PDB-8bvm: Cryo-EM structure of Hfq-Crc-rbsB translation repression complex

Basic information

• Entry: Database: PDB / ID: 8bvm
• Title: Cryo-EM structure of Hfq-Crc-rbsB translation repression complex

Components

• Catabolite repression control protein
• RNA-binding protein Hfq
• rbsB mRNA

• Keywords: RNA BINDING PROTEIN / co-transcriptional RNA folding / Crc / metabolic regulation / ribonucleoprotein assembly / RNA chaperone Hfq / translational regulation

Function / homology

Function:

double-stranded DNA 3'-5' DNA exonuclease activity / exodeoxyribonuclease III / DNA repair / regulation of DNA-templated transcription / RNA binding / metal ion binding

Domain/homology:

Exodeoxyribonuclease III-like / RNA-binding protein Hfq / Hfq protein / AP endonuclease 1 / AP endonucleases family 1 profile. / Endonuclease/exonuclease/phosphatase / Endonuclease/Exonuclease/phosphatase family / : / Sm domain profile. / Endonuclease/exonuclease/phosphatase superfamily / LSM domain superfamily

Component:

RNA / RNA (> 10) / RNA (> 100) / RNA-binding protein Hfq / Catabolite repression control protein

• Biological species: Pseudomonas aeruginosa (bacteria)
• Method: ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.8 Å
• Authors: Dendooven, T. / Luisi, B.F.

Funding support

United Kingdom, 1items

Organization	Grant number	Country
Wellcome Trust		United Kingdom

• Citation: Journal: EMBO J / Year: 2023; Title: Translational regulation by Hfq-Crc assemblies emerges from polymorphic ribonucleoprotein folding.; Authors: Tom Dendooven / Elisabeth Sonnleitner / Udo Bläsi / Ben F Luisi / ; Abstract: The widely occurring bacterial RNA chaperone Hfq is a key factor in the post-transcriptional control of hundreds of genes in Pseudomonas aeruginosa. How this broadly acting protein can contribute to the regulatory requirements of many different genes remains puzzling. Here, we describe cryo-EM structures of higher order assemblies formed by Hfq and its partner protein Crc on control regions of different P. aeruginosa target mRNAs. Our results show that these assemblies have mRNA-specific quaternary architectures resulting from the combination of multivalent protein-protein interfaces and recognition of patterns in the RNA sequence. The structural polymorphism of these ribonucleoprotein assemblies enables selective translational repression of many different target mRNAs. This system elucidates how highly complex regulatory pathways can evolve with a minimal economy of proteinogenic components in combination with RNA sequence and fold.

History

Deposition	Dec 4, 2022	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Jan 25, 2023	Provider: repository / Type: Initial release
Revision 1.1	Feb 8, 2023	Group: Database references / Category: citation / Item: _citation.journal_volume / _citation.year

Assembly

Deposited unit

A: Catabolite repression control protein

B: RNA-binding protein Hfq

C: RNA-binding protein Hfq

D: RNA-binding protein Hfq

E: RNA-binding protein Hfq

F: RNA-binding protein Hfq

G: RNA-binding protein Hfq

H: Catabolite repression control protein

I: RNA-binding protein Hfq

J: RNA-binding protein Hfq

K: RNA-binding protein Hfq

L: RNA-binding protein Hfq

M: RNA-binding protein Hfq

N: Catabolite repression control protein

O: RNA-binding protein Hfq

u: rbsB mRNA

Summary:

• 235 kDa, 16 polymers

Component details:

	Theoretical mass	Number of molelcules
Total (without water)	234,530	16
Polymers	234,530	16
Non-polymers	0	0
Water	0

1

Summary:

• Idetical with deposited unit
• defined by author&software
• Evidence: electron microscopy

Symmetry operations:

Type	Name	Symmetry operation	Number
identity operation	1_555		1

Calculated values:

Buried area	32480 Å2
ΔGint	-182 kcal/mol
Surface area	71750 Å2
Method	PISA

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	A
2	1	H
1	2	A
2	2	N
1	3	B
2	3	C
1	4	B
2	4	D
1	5	B
2	5	E
1	6	B
2	6	F
1	7	B
2	7	G
1	8	B
2	8	I
1	9	B
2	9	J
1	10	B
2	10	K
1	11	B
2	11	L
1	12	B
2	12	M
1	13	B
2	13	O
1	14	C
2	14	D
1	15	C
2	15	E
1	16	C
2	16	F
1	17	C
2	17	G
1	18	C
2	18	I
1	19	C
2	19	J
1	20	C
2	20	K
1	21	C
2	21	L
1	22	C
2	22	M
1	23	C
2	23	O
1	24	D
2	24	E
1	25	D
2	25	F
1	26	D
2	26	G
1	27	D
2	27	I
1	28	D
2	28	J
1	29	D
2	29	K
1	30	D
2	30	L
1	31	D
2	31	M
1	32	D
2	32	O
1	33	E
2	33	F
1	34	E
2	34	G
1	35	E
2	35	I
1	36	E
2	36	J
1	37	E
2	37	K
1	38	E
2	38	L
1	39	E
2	39	M
1	40	E
2	40	O
1	41	F
2	41	G
1	42	F
2	42	I
1	43	F
2	43	J
1	44	F
2	44	K
1	45	F
2	45	L
1	46	F
2	46	M
1	47	F
2	47	O
1	48	G
2	48	I
1	49	G
2	49	J
1	50	G
2	50	K
1	51	G
2	51	L
1	52	G
2	52	M
1	53	G
2	53	O
1	54	H
2	54	N
1	55	I
2	55	J
1	56	I
2	56	K
1	57	I
2	57	L
1	58	I
2	58	M
1	59	I
2	59	O
1	60	J
2	60	K
1	61	J
2	61	L
1	62	J
2	62	M
1	63	J
2	63	O
1	64	K
2	64	L
1	65	K
2	65	M
1	66	K
2	66	O
1	67	L
2	67	M
1	68	L
2	68	O
1	69	M
2	69	O

NCS domain segments:

Dom-ID	Component-ID	Ens-ID	Refine code	Auth asym-ID	Auth seq-ID
1	0	1	0	A	1 - 262
2	0	1	0	H	1 - 262
1	0	2	0	A	1 - 262
2	0	2	0	N	1 - 262
1	0	3	0	B	5 - 68
2	0	3	0	C	5 - 68
1	0	4	0	B	6 - 69
2	0	4	0	D	6 - 69
1	0	5	0	B	5 - 69
2	0	5	0	E	5 - 69
1	0	6	0	B	5 - 70
2	0	6	0	F	5 - 70
1	0	7	0	B	6 - 69
2	0	7	0	G	6 - 69
1	0	8	0	B	5 - 70
2	0	8	0	I	5 - 70
1	0	9	0	B	5 - 68
2	0	9	0	J	5 - 68
1	0	10	0	B	6 - 69
2	0	10	0	K	6 - 69
1	0	11	0	B	5 - 69
2	0	11	0	L	5 - 69
1	0	12	0	B	5 - 70
2	0	12	0	M	5 - 70
1	0	13	0	B	6 - 69
2	0	13	0	O	6 - 69
1	0	14	0	C	6 - 68
2	0	14	0	D	6 - 68
1	0	15	0	C	5 - 68
2	0	15	0	E	5 - 68
1	0	16	0	C	5 - 68
2	0	16	0	F	5 - 68
1	0	17	0	C	6 - 68
2	0	17	0	G	6 - 68
1	0	18	0	C	5 - 68
2	0	18	0	I	5 - 68
1	0	19	0	C	5 - 69
