PDB-8p1f: X-ray structure of acetylcholine-binding protein (AChBP) in compl...

Basic information

• Entry: Database: PDB / ID: 8p1f
• Title: X-ray structure of acetylcholine-binding protein (AChBP) in complex with FL001909.
• Components: Acetylcholine-binding protein
• Keywords: CHOLINE-BINDING PROTEIN / Fragment based drug design / Acetylcholine-binding protein / choline-binding proteins

Function / homology

Function:

acetylcholine receptor activity / acetylcholine-gated monoatomic cation-selective channel activity / synaptic cleft / response to nicotine / neuron projection / synapse / membrane

Domain/homology:

Neurotransmitter-gated ion-channel / Neurotransmitter-gated ion-channel ligand-binding domain / Neurotransmitter-gated ion-channel ligand-binding domain superfamily / Neurotransmitter-gated ion-channel ligand binding domain / Ig-like domain profile. / Immunoglobulin-like domain

Component:

: / Acetylcholine-binding protein

• Biological species: Lymnaea stagnalis (great pond snail)
• Method: X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å
• Authors: Cederfelt, D. / Boronat, P. / Dobritzsch, D. / Hennig, S. / Fitzgerald, E.A. / de Esch, I.J.P. / Danielson, U.H.

Funding support

European Union, 1items

Organization	Grant number	Country
Marie Sklodowska-Curie Actions, FragNET ITN	675899	European Union

• Citation: Journal: To Be Published; Title: Elucidating the regulation of ligand gated ion channels via biophysical studies of ligand-induced conformational dynamics of acetylcholine binding proteins; Authors: Fitzgerald, E.A. / Cederfelt, D. / Boronat, P. / Aarmo Lund, B. / de Esch, I.J.P. / Danielson, U.H.

History

Deposition	May 12, 2023	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	May 8, 2024	Provider: repository / Type: Initial release

Assembly

Deposited unit

A: Acetylcholine-binding protein

B: Acetylcholine-binding protein

C: Acetylcholine-binding protein

D: Acetylcholine-binding protein

E: Acetylcholine-binding protein

F: Acetylcholine-binding protein

G: Acetylcholine-binding protein

H: Acetylcholine-binding protein

I: Acetylcholine-binding protein

J: Acetylcholine-binding protein

K: Acetylcholine-binding protein

L: Acetylcholine-binding protein

M: Acetylcholine-binding protein

N: Acetylcholine-binding protein

O: Acetylcholine-binding protein

P: Acetylcholine-binding protein

Q: Acetylcholine-binding protein

R: Acetylcholine-binding protein

S: Acetylcholine-binding protein

T: Acetylcholine-binding protein

hetero molecules

Summary:

• 545 kDa, 20 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	544,743	36
Polymers	541,206	20
Non-polymers	3,537	16
Water	12,665	703

1

A: Acetylcholine-binding protein

B: Acetylcholine-binding protein

C: Acetylcholine-binding protein

D: Acetylcholine-binding protein

E: Acetylcholine-binding protein

hetero molecules

Summary:

• defined by author
• Evidence: surface plasmon resonance
• 136 kDa, 5 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	135,964	8
Polymers	135,302	5
Non-polymers	663	3
Water	90	5

Symmetry operations:

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

Calculated values:

Buried area	13780 Å2
ΔGint	-56 kcal/mol
Surface area	43030 Å2

2

F: Acetylcholine-binding protein

G: Acetylcholine-binding protein

H: Acetylcholine-binding protein

I: Acetylcholine-binding protein

J: Acetylcholine-binding protein

hetero molecules

Summary:

• defined by author
• 136 kDa, 5 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	136,406	10
Polymers	135,302	5
Non-polymers	1,104	5
Water	90	5

Symmetry operations:

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

Calculated values:

Buried area	13910 Å2
ΔGint	-47 kcal/mol
Surface area	42860 Å2

3

K: Acetylcholine-binding protein

L: Acetylcholine-binding protein

M: Acetylcholine-binding protein

N: Acetylcholine-binding protein

O: Acetylcholine-binding protein

hetero molecules

Summary:

• defined by author
• 136 kDa, 5 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	136,408	10
Polymers	135,302	5
Non-polymers	1,106	5
Water	90	5

Symmetry operations:

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

Calculated values:

Buried area	14410 Å2
ΔGint	-49 kcal/mol
Surface area	43320 Å2

4

P: Acetylcholine-binding protein

Q: Acetylcholine-binding protein

R: Acetylcholine-binding protein

S: Acetylcholine-binding protein

T: Acetylcholine-binding protein

hetero molecules

Summary:

• defined by author
• 136 kDa, 5 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	135,965	8
Polymers	135,302	5
Non-polymers	664	3
Water	90	5

Symmetry operations:

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

Calculated values:

Buried area	14360 Å2
ΔGint	-51 kcal/mol
Surface area	42730 Å2

Unit cell

Length a, b, c (Å)	116.710, 140.710, 147.170
Angle α, β, γ (deg.)	90.00, 109.68, 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
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	M
1	13	A
2	13	N
1	14	A
2	14	O
1	15	A
2	15	P
1	16	A
2	16	Q
1	17	A
2	17	R
1	18	A
2	18	S
1	19	A
2	19	T
1	20	B
2	20	C
1	21	B
2	21	D
1	22	B
2	22	E
1	23	B
2	23	F
1	24	B
2	24	G
1	25	B
2	25	H
1	26	B
2	26	I
1	27	B
2	27	J
1	28	B
2	28	K
1	29	B
2	29	L
1	30	B
2	30	M
1	31	B
2	31	N
1	32	B
2	32	O
1	33	B
2	33	P
1	34	B
2	34	Q
1	35	B
2	35	R
1	36	B
2	36	S
1	37	B
2	37	T
1	38	C
2	38	D
1	39	C
2	39	E
1	40	C
2	40	F
1	41	C
2	41	G
1	42	C
2	42	H
1	43	C
2	43	I
1	44	C
2	44	J
1	45	C
2	45	K
1	46	C
2	46	L
1	47	C
2	47	M
1	48	C
2	48	N
1	49	C
2	49	O
1	50	C
2	50	P
1	51	C
2	51	Q
1	52	C
2	52	R
1	53	C
2	53	S
1	54	C
2	54	T
1	55	D
2	55	E
1	56	D
2	56	F
1	57	D
2	57	G
1	58	D
2	58	H
1	59	D
2	59	I
1	60	D
2	60	J
1	61	D
2	61	K
1	62	D
2	62	L
1	63	D
2	63	M
1	64	D
2	64	N
1	65	D
2	65	O
1	66	D
2	66	P
1	67	D
2	67	Q
1	68	D
2	68	R
1	69	D
2	69	S
1	70	D
2	70	T
1	71	E
2	71	F
1	72	E
2	72	G
1	73	E
2	73	H
1	74	E
2	74	I
1	75	E
2	75	J
1	76	E
2	76	K
1	77	E
2	77	L
1	78	E
2	78	M
1	79	E
2	79	N
1	80	E
2	80	O
1	81	E
2	81	P
1	82	E
2	82	Q
1	83	E
2	83	R
1	84	E
2	84	S
1	85	E
2	85	T
1	86	F
2	86	G
1	87	F
2	87	H
1	88	F
2	88	I
1	89	F
2	89	J
1	90	F
2	90	K
1	91	F
2	91	L
1	92	F
2	92	M
1	93	F
2	93	N
1	94	F
2	94	O
1	95	F
2	95	P
1	96	F
2	96	Q
1	97	F
2	97	R
1	98	F
2	98	S
1	99	F
2	99	T
1	100	G
2	100	H
1	101	G
2	101	I
1	102	G
2	102	J
1	103	G
2	103	K
1	104	G
2	104	L
1	105	G
2	105	M
1	106	G
2	106	N
1	107	G
2	107	O
1	108	G
2	108	P
1	109	G
2	109	Q
1	110	G
2	110	R
1	111	G
2	111	S
1	112	G
2	112	T
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	M
1	118	H
2	118	N
1	119	H
2	119	O
1	120	H
2	120	P
1	121	H
2	121	Q
1	122	H
2	122	R
1	123	H
2	123	S
1	124	H
2	124	T
1	125	I
2	125	J
1	126	I
2	126	K
1	127	I
2	127	L
1	128	I
2	128	M
1	129	I
2	129	N
1	130	I
2	130	O
1	131	I
2	131	P
1	132	I
2	132	Q
1	133	I
2	133	R
1	134	I
2	134	S
1	135	I
2	135	T
1	136	J
2	136	K
1	137	J
2	137	L
1	138	J
2	138	M
1	139	J
2	139	N
1	140	J
2	140	O
1	141	J
2	141	P
1	142	J
2	142	Q
1	143	J
2	143	R
1	144	J
2	144	S
1	145	J
2	145	T
1	146	K
2	146	L
1	147	K
2	147	M
1	148	K
2	148	N
1	149	K
2	149	O
1	150	K
2	150	P
1	151	K
2	151	Q
1	152	K
2	152	R
1	153	K
2	153	S
1	154	K
2	154	T
1	155	L
2	155	M
1	156	L
2	156	N
1	157	L
2	157	O
1	158	L
2	158	P
1	159	L
2	159	Q
1	160	L
2	160	R
1	161	L
2	161	S
1	162	L
2	162	T
1	163	M
2	163	N
1	164	M
2	164	O
1	165	M
2	165	P
1	166	M
2	166	Q
1	167	M
2	167	R
1	168	M
2	168	S
1	169	M
2	169	T
1	170	N
2	170	O
1	171	N
2	171	P
1	172	N
2	172	Q
1	173	N
2	173	R
1	174	N
2	174	S
1	175	N
2	175	T
1	176	O
2	176	P
1	177	O
2	177	Q
1	178	O
2	178	R
1	179	O
2	179	S
1	180	O
2	180	T
1	181	P
2	181	Q
1	182	P
2	182	R
1	183	P
2	183	S
1	184	P
2	184	T
1	185	Q
2	185	R
1	186	Q
2	186	S
1	187	Q
2	187	T
1	188	R
2	188	S
1	189	R
2	189	T
1	190	S
2	190	T

NCS domain segments:

Component-ID: 0 / Beg auth comp-ID: LEU / Beg label comp-ID: LEU / Refine code: 0

