PDB-2y26: Transmission defective mutant of Grapevine Fanleaf virus

ID or keywords:

Entry

Database: PDB / ID: 2y26

Title

Transmission defective mutant of Grapevine Fanleaf virus

Components

COAT PROTEIN

Keywords

VIRUS / GFLV / FANLEAF DISEASE

Function / homology

Function and homology information

transport of virus in host, cell to cell / host cell plasmodesma /

viral capsid / host cell cytoplasm / host cell nucleus / structural molecule activity
Similarity search - Function

Biological species

GRAPEVINE FANLEAF VIRUS

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.7 Å

Authors

Schellenberger, P. / Sauter, C. / Lorber, B. / Bron, P. / Trapani, S. / Bergdoll, M. / Marmonier, A. / Schmitt-Keichinger, C. / Lemaire, O. / Demangeat, G. / Ritzenthaler, C.

Citation

Journal: Plos Pathog. / Year: 2011
Title: Structural Insights Into Viral Determinants of Nematode Mediated Grapevine Fanleaf Virus Transmission.
Authors: Schellenberger, P. / Sauter, C. / Lorber, B. / Bron, P. / Trapani, S. / Bergdoll, M. / Marmonier, A. / Schmitt-Keichinger, C. / Lemaire, O. / Demangeat, G. / Ritzenthaler, C.

History

Deposition	Dec 13, 2010	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Jun 8, 2011	Provider: repository / Type: Initial release
Revision 1.1	Dec 28, 2011	Group: Database references / Refinement description / Version format compliance
Revision 1.2	Oct 22, 2014	Group: Atomic model / Database references / Other
Revision 1.3	Mar 6, 2019	Group: Data collection / Experimental preparation / Other Category: exptl_crystal_grow / pdbx_database_proc / pdbx_database_status Item: _exptl_crystal_grow.temp / _pdbx_database_status.recvd_author_approval
Revision 1.4	May 8, 2019	Group: Data collection / Experimental preparation / Category: exptl_crystal_grow / Item: _exptl_crystal_grow.method

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	2y26.cif.gz	1.8 MB	Display	PDBx/mmCIF format
PDB format	pdb2y26.ent.gz	1.6 MB	Display	PDB format
PDBx/mmJSON format	2y26.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/y2/2y26 ftp://data.pdbj.org/pub/pdb/validation_reports/y2/2y26	HTTPS FTP

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Related structure data

Related structure data	4v5tC C: citing same article (ref.)
Similar structure data	4v5w-d 6sco-1 3dpr-1 2izw-1 4v5t-d 6jjc-1 1ng0-1 7c9y-1 3855 4q4x-1 Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search

