PDB-2oo4: Structure of LNR-HD (Negative Regulatory Region) from human Notch 2

ID or keywords:

Entry

Database: PDB / ID: 2oo4

Title

Structure of LNR-HD (Negative Regulatory Region) from human Notch 2

Components

Neurogenic locus notch homolog protein 2

Keywords

CELL CYCLE /

SIGNALING PROTEIN / alpha-beta-sandwich / SEA domain / LNR / Lin12 Notch Repeat / cysteine-rich /

HD domain

Function / homology

Function and homology information

cholangiocyte proliferation / proximal tubule development / regulation of osteoclast development / intrahepatic bile duct development / glomerular capillary formation / ciliary body morphogenesis / podocyte development / Defective LFNG causes SCDO3 / morphogenesis of an epithelial sheet / marginal zone B cell differentiation ...cholangiocyte proliferation / proximal tubule development / regulation of osteoclast development / intrahepatic bile duct development / glomerular capillary formation / ciliary body morphogenesis / podocyte development / Defective LFNG causes SCDO3 / morphogenesis of an epithelial sheet / marginal zone B cell differentiation / Pre-NOTCH Processing in the Endoplasmic Reticulum / atrioventricular node development / positive regulation of smooth muscle cell differentiation / cellular response to tumor cell / positive regulation of keratinocyte proliferation / atrial septum morphogenesis / hepatocyte proliferation / left/right axis specification / NOTCH2 intracellular domain regulates transcription / Pre-NOTCH Processing in Golgi / placenta blood vessel development / myeloid dendritic cell differentiation / pulmonary valve morphogenesis /

bone remodeling /

cell fate determination / positive regulation of BMP signaling pathway / positive regulation of osteoclast differentiation / inflammatory response to antigenic stimulus / positive regulation of Ras protein signal transduction / embryonic limb morphogenesis / NOTCH4 Intracellular Domain Regulates Transcription / Notch-HLH transcription pathway / heart looping /

humoral immune response /

hemopoiesis /

NF-kappaB binding / BMP signaling pathway / cis-regulatory region sequence-specific DNA binding /

Notch signaling pathway / NOTCH2 Activation and Transmission of Signal to the Nucleus /

axon guidance / animal organ morphogenesis / multicellular organism growth /

wound healing /

cilium / Pre-NOTCH Transcription and Translation / positive regulation of miRNA transcription /

signaling receptor activity /

nervous system development / DNA-binding transcription activator activity, RNA polymerase II-specific / in utero embryonic development / positive regulation of ERK1 and ERK2 cascade /

receptor complex / intracellular signal transduction / defense response to bacterium / positive regulation of apoptotic process /

Golgi membrane / negative regulation of gene expression / apoptotic process /

calcium ion binding / endoplasmic reticulum membrane / negative regulation of apoptotic process / negative regulation of transcription by RNA polymerase II /

enzyme binding /

cell surface / positive regulation of transcription by RNA polymerase II / extracellular region /

nucleoplasm /

membrane /

nucleus /

plasma membrane
Similarity search - Function

Biological species

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MIRAS / Resolution: 2.003 Å

Authors

Gordon, W.R. / Vardar-Ulu, D. / Histen, G. / Sanchez-Irizarry, C. / Aster, J.C. / Blacklow, S.C.

Citation

Journal: Nat.Struct.Mol.Biol. / Year: 2007
Title: Structural basis for autoinhibition of Notch
Authors: Gordon, W.R. / Vardar-Ulu, D. / Histen, G. / Sanchez-Irizarry, C. / Aster, J.C. / Blacklow, S.C.