Dom-ID	Ens-ID	End auth comp-ID	End label comp-ID	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	LYS	LYS	A	A	20 - 223	20 - 223
2	1	LYS	LYS	B	B	20 - 223	20 - 223
1	2	LYS	LYS	A	A	20 - 223	20 - 223
2	2	LYS	LYS	C	C	20 - 223	20 - 223
1	3	LYS	LYS	A	A	20 - 222	20 - 222
2	3	LYS	LYS	D	D	20 - 222	20 - 222
1	4	LYS	LYS	A	A	20 - 223	20 - 223
2	4	LYS	LYS	E	E	20 - 223	20 - 223
1	5	LYS	LYS	A	A	20 - 223	20 - 223
2	5	LYS	LYS	F	F	20 - 223	20 - 223
1	6	LYS	LYS	A	A	20 - 223	20 - 223
2	6	LYS	LYS	G	G	20 - 223	20 - 223
1	7	LYS	LYS	A	A	20 - 223	20 - 223
2	7	LYS	LYS	H	H	20 - 223	20 - 223
1	8	LYS	LYS	A	A	20 - 223	20 - 223
2	8	LYS	LYS	I	I	20 - 223	20 - 223
1	9	LYS	LYS	A	A	20 - 223	20 - 223
2	9	LYS	LYS	J	J	20 - 223	20 - 223
1	10	LYS	LYS	A	A	20 - 223	20 - 223
2	10	LYS	LYS	K	K	20 - 223	20 - 223
1	11	LYS	LYS	A	A	20 - 222	20 - 222
2	11	LYS	LYS	L	L	20 - 222	20 - 222
1	12	LYS	LYS	A	A	20 - 223	20 - 223
2	12	LYS	LYS	M	M	20 - 223	20 - 223
1	13	LYS	LYS	A	A	20 - 223	20 - 223
2	13	LYS	LYS	N	N	20 - 223	20 - 223
1	14	LYS	LYS	A	A	20 - 223	20 - 223
2	14	LYS	LYS	O	O	20 - 223	20 - 223
1	15	LYS	LYS	A	A	20 - 223	20 - 223
2	15	LYS	LYS	P	P	20 - 223	20 - 223
1	16	LYS	LYS	A	A	20 - 223	20 - 223
2	16	LYS	LYS	Q	Q	20 - 223	20 - 223
1	17	LYS	LYS	A	A	20 - 223	20 - 223
2	17	LYS	LYS	R	R	20 - 223	20 - 223
1	18	LYS	LYS	A	A	20 - 223	20 - 223
2	18	LYS	LYS	S	S	20 - 223	20 - 223
1	19	LYS	LYS	A	A	20 - 222	20 - 222
2	19	LYS	LYS	T	T	20 - 222	20 - 222
1	20	LYS	LYS	B	B	20 - 222	20 - 222
2	20	LYS	LYS	C	C	20 - 222	20 - 222
1	21	LYS	LYS	B	B	20 - 222	20 - 222
2	21	LYS	LYS	D	D	20 - 222	20 - 222
1	22	LYS	LYS	B	B	20 - 222	20 - 222
2	22	LYS	LYS	E	E	20 - 222	20 - 222
1	23	LYS	LYS	B	B	20 - 223	20 - 223
2	23	LYS	LYS	F	F	20 - 223	20 - 223
1	24	LYS	LYS	B	B	20 - 223	20 - 223
2	24	LYS	LYS	G	G	20 - 223	20 - 223
1	25	LYS	LYS	B	B	20 - 222	20 - 222
2	25	LYS	LYS	H	H	20 - 222	20 - 222
1	26	LYS	LYS	B	B	20 - 223	20 - 223
2	26	LYS	LYS	I	I	20 - 223	20 - 223
1	27	LYS	LYS	B	B	20 - 223	20 - 223
2	27	LYS	LYS	J	J	20 - 223	20 - 223
1	28	LYS	LYS	B	B	20 - 223	20 - 223
2	28	LYS	LYS	K	K	20 - 223	20 - 223
1	29	LYS	LYS	B	B	20 - 223	20 - 223
2	29	LYS	LYS	L	L	20 - 223	20 - 223
1	30	LYS	LYS	B	B	20 - 223	20 - 223
2	30	LYS	LYS	M	M	20 - 223	20 - 223
1	31	LYS	LYS	B	B	20 - 223	20 - 223
2	31	LYS	LYS	N	N	20 - 223	20 - 223
1	32	LYS	LYS	B	B	20 - 223	20 - 223
2	32	LYS	LYS	O	O	20 - 223	20 - 223
1	33	LYS	LYS	B	B	20 - 223	20 - 223
2	33	LYS	LYS	P	P	20 - 223	20 - 223
1	34	LYS	LYS	B	B	20 - 223	20 - 223
2	34	LYS	LYS	Q	Q	20 - 223	20 - 223
1	35	LYS	LYS	B	B	20 - 223	20 - 223
2	35	LYS	LYS	R	R	20 - 223	20 - 223
1	36	LYS	LYS	B	B	20 - 223	20 - 223
2	36	LYS	LYS	S	S	20 - 223	20 - 223
1	37	LYS	LYS	B	B	20 - 222	20 - 222
2	37	LYS	LYS	T	T	20 - 222	20 - 222
1	38	LYS	LYS	C	C	20 - 223	20 - 223
2	38	LYS	LYS	D	D	20 - 223	20 - 223
1	39	GLY	GLY	C	C	20 - 224	20 - 224
2	39	GLY	GLY	E	E	20 - 224	20 - 224
1	40	GLY	GLY	C	C	20 - 224	20 - 224
2	40	GLY	GLY	F	F	20 - 224	20 - 224
1	41	LYS	LYS	C	C	20 - 223	20 - 223
2	41	LYS	LYS	G	G	20 - 223	20 - 223
1	42	GLY	GLY	C	C	20 - 224	20 - 224
2	42	GLY	GLY	H	H	20 - 224	20 - 224
1	43	GLY	GLY	C	C	20 - 224	20 - 224
2	43	GLY	GLY	I	I	20 - 224	20 - 224
1	44	GLY	GLY	C	C	20 - 224	20 - 224
2	44	GLY	GLY	J	J	20 - 224	20 - 224
1	45	LYS	LYS	C	C	20 - 223	20 - 223
2	45	LYS	LYS	K	K	20 - 223	20 - 223
1	46	GLY	GLY	C	C	20 - 224	20 - 224
2	46	GLY	GLY	L	L	20 - 224	20 - 224
1	47	LYS	LYS	C	C	20 - 222	20 - 222
2	47	LYS	LYS	M	M	20 - 222	20 - 222
1	48	LYS	LYS	C	C	20 - 223	20 - 223
2	48	LYS	LYS	N	N	20 - 223	20 - 223
1	49	LYS	LYS	C	C	20 - 223	20 - 223
2	49	LYS	LYS	O	O	20 - 223	20 - 223
1	50	LYS	LYS	C	C	20 - 223	20 - 223
2	50	LYS	LYS	P	P	20 - 223	20 - 223
1	51	LYS	LYS	C	C	20 - 223	20 - 223
2	51	LYS	LYS	Q	Q	20 - 223	20 - 223
1	52	LYS	LYS	C	C	20 - 222	20 - 222
2	52	LYS	LYS	R	R	20 - 222	20 - 222
1	53	GLY	GLY	C	C	20 - 224	20 - 224
2	53	GLY	GLY	S	S	20 - 224	20 - 224
1	54	LYS	LYS	C	C	20 - 223	20 - 223
2	54	LYS	LYS	T	T	20 - 223	20 - 223
1	55	LYS	LYS	D	D	20 - 223	20 - 223
2	55	LYS	LYS	E	E	20 - 223	20 - 223
1	56	GLY	GLY	D	D	20 - 224	20 - 224
2	56	GLY	GLY	F	F	20 - 224	20 - 224
1	57	LYS	LYS	D	D	20 - 223	20 - 223
2	57	LYS	LYS	G	G	20 - 223	20 - 223
1	58	LYS	LYS	D	D	20 - 223	20 - 223
2	58	LYS	LYS	H	H	20 - 223	20 - 223
1	59	GLY	GLY	D	D	20 - 224	20 - 224
2	59	GLY	GLY	I	I	20 - 224	20 - 224
1	60	ARG	ARG	D	D	20 - 225	20 - 225
2	60	ARG	ARG	J	J	20 - 225	20 - 225
1	61	LYS	LYS	D	D	20 - 222	20 - 222
2	61	LYS	LYS	K	K	20 - 222	20 - 222
1	62	GLY	GLY	D	D	20 - 224	20 - 224
2	62	GLY	GLY	L	L	20 - 224	20 - 224
1	63	LYS	LYS	D	D	20 - 222	20 - 222
2	63	LYS	LYS	M	M	20 - 222	20 - 222
1	64	LYS	LYS	D	D	20 - 222	20 - 222