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Links

PDB pages	PDBj / wwPDB / NCBI

Deposited unit

A: COAT PROTEIN

B: COAT PROTEIN

C: COAT PROTEIN

D: COAT PROTEIN

E: COAT PROTEIN

F: COAT PROTEIN

G: COAT PROTEIN

H: COAT PROTEIN

I: COAT PROTEIN

J: COAT PROTEIN

K: COAT PROTEIN

L: COAT PROTEIN

M: COAT PROTEIN

N: COAT PROTEIN

O: COAT PROTEIN

P: COAT PROTEIN

Q: COAT PROTEIN

R: COAT PROTEIN

S: COAT PROTEIN

T: COAT PROTEIN

1.12 MDa, 20 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: COAT PROTEIN

B: COAT PROTEIN

C: COAT PROTEIN

D: COAT PROTEIN

E: COAT PROTEIN

F: COAT PROTEIN

G: COAT PROTEIN

H: COAT PROTEIN

I: COAT PROTEIN

J: COAT PROTEIN

K: COAT PROTEIN

L: COAT PROTEIN

M: COAT PROTEIN

N: COAT PROTEIN

O: COAT PROTEIN

P: COAT PROTEIN

Q: COAT PROTEIN

R: COAT PROTEIN

S: COAT PROTEIN

T: COAT PROTEIN

A: COAT PROTEIN

B: COAT PROTEIN

C: COAT PROTEIN

D: COAT PROTEIN

E: COAT PROTEIN

F: COAT PROTEIN

G: COAT PROTEIN

H: COAT PROTEIN

I: COAT PROTEIN

J: COAT PROTEIN

K: COAT PROTEIN

L: COAT PROTEIN

M: COAT PROTEIN

N: COAT PROTEIN

O: COAT PROTEIN

P: COAT PROTEIN

Q: COAT PROTEIN

R: COAT PROTEIN

S: COAT PROTEIN

T: COAT PROTEIN

A: COAT PROTEIN

B: COAT PROTEIN

C: COAT PROTEIN

D: COAT PROTEIN

E: COAT PROTEIN

F: COAT PROTEIN

G: COAT PROTEIN

H: COAT PROTEIN

I: COAT PROTEIN

J: COAT PROTEIN

K: COAT PROTEIN

L: COAT PROTEIN

M: COAT PROTEIN

N: COAT PROTEIN

O: COAT PROTEIN

P: COAT PROTEIN

Q: COAT PROTEIN

R: COAT PROTEIN

S: COAT PROTEIN

T: COAT PROTEIN

complete point assembly
60-MERIC
3.37 MDa, 60 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

Idetical with deposited unit in distinct coordinate
point asymmetric unit

3

Idetical with deposited unit in distinct coordinate
point asymmetric unit, std point frame

Unit cell

Length a, b, c (Å)	408.000, 408.000, 408.000
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	198
Space group name H-M	P2₁3

Symmetry

Point symmetry: (Schoenflies symbol: C (n fold cyclic

))

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Dom-ID	Component-ID	Ens-ID	Selection details
1	1	1	CHAIN A AND (RESSEQ 1:8 )
2	1	1	CHAIN B AND (RESSEQ 1:8 )
3	1	1	CHAIN C AND (RESSEQ 1:8 )
4	1	1	CHAIN D AND (RESSEQ 1:8 )
5	1	1	CHAIN E AND (RESSEQ 1:8 )
6	1	1	CHAIN F AND (RESSEQ 1:8 )
7	1	1	CHAIN G AND (RESSEQ 1:8 )
8	1	1	CHAIN H AND (RESSEQ 1:8 )
9	1	1	CHAIN I AND (RESSEQ 1:8 )
10	1	1	CHAIN J AND (RESSEQ 1:8 )
11	1	1	CHAIN K AND (RESSEQ 1:8 )
12	1	1	CHAIN L AND (RESSEQ 1:8 )
13	1	1	CHAIN M AND (RESSEQ 1:8 )
14	1	1	CHAIN N AND (RESSEQ 1:8 )
15	1	1	CHAIN O AND (RESSEQ 1:8 )
16	1	1	CHAIN P AND (RESSEQ 1:8 )
17	1	1	CHAIN Q AND (RESSEQ 1:8 )
18	1	1	CHAIN R AND (RESSEQ 1:8 )
19	1	1	CHAIN S AND (RESSEQ 1:8 )
20	1	1	CHAIN T AND (RESSEQ 1:8 )
1	1	2	CHAIN A AND (RESSEQ 10:14 )
2	1	2	CHAIN B AND (RESSEQ 10:14 )
3	1	2	CHAIN C AND (RESSEQ 10:14 )
4	1	2	CHAIN D AND (RESSEQ 10:14 )
5	1	2	CHAIN E AND (RESSEQ 10:14 )
6	1	2	CHAIN F AND (RESSEQ 10:14 )
7	1	2	CHAIN G AND (RESSEQ 10:14 )
8	1	2	CHAIN H AND (RESSEQ 10:14 )
9	1	2	CHAIN I AND (RESSEQ 10:14 )
10	1	2	CHAIN J AND (RESSEQ 10:14 )
11	1	2	CHAIN K AND (RESSEQ 10:14 )
12	1	2	CHAIN L AND (RESSEQ 10:14 )
13	1	2	CHAIN M AND (RESSEQ 10:14 )
14	1	2	CHAIN N AND (RESSEQ 10:14 )
15	1	2	CHAIN O AND (RESSEQ 10:14 )
16	1	2	CHAIN P AND (RESSEQ 10:14 )
17	1	2	CHAIN Q AND (RESSEQ 10:14 )
18	1	2	CHAIN R AND (RESSEQ 10:14 )
19	1	2	CHAIN S AND (RESSEQ 10:14 )
20	1	2	CHAIN T AND (RESSEQ 10:14 )
1	1	3	CHAIN A AND (RESSEQ 20:258 )
2	1	3	CHAIN B AND (RESSEQ 20:258 )
3	1	3	CHAIN C AND (RESSEQ 20:258 )
4	1	3	CHAIN D AND (RESSEQ 20:258 )
5	1	3	CHAIN E AND (RESSEQ 20:258 )
6	1	3	CHAIN F AND (RESSEQ 20:258 )
7	1	3	CHAIN G AND (RESSEQ 20:258 )
8	1	3	CHAIN H AND (RESSEQ 20:258 )
9	1	3	CHAIN I AND (RESSEQ 20:258 )
10	1	3	CHAIN J AND (RESSEQ 20:258 )
11	1	3	CHAIN K AND (RESSEQ 20:258 )
12	1	3	CHAIN L AND (RESSEQ 20:258 )
13	1	3	CHAIN M AND (RESSEQ 20:258 )
14	1	3	CHAIN N AND (RESSEQ 20:258 )
15	1	3	CHAIN O AND (RESSEQ 20:258 )
16	1	3	CHAIN P AND (RESSEQ 20:258 )
17	1	3	CHAIN Q AND (RESSEQ 20:258 )
18	1	3	CHAIN R AND (RESSEQ 20:258 )
19	1	3	CHAIN S AND (RESSEQ 20:258 )
20	1	3	CHAIN T AND (RESSEQ 20:258 )
1	1	4	CHAIN A AND (RESSEQ 266:504 )
2	1	4	CHAIN B AND (RESSEQ 266:504 )
3	1	4	CHAIN C AND (RESSEQ 266:504 )
4	1	4	CHAIN D AND (RESSEQ 266:504 )
5	1	4	CHAIN E AND (RESSEQ 266:504 )
6	1	4	CHAIN F AND (RESSEQ 266:504 )
7	1	4	CHAIN G AND (RESSEQ 266:504 )
8	1	4	CHAIN H AND (RESSEQ 266:504 )
9	1	4	CHAIN I AND (RESSEQ 266:504 )
10	1	4	CHAIN J AND (RESSEQ 266:504 )
11	1	4	CHAIN K AND (RESSEQ 266:504 )
12	1	4	CHAIN L AND (RESSEQ 266:504 )
13	1	4	CHAIN M AND (RESSEQ 266:504 )
14	1	4	CHAIN N AND (RESSEQ 266:504 )
15	1	4	CHAIN O AND (RESSEQ 266:504 )
16	1	4	CHAIN P AND (RESSEQ 266:504 )
17	1	4	CHAIN Q AND (RESSEQ 266:504 )
18	1	4	CHAIN R AND (RESSEQ 266:504 )
19	1	4	CHAIN S AND (RESSEQ 266:504 )
20	1	4	CHAIN T AND (RESSEQ 266:504 )

