PDB-6qx2: 3.4A structure of benzoisoxazole 3 with S.aureus DNA gyrase and DNA

Basic information

• Entry: Database: PDB / ID: 6qx2
• Title: 3.4A structure of benzoisoxazole 3 with S.aureus DNA gyrase and DNA

Components

• (DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)- ...) x 3
• (DNA gyrase subunit ...) x 9

• Keywords: ISOMERASE / Inhibitor / DNA complex

Function / homology

Function:

DNA negative supercoiling activity / DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity / DNA topoisomerase (ATP-hydrolysing) / DNA topological change / DNA-templated DNA replication / chromosome / response to antibiotic / DNA binding / ATP binding / metal ion binding / cytoplasm

Domain/homology:

DNA gyrase, subunit A / DNA gyrase/topoisomerase IV, subunit A, C-terminal repeat / DNA gyrase/topoisomerase IV, subunit A, C-terminal / DNA gyrase C-terminal domain, beta-propeller / Topoisomerase (Topo) IIA-type catalytic domain profile. / DNA gyrase subunit B, TOPRIM domain / DNA gyrase, subunit B / DNA topoisomerase, type IIA, subunit B / DNA topoisomerase, type IIA, alpha-helical domain superfamily / DNA topoisomerase, type IIA, domain A / DNA topoisomerase, type IIA, domain A, alpha-beta / DNA gyrase/topoisomerase IV, subunit A / DNA Topoisomerase IV / DNA gyrase B subunit, C-terminal / DNA gyrase B subunit, carboxyl terminus / DNA topoisomerase, type IIA, subunit B, domain 2 / DNA gyrase B / DNA topoisomerase, type IIA / DNA topoisomerase, type IIA, conserved site / DNA topoisomerase II signature. / TopoisomeraseII / DNA topoisomerase, type IIA, subunit B, C-terminal / Toprim domain / DNA topoisomerase, type IIA-like domain superfamily / Toprim domain profile. / TOPRIM domain / Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase / Histidine kinase-like ATPases / Histidine kinase/HSP90-like ATPase / Histidine kinase/HSP90-like ATPase superfamily / Ribosomal protein S5 domain 2-type fold, subgroup / Ribosomal protein S5 domain 2-type fold

Component:

Chem-JK8 / DNA / DNA (> 10) / DNA gyrase subunit B / DNA gyrase subunit B / DNA gyrase subunit B / DNA gyrase subunit B / DNA gyrase subunit B / DNA gyrase subunit A

• Biological species: Staphylococcus aureus (bacteria); synthetic construct (others)
• Method: X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.4 Å
• Authors: Bax, B.D.

Funding support

1items

Organization	Grant number	Country
European Union	115583

• Citation: Journal: Bioorg.Med.Chem.Lett. / Year: 2019; Title: Structure-guided design of antibacterials that allosterically inhibit DNA gyrase.; Authors: Thalji, R.K. / Raha, K. / Andreotti, D. / Checchia, A. / Cui, H. / Meneghelli, G. / Profeta, R. / Tonelli, F. / Tommasi, S. / Bakshi, T. / Donovan, B.T. / Howells, A. / Jain, S. / Nixon, C. / Quinque, G. / McCloskey, L. / Bax, B.D. / Neu, M. / Chan, P.F. / Stavenger, R.A.

History

Deposition	Mar 6, 2019	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Apr 17, 2019	Provider: repository / Type: Initial release
Revision 1.1	May 8, 2019	Group: Data collection / Database references Category: citation / pdbx_database_proc / pdbx_seq_map_depositor_info Item: _citation.journal_volume / _citation.page_first / _citation.page_last / _pdbx_seq_map_depositor_info.one_letter_code / _pdbx_seq_map_depositor_info.one_letter_code_mod
Revision 1.2	Jul 10, 2019	Group: Data collection / Category: diffrn_source / pdbx_seq_map_depositor_info Item: _diffrn_source.pdbx_synchrotron_site / _pdbx_seq_map_depositor_info.one_letter_code / _pdbx_seq_map_depositor_info.one_letter_code_mod
Revision 1.3	Jan 24, 2024	Group: Data collection / Database references / Refinement description Category: chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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

B: DNA gyrase subunit B,DNA gyrase subunit B

A: DNA gyrase subunit A

D: DNA gyrase subunit B,DNA gyrase subunit B

C: DNA gyrase subunit A

E: DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)-3')

F: DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)-3')

K: DNA gyrase subunit B,DNA gyrase subunit B

J: DNA gyrase subunit A

M: DNA gyrase subunit B,DNA gyrase subunit B

L: DNA gyrase subunit A

N: DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)-3')

O: DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)-3')

S: DNA gyrase subunit B,DNA gyrase subunit B

R: DNA gyrase subunit A

U: DNA gyrase subunit B,DNA gyrase subunit B

T: DNA gyrase subunit A

V: DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)-3')

W: DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)-3')

b: DNA gyrase subunit B,DNA gyrase subunit B

a: DNA gyrase subunit A

d: DNA gyrase subunit B,DNA gyrase subunit B

c: DNA gyrase subunit A

e: DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)-3')

f: DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)-3')

k: DNA gyrase subunit B,DNA gyrase subunit B

j: DNA gyrase subunit A

m: DNA gyrase subunit B,DNA gyrase subunit B

l: DNA gyrase subunit A

n: DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)-3')

o: DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)-3')

s: DNA gyrase subunit B,DNA gyrase subunit B

r: DNA gyrase subunit A

u: DNA gyrase subunit B,DNA gyrase subunit B

t: DNA gyrase subunit A

v: DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)-3')

w: DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)-3')

hetero molecules

Summary:

• 993 kDa, 36 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	993,375	48
Polymers	988,997	36
Non-polymers	4,378	12
Water	0

1

B: DNA gyrase subunit B,DNA gyrase subunit B

A: DNA gyrase subunit A

D: DNA gyrase subunit B,DNA gyrase subunit B

C: DNA gyrase subunit A

E: DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)-3')

F: DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)-3')

hetero molecules

Summary:

• defined by author&software
• Evidence: gel filtration
• 166 kDa, 6 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	166,064	8
Polymers	165,334	6
Non-polymers	730	2
Water	0

Symmetry operations:

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

Calculated values:

Buried area	19190 Å2
ΔGint	-104 kcal/mol
Surface area	55710 Å2
Method	PISA

2

K: DNA gyrase subunit B,DNA gyrase subunit B

J: DNA gyrase subunit A

M: DNA gyrase subunit B,DNA gyrase subunit B

L: DNA gyrase subunit A

N: DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)-3')

O: DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)-3')

hetero molecules

Summary:

• defined by author&software
• Evidence: gel filtration
• 165 kDa, 6 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	165,223	8
Polymers	164,493	6
Non-polymers	730	2
Water	0

Symmetry operations:

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

Calculated values:

Buried area	19370 Å2
ΔGint	-102 kcal/mol
Surface area	55710 Å2
Method	PISA

3

S: DNA gyrase subunit B,DNA gyrase subunit B

R: DNA gyrase subunit A

U: DNA gyrase subunit B,DNA gyrase subunit B

T: DNA gyrase subunit A

V: DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)-3')

W: DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)-3')

hetero molecules

Summary:

• defined by author&software
• 166 kDa, 6 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	165,760	8
Polymers	165,030	6
Non-polymers	730	2
Water	0

Symmetry operations:

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

Calculated values:

Buried area	19890 Å2
ΔGint	-104 kcal/mol
Surface area	55580 Å2
Method	PISA

4

b: DNA gyrase subunit B,DNA gyrase subunit B

a: DNA gyrase subunit A

d: DNA gyrase subunit B,DNA gyrase subunit B

c: DNA gyrase subunit A

e: DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)-3')

f: DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)-3')

hetero molecules

Summary:

• defined by author&software
• 164 kDa, 6 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	164,369	8
Polymers	163,640	6
Non-polymers	730	2
Water	0

Symmetry operations:

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

Calculated values:

Buried area	19000 Å2
ΔGint	-105 kcal/mol
Surface area	55570 Å2
Method	PISA

5

k: DNA gyrase subunit B,DNA gyrase subunit B

j: DNA gyrase subunit A

m: DNA gyrase subunit B,DNA gyrase subunit B

l: DNA gyrase subunit A

n: DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)-3')

o: DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)-3')

hetero molecules

Summary:

• defined by author&software
• 166 kDa, 6 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	165,994	8
Polymers	165,264	6
Non-polymers	730	2
Water	0

Symmetry operations:

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

Calculated values:

Buried area	19570 Å2
ΔGint	-103 kcal/mol
Surface area	55850 Å2
Method	PISA

6

s: DNA gyrase subunit B,DNA gyrase subunit B

r: DNA gyrase subunit A

u: DNA gyrase subunit B,DNA gyrase subunit B

t: DNA gyrase subunit A

v: DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)-3')

w: DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)-3')

hetero molecules

Summary:

• defined by author&software
• 166 kDa, 6 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	165,965	8
Polymers	165,235	6
Non-polymers	730	2
Water	0

Symmetry operations:

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

Calculated values:

Buried area	20100 Å2
ΔGint	-100 kcal/mol
Surface area	55160 Å2
Method	PISA

Unit cell

Length a, b, c (Å)	187.640, 410.120, 93.940
Angle α, β, γ (deg.)	90.00, 120.22, 90.00
Int Tables number	4
Space group name H-M	P1211

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	B
2	1	D
1	2	B
2	2	K
1	3	B
2	3	M
1	4	B
2	4	S
1	5	B
2	5	U
1	6	B
2	6	b
1	7	B
2	7	d
1	8	B
2	8	k
1	9	B
2	9	m
1	10	B
2	10	s
1	11	B
2	11	u
1	12	A
2	12	C
1	13	A
2	13	J
1	14	A
2	14	L
1	15	A
2	15	R
1	16	A
2	16	T
1	17	A
2	17	a
1	18	A
2	18	c
1	19	A
2	19	j
1	20	A
2	20	l
1	21	A
2	21	r
1	22	A
2	22	t
1	23	D
2	23	K
1	24	D
2	24	M
1	25	D
2	25	S
1	26	D
2	26	U
1	27	D
2	27	b
1	28	D
2	28	d
1	29	D
2	29	k
1	30	D
2	30	m
1	31	D
2	31	s
1	32	D
2	32	u
1	33	C
2	33	J
1	34	C
2	34	L
1	35	C
2	35	R
1	36	C
2	36	T
1	37	C
2	37	a
1	38	C
2	38	c
1	39	C
2	39	j
1	40	C
2	40	l
1	41	C
2	41	r
1	42	C
2	42	t
1	43	E
2	43	F
1	44	E
2	44	N
1	45	E
2	45	O
1	46	E
2	46	V
1	47	E
2	47	W
1	48	E
2	48	e
1	49	E
2	49	f
1	50	E
2	50	n
1	51	E
2	51	o
1	52	E
2	52	v
1	53	E
2	53	w
1	54	F
2	54	N
1	55	F
2	55	O
1	56	F
2	56	V
1	57	F
2	57	W
1	58	F
2	58	e
1	59	F
2	59	f
1	60	F
2	60	n
1	61	F
2	61	o
1	62	F
2	62	v
1	63	F
2	63	w
1	64	K
2	64	M
1	65	K
2	65	S
1	66	K
2	66	U
1	67	K
2	67	b
1	68	K
2	68	d
1	69	K
2	69	k
1	70	K
2	70	m
1	71	K
2	71	s
1	72	K
2	72	u
1	73	J
2	73	L
1	74	J
2	74	R
1	75	J
2	75	T
1	76	J
2	76	a
1	77	J
2	77	c
1	78	J
2	78	j
1	79	J
2	79	l
1	80	J
2	80	r
1	81	J
2	81	t
1	82	M
2	82	S
1	83	M
2	83	U
1	84	M
2	84	b
1	85	M
2	85	d
1	86	M
2	86	k
1	87	M
2	87	m
1	88	M
2	88	s
1	89	M
2	89	u
1	90	L
2	90	R
1	91	L
2	91	T
1	92	L
2	92	a
1	93	L
2	93	c
1	94	L
2	94	j
1	95	L
2	95	l
1	96	L
2	96	r
1	97	L
2	97	t
1	98	N
2	98	O
1	99	N
2	99	V
1	100	N
2	100	W
1	101	N
2	101	e
1	102	N
2	102	f
1	103	N
2	103	n
1	104	N
2	104	o
1	105	N
2	105	v
1	106	N
2	106	w
1	107	O
2	107	V
1	108	O
2	108	W
1	109	O
2	109	e
1	110	O
2	110	f
1	111	O
2	111	n
1	112	O
2	112	o
1	113	O
2	113	v
1	114	O
2	114	w
1	115	S
2	115	U
1	116	S
2	116	b
1	117	S
2	117	d
1	118	S
2	118	k
1	119	S
2	119	m
1	120	S
2	120	s
1	121	S
2	121	u
1	122	R
2	122	T
1	123	R
2	123	a
1	124	R
2	124	c
1	125	R
2	125	j
1	126	R
2	126	l
1	127	R
2	127	r
1	128	R
2	128	t
1	129	U
2	129	b
1	130	U
2	130	d
1	131	U
2	131	k
1	132	U
2	132	m
1	133	U
2	133	s
1	134	U
2	134	u
1	135	T
2	135	a
1	136	T
2	136	c
1	137	T
2	137	j
1	138	T
2	138	l
1	139	T
2	139	r
1	140	T
2	140	t
1	141	V
2	141	W
1	142	V
2	142	e
1	143	V
2	143	f
1	144	V
2	144	n
1	145	V
2	145	o
1	146	V
2	146	v
1	147	V
2	147	w
1	148	W
2	148	e
1	149	W
2	149	f
1	150	W
2	150	n
1	151	W
2	151	o
1	152	W
2	152	v
1	153	W
2	153	w
1	154	b
2	154	d
1	155	b
2	155	k
1	156	b
2	156	m
1	157	b
2	157	s
1	158	b
2	158	u
1	159	a
2	159	c
1	160	a
2	160	j
1	161	a
2	161	l
1	162	a
2	162	r
1	163	a
2	163	t
1	164	d
2	164	k
1	165	d
2	165	m
1	166	d
2	166	s
1	167	d
2	167	u
1	168	c
2	168	j
1	169	c
2	169	l
1	170	c
2	170	r
1	171	c
2	171	t
1	172	e
2	172	f
1	173	e
2	173	n
1	174	e
2	174	o
1	175	e
2	175	v
1	176	e
2	176	w
1	177	f
2	177	n
1	178	f
2	178	o
1	179	f
2	179	v
1	180	f
2	180	w
1	181	k
2	181	m
1	182	k
2	182	s
1	183	k
2	183	u
1	184	j
2	184	l
1	185	j
2	185	r
1	186	j
2	186	t
1	187	m
2	187	s
1	188	m
2	188	u
1	189	l
2	189	r
1	190	l
2	190	t
1	191	n
2	191	o
1	192	n
2	192	v
1	193	n
2	193	w
1	194	o
2	194	v
1	195	o
2	195	w
1	196	s
2	196	u
1	197	r
2	197	t
1	198	v
2	198	w

NCS domain segments:

Component-ID: 0 / Refine code: 0

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	VAL	VAL	B	A	417 - 638	2 - 186
2	1	LYS	LYS	VAL	VAL	D	C	417 - 638	1 - 188
1	2	LYS	LYS	ALA	ALA	B	A	417 - 637	2 - 185
2	2	LYS	LYS	ALA	ALA	K	G	417 - 637	2 - 185
1	3	LYS	LYS	VAL	VAL	B	A	417 - 638	2 - 186
2	3	LYS	LYS	VAL	VAL	M	I	417 - 638	1 - 188
1	4	LYS	LYS	VAL	VAL	B	A	417 - 638	2 - 186
2	4	LYS	LYS	VAL	VAL	S	M	417 - 638	2 - 186
1	5	LYS	LYS	VAL	VAL	B	A	417 - 638	2 - 186
2	5	LYS	LYS	VAL	VAL	U	O	417 - 638	1 - 188
1	6	LYS	LYS	VAL	VAL	B	A	417 - 638	2 - 186
2	6	LYS	LYS	VAL	VAL	b	S	417 - 638	2 - 186
1	7	LYS	LYS	ALA	ALA	B	A	417 - 637	2 - 185
2	7	LYS	LYS	ALA	ALA	d	U	417 - 637	1 - 181
1	8	LYS	LYS	ALA	ALA	B	A	417 - 637	2 - 185
2	8	LYS	LYS	ALA	ALA	k	Y	417 - 637	2 - 185
1	9	LYS	LYS	VAL	VAL	B	A	417 - 638	2 - 186
2	9	LYS	LYS	VAL	VAL	m	AA	417 - 638	1 - 188
1	10	LYS	LYS	ALA	ALA	B	A	417 - 637	2 - 185
2	10	LYS	LYS	ALA	ALA	s	EA	417 - 637	2 - 185
1	11	LYS	LYS	ALA	ALA	B	A	417 - 637	2 - 185
2	11	LYS	LYS	ALA	ALA	u	GA	417 - 637	1 - 187
1	12	GLU	GLU	GLN	GLN	A	B	11 - 489	10 - 488
2	12	GLU	GLU	GLN	GLN	C	D	11 - 489	10 - 488
1	13	GLU	GLU	GLY	GLY	A	B	11 - 491	10 - 490
2	13	GLU	GLU	GLY	GLY	J	H	11 - 491	1 - 480
1	14	GLU	GLU	LEU	LEU	A	B	11 - 490	10 - 489
2	14	GLU	GLU	LEU	LEU	L	J	11 - 490	10 - 489
1	15	GLU	GLU	GLY	GLY	A	B	11 - 491	10 - 490
2	15	GLU	GLU	GLY	GLY	R	N	11 - 491	10 - 490
1	16	GLU	GLU	LEU	LEU	A	B	11 - 490	10 - 489
2	16	GLU	GLU	LEU	LEU	T	P	11 - 490	10 - 489
1	17	GLU	GLU	GLY	GLY	A	B	11 - 491	10 - 490
2	17	GLU	GLU	GLY	GLY	a	T	11 - 491	10 - 490
1	18	GLU	GLU	GLN	GLN	A	B	11 - 489	10 - 488
2	18	GLU	GLU	GLN	GLN	c	V	11 - 489	10 - 488
1	19	GLU	GLU	GLY	GLY	A	B	11 - 491	10 - 490
2	19	GLU	GLU	GLY	GLY	j	Z	11 - 491	10 - 490
1	20	GLU	GLU	LEU	LEU	A	B	11 - 490	10 - 489
2	20	GLU	GLU	LEU	LEU	l	BA	11 - 490	10 - 489
1	21	GLU	GLU	LEU	LEU	A	B	11 - 490	10 - 489
2	21	GLU	GLU	LEU	LEU	r	FA	11 - 490	10 - 489
1	22	GLU	GLU	LEU	LEU	A	B	11 - 490	10 - 489
2	22	GLU	GLU	LEU	LEU	t	HA	11 - 490	10 - 489
1	23	LYS	LYS	VAL	VAL	D	C	417 - 638	1 - 188
2	23	LYS	LYS	VAL	VAL	K	G	417 - 638	2 - 186
1	24	LYS	LYS	ALA	ALA	D	C	417 - 637	1 - 187
2	24	LYS	LYS	ALA	ALA	M	I	417 - 637	1 - 187
1	25	LYS	LYS	VAL	VAL	D	C	417 - 638	1 - 188
2	25	LYS	LYS	VAL	VAL	S	M	417 - 638	2 - 186
1	26	LYS	LYS	VAL	VAL	D	C	417 - 638	1 - 188
2	26	LYS	LYS	VAL	VAL	U	O	417 - 638	1 - 188
1	27	LYS	LYS	VAL	VAL	D	C	417 - 638	1 - 188
2	27	LYS	LYS	VAL	VAL	b	S	417 - 638	2 - 186
1	28	LYS	LYS	ALA	ALA	D	C	417 - 637	1 - 187
2	28	LYS	LYS	ALA	ALA	d	U	417 - 637	1 - 181
1	29	LYS	LYS	VAL	VAL	D	C	417 - 638	1 - 188
2	29	LYS	LYS	VAL	VAL	k	Y	417 - 638	2 - 186
1	30	LYS	LYS	VAL	VAL	D	C	417 - 638	1 - 188
2	30	LYS	LYS	VAL	VAL	m	AA	417 - 638	1 - 188
1	31	LYS	LYS	VAL	VAL	D	C	417 - 638	1 - 188
2	31	LYS	LYS	VAL	VAL	s	EA	417 - 638	2 - 186
1	32	LYS	LYS	ASN	ASN	D	C	417 - 636	1 - 186
2	32	LYS	LYS	ASN	ASN	u	GA	417 - 636	1 - 186
1	33	GLU	GLU	GLN	GLN	C	D	11 - 489	10 - 488
2	33	GLU	GLU	GLN	GLN	J	H	11 - 489	1 - 478
1	34	ASN	ASN	GLN	GLN	C	D	10 - 489	9 - 488
2	34	ASN	ASN	GLN	GLN	L	J	10 - 489	9 - 488
1	35	ASN	ASN	GLN	GLN	C	D	10 - 489	9 - 488
2	35	ASN	ASN	GLN	GLN	R	N	10 - 489	9 - 488
1	36	ASN	ASN	GLN	GLN	C	D	10 - 489	9 - 488
2	36	ASN	ASN	GLN	GLN	T	P	10 - 489	9 - 488
1	37	GLU	GLU	GLN	GLN	C	D	11 - 489	10 - 488
2	37	GLU	GLU	GLN	GLN	a	T	11 - 489	10 - 488
1	38	ILE	ILE	LEU	LEU	C	D	9 - 490	8 - 489
2	38	ILE	ILE	LEU	LEU	c	V	9 - 490	8 - 489
1	39	ASN	ASN	GLN	GLN	C	D	10 - 489	9 - 488
2	39	ASN	ASN	GLN	GLN	j	Z	10 - 489	9 - 488
1	40	ASN	ASN	GLN	GLN	C	D	10 - 489	9 - 488
2	40	ASN	ASN	GLN	GLN	l	BA	10 - 489	9 - 488
1	41	ILE	ILE	GLN	GLN	C	D	9 - 489	8 - 488
2	41	ILE	ILE	GLN	GLN	r	FA	9 - 489	8 - 488
1	42	ASN	ASN	GLN	GLN	C	D	10 - 489	9 - 488
2	42	ASN	ASN	GLN	GLN	t	HA	10 - 489	9 - 488
1	43	DG	DG	DT	DT	E	E	1 - 20	1 - 20
2	43	DG	DG	DT	DT	F	F	1 - 2020	1 - 20
1	44	DG	DG	DT	DT	E	E	1 - 20	1 - 20
2	44	DG	DG	DT	DT	N	K	1 - 2020	1 - 20
1	45	DG	DG	DT	DT	E	E	1 - 20	1 - 20
2	45	DG	DG	DT	DT	O	L	1 - 20	1 - 20
1	46	DG	DG	DC	DC	E	E	1 - 18	1 - 18
2	46	DG	DG	DC	DC	V	Q	1 - 2018	1 - 18
1	47	DG	DG	DT	DT	E	E	1 - 20	1 - 20
2	47	DG	DG	DT	DT	W	R	1 - 2020	1 - 20
1	48	DG	DG	DT	DT	E	E	1 - 20	1 - 20
2	48	DG	DG	DT	DT	e	W	1 - 20	1 - 20
1	49	DG	DG	DC	DC	E	E	3 - 18	3 - 18
2	49	DG	DG	DC	DC	f	X	3 - 18	1 - 16
1	50	DG	DG	DT	DT	E	E	1 - 20	1 - 20
2	50	DG	DG	DT	DT	n	CA	1 - 2020	1 - 20
1	51	DA	DA	DC	DC	E	E	2 - 18	2 - 18
2	51	DA	DA	DC	DC	o	DA	2 - 2018	2 - 18
1	52	DA	DA	DT	DT	E	E	2 - 19	2 - 19
2	52	DA	DA	DT	DT	v	IA	2 - 2019	2 - 19
1	53	DG	DG	DT	DT	E	E	1 - 20	1 - 20
2	53	DG	DG	DT	DT	w	JA	1 - 2020	1 - 20
1	54	DG	DG	DT	DT	F	F	1 - 2020	1 - 20
2	54	DG	DG	DT	DT	N	K	1 - 2020	1 - 20
1	55	DG	DG	DT	DT	F	F	1 - 2020	1 - 20
2	55	DG	DG	DT	DT	O	L	1 - 20	1 - 20
1	56	DG	DG	DC	DC	F	F	1 - 2018	1 - 18
2	56	DG	DG	DC	DC	V	Q	1 - 2018	1 - 18
1	57	DG	DG	DT	DT	F	F	1 - 2020	1 - 20
2	57	DG	DG	DT	DT	W	R	1 - 2020	1 - 20
1	58	DG	DG	DT	DT	F	F	1 - 2020	1 - 20
2	58	DG	DG	DT	DT	e	W	1 - 20	1 - 20
1	59	DG	DG	DC	DC	F	F	3 - 2018	3 - 18
2	59	DG	DG	DC	DC	f	X	3 - 18	1 - 16
1	60	DG	DG	DT	DT	F	F	1 - 2020	1 - 20
2	60	DG	DG	DT	DT	n	CA	1 - 2020	1 - 20
1	61	DA	DA	DC	DC	F	F	2 - 2018	2 - 18
2	61	DA	DA	DC	DC	o	DA	2 - 2018	2 - 18
1	62	DA	DA	DT	DT	F	F	2 - 2019	2 - 19
2	62	DA	DA	DT	DT	v	IA	2 - 2019	2 - 19
1	63	DG	DG	DT	DT	F	F	1 - 2020	1 - 20
2	63	DG	DG	DT	DT	w	JA	1 - 2020	1 - 20
1	64	LYS	LYS	TYR	TYR	K	G	417 - 639	2 - 187
2	64	LYS	LYS	TYR	TYR	M	I	417 - 639	1 - 189
1	65	LYS	LYS	ALA	ALA	K	G	417 - 637	2 - 185
2	65	LYS	LYS	ALA	ALA	S	M	417 - 637	2 - 185
1	66	LYS	LYS	VAL	VAL	K	G	417 - 638	2 - 186
2	66	LYS	LYS	VAL	VAL	U	O	417 - 638	1 - 188
1	67	LYS	LYS	ALA	ALA	K	G	417 - 637	2 - 185
