PDB-6wc2: Crystal Structure of a Ternary MEF2 Chimera/NKX2-5/myocardin enha...

ID or keywords:

Entry

Database: PDB / ID: 6wc2

Title

Crystal Structure of a Ternary MEF2 Chimera/NKX2-5/myocardin enhancer DNA Complex

Components

(Myocardin Enhancer DNA) x 2
Homeobox protein Nkx-2.5
MEF2 Chimera,Myocyte-specific enhancer factor 2B,Myocyte-specific enhancer factor 2A

Keywords

TRANSCRIPTION / Transcription Factor / DNA binding Protein / Cardiogenesis / Carcinogenesis

Function / homology

Function and homology information

Purkinje myocyte differentiation / right ventricular cardiac muscle tissue morphogenesis / septum secundum development / proepicardium development / Nkx-2.5 complex / cardiac ventricle formation / apoptotic process involved in heart morphogenesis / pulmonary myocardium development / atrioventricular node cell fate commitment / bundle of His development ...Purkinje myocyte differentiation / right ventricular cardiac muscle tissue morphogenesis / septum secundum development / proepicardium development / Nkx-2.5 complex / cardiac ventricle formation / apoptotic process involved in heart morphogenesis / pulmonary myocardium development / atrioventricular node cell fate commitment / bundle of His development / atrial cardiac muscle cell development / ERK5 cascade / ventricular cardiac myofibril assembly / mitochondrion distribution / atrioventricular node cell development / embryonic heart tube left/right pattern formation / positive regulation of cardioblast differentiation / atrial cardiac muscle tissue development / atrioventricular node development / regulation of cardiac muscle cell proliferation / atrial septum morphogenesis / positive regulation of heart contraction / ventricular cardiac muscle cell development / negative regulation of myotube differentiation / Physiological factors / cardiac conduction system development / cardiac conduction / YAP1- and WWTR1 (TAZ)-stimulated gene expression / pharyngeal system development / positive regulation of sodium ion transport / negative regulation of epithelial cell apoptotic process / : / ventricular trabecula myocardium morphogenesis / adult heart development / outflow tract septum morphogenesis / heart trabecula formation / cardiac muscle tissue morphogenesis / embryonic heart tube development / aortic valve morphogenesis / Cardiogenesis / cardiac muscle cell development / epithelial cell apoptotic process / negative regulation of cardiac muscle cell apoptotic process / muscle organ development / Myogenesis / DNA-binding transcription activator activity / dendrite morphogenesis / ventricular septum morphogenesis / positive regulation of cardiac muscle hypertrophy / cardiac septum morphogenesis / histone acetyltransferase binding / SMAD binding / heart looping / ERK/MAPK targets / thyroid gland development / hemopoiesis / regulation of cardiac conduction / cardiac muscle cell proliferation / regulation of cardiac muscle contraction / positive regulation of transcription initiation by RNA polymerase II / vasculogenesis / heart morphogenesis / spleen development / cardiac muscle contraction / epithelial cell differentiation / positive regulation of neuron differentiation / cellular response to calcium ion / epithelial cell proliferation / positive regulation of epithelial cell proliferation / positive regulation of D-glucose import / RNA polymerase II transcription regulatory region sequence-specific DNA binding / negative regulation of canonical Wnt signaling pathway / protein-DNA complex / RNA polymerase II transcription regulator complex / histone deacetylase binding / sequence-specific double-stranded DNA binding / cell junction / MAPK cascade / heart development / DNA-binding transcription activator activity, RNA polymerase II-specific / transcription regulator complex / DNA-binding transcription factor binding / sequence-specific DNA binding / RNA polymerase II-specific DNA-binding transcription factor binding / transcription by RNA polymerase II / DNA-binding transcription factor activity, RNA polymerase II-specific / cell differentiation / transcription cis-regulatory region binding / protein dimerization activity / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / protein heterodimerization activity / negative regulation of DNA-templated transcription / positive regulation of cell population proliferation / apoptotic process / DNA-templated transcription / chromatin binding / positive regulation of gene expression / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II
Similarity search - Function

Biological species

Homo sapiens (human)
synthetic construct (others)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.1 Å

Authors

Lei, X. / Chen, L.

Funding support

United States, 1items

Citation

Journal: J.Mol.Biol. / Year: 2020
Title: Crystal Structures of Ternary Complexes of MEF2 and NKX2-5 Bound to DNA Reveal a Disease Related Protein-Protein Interaction Interface.
Authors: Lei, X. / Zhao, J. / Sagendorf, J.M. / Rajashekar, N. / Xu, J. / Dantas Machado, A.C. / Sen, C. / Rohs, R. / Feng, P. / Chen, L.

