PDB-5yb0: Crystal Structure of Wild Type Phosphoserine aminotransferase (PS...

ID or keywords:

Entry

Database: PDB / ID: 5yb0

Title

Crystal Structure of Wild Type Phosphoserine aminotransferase (PSAT) from E. histolytica

Components

Phosphoserine aminotransferase

Keywords

TRANSFERASE / PHOSPHOSERINE AMINOTRANSFERASE

Function / homology

Function and homology information

phosphoserine transaminase / O-phospho-L-serine:2-oxoglutarate aminotransferase activity / L-serine biosynthetic process / pyridoxal phosphate binding / cytoplasm
Similarity search - Function

Biological species

Entamoeba histolytica (eukaryote)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT /

molecular replacement / Resolution: 2.94 Å

Authors

Singh, R.K. / Gourinath, S.

Citation

Journal: Int.J.Biol.Macromol. / Year: 2019
Title: N-terminal residues are crucial for quaternary structure and active site conformation for the phosphoserine aminotransferase from enteric human parasite E. histolytica.
Authors: Singh, R.K. / Tomar, P. / Dharavath, S. / Kumar, S. / Gourinath, S.

History

Deposition	Sep 2, 2017	Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0	Oct 31, 2018	Provider: repository / Type: Initial release
Revision 1.1	Jul 10, 2019	Group: Data collection / Database references / Category: citation / citation_author Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2	Nov 22, 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
Revision 1.3	May 8, 2024	Group: Advisory / Derived calculations / Refinement description Category: pdbx_validate_close_contact / software / struct_conn
Revision 1.4	Sep 17, 2025	Group: Advisory / Derived calculations / Structure summary Category: pdbx_entry_details / pdbx_validate_close_contact / struct_conn

Structure viewer	Molecule: MolmilJmol/JSmol

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Validation report

Summary document	5yb0_validation.pdf.gz	546.4 KB	Display	wwPDB validaton report
Full document	5yb0_full_validation.pdf.gz	617.9 KB	Display
Data in XML	5yb0_validation.xml.gz	149.2 KB	Display
Data in CIF	5yb0_validation.cif.gz	192.3 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/yb/5yb0 ftp://data.pdbj.org/pub/pdb/validation_reports/yb/5yb0	HTTPS FTP

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Related structure data

Related structure data	5yd2C 5yiiC 1bt4S S: Starting model for refinement C: citing same article (ref.)
Similar structure data	5yd2-d 6czy-2 2bhx-d 2vmv-1 2via-1 5wml-d 6xdk-1 1w3u-1 6xdk-2 5u21-1 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) 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

5yd2C

5yiiC

1bt4S

S: Starting model for refinement

C: citing same article (ref.)

Similar structure data

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Links

PDB pages	PDBj / wwPDB / NCBI

Deposited unit

A: Phosphoserine aminotransferase

B: Phosphoserine aminotransferase

C: Phosphoserine aminotransferase

D: Phosphoserine aminotransferase

E: Phosphoserine aminotransferase

F: Phosphoserine aminotransferase

G: Phosphoserine aminotransferase

H: Phosphoserine aminotransferase

I: Phosphoserine aminotransferase

J: Phosphoserine aminotransferase

K: Phosphoserine aminotransferase

L: Phosphoserine aminotransferase

hetero molecules

490 kDa, 12 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Phosphoserine aminotransferase

B: Phosphoserine aminotransferase

hetero molecules

defined by author
Evidence: gel filtration
81.7 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

C: Phosphoserine aminotransferase

D: Phosphoserine aminotransferase

hetero molecules

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

3

E: Phosphoserine aminotransferase

H: Phosphoserine aminotransferase

hetero molecules

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

4

F: Phosphoserine aminotransferase

G: Phosphoserine aminotransferase

hetero molecules

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

5

I: Phosphoserine aminotransferase

J: Phosphoserine aminotransferase

hetero molecules

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

6

K: Phosphoserine aminotransferase

L: Phosphoserine aminotransferase

hetero molecules

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

Unit cell

Length a, b, c (Å)	66.446, 134.073, 139.064
Angle α, β, γ (deg.)	62.85, 88.58, 74.92
Int Tables number	1
Space group name H-M	P1

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Component-ID: 1 / Refine code: 1