2	64	LYS	LYS	N	N	20 - 222	20 - 222
1	65	LYS	LYS	D	D	20 - 222	20 - 222
2	65	LYS	LYS	O	O	20 - 222	20 - 222
1	66	LYS	LYS	D	D	20 - 223	20 - 223
2	66	LYS	LYS	P	P	20 - 223	20 - 223
1	67	LYS	LYS	D	D	20 - 223	20 - 223
2	67	LYS	LYS	Q	Q	20 - 223	20 - 223
1	68	LYS	LYS	D	D	20 - 222	20 - 222
2	68	LYS	LYS	R	R	20 - 222	20 - 222
1	69	ARG	ARG	D	D	20 - 225	20 - 225
2	69	ARG	ARG	S	S	20 - 225	20 - 225
1	70	ARG	ARG	D	D	20 - 225	20 - 225
2	70	ARG	ARG	T	T	20 - 225	20 - 225
1	71	GLY	GLY	E	E	20 - 224	20 - 224
2	71	GLY	GLY	F	F	20 - 224	20 - 224
1	72	LYS	LYS	E	E	20 - 223	20 - 223
2	72	LYS	LYS	G	G	20 - 223	20 - 223
1	73	GLY	GLY	E	E	20 - 224	20 - 224
2	73	GLY	GLY	H	H	20 - 224	20 - 224
1	74	GLY	GLY	E	E	20 - 224	20 - 224
2	74	GLY	GLY	I	I	20 - 224	20 - 224
1	75	GLY	GLY	E	E	20 - 224	20 - 224
2	75	GLY	GLY	J	J	20 - 224	20 - 224
1	76	LYS	LYS	E	E	20 - 223	20 - 223
2	76	LYS	LYS	K	K	20 - 223	20 - 223
1	77	GLY	GLY	E	E	20 - 224	20 - 224
2	77	GLY	GLY	L	L	20 - 224	20 - 224
1	78	LYS	LYS	E	E	20 - 222	20 - 222
2	78	LYS	LYS	M	M	20 - 222	20 - 222
1	79	LYS	LYS	E	E	20 - 223	20 - 223
2	79	LYS	LYS	N	N	20 - 223	20 - 223
1	80	LYS	LYS	E	E	20 - 223	20 - 223
2	80	LYS	LYS	O	O	20 - 223	20 - 223
1	81	LYS	LYS	E	E	20 - 223	20 - 223
2	81	LYS	LYS	P	P	20 - 223	20 - 223
1	82	LYS	LYS	E	E	20 - 223	20 - 223
2	82	LYS	LYS	Q	Q	20 - 223	20 - 223
1	83	LYS	LYS	E	E	20 - 222	20 - 222
2	83	LYS	LYS	R	R	20 - 222	20 - 222
1	84	GLY	GLY	E	E	20 - 224	20 - 224
2	84	GLY	GLY	S	S	20 - 224	20 - 224
1	85	LYS	LYS	E	E	20 - 223	20 - 223
2	85	LYS	LYS	T	T	20 - 223	20 - 223
1	86	LYS	LYS	F	F	20 - 223	20 - 223
2	86	LYS	LYS	G	G	20 - 223	20 - 223
1	87	GLY	GLY	F	F	20 - 224	20 - 224
2	87	GLY	GLY	H	H	20 - 224	20 - 224
1	88	GLY	GLY	F	F	20 - 224	20 - 224
2	88	GLY	GLY	I	I	20 - 224	20 - 224
1	89	GLY	GLY	F	F	20 - 224	20 - 224
2	89	GLY	GLY	J	J	20 - 224	20 - 224
1	90	LYS	LYS	F	F	20 - 223	20 - 223
2	90	LYS	LYS	K	K	20 - 223	20 - 223
1	91	GLY	GLY	F	F	20 - 224	20 - 224
2	91	GLY	GLY	L	L	20 - 224	20 - 224
1	92	LYS	LYS	F	F	20 - 223	20 - 223
2	92	LYS	LYS	M	M	20 - 223	20 - 223
1	93	LYS	LYS	F	F	20 - 223	20 - 223
2	93	LYS	LYS	N	N	20 - 223	20 - 223
1	94	LYS	LYS	F	F	20 - 223	20 - 223
2	94	LYS	LYS	O	O	20 - 223	20 - 223
1	95	LYS	LYS	F	F	20 - 223	20 - 223
2	95	LYS	LYS	P	P	20 - 223	20 - 223
1	96	LYS	LYS	F	F	20 - 223	20 - 223
2	96	LYS	LYS	Q	Q	20 - 223	20 - 223
1	97	LYS	LYS	F	F	20 - 223	20 - 223
2	97	LYS	LYS	R	R	20 - 223	20 - 223
1	98	GLY	GLY	F	F	20 - 224	20 - 224
2	98	GLY	GLY	S	S	20 - 224	20 - 224
1	99	GLY	GLY	F	F	20 - 224	20 - 224
2	99	GLY	GLY	T	T	20 - 224	20 - 224
1	100	LYS	LYS	G	G	20 - 223	20 - 223
2	100	LYS	LYS	H	H	20 - 223	20 - 223
1	101	LYS	LYS	G	G	20 - 222	20 - 222
2	101	LYS	LYS	I	I	20 - 222	20 - 222
1	102	LYS	LYS	G	G	20 - 223	20 - 223
2	102	LYS	LYS	J	J	20 - 223	20 - 223
1	103	LYS	LYS	G	G	20 - 223	20 - 223
2	103	LYS	LYS	K	K	20 - 223	20 - 223
1	104	LYS	LYS	G	G	20 - 223	20 - 223
2	104	LYS	LYS	L	L	20 - 223	20 - 223
1	105	LYS	LYS	G	G	20 - 223	20 - 223
2	105	LYS	LYS	M	M	20 - 223	20 - 223
1	106	LYS	LYS	G	G	20 - 223	20 - 223
2	106	LYS	LYS	N	N	20 - 223	20 - 223
1	107	LYS	LYS	G	G	20 - 223	20 - 223
2	107	LYS	LYS	O	O	20 - 223	20 - 223
1	108	LYS	LYS	G	G	20 - 223	20 - 223
2	108	LYS	LYS	P	P	20 - 223	20 - 223
1	109	LYS	LYS	G	G	20 - 223	20 - 223
2	109	LYS	LYS	Q	Q	20 - 223	20 - 223
1	110	LYS	LYS	G	G	20 - 223	20 - 223
2	110	LYS	LYS	R	R	20 - 223	20 - 223
1	111	LYS	LYS	G	G	20 - 222	20 - 222
2	111	LYS	LYS	S	S	20 - 222	20 - 222
1	112	LYS	LYS	G	G	20 - 223	20 - 223
2	112	LYS	LYS	T	T	20 - 223	20 - 223
1	113	GLY	GLY	H	H	20 - 224	20 - 224
2	113	GLY	GLY	I	I	20 - 224	20 - 224
1	114	GLY	GLY	H	H	20 - 224	20 - 224
2	114	GLY	GLY	J	J	20 - 224	20 - 224
1	115	LYS	LYS	H	H	20 - 223	20 - 223
2	115	LYS	LYS	K	K	20 - 223	20 - 223
1	116	GLY	GLY	H	H	20 - 224	20 - 224
2	116	GLY	GLY	L	L	20 - 224	20 - 224
1	117	LYS	LYS	H	H	20 - 222	20 - 222
2	117	LYS	LYS	M	M	20 - 222	20 - 222
1	118	LYS	LYS	H	H	20 - 223	20 - 223
2	118	LYS	LYS	N	N	20 - 223	20 - 223
1	119	LYS	LYS	H	H	20 - 223	20 - 223
2	119	LYS	LYS	O	O	20 - 223	20 - 223
1	120	LYS	LYS	H	H	20 - 223	20 - 223
2	120	LYS	LYS	P	P	20 - 223	20 - 223
1	121	LYS	LYS	H	H	20 - 223	20 - 223
2	121	LYS	LYS	Q	Q	20 - 223	20 - 223
1	122	LYS	LYS	H	H	20 - 222	20 - 222
2	122	LYS	LYS	R	R	20 - 222	20 - 222
1	123	GLY	GLY	H	H	20 - 224	20 - 224
2	123	GLY	GLY	S	S	20 - 224	20 - 224
1	124	LYS	LYS	H	H	20 - 223	20 - 223
2	124	LYS	LYS	T	T	20 - 223	20 - 223
1	125	GLY	GLY	I	I	20 - 224	20 - 224
2	125	GLY	GLY	J	J	20 - 224	20 - 224
1	126	LYS	LYS	I	I	20 - 223	20 - 223
2	126	LYS	LYS	K	K	20 - 223	20 - 223
1	127	GLY	GLY	I	I	20 - 224	20 - 224
2	127	GLY	GLY	L	L	20 - 224	20 - 224