NCS ensembles :

ID
1
2
3
4

#1: Protein	COAT PROTEIN / 2C-CP / RNA2 POLYPROTEIN CHAIN 3 Mass: 56131.176 Da / Num. of mol.: 20 / Mutation: YES / Source method: isolated from a natural source / Source: (natural) GRAPEVINE FANLEAF VIRUS / Strain: GFLV-TD / References: UniProt: P18474
#2: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 556 / Source method: isolated from a natural source / Formula: H₂O
Compound details	NATURAL MUTATION IN CHAIN A, GLY 902 TO ASP NATURAL MUTATION IN CHAIN B, GLY 902 TO ASP NATURAL ...NATURAL MUTATION IN CHAIN A, GLY 902 TO ASP NATURAL MUTATION IN CHAIN B, GLY 902 TO ASP NATURAL MUTATION IN CHAIN C, GLY 902 TO ASP NATURAL MUTATION IN CHAIN D, GLY 902 TO ASP NATURAL MUTATION IN CHAIN E, GLY 902 TO ASP NATURAL MUTATION IN CHAIN F, GLY 902 TO ASP NATURAL MUTATION IN CHAIN G, GLY 902 TO ASP NATURAL MUTATION IN CHAIN H, GLY 902 TO ASP NATURAL MUTATION IN CHAIN I, GLY 902 TO ASP NATURAL MUTATION IN CHAIN J, GLY 902 TO ASP NATURAL MUTATION IN CHAIN K, GLY 902 TO ASP NATURAL MUTATION IN CHAIN L, GLY 902 TO ASP NATURAL MUTATION IN CHAIN M, GLY 902 TO ASP NATURAL MUTATION IN CHAIN N, GLY 902 TO ASP NATURAL MUTATION IN CHAIN O, GLY 902 TO ASP NATURAL MUTATION IN CHAIN P, GLY 902 TO ASP NATURAL MUTATION IN CHAIN Q, GLY 902 TO ASP NATURAL MUTATION IN CHAIN R, GLY 902 TO ASP NATURAL MUTATION IN CHAIN S, GLY 902 TO ASP NATURAL MUTATION IN CHAIN T, GLY 902 TO ASP
Sequence details	RESIDUES 606 TO 1109 OF RNA2 POLYPROTEIN WITH A MUTATION AT POSITION 902 (G297D VARIANT OF THE COAT PROTEIN)

