SEQUENCE THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS ...SEQUENCE THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
Resolution: 2→69.5 Å / Num. obs: 53921 / % possible obs: 91.6 % / Redundancy: 3.2 % / Rmerge(I) obs: 0.067 / Net I/σ(I): 9.53
Reflection shell
Diffraction-ID: 1
Resolution (Å)
% possible obs (%)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured obs
Num. unique obs
% possible all
2-2.07
79.6
0.424
2.05
10419
8517
79.6
2.07-2.15
85
0.599
2.73
10995
8992
2.15-2.25
87.7
0.599
3.42
12002
9794
2.25-2.37
90.5
0.599
4.37
12170
9971
2.37-2.52
91.4
0.599
5.39
12343
10138
2.52-2.71
93.1
0.599
6.81
12114
9964
2.71-2.99
94.2
0.599
9.6
12711
10484
2.99-3.42
96.7
0.599
14.04
21791
10512
3.42-4.3
98.4
0.599
17.82
33399
10680
4.3-69.5
98.7
0.599
25.04
33563
10852
-
Phasing
Phasing
Method: MAD
-
Processing
Software
Name
Version
Classification
NB
REFMAC
5.2.0005
refinement
XSCALE
datascaling
PDB_EXTRACT
1.601
dataextraction
XDS
datareduction
SHELX
phasing
SHARP
phasing
Refinement
Method to determine structure: MAD / Resolution: 2→69.5 Å / Cor.coef. Fo:Fc: 0.965 / Cor.coef. Fo:Fc free: 0.94 / SU B: 8.233 / SU ML: 0.124 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.172 / ESU R Free: 0.161 Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES Details: 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS 2. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE ...Details: 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS 2. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 3. ADP AND MG WERE MODELED BASED ON ELECTRON DENSITY AND THE PROTEIN'S PROPOSED FUNCTION AS AN ATPASE. 4. RESIDUES 115-119 ARE DISORDERED IN EACH CHAIN AND WERE NOT MODELED.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.226
2733
5.1 %
RANDOM
Rwork
0.174
-
-
-
all
0.177
-
-
-
obs
0.17656
51161
97.51 %
-
Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parameters
Biso mean: 36.569 Å2
Baniso -1
Baniso -2
Baniso -3
1-
-2.3 Å2
0 Å2
-0.71 Å2
2-
-
1.17 Å2
0 Å2
3-
-
-
0.88 Å2
Refinement step
Cycle: LAST / Resolution: 2→69.5 Å
Protein
Nucleic acid
Ligand
Solvent
Total
Num. atoms
5688
0
84
347
6119
Refine LS restraints
Refine-ID
Type
Dev ideal
Dev ideal target
Number
X-RAY DIFFRACTION
r_bond_refined_d
0.014
0.022
5942
X-RAY DIFFRACTION
r_bond_other_d
0.001
0.02
5552
X-RAY DIFFRACTION
r_angle_refined_deg
1.425
2
8020
X-RAY DIFFRACTION
r_angle_other_deg
0.818
3
12865
X-RAY DIFFRACTION
r_dihedral_angle_1_deg
5.772
5
720
X-RAY DIFFRACTION
r_dihedral_angle_2_deg
33.827
23.791
277
X-RAY DIFFRACTION
r_dihedral_angle_3_deg
14.787
15
1092
X-RAY DIFFRACTION
r_dihedral_angle_4_deg
17.074
15
43
X-RAY DIFFRACTION
r_chiral_restr
0.082
0.2
884
X-RAY DIFFRACTION
r_gen_planes_refined
0.005
0.02
6483
X-RAY DIFFRACTION
r_gen_planes_other
0.001
0.02
1256
X-RAY DIFFRACTION
r_nbd_refined
0.214
0.2
1193
X-RAY DIFFRACTION
r_nbd_other
0.176
0.2
5483
X-RAY DIFFRACTION
r_nbtor_refined
0.185
0.2
2880
X-RAY DIFFRACTION
r_nbtor_other
0.082
0.2
3445
X-RAY DIFFRACTION
r_xyhbond_nbd_refined
0.163
0.2
321
X-RAY DIFFRACTION
r_xyhbond_nbd_other
0.018
0.2
1
X-RAY DIFFRACTION
r_symmetry_vdw_refined
0.119
0.2
7
X-RAY DIFFRACTION
r_symmetry_vdw_other
0.218
0.2
53
X-RAY DIFFRACTION
r_symmetry_hbond_refined
0.12
0.2
12
X-RAY DIFFRACTION
r_mcbond_it
1.961
3
3629
X-RAY DIFFRACTION
r_mcbond_other
0.485
3
1440
X-RAY DIFFRACTION
r_mcangle_it
2.923
5
5686
X-RAY DIFFRACTION
r_scbond_it
4.934
8
2634
X-RAY DIFFRACTION
r_scangle_it
6.568
11
2324
LS refinement shell
Resolution: 2→2.052 Å / Total num. of bins used: 20
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