1	128	LYS	LYS	I	I	20 - 223	20 - 223
2	128	LYS	LYS	M	M	20 - 223	20 - 223
1	129	LYS	LYS	I	I	20 - 223	20 - 223
2	129	LYS	LYS	N	N	20 - 223	20 - 223
1	130	LYS	LYS	I	I	20 - 223	20 - 223
2	130	LYS	LYS	O	O	20 - 223	20 - 223
1	131	LYS	LYS	I	I	20 - 223	20 - 223
2	131	LYS	LYS	P	P	20 - 223	20 - 223
1	132	LYS	LYS	I	I	20 - 222	20 - 222
2	132	LYS	LYS	Q	Q	20 - 222	20 - 222
1	133	LYS	LYS	I	I	20 - 223	20 - 223
2	133	LYS	LYS	R	R	20 - 223	20 - 223
1	134	LYS	LYS	I	I	20 - 223	20 - 223
2	134	LYS	LYS	S	S	20 - 223	20 - 223
1	135	GLY	GLY	I	I	20 - 224	20 - 224
2	135	GLY	GLY	T	T	20 - 224	20 - 224
1	136	LYS	LYS	J	J	20 - 223	20 - 223
2	136	LYS	LYS	K	K	20 - 223	20 - 223
1	137	GLY	GLY	J	J	20 - 224	20 - 224
2	137	GLY	GLY	L	L	20 - 224	20 - 224
1	138	LYS	LYS	J	J	20 - 223	20 - 223
2	138	LYS	LYS	M	M	20 - 223	20 - 223
1	139	LYS	LYS	J	J	20 - 223	20 - 223
2	139	LYS	LYS	N	N	20 - 223	20 - 223
1	140	LYS	LYS	J	J	20 - 223	20 - 223
2	140	LYS	LYS	O	O	20 - 223	20 - 223
1	141	LYS	LYS	J	J	20 - 223	20 - 223
2	141	LYS	LYS	P	P	20 - 223	20 - 223
1	142	LYS	LYS	J	J	20 - 223	20 - 223
2	142	LYS	LYS	Q	Q	20 - 223	20 - 223
1	143	LYS	LYS	J	J	20 - 223	20 - 223
2	143	LYS	LYS	R	R	20 - 223	20 - 223
1	144	ARG	ARG	J	J	20 - 225	20 - 225
2	144	ARG	ARG	S	S	20 - 225	20 - 225
1	145	ARG	ARG	J	J	20 - 225	20 - 225
2	145	ARG	ARG	T	T	20 - 225	20 - 225
1	146	LYS	LYS	K	K	20 - 222	20 - 222
2	146	LYS	LYS	L	L	20 - 222	20 - 222
1	147	LYS	LYS	K	K	20 - 223	20 - 223
2	147	LYS	LYS	M	M	20 - 223	20 - 223
1	148	LYS	LYS	K	K	20 - 223	20 - 223
2	148	LYS	LYS	N	N	20 - 223	20 - 223
1	149	LYS	LYS	K	K	20 - 223	20 - 223
2	149	LYS	LYS	O	O	20 - 223	20 - 223
1	150	LYS	LYS	K	K	20 - 223	20 - 223
2	150	LYS	LYS	P	P	20 - 223	20 - 223
1	151	LYS	LYS	K	K	20 - 223	20 - 223
2	151	LYS	LYS	Q	Q	20 - 223	20 - 223
1	152	LYS	LYS	K	K	20 - 223	20 - 223
2	152	LYS	LYS	R	R	20 - 223	20 - 223
1	153	LYS	LYS	K	K	20 - 223	20 - 223
2	153	LYS	LYS	S	S	20 - 223	20 - 223
1	154	LYS	LYS	K	K	20 - 222	20 - 222
2	154	LYS	LYS	T	T	20 - 222	20 - 222
1	155	LYS	LYS	L	L	20 - 223	20 - 223
2	155	LYS	LYS	M	M	20 - 223	20 - 223
1	156	LYS	LYS	L	L	20 - 222	20 - 222
2	156	LYS	LYS	N	N	20 - 222	20 - 222
1	157	LYS	LYS	L	L	20 - 222	20 - 222
2	157	LYS	LYS	O	O	20 - 222	20 - 222
1	158	LYS	LYS	L	L	20 - 223	20 - 223
2	158	LYS	LYS	P	P	20 - 223	20 - 223
1	159	LYS	LYS	L	L	20 - 223	20 - 223
2	159	LYS	LYS	Q	Q	20 - 223	20 - 223
1	160	LYS	LYS	L	L	20 - 223	20 - 223
2	160	LYS	LYS	R	R	20 - 223	20 - 223
1	161	GLY	GLY	L	L	20 - 224	20 - 224
2	161	GLY	GLY	S	S	20 - 224	20 - 224
1	162	GLY	GLY	L	L	20 - 224	20 - 224
2	162	GLY	GLY	T	T	20 - 224	20 - 224
1	163	LYS	LYS	M	M	20 - 223	20 - 223
2	163	LYS	LYS	N	N	20 - 223	20 - 223
1	164	LYS	LYS	M	M	20 - 223	20 - 223
2	164	LYS	LYS	O	O	20 - 223	20 - 223
1	165	LYS	LYS	M	M	20 - 223	20 - 223
2	165	LYS	LYS	P	P	20 - 223	20 - 223
1	166	LYS	LYS	M	M	20 - 223	20 - 223
2	166	LYS	LYS	Q	Q	20 - 223	20 - 223
1	167	LYS	LYS	M	M	20 - 223	20 - 223
2	167	LYS	LYS	R	R	20 - 223	20 - 223
1	168	LYS	LYS	M	M	20 - 223	20 - 223
2	168	LYS	LYS	S	S	20 - 223	20 - 223
1	169	LYS	LYS	M	M	20 - 222	20 - 222
2	169	LYS	LYS	T	T	20 - 222	20 - 222
1	170	LYS	LYS	N	N	20 - 223	20 - 223
2	170	LYS	LYS	O	O	20 - 223	20 - 223
1	171	LYS	LYS	N	N	20 - 223	20 - 223
2	171	LYS	LYS	P	P	20 - 223	20 - 223
1	172	LYS	LYS	N	N	20 - 223	20 - 223
2	172	LYS	LYS	Q	Q	20 - 223	20 - 223
1	173	LYS	LYS	N	N	20 - 223	20 - 223
2	173	LYS	LYS	R	R	20 - 223	20 - 223
1	174	LYS	LYS	N	N	20 - 223	20 - 223
2	174	LYS	LYS	S	S	20 - 223	20 - 223
1	175	LYS	LYS	N	N	20 - 222	20 - 222
2	175	LYS	LYS	T	T	20 - 222	20 - 222
1	176	LYS	LYS	O	O	20 - 223	20 - 223
2	176	LYS	LYS	P	P	20 - 223	20 - 223
1	177	LYS	LYS	O	O	20 - 223	20 - 223
2	177	LYS	LYS	Q	Q	20 - 223	20 - 223
1	178	LYS	LYS	O	O	20 - 223	20 - 223
2	178	LYS	LYS	R	R	20 - 223	20 - 223
1	179	LYS	LYS	O	O	20 - 223	20 - 223
2	179	LYS	LYS	S	S	20 - 223	20 - 223
1	180	LYS	LYS	O	O	20 - 222	20 - 222
2	180	LYS	LYS	T	T	20 - 222	20 - 222
1	181	LYS	LYS	P	P	20 - 223	20 - 223
2	181	LYS	LYS	Q	Q	20 - 223	20 - 223
1	182	LYS	LYS	P	P	20 - 223	20 - 223
2	182	LYS	LYS	R	R	20 - 223	20 - 223
1	183	LYS	LYS	P	P	20 - 223	20 - 223
2	183	LYS	LYS	S	S	20 - 223	20 - 223
1	184	LYS	LYS	P	P	20 - 223	20 - 223
2	184	LYS	LYS	T	T	20 - 223	20 - 223
1	185	LYS	LYS	Q	Q	20 - 223	20 - 223
2	185	LYS	LYS	R	R	20 - 223	20 - 223
1	186	LYS	LYS	Q	Q	20 - 222	20 - 222
2	186	LYS	LYS	S	S	20 - 222	20 - 222
1	187	LYS	LYS	Q	Q	20 - 223	20 - 223
2	187	LYS	LYS	T	T	20 - 223	20 - 223
1	188	LYS	LYS	R	R	20 - 223	20 - 223
2	188	LYS	LYS	S	S	20 - 223	20 - 223
1	189	LYS	LYS	R	R	20 - 222	20 - 222
2	189	LYS	LYS	T	T	20 - 222	20 - 222
1	190	ARG	ARG	S	S	20 - 225	20 - 225
2	190	ARG	ARG	T	T	20 - 225	20 - 225