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	HIS	HIS	GLU	GLU	A	A	7 - 353	7 - 353
2	1	HIS	HIS	GLU	GLU	B	B	7 - 353	7 - 353
1	2	HIS	HIS	GLU	GLU	A	A	7 - 353	7 - 353
2	2	HIS	HIS	GLU	GLU	C	C	7 - 353	7 - 353
1	3	HIS	HIS	GLN	GLN	A	A	7 - 354	7 - 354
2	3	HIS	HIS	GLN	GLN	D	D	7 - 354	7 - 354
1	4	HIS	HIS	GLU	GLU	A	A	7 - 353	7 - 353
2	4	HIS	HIS	GLU	GLU	E	E	7 - 353	7 - 353
1	5	HIS	HIS	CYS	CYS	A	A	7 - 348	7 - 348
2	5	HIS	HIS	CYS	CYS	F	F	7 - 348	7 - 348
1	6	HIS	HIS	GLN	GLN	A	A	7 - 354	7 - 354
2	6	HIS	HIS	GLN	GLN	G	G	7 - 354	7 - 354
1	7	HIS	HIS	GLU	GLU	A	A	7 - 353	7 - 353
2	7	HIS	HIS	GLU	GLU	H	H	7 - 353	7 - 353
1	8	HIS	HIS	GLN	GLN	A	A	7 - 354	7 - 354
2	8	HIS	HIS	GLN	GLN	I	I	7 - 354	7 - 354
1	9	PHE	PHE	GLU	GLU	A	A	9 - 260	9 - 260
2	9	PHE	PHE	GLU	GLU	J	J	9 - 260	9 - 260
1	10	LEU	LEU	PHE	PHE	A	A	38 - 352	38 - 352
2	10	LEU	LEU	PHE	PHE	K	K	38 - 352	38 - 352
1	11	LEU	LEU	ILE	ILE	A	A	35 - 249	35 - 249
2	11	LEU	LEU	ILE	ILE	L	L	35 - 249	35 - 249
1	12	ILE	ILE	GLN	GLN	B	B	6 - 354	6 - 354
2	12	ILE	ILE	GLN	GLN	C	C	6 - 354	6 - 354
1	13	ILE	ILE	GLN	GLN	B	B	6 - 354	6 - 354
2	13	ILE	ILE	GLN	GLN	D	D	6 - 354	6 - 354
1	14	ILE	ILE	GLU	GLU	B	B	6 - 353	6 - 353
2	14	ILE	ILE	GLU	GLU	E	E	6 - 353	6 - 353
1	15	ILE	ILE	CYS	CYS	B	B	6 - 348	6 - 348
2	15	ILE	ILE	CYS	CYS	F	F	6 - 348	6 - 348
1	16	ILE	ILE	GLN	GLN	B	B	6 - 354	6 - 354
2	16	ILE	ILE	GLN	GLN	G	G	6 - 354	6 - 354
1	17	ILE	ILE	GLN	GLN	B	B	6 - 354	6 - 354
2	17	ILE	ILE	GLN	GLN	H	H	6 - 354	6 - 354
1	18	ILE	ILE	GLN	GLN	B	B	6 - 354	6 - 354
2	18	ILE	ILE	GLN	GLN	I	I	6 - 354	6 - 354
1	19	PHE	PHE	GLU	GLU	B	B	9 - 260	9 - 260
2	19	PHE	PHE	GLU	GLU	J	J	9 - 260	9 - 260
1	20	LEU	LEU	PHE	PHE	B	B	38 - 352	38 - 352
2	20	LEU	LEU	PHE	PHE	K	K	38 - 352	38 - 352
1	21	LEU	LEU	ILE	ILE	B	B	35 - 249	35 - 249
2	21	LEU	LEU	ILE	ILE	L	L	35 - 249	35 - 249
1	22	ILE	ILE	GLN	GLN	C	C	6 - 354	6 - 354
2	22	ILE	ILE	GLN	GLN	D	D	6 - 354	6 - 354
1	23	ILE	ILE	GLU	GLU	C	C	6 - 353	6 - 353
2	23	ILE	ILE	GLU	GLU	E	E	6 - 353	6 - 353
1	24	ILE	ILE	CYS	CYS	C	C	6 - 348	6 - 348
2	24	ILE	ILE	CYS	CYS	F	F	6 - 348	6 - 348
1	25	ILE	ILE	GLN	GLN	C	C	6 - 354	6 - 354
2	25	ILE	ILE	GLN	GLN	G	G	6 - 354	6 - 354
1	26	ILE	ILE	GLN	GLN	C	C	6 - 354	6 - 354
2	26	ILE	ILE	GLN	GLN	H	H	6 - 354	6 - 354
1	27	ILE	ILE	GLN	GLN	C	C	6 - 354	6 - 354
2	27	ILE	ILE	GLN	GLN	I	I	6 - 354	6 - 354
1	28	PHE	PHE	GLU	GLU	C	C	9 - 260	9 - 260
2	28	PHE	PHE	GLU	GLU	J	J	9 - 260	9 - 260
1	29	LEU	LEU	PHE	PHE	C	C	38 - 352	38 - 352
2	29	LEU	LEU	PHE	PHE	K	K	38 - 352	38 - 352
1	30	LEU	LEU	ILE	ILE	C	C	35 - 249	35 - 249
2	30	LEU	LEU	ILE	ILE	L	L	35 - 249	35 - 249
1	31	ILE	ILE	GLU	GLU	D	D	6 - 353	6 - 353
2	31	ILE	ILE	GLU	GLU	E	E	6 - 353	6 - 353
1	32	ILE	ILE	CYS	CYS	D	D	6 - 348	6 - 348
2	32	ILE	ILE	CYS	CYS	F	F	6 - 348	6 - 348
1	33	ILE	ILE	GLN	GLN	D	D	6 - 354	6 - 354
2	33	ILE	ILE	GLN	GLN	G	G	6 - 354	6 - 354
