BIOMOLECULE: 1 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 2 CHAINS. ... BIOMOLECULE: 1 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 2 CHAINS. 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 THIS CONSTRUCT IS COMPRISED OF AMINO ACIDS 81-377 OF THE FULL-LENGTH PROTEIN (1-377) AND ... SEQUENCE THIS CONSTRUCT IS COMPRISED OF AMINO ACIDS 81-377 OF THE FULL-LENGTH PROTEIN (1-377) AND WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE FOLLOWED BY THE TARGET SEQUENCE.
Monochromator: Single crystal Si(111) bent (horizontal focusing) Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
ID
Wavelength (Å)
Relative weight
1
0.91837
1
2
0.9792
1
Reflection
Resolution: 2→29.696 Å / Num. obs: 56593 / % possible obs: 99.7 % / Redundancy: 7.29 % / Biso Wilson estimate: 32.83 Å2 / Rmerge(I) obs: 0.062 / Net I/σ(I): 12.89
Reflection shell
Resolution (Å)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured obs
Num. unique all
Diffraction-ID
% possible all
2-2.07
0.507
2.56
39584
9589
1
99.3
2.07-2.15
0.374
3.5
39963
9827
1
94.1
2.15-2.25
0.286
4.5
42396
10550
1
95.5
2.25-2.37
0.236
5.5
41831
10490
1
96.4
2.37-2.52
0.166
7.7
42014
10610
1
97.4
2.52-2.71
0.136
9.2
40730
10322
1
97.8
2.71-2.99
0.095
12.9
42506
10884
1
98.8
2.99-3.42
0.057
19.4
41261
10594
1
99.1
3.42-4.3
0.035
29.3
41164
10659
1
99.6
4.3-29.7
0.028
34.4
40875
1
98
-
Phasing
Phasing
Method: MAD
-
Processing
Software
Name
Version
Classification
NB
MolProbity
3beta29
modelbuilding
SHELX
phasing
REFMAC
5.2.0005
refinement
XSCALE
datascaling
PDB_EXTRACT
2
dataextraction
MAR345
CCD
datacollection
XDS
datareduction
SHELXD
phasing
autoSHARP
phasing
Refinement
Method to determine structure: MAD / Resolution: 2→29.696 Å / Cor.coef. Fo:Fc: 0.968 / Cor.coef. Fo:Fc free: 0.955 / SU B: 5.931 / SU ML: 0.084 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.126 / ESU R Free: 0.121 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. ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY. 4. RESIDUES 81-91, 312-315, 372-377 IN CHAIN A AND 81-91, 372-377 IN CHAIN B ARE DISORDERED AND ARE NOT MODELED. 5. LIGAND MOLECULES NAD AND TYR ARE MODELED.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.194
2870
5.1 %
RANDOM
Rwork
0.161
-
-
-
all
0.163
-
-
-
obs
0.163
56541
99.75 %
-
Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
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