PDB-1pn0: Phenol hydroxylase from Trichosporon cutaneum

Basic information

• Entry: Database: PDB / ID: 1pn0
• Title: Phenol hydroxylase from Trichosporon cutaneum
• Components: Phenol 2-monooxygenase
• Keywords: OXIDOREDUCTASE / two dimers / TLS refinement

Function / homology

Function:

phenol-containing compound catabolic process / phenol 2-monooxygenase (NADPH) / phenol 2-monooxygenase activity / FAD binding

Domain/homology:

Phenol hydroxylase, C-terminal dimerisation domain / Phenol hydroxylase, C-terminal dimerisation domain / Phenol hydroxylase, C-terminal TRX-fold domain superfamily / Phenol hydroxylase, C-terminal dimerisation domain / D-Amino Acid Oxidase, subunit A, domain 2 / D-Amino Acid Oxidase; Chain A, domain 2 / FAD-binding domain / FAD binding domain / FAD/NAD(P)-binding domain / FAD/NAD(P)-binding domain / 3-Layer(bba) Sandwich / FAD/NAD(P)-binding domain superfamily / Glutaredoxin / Thioredoxin-like superfamily / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Alpha Beta

Component:

FLAVIN-ADENINE DINUCLEOTIDE / PHENOL / Phenol hydroxylase

• Biological species: Trichosporon cutaneum (fungus)
• Method: X-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 1.7 Å
• Authors: Enroth, C.

Citation

Journal: Acta Crystallogr.,Sect.D / Year: 2003
Title: High-resolution structure of phenol hydroxylase and correction of sequence errors.
Authors: Enroth, C.

#1: Journal: Structure / Year: 1998
Title: The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis
Authors: Enroth, C. / Neujahr, H. / Schneider, G. / Lindqvist, Y.

History

Deposition	Jun 12, 2003	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Sep 23, 2003	Provider: repository / Type: Initial release
Revision 1.1	Apr 29, 2008	Group: Version format compliance
Revision 1.2	Jul 13, 2011	Group: Advisory / Version format compliance
Revision 1.3	Jun 19, 2013	Group: Refinement description
Revision 1.4	Aug 16, 2023	Group: Data collection / Database references / Derived calculations / Refinement description Category: chem_comp_atom / chem_comp_bond / database_2 / diffrn_source / pdbx_initial_refinement_model / struct_ncs_dom_lim / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _diffrn_source.pdbx_synchrotron_site / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

• Remark 999: SEQUENCE ACCORDING TO THE AUTHOR, THE CONFLICTS REPRESENT ERRORS IN THE ORIGINAL DEPOSITED SEQUENCE.

Assembly

Deposited unit

A: Phenol 2-monooxygenase

B: Phenol 2-monooxygenase

C: Phenol 2-monooxygenase

D: Phenol 2-monooxygenase

hetero molecules

Summary:

• 305 kDa, 4 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	304,916	16
Polymers	301,255	4
Non-polymers	3,660	12
Water	48,424	2688

1

A: Phenol 2-monooxygenase

C: Phenol 2-monooxygenase

hetero molecules

Summary:

• defined by author&software
• 152 kDa, 2 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	152,458	8
Polymers	150,628	2
Non-polymers	1,830	6
Water	36	2

Symmetry operations:

Type	Name	Symmetry operation	Number
identity operation	1_555	x,y,z	1

Calculated values:

Buried area	7520 Å2
ΔGint	-35 kcal/mol
Surface area	47760 Å2
Method	PISA

2

B: Phenol 2-monooxygenase

D: Phenol 2-monooxygenase

hetero molecules

Summary:

• defined by author&software
• 152 kDa, 2 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	152,458	8
Polymers	150,628	2
Non-polymers	1,830	6
Water	36	2

Symmetry operations:

Type	Name	Symmetry operation	Number
identity operation	1_555	x,y,z	1

Calculated values:

Buried area	7520 Å2
ΔGint	-36 kcal/mol
Surface area	47590 Å2
Method	PISA

3

A: Phenol 2-monooxygenase

C: Phenol 2-monooxygenase

hetero molecules

B: Phenol 2-monooxygenase

D: Phenol 2-monooxygenase

hetero molecules

Summary:

• defined by software
• 305 kDa, 4 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	304,916	16
Polymers	301,255	4
Non-polymers	3,660	12
Water	72	4

Symmetry operations:

Type	Name	Symmetry operation	Number
identity operation	1_555	x,y,z	1
crystal symmetry operation	2_746	-x+2,y-1/2,-z+1	1

Calculated values:

Buried area	16360 Å2
ΔGint	-74 kcal/mol
Surface area	94020 Å2
Method	PISA

Unit cell

Length a, b, c (Å)	99.999, 150.948, 114.962
Angle α, β, γ (deg.)	90.00, 114.63, 90.00
Int Tables number	4
Space group name H-M	P1211

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	A
2	1	B
3	1	A
4	1	B
5	1	A
6	1	B
7	1	A
8	1	B
9	1	A
10	1	B
11	1	A
12	1	B
13	1	A
14	1	B
15	1	A
16	1	B
1	2	A
2	2	B
3	2	A
4	2	B
1	3	A
2	3	B
3	3	A
4	3	B
5	3	A
6	3	B
7	3	A
8	3	B
9	3	A
10	3	B
1	4	A
2	4	B
3	4	A
4	4	B
5	4	A
6	4	B
7	4	A
8	4	B
9	4	A
10	4	B
1	5	A
2	5	B
3	5	A
4	5	B
5	5	A
6	5	B
7	5	A
8	5	B
9	5	A
10	5	B
11	5	A
12	5	B
13	5	A
14	5	B
15	5	A
16	5	B
17	5	A
18	5	B
1	6	C
2	6	D
3	6	C
4	6	D
5	6	C
6	6	D
7	6	C
8	6	D
9	6	C
10	6	D
11	6	C
12	6	D
13	6	C
14	6	D
1	7	C
2	7	D
3	7	C
4	7	D
5	7	C
6	7	D
7	7	C
8	7	D
9	7	C
10	7	D
11	7	C
12	7	D
13	7	C
14	7	D
1	8	C
2	8	D
3	8	C
4	8	D
5	8	C
6	8	D
1	9	C
2	9	D
1	10	C
2	10	D
3	10	C
4	10	D
5	10	C
6	10	D
7	10	C
8	10	D
9	10	C
10	10	D
11	10	C
12	10	D
13	10	C
14	10	D
1	11	A
2	11	B
3	11	C
4	11	D
5	11	A
6	11	B
7	11	C
8	11	D
9	11	A
10	11	B
11	11	C
12	11	D
13	11	A
14	11	B
15	11	C
16	11	D
17	11	A
18	11	B
19	11	C
20	11	D
21	11	A
22	11	B
23	11	C
24	11	D
1	12	A
2	12	B
3	12	C
4	12	D
1	13	A
2	13	B
3	13	C
4	13	D
5	13	A
6	13	B
7	13	C
8	13	D
1	14	A
2	14	B
3	14	C
4	14	D
5	14	A
6	14	B
7	14	C
8	14	D
9	14	A
10	14	B
11	14	C
12	14	D
13	14	A
14	14	B
15	14	C
16	14	D
17	14	A
18	14	B
19	14	C
20	14	D
1	15	A
2	15	B
3	15	C
4	15	D
5	15	A
6	15	B
7	15	C
8	15	D
9	15	A
10	15	B
11	15	C
12	15	D
13	15	A
14	15	B
15	15	C
16	15	D
17	15	A
18	15	B
19	15	C
20	15	D
21	15	A
22	15	B
23	15	C
24	15	D
25	15	A
26	15	B
27	15	C
28	15	D
29	15	A
30	15	B
31	15	C
32	15	D
33	15	A
34	15	B
35	15	C
36	15	D
37	15	A
38	15	B
39	15	C
40	15	D
1	16	A
2	16	B
3	16	C
4	16	D
1	17	A
2	17	B
1	18	C
2	18	D
1	19	A
2	19	B
1	20	C
2	20	D
1	21	A
2	21	B
3	21	C
4	21	D
1	22	A
2	22	B
1	23	C
2	23	D
1	24	A
2	24	B
3	24	C
4	24	D
1	25	A
2	25	B
1	26	C
2	26	D
1	27	A
2	27	B
3	27	C
4	27	D
1	28	A
2	28	B
1	29	C
2	29	D
1	30	A
2	30	B
3	30	C
4	30	D
1	31	A
2	31	B
1	32	A
2	32	B
1	33	C
2	33	D
1	34	A
2	34	B
3	34	C
4	34	D
1	35	A
2	35	B
1	36	C
2	36	D
1	37	A
2	37	B
3	37	C
4	37	D
1	38	A
2	38	B
1	39	C
2	39	D

