PDB-5dtl: Crystal structure of mEos2-A69T fluorescent protein

Basic information

• Entry: Database: PDB / ID: 5dtl
• Title: Crystal structure of mEos2-A69T fluorescent protein
• Components: Green to red photoconvertible GFP-like protein EosFP
• Keywords: FLUORESCENT PROTEIN / mEos2 / blinking

Function / homology

Function:

bioluminescence / generation of precursor metabolites and energy

Domain/homology:

Green Fluorescent Protein / Green fluorescent protein / Green fluorescent protein, GFP / Green fluorescent protein-related / Green fluorescent protein / Green fluorescent protein / Beta Barrel / Mainly Beta

Component:

Green to red photoconvertible GFP-like protein EosFP

• Biological species: Lobophyllia hemprichii (invertebrata)
• Method: X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å
• Authors: Berardozzi, R. / Adam, V. / Martins, A. / Bourgeois, D.
• Citation: Journal: J.Am.Chem.Soc. / Year: 2016; Title: Arginine 66 Controls Dark-State Formation in Green-to-Red Photoconvertible Fluorescent Proteins.; Authors: Berardozzi, R. / Adam, V. / Martins, A. / Bourgeois, D.

History

Deposition	Sep 18, 2015	Deposition site: RCSB / Processing site: PDBE
Revision 1.0	Dec 30, 2015	Provider: repository / Type: Initial release
Revision 1.1	Jan 13, 2016	Group: Database references
Revision 1.2	Jan 27, 2016	Group: Database references
Revision 2.0	Sep 1, 2021	Group: Advisory / Atomic model / Data collection / Database references / Derived calculations / Non-polymer description / Polymer sequence / Structure summary Category: atom_site / chem_comp / database_2 / entity / entity_poly / entity_poly_seq / pdbx_poly_seq_scheme / pdbx_struct_assembly_prop / pdbx_struct_mod_residue / pdbx_validate_close_contact / pdbx_validate_rmsd_angle / pdbx_validate_rmsd_bond / struct_conn / struct_ref_seq_dif Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.type_symbol / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _entity.formula_weight / _entity.pdbx_description / _entity_poly.pdbx_seq_one_letter_code / _entity_poly_seq.mon_id / _pdbx_poly_seq_scheme.mon_id / _pdbx_poly_seq_scheme.pdb_mon_id / _pdbx_struct_assembly_prop.value / _pdbx_validate_close_contact.auth_atom_id_1 / _pdbx_validate_close_contact.auth_comp_id_1 / _pdbx_validate_rmsd_bond.auth_comp_id_1 / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_label_comp_id / _struct_ref_seq_dif.mon_id
Revision 3.0	Nov 15, 2023	Group: Advisory / Atomic model / Data collection / Derived calculations / Refinement description Category: atom_site / chem_comp_atom / chem_comp_bond / pdbx_validate_close_contact / pdbx_validate_main_chain_plane / pdbx_validate_rmsd_angle / pdbx_validate_rmsd_bond / struct_conn / struct_ncs_dom_lim Item: _atom_site.auth_atom_id / _atom_site.label_atom_id / _pdbx_validate_close_contact.auth_atom_id_1 / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr2_label_atom_id / _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 3.1	Jan 10, 2024	Group: Refinement description / Category: pdbx_initial_refinement_model

Assembly

Deposited unit

A: Green to red photoconvertible GFP-like protein EosFP

B: Green to red photoconvertible GFP-like protein EosFP

C: Green to red photoconvertible GFP-like protein EosFP

D: Green to red photoconvertible GFP-like protein EosFP

E: Green to red photoconvertible GFP-like protein EosFP

F: Green to red photoconvertible GFP-like protein EosFP

G: Green to red photoconvertible GFP-like protein EosFP

H: Green to red photoconvertible GFP-like protein EosFP

I: Green to red photoconvertible GFP-like protein EosFP

J: Green to red photoconvertible GFP-like protein EosFP

K: Green to red photoconvertible GFP-like protein EosFP

L: Green to red photoconvertible GFP-like protein EosFP

Summary:

• 311 kDa, 12 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	310,721	12
Polymers	310,721	12
Non-polymers	0	0
Water	8,485	471

1

A: Green to red photoconvertible GFP-like protein EosFP

D: Green to red photoconvertible GFP-like protein EosFP

E: Green to red photoconvertible GFP-like protein EosFP

J: Green to red photoconvertible GFP-like protein EosFP

Summary:

• defined by author&software
• 104 kDa, 4 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	103,574	4
Polymers	103,574	4
Non-polymers	0	0
Water	72	4

Symmetry operations:

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

Calculated values:

Buried area	8110 Å2
ΔGint	-27 kcal/mol
Surface area	33980 Å2
Method	PISA

2

B: Green to red photoconvertible GFP-like protein EosFP

F: Green to red photoconvertible GFP-like protein EosFP

G: Green to red photoconvertible GFP-like protein EosFP

K: Green to red photoconvertible GFP-like protein EosFP

Summary:

• defined by author&software
• 104 kDa, 4 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	103,574	4
Polymers	103,574	4
Non-polymers	0	0
Water	72	4

Symmetry operations:

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

Calculated values:

Buried area	7820 Å2
ΔGint	-26 kcal/mol
Surface area	34230 Å2
Method	PISA

3

C: Green to red photoconvertible GFP-like protein EosFP

H: Green to red photoconvertible GFP-like protein EosFP

I: Green to red photoconvertible GFP-like protein EosFP

L: Green to red photoconvertible GFP-like protein EosFP

Summary:

• defined by author&software
• 104 kDa, 4 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	103,574	4
Polymers	103,574	4
Non-polymers	0	0
Water	72	4

Symmetry operations:

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

Calculated values:

Buried area	7790 Å2
ΔGint	-32 kcal/mol
Surface area	34050 Å2
Method	PISA

Unit cell

Length a, b, c (Å)	73.370, 96.500, 100.060
Angle α, β, γ (deg.)	91.68, 107.83, 97.38
Int Tables number	1
Space group name H-M	P1

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	A
2	1	B
1	2	A
2	2	C
1	3	A
2	3	D
1	4	A
2	4	E
1	5	A
2	5	F
1	6	A
2	6	G
1	7	A
2	7	H
1	8	A
2	8	I
1	9	A
2	9	J
1	10	A
2	10	K
1	11	A
2	11	L
1	12	A
2	12	B
1	13	A
2	13	C
1	14	A
2	14	D
1	15	A
2	15	E
1	16	A
2	16	F
1	17	A
2	17	G
1	18	A
2	18	H
1	19	A
2	19	I
1	20	A
2	20	J
1	21	A
2	21	K
1	22	A
2	22	L
1	23	B
2	23	C
1	24	B
2	24	D
1	25	B
2	25	E
1	26	B
2	26	F
1	27	B
2	27	G
1	28	B
2	28	H
1	29	B
2	29	I
1	30	B
2	30	J
1	31	B
2	31	K
1	32	B
2	32	L
1	33	B
2	33	C
1	34	B
2	34	D
1	35	B
2	35	E
1	36	B
2	36	F
1	37	B
2	37	G
1	38	B
2	38	H
1	39	B
2	39	I
1	40	B
2	40	J
1	41	B
2	41	K
1	42	B
2	42	L
1	43	C
2	43	D
1	44	C
2	44	E
1	45	C
2	45	F
1	46	C
2	46	G
1	47	C
2	47	H
1	48	C
2	48	I
1	49	C
2	49	J
1	50	C
2	50	K
1	51	C
2	51	L
1	52	C
2	52	D
1	53	C
2	53	E
1	54	C
2	54	F
1	55	C
2	55	G
1	56	C
2	56	H
1	57	C
2	57	I
1	58	C
2	58	J
1	59	C
2	59	K
1	60	C
2	60	L
1	61	D
2	61	E
1	62	D
2	62	F
1	63	D
2	63	G
1	64	D
2	64	H
1	65	D
2	65	I
1	66	D
2	66	J
1	67	D
2	67	K
1	68	D
2	68	L
1	69	D
2	69	E
1	70	D
2	70	F
1	71	D
2	71	G
1	72	D
2	72	H
1	73	D
2	73	I
1	74	D
2	74	J
1	75	D
2	75	K
1	76	D
2	76	L
1	77	E
2	77	F
1	78	E
2	78	G
1	79	E
2	79	H
1	80	E
2	80	I
1	81	E
2	81	J
1	82	E
2	82	K
1	83	E
2	83	L
1	84	E
2	84	F
1	85	E
2	85	G
1	86	E
2	86	H
1	87	E
2	87	I
1	88	E
2	88	J
1	89	E
2	89	K
1	90	E
2	90	L
1	91	F
2	91	G
1	92	F
2	92	H
1	93	F
2	93	I
1	94	F
2	94	J
1	95	F
2	95	K
1	96	F
2	96	L
1	97	F
2	97	G
1	98	F
2	98	H
1	99	F
2	99	I
1	100	F
2	100	J
1	101	F
2	101	K
1	102	F
2	102	L
1	103	G
2	103	H
1	104	G
2	104	I
1	105	G
2	105	J
1	106	G
2	106	K
1	107	G
2	107	L
1	108	G
2	108	H
1	109	G
2	109	I
1	110	G
2	110	J
1	111	G
2	111	K
1	112	G
2	112	L
1	113	H
2	113	I
1	114	H
2	114	J
1	115	H
2	115	K
1	116	H
2	116	L
1	117	H
2	117	I
1	118	H
2	118	J
1	119	H
2	119	K
1	120	H
2	120	L
1	121	I
2	121	J
1	122	I
2	122	K
1	123	I
2	123	L
1	124	I
2	124	J
1	125	I
2	125	K
1	126	I
2	126	L
1	127	J
2	127	K
1	128	J
2	128	L
1	129	J
2	129	K
1	130	J
2	130	L
1	131	K
2	131	L
1	132	K
2	132	L

NCS domain segments:

Component-ID: _ / Refine code: _

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	SER	SER	PHE	PHE	A	A	2 - 61	2 - 61
2	1	SER	SER	PHE	PHE	B	B	2 - 61	2 - 61
1	2	SER	SER	PHE	PHE	A	A	2 - 61	2 - 61
2	2	SER	SER	PHE	PHE	C	C	2 - 61	2 - 61
1	3	SER	SER	PHE	PHE	A	A	2 - 61	2 - 61
2	3	SER	SER	PHE	PHE	D	D	2 - 61	2 - 61
1	4	SER	SER	PHE	PHE	A	A	2 - 61	2 - 61
2	4	SER	SER	PHE	PHE	E	E	2 - 61	2 - 61
1	5	SER	SER	PHE	PHE	A	A	2 - 61	2 - 61
2	5	SER	SER	PHE	PHE	F	F	2 - 61	2 - 61
1	6	SER	SER	PHE	PHE	A	A	2 - 61	2 - 61
2	6	SER	SER	PHE	PHE	G	G	2 - 61	2 - 61
1	7	SER	SER	PHE	PHE	A	A	2 - 61	2 - 61
2	7	SER	SER	PHE	PHE	H	H	2 - 61	2 - 61
1	8	SER	SER	PHE	PHE	A	A	2 - 61	2 - 61
2	8	SER	SER	PHE	PHE	I	I	2 - 61	2 - 61
1	9	SER	SER	PHE	PHE	A	A	2 - 61	2 - 61
2	9	SER	SER	PHE	PHE	J	J	2 - 61	2 - 61
1	10	SER	SER	PHE	PHE	A	A	2 - 61	2 - 61
2	10	SER	SER	PHE	PHE	K	K	2 - 61	2 - 61
1	11	SER	SER	PHE	PHE	A	A	2 - 61	2 - 61
2	11	SER	SER	PHE	PHE	L	L	2 - 61	2 - 61
1	12	ASN	ASN	ASN	ASN	A	A	65 - 223	63 - 221
2	12	ASN	ASN	ASN	ASN	B	B	65 - 223	63 - 221
1	13	ASN	ASN	ASN	ASN	A	A	65 - 223	63 - 221
2	13	ASN	ASN	ASN	ASN	C	C	65 - 223	63 - 221
1	14	ASN	ASN	ASN	ASN	A	A	65 - 223	63 - 221
2	14	ASN	ASN	ASN	ASN	D	D	65 - 223	63 - 221
1	15	ASN	ASN	ASN	ASN	A	A	65 - 223	63 - 221
2	15	ASN	ASN	ASN	ASN	E	E	65 - 223	63 - 221
1	16	ASN	ASN	ASN	ASN	A	A	65 - 223	63 - 221
2	16	ASN	ASN	ASN	ASN	F	F	65 - 223	63 - 221
1	17	ASN	ASN	ASN	ASN	A	A	65 - 223	63 - 221
2	17	ASN	ASN	ASN	ASN	G	G	65 - 223	63 - 221
1	18	ASN	ASN	ASN	ASN	A	A	65 - 223	63 - 221
2	18	ASN	ASN	ASN	ASN	H	H	65 - 223	63 - 221
1	19	ASN	ASN	ASN	ASN	A	A	65 - 223	63 - 221
2	19	ASN	ASN	ASN	ASN	I	I	65 - 223	63 - 221
1	20	ASN	ASN	ASN	ASN	A	A	65 - 223	63 - 221
2	20	ASN	ASN	ASN	ASN	J	J	65 - 223	63 - 221
1	21	ASN	ASN	ASN	ASN	A	A	65 - 223	63 - 221
2	21	ASN	ASN	ASN	ASN	K	K	65 - 223	63 - 221
1	22	ASN	ASN	ASN	ASN	A	A	65 - 223	63 - 221
2	22	ASN	ASN	ASN	ASN	L	L	65 - 223	63 - 221
1	23	SER	SER	PHE	PHE	B	B	2 - 61	2 - 61
2	23	SER	SER	PHE	PHE	C	C	2 - 61	2 - 61
1	24	SER	SER	PHE	PHE	B	B	2 - 61	2 - 61
2	24	SER	SER	PHE	PHE	D	D	2 - 61	2 - 61
1	25	SER	SER	PHE	PHE	B	B	2 - 61	2 - 61
2	25	SER	SER	PHE	PHE	E	E	2 - 61	2 - 61
1	26	SER	SER	PHE	PHE	B	B	2 - 61	2 - 61
2	26	SER	SER	PHE	PHE	F	F	2 - 61	2 - 61
1	27	SER	SER	PHE	PHE	B	B	2 - 61	2 - 61
2	27	SER	SER	PHE	PHE	G	G	2 - 61	2 - 61
1	28	SER	SER	PHE	PHE	B	B	2 - 61	2 - 61
2	28	SER	SER	PHE	PHE	H	H	2 - 61	2 - 61
1	29	SER	SER	PHE	PHE	B	B	2 - 61	2 - 61
2	29	SER	SER	PHE	PHE	I	I	2 - 61	2 - 61
1	30	SER	SER	PHE	PHE	B	B	2 - 61	2 - 61
2	30	SER	SER	PHE	PHE	J	J	2 - 61	2 - 61
1	31	SER	SER	PHE	PHE	B	B	2 - 61	2 - 61
2	31	SER	SER	PHE	PHE	K	K	2 - 61	2 - 61
1	32	SER	SER	PHE	PHE	B	B	2 - 61	2 - 61
2	32	SER	SER	PHE	PHE	L	L	2 - 61	2 - 61
1	33	ASN	ASN	ASN	ASN	B	B	65 - 223	63 - 221
2	33	ASN	ASN	ASN	ASN	C	C	65 - 223	63 - 221
1	34	ASN	ASN	ASN	ASN	B	B	65 - 223	63 - 221
2	34	ASN	ASN	ASN	ASN	D	D	65 - 223	63 - 221
1	35	ASN	ASN	ASN	ASN	B	B	65 - 223	63 - 221
2	35	ASN	ASN	ASN	ASN	E	E	65 - 223	63 - 221
1	36	ASN	ASN	ASN	ASN	B	B	65 - 223	63 - 221
2	36	ASN	ASN	ASN	ASN	F	F	65 - 223	63 - 221
1	37	ASN	ASN	ASN	ASN	B	B	65 - 223	63 - 221
2	37	ASN	ASN	ASN	ASN	G	G	65 - 223	63 - 221
1	38	ASN	ASN	ASN	ASN	B	B	65 - 223	63 - 221
2	38	ASN	ASN	ASN	ASN	H	H	65 - 223	63 - 221
1	39	ASN	ASN	ASN	ASN	B	B	65 - 223	63 - 221
2	39	ASN	ASN	ASN	ASN	I	I	65 - 223	63 - 221
1	40	ASN	ASN	ASN	ASN	B	B	65 - 223	63 - 221
2	40	ASN	ASN	ASN	ASN	J	J	65 - 223	63 - 221
1	41	ASN	ASN	ASN	ASN	B	B	65 - 223	63 - 221
2	41	ASN	ASN	ASN	ASN	K	K	65 - 223	63 - 221
1	42	ASN	ASN	ASN	ASN	B	B	65 - 223	63 - 221
2	42	ASN	ASN	ASN	ASN	L	L	65 - 223	63 - 221
1	43	SER	SER	PHE	PHE	C	C	2 - 61	2 - 61
2	43	SER	SER	PHE	PHE	D	D	2 - 61	2 - 61
1	44	SER	SER	PHE	PHE	C	C	2 - 61	2 - 61
2	44	SER	SER	PHE	PHE	E	E	2 - 61	2 - 61
