PDB-6fiz: Crystal Structure of CNG mimicking NaK-EAPP mutant (T67A) cocryst...

Basic information

• Entry: Database: PDB / ID: 6fiz
• Title: Crystal Structure of CNG mimicking NaK-EAPP mutant (T67A) cocrystallized with K+
• Components: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein
• Keywords: TRANSPORT PROTEIN / CNG mimick / ion channel / transport channel

Function / homology

Function:

response to stimulus / VxPx cargo-targeting to cilium / intracellularly cGMP-activated cation channel activity / Golgi-associated vesicle membrane / intracellularly cAMP-activated cation channel activity / ciliary membrane / potassium channel activity / cGMP binding / cAMP binding / sensory perception of smell / membrane => GO:0016020 / calmodulin binding / Golgi membrane / identical protein binding / membrane / metal ion binding

Domain/homology:

Cyclic nucleotide-gated channel, C-terminal leucine zipper domain / C-terminal leucine zipper domain of cyclic nucleotide-gated channels / Two pore domain potassium channel / Cyclic nucleotide-binding domain signature 2. / Helix Hairpins - #70 / Cyclic nucleotide-binding domain signature 1. / Cyclic nucleotide-binding, conserved site / Potassium channel domain / Ion channel / Cyclic nucleotide-monophosphate binding domain / Cyclic nucleotide-binding domain / cAMP/cGMP binding motif profile. / Cyclic nucleotide-binding domain / Cyclic nucleotide-binding domain superfamily / RmlC-like jelly roll fold / Ion transport domain / Ion transport protein / Helix Hairpins / Orthogonal Bundle / Mainly Alpha

Component:

GLYCINE / : / Cyclic nucleotide-gated olfactory channel / Potassium channel protein

• Biological species: Bacillus cereus (bacteria); Homo sapiens (human)
• Method: X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.63 Å
• Authors: Napolitano, L.M.R. / De March, M. / Steiner, R.A. / Onesti, S.
• Citation: Journal: To Be Published; Title: Crystal Structure of CNG mimicking NaK-EAPP mutant (T67A) cocrystallized with K+; Authors: Napolitano, L.M.R. / De March, M. / Onesti, S. / Steiner, R.A.

History

Deposition	Jan 19, 2018	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Mar 6, 2019	Provider: repository / Type: Initial release
Revision 1.1	Apr 3, 2019	Group: Data collection / Category: diffrn_source Item: _diffrn_source.pdbx_synchrotron_beamline / _diffrn_source.type
Revision 1.2	Jun 26, 2019	Group: Data collection / Database references / Source and taxonomy / Structure summary Category: audit_author / citation_author / entity / entity_name_com / entity_src_gen / struct_ref / struct_ref_seq / struct_ref_seq_dif Item: _audit_author.name / _citation_author.name / _entity.pdbx_description
Revision 1.3	Jan 17, 2024	Group: Data collection / Database references / Derived calculations / Refinement description Category: chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_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

Assembly

Deposited unit

A: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

B: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

C: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

D: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

E: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

F: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

G: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

H: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

I: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

J: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

K: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

L: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

M: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

N: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

O: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

P: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

hetero molecules

Summary:

• 171 kDa, 16 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	170,506	95
Polymers	164,706	16
Non-polymers	5,800	79
Water	1,711	95

1

A: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

B: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

C: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

D: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

hetero molecules

Summary:

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

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	42,163	18
Polymers	41,176	4
Non-polymers	986	14
Water	72	4

Symmetry operations:

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

Calculated values:

Buried area	6980 Å2
ΔGint	-71 kcal/mol
Surface area	17600 Å2
Method	PISA

2

E: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

F: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

G: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

H: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

hetero molecules

Summary:

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

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	42,431	21
Polymers	41,176	4
Non-polymers	1,254	17
Water	72	4

Symmetry operations:

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

Calculated values:

Buried area	7480 Å2
ΔGint	-85 kcal/mol
Surface area	17300 Å2
Method	PISA

3

I: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

J: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

K: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

L: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

hetero molecules

Summary:

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

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	42,806	26
Polymers	41,176	4
Non-polymers	1,630	22
Water	72	4

Symmetry operations:

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

Calculated values:

Buried area	8390 Å2
ΔGint	-90 kcal/mol
Surface area	17430 Å2
Method	PISA

4

M: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

N: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

O: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

P: Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein

hetero molecules

Summary:

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

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	43,107	30
Polymers	41,176	4
Non-polymers	1,930	26
Water	72	4

Symmetry operations:

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

Calculated values:

Buried area	7940 Å2
ΔGint	-89 kcal/mol
Surface area	17590 Å2
Method	PISA

Unit cell

Length a, b, c (Å)	181.220, 135.250, 67.430
Angle α, β, γ (deg.)	90.00, 91.95, 90.00
Int Tables number	5
Space group name H-M	C121

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	B
2	16	C
1	17	B
2	17	D
1	18	B
2	18	E
1	19	B
2	19	F
1	20	B
2	20	G
1	21	B
2	21	H
1	22	B
2	22	I
1	23	B
2	23	J
1	24	B
2	24	K
1	25	B
2	25	L
1	26	B
2	26	M
1	27	B
2	27	N
1	28	B
2	28	O
1	29	B
2	29	P
1	30	C
2	30	D
1	31	C
2	31	E
1	32	C
2	32	F
1	33	C
2	33	G
1	34	C
2	34	H
1	35	C
2	35	I
1	36	C
2	36	J
1	37	C
2	37	K
1	38	C
2	38	L
1	39	C
2	39	M
1	40	C
2	40	N
1	41	C
2	41	O
1	42	C
2	42	P
1	43	D
2	43	E
1	44	D
2	44	F
1	45	D
2	45	G
1	46	D
2	46	H
1	47	D
2	47	I
1	48	D
2	48	J
1	49	D
2	49	K
1	50	D
2	50	L
1	51	D
2	51	M
1	52	D
2	52	N
1	53	D
2	53	O
1	54	D
2	54	P
1	55	E
2	55	F
1	56	E
2	56	G
1	57	E
2	57	H
1	58	E
2	58	I
1	59	E
2	59	J
1	60	E
2	60	K
1	61	E
2	61	L
1	62	E
2	62	M
1	63	E
2	63	N
1	64	E
2	64	O
1	65	E
2	65	P
1	66	F
2	66	G
1	67	F
2	67	H
1	68	F
2	68	I
1	69	F
2	69	J
1	70	F
2	70	K
1	71	F
2	71	L
1	72	F
2	72	M
1	73	F
2	73	N
1	74	F
2	74	O
1	75	F
2	75	P
1	76	G
2	76	H
1	77	G
2	77	I
1	78	G
2	78	J
1	79	G
2	79	K
1	80	G
2	80	L
1	81	G
2	81	M
1	82	G
2	82	N
1	83	G
2	83	O
1	84	G
2	84	P
1	85	H
2	85	I
1	86	H
2	86	J
1	87	H
2	87	K
1	88	H
2	88	L
1	89	H
2	89	M
1	90	H
2	90	N
1	91	H
2	91	O
1	92	H
2	92	P
1	93	I
2	93	J
1	94	I
2	94	K
1	95	I
2	95	L
1	96	I
2	96	M
1	97	I
2	97	N
1	98	I
2	98	O
1	99	I
2	99	P
1	100	J
2	100	K
1	101	J
2	101	L
1	102	J
2	102	M
1	103	J
2	103	N
1	104	J
2	104	O
1	105	J
2	105	P
1	106	K
2	106	L
1	107	K
2	107	M
1	108	K
2	108	N
1	109	K
2	109	O
1	110	K
2	110	P
1	111	L
2	111	M
1	112	L
2	112	N
1	113	L
2	113	O
1	114	L
2	114	P
1	115	M
2	115	N
1	116	M
2	116	O
1	117	M
2	117	P
1	118	N
2	118	O
1	119	N
2	119	P
1	120	O
2	120	P

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

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

Components

#1: Protein

A B C D E F G H I J K L M N O P
Potassium channel protein,Cyclic nucleotide-gated olfactory channel,Potassium channel protein / Cyclic nucleotide-gated cation channel 2 / Cyclic nucleotide-gated channel alpha-2 / CNG2

Details:

Mass: 10294.113 Da / Num. of mol.: 16
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711) (bacteria), (gene. exp.) Homo sapiens (human)
Strain: ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711
Gene: BC_0669, CNGA2, CNCA, CNCA1, CNCG2 / Production host: Escherichia coli (E. coli) / References: UniProt: Q81HW2, UniProt: Q16280