NCS domain segments:

Dom-ID	Component-ID	Ens-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Refine code	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	1	THR	THR	TYR	TYR	1	A	A	1 - 3	2 - 4
2	1	1	THR	THR	TYR	TYR	1	B	B	1 - 3	2 - 4
3	2	1	LYS	LYS	LYS	LYS	1	A	A	33 - 37	34 - 38
4	2	1	LYS	LYS	LYS	LYS	1	B	B	33 - 37	34 - 38
5	3	1	ARG	ARG	GLY	GLY	1	A	A	44 - 55	45 - 56
6	3	1	ARG	ARG	GLY	GLY	1	B	B	44 - 55	45 - 56
7	4	1	ASN	ASN	ASN	ASN	1	A	A	87	88
8	4	1	ASN	ASN	ASN	ASN	1	B	B	87	88
9	5	1	ARG	ARG	ARG	ARG	2	A	A	95	96
10	5	1	ARG	ARG	ARG	ARG	2	B	B	95	96
11	6	1	VAL	VAL	ASP	ASP	1	A	A	114 - 126	115 - 127
12	6	1	VAL	VAL	ASP	ASP	1	B	B	114 - 126	115 - 127
13	7	1	ASP	ASP	GLU	GLU	1	A	A	133 - 145	134 - 146
14	7	1	ASP	ASP	GLU	GLU	1	B	B	133 - 145	134 - 146
15	8	1	ARG	ARG	SER	SER	1	A	A	167 - 170	168 - 171
16	8	1	ARG	ARG	SER	SER	1	B	B	167 - 170	168 - 171
1	1	2	GLY	GLY	GLU	GLU	1	A	A	180 - 212	181 - 213
2	1	2	GLY	GLY	GLU	GLU	1	B	B	180 - 212	181 - 213
3	2	2	HIS	HIS	PHE	PHE	1	A	A	228 - 237	229 - 238
4	2	2	HIS	HIS	PHE	PHE	1	B	B	228 - 237	229 - 238
1	1	3	THR	THR	ILE	ILE	1	A	A	244 - 247	245 - 248
2	1	3	THR	THR	ILE	ILE	1	B	B	244 - 247	245 - 248
3	2	3	LEU	LEU	LEU	LEU	2	A	A	292	293
4	2	3	LEU	LEU	LEU	LEU	2	B	B	292	293
5	3	3	VAL	VAL	ALA	ALA	2	A	A	312 - 314	313 - 315
6	3	3	VAL	VAL	ALA	ALA	2	B	B	312 - 314	313 - 315
7	4	3	ALA	ALA	PHE	PHE	1	A	A	316 - 320	317 - 321
8	4	3	ALA	ALA	PHE	PHE	1	B	B	316 - 320	317 - 321
9	5	3	TYR	TYR	TYR	TYR	2	A	A	323 - 336	324 - 337
10	5	3	TYR	TYR	TYR	TYR	2	B	B	323 - 336	324 - 337
1	1	4	ILE	ILE	GLN	GLN	1	A	A	338 - 340	339 - 341
2	1	4	ILE	ILE	GLN	GLN	1	B	B	338 - 340	339 - 341
3	2	4	VAL	VAL	THR	THR	1	A	A	342 - 343	343 - 344
4	2	4	VAL	VAL	THR	THR	1	B	B	342 - 343	343 - 344
5	3	4	LYS	LYS	LYS	LYS	2	A	A	345	346
6	3	4	LYS	LYS	LYS	LYS	2	B	B	345	346
7	4	4	ALA	ALA	THR	THR	1	A	A	366 - 372	367 - 373
8	4	4	ALA	ALA	THR	THR	1	B	B	366 - 372	367 - 373
9	5	4	ALA	ALA	ALA	ALA	2	A	A	427	428
10	5	4	ALA	ALA	ALA	ALA	2	B	B	427	428
1	1	5	VAL	VAL	VAL	VAL	1	A	A	436	437
2	1	5	VAL	VAL	VAL	VAL	1	B	B	436	437
3	2	5	GLU	GLU	GLU	GLU	1	A	A	461	462
4	2	5	GLU	GLU	GLU	GLU	1	B	B	461	462
5	3	5	LYS	LYS	LYS	LYS	1	A	A	468	469
6	3	5	LYS	LYS	LYS	LYS	1	B	B	468	469
7	4	5	ARG	ARG	ARG	ARG	2	A	A	544	545
8	4	5	ARG	ARG	ARG	ARG	2	B	B	544	545
9	5	5	GLN	GLN	GLN	GLN	1	A	A	604	605
10	5	5	GLN	GLN	GLN	GLN	1	B	B	604	605
11	6	5	GLU	GLU	THR	THR	1	A	A	610 - 611	611 - 612
12	6	5	GLU	GLU	THR	THR	1	B	B	610 - 611	611 - 612
13	7	5	GLU	GLU	ASP	ASP	1	A	A	635 - 637	636 - 638
14	7	5	GLU	GLU	ASP	ASP	1	B	B	635 - 637	636 - 638
15	8	5	PRO	PRO	GLU	GLU	1	A	A	647 - 649	648 - 650
16	8	5	PRO	PRO	GLU	GLU	1	B	B	647 - 649	648 - 650
17	9	5	SER	SER	THR	THR	1	A	A	651 - 655	652 - 656
18	9	5	SER	SER	THR	THR	1	B	B	651 - 655	652 - 656
1	1	6	THR	THR	TYR	TYR	1	C	C	1 - 3	2 - 4
2	1	6	THR	THR	TYR	TYR	1	D	D	1 - 3	2 - 4
3	2	6	LYS	LYS	LYS	LYS	1	C	C	33 - 37	34 - 38
4	2	6	LYS	LYS	LYS	LYS	1	D	D	33 - 37	34 - 38
5	3	6	ARG	ARG	GLY	GLY	1	C	C	44 - 55	45 - 56
6	3	6	ARG	ARG	GLY	GLY	1	D	D	44 - 55	45 - 56
7	4	6	ASN	ASN	PRO	PRO	1	C	C	87 - 88	88 - 89
8	4	6	ASN	ASN	PRO	PRO	1	D	D	87 - 88	88 - 89
9	5	6	VAL	VAL	ASP	ASP	1	C	C	114 - 126	115 - 127
10	5	6	VAL	VAL	ASP	ASP	1	D	D	114 - 126	115 - 127
11	6	6	ASP	ASP	LYS	LYS	1	C	C	133 - 146	134 - 147
12	6	6	ASP	ASP	LYS	LYS	1	D	D	133 - 146	134 - 147
13	7	6	ARG	ARG	PRO	PRO	1	C	C	167 - 205	168 - 206
14	7	6	ARG	ARG	PRO	PRO	1	D	D	167 - 205	168 - 206
1	1	7	ALA	ALA	GLU	GLU	1	C	C	210 - 212	211 - 213
2	1	7	ALA	ALA	GLU	GLU	1	D	D	210 - 212	211 - 213
3	2	7	HIS	HIS	PHE	PHE	1	C	C	228 - 237	229 - 238
4	2	7	HIS	HIS	PHE	PHE	1	D	D	228 - 237	229 - 238
5	3	7	THR	THR	ILE	ILE	1	C	C	244 - 247	245 - 248
6	3	7	THR	THR	ILE	ILE	1	D	D	244 - 247	245 - 248
7	4	7	GLU	GLU	GLU	GLU	1	C	C	272	273
8	4	7	GLU	GLU	GLU	GLU	1	D	D	272	273
9	5	7	LEU	LEU	LEU	LEU	2	C	C	292	293
10	5	7	LEU	LEU	LEU	LEU	2	D	D	292	293
11	6	7	VAL	VAL	LYS	LYS	1	C	C	302 - 317	303 - 318
12	6	7	VAL	VAL	LYS	LYS	1	D	D	302 - 317	303 - 318
13	7	7	ILE	ILE	TYR	TYR	1	C	C	319 - 336	320 - 337
14	7	7	ILE	ILE	TYR	TYR	1	D	D	319 - 336	320 - 337
1	1	8	ILE	ILE	LYS	LYS	1	C	C	338 - 345	339 - 346
2	1	8	ILE	ILE	LYS	LYS	1	D	D	338 - 345	339 - 346
