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 MONOMER AS A SIGNIFICANT OLIGOMERIZATION STATE IN SOLUTION.
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 FOLLOWED BY THE TARGET SEQUENCE.
Type: MARMOSAIC 325 mm CCD / Detector: CCD / Date: May 3, 2007 / Details: Flat mirror (vertical focusing)
Radiation
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
0.97944
1
3
0.97917
1
Reflection
Resolution: 2→29.604 Å / Num. obs: 43945 / % possible obs: 99.9 % / Redundancy: 3.5 % / Biso Wilson estimate: 26.54 Å2 / Rmerge(I) obs: 0.078 / Rsym value: 0.078 / Net I/σ(I): 6.9
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
2-2.05
3.4
0.382
2
11021
3200
0.382
99.9
2.05-2.11
3.5
0.32
2.3
10954
3129
0.32
99.9
2.11-2.17
3.5
0.271
2.7
10756
3056
0.271
100
2.17-2.24
3.5
0.237
3.1
10343
2947
0.237
100
2.24-2.31
3.5
0.213
3.4
10106
2873
0.213
100
2.31-2.39
3.5
0.183
4
9750
2767
0.183
100
2.39-2.48
3.5
0.156
4.6
9511
2707
0.156
100
2.48-2.58
3.5
0.138
5
9097
2587
0.138
100
2.58-2.7
3.5
0.118
5.8
8667
2477
0.118
100
2.7-2.83
3.5
0.105
6.4
8340
2377
0.105
100
2.83-2.98
3.5
0.095
6.9
7989
2273
0.095
100
2.98-3.16
3.5
0.082
7.5
7544
2157
0.082
100
3.16-3.38
3.5
0.071
8.8
7113
2031
0.071
100
3.38-3.65
3.5
0.06
10
6715
1912
0.06
100
3.65-4
3.5
0.048
12.3
6078
1751
0.048
100
4-4.47
3.5
0.038
15.1
5554
1593
0.038
99.9
4.47-5.16
3.4
0.044
12.4
4840
1407
0.044
99.7
5.16-6.32
3.4
0.058
9.5
4137
1217
0.058
99.6
6.32-8.94
3.3
0.049
11.8
3173
952
0.049
99.5
8.94-29.6
3
0.043
13.5
1610
532
0.043
93.5
-
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
SHARP
phasing
Refinement
Method to determine structure: MAD / Resolution: 2→29.604 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.93 / SU B: 8.572 / SU ML: 0.125 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.184 / ESU R Free: 0.168 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. ZINC WAS MODELED BASED ON GEOMETRY AND COORDINATION ENVIRONMENT, AND CONFIRMED WITH X-RAY FLUORESCENCE AND ANOMALOUS DIFFERENCE FOURIER EXPERIMENTS. THERE IS UNMODELLED DENSITY NEAR THIS ZINC ION WHICH COULD BE ANOTHER ZINC ION, WATER MOLECULE OR OTHER PURIFICATION ARTIFACT WHICH CANNOT BE RELIABLY MODELLED.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.246
2213
5 %
RANDOM
Rwork
0.199
-
-
-
obs
0.202
43897
99.85 %
-
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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