PDB-2eph: Crystal structure of fructose-bisphosphate aldolase from Plasmodi...

ID or keywords:

Entry

Database: PDB / ID: 2eph

Title

Crystal structure of fructose-bisphosphate aldolase from Plasmodium falciparum in complex with TRAP-tail determined at 2.7 angstrom resolution

Components

Fructose-bisphosphate aldolase
PbTRAP

Keywords

LYASE / Aldolase / Invasion machinery / Plasmodium falciparum / Structural Genomics / PSI / Protein Structure Initiative / Structural Genomics of Pathogenic Protozoa Consortium / SGPP

Function / homology

Function and homology information

fructose-bisphosphate aldolase / fructose-bisphosphate aldolase activity / fructose 1,6-bisphosphate metabolic process / glycolytic process / actin binding / host cell plasma membrane / membrane / plasma membrane / cytosol / cytoplasm
Similarity search - Function

Biological species

Plasmodium falciparum (malaria parasite P. falciparum)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.7 Å

Authors

Bosch, J. / Buscaglia, C.A. / Krumm, B. / Cardozo, T. / Nussenzweig, V. / Hol, W.G.J. / Structural Genomics of Pathogenic Protozoa Consortium (SGPP)

Citation

Journal: Proc.Natl.Acad.Sci.Usa / Year: 2007
Title: Aldolase provides an unusual binding site for thrombospondin-related anonymous protein in the invasion machinery of the malaria parasite.
Authors: Bosch, J. / Buscaglia, C.A. / Krumm, B. / Ingason, B.P. / Lucas, R. / Roach, C. / Cardozo, T. / Nussenzweig, V. / Hol, W.G.

History

Deposition	Mar 30, 2007	Deposition site: PDBJ / Processing site: RCSB
Revision 1.0	Apr 17, 2007	Provider: repository / Type: Initial release
Revision 1.1	Apr 30, 2008	Group: Version format compliance
Revision 1.2	Jul 13, 2011	Group: Advisory / Version format compliance
Revision 1.3	Aug 23, 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.end_auth_comp_id

Structure viewer	Molecule: MolmilJmol/JSmol

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Validation report

Summary document	2eph_validation.pdf.gz	464.6 KB	Display	wwPDB validaton report
Full document	2eph_full_validation.pdf.gz	497.9 KB	Display
Data in XML	2eph_validation.xml.gz	53.6 KB	Display
Data in CIF	2eph_validation.cif.gz	74.9 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/ep/2eph ftp://data.pdbj.org/pub/pdb/validation_reports/ep/2eph	HTTPS FTP

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Related structure data

Related structure data	2pc4C 1a5cS S: Starting model for refinement C: citing same article (ref.)
Similar structure data	2pc4-d 6dzl-d 1fdj-1 7k48-d 4tu1-d 3one-1 3e0d-2 3onf-1 Search similar-shape structures by Omokage search (details) Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search
Other databases	TargetDB: Pfal007081AAA

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#50 - Feb 2004 Glycolytic Enzymes similarity (5) #134 - Feb 2011 Integrin similarity (5) #55 - Jul 2004 DNA Ligase similarity (3) #166 - Oct 2013 Proteasome similarity (3)

Deposited unit

A: Fructose-bisphosphate aldolase

B: Fructose-bisphosphate aldolase

C: Fructose-bisphosphate aldolase

D: Fructose-bisphosphate aldolase

H: PbTRAP

161 kDa, 5 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

Idetical with deposited unit
defined by author

Unit cell

Length a, b, c (Å)	70.019, 146.162, 148.961
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:
NCS domain segments:

Ens-ID: 1 / Refine code: 3

Dom-ID	Component-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	ASP	ASP	GLN	GLN	A	A	16 - 30	17 - 31
2	1	ASP	ASP	GLN	GLN	B	B	16 - 30	17 - 31
3	1	ASP	ASP	GLN	GLN	C	C	16 - 30	17 - 31
4	1	ASP	ASP	GLN	GLN	D	D	16 - 30	17 - 31
5	2	GLY	GLY	ALA	ALA	A	A	32 - 37	33 - 38
6	2	GLY	GLY	ALA	ALA	B	B	32 - 37	33 - 38
7	2	GLY	GLY	ALA	ALA	C	C	32 - 37	33 - 38
8	2	GLY	GLY	ALA	ALA	D	D	32 - 37	33 - 38
9	3	THR	THR	THR	THR	A	A	57 - 71	58 - 72
10	3	THR	THR	THR	THR	B	B	57 - 71	58 - 72
11	3	THR	THR	THR	THR	C	C	57 - 71	58 - 72
12	3	THR	THR	THR	THR	D	D	57 - 71	58 - 72
13	4	LYS	LYS	ALA	ALA	A	A	76 - 81	77 - 82
14	4	LYS	LYS	ALA	ALA	B	B	76 - 81	77 - 82
15	4	LYS	LYS	ALA	ALA	C	C	76 - 81	77 - 82
16	4	LYS	LYS	ALA	ALA	D	D	76 - 81	77 - 82
17	5	GLU	GLU	LEU	LEU	A	A	85 - 88	86 - 89
18	5	GLU	GLU	LEU	LEU	B	B	85 - 88	86 - 89
19	5	GLU	GLU	LEU	LEU	C	C	85 - 88	86 - 89
20	5	GLU	GLU	LEU	LEU	D	D	85 - 88	86 - 89
21	6	ILE	ILE	ASP	ASP	A	A	108 - 159	109 - 160
22	6	ILE	ILE	ASP	ASP	B	B	108 - 159	109 - 160
23	6	ILE	ILE	ASP	ASP	C	C	108 - 159	109 - 160
24	6	ILE	ILE	ASP	ASP	D	D	108 - 159	109 - 160
25	7	SER	SER	TYR	TYR	A	A	169 - 180	170 - 181
26	7	SER	SER	TYR	TYR	B	B	169 - 180	170 - 181
27	7	SER	SER	TYR	TYR	C	C	169 - 180	170 - 181
28	7	SER	SER	TYR	TYR	D	D	169 - 180	170 - 181
29	8	GLN	GLN	GLY	GLY	A	A	185 - 201	186 - 202
30	8	GLN	GLN	GLY	GLY	B	B	185 - 201	186 - 202
31	8	GLN	GLN	GLY	GLY	C	C	185 - 201	186 - 202
32	8	GLN	GLN	GLY	GLY	D	D	185 - 201	186 - 202
33	9	HIS	HIS	ALA	ALA	A	A	203 - 222	204 - 223
34	9	HIS	HIS	ALA	ALA	B	B	203 - 222	204 - 223
35	9	HIS	HIS	ALA	ALA	C	C	203 - 222	204 - 223
36	9	HIS	HIS	ALA	ALA	D	D	203 - 222	204 - 223
37	10	ASN	ASN	THR	THR	A	A	226 - 241	227 - 242
38	10	ASN	ASN	THR	THR	B	B	226 - 241	227 - 242
39	10	ASN	ASN	THR	THR	C	C	226 - 241	227 - 242
40	10	ASN	ASN	THR	THR	D	D	226 - 241	227 - 242
41	11	GLY	GLY	PHE	PHE	A	A	256 - 276	257 - 277
42	11	GLY	GLY	PHE	PHE	B	B	256 - 276	257 - 277
43	11	GLY	GLY	PHE	PHE	C	C	256 - 276	257 - 277
44	11	GLY	GLY	PHE	PHE	D	D	256 - 276	257 - 277
45	12	ALA	ALA	ALA	ALA	A	A	286 - 295	287 - 296
46	12	ALA	ALA	ALA	ALA	B	B	286 - 295	287 - 296
47	12	ALA	ALA	ALA	ALA	C	C	286 - 295	287 - 296
48	12	ALA	ALA	ALA	ALA	D	D	286 - 295	287 - 296
49	13	PRO	PRO	TYR	TYR	A	A	300 - 307	301 - 308
50	13	PRO	PRO	TYR	TYR	B	B	300 - 307	301 - 308
51	13	PRO	PRO	TYR	TYR	C	C	300 - 307	301 - 308
52	13	PRO	PRO	TYR	TYR	D	D	300 - 307	301 - 308
53	14	ALA	ALA	ALA	ALA	A	A	310 - 313	311 - 314
54	14	ALA	ALA	ALA	ALA	B	B	310 - 313	311 - 314
55	14	ALA	ALA	ALA	ALA	C	C	310 - 313	311 - 314
56	14	ALA	ALA	ALA	ALA	D	D	310 - 313	311 - 314
57	15	GLN	GLN	LEU	LEU	A	A	335 - 342	336 - 343
58	15	GLN	GLN	LEU	LEU	B	B	335 - 342	336 - 343
59	15	GLN	GLN	LEU	LEU	C	C	335 - 342	336 - 343
60	15	GLN	GLN	LEU	LEU	D	D	335 - 342	336 - 343

