A: Uncharacterized protein B: Uncharacterized protein C: Uncharacterized protein D: Uncharacterized protein E: Uncharacterized protein F: Uncharacterized protein G: Uncharacterized protein H: Uncharacterized protein I: Uncharacterized protein J: Uncharacterized protein hetero molecules
Mass: 18.015 Da / Num. of mol.: 574 / Source method: isolated from a natural source / Formula: H2O
Sequence details
THE CONSTRUCT (RESIDUES 22-174) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG ...THE CONSTRUCT (RESIDUES 22-174) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
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Experimental details
-
Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
Resolution: 2.4→29.277 Å / Num. all: 82726 / Num. obs: 82726 / % possible obs: 97.8 % / Redundancy: 3.6 % / Rsym value: 0.139 / Net I/σ(I): 7.2
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
2.4-2.46
3.7
0.917
0.8
22106
6024
0.917
97.2
2.46-2.53
3.7
0.773
1
21951
5933
0.773
97.3
2.53-2.6
3.7
0.659
1.2
21227
5717
0.659
97.4
2.6-2.68
3.7
0.567
1.3
20604
5563
0.567
97.5
2.68-2.77
3.7
0.456
1.7
20282
5469
0.456
97.6
2.77-2.87
3.7
0.393
1.9
19361
5229
0.393
97.6
2.87-2.98
3.7
0.296
2.6
18731
5078
0.296
97.7
2.98-3.1
3.7
0.212
3.6
17905
4868
0.212
97.8
3.1-3.24
3.7
0.181
4.2
17241
4694
0.181
97.9
3.24-3.39
3.7
0.129
5.7
16490
4499
0.129
97.9
3.39-3.58
3.6
0.102
7.2
15622
4285
0.102
98
3.58-3.79
3.6
0.088
7.9
14790
4083
0.088
98.4
3.79-4.06
3.6
0.08
8.3
13743
3827
0.08
98.2
4.06-4.38
3.6
0.065
10.6
12661
3559
0.065
98.2
4.38-4.8
3.5
0.059
11.1
11398
3277
0.059
98.3
4.8-5.37
3.4
0.059
11.4
10252
3009
0.059
98.4
5.37-6.2
3.3
0.068
9.9
8775
2629
0.068
98.4
6.2-7.59
3.7
0.067
9.5
8451
2261
0.067
98.5
7.59-10.73
3.7
0.041
12.6
6513
1771
0.041
98.8
10.73-29.277
3.5
0.041
12.1
3365
951
0.041
93.5
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Phasing
Phasing
Method: MAD
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Processing
Software
Name
Version
Classification
NB
MolProbity
3beta29
modelbuilding
PDB_EXTRACT
3.1
dataextraction
SHELX
phasing
SHARP
phasing
SCALA
3.3.20
datascaling
BUSTER-TNT
2.10.0
refinement
MOSFLM
datareduction
SHELXD
phasing
BUSTER
2.10.0
refinement
Refinement
Method to determine structure: MAD / Resolution: 2.4→29.277 Å / Cor.coef. Fo:Fc: 0.9398 / Cor.coef. Fo:Fc free: 0.924 / Occupancy max: 1 / Occupancy min: 0.37 / Cross valid method: THROUGHOUT / σ(F): 0 Details: 1. 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 ...Details: 1. 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. 2. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 3. THE MAD PHASES WERE USED AS RESTRAINTS DURING REFINEMENT. 4. NCS RESTRAINTS WERE APPLIED USING BUSTER'S LSSR RESTRAINT REPRESENTATION (-AUTONCS). 5.CHLORIDE FROM THE PURIFICATION BUFFER HAS BEEN MODELED INTO THE STRUCTURE.
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