PDB-3n25: The structure of muscle pyruvate kinase in complex with proline, ...

ID or keywords:

Entry

Database: PDB / ID: 3n25

Title

The structure of muscle pyruvate kinase in complex with proline, pyruvate, and Mn2+

Components

Pyruvate kinase isozymes M1/M2

Keywords

TRANSFERASE / pyruvate kinase / glycolysis / allosteric regulation

Function / homology

Function and homology information

positive regulation of cytoplasmic translation / pyruvate kinase / pyruvate kinase activity / positive regulation of sprouting angiogenesis / potassium ion binding / rough endoplasmic reticulum / non-specific protein-tyrosine kinase / cellular response to insulin stimulus / protein tyrosine kinase activity / non-specific serine/threonine protein kinase ...
Similarity search - Function

Biological species

Oryctolagus cuniculus (rabbit)

Method

X-RAY DIFFRACTION /

MOLECULAR REPLACEMENT / Resolution: 2.41 Å

Authors

Fenton, A.W. / Johnson, T.A. / Holyoak, T.

Citation

Journal: Protein Sci. / Year: 2010
Title: The pyruvate kinase model system, a cautionary tale for the use of osmolyte perturbations to support conformational equilibria in allostery.
Authors: Fenton, A.W. / Johnson, T.A. / Holyoak, T.

History

Deposition	May 17, 2010	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Jul 28, 2010	Provider: repository / Type: Initial release
Revision 1.1	Jul 13, 2011	Group: Advisory / Refinement description / Version format compliance
Revision 1.2	Nov 8, 2017	Group: Refinement description / Category: software
Revision 1.3	Apr 4, 2018	Group: Data collection / Category: diffrn_source / Item: _diffrn_source.type
Revision 2.0	Nov 15, 2023	Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Derived calculations Category: atom_site / chem_comp_atom ...atom_site / chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / struct_conn / struct_site Item: _atom_site.auth_atom_id / _atom_site.label_atom_id ..._atom_site.auth_atom_id / _atom_site.label_atom_id / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _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_asym_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_asym_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_asym_id / _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_asym_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_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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Download

PDBx/mmCIF format	3n25.cif.gz	795.3 KB	Display	PDBx/mmCIF format
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Validation report

Summary document	3n25_validation.pdf.gz	558.6 KB	Display	wwPDB validaton report
Full document	3n25_full_validation.pdf.gz	597.2 KB	Display
Data in XML	3n25_validation.xml.gz	148.7 KB	Display
Data in CIF	3n25_validation.cif.gz	208.4 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/n2/3n25 ftp://data.pdbj.org/pub/pdb/validation_reports/n2/3n25	HTTPS FTP

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Related structure data

Similar structure data	4b2d-d 3gqy-d 2g50-2 2vgf-d 1a49-2 5x1v-d 1a5u-2 4jpg-d 3srf-1 3srf-2 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	#50 - Feb 2004 Glycolytic Enzymes similarity (13) #205 - Jan 2017 Nuclear Pore Complex similarity (1) #102 - Jun 2008 Lactate Dehydrogenase similarity (1) #263 - Nov 2021 Acetohydroxyacid Synthase similarity (1)

Deposited unit

A: Pyruvate kinase isozymes M1/M2

B: Pyruvate kinase isozymes M1/M2

C: Pyruvate kinase isozymes M1/M2

D: Pyruvate kinase isozymes M1/M2

E: Pyruvate kinase isozymes M1/M2

F: Pyruvate kinase isozymes M1/M2

G: Pyruvate kinase isozymes M1/M2

H: Pyruvate kinase isozymes M1/M2

hetero molecules

470 kDa, 8 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Pyruvate kinase isozymes M1/M2

B: Pyruvate kinase isozymes M1/M2

C: Pyruvate kinase isozymes M1/M2

D: Pyruvate kinase isozymes M1/M2

hetero molecules

defined by author&software
235 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

E: Pyruvate kinase isozymes M1/M2

F: Pyruvate kinase isozymes M1/M2

G: Pyruvate kinase isozymes M1/M2

H: Pyruvate kinase isozymes M1/M2

hetero molecules

defined by author&software
235 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	82.373, 108.747, 144.256
Angle α, β, γ (deg.)	95.18, 93.38, 112.23
Int Tables number	1
Space group name H-M	P1