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 5 Å³/Da / Density % sol: 75 % Description: THE PROTEIN CONTENT OF THIS CRYSTAL WAS 0.25 OF THE UNIT CELL WHICH CORRESPONDS TO A VM OF 5. WHEN THE VIRAL CAVITY THAT CONTAINS THE GENOMIC RNA IS EXCLUDED, THE ACTUAL FRACTION OF UNIT ...Description: THE PROTEIN CONTENT OF THIS CRYSTAL WAS 0.25 OF THE UNIT CELL WHICH CORRESPONDS TO A VM OF 5. WHEN THE VIRAL CAVITY THAT CONTAINS THE GENOMIC RNA IS EXCLUDED, THE ACTUAL FRACTION OF UNIT CELL OCCUPIED BY SOLVENT IS ABOUT 0.25.
Crystal grow	Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: LARGE CRYSTALS OF GFLV-TD WERE GROWN IN 10 DAYS AT 293K BY VAPOR DIFFUSION (1 MICROLITER SITTING DROPS) WITH A VIRUS SOLUTION AT 4 MG/ML AND A RESERVOIR CONTAINING 7% (M/V) PEG 3350, 0.1 M ...Details: LARGE CRYSTALS OF GFLV-TD WERE GROWN IN 10 DAYS AT 293K BY VAPOR DIFFUSION (1 MICROLITER SITTING DROPS) WITH A VIRUS SOLUTION AT 4 MG/ML AND A RESERVOIR CONTAINING 7% (M/V) PEG 3350, 0.1 M HEPES NA PH 7.5, 0.2 M PROLINE.

Crystal

Density Matthews: 5 Å³/Da / Density % sol: 75 %
Description: THE PROTEIN CONTENT OF THIS CRYSTAL WAS 0.25 OF THE UNIT CELL WHICH CORRESPONDS TO A VM OF 5. WHEN THE VIRAL CAVITY THAT CONTAINS THE GENOMIC RNA IS EXCLUDED, THE ACTUAL FRACTION OF UNIT ...

Crystal grow

Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: LARGE CRYSTALS OF GFLV-TD WERE GROWN IN 10 DAYS AT 293K BY VAPOR DIFFUSION (1 MICROLITER SITTING DROPS) WITH A VIRUS SOLUTION AT 4 MG/ML AND A RESERVOIR CONTAINING 7% (M/V) PEG 3350, 0.1 M ...

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: ESRF / Beamline: BM30A / Wavelength: 0.98
Detector	Type: ADSC QUANTUM 315r / Detector: CCD / Date: Nov 8, 2008
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.98 Å / Relative weight: 1
Reflection	Resolution: 2.7→38 Å / Num. obs: 604343 / % possible obs: 98.9 % / Observed criterion σ(I): 0 / Redundancy: 10.7 % / B_iso Wilson estimate: 44.49 Å² / R_merge(I) obs: 0.13 / Net I/σ(I): 17.25
Reflection shell	Resolution: 2.7→2.77 Å / Redundancy: 3.1 % / R_merge(I) obs: 0.91 / Mean I/σ(I) obs: 1.31 / % possible all: 91.7

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Processing

Software

Name	Version	Classification
PHENIX	(PHENIX.REFINE)	refinement
XDS		data reduction
XSCALE		data scaling
AMoRE		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: EM MAP

Resolution: 2.7→35.784 Å / SU ML: 0.38 / σ(F): 1.34 / Phase error: 21.69 / Stereochemistry target values: ML / Details: NONE

	R_factor	Num. reflection	% reflection
R_free	0.2103	30292	5 %
R_work	0.1925	-	-
obs	0.1934	604343	98.92 %

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / B_sol: 9.702 Å² / k_sol: 0.318 e/Å³

Displacement parameters

B_iso mean: 40.86 Å²

	B_aniso -1	B_aniso -2
1-	0 Å²	0 Å²
2-	-	0 Å²
3-	-	-

Refinement step

Cycle: LAST / Resolution: 2.7→35.784 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	79100	0	0	556	79656

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.009	81237
X-RAY DIFFRACTION	f_angle_d	1.188	110500
X-RAY DIFFRACTION	f_dihedral_angle_d	14.644	28880
X-RAY DIFFRACTION	f_chiral_restr	0.078	12320
X-RAY DIFFRACTION	f_plane_restr	0.005	14040

