILE	ILE	A	A	232 - 438	4 - 210
2	1	PRO	PRO	ILE	ILE	B	B	233 - 438	5 - 210
3	1	PRO	PRO	ILE	ILE	C	C	233 - 438	5 - 210
4	1	PRO	PRO	ILE	ILE	D	D	233 - 438	5 - 210
5	1	TYR	TYR	ILE	ILE	E	E	234 - 438	6 - 210
6	1	PRO	PRO	ILE	ILE	F	F	233 - 438	5 - 210
1	2	LYS	LYS	GLU	GLU	A	A	439 - 455	211 - 227
2	2	LYS	LYS	GLU	GLU	B	B	439 - 455	211 - 227
3	2	LYS	LYS	GLU	GLU	C	C	439 - 455	211 - 227
1	3	GLY	GLY	GLY	GLY	G	G	1319 - 1330	4 - 15
2	3	GLY	GLY	GLY	GLY	H	H	1319 - 1330	4 - 15
3	3	GLY	GLY	GLY	GLY	I	I	1319 - 1330	4 - 15

NCS ensembles :

ID
1
2
3

#1: Protein	Estrogen-related receptor gamma / / Estrogen receptor-related protein 3 / ERR gamma-2 Mass: 26084.373 Da / Num. of mol.: 6 / Fragment: Ligand Binding Domain (residues 229-458) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ESRRG / Plasmid: pRSET / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P62508
#2: Protein/peptide	Nuclear receptor corepressor 2 / N-CoR2 / Silencing mediator of retinoic acid and thyroid hormone receptor / SMRT / SMRTe / Thyroid- ...N-CoR2 / Silencing mediator of retinoic acid and thyroid hormone receptor / SMRT / SMRTe / Thyroid- / retinoic-acid-receptor-associated corepressor / T3 receptor- associating factor / TRAC / CTG repeat protein 26 / SMAP270 / Mass: 2599.999 Da / Num. of mol.: 3 / Fragment: LXXLL Motif (residues 2338-2359) / Source method: obtained synthetically / Details: Chemically synthesized / References: UniProt: Q9Y618, UniProt: Q4RA23*PLUS
#3: Chemical	ChemComp-OHT / 4-HYDROXYTAMOXIFEN / Afimoxifene Mass: 387.514 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C₂₆H₂₉NO₂
#4: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 61 / Source method: isolated from a natural source / Formula: H₂O

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 3.15 Å³/Da / Density % sol: 60.99 %
Crystal grow	Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.8 Details: 7% PEG3350 0.2M Lithium Acetate, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: APS / Beamline: 17-ID / Wavelength: 1 Å
Detector	Type: MAR CCD 165 mm / Detector: CCD
Radiation	Monochromator: Si 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 1 Å / Relative weight: 1
Reflection	Resolution: 2.85→50 Å / Num. all: 48079 / Num. obs: 43368 / % possible obs: 90.2 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 3.4 % / R_merge(I) obs: 0.093 / Χ²: 1.018
Reflection shell	Resolution: 2.85→2.95 Å / % possible obs: 39.9 % / Redundancy: 1.4 % / R_merge(I) obs: 0.298 / Num. measured obs: 1891 / Χ²: 0.86 / % possible all: 38.21

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Processing

Software

Name	Version	Classification
SCALEPACK		data scaling
REFMAC	5.2.0019	refinement
PDB_EXTRACT	1.7	data extraction
MAR345		data collection
PHENIX		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 2GP7

2gp7

Resolution: 2.85→19.91 Å / Cor.coef. F_o:F_c: 0.9 / Cor.coef. F_o:F_c free: 0.819 / SU B: 34.341 / SU ML: 0.319 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.423 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.279	1359	3.1 %	RANDOM
R_work	0.219	-	-	-
all	0.221	47597	-	-
obs	0.221	43251	90.87 %	-

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: 13.974 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	1.93 Å²	0 Å²	-0.55 Å²
2-	-	0.14 Å²	0 Å²
3-	-	-	-2.31 Å²