#1: Protein	Fructose-bisphosphate aldolase / 41 kDa antigen Mass: 40152.906 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Plasmodium falciparum (malaria parasite P. falciparum) Plasmid: pET14B / Production host: Escherichia coli (E. coli) / Strain (production host): BL21STAR(DE3) / References: UniProt: P14223, fructose-bisphosphate aldolase
#2: Protein/peptide	PbTRAP Mass: 791.720 Da / Num. of mol.: 1 / Fragment: C-terminus: Residues 601-606 / Source method: obtained synthetically Details: Synthetic peptide with the sequence based on PbTRAP protein from Plasmodium berghei, UNP entry P90573, P90573_PLABE, residues 601-606 References: UniProt: P90573
#3: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 336 / 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: 2.36 Å³/Da / Density % sol: 47.89 %
Crystal grow	Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 6 Details: 2.5 mM TRAP-tail, 0.5% n-dodecyl-beta-D-maltoside, 50 mM cacodylic acid pH 6.0, 20% PEG 2000, VAPOR DIFFUSION, SITTING DROP, temperature 298K

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: ALS / Beamline: 8.2.2 / Wavelength: 0.9796 Å
Detector	Type: ADSC QUANTUM 210 / Detector: CCD / Date: Dec 16, 2005
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9796 Å / Relative weight: 1
Reflection	Resolution: 2.68→19.97 Å / Num. all: 40459 / Num. obs: 40459 / % possible obs: 98.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.3 % / B_iso Wilson estimate: 65.2 Å² / R_sym value: 0.07 / Net I/σ(I): 12.4
Reflection shell	Resolution: 2.68→2.822 Å / Redundancy: 2.3 % / Mean I/σ(I) obs: 2.8 / R_sym value: 0.55 / % possible all: 90.49

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Processing

Software

Name	Version	Classification
REFMAC	5.2.0019	refinement
ADSC	QUANTUM	data collection
MOSFLM		data reduction
CCP4	(SCALA)	data scaling
MOLREP		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB entry 1A5C

1a5c

Resolution: 2.7→19.97 Å / Cor.coef. F_o:F_c: 0.955 / Cor.coef. F_o:F_c free: 0.924 / SU B: 30.585 / SU ML: 0.295 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.369 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.2504	2117	5.1 %	RANDOM
R_work	0.19154	-	-	-
obs	0.19445	39693	98 %	-
all	-	39693	-	-

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK

Displacement parameters

B_iso mean: 59.195 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	8.36 Å²	0 Å²	0 Å²
2-	-	-2.21 Å²	0 Å²
3-	-	-	-6.15 Å²

Refinement step

Cycle: LAST / Resolution: 2.7→19.97 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	10887	0	0	336	11223