3	2	8	ALA	ALA	THR	THR	1	C	C	366 - 372	367 - 373
4	2	8	ALA	ALA	THR	THR	1	D	D	366 - 372	367 - 373
5	3	8	ALA	ALA	ALA	ALA	1	C	C	427	428
6	3	8	ALA	ALA	ALA	ALA	1	D	D	427	428
1	1	9	LYS	LYS	MET	MET	2	C	C	428 - 434	429 - 435
2	1	9	LYS	LYS	MET	MET	2	D	D	428 - 434	429 - 435
1	1	10	GLY	GLY	VAL	VAL	1	C	C	435 - 436	436 - 437
2	1	10	GLY	GLY	VAL	VAL	1	D	D	435 - 436	436 - 437
3	2	10	GLU	GLU	GLU	GLU	1	C	C	461	462
4	2	10	GLU	GLU	GLU	GLU	1	D	D	461	462
5	3	10	LYS	LYS	LYS	LYS	1	C	C	468	469
6	3	10	LYS	LYS	LYS	LYS	1	D	D	468	469
7	4	10	ASP	ASP	ASP	ASP	1	C	C	593	594
8	4	10	ASP	ASP	ASP	ASP	1	D	D	593	594
9	5	10	THR	THR	THR	THR	1	C	C	611	612
10	5	10	THR	THR	THR	THR	1	D	D	611	612
11	6	10	ILE	ILE	ILE	ILE	2	C	C	636	637
12	6	10	ILE	ILE	ILE	ILE	2	D	D	636	637
13	7	10	SER	SER	GLN	GLN	1	C	C	651 - 654	652 - 655
14	7	10	SER	SER	GLN	GLN	1	D	D	651 - 654	652 - 655
1	1	11	SER	SER	GLN	GLN	1	A	A	4 - 32	5 - 33
2	1	11	SER	SER	GLN	GLN	1	B	B	4 - 32	5 - 33
3	1	11	SER	SER	GLN	GLN	1	C	C	4 - 32	5 - 33
4	1	11	SER	SER	GLN	GLN	1	D	D	4 - 32	5 - 33
5	2	11	VAL	VAL	LYS	LYS	1	A	A	38 - 43	39 - 44
6	2	11	VAL	VAL	LYS	LYS	1	B	B	38 - 43	39 - 44
7	2	11	VAL	VAL	LYS	LYS	1	C	C	38 - 43	39 - 44
8	2	11	VAL	VAL	LYS	LYS	1	D	D	38 - 43	39 - 44
9	3	11	LEU	LEU	TYR	TYR	1	A	A	56 - 86	57 - 87
10	3	11	LEU	LEU	TYR	TYR	1	B	B	56 - 86	57 - 87
11	3	11	LEU	LEU	TYR	TYR	1	C	C	56 - 86	57 - 87
12	3	11	LEU	LEU	TYR	TYR	1	D	D	56 - 86	57 - 87
13	4	11	ARG	ARG	VAL	VAL	1	A	A	96 - 113	97 - 114
14	4	11	ARG	ARG	VAL	VAL	1	B	B	96 - 113	97 - 114
15	4	11	ARG	ARG	VAL	VAL	1	C	C	96 - 113	97 - 114
16	4	11	ARG	ARG	VAL	VAL	1	D	D	96 - 113	97 - 114
17	5	11	SER	SER	SER	SER	1	A	A	127 - 132	128 - 133
18	5	11	SER	SER	SER	SER	1	B	B	127 - 132	128 - 133
19	5	11	SER	SER	SER	SER	1	C	C	127 - 132	128 - 133
20	5	11	SER	SER	SER	SER	1	D	D	127 - 132	128 - 133
21	6	11	MET	MET	LEU	LEU	1	A	A	147 - 166	148 - 167
22	6	11	MET	MET	LEU	LEU	1	B	B	147 - 166	148 - 167
23	6	11	MET	MET	LEU	LEU	1	C	C	147 - 166	148 - 167
24	6	11	MET	MET	LEU	LEU	1	D	D	147 - 166	148 - 167
1	1	12	ILE	ILE	GLY	GLY	1	A	A	213 - 227	214 - 228
2	1	12	ILE	ILE	GLY	GLY	1	B	B	213 - 227	214 - 228
3	1	12	ILE	ILE	GLY	GLY	1	C	C	213 - 227	214 - 228
4	1	12	ILE	ILE	GLY	GLY	1	D	D	213 - 227	214 - 228
1	1	13	TRP	TRP	ALA	ALA	1	A	A	248 - 271	249 - 272
2	1	13	TRP	TRP	ALA	ALA	1	B	B	248 - 271	249 - 272
3	1	13	TRP	TRP	ALA	ALA	1	C	C	248 - 271	249 - 272
4	1	13	TRP	TRP	ALA	ALA	1	D	D	248 - 271	249 - 272
5	2	13	SER	SER	GLN	GLN	1	A	A	273 - 291	274 - 292
6	2	13	SER	SER	GLN	GLN	1	B	B	273 - 291	274 - 292
7	2	13	SER	SER	GLN	GLN	1	C	C	273 - 291	274 - 292
8	2	13	SER	SER	GLN	GLN	1	D	D	273 - 291	274 - 292
1	1	14	PHE	PHE	LYS	LYS	1	A	A	346 - 365	347 - 366
2	1	14	PHE	PHE	LYS	LYS	1	B	B	346 - 365	347 - 366
3	1	14	PHE	PHE	LYS	LYS	1	C	C	346 - 365	347 - 366
4	1	14	PHE	PHE	LYS	LYS	1	D	D	346 - 365	347 - 366
5	2	14	SER	SER	PRO	PRO	1	A	A	373 - 426	374 - 427
6	2	14	SER	SER	PRO	PRO	1	B	B	373 - 426	374 - 427
7	2	14	SER	SER	PRO	PRO	1	C	C	373 - 426	374 - 427
8	2	14	SER	SER	PRO	PRO	1	D	D	373 - 426	374 - 427
9	3	14	SER	SER	LYS	LYS	1	A	A	437 - 442	438 - 443
10	3	14	SER	SER	LYS	LYS	1	B	B	437 - 442	438 - 443
11	3	14	SER	SER	LYS	LYS	1	C	C	437 - 442	438 - 443
12	3	14	SER	SER	LYS	LYS	1	D	D	437 - 442	438 - 443
13	4	14	ALA	ALA	ASP	ASP	1	A	A	444 - 460	445 - 461
14	4	14	ALA	ALA	ASP	ASP	1	B	B	444 - 460	445 - 461
15	4	14	ALA	ALA	ASP	ASP	1	C	C	444 - 460	445 - 461
16	4	14	ALA	ALA	ASP	ASP	1	D	D	444 - 460	445 - 461
17	5	14	ASN	ASN	LYS	LYS	1	A	A	462 - 467	463 - 468
18	5	14	ASN	ASN	LYS	LYS	1	B	B	462 - 467	463 - 468
19	5	14	ASN	ASN	LYS	LYS	1	C	C	462 - 467	463 - 468
20	5	14	ASN	ASN	LYS	LYS	1	D	D	462 - 467	463 - 468
1	1	15	SER	SER	ALA	ALA	1	A	A	469 - 475	470 - 476
2	1	15	SER	SER	ALA	ALA	1	B	B	469 - 475	470 - 476
3	1	15	SER	SER	ALA	ALA	1	C	C	469 - 475	470 - 476
4	1	15	SER	SER	ALA	ALA	1	D	D	469 - 475	470 - 476
5	2	15	ASN	ASN	LYS	LYS	1	A	A	477 - 529	478 - 530
6	2	15	ASN	ASN	LYS	LYS	1	B	B	477 - 529	478 - 530
7	2	15	ASN	ASN	LYS	LYS	1	C	C	477 - 529	478 - 530
8	2	15	ASN	ASN	LYS	LYS	1	D	D	477 - 529	478 - 530
9	3	15	PHE	PHE	SER	SER	1	A	A	531 - 543	532 - 544
10	3	15	PHE	PHE	SER	SER	1	B	B	531 - 543	532 - 544