1	45	SER	SER	PHE	PHE	C	C	2 - 61	2 - 61
2	45	SER	SER	PHE	PHE	F	F	2 - 61	2 - 61
1	46	SER	SER	PHE	PHE	C	C	2 - 61	2 - 61
2	46	SER	SER	PHE	PHE	G	G	2 - 61	2 - 61
1	47	SER	SER	PHE	PHE	C	C	2 - 61	2 - 61
2	47	SER	SER	PHE	PHE	H	H	2 - 61	2 - 61
1	48	SER	SER	PHE	PHE	C	C	2 - 61	2 - 61
2	48	SER	SER	PHE	PHE	I	I	2 - 61	2 - 61
1	49	SER	SER	PHE	PHE	C	C	2 - 61	2 - 61
2	49	SER	SER	PHE	PHE	J	J	2 - 61	2 - 61
1	50	SER	SER	PHE	PHE	C	C	2 - 61	2 - 61
2	50	SER	SER	PHE	PHE	K	K	2 - 61	2 - 61
1	51	SER	SER	PHE	PHE	C	C	2 - 61	2 - 61
2	51	SER	SER	PHE	PHE	L	L	2 - 61	2 - 61
1	52	ASN	ASN	ASN	ASN	C	C	65 - 223	63 - 221
2	52	ASN	ASN	ASN	ASN	D	D	65 - 223	63 - 221
1	53	ASN	ASN	ASN	ASN	C	C	65 - 223	63 - 221
2	53	ASN	ASN	ASN	ASN	E	E	65 - 223	63 - 221
1	54	ASN	ASN	ASN	ASN	C	C	65 - 223	63 - 221
2	54	ASN	ASN	ASN	ASN	F	F	65 - 223	63 - 221
1	55	ASN	ASN	ASN	ASN	C	C	65 - 223	63 - 221
2	55	ASN	ASN	ASN	ASN	G	G	65 - 223	63 - 221
1	56	ASN	ASN	ASN	ASN	C	C	65 - 223	63 - 221
2	56	ASN	ASN	ASN	ASN	H	H	65 - 223	63 - 221
1	57	ASN	ASN	ASN	ASN	C	C	65 - 223	63 - 221
2	57	ASN	ASN	ASN	ASN	I	I	65 - 223	63 - 221
1	58	ASN	ASN	ASN	ASN	C	C	65 - 223	63 - 221
2	58	ASN	ASN	ASN	ASN	J	J	65 - 223	63 - 221
1	59	ASN	ASN	ASN	ASN	C	C	65 - 223	63 - 221
2	59	ASN	ASN	ASN	ASN	K	K	65 - 223	63 - 221
1	60	ASN	ASN	ASN	ASN	C	C	65 - 223	63 - 221
2	60	ASN	ASN	ASN	ASN	L	L	65 - 223	63 - 221
1	61	SER	SER	PHE	PHE	D	D	2 - 61	2 - 61
2	61	SER	SER	PHE	PHE	E	E	2 - 61	2 - 61
1	62	SER	SER	PHE	PHE	D	D	2 - 61	2 - 61
2	62	SER	SER	PHE	PHE	F	F	2 - 61	2 - 61
1	63	SER	SER	PHE	PHE	D	D	2 - 61	2 - 61
2	63	SER	SER	PHE	PHE	G	G	2 - 61	2 - 61
1	64	SER	SER	PHE	PHE	D	D	2 - 61	2 - 61
2	64	SER	SER	PHE	PHE	H	H	2 - 61	2 - 61
1	65	SER	SER	PHE	PHE	D	D	2 - 61	2 - 61
2	65	SER	SER	PHE	PHE	I	I	2 - 61	2 - 61
1	66	SER	SER	PHE	PHE	D	D	2 - 61	2 - 61
2	66	SER	SER	PHE	PHE	J	J	2 - 61	2 - 61
1	67	SER	SER	PHE	PHE	D	D	2 - 61	2 - 61
2	67	SER	SER	PHE	PHE	K	K	2 - 61	2 - 61
1	68	SER	SER	PHE	PHE	D	D	2 - 61	2 - 61
2	68	SER	SER	PHE	PHE	L	L	2 - 61	2 - 61
1	69	ASN	ASN	ASN	ASN	D	D	65 - 223	63 - 221
2	69	ASN	ASN	ASN	ASN	E	E	65 - 223	63 - 221
1	70	ASN	ASN	ASN	ASN	D	D	65 - 223	63 - 221
2	70	ASN	ASN	ASN	ASN	F	F	65 - 223	63 - 221
1	71	ASN	ASN	ASN	ASN	D	D	65 - 223	63 - 221
2	71	ASN	ASN	ASN	ASN	G	G	65 - 223	63 - 221
1	72	ASN	ASN	ASN	ASN	D	D	65 - 223	63 - 221
2	72	ASN	ASN	ASN	ASN	H	H	65 - 223	63 - 221
1	73	ASN	ASN	ASN	ASN	D	D	65 - 223	63 - 221
2	73	ASN	ASN	ASN	ASN	I	I	65 - 223	63 - 221
1	74	ASN	ASN	ASN	ASN	D	D	65 - 223	63 - 221
2	74	ASN	ASN	ASN	ASN	J	J	65 - 223	63 - 221
1	75	ASN	ASN	ASN	ASN	D	D	65 - 223	63 - 221
2	75	ASN	ASN	ASN	ASN	K	K	65 - 223	63 - 221
1	76	ASN	ASN	ASN	ASN	D	D	65 - 223	63 - 221
2	76	ASN	ASN	ASN	ASN	L	L	65 - 223	63 - 221
1	77	SER	SER	PHE	PHE	E	E	2 - 61	2 - 61
2	77	SER	SER	PHE	PHE	F	F	2 - 61	2 - 61
1	78	SER	SER	PHE	PHE	E	E	2 - 61	2 - 61
2	78	SER	SER	PHE	PHE	G	G	2 - 61	2 - 61
1	79	SER	SER	PHE	PHE	E	E	2 - 61	2 - 61
2	79	SER	SER	PHE	PHE	H	H	2 - 61	2 - 61
1	80	SER	SER	PHE	PHE	E	E	2 - 61	2 - 61
2	80	SER	SER	PHE	PHE	I	I	2 - 61	2 - 61
1	81	SER	SER	PHE	PHE	E	E	2 - 61	2 - 61
2	81	SER	SER	PHE	PHE	J	J	2 - 61	2 - 61
1	82	SER	SER	PHE	PHE	E	E	2 - 61	2 - 61
2	82	SER	SER	PHE	PHE	K	K	2 - 61	2 - 61
1	83	SER	SER	PHE	PHE	E	E	2 - 61	2 - 61
2	83	SER	SER	PHE	PHE	L	L	2 - 61	2 - 61
1	84	ASN	ASN	ASN	ASN	E	E	65 - 223	63 - 221
2	84	ASN	ASN	ASN	ASN	F	F	65 - 223	63 - 221
1	85	ASN	ASN	ASN	ASN	E	E	65 - 223	63 - 221
2	85	ASN	ASN	ASN	ASN	G	G	65 - 223	63 - 221
1	86	ASN	ASN	ASN	ASN	E	E	65 - 223	63 - 221
2	86	ASN	ASN	ASN	ASN	H	H	65 - 223	63 - 221
1	87	ASN	ASN	ASN	ASN	E	E	65 - 223	63 - 221
2	87	ASN	ASN	ASN	ASN	I	I	65 - 223	63 - 221
1	88	ASN	ASN	ASN	ASN	E	E	65 - 223	63 - 221
2	88	ASN	ASN	ASN	ASN	J	J	65 - 223	63 - 221
1	89	ASN	ASN	ASN	ASN	E	E	65 - 223	63 - 221