2	67	LYS	LYS	ALA	ALA	b	S	417 - 637	2 - 185
1	68	LYS	LYS	ALA	ALA	K	G	417 - 637	2 - 185
2	68	LYS	LYS	ALA	ALA	d	U	417 - 637	1 - 181
1	69	GLY	GLY	VAL	VAL	K	G	416 - 638	1 - 186
2	69	GLY	GLY	VAL	VAL	k	Y	416 - 638	1 - 186
1	70	LYS	LYS	VAL	VAL	K	G	417 - 638	2 - 186
2	70	LYS	LYS	VAL	VAL	m	AA	417 - 638	1 - 188
1	71	GLY	GLY	ALA	ALA	K	G	416 - 637	1 - 185
2	71	GLY	GLY	ALA	ALA	s	EA	416 - 637	1 - 185
1	72	LYS	LYS	ALA	ALA	K	G	417 - 637	2 - 185
2	72	LYS	LYS	ALA	ALA	u	GA	417 - 637	1 - 187
1	73	GLU	GLU	GLN	GLN	J	H	11 - 489	1 - 478
2	73	GLU	GLU	GLN	GLN	L	J	11 - 489	10 - 488
1	74	GLU	GLU	GLY	GLY	J	H	11 - 491	1 - 480
2	74	GLU	GLU	GLY	GLY	R	N	11 - 491	10 - 490
1	75	GLU	GLU	GLN	GLN	J	H	11 - 489	1 - 478
2	75	GLU	GLU	GLN	GLN	T	P	11 - 489	10 - 488
1	76	GLU	GLU	GLY	GLY	J	H	11 - 491	1 - 480
2	76	GLU	GLU	GLY	GLY	a	T	11 - 491	10 - 490
1	77	GLU	GLU	GLN	GLN	J	H	11 - 489	1 - 478
2	77	GLU	GLU	GLN	GLN	c	V	11 - 489	10 - 488
1	78	GLU	GLU	GLY	GLY	J	H	11 - 491	1 - 480
2	78	GLU	GLU	GLY	GLY	j	Z	11 - 491	10 - 490
1	79	GLU	GLU	GLN	GLN	J	H	11 - 489	1 - 478
2	79	GLU	GLU	GLN	GLN	l	BA	11 - 489	10 - 488
1	80	GLU	GLU	LEU	LEU	J	H	11 - 490	1 - 479
2	80	GLU	GLU	LEU	LEU	r	FA	11 - 490	10 - 489
1	81	GLU	GLU	GLN	GLN	J	H	11 - 489	1 - 478
2	81	GLU	GLU	GLN	GLN	t	HA	11 - 489	10 - 488
1	82	LYS	LYS	VAL	VAL	M	I	417 - 638	1 - 188
2	82	LYS	LYS	VAL	VAL	S	M	417 - 638	2 - 186
1	83	LYS	LYS	ALA	ALA	M	I	417 - 637	1 - 187
2	83	LYS	LYS	ALA	ALA	U	O	417 - 637	1 - 187
1	84	LYS	LYS	VAL	VAL	M	I	417 - 638	1 - 188
2	84	LYS	LYS	VAL	VAL	b	S	417 - 638	2 - 186
1	85	LYS	LYS	ALA	ALA	M	I	417 - 637	1 - 187
2	85	LYS	LYS	ALA	ALA	d	U	417 - 637	1 - 181
1	86	LYS	LYS	TYR	TYR	M	I	417 - 639	1 - 189
2	86	LYS	LYS	TYR	TYR	k	Y	417 - 639	2 - 187
1	87	LYS	LYS	ALA	ALA	M	I	417 - 637	1 - 187
2	87	LYS	LYS	ALA	ALA	m	AA	417 - 637	1 - 187
1	88	LYS	LYS	VAL	VAL	M	I	417 - 638	1 - 188
2	88	LYS	LYS	VAL	VAL	s	EA	417 - 638	2 - 186
1	89	LYS	LYS	ASN	ASN	M	I	417 - 636	1 - 186
2	89	LYS	LYS	ASN	ASN	u	GA	417 - 636	1 - 186
1	90	ASN	ASN	GLN	GLN	L	J	10 - 489	9 - 488
2	90	ASN	ASN	GLN	GLN	R	N	10 - 489	9 - 488
1	91	ASN	ASN	LEU	LEU	L	J	10 - 490	9 - 489
2	91	ASN	ASN	LEU	LEU	T	P	10 - 490	9 - 489
1	92	GLU	GLU	GLN	GLN	L	J	11 - 489	10 - 488
2	92	GLU	GLU	GLN	GLN	a	T	11 - 489	10 - 488
1	93	ASN	ASN	GLN	GLN	L	J	10 - 489	9 - 488
2	93	ASN	ASN	GLN	GLN	c	V	10 - 489	9 - 488
1	94	ASN	ASN	GLN	GLN	L	J	10 - 489	9 - 488
2	94	ASN	ASN	GLN	GLN	j	Z	10 - 489	9 - 488
1	95	ASN	ASN	LEU	LEU	L	J	10 - 490	9 - 489
2	95	ASN	ASN	LEU	LEU	l	BA	10 - 490	9 - 489
1	96	ASN	ASN	GLN	GLN	L	J	10 - 489	9 - 488
2	96	ASN	ASN	GLN	GLN	r	FA	10 - 489	9 - 488
1	97	ASN	ASN	LEU	LEU	L	J	10 - 490	9 - 489
2	97	ASN	ASN	LEU	LEU	t	HA	10 - 490	9 - 489
1	98	DG	DG	DT	DT	N	K	1 - 2020	1 - 20
2	98	DG	DG	DT	DT	O	L	1 - 20	1 - 20
1	99	DG	DG	DC	DC	N	K	1 - 2018	1 - 18
2	99	DG	DG	DC	DC	V	Q	1 - 2018	1 - 18
1	100	DG	DG	DT	DT	N	K	1 - 2020	1 - 20
2	100	DG	DG	DT	DT	W	R	1 - 2020	1 - 20
1	101	DG	DG	DT	DT	N	K	1 - 2020	1 - 20
2	101	DG	DG	DT	DT	e	W	1 - 20	1 - 20
1	102	DG	DG	DC	DC	N	K	3 - 2018	3 - 18
2	102	DG	DG	DC	DC	f	X	3 - 18	1 - 16
1	103	DG	DG	DT	DT	N	K	1 - 2020	1 - 20
2	103	DG	DG	DT	DT	n	CA	1 - 2020	1 - 20
1	104	DA	DA	DC	DC	N	K	2 - 2018	2 - 18
2	104	DA	DA	DC	DC	o	DA	2 - 2018	2 - 18
1	105	DA	DA	DT	DT	N	K	2 - 2019	2 - 19
2	105	DA	DA	DT	DT	v	IA	2 - 2019	2 - 19
1	106	DG	DG	DT	DT	N	K	1 - 2020	1 - 20
2	106	DG	DG	DT	DT	w	JA	1 - 2020	1 - 20
1	107	DG	DG	DC	DC	O	L	1 - 18	1 - 18
2	107	DG	DG	DC	DC	V	Q	1 - 2018	1 - 18
1	108	DG	DG	DT	DT	O	L	1 - 20	1 - 20
2	108	DG	DG	DT	DT	W	R	1 - 2020	1 - 20
1	109	DG	DG	DT	DT	O	L	1 - 20	1 - 20
2	109	DG	DG	DT	DT	e	W	1 - 20	1 - 20
1	110	DG	DG	DC	DC	O	L	3 - 18	3 - 18
2	110	DG	DG	DC	DC	f	X	3 - 18	1 - 16
1	111	DG	DG	DT	DT	O	L	1 - 20	1 - 20
2	111	DG	DG	DT	DT	n	CA	1 - 2020	1 - 20
1	112	DA	DA	DC	DC	O	L	2 - 18	2 - 18
2	112	DA	DA	DC	DC	o	DA	2 - 2018	2 - 18
1	113	DA	DA	DT	DT	O	L	2 - 19	2 - 19
2	113	DA	DA	DT	DT	v	IA	2 - 2019	2 - 19
1	114	DG	DG	DT	DT	O	L	1 - 20	1 - 20
2	114	DG	DG	DT	DT	w	JA	1 - 2020	1 - 20
1	115	LYS	LYS	VAL	VAL	S	M	417 - 638	2 - 186
2	115	LYS	LYS	VAL	VAL	U	O	417 - 638	1 - 188
1	116	LYS	LYS	VAL	VAL	S	M	417 - 638	2 - 186
2	116	LYS	LYS	VAL	VAL	b	S	417 - 638	2 - 186
1	117	LYS	LYS	ALA	ALA	S	M	417 - 637	2 - 185
2	117	LYS	LYS	ALA	ALA	d	U	417 - 637	1 - 181
1	118	LYS	LYS	ALA	ALA	S	M	417 - 637	2 - 185
2	118	LYS	LYS	ALA	ALA	k	Y	417 - 637	2 - 185
1	119	LYS	LYS	VAL	VAL	S	M	417 - 638	2 - 186
2	119	LYS	LYS	VAL	VAL	m	AA	417 - 638	1 - 188
1	120	LYS	LYS	ALA	ALA	S	M	417 - 637	2 - 185
2	120	LYS	LYS	ALA	ALA	s	EA	417 - 637	2 - 185
1	121	LYS	LYS	ALA	ALA	S	M	417 - 637	2 - 185
2	121	LYS	LYS	ALA	ALA	u	GA	417 - 637	1 - 187
1	122	ASN	ASN	GLN	GLN	R	N	10 - 489	9 - 488
2	122	ASN	ASN	GLN	GLN	T	P	10 - 489	9 - 488
1	123	GLU	GLU	LEU	LEU	R	N	11 - 490	10 - 489
2	123	GLU	GLU	LEU	LEU	a	T	11 - 490	10 - 489
1	124	ASN	ASN	GLN	GLN	R	N	10 - 489	9 - 488
2	124	ASN	ASN	GLN	GLN	c	V	10 - 489	9 - 488
1	125	ASN	ASN	GLY	GLY	R	N	10 - 491	9 - 490
2	125	ASN	ASN	GLY	GLY	j	Z	10 - 491	9 - 490
1	126	ASN	ASN	GLN	GLN	R	N	10 - 489	9 - 488
2	126	ASN	ASN	GLN	GLN	l	BA	10 - 489	9 - 488
1	127	ASN	ASN	LEU	LEU	R	N	10 - 490	9 - 489
2	127	ASN	ASN	LEU	LEU	r	FA	10 - 490	9 - 489
1	128	ASN	ASN	GLN	GLN	R	N	10 - 489	9 - 488
2	128	ASN	ASN	GLN	GLN	t	HA	10 - 489	9 - 488
1	129	LYS	LYS	VAL	VAL	U	O	417 - 638	1 - 188
2	129	LYS	LYS	VAL	VAL	b	S	417 - 638	2 - 186
1	130	LYS	LYS	ALA	ALA	U	O	417 - 637	1 - 187
2	130	LYS	LYS	ALA	ALA	d	U	417 - 637	1 - 181
1	131	LYS	LYS	VAL	VAL	U	O	417 - 638	1 - 188
2	131	LYS	LYS	VAL	VAL	k	Y	417 - 638	2 - 186
1	132	LYS	LYS	VAL	VAL	U	O	417 - 638	1 - 188
2	132	LYS	LYS	VAL	VAL	m	AA	417 - 638	1 - 188