2	0	19	0	J	5 - 69
1	0	20	0	C	6 - 68
2	0	20	0	K	6 - 68
1	0	21	0	C	5 - 68
2	0	21	0	L	5 - 68
1	0	22	0	C	5 - 68
2	0	22	0	M	5 - 68
1	0	23	0	C	6 - 68
2	0	23	0	O	6 - 68
1	0	24	0	D	6 - 70
2	0	24	0	E	6 - 70
1	0	25	0	D	6 - 69
2	0	25	0	F	6 - 69
1	0	26	0	D	6 - 71
2	0	26	0	G	6 - 71
1	0	27	0	D	6 - 69
2	0	27	0	I	6 - 69
1	0	28	0	D	6 - 68
2	0	28	0	J	6 - 68
1	0	29	0	D	6 - 71
2	0	29	0	K	6 - 71
1	0	30	0	D	6 - 70
2	0	30	0	L	6 - 70
1	0	31	0	D	6 - 69
2	0	31	0	M	6 - 69
1	0	32	0	D	6 - 71
2	0	32	0	O	6 - 71
1	0	33	0	E	5 - 69
2	0	33	0	F	5 - 69
1	0	34	0	E	6 - 70
2	0	34	0	G	6 - 70
1	0	35	0	E	5 - 69
2	0	35	0	I	5 - 69
1	0	36	0	E	5 - 68
2	0	36	0	J	5 - 68
1	0	37	0	E	6 - 70
2	0	37	0	K	6 - 70
1	0	38	0	E	3 - 71
2	0	38	0	L	3 - 71
1	0	39	0	E	5 - 69
2	0	39	0	M	5 - 69
1	0	40	0	E	6 - 70
2	0	40	0	O	6 - 70
1	0	41	0	F	6 - 69
2	0	41	0	G	6 - 69
1	0	42	0	F	5 - 70
2	0	42	0	I	5 - 70
1	0	43	0	F	5 - 68
2	0	43	0	J	5 - 68
1	0	44	0	F	6 - 69
2	0	44	0	K	6 - 69
1	0	45	0	F	5 - 69
2	0	45	0	L	5 - 69
1	0	46	0	F	5 - 70
2	0	46	0	M	5 - 70
1	0	47	0	F	6 - 69
2	0	47	0	O	6 - 69
1	0	48	0	G	6 - 69
2	0	48	0	I	6 - 69
1	0	49	0	G	6 - 68
2	0	49	0	J	6 - 68
1	0	50	0	G	6 - 71
2	0	50	0	K	6 - 71
1	0	51	0	G	6 - 70
2	0	51	0	L	6 - 70
1	0	52	0	G	6 - 69
2	0	52	0	M	6 - 69
1	0	53	0	G	6 - 71
2	0	53	0	O	6 - 71
1	0	54	0	H	1 - 262
2	0	54	0	N	1 - 262
1	0	55	0	I	5 - 68
2	0	55	0	J	5 - 68
1	0	56	0	I	6 - 69
2	0	56	0	K	6 - 69
1	0	57	0	I	5 - 69
2	0	57	0	L	5 - 69
1	0	58	0	I	5 - 70
2	0	58	0	M	5 - 70
1	0	59	0	I	6 - 69
2	0	59	0	O	6 - 69
1	0	60	0	J	6 - 68
2	0	60	0	K	6 - 68
1	0	61	0	J	5 - 68
2	0	61	0	L	5 - 68
1	0	62	0	J	5 - 68
2	0	62	0	M	5 - 68
1	0	63	0	J	6 - 68
2	0	63	0	O	6 - 68
1	0	64	0	K	6 - 70
2	0	64	0	L	6 - 70
1	0	65	0	K	6 - 69
2	0	65	0	M	6 - 69
1	0	66	0	K	6 - 71
2	0	66	0	O	6 - 71
1	0	67	0	L	5 - 69
2	0	67	0	M	5 - 69
1	0	68	0	L	6 - 70
2	0	68	0	O	6 - 70
1	0	69	0	M	6 - 69
2	0	69	0	O	6 - 69