11	3	15	PHE	PHE	SER	SER	1	C	C	531 - 543	532 - 544
12	3	15	PHE	PHE	SER	SER	1	D	D	531 - 543	532 - 544
13	4	15	TYR	TYR	CYS	CYS	1	A	A	545 - 592	546 - 593
14	4	15	TYR	TYR	CYS	CYS	1	B	B	545 - 592	546 - 593
15	4	15	TYR	TYR	CYS	CYS	1	C	C	545 - 592	546 - 593
16	4	15	TYR	TYR	CYS	CYS	1	D	D	545 - 592	546 - 593
17	5	15	SER	SER	PRO	PRO	1	A	A	594 - 600	595 - 601
18	5	15	SER	SER	PRO	PRO	1	B	B	594 - 600	595 - 601
19	5	15	SER	SER	PRO	PRO	1	C	C	594 - 600	595 - 601
20	5	15	SER	SER	PRO	PRO	1	D	D	594 - 600	595 - 601
21	6	15	SER	SER	TYR	TYR	1	A	A	602 - 603	603 - 604
22	6	15	SER	SER	TYR	TYR	1	B	B	602 - 603	603 - 604
23	6	15	SER	SER	TYR	TYR	1	C	C	602 - 603	603 - 604
24	6	15	SER	SER	TYR	TYR	1	D	D	602 - 603	603 - 604
25	7	15	ALA	ALA	ASP	ASP	1	A	A	605 - 609	606 - 610
26	7	15	ALA	ALA	ASP	ASP	1	B	B	605 - 609	606 - 610
27	7	15	ALA	ALA	ASP	ASP	1	C	C	605 - 609	606 - 610
28	7	15	ALA	ALA	ASP	ASP	1	D	D	605 - 609	606 - 610
29	8	15	GLY	GLY	ALA	ALA	1	A	A	613 - 634	614 - 635
30	8	15	GLY	GLY	ALA	ALA	1	B	B	613 - 634	614 - 635
31	8	15	GLY	GLY	ALA	ALA	1	C	C	613 - 634	614 - 635
32	8	15	GLY	GLY	ALA	ALA	1	D	D	613 - 634	614 - 635
33	9	15	TYR	TYR	GLU	GLU	1	A	A	639 - 646	640 - 647
34	9	15	TYR	TYR	GLU	GLU	1	B	B	639 - 646	640 - 647
35	9	15	TYR	TYR	GLU	GLU	1	C	C	639 - 646	640 - 647
36	9	15	TYR	TYR	GLU	GLU	1	D	D	639 - 646	640 - 647
37	10	15	ALA	ALA	THR	THR	2	A	A	657 - 660	658 - 661
38	10	15	ALA	ALA	THR	THR	2	B	B	657 - 660	658 - 661
39	10	15	ALA	ALA	THR	THR	2	C	C	657 - 660	658 - 661
40	10	15	ALA	ALA	THR	THR	2	D	D	657 - 660	658 - 661
1	1	16	HOH	HOH	HOH	HOH	1	A	Q	6013 - 6044
2	1	16	HOH	HOH	HOH	HOH	1	B	R	668 - 699
3	1	16	HOH	HOH	HOH	HOH	1	C	S	6035 - 6066
4	1	16	HOH	HOH	HOH	HOH	1	D	T	6053 - 6084
1	1	17	HOH	HOH	HOH	HOH	1	A	Q	6045 - 6118
2	1	17	HOH	HOH	HOH	HOH	1	B	R	700 - 773
1	1	18	HOH	HOH	HOH	HOH	1	C	S	6067 - 6128
2	1	18	HOH	HOH	HOH	HOH	1	D	T	6085 - 6146
1	1	19	HOH	HOH	HOH	HOH	1	A	Q	6130 - 6146
2	1	19	HOH	HOH	HOH	HOH	1	B	R	777 - 793
1	1	20	HOH	HOH	HOH	HOH	1	C	S	6138 - 6151
2	1	20	HOH	HOH	HOH	HOH	1	D	T	6149 - 6162
1	1	21	HOH	HOH	HOH	HOH	1	A	Q	6151 - 6333
2	1	21	HOH	HOH	HOH	HOH	1	B	R	795 - 977
3	1	21	HOH	HOH	HOH	HOH	1	C	S	6155 - 6336
4	1	21	HOH	HOH	HOH	HOH	1	D	T	6164 - 6344
1	1	22	HOH	HOH	HOH	HOH	1	A	Q	6334 - 6379
2	1	22	HOH	HOH	HOH	HOH	1	B	R	978 - 1023
1	1	23	HOH	HOH	HOH	HOH	1	C	S	6337 - 6400
2	1	23	HOH	HOH	HOH	HOH	1	D	T	6345 - 6407
1	1	24	HOH	HOH	HOH	HOH	1	A	Q	6399 - 6413
2	1	24	HOH	HOH	HOH	HOH	1	B	R	1053 - 1067
3	1	24	HOH	HOH	HOH	HOH	1	C	S	6434 - 6448
4	1	24	HOH	HOH	HOH	HOH	1	D	T	6458 - 6472
1	1	25	HOH	HOH	HOH	HOH	1	A	Q	6414 - 6432
2	1	25	HOH	HOH	HOH	HOH	1	B	R	1068 - 1086
1	1	26	HOH	HOH	HOH	HOH	1	C	S	6449 - 6466
2	1	26	HOH	HOH	HOH	HOH	1	D	T	6473 - 6490
1	1	27	HOH	HOH	HOH	HOH	1	A	Q	6441 - 6499
2	1	27	HOH	HOH	HOH	HOH	1	B	R	1094 - 1152
3	1	27	HOH	HOH	HOH	HOH	1	C	S	6472 - 6530
4	1	27	HOH	HOH	HOH	HOH	1	D	T	6493 - 6551
1	1	28	HOH	HOH	HOH	HOH	1	A	Q	6500 - 6522
2	1	28	HOH	HOH	HOH	HOH	1	B	R	1153 - 1175
1	1	29	HOH	HOH	HOH	HOH	1	C	S	6531 - 6544
2	1	29	HOH	HOH	HOH	HOH	1	D	T	6552 - 6565
1	1	30	HOH	HOH	HOH	HOH	1	A	Q	6528 - 6540
2	1	30	HOH	HOH	HOH	HOH	1	B	R	1201 - 1213
3	1	30	HOH	HOH	HOH	HOH	1	C	S	6568 - 6580
4	1	30	HOH	HOH	HOH	HOH	1	D	T	6571 - 6583
1	1	31	HOH	HOH	HOH	HOH	1	A	Q	6541 - 6556
2	1	31	HOH	HOH	HOH	HOH	1	B	R	1214 - 1229
1	1	32	HOH	HOH	HOH	HOH	1	A	Q	6541 - 6556
2	1	32	HOH	HOH	HOH	HOH	1	B	R	1214 - 1229
1	1	33	HOH	HOH	HOH	HOH	1	C	S	6581 - 6597
2	1	33	HOH	HOH	HOH	HOH	1	D	T	6584 - 6600
1	1	34	CL	CL	HOH	HOH	1	A	E - Q	6001 - 6584
2	1	34	CL	CL	HOH	HOH	1	B	H - R	6002 - 1253
3	1	34	CL	CL	HOH	HOH	1	C	K - S	6003 - 6623
4	1	34	CL	CL	HOH	HOH	1	D	N - T	6004 - 6625
1	1	35	HOH	HOH	HOH	HOH	1	A	Q	6585 - 6593
2	1	35	HOH	HOH	HOH	HOH	1	B	R	1254 - 1262
1	1	36	HOH	HOH	HOH	HOH	1	C	S	6624 - 6632
2	1	36	HOH	HOH	HOH	HOH	1	D - B	T - R	6626 - 2618
1	1	37	HOH	HOH	HOH	HOH	1	A	Q	6596 - 6638
2	1	37	HOH	HOH	HOH	HOH	1	B	R	1264 - 1308
3	1	37	HOH	HOH	HOH	HOH	1	C	S	6635 - 6676
4	1	37	HOH	HOH	HOH	HOH	1	D	T	6634 - 6677
1	1	38	HOH	HOH	HOH	HOH	1	A	Q	6639 - 6670
2	1	38	HOH	HOH	HOH	HOH	1	B	R	1309 - 1340
1	1	39	HOH	HOH	HOH	HOH	1	C	S	6677 - 6695
2	1	39	HOH	HOH	HOH	HOH	1	D	T	6678 - 6696