1	34	ILE	ILE	GLN	GLN	D	D	6 - 354	6 - 354
2	34	ILE	ILE	GLN	GLN	H	H	6 - 354	6 - 354
1	35	ILE	ILE	GLN	GLN	D	D	6 - 354	6 - 354
2	35	ILE	ILE	GLN	GLN	I	I	6 - 354	6 - 354
1	36	PHE	PHE	GLU	GLU	D	D	9 - 260	9 - 260
2	36	PHE	PHE	GLU	GLU	J	J	9 - 260	9 - 260
1	37	LEU	LEU	PHE	PHE	D	D	38 - 352	38 - 352
2	37	LEU	LEU	PHE	PHE	K	K	38 - 352	38 - 352
1	38	LEU	LEU	ILE	ILE	D	D	35 - 249	35 - 249
2	38	LEU	LEU	ILE	ILE	L	L	35 - 249	35 - 249
1	39	ILE	ILE	CYS	CYS	E	E	6 - 348	6 - 348
2	39	ILE	ILE	CYS	CYS	F	F	6 - 348	6 - 348
1	40	ILE	ILE	GLU	GLU	E	E	6 - 353	6 - 353
2	40	ILE	ILE	GLU	GLU	G	G	6 - 353	6 - 353
1	41	ILE	ILE	GLU	GLU	E	E	6 - 353	6 - 353
2	41	ILE	ILE	GLU	GLU	H	H	6 - 353	6 - 353
1	42	ILE	ILE	GLU	GLU	E	E	6 - 353	6 - 353
2	42	ILE	ILE	GLU	GLU	I	I	6 - 353	6 - 353
1	43	PHE	PHE	GLU	GLU	E	E	9 - 260	9 - 260
2	43	PHE	PHE	GLU	GLU	J	J	9 - 260	9 - 260
1	44	LEU	LEU	PHE	PHE	E	E	38 - 352	38 - 352
2	44	LEU	LEU	PHE	PHE	K	K	38 - 352	38 - 352
1	45	LEU	LEU	ILE	ILE	E	E	35 - 249	35 - 249
2	45	LEU	LEU	ILE	ILE	L	L	35 - 249	35 - 249
1	46	ILE	ILE	CYS	CYS	F	F	6 - 348	6 - 348
2	46	ILE	ILE	CYS	CYS	G	G	6 - 348	6 - 348
1	47	ILE	ILE	CYS	CYS	F	F	6 - 348	6 - 348
2	47	ILE	ILE	CYS	CYS	H	H	6 - 348	6 - 348
1	48	ILE	ILE	CYS	CYS	F	F	6 - 348	6 - 348
2	48	ILE	ILE	CYS	CYS	I	I	6 - 348	6 - 348
1	49	PHE	PHE	GLU	GLU	F	F	9 - 260	9 - 260
2	49	PHE	PHE	GLU	GLU	J	J	9 - 260	9 - 260
1	50	LEU	LEU	LYS	LYS	F	F	38 - 347	38 - 347
2	50	LEU	LEU	LYS	LYS	K	K	38 - 347	38 - 347
1	51	LEU	LEU	ILE	ILE	F	F	35 - 249	35 - 249
2	51	LEU	LEU	ILE	ILE	L	L	35 - 249	35 - 249
1	52	ILE	ILE	GLN	GLN	G	G	6 - 354	6 - 354
2	52	ILE	ILE	GLN	GLN	H	H	6 - 354	6 - 354
1	53	ILE	ILE	GLN	GLN	G	G	6 - 354	6 - 354
2	53	ILE	ILE	GLN	GLN	I	I	6 - 354	6 - 354
1	54	PHE	PHE	GLU	GLU	G	G	9 - 260	9 - 260
2	54	PHE	PHE	GLU	GLU	J	J	9 - 260	9 - 260
1	55	LEU	LEU	PHE	PHE	G	G	38 - 352	38 - 352
2	55	LEU	LEU	PHE	PHE	K	K	38 - 352	38 - 352
1	56	LEU	LEU	ILE	ILE	G	G	35 - 249	35 - 249
2	56	LEU	LEU	ILE	ILE	L	L	35 - 249	35 - 249
1	57	ILE	ILE	GLN	GLN	H	H	6 - 354	6 - 354
2	57	ILE	ILE	GLN	GLN	I	I	6 - 354	6 - 354
1	58	PHE	PHE	GLU	GLU	H	H	9 - 260	9 - 260
2	58	PHE	PHE	GLU	GLU	J	J	9 - 260	9 - 260
1	59	LEU	LEU	PHE	PHE	H	H	38 - 352	38 - 352
2	59	LEU	LEU	PHE	PHE	K	K	38 - 352	38 - 352
1	60	LEU	LEU	ILE	ILE	H	H	35 - 249	35 - 249
2	60	LEU	LEU	ILE	ILE	L	L	35 - 249	35 - 249
1	61	PHE	PHE	GLU	GLU	I	I	9 - 260	9 - 260
2	61	PHE	PHE	GLU	GLU	J	J	9 - 260	9 - 260
1	62	LEU	LEU	PHE	PHE	I	I	38 - 352	38 - 352
2	62	LEU	LEU	PHE	PHE	K	K	38 - 352	38 - 352
1	63	LEU	LEU	ILE	ILE	I	I	35 - 249	35 - 249
2	63	LEU	LEU	ILE	ILE	L	L	35 - 249	35 - 249
1	64	LEU	LEU	GLU	GLU	J	J	38 - 260	38 - 260
2	64	LEU	LEU	GLU	GLU	K	K	38 - 260	38 - 260
1	65	LEU	LEU	ILE	ILE	J	J	35 - 249	35 - 249
2	65	LEU	LEU	ILE	ILE	L	L	35 - 249	35 - 249
1	66	LEU	LEU	ILE	ILE	K	K	38 - 249	38 - 249
2	66	LEU	LEU	ILE	ILE	L	L	38 - 249	38 - 249