2	89	ASN	ASN	ASN	ASN	K	K	65 - 223	63 - 221
1	90	ASN	ASN	ASN	ASN	E	E	65 - 223	63 - 221
2	90	ASN	ASN	ASN	ASN	L	L	65 - 223	63 - 221
1	91	SER	SER	PHE	PHE	F	F	2 - 61	2 - 61
2	91	SER	SER	PHE	PHE	G	G	2 - 61	2 - 61
1	92	SER	SER	PHE	PHE	F	F	2 - 61	2 - 61
2	92	SER	SER	PHE	PHE	H	H	2 - 61	2 - 61
1	93	SER	SER	PHE	PHE	F	F	2 - 61	2 - 61
2	93	SER	SER	PHE	PHE	I	I	2 - 61	2 - 61
1	94	SER	SER	PHE	PHE	F	F	2 - 61	2 - 61
2	94	SER	SER	PHE	PHE	J	J	2 - 61	2 - 61
1	95	SER	SER	PHE	PHE	F	F	2 - 61	2 - 61
2	95	SER	SER	PHE	PHE	K	K	2 - 61	2 - 61
1	96	SER	SER	PHE	PHE	F	F	2 - 61	2 - 61
2	96	SER	SER	PHE	PHE	L	L	2 - 61	2 - 61
1	97	ASN	ASN	ASN	ASN	F	F	65 - 223	63 - 221
2	97	ASN	ASN	ASN	ASN	G	G	65 - 223	63 - 221
1	98	ASN	ASN	ASN	ASN	F	F	65 - 223	63 - 221
2	98	ASN	ASN	ASN	ASN	H	H	65 - 223	63 - 221
1	99	ASN	ASN	ASN	ASN	F	F	65 - 223	63 - 221
2	99	ASN	ASN	ASN	ASN	I	I	65 - 223	63 - 221
1	100	ASN	ASN	ASN	ASN	F	F	65 - 223	63 - 221
2	100	ASN	ASN	ASN	ASN	J	J	65 - 223	63 - 221
1	101	ASN	ASN	ASN	ASN	F	F	65 - 223	63 - 221
2	101	ASN	ASN	ASN	ASN	K	K	65 - 223	63 - 221
1	102	ASN	ASN	ASN	ASN	F	F	65 - 223	63 - 221
2	102	ASN	ASN	ASN	ASN	L	L	65 - 223	63 - 221
1	103	SER	SER	PHE	PHE	G	G	2 - 61	2 - 61
2	103	SER	SER	PHE	PHE	H	H	2 - 61	2 - 61
1	104	SER	SER	PHE	PHE	G	G	2 - 61	2 - 61
2	104	SER	SER	PHE	PHE	I	I	2 - 61	2 - 61
1	105	SER	SER	PHE	PHE	G	G	2 - 61	2 - 61
2	105	SER	SER	PHE	PHE	J	J	2 - 61	2 - 61
1	106	SER	SER	PHE	PHE	G	G	2 - 61	2 - 61
2	106	SER	SER	PHE	PHE	K	K	2 - 61	2 - 61
1	107	SER	SER	PHE	PHE	G	G	2 - 61	2 - 61
2	107	SER	SER	PHE	PHE	L	L	2 - 61	2 - 61
1	108	ASN	ASN	ASN	ASN	G	G	65 - 223	63 - 221
2	108	ASN	ASN	ASN	ASN	H	H	65 - 223	63 - 221
1	109	ASN	ASN	ASN	ASN	G	G	65 - 223	63 - 221
2	109	ASN	ASN	ASN	ASN	I	I	65 - 223	63 - 221
1	110	ASN	ASN	ASN	ASN	G	G	65 - 223	63 - 221
2	110	ASN	ASN	ASN	ASN	J	J	65 - 223	63 - 221
1	111	ASN	ASN	ASN	ASN	G	G	65 - 223	63 - 221
2	111	ASN	ASN	ASN	ASN	K	K	65 - 223	63 - 221
1	112	ASN	ASN	ASN	ASN	G	G	65 - 223	63 - 221
2	112	ASN	ASN	ASN	ASN	L	L	65 - 223	63 - 221
1	113	SER	SER	PHE	PHE	H	H	2 - 61	2 - 61
2	113	SER	SER	PHE	PHE	I	I	2 - 61	2 - 61
1	114	SER	SER	PHE	PHE	H	H	2 - 61	2 - 61
2	114	SER	SER	PHE	PHE	J	J	2 - 61	2 - 61
1	115	SER	SER	PHE	PHE	H	H	2 - 61	2 - 61
2	115	SER	SER	PHE	PHE	K	K	2 - 61	2 - 61
1	116	SER	SER	PHE	PHE	H	H	2 - 61	2 - 61
2	116	SER	SER	PHE	PHE	L	L	2 - 61	2 - 61
1	117	ASN	ASN	ASN	ASN	H	H	65 - 223	63 - 221
2	117	ASN	ASN	ASN	ASN	I	I	65 - 223	63 - 221
1	118	ASN	ASN	ASN	ASN	H	H	65 - 223	63 - 221
2	118	ASN	ASN	ASN	ASN	J	J	65 - 223	63 - 221
1	119	ASN	ASN	ASN	ASN	H	H	65 - 223	63 - 221
2	119	ASN	ASN	ASN	ASN	K	K	65 - 223	63 - 221
1	120	ASN	ASN	ASN	ASN	H	H	65 - 223	63 - 221
2	120	ASN	ASN	ASN	ASN	L	L	65 - 223	63 - 221
1	121	SER	SER	PHE	PHE	I	I	2 - 61	2 - 61
2	121	SER	SER	PHE	PHE	J	J	2 - 61	2 - 61
1	122	SER	SER	PHE	PHE	I	I	2 - 61	2 - 61
2	122	SER	SER	PHE	PHE	K	K	2 - 61	2 - 61
1	123	SER	SER	PHE	PHE	I	I	2 - 61	2 - 61
2	123	SER	SER	PHE	PHE	L	L	2 - 61	2 - 61
1	124	ASN	ASN	ASN	ASN	I	I	65 - 223	63 - 221
2	124	ASN	ASN	ASN	ASN	J	J	65 - 223	63 - 221
1	125	ASN	ASN	ASN	ASN	I	I	65 - 223	63 - 221
2	125	ASN	ASN	ASN	ASN	K	K	65 - 223	63 - 221
1	126	ASN	ASN	ASN	ASN	I	I	65 - 223	63 - 221
2	126	ASN	ASN	ASN	ASN	L	L	65 - 223	63 - 221
1	127	SER	SER	PHE	PHE	J	J	2 - 61	2 - 61
2	127	SER	SER	PHE	PHE	K	K	2 - 61	2 - 61
1	128	SER	SER	PHE	PHE	J	J	2 - 61	2 - 61
2	128	SER	SER	PHE	PHE	L	L	2 - 61	2 - 61
1	129	ASN	ASN	ASN	ASN	J	J	65 - 223	63 - 221
2	129	ASN	ASN	ASN	ASN	K	K	65 - 223	63 - 221
1	130	ASN	ASN	ASN	ASN	J	J	65 - 223	63 - 221
2	130	ASN	ASN	ASN	ASN	L	L	65 - 223	63 - 221
1	131	SER	SER	PHE	PHE	K	K	2 - 61	2 - 61
2	131	SER	SER	PHE	PHE	L	L	2 - 61	2 - 61
1	132	ASN	ASN	ASN	ASN	K	K	65 - 223	63 - 221
2	132	ASN	ASN	ASN	ASN	L	L	65 - 223	63 - 221