History

Deposition	Jan 25, 2007	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Apr 3, 2007	Provider: repository / Type: Initial release
Revision 1.1	May 1, 2008	Group: Version format compliance
Revision 1.2	Jul 13, 2011	Group: Non-polymer description / Version format compliance
Revision 1.3	Apr 8, 2015	Group: Database references
Revision 1.4	Oct 18, 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 1.5	Dec 27, 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_struct_conn_angle / struct_conn / struct_ncs_dom_lim / struct_ref_seq_dif / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ref_seq_dif.details / _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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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/oo/2oo4 ftp://data.pdbj.org/pub/pdb/validation_reports/oo/2oo4	HTTPS FTP

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Related structure data

Similar structure data	4ijd-1 5bp7-1 1eu3-2 2ji3-2 5bp7-3 1i4r-d 1vzi-d 5njv-2 6h96-1 2ji1-1 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	#126 - Jun 2010 Epidermal Growth Factor similarity (10) #75 - Mar 2006 Tissue Factor similarity (8) #122 - Feb 2010 Enhanceosome similarity (3) #182 - Feb 2015 Insulin receptor similarity (1) #17 - May 2001 Cyclooxygenase similarity (1) #60 - Dec 2004 Ubiquitin similarity (1) #250 - Oct 2020 Capsaicin Receptor TRPV1 similarity (1) #234 - Jun 2019 MDM2 and Cancer similarity (1) #223 - Jul 2018 Piezo1 Mechanosensitive Channel similarity (1) #184 - Apr 2015 Glucagon similarity (1)

PDB pages

PDBj /

wwPDB /

NCBI

Related items in Molecule of the Month

#126 - Jun 2010
Epidermal Growth Factor
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#17 - May 2001
Cyclooxygenase
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#60 - Dec 2004
Ubiquitin
similarity (1)
#250 - Oct 2020
Capsaicin Receptor TRPV1
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similarity (1)

Deposited unit

A: Neurogenic locus notch homolog protein 2

B: Neurogenic locus notch homolog protein 2

hetero molecules

53 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Neurogenic locus notch homolog protein 2

hetero molecules

defined by author
26.8 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: Neurogenic locus notch homolog protein 2

hetero molecules

defined by author
26.2 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	45.372, 74.706, 139.412
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	19
Space group name H-M	P2₁2₁2₁

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	A
2	1	B

NCS domain segments:

Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: ASN / Beg label comp-ID: ASN / End auth comp-ID: ASP / End label comp-ID: ASP / Refine code: 5 / Auth seq-ID: 1541 - 1628 / Label seq-ID: 120 - 185

Dom-ID	Auth asym-ID	Label asym-ID
1	A	A
2	B	B

Details

There are two biological assemblies in the asymmetric unit

#1: Protein	Neurogenic locus notch homolog protein 2 / Notch 2 / hN2 / Notch 2 extracellular truncation / Notch 2 intracellular domain Mass: 25872.744 Da / Num. of mol.: 2 / Fragment: LNR-HD/NRR / Mutation: excision of furin loop Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: NOTCH2 / Plasmid: LNR-HD / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta PLysS (DE3) BL21 / References: UniProt: Q04721
#2: Chemical	ChemComp-CA / CALCIUM ION Mass: 40.078 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Ca
#3: Chemical	ChemComp-ZN / ZINC ION Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn
#4: Chemical	ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol Mass: 92.094 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C₃H₈O₃
#5: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 164 / Source method: isolated from a natural source / Formula: H₂O

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Experiment

Experiment	Method: X-RAY DIFFRACTION / Number of used crystals: 5

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Sample preparation

Crystal

ID	Density Matthews (Å³/Da)	Density % sol (%)
1	2.28	46.11
2

Crystal grow

Temperature (K)	Crystal-ID	pH	Details
298	1	6.5	100 mM BisTris, 200mM MgCl2, 18% PEG3350, 10% glycerol, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
298	2		100mM Tris, 200mM MgCl2, 24% PEG3350, 10% glycerol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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Data collection

Diffraction

ID	Mean temperature (K)	Crystal-ID
1	77.2	1
2	77.2	1
3	77.2	1
4	77.2	1

Diffraction source

Source:

SYNCHROTRON / Site:

NSLS

/ Beamline: X29A / Wavelength: 1.006

Detector

Type: ADSC QUANTUM 315 / Detector: CCD / Date: Feb 25, 2006
Details: BEAMLINE X29 FEATURES HIGH- FLUX RADIATION DERIVED FROM A 54-POLE HARMONIC EMISSION UNDULATOR, A VERTICALLY FOCUSING MIRROR AND A HORIZONTALLY FOCUSING MONOCHROMATOR

Radiation

ID	Monochromator	Protocol	Monochromatic (M) / Laue (L)	Scattering type	Wavelength-ID
1	SI(111)	SINGLE WAVELENGTH	M	x-ray	1
2	SI(111)	SINGLE WAVELENGTH	M	x-ray	1
3	SI(111)	SINGLE WAVELENGTH	M	x-ray	1
4	SI(111)	SINGLE WAVELENGTH	M	x-ray	1

Radiation wavelength

Wavelength: 1.006 Å / Relative weight: 1

Reflection

Redundancy (%)	ID	Av σ(I) over netI	Number	R_merge(I) obs	Χ²	D res high (Å)	D res low (Å)	Num. obs	% possible obs
5.6	1	17.3	94671	0.069	1.02	2.5	40	16807	99.2
6.7	2	17.6	164465	0.095	1.14	2.2	30	24723	99.8
9.7	3	17.2	183833	0.074	0.82	2.4	30	19028	99.2
4.8	4	17.7	88842	0.076	1.16	2.4	40	18347	95.7

Diffraction reflection shell

Highest resolution (Å)	Lowest resolution (Å)	% possible obs (%)	ID	R_merge(I) obs	Chi squared	Redundancy
5.38	40	95	1	0.059	1.38	5.9
4.27	5.38	98.6	1	0.051	1.075	5.7
3.73	4.27	99.8	1	0.059	1.039	5.9
3.39	3.73	99.9	1	0.07	1.071	5.9
3.15	3.39	100	1	0.082	0.985	5.7
2.96	3.15	99.9	1	0.109	1.03	5.6
2.82	2.96	99.9	1	0.152	1.028	5.5
2.69	2.82	99.9	1	0.22	0.906	5.4
2.59	2.69	99.8	1	0.291	0.795	5.3
2.5	2.59	100	1	0.382	0.774	5.2
4.73	30	98.8	2	0.089	1.294	6.5
3.76	4.73	99.6	2	0.084	1.232	6.8
3.29	3.76	99.9	2	0.093	1.296	6.8
2.99	3.29	100	2	0.092	1.204	6.7
2.77	2.99	100	2	0.106	1.176	6.7
2.61	2.77	99.9	2	0.123	1.157	6.7
2.48	2.61	100	2	0.142	1.165	6.6
2.37	2.48	100	2	0.175	1.08	6.5
2.28	2.37	100	2	0.216	0.95	6.6
2.2	2.28	100	2	0.282	0.804	6.5
5.16	30	98.8	3	0.077	1.267	9.9
4.1	5.16	99.8	3	0.06	0.93	9.8
3.58	4.1	100	3	0.064	0.955	10.2
3.26	3.58	99.8	3	0.067	0.881	9.8
3.02	3.26	99.8	3	0.076	0.873	9.6
2.85	3.02	99.5	3	0.093	0.847	9.5
2.7	2.85	99.2	3	0.122	0.743	9.4
2.59	2.7	98.6	3	0.155	0.644	9.4
2.49	2.59	98.5	3	0.196	0.53	9.4
2.4	2.49	98	3	0.242	0.466	9.5
5.17	40	91.7	4	0.058	1.378	4.8
4.1	5.17	93.8	4	0.056	1.208	4.6
3.58	4.1	94.7	4	0.068	1.195	4.8
3.26	3.58	96.2	4	0.077	1.272	4.9
3.02	3.26	96.2	4	0.09	1.124	4.9
2.85	3.02	96.6	4	0.12	1.154	4.9
2.7	2.85	96.4	4	0.161	1.195	4.9
2.59	2.7	96.7	4	0.213	1.138	4.9
2.49	2.59	97.1	4	0.271	0.993	4.9
2.4	2.49	98.3	4	0.339	0.924	4.9