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.008	0.022	11091
X-RAY DIFFRACTION	r_bond_other_d	0.001	0.02	7504
X-RAY DIFFRACTION	r_angle_refined_deg	1.048	1.973	15031
X-RAY DIFFRACTION	r_angle_other_deg	0.877	3	18455
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.375	5	1424
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	40.771	25.066	456
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	16.503	15	1962
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	14.075	15	56
X-RAY DIFFRACTION	r_chiral_restr	0.075	0.2	1741
X-RAY DIFFRACTION	r_gen_planes_refined	0.003	0.02	12307
X-RAY DIFFRACTION	r_gen_planes_other	0.001	0.02	2060
X-RAY DIFFRACTION	r_nbd_refined	0.195	0.2	2866
X-RAY DIFFRACTION	r_nbd_other	0.175	0.2	7900
X-RAY DIFFRACTION	r_nbtor_refined	0.172	0.2	5530
X-RAY DIFFRACTION	r_nbtor_other	0.083	0.2	5858
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.157	0.2	401
X-RAY DIFFRACTION	r_xyhbond_nbd_other	0.098	0.2	3
X-RAY DIFFRACTION	r_metal_ion_refined
X-RAY DIFFRACTION	r_metal_ion_other
X-RAY DIFFRACTION	r_symmetry_vdw_refined	0.164	0.2	28
X-RAY DIFFRACTION	r_symmetry_vdw_other	0.196	0.2	104
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.135	0.2	11
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	1.219	4	9155
X-RAY DIFFRACTION	r_mcbond_other	0.169	4	2903
X-RAY DIFFRACTION	r_mcangle_it	1.654	6	11352
X-RAY DIFFRACTION	r_scbond_it	2.205	6	4672
X-RAY DIFFRACTION	r_scangle_it	3.33	10	3676
X-RAY DIFFRACTION	r_rigid_bond_restr
X-RAY DIFFRACTION	r_sphericity_free
X-RAY DIFFRACTION	r_sphericity_bonded

Refine LS restraints NCS

Ens-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Dom-ID	Auth asym-ID	Number	Type	Rms dev position (Å)	Weight position
1	A	1256	tight positional	0.02	0.05
2	B	1256	tight positional	0.02	0.05
3	C	1256	tight positional	0.02	0.05
4	D	1256	tight positional	0.02	0.05
1	A	1484	loose positional	0.22	5
2	B	1484	loose positional	0.24	5
3	C	1484	loose positional	0.23	5
4	D	1484	loose positional	0.23	5
1	A	1256	tight thermal	0.04	0.5
2	B	1256	tight thermal	0.04	0.5
3	C	1256	tight thermal	0.05	0.5
4	D	1256	tight thermal	0.05	0.5
1	A	1484	loose thermal	1.27	10
2	B	1484	loose thermal	1.29	10
3	C	1484	loose thermal	1.47	10
4	D	1484	loose thermal	1.42	10

LS refinement shell

Resolution: 2.7→2.82 Å / Total num. of bins used: 5

	R_factor	Num. reflection	% reflection
R_free	0.347	557	-
R_work	0.284	10553	-
obs	-	-	94.44 %