History

Deposition	Mar 29, 2020	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Jul 22, 2020	Provider: repository / Type: Initial release
Revision 1.1	Jul 29, 2020	Group: Database references / Category: citation / citation_author Item: _citation.pdbx_database_id_PubMed / _citation.title ..._citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2	Sep 30, 2020	Group: Database references / Category: citation / citation_author Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.name
Revision 1.3	Oct 18, 2023	Group: Data collection / Database references / 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 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.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	6wc2.cif.gz	454.7 KB	Display	PDBx/mmCIF format
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Validation report

Summary document	6wc2_validation.pdf.gz	515.1 KB	Display	wwPDB validaton report
Full document	6wc2_full_validation.pdf.gz	527.1 KB	Display
Data in XML	6wc2_validation.xml.gz	34.8 KB	Display
Data in CIF	6wc2_validation.cif.gz	51.4 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/wc/6wc2 ftp://data.pdbj.org/pub/pdb/validation_reports/wc/6wc2	HTTPS FTP

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Related structure data

Related structure data	6wc5C 6byyS S: Starting model for refinement C: citing same article (ref.)
Similar structure data	4c07-d 6pfv-2 6pfv-3 2pv0-3 3dsc-d 5bmu-4 1lqw-d 3qd9-3 4je3-d 6wc5-1 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) Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search

Related structure data

6wc5C

6byyS

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	#67 - Jul 2005 TATA-Binding Protein similarity (1) #168 - Dec 2013 DNA Helicase similarity (1) #255 - Mar 2021 Cisplatin and DNA similarity (1) #91 - Jul 2007 Thymine Dimers similarity (1) #122 - Feb 2010 Enhanceosome similarity (1) #172 - Apr 2014 RecA and Rad51 similarity (1) #181 - Jan 2015 Cascade and CRISPR similarity (1) #253 - Jan 2021 Expressome similarity (1) #112 - Apr 2009 Oct and Sox Transcription Factors similarity (7) #135 - Mar 2011 Integrase similarity (1) #150 - Jun 2012 Sliding Clamps similarity (1) #180 - Dec 2014 TAL Effectors similarity (1) #227 - Nov 2018 Telomerase similarity (1) #48 - Dec 2003 Catabolite Activator Protein similarity (1) #84 - Dec 2006 Transposase similarity (1) #139 - Jul 2011 DNA Methyltransferase similarity (1) #155 - Nov 2012 Vitamin D Receptor similarity (1) #3 - Mar 2000 DNA Polymerase similarity (1) #40 - Apr 2003 RNA Polymerase similarity (1) #73 - Jan 2006 Topoisomerase similarity (1) #87 - Mar 2007 Zinc Fingers similarity (1) #119 - Nov 2009 Designed DNA Crystal similarity (1) #125 - May 2010 Parvoviruses similarity (1) #131 - Nov 2010 Inteins similarity (1) #160 - Apr 2013 Actinomycin similarity (1) #190 - Oct 2015 Two-component Systems similarity (1) #23 - Nov 2001 DNA similarity (1) #240 - Dec 2019 Hypoxia-Inducible Factors similarity (1) #257 - May 2021 Fetal Hemoglobin similarity (1) #258 - Jun 2021 Glucocorticoid Receptor and Dexamethasone similarity (1) #31 - Jul 2002 p53 Tumor Suppressor similarity (1) #33 - Sep 2002 HIV Reverse Transcriptase similarity (1) #39 - Mar 2003 lac Repressor similarity (1) #45 - Sep 2003 Estrogen Receptor similarity (1) #55 - Jul 2004 DNA Ligase similarity (1) #7 - Jul 2000 Nucleosome similarity (1) #8 - Aug 2000 Restriction Enzymes similarity (1) #92 - Aug 2007 Anabolic Steroids similarity (1) #241 - Jan 2020 Twenty Years of Molecules similarity (1) #43 - Jul 2003 Src Tyrosine Kinase similarity (1)

PDB pages

PDBj /

wwPDB /

NCBI

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Deposited unit

A: MEF2 Chimera,Myocyte-specific enhancer factor 2B,Myocyte-specific enhancer factor 2A

B: MEF2 Chimera,Myocyte-specific enhancer factor 2B,Myocyte-specific enhancer factor 2A