NCS ensembles :

ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16
17
18
19
20
21
22
23
24
25
26
27
28
29
30
31
32
33
34
35
36
37
38
39

• Details: A dimer is the biologically active unit (the asymmetric unit contains two dimers)

Components

#1: Protein

A B C D
Phenol 2-monooxygenase / / Phenol hydroxylase

Details:

Mass: 75313.852 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Trichosporon cutaneum (fungus) / Production host: Escherichia coli (E. coli) / References: UniProt: P15245, phenol 2-monooxygenase (NADPH)

#2: Chemical

A-6001 B-6002 C-6003 D-6004
ChemComp-CL / CHLORIDE ION / Chloride

Details:

Mass: 35.453 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Cl

#3: Chemical

A-6011 B-6021 C-6031 D-6041
ChemComp-FAD / FLAVIN-ADENINE DINUCLEOTIDE / Flavin adenine dinucleotide

Details:

Mass: 785.550 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₂₇H₃₃N₉O₁₅P₂ / Comment: FAD*YM

#4: Chemical

A-6012 B-6022 C-6032 D-6042
ChemComp-IPH / PHENOL / Phenol

Details:

Mass: 94.111 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₆H₆O

#5: Water

ChemComp-HOH / water / Water

Details:

Mass: 18.015 Da / Num. of mol.: 2688 / Source method: isolated from a natural source / Formula: H₂O

Experimental details

Experiment

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

Sample preparation

• Crystal: Density Matthews: 2.62 ų/Da / Density % sol: 53 %
• Crystal grow: Temperature: 4 ℃ / pH: 8.5 / Method: vapor diffusion, hanging drop / Details: Enroth, C., (1994) J.Mol.Biol., 238, 128.

Components of the solutions

ID	Conc.	Common name	Crystal-ID	Sol-ID	Details
1	20 mg/ml	enzyme	1	drop
2	20 mM	phenol	1	drop
3	120 mM	Tris-HCl	1	reservoir	or 0.21M KCl and 16% PEG4000
4	0.52 M	ammonium acetate	1	reservoir

Data collection

• Diffraction: Mean temperature: 100 K
• Diffraction source: Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: BW7B / Wavelength: 0.8452 Å
• Detector: Type: MARRESEARCH / Detector: AREA DETECTOR / Date: Jun 17, 2001
• Radiation: Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
• Radiation wavelength: Wavelength: 0.8452 Å / Relative weight: 1
• Reflection: Resolution: 1.68→20 Å / Num. all: 297900 / Num. obs: 297900 / % possible obs: 83.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 2.1 % / B_iso Wilson estimate: 22.3 Ų / R_sym value: 0.024 / Net I/σ(I): 23
• Reflection shell: Resolution: 1.68→1.7 Å / Redundancy: 0.77 % / Mean I/σ(I) obs: 2.2 / Num. unique all: 3440 / R_sym value: 0.256 / % possible all: 38.7
• Reflection: R_merge(I) obs: 0.033
• Reflection shell: Lowest resolution: 1.69 Å / % possible obs: 38.7 % / Num. unique obs: 3440 / R_merge(I) obs: 0.256

Processing

Software

Name	Version	Classification
REFMAC	5	refinement
DENZO		data reduction
SCALEPACK		data scaling

Refinement

Method to determine structure: FOURIER SYNTHESIS
Starting model: PDB ID ENTRY 1FOH

1foh

Resolution: 1.7→19.96 Å / Cor.coef. F_o:F_c: 0.974 / Cor.coef. F_o:F_c free: 0.965 / SU B: 1.943 / SU ML: 0.062 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.103 / ESU R Free: 0.096 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	Rfactor	Num. reflection	% reflection	Selection details
Rfree	0.17988	14783	5.1 %	RANDOM
Rwork	0.15698	-	-	-
all	0.15816	277056	-	-
obs	0.15698	277056	86.12 %	-

• 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: 12.127 Ų

	Baniso -1	Baniso -2	Baniso -3
1-	2.8 Å2	0 Å2	0.93 Å2
2-	-	-3.21 Å2	0 Å2
3-	-	-	1.18 Å2

Refinement step

Cycle: LAST / Resolution: 1.7→19.96 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	20840	0	244	2688	23772

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.012	0.021	21514
X-RAY DIFFRACTION	r_angle_refined_deg	1.389	1.953	29132
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	4.403	3	2604
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	15.765	15	3878
X-RAY DIFFRACTION	r_chiral_restr	0.102	0.2	3128
X-RAY DIFFRACTION	r_gen_planes_refined	0.006	0.02	16424
X-RAY DIFFRACTION	r_nbd_refined	0.203	0.3	10468
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.141	0.5	2943
X-RAY DIFFRACTION	r_symmetry_vdw_refined	0.277	0.3	43
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.226	0.5	26
X-RAY DIFFRACTION	r_mcbond_it	1.074	1.5	12992
X-RAY DIFFRACTION	r_mcangle_it	1.79	2	21000
X-RAY DIFFRACTION	r_scbond_it	2.793	3	8522
X-RAY DIFFRACTION	r_scangle_it	4.417	4.5	8132

Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-ID	Dom-ID	Auth asym-ID	Number	Type	Rms dev position (Å)	Weight position
1	1	A	436	tight positional	0.04	0.05
2	1	A	783	tight positional	0.02	0.05
3	1	A	1016	tight positional	0.02	0.05
4	1	A	1110	tight positional	0.01	0.05
5	1	A	1252	tight positional	0.02	0.05
6	1	C	1976	tight positional	0.02	0.05
7	1	C	2424	tight positional	0.01	0.05
8	1	C	2538	tight positional	0.01	0.05
9	1	C	2592	tight positional	0	0.05
10	1	C	2668	tight positional	0.01	0.05
11	1	A	3512	tight positional	0.03	0.05
11	2	B	3512	tight positional	0.04	0.05
11	3	C	3512	tight positional	0.03	0.05
11	4	D	3512	tight positional	0.02	0.05
12	1	A	3621	tight positional	0.01	0.05
12	2	B	3621	tight positional	0.01	0.05
12	3	C	3621	tight positional	0.01	0.05
12	4	D	3621	tight positional	0.01	0.05
13	1	A	3958	tight positional	0.01	0.05
13	2	B	3958	tight positional	0.01	0.05
13	3	C	3958	tight positional	0.01	0.05
13	4	D	3958	tight positional	0.01	0.05
14	1	A	4785	tight positional	0.02	0.05
14	2	B	4785	tight positional	0.02	0.05
14	3	C	4785	tight positional	0.02	0.05
14	4	D	4785	tight positional	0.01	0.05
15	1	A	6130	tight positional	0.02	0.05
15	2	B	6130	tight positional	0.02	0.05
15	3	C	6130	tight positional	0.02	0.05
15	4	D	6130	tight positional	0.02	0.05
16	1	A	6162	tight positional	0.01	0.05
16	2	B	6162	tight positional	0	0.05
16	3	C	6162	tight positional	0	0.05
16	4	D	6162	tight positional	0.01	0.05
17	1	A	6236	tight positional	0.01	0.05
18	18	A	6298	tight positional	0	0.05
19	1	A	6315	tight positional	0	0.05
20	20	A	6329	tight positional	0	0.05
21	1	A	6512	tight positional	0.01	0.05
21	2	B	6512	tight positional	0.01	0.05
21	3	C	6512	tight positional	0.01	0.05
21	4	D	6512	tight positional	0.01	0.05
22	1	A	6558	tight positional	0	0.05
23	23	A	6623	tight positional	0.01	0.05
24	1	A	6638	tight positional	0	0.05
24	2	B	6638	tight positional	0.01	0.05
24	3	C	6638	tight positional	0	0.05
24	4	D	6638	tight positional	0	0.05
25	1	A	6657	tight positional	0	0.05
26	26	A	6675	tight positional	0	0.05
27	1	A	6734	tight positional	0.01	0.05
27	2	B	6734	tight positional	0.01	0.05
27	3	C	6734	tight positional	0.01	0.05
27	4	D	6734	tight positional	0	0.05
28	1	A	6757	tight positional	0	0.05
29	29	B	6771	tight positional	0	0.05
30	1	A	6784	tight positional	0	0.05
30	2	B	6784	tight positional	0	0.05
30	3	C	6784	tight positional	0	0.05
30	4	D	6784	tight positional	0	0.05
31	31	C	6800	tight positional	0	0.05
32	32	D	6816	tight positional	0	0.05
33	33	A	6833	tight positional	0	0.05
34	1	A	6858	tight positional	0	0.05
34	2	B	6858	tight positional	0	0.05
34	3	C	6858	tight positional	0	0.05
34	4	D	6858	tight positional	0	0.05
35	2	B	6867	tight positional	0	0.05
36	1	C	6877	tight positional	0	0.05
37	1	A	6922	tight positional	0	0.05
37	2	B	6922	tight positional	0	0.05
37	3	C	6922	tight positional	0	0.05
37	4	D	6922	tight positional	0	0.05
38	1	A	6954	tight positional	0	0.05
39	39	A	6973	tight positional	0	0.05
1	1	A	436	tight thermal	0.2	0.5
2	1	A	783	tight thermal	1.27	0.5
3	1	A	1016	tight thermal	2.8	0.5
4	1	A	1110	tight thermal	3.96	0.5
5	1	A	1252	tight thermal	4.44	0.5
6	1	C	1976	tight thermal	3.75	0.5
7	1	C	2424	tight thermal	3.1	0.5
8	1	C	2538	tight thermal	2.76	0.5
9	1	C	2592	tight thermal	2.58	0.5
10	1	C	2668	tight thermal	2.45	0.5
11	1	A	3512	tight thermal	2.09	0.5
11	2	B	3512	tight thermal	0.18	0.5
11	3	C	3512	tight thermal	0.11	0.5
11	4	D	3512	tight thermal	0.11	0.5
12	1	A	3621	tight thermal	1.9	0.5
12	2	B	3621	tight thermal	0.55	0.5
12	3	C	3621	tight thermal	0.44	0.5
12	4	D	3621	tight thermal	0.43	0.5
13	1	A	3958	tight thermal	1.73	0.5
13	2	B	3958	tight thermal	0.93	0.5
13	3	C	3958	tight thermal	0.83	0.5
13	4	D	3958	tight thermal	0.83	0.5
14	1	A	4785	tight thermal	1.5	0.5
14	2	B	4785	tight thermal	1.11	0.5
14	3	C	4785	tight thermal	1.04	0.5
14	4	D	4785	tight thermal	1.04	0.5
15	1	A	6130	tight thermal	1.24	0.5
15	2	B	6130	tight thermal	1.07	0.5
15	3	C	6130	tight thermal	1.04	0.5
15	4	D	6130	tight thermal	1.03	0.5
16	1	A	6162	tight thermal	1.12	0.5
16	2	B	6162	tight thermal	1.04	0.5
16	3	C	6162	tight thermal	1.02	0.5
16	4	D	6162	tight thermal	1.02	0.5
17	1	A	6236	tight thermal	1.06	0.5
18	18	B	6298	tight thermal	1.02	0.5
19	19	C	6315	tight thermal	1.01	0.5
20	2	D	6329	tight thermal	1	0.5
21	1	A	6512	tight thermal	0.98	0.5
21	2	B	6512	tight thermal	1	0.5
21	3	C	6512	tight thermal	0.99	0.5
21	4	D	6512	tight thermal	0.99	0.5
22	1	A	6558	tight thermal	0.96	0.5
23	23	B	6623	tight thermal	0.95	0.5
24	1	A	6638	tight thermal	0.95	0.5
24	2	B	6638	tight thermal	0.97	0.5
24	3	C	6638	tight thermal	0.96	0.5
24	4	D	6638	tight thermal	0.96	0.5
25	1	A	6657	tight thermal	0.94	0.5
26	26	B	6675	tight thermal	0.94	0.5
27	1	A	6734	tight thermal	0.93	0.5
27	2	B	6734	tight thermal	0.95	0.5
27	3	C	6734	tight thermal	0.95	0.5
27	4	D	6734	tight thermal	0.95	0.5
28	1	A	6757	tight thermal	0.93	0.5
29	29	B	6771	tight thermal	0.92	0.5
30	1	A	6784	tight thermal	0.92	0.5
30	2	B	6784	tight thermal	0.93	0.5
30	3	C	6784	tight thermal	0.93	0.5
30	4	D	6784	tight thermal	0.93	0.5
31	1	A	6800	tight thermal	0.92	0.5
32	2	B	6816	tight thermal	0.92	0.5
33	33	A	6833	tight thermal	0.91	0.5
34	1	A	6858	tight thermal	0.91	0.5
34	2	B	6858	tight thermal	0.92	0.5
34	3	C	6858	tight thermal	0.92	0.5
34	4	D	6858	tight thermal	0.92	0.5
35	1	A	6867	tight thermal	0.91	0.5
36	36	B	6877	tight thermal	0.91	0.5
37	1	A	6922	tight thermal	0.9	0.5
37	2	B	6922	tight thermal	0.91	0.5
37	3	C	6922	tight thermal	0.91	0.5
37	4	D	6922	tight thermal	0.91	0.5
38	1	A	6954	tight thermal	0.9	0.5
39	39	B	6973	tight thermal	0.9	0.5