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

Components

#1: Protein

A H N Catabolite repression control protein / Exodeoxyribonuclease III

Details:

Mass: 30101.869 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas aeruginosa (bacteria)
Gene: crc, exoA, ALP65_01013, CAZ10_32350, CGU42_22755, DT376_09125, E4V10_18585, E5D53_27785, E5Z62_16095, E5Z63_23405, ECC04_031800, GNQ48_25180, GUL26_21635, IPC111_12165, IPC112_13745, IPC113_22800, IPC114_17225, IPC115_20105, IPC116_23795, IPC117_25625, IPC118_26680, IPC119_29495, IPC120_26430, IPC121_21355, IPC122_22810, IPC123_28525, IPC124_13695, IPC125_17530, IPC126_13890, IPC127_14855, IPC128_10355, IPC1295_10410, IPC129_12605, IPC1306_08360, IPC1307_28280, IPC1308_08250, IPC1309_21675, IPC130_13760, IPC1310_18070, IPC1311_27715, IPC1312_27760, IPC1313_12995, IPC1314_23305, IPC1315_13925, IPC1316_03820, IPC1317_21325, IPC1319_28440, IPC131_02850, IPC1320_21925, IPC1321_13670, IPC1322_08030, IPC1323_08650, IPC1324_08655, IPC1325_28715, IPC1326_03390, IPC1327_03390, IPC1329_17010, IPC132_06970, IPC1330_11465, IPC1331_28200, IPC1332_29425, IPC1333_11845, IPC1334_25345, IPC1335_28860, IPC1336_09225, IPC1337_29545, IPC1339_28790, IPC133_03360, IPC1340_28180, IPC1341_12600, IPC1342_25815, IPC1343_28125, IPC1345_26635, IPC1346_12480, IPC1347_06540, IPC1349_02495, IPC134_02845, IPC135_03360, IPC137_05170, IPC139_09290, IPC140_06730, IPC141_03365, IPC142_07260, IPC143_27785, IPC144_27850, IPC145_26565, IPC146_07875, IPC1474_29365, IPC1476_04745, IPC1477_00205, IPC1478_21530, IPC1479_05830, IPC147_27530, IPC1480_09320, IPC1481_08100, IPC1482_03390, IPC1485_09070, IPC1486_00200, IPC1487_09730, IPC1488_23420, IPC1489_30180, IPC148_13460, IPC1490_30060, IPC1491_03590, IPC1492_29195, IPC1494_10055, IPC1496_07955, IPC1498_13815, IPC1499_04620, IPC149_07870, IPC1500_13950, IPC1501_16685, IPC1502_17430, IPC1503_12005, IPC1504_12415, IPC1505_29825, IPC1506_17410, IPC1507_24155, IPC1508_30170, IPC1509_28695, IPC150_28080, IPC1510_28915, IPC1511_30420, IPC1512_29660, IPC1515_25380, IPC1516_25030, IPC1517_08725, IPC1518_07355, IPC1519_08150, IPC151_23655, IPC1521_08375, IPC1522_08210, IPC1523_29925, IPC152_28760, IPC153_23345, IPC154_17265, IPC155_18160, IPC156_17280, IPC157_20765, IPC1583_04500, IPC1584_21700, IPC1585_03355, IPC1586_12135, IPC1587_07630, IPC1588_00205, IPC1589_12850, IPC158_22475, IPC1590_04505, IPC1591_26650, IPC1592_03360, IPC1593_28620, IPC1594_08340, IPC1595_28610, IPC1596_08050, IPC1597_07705, IPC1598_07535, IPC1599_12520, IPC159_19675, IPC1600_03625, IPC1601_25405, IPC1602_28860, IPC1603_04480, IPC1604_17280, IPC1605_06980, IPC1606_28085, IPC161_21475, IPC168_27215, IPC172_03365, IPC173_03365, IPC174_04115, IPC175_27990, IPC176_00200, IPC177_23820, IPC178_12645, IPC179_03225, IPC180_03440, IPC181_03440, IPC182_27410, IPC183_07620, IPC184_23205, IPC26_03230, IPC27_25570, IPC29_25820, IPC30_25775, IPC31_26330, IPC32_23895, IPC33_16805, IPC34_07650, IPC35_07645, IPC36_11985, IPC37_11015, IPC38_07925, IPC40_27470, IPC41_03360, IPC42_03360, IPC43_23085, IPC44_22815, IPC45_21905, IPC46_07155, IPC47_03385, IPC48_27355, IPC49_03360, IPC50_30570, IPC51_28835, IPC54_18710, IPC55_30750, IPC56_25845, IPC574_05650, IPC575_13820, IPC576_07870, IPC577_30530, IPC578_05650, IPC579_06085, IPC57_11625, IPC580_13610, IPC582_05645, IPC584_14310, IPC586_05655, IPC589_14875, IPC58_27585, IPC596_07850, IPC597_03535, IPC598_09625, IPC599_08585, IPC59_11860, IPC600_09330, IPC601_08240, IPC602_08660, IPC603_03370, IPC604_03350, IPC605_03350, IPC606_24980, IPC607_31450, IPC608_28595, IPC609_14300, IPC60_11070, IPC610_25045, IPC611_03630, IPC612_03625, IPC613_03625, IPC614_10255, IPC615_03650, IPC616_03650, IPC618_03645, IPC61_27990, IPC620_03665, IPC621_02265, IPC622_09600, IPC623_28715, IPC624_03390, IPC625_10215, IPC627_06380, IPC629_12080, IPC630_04660, IPC632_00200, IPC633_27305, IPC634_00200, IPC64_27165, IPC65_28585, IPC66_27855, IPC67_03650, IPC68_03420, IPC70_17275, IPC71_27005, IPC737_07685, IPC73_27875, IPC74_28395, IPC75_18330, IPC76_17335, IPC77_23945, IPC78_12120, NCTC13621_05232, PA52Ts2_6132, PAMH19_3299
Production host: Pseudomonas aeruginosa (bacteria) / References: UniProt: Q51380, exodeoxyribonuclease III