C: MEF2 Chimera,Myocyte-specific enhancer factor 2B,Myocyte-specific enhancer factor 2A

D: MEF2 Chimera,Myocyte-specific enhancer factor 2B,Myocyte-specific enhancer factor 2A

E: Myocardin Enhancer DNA

F: Myocardin Enhancer DNA

G: Myocardin Enhancer DNA

H: Myocardin Enhancer DNA

I: MEF2 Chimera,Myocyte-specific enhancer factor 2B,Myocyte-specific enhancer factor 2A

J: MEF2 Chimera,Myocyte-specific enhancer factor 2B,Myocyte-specific enhancer factor 2A

K: Myocardin Enhancer DNA

L: Myocardin Enhancer DNA

M: Homeobox protein Nkx-2.5

N: Homeobox protein Nkx-2.5

O: Homeobox protein Nkx-2.5

130 kDa, 15 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: MEF2 Chimera,Myocyte-specific enhancer factor 2B,Myocyte-specific enhancer factor 2A

B: MEF2 Chimera,Myocyte-specific enhancer factor 2B,Myocyte-specific enhancer factor 2A

K: Myocardin Enhancer DNA

L: Myocardin Enhancer DNA

O: Homeobox protein Nkx-2.5

defined by author&software
Evidence: native gel electrophoresis
43.2 kDa, 5 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

C: MEF2 Chimera,Myocyte-specific enhancer factor 2B,Myocyte-specific enhancer factor 2A

D: MEF2 Chimera,Myocyte-specific enhancer factor 2B,Myocyte-specific enhancer factor 2A

G: Myocardin Enhancer DNA

H: Myocardin Enhancer DNA

M: Homeobox protein Nkx-2.5

defined by author&software
43.2 kDa, 5 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

E: Myocardin Enhancer DNA

F: Myocardin Enhancer DNA

I: MEF2 Chimera,Myocyte-specific enhancer factor 2B,Myocyte-specific enhancer factor 2A

J: MEF2 Chimera,Myocyte-specific enhancer factor 2B,Myocyte-specific enhancer factor 2A

N: Homeobox protein Nkx-2.5

defined by author&software
43.2 kDa, 5 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	69.370, 133.900, 140.040
Angle α, β, γ (deg.)	90.000, 90.000, 90.000
Int Tables number	19
Space group name H-M	P2₁2₁2₁

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Component-ID: _ / Refine code: _

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	ARG	ARG	A	A	5 - 91	5 - 91
2	1	LYS	LYS	ARG	ARG	B	B	5 - 91	5 - 91
1	2	GLY	GLY	LYS	LYS	A	A	2 - 89	2 - 89
2	2	GLY	GLY	LYS	LYS	C	C	2 - 89	2 - 89
1	3	GLY	GLY	ARG	ARG	A	A	2 - 91	2 - 91
2	3	GLY	GLY	ARG	ARG	D	D	2 - 91	2 - 91
1	4	GLY	GLY	GLU	GLU	A	A	2 - 92	2 - 92
2	4	GLY	GLY	GLU	GLU	I	I	2 - 92	2 - 92
1	5	GLY	GLY	ARG	ARG	A	A	2 - 91	2 - 91
2	5	GLY	GLY	ARG	ARG	J	J	2 - 91	2 - 91
1	6	LYS	LYS	LYS	LYS	B	B	5 - 89	5 - 89
2	6	LYS	LYS	LYS	LYS	C	C	5 - 89	5 - 89
1	7	LYS	LYS	ARG	ARG	B	B	5 - 91	5 - 91
2	7	LYS	LYS	ARG	ARG	D	D	5 - 91	5 - 91
1	8	LYS	LYS	ARG	ARG	B	B	5 - 91	5 - 91
2	8	LYS	LYS	ARG	ARG	I	I	5 - 91	5 - 91
1	9	LYS	LYS	ARG	ARG	B	B	5 - 91	5 - 91
2	9	LYS	LYS	ARG	ARG	J	J	5 - 91	5 - 91
1	10	GLY	GLY	LYS	LYS	C	C	2 - 89	2 - 89
2	10	GLY	GLY	LYS	LYS	D	D	2 - 89	2 - 89
1	11	GLY	GLY	LYS	LYS	C	C	2 - 89	2 - 89
2	11	GLY	GLY	LYS	LYS	I	I	2 - 89	2 - 89
1	12	GLY	GLY	LYS	LYS	C	C	2 - 89	2 - 89
2	12	GLY	GLY	LYS	LYS	J	J	2 - 89	2 - 89
1	13	GLY	GLY	ARG	ARG	D	D	2 - 91	2 - 91
2	13	GLY	GLY	ARG	ARG	I	I	2 - 91	2 - 91
1	14	GLY	GLY	GLU	GLU	D	D	2 - 92	2 - 92
2	14	GLY	GLY	GLU	GLU	J	J	2 - 92	2 - 92
1	15	DA	DA	DG	DG	E	E	1 - 21	1 - 21
2	15	DA	DA	DG	DG	G	G	1 - 21	1 - 21
1	16	DA	DA	DG	DG	E	E	1 - 21	1 - 21
2	16	DA	DA	DG	DG	K	K	1 - 21	1 - 21
1	17	DC	DC	DT	DT	F	F	1 - 21	1 - 21
2	17	DC	DC	DT	DT	H	H	1 - 21	1 - 21
1	18	DC	DC	DT	DT	F	F	1 - 21	1 - 21
2	18	DC	DC	DT	DT	L	L	1 - 21	1 - 21
1	19	DA	DA	DG	DG	G	G	1 - 21	1 - 21
2	19	DA	DA	DG	DG	K	K	1 - 21	1 - 21
1	20	DC	DC	DT	DT	H	H	1 - 21	1 - 21
2	20	DC	DC	DT	DT	L	L	1 - 21	1 - 21
1	21	GLY	GLY	ARG	ARG	I	I	2 - 91	2 - 91
2	21	GLY	GLY	ARG	ARG	J	J	2 - 91	2 - 91
1	22	ARG	ARG	SER	SER	M	M	142 - 193	6 - 57
2	22	ARG	ARG	SER	SER	N	N	142 - 193	6 - 57
1	23	VAL	VAL	LYS	LYS	M	M	143 - 194	7 - 58
2	23	VAL	VAL	LYS	LYS	O	O	143 - 194	7 - 58
1	24	VAL	VAL	SER	SER	N	N	143 - 193	7 - 57
2	24	VAL	VAL	SER	SER	O	O	143 - 193	7 - 57