1	133	LYS	LYS	VAL	VAL	U	O	417 - 638	1 - 188
2	133	LYS	LYS	VAL	VAL	s	EA	417 - 638	2 - 186
1	134	LYS	LYS	ASN	ASN	U	O	417 - 636	1 - 186
2	134	LYS	LYS	ASN	ASN	u	GA	417 - 636	1 - 186
1	135	GLU	GLU	GLN	GLN	T	P	11 - 489	10 - 488
2	135	GLU	GLU	GLN	GLN	a	T	11 - 489	10 - 488
1	136	ASN	ASN	GLN	GLN	T	P	10 - 489	9 - 488
2	136	ASN	ASN	GLN	GLN	c	V	10 - 489	9 - 488
1	137	ASN	ASN	GLN	GLN	T	P	10 - 489	9 - 488
2	137	ASN	ASN	GLN	GLN	j	Z	10 - 489	9 - 488
1	138	ASN	ASN	LEU	LEU	T	P	10 - 490	9 - 489
2	138	ASN	ASN	LEU	LEU	l	BA	10 - 490	9 - 489
1	139	ASN	ASN	GLN	GLN	T	P	10 - 489	9 - 488
2	139	ASN	ASN	GLN	GLN	r	FA	10 - 489	9 - 488
1	140	ASN	ASN	LEU	LEU	T	P	10 - 490	9 - 489
2	140	ASN	ASN	LEU	LEU	t	HA	10 - 490	9 - 489
1	141	DG	DG	DC	DC	V	Q	1 - 2018	1 - 18
2	141	DG	DG	DC	DC	W	R	1 - 2018	1 - 18
1	142	DG	DG	DC	DC	V	Q	1 - 2018	1 - 18
2	142	DG	DG	DC	DC	e	W	1 - 18	1 - 18
1	143	DG	DG	DC	DC	V	Q	3 - 2018	3 - 18
2	143	DG	DG	DC	DC	f	X	3 - 18	1 - 16
1	144	DG	DG	DC	DC	V	Q	1 - 2018	1 - 18
2	144	DG	DG	DC	DC	n	CA	1 - 2018	1 - 18
1	145	DA	DA	DC	DC	V	Q	2 - 2018	2 - 18
2	145	DA	DA	DC	DC	o	DA	2 - 2018	2 - 18
1	146	DA	DA	DC	DC	V	Q	2 - 2018	2 - 18
2	146	DA	DA	DC	DC	v	IA	2 - 2018	2 - 18
1	147	DG	DG	DC	DC	V	Q	1 - 2018	1 - 18
2	147	DG	DG	DC	DC	w	JA	1 - 2018	1 - 18
1	148	DG	DG	DT	DT	W	R	1 - 2020	1 - 20
2	148	DG	DG	DT	DT	e	W	1 - 20	1 - 20
1	149	DG	DG	DC	DC	W	R	3 - 2018	3 - 18
2	149	DG	DG	DC	DC	f	X	3 - 18	1 - 16
1	150	DG	DG	DT	DT	W	R	1 - 2020	1 - 20
2	150	DG	DG	DT	DT	n	CA	1 - 2020	1 - 20
1	151	DA	DA	DC	DC	W	R	2 - 2018	2 - 18
2	151	DA	DA	DC	DC	o	DA	2 - 2018	2 - 18
1	152	DA	DA	DT	DT	W	R	2 - 2019	2 - 19
2	152	DA	DA	DT	DT	v	IA	2 - 2019	2 - 19
1	153	DG	DG	DT	DT	W	R	1 - 2020	1 - 20
2	153	DG	DG	DT	DT	w	JA	1 - 2020	1 - 20
1	154	LYS	LYS	ALA	ALA	b	S	417 - 637	2 - 185
2	154	LYS	LYS	ALA	ALA	d	U	417 - 637	1 - 181
1	155	LYS	LYS	ALA	ALA	b	S	417 - 637	2 - 185
2	155	LYS	LYS	ALA	ALA	k	Y	417 - 637	2 - 185
1	156	LYS	LYS	VAL	VAL	b	S	417 - 638	2 - 186
2	156	LYS	LYS	VAL	VAL	m	AA	417 - 638	1 - 188
1	157	LYS	LYS	ALA	ALA	b	S	417 - 637	2 - 185
2	157	LYS	LYS	ALA	ALA	s	EA	417 - 637	2 - 185
1	158	LYS	LYS	ALA	ALA	b	S	417 - 637	2 - 185
2	158	LYS	LYS	ALA	ALA	u	GA	417 - 637	1 - 187
1	159	GLU	GLU	GLN	GLN	a	T	11 - 489	10 - 488
2	159	GLU	GLU	GLN	GLN	c	V	11 - 489	10 - 488
1	160	GLU	GLU	LEU	LEU	a	T	11 - 490	10 - 489
2	160	GLU	GLU	LEU	LEU	j	Z	11 - 490	10 - 489
1	161	GLU	GLU	GLN	GLN	a	T	11 - 489	10 - 488
2	161	GLU	GLU	GLN	GLN	l	BA	11 - 489	10 - 488
1	162	GLU	GLU	LEU	LEU	a	T	11 - 490	10 - 489
2	162	GLU	GLU	LEU	LEU	r	FA	11 - 490	10 - 489
1	163	GLU	GLU	GLN	GLN	a	T	11 - 489	10 - 488
2	163	GLU	GLU	GLN	GLN	t	HA	11 - 489	10 - 488
1	164	LYS	LYS	ASN	ASN	d	U	417 - 636	1 - 180
2	164	LYS	LYS	ASN	ASN	k	Y	417 - 636	2 - 184
1	165	LYS	LYS	ALA	ALA	d	U	417 - 637	1 - 181
2	165	LYS	LYS	ALA	ALA	m	AA	417 - 637	1 - 187
1	166	LYS	LYS	ALA	ALA	d	U	417 - 637	1 - 181
2	166	LYS	LYS	ALA	ALA	s	EA	417 - 637	2 - 185
1	167	LYS	LYS	ALA	ALA	d	U	417 - 637	1 - 181
2	167	LYS	LYS	ALA	ALA	u	GA	417 - 637	1 - 187
1	168	ASN	ASN	GLN	GLN	c	V	10 - 489	9 - 488
2	168	ASN	ASN	GLN	GLN	j	Z	10 - 489	9 - 488
1	169	ASN	ASN	GLN	GLN	c	V	10 - 489	9 - 488
2	169	ASN	ASN	GLN	GLN	l	BA	10 - 489	9 - 488
1	170	ILE	ILE	GLN	GLN	c	V	9 - 489	8 - 488
2	170	ILE	ILE	GLN	GLN	r	FA	9 - 489	8 - 488
1	171	ASN	ASN	GLN	GLN	c	V	10 - 489	9 - 488
2	171	ASN	ASN	GLN	GLN	t	HA	10 - 489	9 - 488
1	172	DG	DG	DC	DC	e	W	3 - 18	3 - 18
2	172	DG	DG	DC	DC	f	X	3 - 18	1 - 16
1	173	DG	DG	DT	DT	e	W	1 - 20	1 - 20
2	173	DG	DG	DT	DT	n	CA	1 - 2020	1 - 20
1	174	DA	DA	DC	DC	e	W	2 - 18	2 - 18
2	174	DA	DA	DC	DC	o	DA	2 - 2018	2 - 18
1	175	DA	DA	DT	DT	e	W	2 - 19	2 - 19
2	175	DA	DA	DT	DT	v	IA	2 - 2019	2 - 19
1	176	DG	DG	DT	DT	e	W	1 - 20	1 - 20
2	176	DG	DG	DT	DT	w	JA	1 - 2020	1 - 20
1	177	DG	DG	DC	DC	f	X	3 - 18	1 - 16
2	177	DG	DG	DC	DC	n	CA	3 - 2018	3 - 18
1	178	DG	DG	DC	DC	f	X	3 - 18	1 - 16
2	178	DG	DG	DC	DC	o	DA	3 - 2018	3 - 18
1	179	DG	DG	DC	DC	f	X	3 - 18	1 - 16
2	179	DG	DG	DC	DC	v	IA	3 - 2018	3 - 18
1	180	DG	DG	DC	DC	f	X	3 - 18	1 - 16
2	180	DG	DG	DC	DC	w	JA	3 - 2018	3 - 18
1	181	LYS	LYS	VAL	VAL	k	Y	417 - 638	2 - 186
2	181	LYS	LYS	VAL	VAL	m	AA	417 - 638	1 - 188
1	182	GLY	GLY	ALA	ALA	k	Y	416 - 637	1 - 185
2	182	GLY	GLY	ALA	ALA	s	EA	416 - 637	1 - 185
1	183	LYS	LYS	ASN	ASN	k	Y	417 - 636	2 - 184
2	183	LYS	LYS	ASN	ASN	u	GA	417 - 636	1 - 186
1	184	ASN	ASN	GLN	GLN	j	Z	10 - 489	9 - 488
2	184	ASN	ASN	GLN	GLN	l	BA	10 - 489	9 - 488
1	185	ASN	ASN	LEU	LEU	j	Z	10 - 490	9 - 489
2	185	ASN	ASN	LEU	LEU	r	FA	10 - 490	9 - 489
1	186	ASN	ASN	GLN	GLN	j	Z	10 - 489	9 - 488
2	186	ASN	ASN	GLN	GLN	t	HA	10 - 489	9 - 488
1	187	LYS	LYS	VAL	VAL	m	AA	417 - 638	1 - 188
2	187	LYS	LYS	VAL	VAL	s	EA	417 - 638	2 - 186
1	188	LYS	LYS	ASN	ASN	m	AA	417 - 636	1 - 186
2	188	LYS	LYS	ASN	ASN	u	GA	417 - 636	1 - 186
1	189	ASN	ASN	GLN	GLN	l	BA	10 - 489	9 - 488
2	189	ASN	ASN	GLN	GLN	r	FA	10 - 489	9 - 488
1	190	ASN	ASN	LEU	LEU	l	BA	10 - 490	9 - 489
2	190	ASN	ASN	LEU	LEU	t	HA	10 - 490	9 - 489
1	191	DA	DA	DC	DC	n	CA	2 - 2018	2 - 18
2	191	DA	DA	DC	DC	o	DA	2 - 2018	2 - 18
1	192	DA	DA	DT	DT	n	CA	2 - 2019	2 - 19
2	192	DA	DA	DT	DT	v	IA	2 - 2019	2 - 19
1	193	DG	DG	DT	DT	n	CA	1 - 2020	1 - 20
2	193	DG	DG	DT	DT	w	JA	1 - 2020	1 - 20
1	194	DA	DA	DC	DC	o	DA	2 - 2018	2 - 18
2	194	DA	DA	DC	DC	v	IA	2 - 2018	2 - 18
1	195	DA	DA	DC	DC	o	DA	2 - 2018	2 - 18
2	195	DA	DA	DC	DC	w	JA	2 - 2018	2 - 18
1	196	LYS	LYS	ALA	ALA	s	EA	417 - 637	2 - 185
2	196	LYS	LYS	ALA	ALA	u	GA	417 - 637	1 - 187
1	197	ASN	ASN	GLN	GLN	r	FA	10 - 489	9 - 488
2	197	ASN	ASN	GLN	GLN	t	HA	10 - 489	9 - 488
1	198	DA	DA	DT	DT	v	IA	2 - 2019	2 - 19
2	198	DA	DA	DT	DT	w	JA	2 - 2019	2 - 19