#2: Chemical

A-201 A-202 B-201 B-202 B-203 C-201 D-201 D-202 D-203 D-204 E-201 E-202 E-203 E-204 F-201 F-202 G-201 G-202 H-201 H-202 ...
ChemComp-GLY / GLYCINE

Details:

Type: peptide linking / Mass: 75.067 Da / Num. of mol.: 60 / Source method: obtained synthetically / Formula: C₂H₅NO₂

#3: Chemical

A-203 A-204 A-205 E-205 E-206 E-207 I-204 I-205 I-206 M-207 M-208 M-209
ChemComp-K / POTASSIUM ION

Details:

Mass: 39.098 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: K

#4: Chemical

D-205 F-203 G-203 J-210 J-211 M-210 N-209
ChemComp-MPD / (4S)-2-METHYL-2,4-PENTANEDIOL

Details:

Mass: 118.174 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C₆H₁₄O₂ / Comment: precipitant*YM

#5: Water

ChemComp-HOH / water

Details:

Mass: 18.015 Da / Num. of mol.: 95 / 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: 2.46 ų/Da / Density % sol: 49.91 %
• Crystal grow: Temperature: 277 K / Method: vapor diffusion, hanging drop / Details: 40-44% MPD 100 mM MES pH 6.5 25mM Glycine

Data collection

• Diffraction: Mean temperature: 100 K / Serial crystal experiment: N
• Diffraction source: Source: SYNCHROTRON / Site: ELETTRA / Beamline: 11.2C / Wavelength: 0.95389 Å
• Detector: Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Jan 23, 2017
• Radiation: Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
• Radiation wavelength: Wavelength: 0.95389 Å / Relative weight: 1

Reflection twin

Crystal-ID	ID	Operator	Domain-ID	Fraction
1	1	H, K, L	1	0.914
1	1	h,-k,-l	2	0.086

• Reflection: Resolution: 2.63→67.62 Å / Num. obs: 44752 / % possible obs: 92.8 % / Redundancy: 3.6 % / CC_1/2: 0.987 / R_merge(I) obs: 0.19 / Net I/σ(I): 4.3
• Reflection shell: Resolution: 2.63→2.68 Å / Redundancy: 2.6 % / R_merge(I) obs: 0.97 / Num. unique obs: 2175 / CC_1/2: 0.54 / % possible all: 91

Processing

Software

Name	Version	Classification
REFMAC	5.8.0238	refinement
XDS		data reduction
SCALA		data scaling
MOLREP		phasing

Refinement

Method to determine structure: MOLECULAR REPLACEMENT
Starting model: 3K0D

3k0d

Resolution: 2.63→67.62 Å / Cor.coef. F_o:F_c: 0.932 / Cor.coef. F_o:F_c free: 0.91 / SU B: 8.502 / SU ML: 0.192 / Cross valid method: THROUGHOUT / ESU R Free: 0.083 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	Rfactor	Num. reflection	% reflection	Selection details
Rfree	0.26934	2291	5.1 %	RANDOM
Rwork	0.23534	-	-	-
obs	0.23708	42458	84.5 %	-

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

Displacement parameters

B_iso mean: 45.784 Ų

	Baniso -1	Baniso -2	Baniso -3
1-	20.56 Å2	0 Å2	6 Å2
2-	-	-18.53 Å2	0 Å2
3-	-	-	-2.02 Å2

Refinement step

Cycle: 1 / Resolution: 2.63→67.62 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	11672	0	68	95	11835