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Protein , 1 types, 8 molecules ABCDEFGH

#1: Protein	Pyruvate kinase isozymes M1/M2 / Pyruvate kinase muscle isozyme Mass: 58101.984 Da / Num. of mol.: 8 / Source method: isolated from a natural source / Source: (natural) Oryctolagus cuniculus (rabbit) / Tissue: muscle / References: UniProt: P11974, pyruvate kinase

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Non-polymers , 8 types, 1505 molecules

#2: Chemical	ChemComp-PRO / PROLINE Type: L-peptide linking / Mass: 115.130 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C₅H₉NO₂
#3: Chemical	ChemComp-MN / MANGANESE (II) ION Mass: 54.938 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Mn
#4: Chemical	ChemComp-PYR / PYRUVIC ACID Mass: 88.062 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C₃H₄O₃
#5: Chemical	ChemComp-K / POTASSIUM ION Mass: 39.098 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: K
#6: Chemical	ChemComp-NA / SODIUM ION Mass: 22.990 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: Na
#7: Chemical	ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL Mass: 92.094 Da / Num. of mol.: 19 / Source method: obtained synthetically / Formula: C₃H₈O₃
#8: Chemical	ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL Mass: 62.068 Da / Num. of mol.: 15 / Source method: obtained synthetically / Formula: C₂H₆O₂
#9: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 1427 / Source method: isolated from a natural source / Formula: H₂O

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Details

Sequence details	SER401 TO ALA CONFLICT IN UNP ENTRY P11974. RESIDUES 29 AND 404 ARE CONFLICTS BETWEEN WHAT THE ...SER401 TO ALA CONFLICT IN UNP ENTRY P11974. RESIDUES 29 AND 404 ARE CONFLICTS BETWEEN WHAT THE AUTHORS SEE EVIDENCE FOR IN THE ELECTRON DENSITY AND THE DEPOSITED SEQUENCE P11974.

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.55 Å³/Da / Density % sol: 51.77 %
Crystal grow	Temperature: 298 K / Method: hanging drop vapor diffusion / pH: 5.5 Details: 60 mM Succinate (pH 5.5), 5.8 mM sodium pyruvate, 2.4 mM MnCl2, 450 mM KCl, 444 mM Proline and a range of 18 to 20% PEG 8000., hanging drop vapor diffusion, temperature 298K

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Data collection

Diffraction

Mean temperature: 100 K

Diffraction source

Source:

ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.54 Å

Detector

Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Jul 18, 2008

Radiation

Protocol: SINGLE WAVELENGTH / Scattering type: x-ray

Radiation wavelength

Wavelength: 1.54 Å / Relative weight: 1

Reflection

Resolution: 2.4→50 Å / Num. obs: 146924 / % possible obs: 83.6 % / Redundancy: 3.5 % / R_merge(I) obs: 0.123 / Χ²: 1.033 / Net I/σ(I): 8.9

Reflection shell

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Num. unique all	Χ²	Diffraction-ID	% possible all
2.4-2.49	3	0.504	13799	1.097	1	78.8
2.49-2.59	3.3	0.44	15148	1.079	1	86
2.59-2.7	3.4	0.354	14996	1.045	1	85.1
2.7-2.85	3.5	0.283	14849	1.055	1	84.6
2.85-3.02	3.5	0.22	14654	1.01	1	83.2
3.02-3.26	3.5	0.165	14423	1.053	1	82
3.26-3.58	3.5	0.118	14186	1.031	1	80.6
3.58-4.1	3.6	0.088	13816	0.997	1	78.7
4.1-5.17	3.5	0.07	14178	1.039	1	80.5
5.17-50	3.7	0.058	16875	0.964	1	96

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Processing

Software

Name	Version	Classification
DENZO		data reduction
SCALEPACK		data scaling
REFMAC		refinement
PDB_EXTRACT	3.1	data extraction
CrystalClear		data collection
HKL-2000		data reduction
HKL-2000		data scaling
MOLREP		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 2.41→36.59 Å / Cor.coef. F_o:F_c: 0.927 / Cor.coef. F_o:F_c free: 0.874 / WR_factor R_free: 0.271 / WR_factor R_work: 0.209 / Occupancy max: 1 / Occupancy min: 0.38 / FOM work R set: 0.804 / SU B: 21.314 / SU ML: 0.23 / SU R Cruickshank DPI: 1.63 / SU R_free: 0.345 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.346 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES: RESIDUAL ONLY