NCS ensembles :
NCS oper:

ID	Code	Matrix	Vector
1	given	(1), (1), (1)
2	given	(0.991396, -0.028755, -0.127698), (-0.028831, -0.999584, 0.00125), (-0.12768, 0.002443, -0.991812)	-4.42575, -29.810089, -61.692909
3	given	(1), (1), (1)
4	given	(-0.997227, -0.004659, -0.074274), (0.031301, 0.879202, -0.47542), (0.067517, -0.476426, -0.876618)	-9.85708, -17.743139, -135.035782
5	given	(1), (1), (1)
6	given	(-0.997919, 0.062511, 0.015802), (-0.047176, -0.874942, 0.481924), (0.043952, 0.480175, 0.876071)	1.67634, -10.79655, 73.258339
7	given	(1), (1), (1)
8	given	(0.104575, 0.674384, 0.730938), (0.62579, -0.615846, 0.478666), (0.77295, 0.407357, -0.486425)	39.960041, -41.27449, -23.780121
9	given	(1), (1), (1)
10	given	(0.018616, -0.717311, -0.696504), (0.604821, 0.562789, -0.563436), (0.796144, -0.410772, 0.444322)	-23.14794, -54.646198, -6.91186
11	given	(1), (1), (1)
12	given	(-0.081285, -0.661993, -0.74509), (-0.605443, -0.561035, 0.564516), (-0.791727, 0.496996, -0.355195)	-25.99765, 25.165211, -52.33287
13	given	(1), (1), (1)
14	given	(0.00126, 0.61889, 0.785476), (-0.623019, 0.614891, -0.483484), (-0.782206, -0.488757, 0.386355)	38.661049, 11.60818, -43.534389
15	given	(1), (1), (1)
16	given	(-0.329173, 0.379945, -0.864458), (0.796919, 0.602858, -0.038488), (0.506522, -0.701572, -0.50123)	-52.373562, 42.406849, -122.738564
17	given	(1), (1), (1)
18	given	(-0.384335, 0.447571, -0.807445), (-0.789533, -0.612638, 0.036221), (-0.47846, 0.651425, 0.58883)	-42.718609, -72.819763, 65.260307
19	given	(1), (1), (1)
20	given	(-0.232045, -0.370012, 0.899581), (0.812964, -0.581566, -0.029505), (0.534083, 0.724481, 0.435756)	76.590363, -14.28892, 28.601971
21	given	(1), (1), (1)
22	given	(-0.285363, -0.453918, 0.844112), (-0.813873, 0.579883, 0.036689), (-0.50614, -0.676531, -0.534909)	69.278214, -14.54181, -98.933144
23	given	(1), (1), (1)
24	given	(-0.998183, 0.030966, 0.051686), (-0.002679, -0.879789, 0.475357), (0.060192, 0.474355, 0.878274)	3.60978, -12.07102, 73.452797
25	given	(1), (1), (1)
26	given	(-0.99362, 0.025701, -0.109811), (0.075679, 0.873863, -0.480246), (0.083617, -0.485492, -0.870233)	-11.71079, -18.87915, -134.599579
27	given	(1), (1), (1)
28	given	(-0.012886, 0.634333, 0.772953), (-0.626913, 0.597091, -0.500462), (-0.778983, -0.491023, 0.389977)	39.49395, 10.26837, -43.279362
29	given	(1), (1), (1)
30	given	(-0.100691, -0.674797, -0.731102), (-0.603784, -0.542605, 0.583973), (-0.790763, 0.500229, -0.352796)	-24.848261, 25.46814, -51.988319
31	given	(1), (1), (1)
32	given	(0.037649, -0.703646, -0.709552), (0.605893, 0.580723, -0.543741), (0.794655, -0.409441, 0.448198)	-24.159161, -54.315159, -6.44318
33	given	(1), (1), (1)
34	given	(0.118771, 0.658178, 0.743435), (0.62078, -0.63358, 0.461746), (0.774936, 0.406667, -0.483834)	39.20779, -42.594582, -23.44206
35	given	(1), (1), (1)
36	given	(-0.413749, 0.448655, -0.792162), (-0.785941, -0.615177, 0.062083), (-0.459466, 0.648279, 0.607145)	-41.855289, -70.961929, 66.752724
37	given	(1), (1), (1)
38	given	(-0.29659, 0.378212, -0.876921), (0.800002, 0.59988, -0.011849), (0.521566, -0.705053, -0.480489)	-52.94722, 44.271351, -121.117363
39	given	(1), (1), (1)
40	given	(-0.321576, -0.442372, 0.837195), (-0.804715, 0.593644, 0.00458), (-0.499022, -0.672231, -0.546885)	68.362762, -17.6444, -99.857246
41	given	(1), (1), (1)
42	given	(-0.193383, -0.380503, 0.904334), (0.821808, -0.56632, -0.062546), (0.535942, 0.731094, 0.422218)	77.407021, -17.476339, 27.524389
43	given	(1), (1), (1)
44	given	(0.996646, -0.057267, 0.058456), (-0.05774, -0.998311, 0.006441), (0.057989, -0.009795, -0.998269)	2.77827, -93.161171, -186.759979
45	given	(1), (1), (1)
46	given	(-0.03217, -0.664431, -0.746657), (0.182067, -0.73844, 0.649275), (-0.98276, -0.115055, 0.144727)	-42.905041, -73.905647, -90.064659
47	given	(1), (1), (1)
48	given	(0.055152, 0.705717, 0.706344), (0.154069, 0.692933, -0.704348), (-0.98652, 0.147672, -0.070513)	20.725691, -93.409233, -93.834213
49	given	(1), (1), (1)
50	given	(0.008859, 0.676145, 0.736715), (-0.155359, -0.726867, 0.668975), (0.987818, -0.120382, 0.098605)	23.019609, -1.58895, -91.671066
51	given	(1), (1), (1)
52	given	(-0.073841, -0.630754, -0.772462), (-0.175253, 0.77073, -0.612586), (0.98175, 0.090142, -0.167453)	-41.275982, -17.99498, -97.768806
53	given	(1), (1), (1)
54	given	(0.387321, -0.407421, 0.827037), (0.461102, 0.862407, 0.208901), (-0.798353, 0.300437, 0.521891)	45.110378, 47.218208, -36.192139
55	given	(1), (1), (1)
56	given	(0.322699, -0.423092, 0.846675), (-0.468778, -0.848554, -0.245363), (0.822261, -0.317724, -0.472164)	44.49276, -143.524719, -147.212723
57	given	(1), (1), (1)
58	given	(0.291623, 0.399306, -0.869201), (0.46224, -0.854382, -0.237414), (-0.837431, -0.332544, -0.433732)	-75.158653, -75.255493, -151.426208
59	given	(1), (1), (1)
60	given	(0.221254, 0.426985, -0.876773), (-0.478188, 0.831055, 0.28405), (0.849931, 0.356415, 0.388053)	-76.36348, -14.69936, -39.03511
61	given	(1), (1), (1)
62	given	(-0.099839, -0.626926, -0.772655), (-0.168178, 0.775995, -0.607904), (0.980688, 0.069251, -0.18291)	-41.053299, -17.58007, -99.147217
63	given	(1), (1), (1)
64	given	(-0.011306, 0.672081, 0.740392), (-0.146496, -0.733563, 0.663645), (0.989147, -0.100961, 0.106751)	23.28063, -1.67457, -91.746109
65	given	(1), (1), (1)
66	given	(0.075365, 0.707063, 0.703124), (0.140293, 0.690597, -0.709503), (-0.987238, 0.152114, -0.047149)	20.526739, -93.40197, -92.886803
