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→72.548 Å / Num. obs: 53741 / % possible obs: 99.8 % / Redundancy: 6 % / Biso Wilson estimate: 24.27 Å2 / Rmerge(I) obs: 0.11 / Rsym value: 0.11 / Net I/σ(I): 6.1
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
2-2.11
6.1
0.691
1
46753
7646
0.691
99.5
2.11-2.24
6.1
0.463
1.4
44384
7265
0.463
99.6
2.24-2.39
6.1
0.352
1.8
41733
6853
0.352
99.7
2.39-2.58
6.1
0.256
2.8
39038
6419
0.256
99.8
2.58-2.83
6
0.176
4.2
35962
5951
0.176
99.9
2.83-3.16
6
0.104
7.1
32587
5413
0.104
100
3.16-3.65
6
0.061
11.6
28773
4813
0.061
100
3.65-4.47
5.9
0.043
15.4
24345
4146
0.043
100
4.47-6.32
5.7
0.039
15.4
18735
3281
0.039
100
6.32-78.09
5.1
0.032
17.1
9962
1954
0.032
99.8
-
Phasing
Phasing
Method: MAD
-
Processing
Software
Name
Version
Classification
NB
MolProbity
3beta29
modelbuilding
SOLVE
phasing
REFMAC
5.2.0019
refinement
SCALA
datascaling
PDB_EXTRACT
2
dataextraction
ADSC
QUANTUM
datacollection
MOSFLM
datareduction
CCP4
(SCALA)
datascaling
Refinement
Method to determine structure: MAD / Resolution: 2→72.548 Å / Cor.coef. Fo:Fc: 0.943 / Cor.coef. Fo:Fc free: 0.926 / SU B: 7.656 / SU ML: 0.113 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.158 / ESU R Free: 0.149 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 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 3. RESIDUES 1-2, 259-261 IN CHAIN A AND 1-2, 143 IN CHAIN B ARE DISORDERED AND NOT INCLUDED IN THE MODEL. 5. THERE ARE SOME UNMODELED DENSITIES NEAR A11, A103. 4. ACT, GOL, AND SO4 MOLECULES FROM THE CRYSTALLIZATION/CRYO SOLUTIONS ARE MODELED. 5. AN UNKNOWN LIGAND (UNL) MOLECULE IS MODELED IN BOTH CHAINS. 6. ATOM RECORDS CONTAIN RESIDUAL B FACTORS ONLY.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.242
2725
5.1 %
RANDOM
Rwork
0.204
-
-
-
all
0.206
-
-
-
obs
0.206
53697
99.65 %
-
Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK
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