NCS ensembles :

#1: Protein	MEF2 Chimera,Myocyte-specific enhancer factor 2B,Myocyte-specific enhancer factor 2A / Serum response factor-like protein 1 / RSRFR2 / Serum response factor-like protein 2 / Serum ...Serum response factor-like protein 1 / RSRFR2 / Serum response factor-like protein 2 / Serum response factor-like protein 1 Mass: 11343.173 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: MEF2A, MEF2, MEF2B, XMEF2 / Production host: Escherichia coli (E. coli) / References: UniProt: Q02078, UniProt: Q02080
#2: DNA chain	Myocardin Enhancer DNA Mass: 6445.210 Da / Num. of mol.: 3 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)
#3: DNA chain	Myocardin Enhancer DNA Mass: 6436.195 Da / Num. of mol.: 3 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)
#4: Protein	Homeobox protein Nkx-2.5 / Cardiac-specific homeobox / Homeobox protein CSX / Homeobox protein NK-2 homolog E Mass: 7671.920 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: NKX2-5, CSX, NKX2.5, NKX2E / Production host: Escherichia coli (E. coli) / References: UniProt: P52952
#5: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 445 / 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: 2.51 Å³/Da / Density % sol: 50.94 %
Crystal grow	Temperature: 291 K / Method: vapor diffusion Details: 0.15 M DL-Malic acid pH 7.0, 20% Polyethylene glycol 3350

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Data collection

Diffraction	Mean temperature: 80 K / Serial crystal experiment: N
Diffraction source	Source: SYNCHROTRON / Site: APS / Beamline: 23-ID-B / Wavelength: 0.9999 Å
Detector	Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Feb 3, 2017
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9999 Å / Relative weight: 1
Reflection	Resolution: 2.1→71 Å / Num. obs: 76673 / % possible obs: 99.65 % / Redundancy: 6.5 % / CC_1/2: 0.997 / Net I/σ(I): 12.92
Reflection shell	Resolution: 2.1→2.175 Å / Num. unique obs: 7471 / CC_1/2: 0.854

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Processing

Software

Name	Version	Classification
REFMAC	5.8.0232	refinement
PDB_EXTRACT	3.25	data extraction
iMOSFLM		data reduction
Aimless		data scaling
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 6BYY