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	3.192	0.831	-2.479	2.7914	3.7184	9.32	-0.1257	0.0653	0.0797	0.7174	0.3429	-0.8001	0.2326	1.1775	-0.2172	-0.1778	-0.1367	-0.0601	0.1066	0.0021	0.0582	7.3687	10.9237	-13.4095
2	2.2145	-3.7121	1.8947	10.1517	-5.1889	6.4923	-0.1529	-0.0098	0.6455	0.2465	-0.0968	-0.2648	-1.1468	-0.4263	0.2497	0.0994	-0.0129	0.1593	-0.1551	-0.0101	-0.0687	-17.4536	33.8103	-12.094
3	3.9404	0.2023	-0.2081	3.7085	-1.0514	4.1389	0.1159	0.0605	0.4244	-0.1784	0.0852	0.2327	-1.2235	0.1977	-0.2011	0.3885	-0.06	0.1006	-0.3565	-0.043	-0.1394	-11.7239	37.7964	-9.0825
4	0.8691	1.0792	0.2478	3.245	0.8768	2.8184	0.0209	0.0617	0.1925	-0.3558	-0.0186	0.0579	-0.9302	0.1528	-0.0023	0.0445	-0.0495	0.0859	-0.1614	-0.0061	-0.0299	-9.7955	25.5985	-19.2659
5	2.2318	0.4892	-0.2647	2.3589	-0.3765	3.4544	0.1306	-0.0272	-0.0416	-0.0481	-0.0306	0.0215	-0.4541	-0.0463	-0.1	-0.2927	-0.0045	0.0458	-0.164	-0.023	-0.091	-12.6627	12.6096	-16.2391
6	1.5607	1.9184	1.8967	5.3244	-1.3585	6.8943	0.3831	-0.2119	-0.3041	0.1975	-0.3206	0.8671	-0.4245	-1.3832	-0.0625	-0.2084	0.0319	0.1212	0.0084	-0.0652	-0.0873	-25.4623	8.5513	-5.0585
7	1.2173	0.0305	-0.3514	4.043	1.1132	1.6867	0.1556	-0.2045	0.4176	-0.0324	-0.1078	0.2986	-0.709	-0.3424	-0.0478	-0.0089	0.0659	0.1029	-0.1153	-0.0287	-0.1062	-19.2669	26.5133	-1.5851
8	22.1349	8.2529	3.1584	18.5194	1.927	0.487	0.8835	-0.1444	-0.813	0.9909	-1.2427	-0.8194	-1.7374	0.6852	0.3592	0.0207	-0.0116	-0.0524	0.0146	0.0513	0.1991	-37.3028	16.6542	21.7964
9	4.1625	-0.2577	-2.1783	0.9117	0.8666	6.2376	-0.2262	0.3078	0.1086	-0.9202	0.0741	0.482	0.0094	-0.8171	0.1522	0.1238	0.0395	-0.0731	-0.1664	0.0282	-0.0733	-17.1639	8.7548	-48.1805
10	0.7616	-0.5801	2.1534	1.7329	0.0225	8.2305	0.4569	-0.7358	0.9892	0.5045	-0.2897	-0.3884	-0.5291	1.3535	-0.1671	0.4547	-0.5065	0.2474	0.3268	0.0001	0.2221	13.5558	26.2592	-49.6459
11	3.6667	-0.6043	-0.2627	1.9698	-1.2341	0.8913	-0.0437	-0.0783	0.55	-0.4618	0.051	0.0416	-0.8734	0.4586	-0.0072	0.848	-0.4022	0.2841	-0.1268	-0.0035	-0.1989	2.0682	24.6878	-57.4896
12	0.3578	-0.1485	0.3648	2.152	-0.0507	3.3079	-0.0128	0.0007	0.0152	-0.4275	0.1388	-0.1642	-0.7108	0.4176	-0.1261	-0.0245	-0.1473	0.1233	-0.0818	-0.0223	-0.0658	-2.4863	12.4022	-41.9505
13	4.0533	0.499	-0.1644	2.8846	0.0178	3.6181	0.2483	-0.2185	-0.1768	-0.4309	-0.1153	-0.4989	-0.2987	1.0146	-0.133	-0.0874	-0.1443	0.1518	0.0626	-0.0727	-0.1352	6.3755	-1.3872	-49.2442
14	5.2662	-0.0782	-1.2705	0.8234	-1.2903	2.3909	0.0316	0.2098	-0.0427	-0.4047	-0.0394	-0.2576	-0.5903	0.9004	0.0078	0.2311	-0.2237	0.2105	-0.0022	-0.0682	-0.1709	3.7723	3.2039	-56.0916
15	7.9358	7.9307	4.103	7.9257	4.1003	2.1213	0.4404	0.3863	0.6333	-1.1855	-0.8242	-0.5583	0.3785	0.5532	0.3838	0.8067	-0.3811	0.4288	0.4236	0.0146	0.1438	12.7678	24.2479	-64.9806
16	3.5172	4.0723	-1.1418	14.0279	3.233	3.4466	0.4506	0.4093	0.2084	-0.0614	-0.0051	-0.2765	-0.1187	1.1702	-0.4455	0.3176	-0.2171	0.2393	0.1485	-0.0212	-0.2157	6.6328	4.2433	-65.3525