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
191
192
193
194
195
196
197
198

Components

DNA gyrase subunit ... , 9 types, 24 molecules B S b s A C L R T a c j l r t D U m K J M d k u

#1: Protein

B S b s
DNA gyrase subunit B,DNA gyrase subunit B /

Details:

Mass: 20846.738 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Staphylococcus aureus (bacteria) / Gene: gyrB, gyrB, SAV0005 / Production host: Escherichia coli (E. coli) / References: UniProt: P0A0K8, UniProt: P66936, EC: 5.99.1.3

#2: Protein

A C L R T a c j l r t
DNA gyrase subunit A /

Details:

Mass: 55537.312 Da / Num. of mol.: 11 / Mutation: 123 phosphotyrosine
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Staphylococcus aureus (bacteria) / Gene: gyrA, SA0006 / Production host: Escherichia coli (E. coli) / References: UniProt: Q99XG5, EC: 5.99.1.3

#3: Protein

D U m DNA gyrase subunit B,DNA gyrase subunit B /

Details:

Mass: 21111.018 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Staphylococcus aureus (bacteria) / Gene: gyrB, gyrB, SAR0005 / Production host: Escherichia coli (E. coli) / References: UniProt: P0A0K8, UniProt: Q6GKU0, EC: 5.99.1.3

#5: Protein

K DNA gyrase subunit B,DNA gyrase subunit B /

Details:

Mass: 21009.914 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Staphylococcus aureus (bacteria) / Gene: gyrB, SA0005, gyrB, SAUSA300_0005 / Production host: Escherichia coli (E. coli)
References: UniProt: P66937, UniProt: Q2FKQ1, UniProt: P0A0K8*PLUS, EC: 5.99.1.3

#6: Protein

J DNA gyrase subunit A /

Details:

Mass: 54370.000 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Staphylococcus aureus (bacteria) / Gene: gyrA, SA0006 / Production host: Escherichia coli (E. coli) / References: UniProt: Q99XG5, EC: 5.99.1.3

#7: Protein

M DNA gyrase subunit B,DNA gyrase subunit B /

Details:

Mass: 21274.191 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Staphylococcus aureus (bacteria) / Gene: gyrB, SA0005, gyrB, SAUSA300_0005 / Production host: Escherichia coli (E. coli)
References: UniProt: P66937, UniProt: Q2FKQ1, UniProt: P0A0K8*PLUS, EC: 5.99.1.3

#9: Protein

d DNA gyrase subunit B,DNA gyrase subunit B /

Details:

Mass: 20363.156 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Staphylococcus aureus (bacteria) / Gene: gyrB, SA0005, gyrB, SAR0005 / Production host: Escherichia coli (E. coli)
References: UniProt: P66937, UniProt: Q6GKU0, UniProt: P0A0K8*PLUS, EC: 5.99.1.3

#11: Protein

k DNA gyrase subunit B,DNA gyrase subunit B /

Details:

Mass: 21080.992 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Staphylococcus aureus (bacteria) / Gene: gyrB, SA0005, gyrB, SAR0005 / Production host: Escherichia coli (E. coli)
References: UniProt: P66937, UniProt: Q6GKU0, UniProt: P0A0K8*PLUS, EC: 5.99.1.3

#12: Protein

u DNA gyrase subunit B,DNA gyrase subunit B /

Details:

Mass: 21011.887 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Staphylococcus aureus (bacteria) / Gene: gyrB, SA0005, gyrB, SAUSA300_0005 / Production host: Escherichia coli (E. coli)
References: UniProt: P66937, UniProt: Q2FKQ1, UniProt: P0A0K8*PLUS, EC: 5.99.1.3

DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)- ... , 3 types, 12 molecules E F N O W e n v w V o f

#4: DNA chain

E F N O W e n v w
DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)-3')

Details:

Mass: 6150.966 Da / Num. of mol.: 9
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) synthetic construct (others) / Production host: synthetic construct (others)

#8: DNA chain

V o DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)-3')

Details:

Mass: 5846.773 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) synthetic construct (others) / Production host: synthetic construct (others)

#10: DNA chain

f DNA (5'-D(*GP*AP*GP*CP*GP*TP*AP*CP*GP*GP*CP*CP*GP*TP*AP*CP*GP*CP*TP*T)-3')

Details:

Mass: 5204.360 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) synthetic construct (others) / Production host: synthetic construct (others)

Non-polymers , 1 types, 12 molecules

#13: Chemical

A-501 C-501 J-501 L-501 R-501 U-701 b-701 d-701 k-701 l-501 s-701 t-501
ChemComp-JK8 / (2~{R})-2-[[5-(2-chlorophenyl)-1,2-benzoxazol-3-yl]oxy]-2-phenyl-ethanamine

Details:

Mass: 364.825 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C₂₁H₁₇ClN₂O₂

Experimental details

Experiment

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

Sample preparation

• Crystal: Density Matthews: 3.2 ų/Da / Density % sol: 61.55 %
• Crystal grow: Temperature: 293 K / Method: microbatch; Details: 10% perg 5k mme, 150mM Bis Tris pH6.2 - see paper for details.