6byy

Resolution: 2.1→70.12 Å / Cor.coef. F_o:F_c: 0.964 / Cor.coef. F_o:F_c free: 0.949 / SU B: 10.075 / SU ML: 0.132 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.196 / ESU R Free: 0.169
Details: U VALUES : WITH TLS ADDED HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.2247	3807	5 %	RANDOM
R_work	0.1857	-	-	-
obs	0.1876	72858	99.76 %	-

Solvent computation

Ion probe radii: 0.7 Å / Shrinkage radii: 0.7 Å / VDW probe radii: 1 Å

Displacement parameters

B_iso max: 144.81 Å² / B_iso mean: 47.851 Å² / B_iso min: 18.63 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	2.5 Å²	0 Å²	-0 Å²
2-	-	-4.28 Å²	0 Å²
3-	-	-	1.78 Å²

Refinement step

Cycle: final / Resolution: 2.1→70.12 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	5929	2565	0	445	8939
B_iso mean	-	-	-	42.01	-
Num. residues	-	-	-	-	830

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.012	0.012	8922
X-RAY DIFFRACTION	r_bond_other_d	0.001	0.018	7335
X-RAY DIFFRACTION	r_angle_refined_deg	1.858	1.493	12510
X-RAY DIFFRACTION	r_angle_other_deg	1.491	1.872	17073
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	6.257	5	705
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	30.04	20.399	376
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	14.608	15	1279
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	16.273	15	71
X-RAY DIFFRACTION	r_chiral_restr	0.093	0.2	1175
X-RAY DIFFRACTION	r_gen_planes_refined	0.012	0.02	8021
X-RAY DIFFRACTION	r_gen_planes_other	0.002	0.02	1953

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	2471	0.14
1	2	B	2471	0.14
2	1	A	2493	0.12
2	2	C	2493	0.12
3	1	A	2511	0.14
3	2	D	2511	0.14
4	1	A	2535	0.14
4	2	I	2535	0.14
5	1	A	2538	0.13
5	2	J	2538	0.13
6	1	B	2381	0.15
6	2	C	2381	0.15
7	1	B	2377	0.17
7	2	D	2377	0.17
8	1	B	2412	0.16
8	2	I	2412	0.16
9	1	B	2461	0.14
9	2	J	2461	0.14
10	1	C	2428	0.14
10	2	D	2428	0.14
11	1	C	2406	0.15
11	2	I	2406	0.15
12	1	C	2453	0.13
12	2	J	2453	0.13
13	1	D	2467	0.15
13	2	I	2467	0.15
14	1	D	2500	0.15
14	2	J	2500	0.15
15	1	E	1812	0.11
15	2	G	1812	0.11
16	1	E	1800	0.11
16	2	K	1800	0.11
17	1	F	1817	0.08
17	2	H	1817	0.08
18	1	F	1798	0.11
18	2	L	1798	0.11
19	1	G	1856	0.1
19	2	K	1856	0.1
20	1	H	1817	0.11
20	2	L	1817	0.11
21	1	I	2543	0.12
21	2	J	2543	0.12
22	1	M	1713	0.12
22	2	N	1713	0.12
23	1	M	1674	0.13
23	2	O	1674	0.13
24	1	N	1669	0.12
24	2	O	1669	0.12

LS refinement shell

Resolution: 2.1→2.155 Å / R_factor R_free error: 0 / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.28	248	-
R_work	0.268	5289	-
all	-	5537	-
obs	-	-	98.79 %

