BIOMOLECULE: 1 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 2 ... BIOMOLECULE: 1 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). SIZE EXCLUSION CHROMATOGRAPHY SUPPORTS THE ASSIGNMENT OF A DIMER AS A SIGNIFICANT OLIGOMERIZATION STATE.
Remark 999
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: 1.35→29.348 Å / Num. obs: 170743 / % possible obs: 95.9 % / Redundancy: 4.8 % / Biso Wilson estimate: 13.57 Å2 / Rmerge(I) obs: 0.052 / Rsym value: 0.052 / Net I/σ(I): 8.2
Reflection shell
Diffraction-ID: 1,2
Resolution (Å)
Redundancy (%)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured all
Num. unique all
Rsym value
% possible all
1.35-1.39
2.1
0.346
1.1
19621
9561
0.346
73.9
1.39-1.42
2.3
0.273
2.6
24616
10497
0.273
82.9
1.42-1.47
2.7
0.231
2.5
30402
11207
0.231
91
1.47-1.51
3.4
0.201
2.6
40027
11724
0.201
97.3
1.51-1.56
4
0.182
3
46728
11686
0.182
100
1.56-1.61
4
0.144
4.7
45483
11283
0.144
100
1.61-1.68
4
0.118
6
44071
10896
0.118
100
1.68-1.74
4
0.098
6.8
42399
10493
0.098
100
1.74-1.82
4.1
0.079
8.5
41058
10096
0.079
100
1.82-1.91
4.7
0.089
6.9
45851
9673
0.089
100
1.91-2.01
5.2
0.088
3.9
47649
9190
0.088
100
2.01-2.14
5.8
0.076
8.1
50400
8696
0.076
100
2.14-2.28
6.8
0.07
9
56227
8212
0.07
100
2.28-2.47
7.7
0.063
9.6
59252
7706
0.063
100
2.47-2.7
7.7
0.058
10.5
54309
7056
0.058
100
2.7-3.02
7.7
0.05
12.3
49310
6409
0.05
99.8
3.02-3.49
7.7
0.044
13.4
43285
5655
0.044
99.6
3.49-4.27
7.6
0.038
15.3
36485
4819
0.038
99.3
4.27-6.04
7.4
0.035
16.3
27793
3758
0.035
98.7
6.04-29.348
6.8
0.035
15.8
14463
2126
0.035
96.8
-
Phasing
Phasing
Method: MAD
-
Processing
Software
Name
Version
Classification
NB
REFMAC
5.2.0019
refinement
PHENIX
refinement
SHELX
phasing
MolProbity
3beta29
modelbuilding
SCALA
datascaling
PDB_EXTRACT
3
dataextraction
MAR345
CCD
datacollection
MOSFLM
datareduction
SHELXD
phasing
SHARP
phasing
Refinement
Method to determine structure: MAD / Resolution: 1.35→29.348 Å / Cor.coef. Fo:Fc: 0.982 / Cor.coef. Fo:Fc free: 0.975 / SU B: 1.193 / SU ML: 0.022 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.04 / ESU R Free: 0.04 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. SO4, GOL ARE FROM CRYSTALLIZATION OR CRYO CONDITIONS. 4. PEG 200 ARE MODELED BASED ON ELECTRON DENSITY, BUT PEG 200 IS NOT PRESENT IN CRYSTALLIZATION OR CRYO CONDITION. 5. AN UNKNOWN LIGAND (UNL) IS MODELED FOR EACH MONOMER. THEY COULD BE WATER CHAINS. 6. THE OCCUPANCIES FOR A FEW SURFACE SIDE CHAINS AND B341/B342 ARE SET AS PARTIAL BASED ON DENSITY.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.144
8613
5 %
RANDOM
Rwork
0.116
-
-
-
obs
0.117
170682
95.79 %
-
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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