Refine LS restraints NCS

Ens-ID	Dom-ID	Auth asym-ID	Number	Refine-ID	Type	Rms dev position (Å)
1	1	A	51	X-RAY DIFFRACTION	POSITIONAL
1	2	B	51	X-RAY DIFFRACTION	POSITIONAL	0.033
1	3	C	51	X-RAY DIFFRACTION	POSITIONAL	0.033
1	4	D	51	X-RAY DIFFRACTION	POSITIONAL	0.036
1	5	E	51	X-RAY DIFFRACTION	POSITIONAL	0.037
1	6	F	51	X-RAY DIFFRACTION	POSITIONAL	0.038
1	7	G	51	X-RAY DIFFRACTION	POSITIONAL	0.037
1	8	H	51	X-RAY DIFFRACTION	POSITIONAL	0.031
1	9	I	51	X-RAY DIFFRACTION	POSITIONAL	0.039
1	10	J	51	X-RAY DIFFRACTION	POSITIONAL	0.032
1	11	K	51	X-RAY DIFFRACTION	POSITIONAL	0.035
1	12	L	51	X-RAY DIFFRACTION	POSITIONAL	0.036
1	13	M	51	X-RAY DIFFRACTION	POSITIONAL	0.033
1	14	N	51	X-RAY DIFFRACTION	POSITIONAL	0.065
1	15	O	51	X-RAY DIFFRACTION	POSITIONAL	0.041
1	16	P	51	X-RAY DIFFRACTION	POSITIONAL	0.053
1	17	Q	51	X-RAY DIFFRACTION	POSITIONAL	0.035
1	18	R	51	X-RAY DIFFRACTION	POSITIONAL	0.035
1	19	S	51	X-RAY DIFFRACTION	POSITIONAL	0.037
1	20	T	51	X-RAY DIFFRACTION	POSITIONAL	0.036
2	1	A	38	X-RAY DIFFRACTION	POSITIONAL
2	2	B	38	X-RAY DIFFRACTION	POSITIONAL	0.031
2	3	C	38	X-RAY DIFFRACTION	POSITIONAL	0.033
2	4	D	38	X-RAY DIFFRACTION	POSITIONAL	0.031
2	5	E	38	X-RAY DIFFRACTION	POSITIONAL	0.038
2	6	F	38	X-RAY DIFFRACTION	POSITIONAL	0.028
2	7	G	38	X-RAY DIFFRACTION	POSITIONAL	0.025
2	8	H	38	X-RAY DIFFRACTION	POSITIONAL	0.028
2	9	I	38	X-RAY DIFFRACTION	POSITIONAL	0.034
2	10	J	38	X-RAY DIFFRACTION	POSITIONAL	0.031
2	11	K	38	X-RAY DIFFRACTION	POSITIONAL	0.027
2	12	L	38	X-RAY DIFFRACTION	POSITIONAL	0.036
2	13	M	38	X-RAY DIFFRACTION	POSITIONAL	0.029
2	14	N	38	X-RAY DIFFRACTION	POSITIONAL	0.038
2	15	O	38	X-RAY DIFFRACTION	POSITIONAL	0.035
2	16	P	38	X-RAY DIFFRACTION	POSITIONAL	0.042
2	17	Q	38	X-RAY DIFFRACTION	POSITIONAL	0.032
2	18	R	38	X-RAY DIFFRACTION	POSITIONAL	0.043
2	19	S	38	X-RAY DIFFRACTION	POSITIONAL	0.035
2	20	T	38	X-RAY DIFFRACTION	POSITIONAL	0.03
3	1	A	1869	X-RAY DIFFRACTION	POSITIONAL
3	2	B	1869	X-RAY DIFFRACTION	POSITIONAL	0.115
3	3	C	1869	X-RAY DIFFRACTION	POSITIONAL	0.034
3	4	D	1869	X-RAY DIFFRACTION	POSITIONAL	0.035
3	5	E	1869	X-RAY DIFFRACTION	POSITIONAL	0.144
3	6	F	1869	X-RAY DIFFRACTION	POSITIONAL	0.116
3	7	G	1869	X-RAY DIFFRACTION	POSITIONAL	0.116
3	8	H	1869	X-RAY DIFFRACTION	POSITIONAL	0.116
3	9	I	1869	X-RAY DIFFRACTION	POSITIONAL	0.117
3	10	J	1869	X-RAY DIFFRACTION	POSITIONAL	0.116
3	11	K	1869	X-RAY DIFFRACTION	POSITIONAL	0.036
3	12	L	1869	X-RAY DIFFRACTION	POSITIONAL	0.038
3	13	M	1869	X-RAY DIFFRACTION	POSITIONAL	0.118
3	14	N	1869	X-RAY DIFFRACTION	POSITIONAL	0.118
3	15	O	1869	X-RAY DIFFRACTION	POSITIONAL	0.039
3	16	P	1869	X-RAY DIFFRACTION	POSITIONAL	0.043
3	17	Q	1869	X-RAY DIFFRACTION	POSITIONAL	0.042
3	18	R	1869	X-RAY DIFFRACTION	POSITIONAL	0.118
3	19	S	1869	X-RAY DIFFRACTION	POSITIONAL	0.036
3	20	T	1869	X-RAY DIFFRACTION	POSITIONAL	0.036
4	1	A	1878	X-RAY DIFFRACTION	POSITIONAL
4	2	B	1878	X-RAY DIFFRACTION	POSITIONAL	0.041
4	3	C	1878	X-RAY DIFFRACTION	POSITIONAL	0.117
4	4	D	1878	X-RAY DIFFRACTION	POSITIONAL	0.117
4	5	E	1878	X-RAY DIFFRACTION	POSITIONAL	0.119
4	6	F	1878	X-RAY DIFFRACTION	POSITIONAL	0.039
4	7	G	1878	X-RAY DIFFRACTION	POSITIONAL	0.041
4	8	H	1878	X-RAY DIFFRACTION	POSITIONAL	0.039
4	9	I	1878	X-RAY DIFFRACTION	POSITIONAL	0.041
4	10	J	1878	X-RAY DIFFRACTION	POSITIONAL	0.117
4	11	K	1878	X-RAY DIFFRACTION	POSITIONAL	0.045
4	12	L	1878	X-RAY DIFFRACTION	POSITIONAL	0.041
4	13	M	1878	X-RAY DIFFRACTION	POSITIONAL	0.045
4	14	N	1878	X-RAY DIFFRACTION	POSITIONAL	0.04
4	15	O	1878	X-RAY DIFFRACTION	POSITIONAL	0.119
4	16	P	1878	X-RAY DIFFRACTION	POSITIONAL	0.119
4	17	Q	1878	X-RAY DIFFRACTION	POSITIONAL	0.043
4	18	R	1878	X-RAY DIFFRACTION	POSITIONAL	0.04
4	19	S	1878	X-RAY DIFFRACTION	POSITIONAL	0.12
4	20	T	1878	X-RAY DIFFRACTION	POSITIONAL	0.041