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.268	7394	5 %	RANDOM
R_work	0.204	-	-	-
obs	0.207	146918	82.98 %	-

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 max: 66.42 Å² / B_iso mean: 5.045 Å² / B_iso min: 2 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	0.56 Å²	0.24 Å²	0.3 Å²
2-	-	-0.36 Å²	0.14 Å²
3-	-	-	0.05 Å²

Refinement step

Cycle: LAST / Resolution: 2.41→36.59 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	31683	0	314	1427	33424

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.009	0.022	33056
X-RAY DIFFRACTION	r_angle_refined_deg	1.125	1.971	44621
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.275	5	4275
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	36.381	23.959	1407
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	15.039	15	6082
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	16.233	15	259
X-RAY DIFFRACTION	r_chiral_restr	0.073	0.2	5085
X-RAY DIFFRACTION	r_gen_planes_refined	0.004	0.021	24518
X-RAY DIFFRACTION	r_mcbond_it	0.269	1.5	20828
X-RAY DIFFRACTION	r_mcangle_it	0.497	2	33623
X-RAY DIFFRACTION	r_scbond_it	0.893	3	12228
X-RAY DIFFRACTION	r_scangle_it	1.482	4.5	10933

LS refinement shell

Resolution: 2.41→2.473 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.392	478	-
R_work	0.301	8680	-
all	-	9158	-
obs	-	-	70.14 %