#2: Protein

B C D E F G I J K L M O
RNA-binding protein Hfq

Details:

Mass: 9114.487 Da / Num. of mol.: 12
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas aeruginosa (bacteria) / Gene: hfq, PSPA7_5673 / Production host: Escherichia coli (E. coli) / References: UniProt: A6VD57

#3: RNA chain

u rbsB mRNA

Details:

Mass: 34850.766 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Pseudomonas aeruginosa (bacteria)

Experimental details

Experiment

• Experiment: Method: ELECTRON MICROSCOPY
• EM experiment: Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

Sample preparation

Component

ID	Name	Type	Entity ID	Parent-ID	Source
1	Complex of the RNA chaperone Hfq and helper protein Crc assembled on a rbsB mRNA fragment	COMPLEX	all	0	RECOMBINANT
2	Catabolite repression control protein	COMPLEX	#1	1	RECOMBINANT
3	rbsB mRNA	COMPLEX	#3	1	RECOMBINANT
4	RNA-binding protein Hfq	COMPLEX	#2	1	RECOMBINANT

• Molecular weight: Value: 0.180 MDa / Experimental value: NO

Source (natural)

ID	Entity assembly-ID	Organism	Ncbi tax-ID
2	2	Pseudomonas aeruginosa (bacteria)	287
3	3	Pseudomonas aeruginosa (bacteria)	287
4	4	Pseudomonas aeruginosa (bacteria)	287

Source (recombinant)

ID	Entity assembly-ID	Organism	Ncbi tax-ID
2	2	Pseudomonas aeruginosa (bacteria)	287
3	3	Synthetic construct (others)	32630
4	4	Escherichia coli (E. coli)	562

• Buffer solution: pH: 7.5
• Specimen: Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
• Specimen support: Grid material: COPPER / Grid type: Quantifoil R1.2/1.3
• Vitrification: Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K

Electron microscopy imaging

• Experimental equipment: Model: Titan Krios / Image courtesy: FEI Company
• Microscopy: Model: FEI TITAN KRIOS
• Electron gun: Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: SPOT SCAN
• Electron lens: Mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2600 nm / Nominal defocus min: 1000 nm
• Image recording: Electron dose: 50 e/Ų / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k)

Processing

• Software: Name: PHENIX / Version: 1.18rc5_3822: / Classification: refinement

EM software

ID	Name	Version	Category
2	EPU		image acquisition
4	CTFFIND	4.1	CTF correction
7	UCSF Chimera	1.13.1	model fitting
9	cryoSPARC	2.15	initial Euler assignment
10	cryoSPARC	2.15	final Euler assignment
12	cryoSPARC	2.15	3D reconstruction
13	REFMAC		model refinement
14	PHENIX		model refinement

• CTF correction: Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
• 3D reconstruction: Resolution: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 148700 / Symmetry type: POINT
• Atomic model building: Protocol: RIGID BODY FIT

Refinement

Resolution: 3.6→240.7 Å / Cor.coef. F_o:F_c: 0.915 / SU B: 17.532 / SU ML: 0.247 / ESU R: 0.264
Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

	Rfactor	Num. reflection	% reflection
Rwork	0.39935	-	-
obs	0.39935	471805	100 %

• Solvent computation: Solvent model: PARAMETERS FOR MASK CACLULATION

Displacement parameters

B_iso mean: 251.902 Ų

	Baniso -1	Baniso -2	Baniso -3
1-	11.97 Å2	3.08 Å2	-5.64 Å2
2-	-	-5.23 Å2	-1.64 Å2
3-	-	-	-6.73 Å2

• Refinement step: Cycle: 1 / Total: 14008

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
ELECTRON MICROSCOPY	f_bond_d	0.001	14342
ELECTRON MICROSCOPY	f_angle_d	0.38	19692
ELECTRON MICROSCOPY	f_dihedral_angle_d	15.142	2352
ELECTRON MICROSCOPY	f_chiral_restr	0.04	2226
ELECTRON MICROSCOPY	f_plane_restr	0.003	2351

Refine LS restraints NCS

Refine-ID: ELECTRON MICROSCOPY / Type: interatomic distance / Weight position: 0.05