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
133
134
135
136
137
138
139
140
141
142
143
144
145
146
147
148
149
150
151
152
153
154
155
156
157
158
159
160
161
162
163
164
165
166
167
168
169
170
171
172
173
174
175
176
177
178
179
180
181
182
183
184
185
186
187
188
189
190

Components

#1: Protein

A B C D E F G H I J K L M N O P Q R S T
Acetylcholine-binding protein / ACh-binding protein / AchBP

Details:

Mass: 27060.320 Da / Num. of mol.: 20
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lymnaea stagnalis (great pond snail) / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P58154

#2: Sugar

C-301 E-302 F-301 I-302 J-301 K-301 L-301 M-301 N-301 O-301 Q-301 R-301 T-301
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE / N-Acetylglucosamine

Details:

Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 13 / Source method: obtained synthetically / Formula: C₈H₁₅NO₆

Identifier:

Identifier	Type	Program
DGlcpNAcb	CONDENSED IUPAC CARBOHYDRATE SYMBOL	GMML 1.0
N-acetyl-b-D-glucopyranosamine	COMMON NAME	GMML 1.0
b-D-GlcpNAc	IUPAC CARBOHYDRATE SYMBOL	PDB-CARE 1.0
GlcNAc	SNFG CARBOHYDRATE SYMBOL	GMML 1.0

#3: Chemical

E-301 G-301 I-301 ChemComp-WCW / 4-azanyl-1-phenyl-piperidine-4-carboxylic acid

Details:

Mass: 220.268 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C₁₂H₁₆N₂O₂ / Feature type: SUBJECT OF INVESTIGATION

#4: Water

ChemComp-HOH / water / Water

Details:

Mass: 18.015 Da / Num. of mol.: 703 / Source method: isolated from a natural source / Formula: H₂O

• Has ligand of interest: Y

Experimental details

Experiment

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

Sample preparation

• Crystal: Density Matthews: 2.48 ų/Da / Density % sol: 50.36 %
• Crystal grow: Temperature: 293 K / Method: vapor diffusion, hanging drop; Details: PEG3350 3% Ammonium sulphate 1.8M HEPES buffer 0.1M, pH 7.75

Data collection

• Diffraction: Mean temperature: 100 K / Serial crystal experiment: N
• Diffraction source: Source: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.979 Å
• Detector: Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jul 22, 2020
• Radiation: Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
• Radiation wavelength: Wavelength: 0.979 Å / Relative weight: 1
• Reflection: Resolution: 2.1→49.37 Å / Num. obs: 259396 / % possible obs: 99.68 % / Redundancy: 6.9 % / CC_1/2: 0.999 / R_rim(I) all: 0.079871 / Net I/σ(I): 15.49
• Reflection shell: Resolution: 2.1→2.175 Å / Num. unique obs: 25710 / CC_1/2: 0.507 / R_rim(I) all: 1.578

Processing

Software

Name	Version	Classification
REFMAC	5.8.0238	refinement
PHASER		phasing
XDS		data scaling
XDS		data reduction

Refinement

Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.1→49.37 Å / Cor.coef. F_o:F_c: 0.954 / Cor.coef. F_o:F_c free: 0.94 / SU B: 8.238 / SU ML: 0.2 / Cross valid method: THROUGHOUT / ESU R: 0.262 / ESU R Free: 0.201 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	Rfactor	Num. reflection	% reflection	Selection details
Rfree	0.25479	12970	5 %	RANDOM
Rwork	0.2251	-	-	-
obs	0.22657	246406	99.7 %	-

• 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: 57.42 Ų

	Baniso -1	Baniso -2	Baniso -3
1-	-1.59 Å2	0 Å2	1.03 Å2
2-	-	-0.81 Å2	0 Å2
3-	-	-	1.32 Å2

Refinement step

Cycle: 1 / Resolution: 2.1→49.37 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	32303	0	230	703	33236