Reflection

Resolution: 2.003→30 Å / Num. obs: 31791 / % possible obs: 97.2 % / Redundancy: 4.9 % / B_iso Wilson estimate: 33 Å² / R_merge(I) obs: 0.075 / Net I/σ(I): 15.5

Reflection shell

Resolution: 2.003→2.07 Å / Redundancy: 4.7 % / R_merge(I) obs: 0.405 / % possible all: 98.1

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Phasing

Phasing	Method: MIRAS

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Processing

Software

Name	Version	Classification
DENZO		data reduction
SCALEPACK		data scaling
SHARP		phasing
SOLOMON		phasing
REFMAC	5.2.0019	refinement
PDB_EXTRACT	2	data extraction
HKL-2000		data reduction

Refinement

Method to determine structure:

MIRAS / Resolution: 2.003→30 Å / Cor.coef. F_o:F_c: 0.939 / Cor.coef. F_o:F_c free: 0.919 / SU B: 9.726 / SU ML: 0.141 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.225 / ESU R Free: 0.192 / Stereochemistry target values: MAXIMUM LIKELIHOOD

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.268	1603	5.1 %	RANDOM
R_work	0.226	-	-	-
obs	0.229	31732	97.1 %	-

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: 49.12 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	0.22 Å²	0 Å²	0 Å²
2-	-	-0.88 Å²	0 Å²
3-	-	-	0.66 Å²

Refinement step

Cycle: LAST / Resolution: 2.003→30 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	3411	0	67	164	3642

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.01	0.021	3548
X-RAY DIFFRACTION	r_bond_other_d
X-RAY DIFFRACTION	r_angle_refined_deg	1.174	1.948	4824
X-RAY DIFFRACTION	r_angle_other_deg
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.348	5	450
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	35.916	25.954	173
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	13.579	15	529
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	14.322	15	12
X-RAY DIFFRACTION	r_chiral_restr	0.088	0.2	520
X-RAY DIFFRACTION	r_gen_planes_refined	0.003	0.02	2732
X-RAY DIFFRACTION	r_gen_planes_other
X-RAY DIFFRACTION	r_nbd_refined	0.212	0.2	1653
X-RAY DIFFRACTION	r_nbd_other
X-RAY DIFFRACTION	r_nbtor_refined	0.298	0.2	2419
X-RAY DIFFRACTION	r_nbtor_other
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.13	0.2	193
X-RAY DIFFRACTION	r_xyhbond_nbd_other
X-RAY DIFFRACTION	r_metal_ion_refined	0.131	0.2	22
X-RAY DIFFRACTION	r_metal_ion_other
X-RAY DIFFRACTION	r_symmetry_vdw_refined	0.133	0.2	50
X-RAY DIFFRACTION	r_symmetry_vdw_other
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.085	0.2	10
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	0.403	1.5	2314
X-RAY DIFFRACTION	r_mcbond_other
X-RAY DIFFRACTION	r_mcangle_it	0.677	2	3576
X-RAY DIFFRACTION	r_scbond_it	1.088	3	1411
X-RAY DIFFRACTION	r_scangle_it	1.645	4.5	1248
X-RAY DIFFRACTION	r_rigid_bond_restr
X-RAY DIFFRACTION	r_sphericity_free
X-RAY DIFFRACTION	r_sphericity_bonded

Refine LS restraints NCS

Dom-ID: 1 / Auth asym-ID: A / Ens-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Number	Type	Rms dev position (Å)	Weight position
260	medium positional	0.19	0.5
251	loose positional	0.57	5
260	medium thermal	0.51	2
251	loose thermal	1.21	10

LS refinement shell

Resolution: 2.003→2.06 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.283	137	-
R_work	0.248	2132	-
obs	-	-	96.02 %