LS refinement shell

Resolution: 1.7→1.744 Å / Total num. of bins used: 20

	Rfactor	Num. reflection
Rfree	0.278	600
Rwork	0.235	11207
obs	-	11207

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	0.9845	-0.1515	-0.0032	0.4967	-0.0295	2.0869	-0.0523	0.1831	-0.0932	-0.1449	-0.0519	-0.0532	0.1472	0.1157	0.1041	0.104	0.0127	0.0151	0.6959	-0.037	0.0787	60.974	45.334	19.22
2	4.5132	-3.0868	-0.9303	5.1788	3.1625	3.8366	0.0785	0.1714	-0.2809	0.1749	-0.2294	0.3295	0.1622	-0.2949	0.1508	0.0423	-0.0603	0.0022	0.6631	-0.0351	0.0527	40.002	45.575	36.287
3	0.9653	0.1085	-0.2498	0.5279	-0.048	1.0561	0.0239	-0.138	0.0889	0.0448	-0.0226	-0.1213	-0.2125	0.5284	-0.0013	0.0725	-0.1561	-0.0508	0.8256	-0.0239	0.1176	73.548	72.935	47.982
4	0.8739	0.3831	-0.9307	0.8108	-0.6001	2.0951	-0.1254	-0.1213	-0.2063	-0.0676	-0.1129	-0.1856	0.4527	0.5692	0.2383	0.15	0.1516	0.0529	0.7484	0.0324	0.1552	71.334	34.912	34.837
5	0.6403	0.1197	-0.3773	0.7204	-0.33	1.3981	-0.1322	-0.2013	-0.1199	0.0048	-0.0078	-0.195	0.25	0.5842	0.1401	0.075	0.1419	-0.0033	0.8969	0.0404	0.1467	72.815	42.478	47.014
6	0.5685	0.8736	-0.3925	1.392	-0.9551	1.4473	-0.0647	-0.0075	0.1062	-0.0354	0.0546	0.0675	-0.0238	0.097	0.0101	0.0608	-0.005	-0.0174	0.6896	-0.0077	0.0948	56.767	54.945	33.935
7	0.9939	0.797	-0.2798	0.7141	-0.2821	1.0062	-0.0573	-0.0876	0.053	0.0108	0.0307	0.002	0.0611	0.1192	0.0265	0.0505	0.0097	-0.0183	0.6915	0.0092	0.0913	56.142	50.604	46.459
8	1.0408	0.1145	-0.2767	0.6212	0.0926	1.8256	-0.1677	-0.1609	-0.245	0.0959	0.0344	-0.0227	0.5199	0.1951	0.1334	0.1871	0.0932	0.0437	0.6721	0.0717	0.1348	54.156	32.411	57.455
9	0.9762	0.107	0.4974	0.6082	-0.0246	1.8964	-0.0202	-0.0719	0.0762	0.0917	-0.0064	-0.0468	-0.1115	0.2941	0.0267	0.088	-0.087	-0.0447	0.7849	-0.0417	0.07	112.579	74.121	116.07
10	5.4063	5.4802	-0.5503	3.9704	0.3821	2.9755	0.2021	-0.4978	0.2148	0.015	-0.1358	0.3683	-0.2812	-0.1345	-0.0663	0.1341	-0.0268	-0.0323	0.9319	-0.0474	0.1376	85.704	77.731	116.203
11	0.7701	-0.0258	-0.0514	0.5297	-0.0264	0.7864	-0.0344	0.0886	-0.1535	-0.0672	0.0322	0.0212	0.2079	0.1485	0.0022	0.1181	0.0042	-0.007	0.7416	-0.0602	0.0791	99.842	46.247	87.208
12	1.8222	-0.7467	0.5188	0.8733	-0.3053	0.5174	-0.0394	0.2131	0.3312	0.0453	-0.112	-0.154	-0.1989	0.401	0.1513	0.0969	-0.17	-0.0341	0.8502	0.0038	0.1152	111.709	83.569	96.781
13	0.786	-0.5334	0.1732	0.7682	-0.1337	0.6942	-0.008	0.1403	0.1279	-0.0716	0.0041	-0.1262	-0.0949	0.2848	0.0039	0.0738	-0.1154	-0.0039	0.7967	-0.0055	0.0693	104.146	76.655	86.672
14	0.73	-1.1106	0.5544	1.5162	-0.5148	1.348	-0.1612	-0.1781	-0.1235	0.133	0.2103	0.1267	-0.0068	-0.0963	-0.0491	0.099	-0.0116	-0.0204	0.7675	-0.0165	0.0794	98.534	65.99	107.914
15	1.2179	-0.8827	-0.1065	1.3637	-0.0245	0.8345	-0.0957	-0.1186	-0.0346	0.0681	0.1328	0.0599	-0.0249	0.063	-0.037	0.0778	-0.0359	-0.0217	0.7167	-0.0168	0.058	90.823	70.747	98.424
16	1.0488	-0.0608	0.1117	1.1083	0.138	0.9131	-0.0591	-0.017	0.2322	-0.0649	0.0314	0.0087	-0.2213	0.0881	0.0277	0.1106	-0.0796	-0.0527	0.6225	-0.0067	0.0887	84.687	89.49	89.93
17	2.0051	0.3875	0.9619	0.6238	0.2164	1.5333	-0.1634	0.1912	0.1864	-0.1093	0.115	0.0941	-0.1862	-0.3274	0.0484	0.0715	0.0275	-0.0619	0.7345	0.0487	0.0622	14.573	69.703	43.183
18	6.0971	0.7642	-1.5836	0.4082	-1.5885	6.0729	-0.189	0.5512	0.4743	-0.0891	0.1419	0.1615	-0.5554	-0.223	0.0471	0.2194	0.0056	-0.083	0.6468	0.0706	0.1598	28.572	87.698	41.1
19	1.0439	-0.2158	-0.2206	0.5325	0.0884	1.219	-0.0776	-0.2037	-0.1323	0.0945	0.0035	-0.0071	0.1932	0.0207	0.0741	0.0739	-0.0133	-0.017	0.6175	0.0349	0.0432	37.161	48.657	72.919
20	1.9625	1.3469	-0.597	1.4765	-0.2001	1.0983	0.0684	-0.0819	0.4342	-0.0093	-0.0357	0.2181	-0.3974	-0.2558	-0.0327	0.1486	0.1006	-0.0389	0.7393	-0.0075	0.1593	22.269	82.714	56.958
21	1.2729	0.6641	-0.2386	0.7794	-0.1759	1.0333	0.0657	-0.2014	0.2621	0.077	-0.0251	0.1088	-0.3122	-0.0444	-0.0406	0.13	0.0149	-0.0218	0.6244	-0.0581	0.0895	32.852	77.801	65.613
22	1.9874	1.0855	0.2726	1.0341	0.4916	1.1703	-0.074	0.1541	-0.0808	-0.0031	0.069	-0.0604	-0.0725	-0.0237	0.005	0.0488	-0.0173	-0.0332	0.6131	-0.0081	0.0444	31.46	61.516	47.869
23	0.9938	0.3253	-0.3646	0.8963	-0.3569	1.0416	-0.0547	0.1026	-0.0018	-0.0903	0.0703	-0.0574	-0.09	0.1375	-0.0156	0.0882	-0.0465	-0.0365	0.5989	-0.0155	0.0554	41.386	68.01	52.431
24	1.3495	0.0796	0.0202	0.5067	-0.279	1.7374	0.0434	0.0416	0.4156	0.012	0.0358	-0.0254	-0.5212	0.2128	-0.0792	0.2331	-0.1201	0.0075	0.6138	-0.0315	0.1857	49.066	88.011	51.561
25	1.0512	-0.2149	-0.2934	0.9836	0.3667	2.452	-0.06	-0.3863	-0.0863	0.0814	0.1127	0.0127	0.1943	-0.2113	-0.0527	0.0694	-0.0483	-0.0599	0.8028	0.0688	0.0643	58.596	57.835	128.237
26	3.9031	-1.1057	-1.0086	0.6635	0.1849	5.411	-0.2559	-0.5083	-0.2065	0.0989	0.1718	0.0284	0.7599	-0.0737	0.0841	0.248	-0.0571	-0.0242	0.7524	0.101	0.1346	68.146	37.796	122.167
27	0.9377	0.2282	0.0729	0.3983	-0.0647	0.7254	-0.0349	-0.0326	0.0995	-0.0493	0.0216	0.0531	-0.1344	-0.132	0.0133	0.1053	-0.0068	-0.0794	0.5897	-0.0101	0.0603	59.889	76.479	89.523
28	1.1855	-0.9268	-0.6165	1.5136	0.5964	0.6991	-0.1125	-0.1119	-0.295	0.1014	-0.0447	0.1536	0.2763	-0.2357	0.1572	0.1202	-0.1483	-0.0306	0.8718	0.0787	0.1677	53.922	44.462	113.603
29	1.0891	-0.5427	-0.1582	0.7658	0.1664	0.8193	-0.0242	0.0138	-0.2977	-0.0262	-0.0135	0.1757	0.1865	-0.2175	0.0377	0.1096	-0.1192	-0.0631	0.6844	0.0112	0.1484	57.214	47.898	100.065
30	1.3143	-0.9831	-0.3081	1.738	0.9885	1.3082	-0.0184	-0.1893	0.058	0.0392	0.0863	-0.1096	0.0149	0.0833	-0.0679	0.0808	-0.0516	-0.0547	0.6843	0.011	0.0776	69.568	63.627	113.46
31	1.0666	-0.375	-0.0112	1.3216	0.1277	0.7015	-0.048	-0.0921	-0.0629	0.0372	0.0873	-0.1103	0.0519	0.1303	-0.0393	0.0851	-0.0481	-0.0606	0.6528	0.0097	0.1011	73.266	55.915	104.083
32	1.0072	-0.3397	-0.0354	0.983	-0.1155	1.5307	-0.0722	-0.1279	-0.3195	-0.0288	0.0383	0.0571	0.4442	-0.0501	0.0339	0.1831	-0.0769	-0.0112	0.6896	0.0271	0.2001	76.957	35.016	101.029
33	1.7964	1.049	-3.3811	-1.9162	-0.4478	5.4844	-0.2727	-0.0992	-0.2387	-0.1527	-0.2306	-0.1482	0.7324	0.1672	0.5034	0.1902	0.0374	0.0408	0.6415	-0.0053	0.1335	59.636	37.674	36.28
34	15.0147	-3.451	5.0773	-1.0282	-0.9577	6.7681	-0.0956	0.4687	0.6345	0.0125	-0.3494	-0.0615	-0.3574	0.3668	0.445	0.1886	-0.0904	-0.0679	0.6624	-0.0325	0.144	101.761	82.687	103.307
35	9.1622	2.3265	0.8594	2.7114	-1.0981	7.6192	0.3657	-0.0095	0.3046	0.1308	-0.0676	0.0622	-0.0827	-0.1586	-0.2981	0.0828	0.0354	-0.0349	0.6719	0.0101	0.092	30.138	78.323	49.356
36	10.4107	-5.976	-9.7094	5.1943	11.5105	25.3613	-0.1127	-0.0971	-0.341	0.1111	-0.3224	0.062	0.2846	-0.5891	0.4351	0.1225	-0.0843	-0.0322	0.723	0.0908	0.1166	65.329	47.242	114.153