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.009	0.013	33503
X-RAY DIFFRACTION	r_bond_other_d	0.001	0.017	30103
X-RAY DIFFRACTION	r_angle_refined_deg	1.549	1.652	45770
X-RAY DIFFRACTION	r_angle_other_deg	1.238	1.582	69959
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	7.543	5	4045
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	26.781	21.894	1880
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	13.741	15	5515
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	20.832	15	276
X-RAY DIFFRACTION	r_chiral_restr	0.06	0.2	4568
X-RAY DIFFRACTION	r_gen_planes_refined	0.007	0.02	37271
X-RAY DIFFRACTION	r_gen_planes_other	0.001	0.02	7111
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	4.721	5.867	16207
X-RAY DIFFRACTION	r_mcbond_other	4.72	5.867	16206
X-RAY DIFFRACTION	r_mcangle_it	6.758	8.782	20210
X-RAY DIFFRACTION	r_mcangle_other	6.758	8.782	20211
X-RAY DIFFRACTION	r_scbond_it	5.457	6.501	17296
X-RAY DIFFRACTION	r_scbond_other	5.457	6.502	17297
X-RAY DIFFRACTION	r_scangle_it
X-RAY DIFFRACTION	r_scangle_other	8.051	9.513	25550
X-RAY DIFFRACTION	r_long_range_B_refined	10.835	66.262	34690
X-RAY DIFFRACTION	r_long_range_B_other	10.842	66.241	34603
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	6172	0.1
1	2	B	6172	0.1
2	1	A	6216	0.09
2	2	C	6216	0.09
3	1	A	6149	0.1
3	2	D	6149	0.1
4	1	A	6188	0.1
4	2	E	6188	0.1
5	1	A	6060	0.1
5	2	F	6060	0.1
6	1	A	6089	0.11
6	2	G	6089	0.11
7	1	A	6184	0.09
7	2	H	6184	0.09
8	1	A	6126	0.1
8	2	I	6126	0.1
9	1	A	5955	0.1
9	2	J	5955	0.1
10	1	A	6191	0.09
10	2	K	6191	0.09
11	1	A	6144	0.1
11	2	L	6144	0.1
12	1	A	6196	0.09
12	2	M	6196	0.09
13	1	A	6156	0.1
13	2	N	6156	0.1
14	1	A	6213	0.09
14	2	O	6213	0.09
15	1	A	6173	0.08
15	2	P	6173	0.08
16	1	A	6158	0.1
16	2	Q	6158	0.1
17	1	A	6218	0.09
17	2	R	6218	0.09
18	1	A	6085	0.1
18	2	S	6085	0.1
19	1	A	6141	0.09
19	2	T	6141	0.09
20	1	B	6179	0.09
20	2	C	6179	0.09
21	1	B	6141	0.1
21	2	D	6141	0.1
22	1	B	6135	0.1
22	2	E	6135	0.1
23	1	B	6080	0.1
23	2	F	6080	0.1
24	1	B	6141	0.09
24	2	G	6141	0.09
25	1	B	6156	0.09
25	2	H	6156	0.09
26	1	B	6141	0.1
26	2	I	6141	0.1
27	1	B	5970	0.09
27	2	J	5970	0.09
28	1	B	6116	0.1
28	2	K	6116	0.1
29	1	B	6188	0.09
29	2	L	6188	0.09
30	1	B	6142	0.09
30	2	M	6142	0.09
31	1	B	6122	0.1
31	2	N	6122	0.1
32	1	B	6131	0.09
32	2	O	6131	0.09
33	1	B	6099	0.1
33	2	P	6099	0.1
34	1	B	6174	0.09
34	2	Q	6174	0.09
35	1	B	6217	0.08
35	2	R	6217	0.08
36	1	B	6111	0.1
36	2	S	6111	0.1
37	1	B	6111	0.1
37	2	T	6111	0.1
38	1	C	6204	0.08
38	2	D	6204	0.08
39	1	C	6172	0.1
39	2	E	6172	0.1
40	1	C	6170	0.1
40	2	F	6170	0.1
41	1	C	6152	0.1
41	2	G	6152	0.1
42	1	C	6336	0.08
42	2	H	6336	0.08
43	1	C	6235	0.09
43	2	I	6235	0.09
44	1	C	6025	0.09
44	2	J	6025	0.09
45	1	C	6220	0.09
45	2	K	6220	0.09
46	1	C	6215	0.08
46	2	L	6215	0.08
47	1	C	6199	0.09
47	2	M	6199	0.09
48	1	C	6209	0.09
48	2	N	6209	0.09
49	1	C	6179	0.09
49	2	O	6179	0.09
50	1	C	6123	0.09
50	2	P	6123	0.09
51	1	C	6187	0.1
51	2	Q	6187	0.1
52	1	C	6277	0.08
52	2	R	6277	0.08
53	1	C	6249	0.09
53	2	S	6249	0.09
54	1	C	6179	0.09
54	2	T	6179	0.09
55	1	D	6160	0.09
55	2	E	6160	0.09
56	1	D	6038	0.1
56	2	F	6038	0.1
57	1	D	6082	0.1
57	2	G	6082	0.1
58	1	D	6162	0.09
58	2	H	6162	0.09
59	1	D	6213	0.08
59	2	I	6213	0.08
60	1	D	6008	0.1
60	2	J	6008	0.1
61	1	D	6087	0.09
61	2	K	6087	0.09
62	1	D	6182	0.09
62	2	L	6182	0.09
63	1	D	6133	0.09
63	2	M	6133	0.09
64	1	D	6148	0.08
64	2	N	6148	0.08
65	1	D	6149	0.08
65	2	O	6149	0.08
66	1	D	6054	0.1
66	2	P	6054	0.1
67	1	D	6197	0.08
67	2	Q	6197	0.08
68	1	D	6154	0.08
68	2	R	6154	0.08
69	1	D	6208	0.08
69	2	S	6208	0.08
70	1	D	6201	0.09
70	2	T	6201	0.09
71	1	E	6057	0.1
71	2	F	6057	0.1
72	1	E	6152	0.09
72	2	G	6152	0.09
73	1	E	6163	0.09
73	2	H	6163	0.09
74	1	E	6225	0.09
74	2	I	6225	0.09
75	1	E	6044	0.09
75	2	J	6044	0.09
76	1	E	6117	0.1
76	2	K	6117	0.1
77	1	E	6165	0.09
77	2	L	6165	0.09
78	1	E	6099	0.1
78	2	M	6099	0.1
79	1	E	6134	0.1
79	2	N	6134	0.1
80	1	E	6197	0.08
80	2	O	6197	0.08
81	1	E	6107	0.1
81	2	P	6107	0.1
82	1	E	6185	0.09
82	2	Q	6185	0.09