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	38.434	36.0304	-64.6786	109.9828	-129.8061	171.6325	1.0631	1.502	0.8668	3.752	-2.5944	2.0231	-3.8248	4.9565	1.5314	0.1594	-0.1686	-0.2063	0.3222	-0.0681	0.4173	27.6999	-25.7317	2.2973
2	2.737	1.5748	1.1775	3.6339	-1.3139	6.0185	0.0283	-0.0998	-0.099	0.4783	-0.187	-0.6485	0.1217	0.726	0.1588	-0.1571	0.0293	-0.1671	-0.0112	-0.0183	-0.0369	20.4711	-21.6564	-8.0927
3	10.0655	-1.0078	-8.4159	6.4491	-2.1653	8.4619	0.1433	0.4313	0.802	0.4763	-0.0688	-0.7383	-1.3536	-0.0755	-0.0745	0.0904	-0.2271	-0.1817	0.1216	0.0905	0.1384	22.8702	-5.7659	-17.9237
4	8.5313	5.0083	-0.008	10.8906	-0.4303	7.1327	-0.0017	0.3256	0.4489	-0.321	-0.3487	-0.4443	-0.708	0.7937	0.3504	-0.1594	-0.1063	-0.0396	0.0555	0.0857	-0.0927	20.0576	-11.8702	-22.606
5	5.6864	-2.0104	-1.0711	9.264	2.6287	5.8821	-0.1635	0.4113	0.5333	0.111	0.4175	0.5679	-0.6005	-0.2669	-0.2541	-0.0635	0.0449	0.0491	-0.1919	0.0799	-0.1739	-4.1849	-4.0044	-25.6751
6	17.0587	-18.6105	-5.8029	78.9226	14.878	3.2203	1.4628	1.0829	-1.0429	-1.5198	-0.8238	1.4813	0.2598	-0.9721	-0.639	0.2445	0.0301	-0.2368	0.1083	-0.0066	-0.144	-2.9901	-14.68	-37.664
7	2.1454	2.0529	0.2064	4.4876	-0.6486	2.9886	0.0096	-0.1193	0.0343	0.079	0.0714	0.232	-0.0584	-0.1638	-0.0811	-0.2571	0.0481	-0.0281	-0.2055	0.0265	-0.2625	-1.9314	-21.2202	-19.5769
8	0.0042	-0.3662	-0.0486	51.0064	34.204	48.2502	1.5926	-1.0944	-0.6893	2.6761	0.1451	-1.3214	1.6101	-0.6815	-1.7376	0.241	-0.0176	0.0942	0.2757	0.1402	-0.1048	-2.3227	-28.9678	-2.7391
9	2.0323	0.7638	0.048	3.681	-2.755	5.2692	0.0079	0.0949	-0.0457	-0.0745	0.017	-0.2855	-0.0515	0.2707	-0.0249	-0.2961	0.018	-0.0067	-0.1987	-0.0149	-0.2544	7.7633	-18.0162	-21.0345
10	11.6179	-1.8224	2.2674	7.8597	-3.7428	7.5238	-0.1626	0.6338	1.1295	-0.6845	-0.0243	-0.0119	-0.15	0.0812	0.1869	0.4435	-0.0764	0.0072	0.4676	0.0496	0.0647	13.8738	-0.7987	-73.942
11	11.9612	-3.2145	-2.4875	11.4063	-0.0681	2.5032	0.1892	1.1875	0.7562	-0.8427	-0.0712	-0.9135	0.0598	0.4497	-0.118	0.1888	-0.0726	0.1356	0.1527	-0.0452	-0.1797	21.7417	-4.491	-64.8486
12	9.7446	-7.1072	1.492	15.5213	-9.2484	12.8611	-0.1256	1.3731	-0.6244	-0.8409	0.6064	0.3151	0.2892	0.1138	-0.4808	0.2431	0.0573	0.0734	0.5977	-0.1662	0.132	28.8823	-16.332	-70.137
13	9.1558	-2.0958	-2.0907	17.8625	0.2843	12.1647	0.1303	0.2613	-0.7129	0.2535	-0.1412	-0.4208	1.1684	0.9074	0.0109	0.1078	0.0731	0.1133	0.1963	-0.208	0.0604	28.4642	-16.8808	-61.6705
14	85.2389	0.691	-26.3552	38.2403	-2.613	10.7529	-0.4422	4.397	0.5748	0.0439	-0.1769	0.8465	-0.6366	0.3461	0.6191	0.4247	-0.0071	0.0282	0.567	0.1142	0.4937	21.8985	-27.6066	-58.8639
15	1.5468	3.1199	0.0451	6.5964	0.5895	2.8911	-0.325	-0.0676	-0.3791	-0.0504	0.0334	-0.876	0.5542	0.2554	0.2916	0.0904	-0.0379	-0.0046	-0.1912	0.0667	0.2485	13.652	-27.3854	-45.6309
16	14.2735	36.6927	10.1233	94.325	26.0237	7.1798	-0.2368	-2.3487	0.5266	1.3113	0.3325	0.6872	0.8964	0.0944	-0.0957	0.2523	-0.0573	-0.2158	0.3321	0.2128	0.4283	24.4074	-20.0157	-35.7567
17	4.6782	-0.5842	0.8813	7.0866	0.3692	4.6743	0.1429	-0.2932	-0.6238	-0.3767	-0.0548	-0.1627	0.2143	-0.3329	-0.0881	-0.1838	-0.0442	0.0287	-0.2272	0.0382	-0.1977	12.7856	-9.1833	-46.8541
18	22.2324	-7.8021	10.9403	23.5901	-3.8809	5.3837	0.6907	0.589	-0.6667	-1.0695	0.0119	-0.3293	0.4913	-0.8428	-0.7026	0.1204	-0.1275	-0.0807	-0.0109	-0.0333	-0.119	0.6004	1.0967	-55.7002
19	4.4776	-0.1919	0.3821	3.492	0.1988	6.4585	0.1428	0.2548	-0.7546	-0.6308	0.0638	-0.708	0.4213	0.3843	-0.2066	-0.0555	-0.0129	0.1158	-0.1838	-0.0683	-0.01	19.8941	-11.6642	-53.5208

