BIOMOLECULE: 1, 2, 3 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND PROGRAM GENERATED ASSEMBLY ... BIOMOLECULE: 1, 2, 3 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND PROGRAM GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN THIS ENTRY. THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 3 CHAINS BUT THEY DO NOT FORM OLIGOMERS BASED ON CRYSTAL PACKING ANALYSIS. SIZE EXCLUSION CHROMATOGRAPHY SUPPORTS THE ASSIGNMENT OF A MONOMER AS THE 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 FOLLOWED BY THE TARGET SEQUENCE.
THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 3 CHAINS BUT THEY DO NOT FORM OLIGOMERS BASED ON CRYSTAL PACKING ANALYSIS. SIZE EXCLUSION CHROMATOGRAPHY SUPPORTS THE ASSIGNMENT OF A MONOMER AS THE SIGNIFICANT OLIGOMERIZATION STATE.
-
Components
#1: Protein
Uncharacterizedprotein
Mass: 30339.539 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Shewanella amazonensis (bacteria) / Strain: SB2B / Gene: YP_926603.1, Sama_0725 / Plasmid: speedET / Production host: Escherichia coli (E. coli) / Strain (production host): HK100 / References: UniProt: A1S3H7
Type: MARMOSAIC 325 mm CCD / Detector: CCD / Date: Jun 22, 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
Reflection
Resolution: 2→29.63 Å / Num. obs: 57061 / % possible obs: 92.8 % / Redundancy: 3.36 % / Biso Wilson estimate: 20.14 Å2 / Rmerge(I) obs: 0.107 / Net I/σ(I): 7.41
Reflection shell
Resolution (Å)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured obs
Diffraction-ID
% possible all
2-2.07
0.518
1.87
19189
1
99.5
2.07-2.15
0.434
2.3
19546
1
99.8
2.15-2.25
0.368
2.7
10720
1
53.8
2.25-2.37
0.303
3.3
18632
1
91.7
2.37-2.52
0.252
4.1
20909
1
99.9
2.52-2.71
0.198
5.2
20392
1
99.9
2.71-2.99
0.133
7.2
21634
1
99.8
2.99-3.42
0.078
11.1
20982
1
99.9
3.42-4.3
0.05
15.5
17921
1
85.7
4.3-29.63
0.035
19.4
21955
1
99.6
-
Phasing
Phasing
Method: MAD
-
Processing
Software
Name
Version
Classification
NB
REFMAC
5.2.0019
refinement
PHENIX
refinement
SHELX
phasing
MolProbity
3beta29
modelbuilding
XSCALE
datascaling
PDB_EXTRACT
2
dataextraction
MAR345
CCD
datacollection
XDS
datareduction
SHELXD
phasing
SHARP
phasing
Refinement
Method to determine structure: MAD / Resolution: 2→29.63 Å / Cor.coef. Fo:Fc: 0.959 / Cor.coef. Fo:Fc free: 0.929 / SU B: 7.307 / SU ML: 0.108 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.172 / ESU R Free: 0.159 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 A1-A6, A273-A274, B1-B5, B273-B274, AND C1-C5 ARE DISORDERED AND HAVE NOT BEEN MODELLED. 4. TEN SULFATE ANIONS AND TWELVE GLYCEROL MOLECULES HAVE BEEN MODELED IN THE SOLVENT STRUCTURE. 5. DIFFRACTION DATA IMAGES WERE PROCESSED BY MASKING OUT REFLECTIONS IN RESOLUTION RANGES 3.89A-3.87A, 3.70A-3.64A, 2.26A-2.24A AND 2.24A-2.21A CORRESPONDING TO ICE RINGS.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.213
2870
5 %
RANDOM
Rwork
0.161
-
-
-
all
0.164
-
-
-
obs
0.164
57042
93.32 %
-
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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