PROTEIN CONSTRUCT IS A SPLICE FORM THAT DOES NOT CONTAIN SPLICE INSERTS AT SITES SS1 [DEL(258-277)] ...PROTEIN CONSTRUCT IS A SPLICE FORM THAT DOES NOT CONTAIN SPLICE INSERTS AT SITES SS1 [DEL(258-277)], SS2 [DEL(378-393)], SS3 [DEL(790-799),D790G], AND SS4 [DEL(1248-1278)]. Q612E AND I1112F ARE NATURAL ISOFORMS.
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 4.05 Å3/Da / Density % sol: 69.62 %
Crystal grow
Temperature: 293 K / Method: vapor diffusion, hanging drop Details: 5-10% PEG8000 or PEG10000, 2.5 mM calcium chloride, 100 mM bicine, pH 8.0-9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Jun 12, 2010
Radiation
Monochromator: Kohzu / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 1.1272 Å / Relative weight: 1
Reflection
Redundancy: 4 % / Av σ(I) over netI: 17.83 / Number: 267276 / Rmerge(I) obs: 0.135 / Χ2: 1.9 / D res high: 3.25 Å / D res low: 50 Å / Num. obs: 67601 / % possible obs: 98.6
Diffraction reflection shell
Highest resolution (Å)
Lowest resolution (Å)
% possible obs (%)
ID
Rmerge(I) obs
Chi squared
Redundancy
8.81
50
96.2
1
0.035
4.014
3.9
7
8.81
98.3
1
0.051
2.789
4
6.11
7
98.8
1
0.074
2.313
4
5.56
6.11
98.7
1
0.083
1.995
4
5.16
5.56
98.7
1
0.088
2.158
4
4.85
5.16
99
1
0.094
2.047
4
4.61
4.85
99
1
0.091
2.008
4
4.41
4.61
98.6
1
0.107
1.96
4
4.24
4.41
99.2
1
0.13
1.824
4
4.09
4.24
98.7
1
0.174
1.715
4
3.97
4.09
99.2
1
0.182
1.685
4
3.85
3.97
98.8
1
0.218
1.582
4
3.75
3.85
99.1
1
0.26
1.579
4
3.66
3.75
98.8
1
0.307
1.529
4
3.58
3.66
98.9
1
0.36
1.554
4
3.5
3.58
98.7
1
0.388
1.511
4
3.43
3.5
98.8
1
0.487
1.474
3.9
3.37
3.43
98.9
1
0.558
1.438
3.9
3.31
3.37
98.4
1
0.634
1.394
3.8
3.25
3.31
97.9
1
0.802
1.453
3.7
Reflection
Resolution: 2.65→50 Å / Num. obs: 124701 / % possible obs: 98.5 % / Redundancy: 3.4 % / Rmerge(I) obs: 0.079 / Χ2: 1.591 / Net I/σ(I): 14.5
Reflection shell
Resolution (Å)
Redundancy (%)
Rmerge(I) obs
Num. unique all
Χ2
Diffraction-ID
% possible all
2.65-2.7
3.2
0.526
6206
1.239
1
98.2
2.7-2.74
3.3
0.45
6169
1.203
1
97.7
2.74-2.8
3.3
0.424
6187
1.306
1
97.3
2.8-2.85
3.3
0.38
6211
1.331
1
98.4
2.85-2.92
3.3
0.321
6191
1.33
1
96.9
2.92-2.98
3.3
0.252
6222
1.39
1
99.2
2.98-3.06
3.4
0.215
6200
1.479
1
97
3.06-3.14
3.4
0.182
6240
1.575
1
99.4
3.14-3.23
3.4
0.146
6187
1.441
1
97.5
3.23-3.34
3.4
0.13
6251
1.544
1
99.3
3.34-3.46
3.4
0.111
6226
1.687
1
98.3
3.46-3.6
3.4
0.092
6291
1.75
1
98
3.6-3.76
3.4
0.082
6204
1.814
1
99.6
3.76-3.96
3.4
0.076
6278
1.93
1
98.8
3.96-4.21
3.4
0.066
6231
1.958
1
98.7
4.21-4.53
3.4
0.06
6291
1.954
1
99.1
4.53-4.99
3.4
0.053
6312
1.948
1
99.1
4.99-5.71
3.4
0.052
6267
1.822
1
99.1
5.71-7.19
3.4
0.048
6298
1.615
1
99.5
7.19-50
3.3
0.036
6239
1.398
1
98.6
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Phasing
Phasing
Method
SAD
molecular replacement
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Processing
Software
Name
Version
Classification
NB
DENZO
datareduction
SCALEPACK
datascaling
PHASER
phasing
REFMAC
refinement
PDB_EXTRACT
3.1
dataextraction
HKL-2000
datacollection
Refinement
Method to determine structure: SAD, MOLECULAR REPLACEMENT / Resolution: 2.65→30 Å / Cor.coef. Fo:Fc: 0.936 / Cor.coef. Fo:Fc free: 0.925 / WRfactor Rfree: 0.2745 / WRfactor Rwork: 0.2672 / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.8568 / SU B: 16.733 / SU ML: 0.161 / SU R Cruickshank DPI: 0.3693 / SU Rfree: 0.2628 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.299 / ESU R Free: 0.226 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.2296
6451
5.2 %
RANDOM
Rwork
0.2082
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-
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obs
0.2093
116726
98.43 %
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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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