67	given	(1), (1), (1)
68	given	(-0.006612, -0.668304, -0.743859), (0.169782, -0.733825, 0.65778), (-0.98546, -0.121945, 0.118318)	-43.097881, -73.359009, -90.92762
69	given	(1), (1), (1)
70	given	(0.313274, -0.438275, 0.842481), (-0.473853, -0.84095, -0.261277), (0.822996, -0.317361, -0.471126)	42.835911, -144.067032, -146.835571
71	given	(1), (1), (1)
72	given	(0.39648, -0.390927, 0.83065), (0.4405, 0.874853, 0.201474), (-0.805459, 0.286021, 0.519065)	46.79541, 47.569809, -37.46006
73	given	(1), (1), (1)
74	given	(0.215799, 0.428833, -0.877231), (-0.47046, 0.832907, 0.291432), (0.855627, 0.349812, 0.381489)	-76.58802, -13.72942, -39.636742
75	given	(1), (1), (1)
76	given	(0.29661, 0.398025, -0.8681), (0.455639, -0.857856, -0.237646), (-0.839294, -0.325052, -0.435805)	-74.874687, -75.292641, -151.493866
77	given	(1), (1), (1)
78	given	(0.995793, -0.041056, -0.081913), (-0.036312, -0.997622, 0.058583), (-0.084123, -0.055363, -0.994916)	-1.91329, -27.450121, -60.72863
79	given	(1), (1), (1)
80	given	(-0.999255, -0.038384, 0.003923), (-0.007896, 0.103924, -0.994554), (0.037768, -0.993844, -0.10415)	12.81047, -97.006157, -2.68751
81	given	(1), (1), (1)
82	given	(-0.99435, 0.071803, 0.078186), (0.065852, -0.160456, 0.984844), (0.083261, 0.984428, 0.154821)	17.690201, -41.49107, 33.970921
83	given	(1), (1), (1)
84	given	(0.856109, -0.124734, -0.501516), (-0.505855, -0.400873, -0.763814), (-0.105771, 0.907602, -0.406289)	-33.69566, -154.130615, 20.713051
85	given	(1), (1), (1)
86	given	(-0.903926, 0.169829, 0.392526), (0.035474, 0.944391, -0.326906), (-0.426216, -0.281575, -0.859683)	40.587608, -0.06019, -118.760178
87	given	(1), (1), (1)
88	given	(0.897311, 0.158055, 0.41213), (-0.439648, 0.403094, 0.802636), (-0.039266, -0.901407, 0.431189)	61.18903, 29.44417, 14.20877
89	given	(1), (1), (1)
90	given	(-0.92981, -0.211455, -0.301231), (0.106948, -0.938392, 0.328606), (-0.352159, 0.273325, 0.895141)	-38.261002, -27.319071, 70.813057
91	given	(1), (1), (1)
92	given	(-0.997937, 0.042901, 0.047761), (0.045792, -0.045763, 0.997902), (0.044997, 0.998031, 0.043704)	12.22714, 65.580322, -63.116161
93	given	(1), (1), (1)
94	given	(-0.999574, -0.005238, 0.028718), (-0.029104, 0.102218, -0.994336), (0.002272, -0.994748, -0.102327)	12.07324, 7.93124, -96.638359
95	given	(1), (1), (1)
96	given	(0.879703, -0.186114, -0.43759), (0.475495, 0.354467, 0.805144), (0.005263, -0.91636, 0.400322)	-33.917141, 123.154831, -85.877678
97	given	(1), (1), (1)
98	given	(-0.86559, 0.158297, 0.475074), (0.025394, -0.933623, 0.357356), (0.500108, 0.321388, 0.804115)	46.194321, -25.87759, 55.858639
99	given	(1), (1), (1)
100	given	(0.913078, 0.218112, 0.344553), (0.403352, -0.358806, -0.841763), (-0.059971, 0.907571, -0.415594)	54.42387, -63.538601, -76.372993
101	given	(1), (1), (1)
102	given	(-0.900171, -0.19908, -0.387375), (-0.048822, 0.929937, -0.364463), (0.432791, -0.309167, -0.846822)	-47.275059, -5.85769, -127.892563
103	given	(1), (1), (1)
104	given	(0.996354, -0.035992, -0.077355), (-0.040459, -0.997555, -0.056988), (-0.075115, 0.05991, -0.995374)	-4.03523, -30.819651, -58.93116
105	given	(1), (1), (1)
106	given	(-0.855741, 0.161301, 0.49162), (0.020528, -0.938832, 0.343764), (0.516998, 0.304265, 0.800085)	47.712952, -27.360229, 54.209049
107	given	(1), (1), (1)
108	given	(0.887738, -0.185222, -0.421444), (0.460301, 0.370448, 0.806778), (0.00669, -0.910198, 0.414119)	-32.63908, 124.411667, -84.473808
109	given	(1), (1), (1)
110	given	(-0.8965, -0.191399, -0.399567), (-0.03714, 0.931161, -0.362711), (0.441484, -0.310331, -0.841895)	-48.467312, -5.59385, -127.507507
111	given	(1), (1), (1)
112	given	(0.915931, 0.226187, 0.331528), (0.394858, -0.360049, -0.845252), (-0.071819, 0.905099, -0.419092)	53.153728, -63.957039, -76.942467
113	given	(1), (1), (1)
114	given	(-0.893308, 0.173735, 0.414508), (0.038964, 0.94873, -0.313676), (-0.447753, -0.264058, -0.854278)	42.61758, 1.3149, -117.002579
115	given	(1), (1), (1)
116	given	(0.865544, -0.130568, -0.483514), (-0.490485, -0.416217, -0.765629), (-0.10128, 0.899842, -0.424296)	-32.80286, -155.335709, 18.952789
117	given	(1), (1), (1)
118	given	(-0.924568, -0.205794, -0.320659), (0.096232, -0.940431, 0.326082), (-0.368663, 0.270627, 0.889296)	-40.18924, -27.62015, 70.203506
119	given	(1), (1), (1)
120	given	(0.902134, 0.171203, 0.396036), (-0.430911, 0.403672, 0.807072), (-0.021696, -0.898743, 0.437939)	59.670841, 29.98218, 15.21114
121	given	(1), (1), (1)
122	given	(-0.746757, -0.302973, 0.592082), (-0.288094, -0.65502, -0.698535), (0.599462, -0.692211, 0.401856)	0.36104, -197.627258, -98.291847
123	given	(1), (1), (1)
124	given	(0.994741, 0.025525, -0.099187), (0.02751, -0.999447, 0.01869), (-0.098655, -0.02132, -0.994893)	-11.00028, -91.303497, -185.171509
125	given	(1), (1), (1)
126	given	(-0.813104, 0.265436, -0.518078), (-0.246221, 0.649633, 0.719272), (0.527481, 0.712405, -0.462863)	-73.273888, -4.72043, -114.836388
127	given	(1), (1), (1)
128	given	(-0.810067, 0.255851, -0.527572), (-0.250876, 0.662011, 0.706259), (0.529956, 0.704472, -0.472086)	-74.221336, -6.0902, -115.959991
129	given	(1), (1), (1)
130	given	(0.994356, 0.041482, -0.097654), (0.042371, -0.999077, 0.007047), (-0.097271, -0.011145, -0.995196)	-10.49731, -92.517967, -185.011292
131	given	(1), (1), (1)
132	given	(-0.86749, 0.211481, -0.450264), (0.21385, -0.658691, -0.721384), (-0.449144, -0.722082, 0.526182)	-66.54425, -89.553093, -62.073631