17	70.4486	-86.5675	18.4859	112.3436	-14.8547	15.2029	1.3632	-0.2346	-1.88	-0.6421	-0.5717	-1.664	0.978	2.1566	-0.7915	0.1584	-0.0141	0.3079	0.4356	-0.1689	0.3196	14.0712	-8.0779	-31.4778
18	2.2657	0.4711	0.4995	1.3363	1.333	4.0798	0.02	0.2238	-0.3961	-0.4918	0.403	-0.5484	0.5189	0.9547	-0.423	0.0273	0.116	-0.0132	-0.1015	-0.0233	0.0212	-3.3556	-21.6084	-43.2812
19	20.565	4.4528	-4.2478	3.7653	-2.1612	1.4276	-0.1772	-0.6456	0.2038	0.394	0.3208	0.429	0.7259	-0.7876	-0.1436	0.5617	-0.4818	0.1034	0.1165	-0.0122	-0.0049	-32.1135	-35.8875	-34.8964
20	2.8852	-0.5936	1.6862	5.6252	-0.5534	0.9932	0.1565	-0.3293	-0.3621	0.2291	-0.1339	0.3525	1.3651	-0.1328	-0.0225	0.557	-0.2849	-0.1765	-0.2308	-0.007	-0.1299	-21.5553	-37.904	-43.0924
21	1.0235	-0.2673	0.2474	2.6668	1.0583	2.9911	0.0948	0.0309	-0.0731	0.2446	-0.0478	0.06	1.0517	-0.3108	-0.047	0.0359	-0.1687	-0.0569	-0.144	0.0414	-0.0818	-16.6055	-26.6702	-32.8734
22	2.8873	-0.5324	1.3087	2.0273	-0.4095	3.8784	0.2193	-0.2227	0.0188	-0.2159	-0.0631	-0.0269	0.4648	-0.1699	-0.1562	-0.2813	-0.0705	-0.0279	-0.1377	0.0178	-0.113	-15.5054	-13.3609	-35.784
23	0.9271	0.43	0.0049	4.3633	0.2677	1.9123	0.0914	-0.0153	0.0056	-0.282	-0.1235	0.5886	0.466	-0.5927	0.0321	-0.0342	-0.1604	-0.1089	-0.0612	0.0068	-0.1401	-26.0403	-20.6948	-49.7833
24	6.9513	-1.3969	8.3177	8.0995	-8.0707	18.8022	0.311	-0.8498	0.1565	0.4342	-0.254	0.2471	-0.4263	-1.0404	-0.057	0.4908	0.0603	-0.0646	0.5609	-0.0717	0.7279	-39.0269	-11.8467	-70.1708
25	1.0361	-0.5483	0.5124	2.3533	-0.4502	3.236	-0.0541	-0.0165	-0.0664	0.3297	0.015	0.0612	0.4538	-0.209	0.0392	-0.0699	-0.0864	0.0394	-0.2008	-0.0042	-0.1016	-10.6665	-17.5181	-3.116
26	2.7336	-1.7567	0.2163	5.7234	-0.5124	2.1122	-0.0537	-0.109	-0.4739	0.7885	0.0813	0.1127	0.9477	-0.1005	-0.0276	0.2232	-0.0018	-0.0618	-0.253	0.0334	-0.2652	-6.4647	-30.1519	5.9122
27	20.0807	18.9281	1.3459	18.0289	0.0941	7.4613	0.2349	-0.5485	0.0645	1.6252	-0.4814	-0.24	1.4298	-1.3032	0.2465	0.4699	0.0268	0.0378	0.034	0.0982	0.0011	-13.7029	-27.8541	10.3449
28	1.5742	0.4322	-1.0179	1.5372	-0.282	3.9253	-0.183	-0.0347	-0.1104	0.0112	0.1348	-0.1046	0.933	0.2971	0.0482	-0.1699	0.0342	-0.0137	-0.1697	-0.0109	-0.0477	-6.2717	-19.4021	-13.1635
29	1.1605	-0.1565	-1.0192	2.8026	-0.3505	3.2981	0.061	0.1227	0.063	0.2536	0.0971	-0.0642	0.3384	0.2398	-0.1581	-0.3536	-0.0146	-0.0373	-0.134	-0.0275	-0.083	-5.5643	-9.0369	-11.5562
30	1.5283	-4.6558	1.7237	16.2867	0.6148	18.3045	0.2153	0.1427	0.6201	0.1163	1.5657	-1.4724	0.7309	2.8495	-1.781	-0.2217	-0.049	-0.1724	0.5636	-0.2931	0.2426	16.953	-6.0714	-3.6518
31	1.5299	0.143	-0.3732	3.5953	-1.1066	1.3675	-0.019	-0.1857	0.061	0.3881	-0.0729	-0.5696	0.4975	0.4432	0.0919	-0.0892	0.0958	-0.127	-0.0753	-0.079	-0.1655	2.3979	-13.0628	4.4201
32	9.4671	-2.662	-2.4721	8.8837	7.9714	9.6452	0.3262	-0.5398	0.4333	0.9381	-0.501	-1.1834	0.0326	1.3914	0.1749	0.2158	-0.0525	-0.2323	-0.0444	0.0397	-0.1482	4.5556	-9.7347	13.5099