83	1	E	6198	0.09
83	2	R	6198	0.09
84	1	E	6163	0.1
84	2	S	6163	0.1
85	1	E	6248	0.08
85	2	T	6248	0.08
86	1	F	6069	0.11
86	2	G	6069	0.11
87	1	F	6124	0.1
87	2	H	6124	0.1
88	1	F	6110	0.1
88	2	I	6110	0.1
89	1	F	5927	0.11
89	2	J	5927	0.11
90	1	F	6060	0.1
90	2	K	6060	0.1
91	1	F	6034	0.11
91	2	L	6034	0.11
92	1	F	6105	0.1
92	2	M	6105	0.1
93	1	F	6054	0.1
93	2	N	6054	0.1
94	1	F	6000	0.1
94	2	O	6000	0.1
95	1	F	5992	0.1
95	2	P	5992	0.1
96	1	F	6073	0.11
96	2	Q	6073	0.11
97	1	F	6084	0.1
97	2	R	6084	0.1
98	1	F	6073	0.11
98	2	S	6073	0.11
99	1	F	6055	0.1
99	2	T	6055	0.1
100	1	G	6170	0.1
100	2	H	6170	0.1
101	1	G	6304	0.08
101	2	I	6304	0.08
102	1	G	6129	0.09
102	2	J	6129	0.09
103	1	G	6122	0.1
103	2	K	6122	0.1
104	1	G	6137	0.09
104	2	L	6137	0.09
105	1	G	6106	0.09
105	2	M	6106	0.09
106	1	G	6128	0.1
106	2	N	6128	0.1
107	1	G	6128	0.09
107	2	O	6128	0.09
108	1	G	6100	0.1
108	2	P	6100	0.1
109	1	G	6183	0.1
109	2	Q	6183	0.1
110	1	G	6194	0.09
110	2	R	6194	0.09
111	1	G	6243	0.09
111	2	S	6243	0.09
112	1	G	6164	0.09
112	2	T	6164	0.09
113	1	H	6265	0.08
113	2	I	6265	0.08
114	1	H	6040	0.09
114	2	J	6040	0.09
115	1	H	6221	0.09
115	2	K	6221	0.09
116	1	H	6214	0.09
116	2	L	6214	0.09
117	1	H	6146	0.09
117	2	M	6146	0.09
118	1	H	6198	0.09
118	2	N	6198	0.09
119	1	H	6183	0.08
119	2	O	6183	0.08
120	1	H	6134	0.09
120	2	P	6134	0.09
121	1	H	6155	0.1
121	2	Q	6155	0.1
122	1	H	6224	0.08
122	2	R	6224	0.08
123	1	H	6235	0.09
123	2	S	6235	0.09
124	1	H	6207	0.08
124	2	T	6207	0.08
125	1	I	6252	0.09
125	2	J	6252	0.09
126	1	I	6229	0.09
126	2	K	6229	0.09
127	1	I	6263	0.09
127	2	L	6263	0.09
128	1	I	6202	0.09
128	2	M	6202	0.09
129	1	I	6300	0.08
129	2	N	6300	0.08
130	1	I	6255	0.08
130	2	O	6255	0.08
131	1	I	6164	0.1
131	2	P	6164	0.1
132	1	I	6300	0.09
132	2	Q	6300	0.09
133	1	I	6305	0.07
133	2	R	6305	0.07
134	1	I	6452	0.07
134	2	S	6452	0.07
135	1	I	6324	0.08
135	2	T	6324	0.08
136	1	J	6029	0.1
136	2	K	6029	0.1
137	1	J	6051	0.09
137	2	L	6051	0.09
138	1	J	5995	0.1
138	2	M	5995	0.1
139	1	J	6022	0.1
139	2	N	6022	0.1
140	1	J	6056	0.08
140	2	O	6056	0.08
141	1	J	5971	0.09
141	2	P	5971	0.09
142	1	J	6091	0.11
142	2	Q	6091	0.11
143	1	J	6073	0.09
143	2	R	6073	0.09
144	1	J	6227	0.09
144	2	S	6227	0.09
145	1	J	6144	0.09
145	2	T	6144	0.09
146	1	K	6188	0.1
146	2	L	6188	0.1
147	1	K	6199	0.09
147	2	M	6199	0.09
148	1	K	6213	0.1
148	2	N	6213	0.1
149	1	K	6206	0.09
149	2	O	6206	0.09
150	1	K	6187	0.09
150	2	P	6187	0.09
151	1	K	6177	0.1
151	2	Q	6177	0.1
152	1	K	6223	0.1
152	2	R	6223	0.1
153	1	K	6183	0.1
153	2	S	6183	0.1
154	1	K	6159	0.09
154	2	T	6159	0.09
155	1	L	6126	0.1
155	2	M	6126	0.1
156	1	L	6143	0.09
156	2	N	6143	0.09
157	1	L	6163	0.09
157	2	O	6163	0.09
158	1	L	6096	0.1
158	2	P	6096	0.1
159	1	L	6173	0.08
159	2	Q	6173	0.08
160	1	L	6178	0.09
160	2	R	6178	0.09
161	1	L	6165	0.09
161	2	S	6165	0.09
162	1	L	6198	0.09
162	2	T	6198	0.09
163	1	M	6167	0.09
163	2	N	6167	0.09
164	1	M	6150	0.09
164	2	O	6150	0.09
165	1	M	6129	0.1
165	2	P	6129	0.1
166	1	M	6193	0.09
166	2	Q	6193	0.09
167	1	M	6209	0.09
167	2	R	6209	0.09
168	1	M	6121	0.1
168	2	S	6121	0.1
169	1	M	6085	0.09
169	2	T	6085	0.09
170	1	N	6234	0.08
170	2	O	6234	0.08
171	1	N	6172	0.1
171	2	P	6172	0.1
172	1	N	6212	0.09
172	2	Q	6212	0.09
173	1	N	6220	0.09
173	2	R	6220	0.09
174	1	N	6221	0.09
174	2	S	6221	0.09
175	1	N	6190	0.08
175	2	T	6190	0.08
176	1	O	6163	0.08
176	2	P	6163	0.08
177	1	O	6190	0.09
177	2	Q	6190	0.09
178	1	O	6219	0.09
178	2	R	6219	0.09
179	1	O	6198	0.08
179	2	S	6198	0.08
180	1	O	6192	0.08
180	2	T	6192	0.08
181	1	P	6073	0.11
181	2	Q	6073	0.11
182	1	P	6174	0.09
182	2	R	6174	0.09
183	1	P	6088	0.11
183	2	S	6088	0.11
184	1	P	6114	0.09
184	2	T	6114	0.09
185	1	Q	6203	0.1
185	2	R	6203	0.1
186	1	Q	6196	0.1
186	2	S	6196	0.1
187	1	Q	6151	0.1
187	2	T	6151	0.1
188	1	R	6216	0.09
188	2	S	6216	0.09
189	1	R	6176	0.09
189	2	T	6176	0.09
190	1	S	6239	0.1
190	2	T	6239	0.1

LS refinement shell

Resolution: 2.1→2.154 Å / Total num. of bins used: 20

	Rfactor	Num. reflection	% reflection
Rfree	0.365	950	-
Rwork	0.354	18044	-
obs	-	-	99.28 %