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	0.4922	-0.1856	0.346	0.6998	-0.1521	0.6422	-0.0134	-0.0464	0.1273	-0.0925	-0.0373	-0.0615	-0.1235	0.0428	0.0507	0.0898	-0.0804	-0.0318	0.3064	-0.0286	0.1931	-9.921	33.286	-6.411
2	1.494	-1.7976	-0.4753	2.2162	0.5459	3.3374	-0.0794	-0.2909	-0.4876	0.1017	0.3079	0.7367	-0.5838	-0.2016	-0.2284	0.1762	-0.0479	0.0477	0.4847	0.0521	0.628	-46.094	34.011	3.962
3	1.3368	-0.3042	-0.4791	1.1975	0.1447	1.8761	-0.0525	0.0316	-0.1923	-0.0893	0.0826	0.5652	0.1526	-0.3429	-0.0302	0.0738	-0.0694	-0.1051	0.3388	-0.0086	0.3994	-38.478	25.216	-5.117
4	0.6206	-0.171	-0.2003	0.9839	-0.1491	0.9471	0.0499	0.0675	0.0142	-0.2201	-0.0471	0.0858	-0.0155	-0.0508	-0.0028	0.1194	-0.0516	-0.0931	0.2779	-0.0402	0.1468	-12.588	21.657	-7.432
5	0.9879	-0.4705	-0.1195	2.524	-0.6885	2.1471	0.0913	0.2508	0.1633	-0.5084	-0.1257	-0.3166	-0.0089	0.06	0.0344	0.2083	-0.0445	0.0323	0.3464	0.0121	0.2633	4.809	27.249	-22.937
6	1.1235	0.2921	-0.8757	1.0112	-0.0218	1.3469	0.0096	0.2149	-0.0021	-0.296	-0.0453	-0.1796	-0.0028	0.0274	0.0358	0.2241	-0.036	-0.0154	0.3741	-0.0147	0.2359	21.899	-14.536	-23.324
7	7.9037	-1.1059	-0.5309	4.4951	-1.0847	0.4333	0.0421	-0.7436	-1.0709	0.1021	-0.377	-0.9396	0.0532	0.4054	0.3349	0.2243	0.0329	-0.066	0.9158	0.2271	1.0496	43.652	-31.919	1.607
8	4.7487	1.0124	-0.7456	0.5235	0.2226	0.6713	0.0034	-0.1604	-0.2267	0.0013	0.0897	-0.2697	-0.0723	0.3069	-0.0931	0.2211	-0.0743	-0.0329	0.5719	-0.0237	0.6204	38.134	-9.599	-9.343
9	0.2109	-0.1874	0.0201	1.0516	0.0468	0.4983	0.0624	0.0164	0.0747	-0.1985	-0.0593	-0.2368	-0.0258	0.0715	-0.0031	0.0923	-0.0693	0.0019	0.3493	-0.034	0.1936	17.518	-8.035	-15.255
10	2.65	-1.7113	0.4754	3.2414	0.1593	3.0884	0.3117	0.5378	0.1655	-0.9249	-0.249	-0.2979	0.0381	0.1537	-0.0626	0.4224	0.0601	0.0804	0.4753	0.0345	0.1705	13.961	7.359	-32.351
11	0.5083	0.2046	-0.4556	0.4856	-0.3575	0.6377	0.0309	-0.0807	0.0598	0.0346	-0.0482	0.1579	-0.0442	-0.0332	0.0173	0.0494	-0.0671	-0.0413	0.3002	-0.057	0.2056	-20.514	14.46	25.104
12	3.6167	-1.5219	2.5216	7.7637	1.4017	4.4514	-0.4111	0.0183	0.7981	-0.2724	-0.0875	0.0277	-1.1404	-0.0589	0.4985	0.4445	-0.1162	-0.1553	0.4167	-0.0684	0.5314	-3.959	47.748	24.473
13	0.9164	-0.2342	0.2927	0.5804	0.4371	1.3514	-0.0238	-0.1604	0.1228	0.1441	-0.0272	-0.0767	-0.1059	0.243	0.0509	0.1314	-0.1235	-0.0844	0.3598	-0.0645	0.1802	-0.996	23.537	29.091
14	0.3319	-0.1758	-0.028	1.1654	-0.0639	0.8556	-0.0141	-0.062	-0.0337	0.051	-0.0353	0.0435	-0.0006	0.0173	0.0495	0.0587	-0.084	-0.0444	0.2821	-0.0499	0.1562	-13.086	8.733	20.137
15	1.2558	-0.1752	-0.9157	1.2744	0.1773	2.4376	-0.0647	-0.1509	-0.2438	0.1142	-0.0068	0.142	0.2766	0.1184	0.0715	0.0927	-0.0904	0.01	0.3087	-0.0338	0.261	-18.238	-10.037	30.516
16	0.6593	0.02	-0.244	2.8971	-0.2324	0.7118	-0.0071	-0.0664	-0.0719	0.4284	0.0237	0.0281	0.0526	0.1444	-0.0166	0.1296	-0.0482	-0.0746	0.3832	-0.0309	0.171	9.384	-32.903	6.476
17	3.5569	-0.2261	-1.648	2.6271	-0.1693	2.5219	0.2262	0.3139	-0.0698	-0.6856	-0.2452	-0.0047	-0.0975	-0.0808	0.019	0.3641	-0.0184	-0.1252	0.4158	-0.0901	0.2235	5.932	-45.139	-29.039
18	0.8461	-0.2978	-0.0637	1.9914	0.1533	0.5694	0.0032	0.0494	-0.1564	-0.1393	-0.0422	0.2061	0.0675	-0.0003	0.039	0.0788	-0.0483	-0.0728	0.2994	-0.045	0.1431	1.14	-32.43	-5.871
19	0.8304	-0.8944	-0.769	1.6377	0.3754	1.0207	-0.0128	0.0187	-0.1069	-0.0536	-0.0674	0.1631	0.0607	0.0319	0.0801	0.06	-0.0735	-0.0624	0.3192	-0.0245	0.1708	-4.433	-20.894	11.582
20	3.1547	-1.3916	-0.6633	2.6026	-0.0013	1.4384	-0.098	-0.1402	-0.2415	0.5637	-0.0325	0.0958	0.3451	0.0885	0.1305	0.2913	-0.0333	-0.0128	0.4096	-0.0096	0.2194	-2.801	-26.216	25.424