#1: Protein	Phosphoserine aminotransferase / Phosphoserine aminotransferase / putative Mass: 40584.965 Da / Num. of mol.: 12 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Entamoeba histolytica (eukaryote) / Gene: EhPSAT, EHI_026360 / Plasmid: pET21C / Production host: Escherichia coli (E. coli) / References: UniProt: Q60I38, phosphoserine transaminase
#2: Chemical	ChemComp-PLP / PYRIDOXAL-5'-PHOSPHATE / VITAMIN B6 Phosphate Mass: 247.142 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C₈H₁₀NO₆P
#3: Chemical	ChemComp-CL / CHLORIDE ION Mass: 35.453 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Cl
#4: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 155 / Source method: isolated from a natural source / Formula: H₂O
Has protein modification	N

-
Experiment

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

-
Sample preparation

Crystal	Density Matthews: 2.37 Å³/Da / Density % sol: 43.38 %
Crystal grow	Temperature: 289.15 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 25-30% PEG 3350 (w/v), 100 mM Tris pH 6.5, 200mM sodium formate, 5 % glycerol (v/v)

-
Data collection

Diffraction

Mean temperature: 77.15 K

Diffraction source

Source:

SYNCHROTRON / Site:

ESRF

/ Beamline: BM14 / Wavelength: 0.97 Å

Detector

Type: MAR CCD 165 mm / Detector: CCD / Date: Apr 10, 2011

Radiation

Monochromator: Si 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray

Radiation wavelength

Wavelength: 0.97 Å / Relative weight: 1

Reflection twin

Crystal-ID	ID	Operator	Domain-ID	Fraction
1	1	H, K, L	1	0.888
1	1	H, H-K, -L	2	0.112

Reflection

Resolution: 2.94→50.15 Å / Num. obs: 76771 / % possible obs: 94.2 % / Redundancy: 3.7 % / R_merge(I) obs: 0.083 / R_sym value: 0.051 / Net I/σ(I): 14.911

Reflection shell

Resolution: 3→3.05 Å / Redundancy: 1.9 % / R_merge(I) obs: 0.881 / % possible all: 85.8

-
Phasing

Phasing	Method: molecular replacement

-
Processing

Software

Name	Version	Classification
REFMAC	5.8.0049	refinement
HKL-2000		data collection
PDB_EXTRACT	3.22	data extraction
HKL-2000		data reduction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 1BT4

1bt4

Resolution: 2.94→50.15 Å / Cor.coef. F_o:F_c: 0.883 / Cor.coef. F_o:F_c free: 0.862 / SU B: 42.403 / SU ML: 0.389 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.122 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.301	3764	4.9 %	RANDOM
R_work	0.265	-	-	-
obs	0.267	73001	87.9 %	-

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å

Displacement parameters

B_iso mean: 76.93 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	9.03 Å²	-37.97 Å²	23.05 Å²
2-	-	-6.13 Å²	8.3 Å²
3-	-	-	-2.91 Å²

Refinement step

Cycle: LAST / Resolution: 2.94→50.15 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	27082	0	165	155	27402

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.012	0.019	27656
X-RAY DIFFRACTION	r_bond_other_d	0.008	0.02	25136
X-RAY DIFFRACTION	r_angle_refined_deg	1.553	1.967	37611
X-RAY DIFFRACTION	r_angle_other_deg	1.091	3	57361
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	8.333	5	3849
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	37.526	25.109	873
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	18.187	15	4088
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	11.811	15	68
X-RAY DIFFRACTION	r_chiral_restr	0.083	0.2	4485
X-RAY DIFFRACTION	r_gen_planes_refined	0.006	0.02	32192
X-RAY DIFFRACTION	r_gen_planes_other	0.003	0.02	5782
X-RAY DIFFRACTION	r_nbd_refined
X-RAY DIFFRACTION	r_nbd_other
X-RAY DIFFRACTION	r_nbtor_refined
X-RAY DIFFRACTION	r_nbtor_other
X-RAY DIFFRACTION	r_xyhbond_nbd_refined
X-RAY DIFFRACTION	r_xyhbond_nbd_other
X-RAY DIFFRACTION	r_metal_ion_refined
X-RAY DIFFRACTION	r_metal_ion_other
X-RAY DIFFRACTION	r_symmetry_vdw_refined
X-RAY DIFFRACTION	r_symmetry_vdw_other
X-RAY DIFFRACTION	r_symmetry_hbond_refined
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
X-RAY DIFFRACTION	r_mcbond_other
X-RAY DIFFRACTION	r_mcangle_it
X-RAY DIFFRACTION	r_mcangle_other
X-RAY DIFFRACTION	r_scbond_it
X-RAY DIFFRACTION	r_scbond_other
X-RAY DIFFRACTION	r_scangle_it
X-RAY DIFFRACTION	r_scangle_other
X-RAY DIFFRACTION	r_long_range_B_refined
X-RAY DIFFRACTION	r_long_range_B_other
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 / Refine-ID: X-RAY DIFFRACTION