Data collection

• Diffraction: Mean temperature: 100 K / Serial crystal experiment: N
• Diffraction source: Source: SYNCHROTRON / Site: Diamond / Beamline: I23 / Wavelength: 0.9795 Å
• Detector: Type: ADSC QUANTUM 315 / Detector: CCD / Date: Apr 18, 2012
• Radiation: Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
• Radiation wavelength: Wavelength: 0.9795 Å / Relative weight: 1

Reflection twin

Crystal-ID	ID	Operator	Domain-ID	Fraction
1	1	H, K, L	1	0.525
1	1	-H-4/2L, -K, L	2	0.475

• Reflection: Resolution: 3.4→162.15 Å / Num. obs: 135780 / % possible obs: 81.1 % / Redundancy: 3.1 % / R_merge(I) obs: 0.121 / R_pim(I) all: 0.077 / R_rim(I) all: 0.144 / Net I/σ(I): 10.6
• Reflection shell: Resolution: 3.4→3.58 Å / Redundancy: 3.1 % / R_merge(I) obs: 0.369 / Num. unique obs: 20498 / R_pim(I) all: 0.237 / R_rim(I) all: 0.44 / % possible all: 83.9

Processing

Software

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

Refinement

Method to determine structure: MOLECULAR REPLACEMENT
Starting model: 2XCS

2xcs

Resolution: 3.4→162.15 Å / Cor.coef. F_o:F_c: 0.911 / Cor.coef. F_o:F_c free: 0.879 / SU B: 20.499 / SU ML: 0.343 / Cross valid method: THROUGHOUT / ESU R Free: 0.119 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	Rfactor	Num. reflection	% reflection	Selection details
Rfree	0.20834	6786	5 %	RANDOM
Rwork	0.17627	-	-	-
obs	0.17787	128993	80.35 %	-

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

Displacement parameters

B_iso mean: 53.745 Ų

	Baniso -1	Baniso -2	Baniso -3
1-	7.76 Å2	0 Å2	-1.93 Å2
2-	-	15.83 Å2	0 Å2
3-	-	-	-23.59 Å2

Refinement step

Cycle: LAST / Resolution: 3.4→162.15 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	61755	4642	312	0	66709