21	0.3928	-0.0618	0.3769	2.794	-0.2412	0.9814	-0.0378	0.1131	0.0502	-0.3442	0.0917	-0.1233	-0.1049	0.1701	-0.0539	0.1262	-0.1488	-0.0275	0.3638	-0.0346	0.2092	-30.997	48.561	58.755
22	0.4976	0.461	0.5291	1.576	0.6347	1.3143	-0.0449	-0.0973	0.0881	0.1898	-0.0148	-0.0746	-0.0399	0.2118	0.0596	0.2411	-0.1121	-0.077	0.3938	-0.0443	0.2197	-34.03	64.229	86.34
23	1.2308	0.694	0.9337	1.297	0.4298	1.7095	0.1485	-0.2732	0.1272	0.3784	-0.132	0.0611	0.006	-0.1434	-0.0165	0.1973	-0.1553	-0.0144	0.3225	-0.0752	0.2537	-41.345	60.069	87.31
24	0.3869	0.3081	0.2281	1.4349	0.395	0.8288	-0.0156	0.0089	0.0429	0.0273	-0.0016	0.0522	-0.0087	-0.0184	0.0172	0.0861	-0.1225	-0.0623	0.2923	-0.0185	0.1537	-40.616	43.175	64.888
25	1.3096	1.6385	0.1273	3.4938	-0.4037	0.3618	-0.2774	0.1702	0.1224	-0.4246	0.1736	0.051	-0.1545	0.0774	0.1038	0.2696	-0.1445	-0.11	0.4321	-0.0134	0.1837	-43.724	42.653	40.827
26	4.2507	-0.7432	5.6611	2.396	-3.3391	9.9965	-0.1888	-0.2988	0.7612	0.1961	-0.097	0.5335	-0.4288	-0.1751	0.2859	0.1565	-0.1153	-0.0524	0.3653	-0.1201	0.4698	-58.902	15.44	63.292
27	0.6909	0.1289	0.2007	0.4739	-0.2611	0.4975	-0.0276	0.1738	-0.0314	-0.0941	-0.0483	0.1223	0.065	-0.0391	0.0759	0.08	-0.1021	-0.0617	0.3305	-0.0547	0.1957	-61.142	-2.311	36.472
28	6.4746	2.2538	-2.1677	7.7125	0.923	2.8653	-0.4432	0.2349	-0.958	0.5739	-0.0965	-0.0581	1.2949	0.03	0.5397	0.7092	-0.0652	0.1012	0.4244	-0.1034	0.5233	-44.491	-31.178	41.807
29	0.6351	0.0275	-0.0091	0.4643	0.0397	0.7646	-0.0054	0.0621	-0.0421	-0.0388	-0.01	-0.0563	0.0301	0.0602	0.0155	0.0818	-0.0835	-0.0664	0.2972	-0.0445	0.1599	-48.787	-1.523	42.659
30	0.7671	0.5697	0.695	1.3246	0.4348	0.9448	-0.0458	0.1412	0.088	-0.2241	-0.029	0.0321	-0.0992	0.0808	0.0747	0.1663	-0.0735	-0.0947	0.3246	0.0001	0.1982	-56.505	21.499	37.288
31	1.204	-0.2107	0.4588	1.7477	-0.0828	1.2826	0.1411	-0.2356	0.0184	0.5648	-0.1073	-0.4475	-0.0346	0.0646	-0.0338	0.3408	-0.1625	-0.2526	0.3508	-0.0129	0.2652	-19.691	31.226	89.309
32	5.653	-1.0192	4.4934	4.1636	-1.5624	5.0625	-0.1135	0.9028	0.7448	0.6215	-0.513	-0.6772	-0.2565	0.817	0.6265	0.2002	-0.1778	-0.0178	0.8473	0.0801	1.0858	5.524	48.367	66.095
33	3.1547	0.2967	0.5778	2.6131	-2.5026	4.1173	-0.1767	0.5472	0.5524	0.0669	0.049	-0.8618	0.0262	0.6084	0.1277	0.1215	-0.1752	-0.1937	0.6876	-0.0768	0.9843	-0.838	39.028	70.803
34	0.7069	0.6101	0.0631	1.7635	-0.1285	0.3953	0.1141	0.0122	-0.1663	0.3385	-0.1098	-0.5846	0.028	0.0703	-0.0043	0.1754	-0.0992	-0.2116	0.3871	-0.0329	0.3524	-20.284	24.445	79.699
35	1.043	0.0938	0.2167	4.8985	-2.106	2.1921	0.1129	-0.3686	-0.1093	1.0288	-0.1547	-0.4265	0.074	0.0745	0.0418	0.6593	-0.1953	-0.3367	0.4897	0.0208	0.3198	-27.884	9.843	98.074
36	0.8953	1.0968	-0.4809	3.322	-1.0878	1.7192	0.0496	0.017	-0.2269	0.1228	-0.0868	-0.2911	0.0584	0.0904	0.0372	0.0697	-0.0574	-0.0927	0.3238	-0.0302	0.1955	-45.83	-11.318	66.432
37	2.0372	0.8581	0.6141	1.5302	-0.2437	1.1589	0.1042	0.2002	-0.0241	0.0453	0.1137	0.5734	0.0371	-0.0849	-0.2179	0.1251	-0.1422	-0.027	0.3381	-0.0309	0.3473	-77.379	-17.131	67.4
38	1.5111	0.4268	0.1972	2.1567	-0.0796	1.6894	-0.018	-0.0382	0.1513	0.265	0.0952	0.4759	0.0509	-0.3136	-0.0772	0.1376	-0.1577	0.0333	0.3349	-0.0013	0.3695	-77.749	-11.147	72.545
39	0.5324	0.3956	0.23	1.0557	0.0024	0.4058	0.082	-0.0536	-0.0144	0.2362	-0.0485	0.0315	0.0491	0.0238	-0.0335	0.1422	-0.1152	-0.0633	0.3002	-0.0168	0.1619	-54.78	-4.899	73.812
40	1.5397	-0.1758	-0.0547	3.6836	-0.0079	4.5468	0.1393	-0.2249	-0.228	0.801	-0.1477	-0.4088	0.2286	0.1688	0.0084	0.3651	-0.1965	-0.2754	0.4032	0.0513	0.3418	-35.957	-10.91	89.535