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.007	0.013	11959
X-RAY DIFFRACTION	r_bond_other_d	0.001	0.017	11984
X-RAY DIFFRACTION	r_angle_refined_deg	1.319	1.649	16286
X-RAY DIFFRACTION	r_angle_other_deg	1.271	1.573	27609
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	4.963	5	1448
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	25.679	23.234	402
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	14.617	15	1854
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	35.478	15	16
X-RAY DIFFRACTION	r_chiral_restr	0.061	0.2	1678
X-RAY DIFFRACTION	r_gen_planes_refined	0.006	0.02	12944
X-RAY DIFFRACTION	r_gen_planes_other	0.001	0.02	2376
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	4.529	4.722	6017
X-RAY DIFFRACTION	r_mcbond_other	4.528	4.721	6015
X-RAY DIFFRACTION	r_mcangle_it	6.699	7.047	7390
X-RAY DIFFRACTION	r_mcangle_other	6.698	7.047	7390
X-RAY DIFFRACTION	r_scbond_it	4.316	5.011	5942
X-RAY DIFFRACTION	r_scbond_other	4.315	5.011	5943
X-RAY DIFFRACTION	r_scangle_it
X-RAY DIFFRACTION	r_scangle_other	6.471	7.396	8897
X-RAY DIFFRACTION	r_long_range_B_refined	10.994	88.541	48867
X-RAY DIFFRACTION	r_long_range_B_other	10.99	88.544	48854
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	2995	0.04
1	2	B	2995	0.04
2	1	A	2994	0.04
2	2	C	2994	0.04
3	1	A	3008	0.03
3	2	D	3008	0.03
4	1	A	3005	0.04
4	2	E	3005	0.04
5	1	A	2995	0.03
5	2	F	2995	0.03
6	1	A	3006	0.02
6	2	G	3006	0.02
7	1	A	3008	0.02
7	2	H	3008	0.02
8	1	A	2965	0.04
8	2	I	2965	0.04
9	1	A	2987	0.04
9	2	J	2987	0.04
10	1	A	2997	0.03
10	2	K	2997	0.03
11	1	A	2991	0.04
11	2	L	2991	0.04
12	1	A	2959	0.04
12	2	M	2959	0.04
13	1	A	2988	0.04
13	2	N	2988	0.04
14	1	A	2996	0.04
14	2	O	2996	0.04
15	1	A	2992	0.04
15	2	P	2992	0.04
16	1	B	2983	0.05
16	2	C	2983	0.05
17	1	B	2994	0.04
17	2	D	2994	0.04
18	1	B	2992	0.05
18	2	E	2992	0.05
19	1	B	2991	0.04
19	2	F	2991	0.04
20	1	B	2990	0.03
20	2	G	2990	0.03
21	1	B	3019	0.03
21	2	H	3019	0.03
22	1	B	2949	0.06
22	2	I	2949	0.06
23	1	B	2972	0.05
23	2	J	2972	0.05
24	1	B	2981	0.05
24	2	K	2981	0.05
25	1	B	2975	0.05
25	2	L	2975	0.05
26	1	B	2942	0.05
26	2	M	2942	0.05
27	1	B	2973	0.05
27	2	N	2973	0.05
28	1	B	2982	0.04
28	2	O	2982	0.04
29	1	B	2976	0.05
29	2	P	2976	0.05
30	1	C	3008	0.03
30	2	D	3008	0.03
31	1	C	2995	0.05
31	2	E	2995	0.05
32	1	C	2982	0.04
32	2	F	2982	0.04
33	1	C	3003	0.04
33	2	G	3003	0.04
34	1	C	2991	0.05
34	2	H	2991	0.05
35	1	C	2977	0.03
35	2	I	2977	0.03
36	1	C	3002	0.03
36	2	J	3002	0.03
37	1	C	3009	0.03
37	2	K	3009	0.03
38	1	C	3006	0.03
38	2	L	3006	0.03
39	1	C	2971	0.03
39	2	M	2971	0.03
40	1	C	3003	0.03
40	2	N	3003	0.03
41	1	C	2998	0.03
41	2	O	2998	0.03
42	1	C	3004	0.03
42	2	P	3004	0.03
43	1	D	3003	0.05
43	2	E	3003	0.05
44	1	D	2992	0.04
44	2	F	2992	0.04
45	1	D	3004	0.03
45	2	G	3004	0.03
