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.
A: NTF2-like protein of unknown function B: NTF2-like protein of unknown function C: NTF2-like protein of unknown function D: NTF2-like protein of unknown function E: NTF2-like protein of unknown function F: NTF2-like protein of unknown function G: NTF2-like protein of unknown function H: NTF2-like protein of unknown function I: NTF2-like protein of unknown function J: NTF2-like protein of unknown function K: NTF2-like protein of unknown function L: NTF2-like protein of unknown function hetero molecules
A: NTF2-like protein of unknown function B: NTF2-like protein of unknown function C: NTF2-like protein of unknown function D: NTF2-like protein of unknown function hetero molecules
E: NTF2-like protein of unknown function F: NTF2-like protein of unknown function G: NTF2-like protein of unknown function H: NTF2-like protein of unknown function hetero molecules
I: NTF2-like protein of unknown function J: NTF2-like protein of unknown function K: NTF2-like protein of unknown function L: NTF2-like protein of unknown function hetero molecules
Resolution: 1.75→29.348 Å / Num. obs: 126809 / % possible obs: 81.7 % / Redundancy: 1.9 % / Rmerge(I) obs: 0.042 / Rsym value: 0.042 / Net I/σ(I): 11.9
Reflection shell
Diffraction-ID: 1
Resolution (Å)
Redundancy (%)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured all
Num. unique all
Rsym value
% possible all
1.75-1.8
1.9
0.456
1.5
8054
4345
0.456
37.8
1.8-1.84
1.9
0.356
1.9
9851
5254
0.356
46.6
1.84-1.9
1.9
0.289
2.3
11717
6239
0.289
57.6
1.9-1.96
1.8
0.213
3.3
14039
7661
0.213
72.5
1.96-2.02
1.8
0.165
4.3
17406
9434
0.165
92
2.02-2.09
1.9
0.14
5
17884
9190
0.14
92.8
2.09-2.17
1.9
0.108
6.6
17319
8893
0.108
92.7
2.17-2.26
1.9
0.086
8.2
16610
8545
0.086
93.1
2.26-2.36
1.9
0.077
9.2
15943
8192
0.077
93
2.36-2.47
1.9
0.064
10.8
15352
7882
0.064
93.2
2.47-2.61
1.9
0.058
11.5
14514
7464
0.058
93.1
2.61-2.77
1.9
0.047
9.8
13808
7086
0.047
93.1
2.77-2.96
1.9
0.038
16.2
12787
6594
0.038
93.4
2.96-3.2
1.9
0.033
19.4
12002
6217
0.033
93.1
3.2-3.5
1.9
0.028
20.8
10872
5665
0.028
93.1
3.5-3.91
1.9
0.026
20.6
9818
5128
0.026
92.8
3.91-4.52
1.9
0.024
23.3
8416
4496
0.024
92.5
4.52-5.53
1.7
0.024
21.2
6661
3815
0.024
93
5.53-7.83
1.9
0.023
24.2
5919
3050
0.023
96.5
7.83-29.348
2
0.019
26
3296
1659
0.019
94.8
-
Phasing
Phasing
Method: MAD
-
Processing
Software
Name
Version
Classification
NB
REFMAC
5.2.0019
refinement
PHENIX
refinement
SOLVE
phasing
MolProbity
3beta29
modelbuilding
SCALA
datascaling
PDB_EXTRACT
3
dataextraction
ADSC
Quantum
datacollection
MOSFLM
datareduction
Refinement
Method to determine structure: MAD / Resolution: 1.75→29.348 Å / Cor.coef. Fo:Fc: 0.971 / Cor.coef. Fo:Fc free: 0.953 / SU B: 4.559 / SU ML: 0.073 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.128 / ESU R Free: 0.123 Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES Details: 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2. ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY. 3. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN ...Details: 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2. ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY. 3. 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. 4. PEG 4000 FRAGMENTS (PEG) FROM CRYSTALLIZATION CONDITIONS AND ETHYLENE GLYCOL (EDO) FROM CRYO CONDITIONS ARE MODELED IN THE STRUCTURE. 5. THE NOMINAL RESOLUTION IS 1.90 A WITH 16060 OBSERVED REFLECTIONS BETWEEN 1.90-1.75 (47.4% COMPLETE FOR THIS SHELL) INCLUDED IN THE REFINEMENT.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.194
6400
5 %
RANDOM
Rwork
0.152
-
-
-
obs
0.154
126808
81.57 %
-
Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
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