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	12 - 112
2	X-RAY DIFFRACTION	2	A	113 - 161
3	X-RAY DIFFRACTION	3	A	162 - 256
4	X-RAY DIFFRACTION	4	A	257 - 464
5	X-RAY DIFFRACTION	5	A	465 - 530
6	X-RAY DIFFRACTION	6	B	11 - 122
7	X-RAY DIFFRACTION	7	B	132 - 200
8	X-RAY DIFFRACTION	8	B	201 - 283
9	X-RAY DIFFRACTION	9	B	284 - 465
10	X-RAY DIFFRACTION	10	B	466 - 530
11	X-RAY DIFFRACTION	11	C	12 - 114
12	X-RAY DIFFRACTION	12	C	115 - 207
13	X-RAY DIFFRACTION	13	C	208 - 309
14	X-RAY DIFFRACTION	14	C	310 - 472
15	X-RAY DIFFRACTION	15	C	473 - 530
16	X-RAY DIFFRACTION	16	D	10 - 113
17	X-RAY DIFFRACTION	17	D	114 - 214
18	X-RAY DIFFRACTION	18	D	215 - 390
19	X-RAY DIFFRACTION	19	D	391 - 466
20	X-RAY DIFFRACTION	20	D	467 - 530
21	X-RAY DIFFRACTION	21	E	10 - 104
22	X-RAY DIFFRACTION	22	E	105 - 148
23	X-RAY DIFFRACTION	23	E	149 - 249
24	X-RAY DIFFRACTION	24	E	250 - 464
25	X-RAY DIFFRACTION	25	E	465 - 530
26	X-RAY DIFFRACTION	26	F	11 - 26
27	X-RAY DIFFRACTION	27	F	27 - 124
28	X-RAY DIFFRACTION	28	F	128 - 215
29	X-RAY DIFFRACTION	29	F	216 - 413
30	X-RAY DIFFRACTION	30	F	414 - 530
31	X-RAY DIFFRACTION	31	G	11 - 122
32	X-RAY DIFFRACTION	32	G	130 - 170
33	X-RAY DIFFRACTION	33	G	171 - 238
34	X-RAY DIFFRACTION	34	G	239 - 464
35	X-RAY DIFFRACTION	35	G	465 - 530
36	X-RAY DIFFRACTION	36	H	11 - 73
37	X-RAY DIFFRACTION	37	H	74 - 188
38	X-RAY DIFFRACTION	38	H	190 - 248
39	X-RAY DIFFRACTION	39	H	249 - 468
40	X-RAY DIFFRACTION	40	H	469 - 530

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