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
40
41
42
43
44
45
46
47
48
49
50
51
52
53
54
55
56
57
58
59
60
61
62
63
64
65
66
67
68
69
70
71
72
73
74
75
76
77
78
79
80
81
82
83
84
85
86
87
88
89
90
91
92
93
94
95
96
97
98
99
100
101
102
103
104
105
106
107
108
109
110
111
112
113
114
115
116
117
118
119
120
121
122
123
124
125
126
127
128
129
130
131
132

Components

#1: Protein

A B C D E F G H I J K L
Green to red photoconvertible GFP-like protein EosFP

Details:

Mass: 25893.434 Da / Num. of mol.: 12 / Mutation: A69T
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lobophyllia hemprichii (invertebrata) / Plasmid: pRSET-A / Production host: Escherichia coli (E. coli) / References: UniProt: Q5S6Z9

#2: Water

ChemComp-HOH / water

Details:

Mass: 18.015 Da / Num. of mol.: 471 / Source method: isolated from a natural source / Formula: H₂O

Experimental details

Experiment

• Experiment: Method: X-RAY DIFFRACTION

Sample preparation

• Crystal: Density Matthews: 2.15 ų/Da / Density % sol: 42.71 %
• Crystal grow: Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 9 ; Details: 0.2 M chloride hexahydrate, 0.1 M Tris, 30% w/v polyethylene glycol 3,350

Data collection

• Diffraction: Mean temperature: 100 K
• Diffraction source: Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-2 / Wavelength: 0.872 Å
• Detector: Type: DECTRIS PILATUS 2M / Detector: PIXEL / Date: May 15, 2014
• Radiation: Monochromator: Si (111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
• Radiation wavelength: Wavelength: 0.872 Å / Relative weight: 1
• Reflection: Resolution: 2.7→95.45 Å / Num. obs: 67723 / % possible obs: 95.42 % / Redundancy: 1.7 % / B_iso Wilson estimate: 35.46 Ų / R_sym value: 0.101 / Net I/σ(I): 6.9
• Reflection shell: Resolution: 2.7→2.78 Å / Redundancy: 1.7 % / Mean I/σ(I) obs: 1.8 / % possible all: 95.48