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	2.4767	0.8771	0.2944	4.0149	-0.9283	3.3257	-0.1441	-0.0332	0.0734	-0.3336	0.107	0.5786	0.0346	-0.3992	0.0371	0.048	0.0166	-0.0505	0.2142	-0.015	0.0964	-0.917	-107.111	21.904
2	2.075	0.3276	0.4546	4.2295	-0.8388	2.604	-0.1806	-0.0578	0.1264	-0.0766	0.057	0.1629	-0.1085	-0.0659	0.1235	0.0535	0.0316	-0.0294	0.1636	-0.0379	0.0316	3.678	-103.068	24.258
3	3.6949	1.9007	-0.2094	5.15	-0.4136	3.0599	-0.1239	-0.1913	-0.4164	-0.1299	-0.0017	-0.8098	0.3248	0.3609	0.1256	0.0881	0.0718	0.0569	0.2573	0.0171	0.2087	42.687	-50.791	5.745
4	2.087	0.8471	-0.5581	2.8688	-0.8687	2.8057	-0.2168	-0.1138	-0.3618	-0.3323	0.0335	-0.3887	0.4792	-0.0205	0.1833	0.1686	0.0364	0.089	0.2379	0.0109	0.1805	37.615	-54.544	3.667
5	1.467	2.148	0.2294	6.5454	0.6498	0.2693	0.0672	0.007	0.2244	-0.5069	-0.2502	0.0336	-0.143	-0.0082	0.183	0.1763	-0.0274	-0.0222	0.2553	0.0411	0.209	37.075	-74.877	35.92
6	1.7437	1.9165	0.2045	5.8683	1.2498	1.297	0.0482	-0.0284	0.1249	-0.0438	-0.1719	-0.0262	-0.0959	-0.0087	0.1237	0.0498	-0.0451	-0.0171	0.2595	0.0292	0.0859	36.617	-75.329	36.117
7	1.0559	1.3602	-0.2057	7.8644	-0.8095	0.9446	-0.071	0.0769	-0.0875	-0.3102	-0.2069	-0.085	0.2652	-0.0459	0.2779	0.2354	-0.0302	0.1389	0.289	-0.025	0.1727	42.505	-40.97	-11.057
8	0.9561	2.0381	0.2426	7.5026	-0.9798	1.5664	-0.0104	0.014	-0.0647	-0.0401	-0.3225	-0.2567	0.3996	-0.1027	0.3328	0.2455	-0.0548	0.1544	0.2961	-0.0175	0.1958	42.439	-40.936	-10.717
9	2.6562	0.6869	0.1591	2.3256	1.8294	3.7438	0.1165	-0.1557	0.3298	-0.1374	-0.2314	0.1965	-0.3755	-0.0875	0.1148	0.056	-0.0114	-0.0137	0.228	-0.0173	0.0791	21.649	-86.105	44.156
10	1.9892	0.5756	-0.5342	1.6873	-0.2395	2.1112	0.0601	-0.31	0.1519	0.032	-0.1612	-0.0553	-0.2568	0.2431	0.1011	0.0585	-0.0475	-0.0361	0.2874	-0.0539	0.0741	25.978	-83.713	48.61
11	0.9095	1.4317	0.001	9.275	-1.5101	0.6223	0.1647	0.1349	0.1735	-0.4581	-0.172	0.3044	0.0817	-0.0027	0.0073	0.3153	-0.0043	0.0159	0.2921	0.0055	0.0716	5.491	-93.073	5.983
12	0.6319	1.258	0.3906	9.2324	-0.1166	1.2687	0.1668	0.0847	0.1451	-0.4987	-0.1173	-0.439	0.1904	-0.0083	-0.0494	0.2695	-0.0146	0.0932	0.2841	0.03	0.2117	5.445	-92.945	6.187
13	4.5716	-0.2532	-0.2269	5.9902	0.8328	6.2497	-0.0301	0.2389	-0.033	-0.0467	-0.1139	0.2032	-0.0539	0.1403	0.144	0.0047	-0.0106	-0.0153	0.2258	0.0145	0.0598	51.636	-22.155	-17.754
14	7.4409	2.5878	-1.6785	6.3152	-0.9979	4.2227	-0.0272	0.0272	-0.3716	-0.396	-0.0558	-0.0561	0.2431	0.153	0.083	0.1032	-0.0635	-0.0463	0.2066	0.0324	0.0792	52.328	-58.602	37.136
15	6.2897	0.0212	-1.5666	7.5526	-0.7355	6.6415	-0.2446	0.0628	-0.2926	-0.5402	-0.0206	-0.8161	0.0824	0.4288	0.2652	0.264	-0.0398	0.1326	0.2442	0.0411	0.2795	15.484	-75.727	-1.342

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	2 - 92
2	X-RAY DIFFRACTION	2	B	5 - 92
3	X-RAY DIFFRACTION	3	C	2 - 90
4	X-RAY DIFFRACTION	4	D	2 - 94
5	X-RAY DIFFRACTION	5	E	1 - 21
6	X-RAY DIFFRACTION	6	F	1 - 21
7	X-RAY DIFFRACTION	7	G	1 - 21
8	X-RAY DIFFRACTION	8	H	1 - 21
9	X-RAY DIFFRACTION	9	I	2 - 92
10	X-RAY DIFFRACTION	10	J	2 - 93
11	X-RAY DIFFRACTION	11	K	1 - 21
12	X-RAY DIFFRACTION	12	L	1 - 21
13	X-RAY DIFFRACTION	13	M	142 - 195
14	X-RAY DIFFRACTION	14	N	142 - 194
15	X-RAY DIFFRACTION	15	O	143 - 195

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