BIOMOLECULE: 1 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 1 CHAIN(S) ...BIOMOLECULE: 1 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). SIZE EXCLUSION CHROMATOGRAPHY WITH STATIC LIGHT SCATTERING SUPPORTS THE ASSIGNMENT OF A DIMER AS A BIOLOGICALLY 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. THE CONSTRUCT IS A TRUNCATION OF THE FULL LENGTH PROTEIN, WITH ONLY RESIDUES 149-225 EXPRESSED.
Type: MARMOSAIC 325 mm CCD / Detector: CCD / Date: Nov 19, 2006 / Details: Flat mirror (vertical focusing)
Radiation
Monochromator: Single crystal Si(111) bent monochromator (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
0.97971
1
3
0.97925
1
Reflection
Resolution: 1.41→48.507 Å / Num. obs: 26400 / % possible obs: 91.5 % / Biso Wilson estimate: 23.109 Å2 / Rmerge(I) obs: 0.051 / Net I/σ(I): 21.48
Reflection shell
Diffraction-ID: 1
Resolution (Å)
Highest resolution (Å)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured obs
Num. unique all
% possible all
1.41-1.46
0.457
2.6
5654
1638
59.5
1.46-1.52
0.388
3.3
8649
2091
73.4
1.52-1.59
0.301
5
12084
2409
86.2
1.59-1.67
0.247
7.2
17096
2600
97.7
1.67-1.78
0.183
10
20665
2894
99
1.78-1.91
0.121
15
22357
2636
99
1.91-2.11
0.084
24.2
32410
2927
99.7
2.11-2.41
0.065
34
38854
2783
99.8
2.41
0.051
42.8
40047
2865
99.9
-
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
XDS
datareduction
SHELXD
phasing
autoSHARP
phasing
Refinement
Method to determine structure: MAD / Resolution: 1.41→48.507 Å / Cor.coef. Fo:Fc: 0.973 / Cor.coef. Fo:Fc free: 0.966 / SU B: 2.766 / SU ML: 0.049 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.061 / ESU R Free: 0.062 Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES Details: 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2. ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY. 3. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN ...Details: 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2. ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY. 3. 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. 4. RESIDUES 149-157 AND 290-295 ARE DISORDERED AND WERE NOT MODELED.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.189
1314
5 %
RANDOM
Rwork
0.165
-
-
-
obs
0.166
26355
93.47 %
-
Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parameters
Biso mean: 19.041 Å2
Baniso -1
Baniso -2
Baniso -3
1-
-0.85 Å2
0 Å2
0 Å2
2-
-
-0.85 Å2
0 Å2
3-
-
-
1.69 Å2
Refinement step
Cycle: LAST / Resolution: 1.41→48.507 Å
Protein
Nucleic acid
Ligand
Solvent
Total
Num. atoms
1052
0
0
143
1195
Refine LS restraints
Refine-ID
Type
Dev ideal
Dev ideal target
Number
X-RAY DIFFRACTION
r_bond_refined_d
0.017
0.021
1157
X-RAY DIFFRACTION
r_bond_other_d
0.001
0.02
1046
X-RAY DIFFRACTION
r_angle_refined_deg
1.709
1.928
1593
X-RAY DIFFRACTION
r_angle_other_deg
0.823
3
2440
X-RAY DIFFRACTION
r_dihedral_angle_1_deg
6.165
5
154
X-RAY DIFFRACTION
r_dihedral_angle_2_deg
35.417
23.934
61
X-RAY DIFFRACTION
r_dihedral_angle_3_deg
12.415
15
193
X-RAY DIFFRACTION
r_dihedral_angle_4_deg
20.268
15
8
X-RAY DIFFRACTION
r_chiral_restr
0.101
0.2
175
X-RAY DIFFRACTION
r_gen_planes_refined
0.008
0.02
1322
X-RAY DIFFRACTION
r_gen_planes_other
0.001
0.02
236
X-RAY DIFFRACTION
r_nbd_refined
0.198
0.2
195
X-RAY DIFFRACTION
r_nbd_other
0.186
0.2
1028
X-RAY DIFFRACTION
r_nbtor_refined
0.175
0.2
523
X-RAY DIFFRACTION
r_nbtor_other
0.088
0.2
699
X-RAY DIFFRACTION
r_xyhbond_nbd_refined
0.162
0.2
97
X-RAY DIFFRACTION
r_symmetry_vdw_refined
0.058
0.2
3
X-RAY DIFFRACTION
r_symmetry_vdw_other
0.278
0.2
57
X-RAY DIFFRACTION
r_symmetry_hbond_refined
0.141
0.2
30
X-RAY DIFFRACTION
r_mcbond_it
2.006
3
739
X-RAY DIFFRACTION
r_mcbond_other
0.5
3
280
X-RAY DIFFRACTION
r_mcangle_it
2.666
5
1139
X-RAY DIFFRACTION
r_scbond_it
4.168
8
497
X-RAY DIFFRACTION
r_scangle_it
5.485
11
442
LS refinement shell
Resolution: 1.411→1.448 Å / Total num. of bins used: 20
Rfactor
Num. reflection
% reflection
Rfree
0.312
71
-
Rwork
0.328
1263
-
obs
-
1334
64.79 %
Refinement TLS params.
Method: refined / Origin x: 21.4539 Å / Origin y: 24.7055 Å / Origin z: 19.7693 Å
11
12
13
21
22
23
31
32
33
T
-0.0658 Å2
-0.0089 Å2
-0.0057 Å2
-
-0.049 Å2
-0.0103 Å2
-
-
-0.008 Å2
L
0.7261 °2
0.076 °2
0.2592 °2
-
0.6543 °2
0.4532 °2
-
-
2.0416 °2
S
-0.0307 Å °
0.151 Å °
0.0273 Å °
-0.1218 Å °
-0.0273 Å °
0.0869 Å °
-0.1762 Å °
0.0261 Å °
0.0579 Å °
Refinement TLS group
Selection: ALL
+
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