LS refinement shell

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Refine-ID	% reflection obs (%)
2.7-2.7307	0.346	915	0.3268	17525	X-RAY DIFFRACTION	91
2.7307-2.7628	0.348	915	0.3238	17819	X-RAY DIFFRACTION	93
2.7628-2.7965	0.3457	929	0.3126	18183	X-RAY DIFFRACTION	94
2.7965-2.8319	0.3345	1034	0.306	18434	X-RAY DIFFRACTION	96
2.8319-2.8691	0.319	971	0.2978	18870	X-RAY DIFFRACTION	98
2.8691-2.9084	0.3183	1009	0.2808	19025	X-RAY DIFFRACTION	99
2.9084-2.9499	0.2872	1007	0.2673	19211	X-RAY DIFFRACTION	100
2.9499-2.994	0.2834	1057	0.2645	19173	X-RAY DIFFRACTION	100
2.994-3.0407	0.2801	987	0.2571	19322	X-RAY DIFFRACTION	100
3.0407-3.0905	0.2812	1036	0.2445	19223	X-RAY DIFFRACTION	100
3.0905-3.1438	0.2576	978	0.236	19248	X-RAY DIFFRACTION	100
3.1438-3.2009	0.2481	949	0.2273	19338	X-RAY DIFFRACTION	100
3.2009-3.2625	0.2441	1020	0.2236	19300	X-RAY DIFFRACTION	100
3.2625-3.329	0.2411	1050	0.2193	19238	X-RAY DIFFRACTION	100
3.329-3.4013	0.2236	1024	0.206	19277	X-RAY DIFFRACTION	100
3.4013-3.4804	0.2325	1036	0.2056	19228	X-RAY DIFFRACTION	100
3.4804-3.5674	0.2185	1004	0.1962	19362	X-RAY DIFFRACTION	100
3.5674-3.6637	0.2226	962	0.1884	19328	X-RAY DIFFRACTION	100
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