Refinement step

Cycle: LAST / Resolution: 2.85→19.91 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	10545	0	174	61	10780

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.01	0.022	10995
X-RAY DIFFRACTION	r_bond_other_d	0.001	0.02	7335
X-RAY DIFFRACTION	r_angle_refined_deg	1.164	2.006	14878
X-RAY DIFFRACTION	r_angle_other_deg	0.863	3	18121
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.155	5	1340
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	36.385	25.804	460
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	17.053	15	2066
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	14.966	15	33
X-RAY DIFFRACTION	r_chiral_restr	0.056	0.2	1716
X-RAY DIFFRACTION	r_gen_planes_refined	0.003	0.02	12144
X-RAY DIFFRACTION	r_gen_planes_other	0.001	0.02	2049
X-RAY DIFFRACTION	r_nbd_refined	0.231	0.2	2846
X-RAY DIFFRACTION	r_nbd_other	0.18	0.2	7227
X-RAY DIFFRACTION	r_nbtor_refined	0.183	0.2	5449
X-RAY DIFFRACTION	r_nbtor_other	0.086	0.2	5602
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.147	0.2	257
X-RAY DIFFRACTION	r_xyhbond_nbd_other	0.027	0.2	2
X-RAY DIFFRACTION	r_symmetry_vdw_refined	0.17	0.2	33
X-RAY DIFFRACTION	r_symmetry_vdw_other	0.252	0.2	47
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.157	0.2	2
X-RAY DIFFRACTION	r_mcbond_it	0.335	1.5	7033
X-RAY DIFFRACTION	r_mcbond_other	0.068	1.5	2678
X-RAY DIFFRACTION	r_mcangle_it	0.536	2	10833
X-RAY DIFFRACTION	r_scbond_it	0.83	3	4638
X-RAY DIFFRACTION	r_scangle_it	1.297	4.5	4045

Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-ID	Dom-ID	Auth asym-ID	Number	Rms	Type	Weight
1	1	A	1192	0.19	MEDIUM POSITIONAL	0.5
1	2	B	1192	0.19	MEDIUM POSITIONAL	0.5
1	3	C	1192	0.18	MEDIUM POSITIONAL	0.5
1	4	D	1192	0.2	MEDIUM POSITIONAL	0.5
1	5	E	1192	0.2	MEDIUM POSITIONAL	0.5
1	6	F	1192	0.2	MEDIUM POSITIONAL	0.5
1	1	A	1463	0.57	LOOSE POSITIONAL	5
1	2	B	1463	0.59	LOOSE POSITIONAL	5
1	3	C	1463	0.53	LOOSE POSITIONAL	5
1	4	D	1463	0.78	LOOSE POSITIONAL	5
1	5	E	1463	0.55	LOOSE POSITIONAL	5
1	6	F	1463	0.56	LOOSE POSITIONAL	5
1	1	A	1192	0.32	MEDIUM THERMAL	2
1	2	B	1192	0.27	MEDIUM THERMAL	2
1	3	C	1192	0.27	MEDIUM THERMAL	2
1	4	D	1192	0.27	MEDIUM THERMAL	2
1	5	E	1192	0.3	MEDIUM THERMAL	2
1	6	F	1192	0.32	MEDIUM THERMAL	2
1	1	A	1463	0.89	LOOSE THERMAL	10
1	2	B	1463	0.85	LOOSE THERMAL	10
1	3	C	1463	0.88	LOOSE THERMAL	10
1	4	D	1463	0.8	LOOSE THERMAL	10
1	5	E	1463	0.78	LOOSE THERMAL	10
1	6	F	1463	0.93	LOOSE THERMAL	10
2	1	A	94	0.35	MEDIUM POSITIONAL	0.5
2	2	B	94	0.32	MEDIUM POSITIONAL	0.5
2	3	C	94	0.32	MEDIUM POSITIONAL	0.5
2	1	A	130	0.9	LOOSE POSITIONAL	5
2	2	B	130	0.86	LOOSE POSITIONAL	5
2	3	C	130	0.73	LOOSE POSITIONAL	5
2	1	A	94	0.25	MEDIUM THERMAL	2
2	2	B	94	0.2	MEDIUM THERMAL	2
2	3	C	94	0.2	MEDIUM THERMAL	2
2	1	A	130	0.58	LOOSE THERMAL	10
2	2	B	130	0.47	LOOSE THERMAL	10
2	3	C	130	0.49	LOOSE THERMAL	10
3	1	G	63	0.51	MEDIUM POSITIONAL	0.5
3	2	H	63	0.31	MEDIUM POSITIONAL	0.5
3	3	I	63	0.37	MEDIUM POSITIONAL	0.5
3	1	G	66	0.99	LOOSE POSITIONAL	5
3	2	H	66	0.91	LOOSE POSITIONAL	5
3	3	I	66	0.81	LOOSE POSITIONAL	5
3	1	G	63	0.17	MEDIUM THERMAL	2
3	2	H	63	0.25	MEDIUM THERMAL	2
3	3	I	63	0.25	MEDIUM THERMAL	2
3	1	G	66	0.96	LOOSE THERMAL	10
3	2	H	66	0.99	LOOSE THERMAL	10
3	3	I	66	0.6	LOOSE THERMAL	10