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.007	0.013	69826
X-RAY DIFFRACTION	r_bond_other_d	0.003	0.017	62645
X-RAY DIFFRACTION	r_angle_refined_deg	1.479	1.611	95659
X-RAY DIFFRACTION	r_angle_other_deg	1.237	1.642	144583
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	6.147	5	8294
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	30.382	21.451	3735
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	15.82	15	11236
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	18.574	15	652
X-RAY DIFFRACTION	r_chiral_restr	0.058	0.2	9378
X-RAY DIFFRACTION	r_gen_planes_refined	0.005	0.02	77551
X-RAY DIFFRACTION	r_gen_planes_other	0.002	0.02	15141
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	5.195	5.766	32804
X-RAY DIFFRACTION	r_mcbond_other	5.195	5.766	32803
X-RAY DIFFRACTION	r_mcangle_it	8.43	8.64	41197
X-RAY DIFFRACTION	r_mcangle_other	8.43	8.64	41198
X-RAY DIFFRACTION	r_scbond_it	4.944	6.025	37022
X-RAY DIFFRACTION	r_scbond_other	4.944	6.025	37023
X-RAY DIFFRACTION	r_scangle_it
X-RAY DIFFRACTION	r_scangle_other	8.069	8.94	54454
X-RAY DIFFRACTION	r_long_range_B_refined	15.951		284993
X-RAY DIFFRACTION	r_long_range_B_other	15.951		284994
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	B	5576	0.08
1	2	D	5576	0.08
2	1	B	5763	0.04
2	2	K	5763	0.04
3	1	B	5567	0.08
3	2	M	5567	0.08
4	1	B	5788	0.04
4	2	S	5788	0.04
5	1	B	5585	0.08
5	2	U	5585	0.08
6	1	B	5766	0.03
6	2	b	5766	0.03
7	1	B	5408	0.08
7	2	d	5408	0.08
8	1	B	5756	0.02
8	2	k	5756	0.02
9	1	B	5559	0.08
9	2	m	5559	0.08
10	1	B	5770	0.02
10	2	s	5770	0.02
11	1	B	5555	0.08
11	2	u	5555	0.08
12	1	A	15445	0.07
12	2	C	15445	0.07
13	1	A	15829	0.05
13	2	J	15829	0.05
14	1	A	15444	0.07
14	2	L	15444	0.07
15	1	A	15744	0.06
15	2	R	15744	0.06
16	1	A	15463	0.07
16	2	T	15463	0.07
17	1	A	15783	0.05
17	2	a	15783	0.05
18	1	A	15482	0.07
18	2	c	15482	0.07
19	1	A	15805	0.05
19	2	j	15805	0.05
20	1	A	15486	0.07
20	2	l	15486	0.07
21	1	A	15818	0.05
21	2	r	15818	0.05
22	1	A	15492	0.07
22	2	t	15492	0.07
23	1	D	5499	0.08
23	2	K	5499	0.08
24	1	D	5856	0.04
24	2	M	5856	0.04
25	1	D	5457	0.08
25	2	S	5457	0.08
26	1	D	5897	0.04
26	2	U	5897	0.04
27	1	D	5436	0.08
27	2	b	5436	0.08
28	1	D	5647	0.03
28	2	d	5647	0.03
29	1	D	5461	0.08
29	2	k	5461	0.08
30	1	D	5857	0.04
30	2	m	5857	0.04
31	1	D	5469	0.08
31	2	s	5469	0.08
32	1	D	5842	0.04
32	2	u	5842	0.04
33	1	C	15405	0.06
33	2	J	15405	0.06
34	1	C	15810	0.03
34	2	L	15810	0.03
35	1	C	15402	0.06
35	2	R	15402	0.06
36	1	C	15800	0.03
36	2	T	15800	0.03
37	1	C	15453	0.06
37	2	a	15453	0.06
38	1	C	15882	0.03
38	2	c	15882	0.03
39	1	C	15422	0.06
39	2	j	15422	0.06
40	1	C	15859	0.02
40	2	l	15859	0.02
41	1	C	15458	0.06
41	2	r	15458	0.06
42	1	C	15865	0.03
42	2	t	15865	0.03
43	1	E	1323	0.07
43	2	F	1323	0.07
44	1	E	1338	0.07
44	2	N	1338	0.07
45	1	E	1330	0.07
45	2	O	1330	0.07
46	1	E	1238	0.05
46	2	V	1238	0.05
47	1	E	1326	0.1
47	2	W	1326	0.1
48	1	E	1307	0.08
48	2	e	1307	0.08
49	1	E	1243	0.06
49	2	f	1243	0.06
50	1	E	1309	0.1
50	2	n	1309	0.1
51	1	E	1222	0.07
51	2	o	1222	0.07
52	1	E	1321	0.05
52	2	v	1321	0.05
53	1	E	1314	0.08
53	2	w	1314	0.08
54	1	F	1489	0.09
54	2	N	1489	0.09
55	1	F	1525	0.07
55	2	O	1525	0.07
56	1	F	1377	0.1
56	2	V	1377	0.1
57	1	F	1478	0.09
57	2	W	1478	0.09
58	1	F	1425	0.12
58	2	e	1425	0.12
59	1	F	1239	0.07
59	2	f	1239	0.07
60	1	F	1471	0.1
60	2	n	1471	0.1
61	1	F	1321	0.07
61	2	o	1321	0.07
62	1	F	1407	0.07
62	2	v	1407	0.07
63	1	F	1497	0.08
63	2	w	1497	0.08
64	1	K	5583	0.08
64	2	M	5583	0.08
65	1	K	5721	0.05
65	2	S	5721	0.05
66	1	K	5581	0.08
66	2	U	5581	0.08
67	1	K	5699	0.04
67	2	b	5699	0.04
68	1	K	5413	0.08
68	2	d	5413	0.08
69	1	K	5749	0.05
69	2	k	5749	0.05
70	1	K	5565	0.08
70	2	m	5565	0.08
71	1	K	5750	0.04
71	2	s	5750	0.04
72	1	K	5565	0.08
72	2	u	5565	0.08
73	1	J	15616	0.06
73	2	L	15616	0.06
74	1	J	16003	0.04
74	2	R	16003	0.04
75	1	J	15599	0.07
75	2	T	15599	0.07
76	1	J	16007	0.03
76	2	a	16007	0.03
77	1	J	15649	0.07
77	2	c	15649	0.07
78	1	J	16054	0.04
78	2	j	16054	0.04
79	1	J	15668	0.06
79	2	l	15668	0.06
80	1	J	16020	0.04
80	2	r	16020	0.04
81	1	J	15647	0.06
81	2	t	15647	0.06
82	1	M	5472	0.09
82	2	S	5472	0.09
83	1	M	5913	0.04
83	2	U	5913	0.04
84	1	M	5459	0.08
84	2	b	5459	0.08
85	1	M	5663	0.04
85	2	d	5663	0.04
86	1	M	5505	0.09
86	2	k	5505	0.09
87	1	M	5878	0.03
87	2	m	5878	0.03
88	1	M	5479	0.08
88	2	s	5479	0.08
89	1	M	5882	0.04
89	2	u	5882	0.04
90	1	L	15333	0.07
90	2	R	15333	0.07
91	1	L	15748	0.04
91	2	T	15748	0.04
92	1	L	15342	0.06
92	2	a	15342	0.06
93	1	L	15777	0.04
93	2	c	15777	0.04
94	1	L	15330	0.07
94	2	j	15330	0.07
95	1	L	15770	0.04
95	2	l	15770	0.04
96	1	L	15429	0.06
96	2	r	15429	0.06
97	1	L	15804	0.04
97	2	t	15804	0.04
98	1	N	1343	0.07
98	2	O	1343	0.07
99	1	N	1236	0.07
99	2	V	1236	0.07
100	1	N	1328	0.09
100	2	W	1328	0.09
101	1	N	1317	0.09
101	2	e	1317	0.09
102	1	N	1240	0.06
102	2	f	1240	0.06
103	1	N	1339	0.1
103	2	n	1339	0.1
104	1	N	1228	0.06
104	2	o	1228	0.06
105	1	N	1323	0.06
105	2	v	1323	0.06
106	1	N	1310	0.07
106	2	w	1310	0.07
107	1	O	1378	0.1
107	2	V	1378	0.1
108	1	O	1480	0.08
108	2	W	1480	0.08
109	1	O	1434	0.11
109	2	e	1434	0.11
110	1	O	1242	0.06
110	2	f	1242	0.06
111	1	O	1487	0.09
111	2	n	1487	0.09
112	1	O	1335	0.06
112	2	o	1335	0.06
113	1	O	1407	0.07
113	2	v	1407	0.07
114	1	O	1497	0.08
114	2	w	1497	0.08
115	1	S	5587	0.08
115	2	U	5587	0.08
116	1	S	5784	0.04
116	2	b	5784	0.04
117	1	S	5424	0.08
117	2	d	5424	0.08
118	1	S	5767	0.03
118	2	k	5767	0.03
119	1	S	5577	0.08
119	2	m	5577	0.08
120	1	S	5784	0.03
120	2	s	5784	0.03
121	1	S	5571	0.08
121	2	u	5571	0.08
122	1	R	15517	0.07
122	2	T	15517	0.07
123	1	R	15895	0.04
123	2	a	15895	0.04
124	1	R	15554	0.07
124	2	c	15554	0.07
125	1	R	15912	0.05
125	2	j	15912	0.05
126	1	R	15604	0.06
126	2	l	15604	0.06
127	1	R	15911	0.05
127	2	r	15911	0.05
128	1	R	15537	0.07
128	2	t	15537	0.07
129	1	U	5472	0.08
129	2	b	5472	0.08
130	1	U	5683	0.03
130	2	d	5683	0.03
131	1	U	5492	0.08
131	2	k	5492	0.08
132	1	U	5932	0.03
132	2	m	5932	0.03
133	1	U	5497	0.08
133	2	s	5497	0.08
134	1	U	5925	0.03
134	2	u	5925	0.03
135	1	T	15347	0.06
135	2	a	15347	0.06
136	1	T	15807	0.04
136	2	c	15807	0.04
137	1	T	15363	0.07
137	2	j	15363	0.07
138	1	T	15810	0.04
138	2	l	15810	0.04
139	1	T	15397	0.07
139	2	r	15397	0.07
140	1	T	15873	0.03
140	2	t	15873	0.03
141	1	V	1375	0.1
141	2	W	1375	0.1
142	1	V	1334	0.09
142	2	e	1334	0.09
143	1	V	1225	0.06
143	2	f	1225	0.06
144	1	V	1366	0.1
144	2	n	1366	0.1
145	1	V	1304	0.08
145	2	o	1304	0.08
146	1	V	1319	0.08
146	2	v	1319	0.08
147	1	V	1368	0.1
147	2	w	1368	0.1
148	1	W	1425	0.12
148	2	e	1425	0.12
149	1	W	1225	0.06
149	2	f	1225	0.06
150	1	W	1469	0.1
150	2	n	1469	0.1
151	1	W	1322	0.06
151	2	o	1322	0.06
152	1	W	1404	0.08
152	2	v	1404	0.08
153	1	W	1486	0.11
153	2	w	1486	0.11
154	1	b	5406	0.08
154	2	d	5406	0.08
155	1	b	5714	0.03
155	2	k	5714	0.03
156	1	b	5552	0.08
156	2	m	5552	0.08
157	1	b	5730	0.02
157	2	s	5730	0.02
158	1	b	5542	0.07
158	2	u	5542	0.07
159	1	a	15546	0.06
159	2	c	15546	0.06
160	1	a	15917	0.04
160	2	j	15917	0.04
161	1	a	15559	0.06
161	2	l	15559	0.06
162	1	a	15927	0.04
162	2	r	15927	0.04
163	1	a	15536	0.06
163	2	t	15536	0.06
164	1	d	5284	0.08
164	2	k	5284	0.08
165	1	d	5640	0.03
165	2	m	5640	0.03
166	1	d	5310	0.08
166	2	s	5310	0.08
167	1	d	5650	0.03
167	2	u	5650	0.03
168	1	c	15392	0.07
168	2	j	15392	0.07
169	1	c	15827	0.03
169	2	l	15827	0.03
170	1	c	15439	0.07
170	2	r	15439	0.07
171	1	c	15852	0.03
171	2	t	15852	0.03
172	1	e	1211	0.07
172	2	f	1211	0.07
173	1	e	1414	0.12
173	2	n	1414	0.12
174	1	e	1304	0.09
174	2	o	1304	0.09
175	1	e	1368	0.1
175	2	v	1368	0.1
176	1	e	1407	0.11
176	2	w	1407	0.11
177	1	f	1214	0.08
177	2	n	1214	0.08
178	1	f	1219	0.07
178	2	o	1219	0.07
179	1	f	1225	0.05
179	2	v	1225	0.05
180	1	f	1221	0.07
180	2	w	1221	0.07
181	1	k	5538	0.08
181	2	m	5538	0.08
182	1	k	5755	0.03
182	2	s	5755	0.03
183	1	k	5512	0.08
183	2	u	5512	0.08
184	1	j	15624	0.06
184	2	l	15624	0.06
185	1	j	15967	0.05
185	2	r	15967	0.05
186	1	j	15590	0.06
186	2	t	15590	0.06
187	1	m	5424	0.08
187	2	s	5424	0.08
188	1	m	5830	0.03
188	2	u	5830	0.03
189	1	l	15376	0.07
189	2	r	15376	0.07
190	1	l	15794	0.03
190	2	t	15794	0.03
191	1	n	1321	0.08
191	2	o	1321	0.08
192	1	n	1391	0.09
192	2	v	1391	0.09
193	1	n	1442	0.1
193	2	w	1442	0.1
194	1	o	1310	0.08
194	2	v	1310	0.08
195	1	o	1313	0.08
195	2	w	1313	0.08
196	1	s	5531	0.08
196	2	u	5531	0.08
197	1	r	15696	0.07
197	2	t	15696	0.07
198	1	v	1394	0.08
198	2	w	1394	0.08

LS refinement shell

Resolution: 3.39→3.478 Å / Total num. of bins used: 20

	Rfactor	Num. reflection	% reflection
Rfree	0.276	451	-
Rwork	0.209	8831	-
obs	-	-	74.07 %