Ens-ID	Dom-ID	Auth asym-ID	Number	Rms dev position (Å)
1	1	A	17576	0.09
1	2	H	17576	0.09
2	1	A	17432	0.09
2	2	N	17432	0.09
3	1	B	3640	0.14
3	2	C	3640	0.14
4	1	B	3628	0.13
4	2	D	3628	0.13
5	1	B	3684	0.12
5	2	E	3684	0.12
6	1	B	3754	0.13
6	2	F	3754	0.13
7	1	B	3656	0.13
7	2	G	3656	0.13
8	1	B	3894	0.08
8	2	I	3894	0.08
9	1	B	3686	0.12
9	2	J	3686	0.12
10	1	B	3616	0.12
10	2	K	3616	0.12
11	1	B	3688	0.11
11	2	L	3688	0.11
12	1	B	3722	0.14
12	2	M	3722	0.14
13	1	B	3668	0.13
13	2	O	3668	0.13
14	1	C	3526	0.14
14	2	D	3526	0.14
15	1	C	3532	0.15
15	2	E	3532	0.15
16	1	C	3656	0.12
16	2	F	3656	0.12
17	1	C	3526	0.15
17	2	G	3526	0.15
18	1	C	3616	0.14
18	2	I	3616	0.14
19	1	C	3786	0.1
19	2	J	3786	0.1
20	1	C	3504	0.14
20	2	K	3504	0.14
21	1	C	3550	0.14
21	2	L	3550	0.14
22	1	C	3612	0.13
22	2	M	3612	0.13
23	1	C	3546	0.15
23	2	O	3546	0.15
24	1	D	3684	0.11
24	2	E	3684	0.11
25	1	D	3624	0.12
25	2	F	3624	0.12
26	1	D	3810	0.12
26	2	G	3810	0.12
27	1	D	3658	0.12
27	2	I	3658	0.12
28	1	D	3548	0.13
28	2	J	3548	0.13
29	1	D	3846	0.08
29	2	K	3846	0.08
30	1	D	3688	0.1
30	2	L	3688	0.1
31	1	D	3588	0.13
31	2	M	3588	0.13
32	1	D	3758	0.12
32	2	O	3758	0.12
33	1	E	3704	0.12
33	2	F	3704	0.12
34	1	E	3692	0.13
34	2	G	3692	0.13
35	1	E	3716	0.12
35	2	I	3716	0.12
36	1	E	3586	0.14
36	2	J	3586	0.14
37	1	E	3692	0.11
37	2	K	3692	0.11
38	1	E	3934	0.09
38	2	L	3934	0.09
39	1	E	3652	0.13
39	2	M	3652	0.13
40	1	E	3702	0.13
40	2	O	3702	0.13
41	1	F	3676	0.13
41	2	G	3676	0.13
42	1	F	3792	0.12
42	2	I	3792	0.12
43	1	F	3694	0.1
43	2	J	3694	0.1
44	1	F	3624	0.12
44	2	K	3624	0.12
45	1	F	3712	0.11
45	2	L	3712	0.11
46	1	F	3848	0.08
46	2	M	3848	0.08
47	1	F	3664	0.12
47	2	O	3664	0.12
48	1	G	3706	0.12
48	2	I	3706	0.12
49	1	G	3574	0.14
49	2	J	3574	0.14
50	1	G	3796	0.12
50	2	K	3796	0.12
51	1	G	3698	0.12
51	2	L	3698	0.12
52	1	G	3632	0.14
52	2	M	3632	0.14
53	1	G	3874	0.08
53	2	O	3874	0.08
54	1	H	17746	0.09
54	2	N	17746	0.09
55	1	I	3686	0.12
55	2	J	3686	0.12
56	1	I	3654	0.12
56	2	K	3654	0.12
57	1	I	3722	0.11
57	2	L	3722	0.11
58	1	I	3732	0.14
58	2	M	3732	0.14
59	1	I	3696	0.12
59	2	O	3696	0.12
60	1	J	3542	0.13
60	2	K	3542	0.13
61	1	J	3616	0.13
61	2	L	3616	0.13
62	1	J	3682	0.11
62	2	M	3682	0.11
63	1	J	3564	0.13
63	2	O	3564	0.13
64	1	K	3704	0.1
64	2	L	3704	0.1
65	1	K	3582	0.13
65	2	M	3582	0.13
66	1	K	3766	0.12
66	2	O	3766	0.12
67	1	L	3658	0.12
67	2	M	3658	0.12
68	1	L	3702	0.12
68	2	O	3702	0.12
69	1	M	3622	0.14
69	2	O	3622	0.14

LS refinement shell

Resolution: 3.6→3.693 Å / Total num. of bins used: 20

	Rfactor	Num. reflection	% reflection
Rfree	0	0	-
Rwork	1.883	34782	-
obs	-	-	100 %