LS refinement shell

Resolution: 2.85→2.922 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.444	40	-
R_work	0.299	1272	-
all	-	1312	-
obs	-	-	38.21 %

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	1.1299	0.4065	0.0508	2.964	0.9184	4.2817	0.1058	-0.1082	0.0659	0.2227	-0.1272	0.1168	-0.1978	0.0031	0.0214	-0.1491	0.0284	0.0927	-0.2671	0.0261	-0.1417	38.529	0.949	43.962
2	1.6328	-1.061	-1.0771	5.0717	1.2065	3.976	-0.0384	0.145	-0.1079	-0.1703	-0.1446	0.1461	0.4402	0.0324	0.1829	-0.0695	0.0802	0.109	-0.2278	0.0268	-0.123	28.379	-16.923	87.165
3	4.0818	-0.6747	-1.1429	1.7229	0.6444	4.5301	0.0145	-0.1792	-0.0374	0.094	0.052	0.0562	-0.2576	-0.5111	-0.0664	-0.1779	0.0746	-0.0264	-0.1167	0.019	-0.0944	67.056	-17.736	109.052
4	0.8674	-0.1713	0.0314	3.9246	0.7288	3.2174	-0.1523	-0.1122	-0.1366	0.2104	-0.0894	0.5884	0.4333	-0.4552	0.2418	-0.017	-0.0316	0.1386	-0.1321	0.0167	-0.0272	26.162	-20.49	43.048
5	1.9945	-1.0331	0.6678	2.3765	-1.0926	2.5239	0.1367	0.227	0.0078	-0.1592	-0.1193	0.2025	-0.2637	-0.0824	-0.0174	-0.0426	0.062	0.112	-0.2112	-0.0329	-0.1298	20.144	5.705	88.841
6	1.5898	-0.1315	1.1627	0.4282	-0.2303	2.5552	-0.0129	-0.1041	-0.1606	0.0502	0.0025	-0.0591	0.0982	0.3676	0.0104	-0.124	0.0651	0.0722	-0.1149	-0.0111	0.0097	86.417	-29.24	109.651

Refinement TLS group

Refine-ID: X-RAY DIFFRACTION / Selection: ALL

ID	Refine TLS-ID	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	A	A	232 - 439	4 - 211
2	1	G	G	1319 - 1330	4 - 15
3	2	B	B	233 - 439	5 - 211
4	2	H	H	1319 - 1330	4 - 15
5	3	C	C	233 - 439	5 - 211
6	3	I	I	1319 - 1330	4 - 15
7	4	D	D	233 - 441	5 - 213
8	4	A	A	440 - 455	212 - 227
9	5	E	E	234 - 441	6 - 213
10	5	C	C	440 - 455	212 - 227
11	6	F	F	233 - 440	5 - 212
12	6	B	B	440 - 455	212 - 227

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About Yorodumi

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Yorodumi