46	1	D	3005	0.04
46	2	H	3005	0.04
47	1	D	2973	0.04
47	2	I	2973	0.04
48	1	D	2997	0.04
48	2	J	2997	0.04
49	1	D	3007	0.02
49	2	K	3007	0.02
50	1	D	3000	0.03
50	2	L	3000	0.03
51	1	D	2966	0.03
51	2	M	2966	0.03
52	1	D	2998	0.04
52	2	N	2998	0.04
53	1	D	3007	0.02
53	2	O	3007	0.02
54	1	D	3000	0.03
54	2	P	3000	0.03
55	1	E	2989	0.04
55	2	F	2989	0.04
56	1	E	2999	0.04
56	2	G	2999	0.04
57	1	E	3002	0.04
57	2	H	3002	0.04
58	1	E	2957	0.06
58	2	I	2957	0.06
59	1	E	2984	0.05
59	2	J	2984	0.05
60	1	E	2991	0.05
60	2	K	2991	0.05
61	1	E	2987	0.05
61	2	L	2987	0.05
62	1	E	2949	0.05
62	2	M	2949	0.05
63	1	E	2984	0.05
63	2	N	2984	0.05
64	1	E	2990	0.05
64	2	O	2990	0.05
65	1	E	2985	0.05
65	2	P	2985	0.05
66	1	F	2989	0.03
66	2	G	2989	0.03
67	1	F	2991	0.03
67	2	H	2991	0.03
68	1	F	2954	0.04
68	2	I	2954	0.04
69	1	F	2981	0.03
69	2	J	2981	0.03
70	1	F	2982	0.04
70	2	K	2982	0.04
71	1	F	2984	0.03
71	2	L	2984	0.03
72	1	F	2949	0.05
72	2	M	2949	0.05
73	1	F	2982	0.03
73	2	N	2982	0.03
74	1	F	2980	0.04
74	2	O	2980	0.04
75	1	F	2986	0.03
75	2	P	2986	0.03
76	1	G	3003	0.03
76	2	H	3003	0.03
77	1	G	2970	0.05
77	2	I	2970	0.05
78	1	G	2992	0.04
78	2	J	2992	0.04
79	1	G	3003	0.03
79	2	K	3003	0.03
80	1	G	2995	0.04
80	2	L	2995	0.04
81	1	G	2963	0.04
81	2	M	2963	0.04
82	1	G	2993	0.04
82	2	N	2993	0.04
83	1	G	2992	0.03
83	2	O	2992	0.03
84	1	G	2996	0.04
84	2	P	2996	0.04
85	1	H	2961	0.05
85	2	I	2961	0.05
86	1	H	2981	0.04
86	2	J	2981	0.04
87	1	H	2992	0.03
87	2	K	2992	0.03
88	1	H	2987	0.04
88	2	L	2987	0.04
89	1	H	2955	0.05
89	2	M	2955	0.05
90	1	H	2984	0.04
90	2	N	2984	0.04
91	1	H	2993	0.04
91	2	O	2993	0.04
92	1	H	2989	0.04
92	2	P	2989	0.04
93	1	I	2974	0.03
93	2	J	2974	0.03
94	1	I	2978	0.03
94	2	K	2978	0.03
95	1	I	2979	0.03
95	2	L	2979	0.03
96	1	I	3095	0.03
96	2	M	3095	0.03
97	1	I	2975	0.03
97	2	N	2975	0.03
98	1	I	2966	0.04
98	2	O	2966	0.04
99	1	I	2979	0.03
99	2	P	2979	0.03
100	1	J	3050	0.04
100	2	K	3050	0.04
101	1	J	3053	0.03
101	2	L	3053	0.03
102	1	J	3016	0.04
102	2	M	3016	0.04
103	1	J	3064	0.02
103	2	N	3064	0.02
104	1	J	3047	0.04
104	2	O	3047	0.04
105	1	J	3050	0.03
105	2	P	3050	0.03
106	1	K	3006	0.02
106	2	L	3006	0.02
107	1	K	2972	0.03
107	2	M	2972	0.03
108	1	K	3001	0.03
108	2	N	3001	0.03
109	1	K	3005	0.03
109	2	O	3005	0.03
110	1	K	3006	0.02
110	2	P	3006	0.02
111	1	L	2973	0.03
111	2	M	2973	0.03
112	1	L	3009	0.02
112	2	N	3009	0.02
113	1	L	2996	0.04
113	2	O	2996	0.04
114	1	L	3007	0.01
114	2	P	3007	0.01
115	1	M	2969	0.04
115	2	N	2969	0.04
116	1	M	2963	0.03
116	2	O	2963	0.03
117	1	M	2972	0.03
117	2	P	2972	0.03
118	1	N	3003	0.03
118	2	O	3003	0.03
119	1	N	3005	0.02
119	2	P	3005	0.02
120	1	O	2993	0.04
120	2	P	2993	0.04

LS refinement shell

Resolution: 2.549→2.615 Å / Total num. of bins used: 20

	Rfactor	Num. reflection	% reflection
Rfree	0	0	-
Rwork	0	0	-
obs	-	-	0 %