Ens-ID	Auth asym-ID	Number	Type	Rms dev position (Å)	Weight position
1	A	1601	tight positional	0.13	0.17
1	A	1221	tight positional	0.1	0.17
1	A	3213	tight positional	0.13	0.17
1	A	3076	tight positional	0.13	0.17
1	A	2845	tight positional	0.12	0.17
1	A	2599	tight positional	0.17	0.17
1	A	2891	tight positional	0.15	0.17
1	A	2354	tight positional	0.15	0.17
1	A	2426	tight positional	0.12	0.17
1	A	1480	tight positional	0.12	0.17
2	A	1601	tight positional	0.12	0.17
2	A	1221	tight positional	0.11	0.17
2	A	3074	tight positional	0.11	0.17
2	A	2835	tight positional	0.11	0.17
2	A	2599	tight positional	0.16	0.17
2	A	2881	tight positional	0.13	0.17
2	A	2354	tight positional	0.13	0.17
2	A	2416	tight positional	0.09	0.17
2	A	1480	tight positional	0.09	0.17
2	A	1601	tight positional	0.13	0.17
3	A	1221	tight positional	0.1	0.17
3	A	2790	tight positional	0.22	0.17
3	A	2567	tight positional	0.15	0.17
3	A	2822	tight positional	0.3	0.17
3	A	2333	tight positional	0.12	0.17
3	A	2362	tight positional	0.09	0.17
3	A	1469	tight positional	0.1	0.17
3	A	1580	tight positional	0.12	0.17
3	A	1215	tight positional	0.09	0.17
3	A	2536	tight positional	0.15	0.17
4	A	2686	tight positional	0.29	0.17
4	A	2248	tight positional	0.12	0.17
4	A	2262	tight positional	0.08	0.17
4	A	1471	tight positional	0.1	0.17
4	A	1546	tight positional	0.12	0.17
4	A	1212	tight positional	0.1	0.17
4	A	2435	tight positional	0.14	0.17
4	A	2094	tight positional	0.16	0.17
4	A	2096	tight positional	0.14	0.17
4	A	1480	tight positional	0.11	0.17
5	A	1429	tight positional	0.18	0.17
5	A	1221	tight positional	0.09	0.17
5	A	2209	tight positional	0.16	0.17
5	A	2308	tight positional	0.25	0.17
5	A	1407	tight positional	0.1	0.17
5	A	1564	tight positional	0.15	0.17
5	A	1177	tight positional	0.08	0.17
5	A	2012	tight positional	0.1	0.17
5	A	1387	tight positional	0.12	0.17
5	A	1525	tight positional	0.14	0.17
6	A	1168	tight positional	0.11	0.17
6	A	1418	tight positional	0.09	0.17
6	A	1424	tight positional	0.08	0.17
6	A	1178	tight positional	0.08	0.17
6	A	1023	tight positional	0.08	0.17
6	A	1141	tight positional	0.1	0.17
6	A	990	tight positional	0.09	0.17
1	A	3279	tight thermal	4.61	1.66
2	A	3188	tight thermal	5.97	1.66
3	A	3061	tight thermal	5.58	1.66
4	A	2830	tight thermal	5.33	1.66
5	A	2593	tight thermal	7.37	1.66
6	A	2876	tight thermal	9.11	1.66
7	A	2338	tight thermal	6.9	1.66
8	A	2411	tight thermal	7.36	1.66
9	A	1480	tight thermal	5.78	1.66
10	A	1601	tight thermal	12.65	1.66
11	A	1221	tight thermal	11.59	1.66
12	B	3213	tight thermal	5.39	1.66
13	B	3076	tight thermal	5.46	1.66
14	B	2845	tight thermal	5.1	1.66
15	B	2599	tight thermal	6.81	1.66
16	B	2891	tight thermal	8.68	1.66
17	B	2354	tight thermal	7.76	1.66
18	B	2426	tight thermal	7.23	1.66
19	B	1480	tight thermal	5.28	1.66
20	B	1601	tight thermal	11.82	1.66
21	B	1221	tight thermal	10.96	1.66
22	C	3074	tight thermal	5.38	1.66
23	C	2835	tight thermal	5.43	1.66
24	C	2599	tight thermal	5.21	1.66
25	C	2881	tight thermal	6.95	1.66
26	C	2354	tight thermal	9.05	1.66
27	C	2416	tight thermal	6.22	1.66
28	C	1480	tight thermal	5.73	1.66
29	C	1601	tight thermal	10.2	1.66
30	C	1221	tight thermal	9.37	1.66
31	D	2790	tight thermal	5.95	1.66
32	D	2567	tight thermal	5.84	1.66
33	D	2822	tight thermal	8	1.66
34	D	2333	tight thermal	8.76	1.66
35	D	2362	tight thermal	6.68	1.66
36	D	1469	tight thermal	5.97	1.66
37	D	1580	tight thermal	11.69	1.66
38	D	1215	tight thermal	10.19	1.66
39	E	2536	tight thermal	6.65	1.66
40	E	2686	tight thermal	8.27	1.66
41	E	2248	tight thermal	6.72	1.66
42	E	2262	tight thermal	7.18	1.66
43	E	1471	tight thermal	4.78	1.66
44	E	1546	tight thermal	11.76	1.66
45	E	1212	tight thermal	10.74	1.66
46	F	2435	tight thermal	5.67	1.66
47	F	2094	tight thermal	10.62	1.66
48	F	2096	tight thermal	6.64	1.66
49	F	1480	tight thermal	6.47	1.66
50	F	1429	tight thermal	8.87	1.66
51	F	1221	tight thermal	7.64	1.66
52	G	2209	tight thermal	12.41	1.66
53	G	2308	tight thermal	7.28	1.66
54	G	1407	tight thermal	8.67	1.66
55	G	1564	tight thermal	7.44	1.66
56	G	1177	tight thermal	6.27	1.66
57	H	2012	tight thermal	10.35	1.66
58	H	1387	tight thermal	6.95	1.66
59	H	1525	tight thermal	15.71	1.66
60	H	1168	tight thermal	14.07	1.66
61	I	1418	tight thermal	8.25	1.66
62	I	1424	tight thermal	11.18	1.66
63	I	1178	tight thermal	9.07	1.66
64	J	1023	tight thermal	13.07	1.66
65	J	1141	tight thermal	10.63	1.66
66	K	990	tight thermal	8.04	1.66