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	4 - 26	5 - 27
2	X-RAY DIFFRACTION	2	A	A	27 - 55	28 - 56
3	X-RAY DIFFRACTION	3	A	A	56 - 88	57 - 89
4	X-RAY DIFFRACTION	4	A	A	89 - 168	90 - 169
5	X-RAY DIFFRACTION	5	A	A	169 - 244	170 - 245
6	X-RAY DIFFRACTION	6	A	A	245 - 267	246 - 268
7	X-RAY DIFFRACTION	7	A	A	268 - 348	269 - 349
8	X-RAY DIFFRACTION	8	A	A	349 - 365	350 - 366
9	X-RAY DIFFRACTION	9	B	B	3 - 38	4 - 39
10	X-RAY DIFFRACTION	10	B	B	39 - 55	40 - 56
11	X-RAY DIFFRACTION	11	B	B	56 - 89	57 - 90
12	X-RAY DIFFRACTION	12	B	B	90 - 242	91 - 243
13	X-RAY DIFFRACTION	13	B	B	243 - 285	244 - 286
14	X-RAY DIFFRACTION	14	B	B	286 - 313	287 - 314
15	X-RAY DIFFRACTION	15	B	B	314 - 334	315 - 335
16	X-RAY DIFFRACTION	16	B	B	335 - 351	336 - 352
17	X-RAY DIFFRACTION	17	C	C	2 - 6	3 - 7
18	X-RAY DIFFRACTION	18	C	C	7 - 37	8 - 38
19	X-RAY DIFFRACTION	19	C	C	38 - 55	39 - 56
20	X-RAY DIFFRACTION	20	C	C	56 - 88	57 - 89
21	X-RAY DIFFRACTION	21	C	C	89 - 168	90 - 169
22	X-RAY DIFFRACTION	22	C	C	169 - 243	170 - 244
23	X-RAY DIFFRACTION	23	C	C	244 - 348	245 - 349
24	X-RAY DIFFRACTION	24	C	C	349 - 364	350 - 365
25	X-RAY DIFFRACTION	25	D	D	3 - 55	4 - 56
26	X-RAY DIFFRACTION	26	D	D	56 - 95	57 - 96
27	X-RAY DIFFRACTION	27	D	D	96 - 106	97 - 107
28	X-RAY DIFFRACTION	28	D	D	107 - 168	108 - 169
29	X-RAY DIFFRACTION	29	D	D	169 - 241	170 - 242
30	X-RAY DIFFRACTION	30	D	D	242 - 254	243 - 255
31	X-RAY DIFFRACTION	31	D	D	255 - 334	256 - 335
32	X-RAY DIFFRACTION	32	D	D	335 - 353	336 - 354

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