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	1425 - 1428	4 - 7
2	X-RAY DIFFRACTION	2	A	A	1429 - 1475	8 - 54
3	X-RAY DIFFRACTION	3	A	A	1476 - 1482	55 - 61
4	X-RAY DIFFRACTION	4	A	A	1483 - 1496	62 - 75
5	X-RAY DIFFRACTION	5	A	A	1503 - 1534	82 - 113
6	X-RAY DIFFRACTION	6	A	A	1535 - 1540	114 - 119
7	X-RAY DIFFRACTION	7	A	A	1541 - 1591	120 - 170
8	X-RAY DIFFRACTION	8	A	A	1593 - 1619	172 - 176
9	X-RAY DIFFRACTION	9	A	A	1620 - 1669	177 - 226
10	X-RAY DIFFRACTION	10	B	B	1425 - 1452	4 - 31
11	X-RAY DIFFRACTION	11	B	B	1453 - 1466	32 - 45
12	X-RAY DIFFRACTION	12	B	B	1467 - 1484	46 - 63
13	X-RAY DIFFRACTION	13	B	B	1485 - 1496	64 - 75
14	X-RAY DIFFRACTION	14	B	B	1497 - 1502	76 - 81
15	X-RAY DIFFRACTION	15	B	B	1503 - 1534	82 - 113
16	X-RAY DIFFRACTION	16	B	B	1535 - 1540	114 - 119
17	X-RAY DIFFRACTION	17	B	B	1541 - 1592	120 - 171
18	X-RAY DIFFRACTION	18	B	B	1593 - 1619	172 - 176
19	X-RAY DIFFRACTION	19	B	B	1620 - 1669	177 - 226

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