Processing

Software

Name	Version	Classification
REFMAC	5.8.0071	refinement
XDS		data reduction
XSCALE		data scaling
PHASER		phasing

Refinement

Method to determine structure: MOLECULAR REPLACEMENT
Starting model: 3S05

3s05

Resolution: 2.7→95.45 Å / Cor.coef. F_o:F_c: 0.924 / Cor.coef. F_o:F_c free: 0.91 / SU B: 15.972 / SU ML: 0.3 / Cross valid method: THROUGHOUT / ESU R Free: 0.377 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	Rfactor	Num. reflection	% reflection	Selection details
Rfree	0.23151	3344	4.9 %	RANDOM
Rwork	0.21088	-	-	-
obs	0.21189	64379	95.4 %	-

• Solvent computation: Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK

Displacement parameters

B_iso mean: 35.66 Ų

	Baniso -1	Baniso -2	Baniso -3
1-	0.03 Å2	0.06 Å2	-0.01 Å2
2-	-	-0.09 Å2	0.01 Å2
3-	-	-	0.04 Å2

Refinement step

Cycle: LAST / Resolution: 2.7→95.45 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	21444	0	0	471	21915

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.005	0.019	22056
X-RAY DIFFRACTION	r_bond_other_d	0.004	0.02	20412
X-RAY DIFFRACTION	r_angle_refined_deg	1.195	1.963	29688
X-RAY DIFFRACTION	r_angle_other_deg	0.968	3	47172
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	7.335	5	2604
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	31.315	24.157	1068
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	15.77	15	3756
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	17.726	15	96
X-RAY DIFFRACTION	r_chiral_restr	0.064	0.2	3000
X-RAY DIFFRACTION	r_gen_planes_refined	0.01	0.021	24816
X-RAY DIFFRACTION	r_gen_planes_other	0.008	0.02	5280
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	2.114	3.43	10512
X-RAY DIFFRACTION	r_mcbond_other	2.113	3.429	10511
X-RAY DIFFRACTION	r_mcangle_it	3.407	5.139	13068
X-RAY DIFFRACTION	r_mcangle_other	3.408	5.139	13069
X-RAY DIFFRACTION	r_scbond_it	2.414	3.644	11544
X-RAY DIFFRACTION	r_scbond_other	2.414	3.645	11545
X-RAY DIFFRACTION	r_scangle_it
X-RAY DIFFRACTION	r_scangle_other	3.941	5.358	16621
X-RAY DIFFRACTION	r_long_range_B_refined	6.237	26.596	23250
X-RAY DIFFRACTION	r_long_range_B_other	6.226	26.605	23185
X-RAY DIFFRACTION	r_rigid_bond_restr
X-RAY DIFFRACTION	r_sphericity_free
X-RAY DIFFRACTION	r_sphericity_bonded

Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-ID	Dom-ID	Auth asym-ID	Number	Rms dev position (Å)
1	1	A	2949	0.14
1	2	B	2949	0.14
2	1	A	2905	0.17
2	2	C	2905	0.17
3	1	A	2925	0.16
3	2	D	2925	0.16
4	1	A	2916	0.15
4	2	E	2916	0.15
5	1	A	2875	0.15
5	2	F	2875	0.15
6	1	A	2921	0.15
6	2	G	2921	0.15
7	1	A	2976	0.15
7	2	H	2976	0.15
8	1	A	2915	0.16
8	2	I	2915	0.16
9	1	A	2961	0.14
9	2	J	2961	0.14
10	1	A	2945	0.15
10	2	K	2945	0.15
11	1	A	2883	0.16
11	2	L	2883	0.16
12	1	A	8641	0.11
12	2	B	8641	0.11
13	1	A	8727	0.11
13	2	C	8727	0.11
14	1	A	8515	0.13
14	2	D	8515	0.13
15	1	A	8601	0.11
15	2	E	8601	0.11
16	1	A	8543	0.12
16	2	F	8543	0.12
17	1	A	8472	0.12
17	2	G	8472	0.12
18	1	A	8528	0.12
18	2	H	8528	0.12
19	1	A	8589	0.12
19	2	I	8589	0.12
20	1	A	8518	0.12
20	2	J	8518	0.12
21	1	A	8488	0.13
21	2	K	8488	0.13
22	1	A	8730	0.11
22	2	L	8730	0.11
23	1	B	2979	0.15
23	2	C	2979	0.15
24	1	B	3021	0.14
24	2	D	3021	0.14
25	1	B	3150	0.09
25	2	E	3150	0.09
26	1	B	3007	0.14
26	2	F	3007	0.14
27	1	B	2977	0.14
27	2	G	2977	0.14
28	1	B	3028	0.12
28	2	H	3028	0.12
29	1	B	2993	0.14
29	2	I	2993	0.14
30	1	B	3034	0.13
30	2	J	3034	0.13
31	1	B	2957	0.14
31	2	K	2957	0.14
32	1	B	2986	0.12
32	2	L	2986	0.12
33	1	B	8638	0.12
33	2	C	8638	0.12
34	1	B	8626	0.13
34	2	D	8626	0.13
35	1	B	8600	0.12
35	2	E	8600	0.12
36	1	B	8526	0.12
36	2	F	8526	0.12
37	1	B	8456	0.13
37	2	G	8456	0.13
38	1	B	8626	0.12
38	2	H	8626	0.12
39	1	B	8531	0.12
39	2	I	8531	0.12
40	1	B	8482	0.13
40	2	J	8482	0.13
41	1	B	8537	0.12
41	2	K	8537	0.12
42	1	B	8702	0.11
42	2	L	8702	0.11
43	1	C	2976	0.13
43	2	D	2976	0.13
44	1	C	2949	0.14
44	2	E	2949	0.14
45	1	C	2928	0.16
45	2	F	2928	0.16
46	1	C	2949	0.16
46	2	G	2949	0.16
47	1	C	2975	0.15
47	2	H	2975	0.15
48	1	C	3042	0.14
48	2	I	3042	0.14
49	1	C	2996	0.14
49	2	J	2996	0.14
50	1	C	2942	0.15
50	2	K	2942	0.15
51	1	C	2925	0.15
51	2	L	2925	0.15
52	1	C	8546	0.13
52	2	D	8546	0.13
53	1	C	8678	0.11
53	2	E	8678	0.11
54	1	C	8607	0.12
54	2	F	8607	0.12
55	1	C	8517	0.12
55	2	G	8517	0.12
56	1	C	8643	0.12
56	2	H	8643	0.12
57	1	C	8581	0.12
57	2	I	8581	0.12
58	1	C	8555	0.12
58	2	J	8555	0.12
59	1	C	8445	0.13
59	2	K	8445	0.13
60	1	C	8717	0.11
60	2	L	8717	0.11
61	1	D	3016	0.13
61	2	E	3016	0.13
62	1	D	2963	0.14
62	2	F	2963	0.14
63	1	D	2968	0.16
63	2	G	2968	0.16
64	1	D	3036	0.13
64	2	H	3036	0.13
65	1	D	2977	0.14
65	2	I	2977	0.14
66	1	D	3012	0.14
66	2	J	3012	0.14
67	1	D	3007	0.13
67	2	K	3007	0.13
68	1	D	2973	0.15
68	2	L	2973	0.15
69	1	D	8555	0.12
69	2	E	8555	0.12
70	1	D	8410	0.13
70	2	F	8410	0.13
71	1	D	8516	0.12
71	2	G	8516	0.12
72	1	D	8462	0.13
72	2	H	8462	0.13
73	1	D	8491	0.13
73	2	I	8491	0.13
74	1	D	8401	0.14
74	2	J	8401	0.14
75	1	D	8322	0.14
75	2	K	8322	0.14
76	1	D	8600	0.12
76	2	L	8600	0.12
77	1	E	3006	0.14
77	2	F	3006	0.14
78	1	E	2973	0.14
78	2	G	2973	0.14
79	1	E	3029	0.11
79	2	H	3029	0.11
80	1	E	2959	0.14
80	2	I	2959	0.14
81	1	E	3006	0.13
81	2	J	3006	0.13
82	1	E	2940	0.14
82	2	K	2940	0.14
83	1	E	2974	0.13
83	2	L	2974	0.13
84	1	E	8575	0.12
84	2	F	8575	0.12
85	1	E	8633	0.12
85	2	G	8633	0.12
86	1	E	8564	0.12
86	2	H	8564	0.12
87	1	E	8577	0.12
87	2	I	8577	0.12
88	1	E	8583	0.12
88	2	J	8583	0.12
89	1	E	8435	0.13
89	2	K	8435	0.13
90	1	E	8578	0.11
90	2	L	8578	0.11
91	1	F	2926	0.13
91	2	G	2926	0.13
92	1	F	2944	0.14
92	2	H	2944	0.14
93	1	F	2878	0.16
93	2	I	2878	0.16
94	1	F	2947	0.14
94	2	J	2947	0.14
95	1	F	2883	0.15
95	2	K	2883	0.15
96	1	F	2865	0.16
96	2	L	2865	0.16
97	1	F	8472	0.13
97	2	G	8472	0.13
98	1	F	8506	0.12
98	2	H	8506	0.12
99	1	F	8550	0.12
99	2	I	8550	0.12
100	1	F	8446	0.13
100	2	J	8446	0.13
101	1	F	8567	0.13
101	2	K	8567	0.13
102	1	F	8520	0.12
102	2	L	8520	0.12
103	1	G	3067	0.12
103	2	H	3067	0.12
104	1	G	2988	0.14
104	2	I	2988	0.14
105	1	G	2968	0.14
105	2	J	2968	0.14
106	1	G	2978	0.15
106	2	K	2978	0.15
107	1	G	2981	0.14
107	2	L	2981	0.14
108	1	G	8404	0.13
108	2	H	8404	0.13
109	1	G	8589	0.12
109	2	I	8589	0.12
110	1	G	8362	0.14
110	2	J	8362	0.14
111	1	G	8437	0.14
111	2	K	8437	0.14
112	1	G	8409	0.13
112	2	L	8409	0.13
113	1	H	2961	0.15
113	2	I	2961	0.15
114	1	H	3039	0.11
114	2	J	3039	0.11
115	1	H	3041	0.13
115	2	K	3041	0.13
116	1	H	3058	0.13
116	2	L	3058	0.13
117	1	H	8473	0.12
117	2	I	8473	0.12
118	1	H	8503	0.13
118	2	J	8503	0.13
119	1	H	8346	0.14
119	2	K	8346	0.14
120	1	H	8576	0.12
120	2	L	8576	0.12
121	1	I	2951	0.15
121	2	J	2951	0.15
122	1	I	2945	0.15
122	2	K	2945	0.15
123	1	I	2916	0.16
123	2	L	2916	0.16
124	1	I	8426	0.14
124	2	J	8426	0.14
125	1	I	8507	0.13
125	2	K	8507	0.13
126	1	I	8565	0.12
126	2	L	8565	0.12
127	1	J	2990	0.13
127	2	K	2990	0.13
128	1	J	3005	0.14
128	2	L	3005	0.14
129	1	J	8352	0.14
129	2	K	8352	0.14
130	1	J	8512	0.13
130	2	L	8512	0.13
131	1	K	3007	0.13
131	2	L	3007	0.13
132	1	K	8490	0.13
132	2	L	8490	0.13

LS refinement shell

Resolution: 2.7→2.77 Å / Total num. of bins used: 20

	Rfactor	Num. reflection	% reflection
Rfree	0.332	259	-
Rwork	0.32	4771	-
obs	-	-	95.45 %