LS refinement shell

Resolution: 2.94→3.02 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.432	19	-
R_work	0.272	515	-
obs	-	-	8.21 %

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	1.3436	0.0785	0.4333	1.5958	-0.2324	2.8989	-0.0212	0.1488	-0.1079	-0.2775	0.0961	0.1087	-0.0145	-0.206	-0.0749	0.2719	0.1514	-0.1045	0.1657	-0.0732	0.0666	-12.6961	-20.2716	-45.9012
2	1.4312	0.2053	-0.1176	2.0681	0.1861	3.0281	0.0905	-0.1826	0.1582	0.3851	-0.0111	0.0764	-0.3698	-0.1125	-0.0794	0.3766	0.1821	-0.0088	0.1592	-0.064	0.0715	-10.5102	-9.2821	-14.592
3	1.6149	1.2737	0.5022	3.6921	1.8578	2.5012	0.0942	-0.3358	0.0021	0.3396	-0.1447	0.0897	0.0735	0.279	0.0506	0.1354	0.0702	-0.0483	0.3192	-0.0701	0.0397	8.6225	-45.1011	-76.925
4	1.5551	0.9777	0.4851	3.2706	1.3527	2.585	-0.462	0.2776	0.0962	-1.2447	0.5942	0.1614	-0.6434	0.4766	-0.1322	0.589	-0.1244	-0.1039	0.4432	-0.0893	0.1076	9.1026	-48.8812	-108.7573
5	1.6796	0.9195	-0.1514	3.2184	-1.5275	3.8091	0.1426	-0.168	-0.3898	0.3294	0.0035	0.1225	-0.2972	-0.1928	-0.1462	0.2401	0.1592	-0.1011	0.2549	0.071	0.2775	-9.1253	-55.7417	-18.5853
6	2.2992	0.5768	0.162	2.2636	-0.7007	3.6167	-0.0423	-0.053	0.5802	-0.2584	0.083	0.297	0.2487	-0.5119	-0.0407	0.2192	0.1112	-0.0612	0.2094	-0.0058	0.1849	-8.9574	24.1518	-42.4297
7	2.3083	0.1781	1.834	2.4014	-1.1717	3.2222	-0.0449	0.4317	0.3688	-0.1723	-0.4764	-0.4558	0.1075	1.114	0.5212	0.193	0.2144	0.0962	0.5734	0.2238	0.1926	21.6822	20.2516	-38.2688
8	2.3927	1.2833	-1.2305	2.5737	-1.7573	2.1222	0.039	-0.2165	-0.7794	0.1957	-0.6475	-0.7846	-0.1301	1.1716	0.6085	0.4606	0.072	-0.3943	1.027	0.2233	0.7531	20.7068	-51.4708	-25.3582
9	2.5086	0.2734	-1.4622	2.1655	-0.4012	3.1003	-0.3954	0.2722	0.152	-0.4535	0.2743	0.7061	0.5004	-0.512	0.1211	0.448	-0.0418	-0.2464	0.4152	0.0437	0.5311	-23.6047	-77.3737	-70.399
10	3.2792	1.3639	-2.3576	3.392	-1.6646	2.0878	-0.8109	0.1927	-0.4927	-1.0371	0.4362	-0.1307	0.8317	0.0954	0.3748	1.0373	0.0625	-0.0426	0.5215	-0.0171	0.2313	-1.7038	-83.0144	-85.928
11	2.4609	-0.8027	0.0008	3.1044	1.588	4.0487	0.1476	-0.2524	-0.0209	-0.4198	-0.3425	0.7962	-0.4593	-0.5624	0.1949	0.5316	0.0381	-0.3104	0.2053	-0.055	0.3563	-24.5984	-18.7136	-110.9696
12	4.4812	0.1686	1.3163	4.6186	0.8272	2.3075	-0.0713	-0.4772	0.4728	0.112	0.2019	-0.5844	-0.3321	0.5002	-0.1306	0.6236	-0.1289	-0.1591	0.4414	-0.088	0.2422	-1.1278	-11.7194	-96.525

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	7 - 354
2	X-RAY DIFFRACTION	1	A	401 - 402
3	X-RAY DIFFRACTION	1	A	501 - 514
4	X-RAY DIFFRACTION	2	B	6 - 354
5	X-RAY DIFFRACTION	2	B	401 - 402
6	X-RAY DIFFRACTION	2	B	501 - 512
7	X-RAY DIFFRACTION	3	C	6 - 354
8	X-RAY DIFFRACTION	3	C	401 - 402
9	X-RAY DIFFRACTION	3	C	501 - 516
10	X-RAY DIFFRACTION	4	D	6 - 354
11	X-RAY DIFFRACTION	4	D	401 - 402
12	X-RAY DIFFRACTION	4	D	501 - 511
13	X-RAY DIFFRACTION	5	E	6 - 353
14	X-RAY DIFFRACTION	5	E	401 - 402
15	X-RAY DIFFRACTION	5	E	501 - 518
16	X-RAY DIFFRACTION	6	F	6 - 348
17	X-RAY DIFFRACTION	6	F	401
18	X-RAY DIFFRACTION	6	F	501 - 509
19	X-RAY DIFFRACTION	7	G	6 - 354
20	X-RAY DIFFRACTION	7	G	401
21	X-RAY DIFFRACTION	7	G	501 - 513
22	X-RAY DIFFRACTION	8	H	6 - 354
23	X-RAY DIFFRACTION	8	H	401
24	X-RAY DIFFRACTION	8	H	501 - 519
25	X-RAY DIFFRACTION	9	I	6 - 354
26	X-RAY DIFFRACTION	9	I	401
27	X-RAY DIFFRACTION	9	I	501 - 523
28	X-RAY DIFFRACTION	10	J	9 - 261
29	X-RAY DIFFRACTION	10	J	401 - 410
30	X-RAY DIFFRACTION	11	K	38 - 353
31	X-RAY DIFFRACTION	11	K	401
32	X-RAY DIFFRACTION	11	K	501 - 508
33	X-RAY DIFFRACTION	12	L	35 - 250
34	X-RAY DIFFRACTION	12	L	401 - 402

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