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	1 - 15
2	X-RAY DIFFRACTION	1	A	35 - 47
3	X-RAY DIFFRACTION	1	A	135 - 176
4	X-RAY DIFFRACTION	1	A	202 - 224
5	X-RAY DIFFRACTION	1	A	6013 - 6129
6	X-RAY DIFFRACTION	2	A	177 - 201
7	X-RAY DIFFRACTION	2	A	6130 - 6150
8	X-RAY DIFFRACTION	3	A	464 - 662
9	X-RAY DIFFRACTION	3	A	6151 - 6398
10	X-RAY DIFFRACTION	3	D	6043
11	X-RAY DIFFRACTION	4	A	225 - 247
12	X-RAY DIFFRACTION	4	A	336 - 363
13	X-RAY DIFFRACTION	4	A	6399 - 6440
14	X-RAY DIFFRACTION	5	A	364 - 463
15	X-RAY DIFFRACTION	5	A	6441 - 6527
16	X-RAY DIFFRACTION	6	A	16 - 34
17	X-RAY DIFFRACTION	6	A	115 - 134
18	X-RAY DIFFRACTION	6	A	6528 - 6560
19	X-RAY DIFFRACTION	7	A	48 - 78
20	X-RAY DIFFRACTION	7	A	6001
21	X-RAY DIFFRACTION	7	A	6561 - 6595
22	X-RAY DIFFRACTION	8	A	79 - 114
23	X-RAY DIFFRACTION	8	A	248 - 294
24	X-RAY DIFFRACTION	8	A	306 - 335
25	X-RAY DIFFRACTION	8	A	6596 - 6676
26	X-RAY DIFFRACTION	8	C	6033 - 6034
27	X-RAY DIFFRACTION	9	B	1 - 15
28	X-RAY DIFFRACTION	9	B	35 - 47
29	X-RAY DIFFRACTION	9	B	135 - 176
30	X-RAY DIFFRACTION	9	B	202 - 224
31	X-RAY DIFFRACTION	9	B	668 - 776
32	X-RAY DIFFRACTION	10	B	177 - 201
33	X-RAY DIFFRACTION	10	B	777 - 794
34	X-RAY DIFFRACTION	11	B	464 - 662
35	X-RAY DIFFRACTION	11	B	795 - 1052
36	X-RAY DIFFRACTION	11	D	6044 - 6045
37	X-RAY DIFFRACTION	12	B	225 - 247
38	X-RAY DIFFRACTION	12	B	336 - 363
39	X-RAY DIFFRACTION	12	B	1053 - 1093
40	X-RAY DIFFRACTION	13	B	364 - 463
41	X-RAY DIFFRACTION	13	B	1094 - 1200
42	X-RAY DIFFRACTION	14	B	16 - 34
43	X-RAY DIFFRACTION	14	B	115 - 134
44	X-RAY DIFFRACTION	14	B	1201 - 1229
45	X-RAY DIFFRACTION	15	B	48 - 78
46	X-RAY DIFFRACTION	15	B	6002
47	X-RAY DIFFRACTION	15	B	1230 - 1263
48	X-RAY DIFFRACTION	16	B	79 - 114
49	X-RAY DIFFRACTION	16	B	248 - 294
50	X-RAY DIFFRACTION	16	B	307 - 335
51	X-RAY DIFFRACTION	16	B	1264 - 1354
52	X-RAY DIFFRACTION	16	D	6046 - 6048
53	X-RAY DIFFRACTION	17	C	1 - 15
54	X-RAY DIFFRACTION	17	C	35 - 47
55	X-RAY DIFFRACTION	17	C	135 - 176
56	X-RAY DIFFRACTION	17	C	202 - 224
57	X-RAY DIFFRACTION	17	C	6035 - 6137
58	X-RAY DIFFRACTION	18	C	177 - 201
59	X-RAY DIFFRACTION	18	C	6138 - 6154
60	X-RAY DIFFRACTION	19	C	464 - 662
61	X-RAY DIFFRACTION	19	A	6677
62	X-RAY DIFFRACTION	19	C	6155 - 6433
63	X-RAY DIFFRACTION	19	D	6049 - 6050
64	X-RAY DIFFRACTION	20	C	225 - 247
65	X-RAY DIFFRACTION	20	C	336 - 363
66	X-RAY DIFFRACTION	20	C	6434 - 6471
67	X-RAY DIFFRACTION	21	C	364 - 463
68	X-RAY DIFFRACTION	21	C	6472 - 6567
69	X-RAY DIFFRACTION	22	C	16 - 34
70	X-RAY DIFFRACTION	22	C	115 - 134
71	X-RAY DIFFRACTION	22	C	6568 - 6599
72	X-RAY DIFFRACTION	23	C	48 - 78
73	X-RAY DIFFRACTION	23	C	6003
74	X-RAY DIFFRACTION	23	A	6678
75	X-RAY DIFFRACTION	23	C	6600 - 6634
76	X-RAY DIFFRACTION	24	C	79 - 114
77	X-RAY DIFFRACTION	24	C	248 - 294
78	X-RAY DIFFRACTION	24	C	301 - 335
79	X-RAY DIFFRACTION	24	A	6679 - 6680
80	X-RAY DIFFRACTION	24	C	6635 - 6700
81	X-RAY DIFFRACTION	24	D	6051 - 6052
82	X-RAY DIFFRACTION	25	D	1 - 15
83	X-RAY DIFFRACTION	25	D	35 - 47
84	X-RAY DIFFRACTION	25	D	135 - 176
85	X-RAY DIFFRACTION	25	D	202 - 224
86	X-RAY DIFFRACTION	25	D	6053 - 6148
87	X-RAY DIFFRACTION	26	D	177 - 201
88	X-RAY DIFFRACTION	26	D	6149 - 6163
89	X-RAY DIFFRACTION	27	D	464 - 662
90	X-RAY DIFFRACTION	27	B	2326
91	X-RAY DIFFRACTION	27	C	6701 - 6705
92	X-RAY DIFFRACTION	27	D	6164 - 6457
93	X-RAY DIFFRACTION	28	D	225 - 247
94	X-RAY DIFFRACTION	28	D	336 - 363
95	X-RAY DIFFRACTION	28	D	6458 - 6492
96	X-RAY DIFFRACTION	29	D	364 - 463
97	X-RAY DIFFRACTION	29	C	6706
98	X-RAY DIFFRACTION	29	D	6493 - 6570
99	X-RAY DIFFRACTION	30	D	16 - 34
100	X-RAY DIFFRACTION	30	D	115 - 134
101	X-RAY DIFFRACTION	30	D	6571 - 6601
102	X-RAY DIFFRACTION	31	D	48 - 78
103	X-RAY DIFFRACTION	31	D	6004
104	X-RAY DIFFRACTION	31	B	2616 - 2618
105	X-RAY DIFFRACTION	31	D	6602 - 6633
106	X-RAY DIFFRACTION	32	D	79 - 114
107	X-RAY DIFFRACTION	32	D	248 - 294
108	X-RAY DIFFRACTION	32	D	301 - 335
109	X-RAY DIFFRACTION	32	B	2662
110	X-RAY DIFFRACTION	32	D	6634 - 6702
111	X-RAY DIFFRACTION	33	A	6011
112	X-RAY DIFFRACTION	34	B	6021
113	X-RAY DIFFRACTION	35	C	6031
114	X-RAY DIFFRACTION	36	D	6041

• Software: Version: 5 / Classification: refinement
• Refinement: Highest resolution: 1.7 Å / Lowest resolution: 20 Å / Num. reflection R_free: 14145 / R_factor R_free: 0.1799 / R_factor R_work: 0.157

Refine LS restraints

Refine-ID	Type	Dev ideal
X-RAY DIFFRACTION	r_bond_d	0.012
X-RAY DIFFRACTION	r_angle_d
X-RAY DIFFRACTION	r_angle_deg	1.4

• LS refinement shell: Highest resolution: 1.7 Å / Lowest resolution: 1.74 Å