Parkincoregulatedgeneprotein / Molecular chaperone/chaperonin-binding protein / PARK2 coregulated gene protein
Mass: 22298.510 Da / Num. of mol.: 1 / Mutation: Deletion 1-69, Y189PHI Source method: isolated from a genetically manipulated source Details: Generated from GST-fusion, and cleaved with 3C protease, leaving a GPLGS linker at N-terminus. Tyrosine 189 was mutated in Iodo-phenylalanine in order to incorporate anomalous scattering atom for phasing. Source: (gene. exp.) Homo sapiens (human) / Gene: PACRG, GLUP / Plasmid: pGEX-6P1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q96M98
#2: Protein
Meiosisexpressedgene1proteinhomolog
Mass: 11226.584 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: Full-length MEIG1 expressed as His-tagged protein, cleaved with the 3C protease, leaving GPLGS at N-terminus Source: (gene. exp.) Homo sapiens (human) / Gene: MEIG1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q5JSS6
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 1.476 Å / Relative weight: 1
Reflection
Resolution: 2.09→47.64 Å / Num. obs: 253322 / % possible obs: 99.8 % / Redundancy: 11.3 % / Biso Wilson estimate: 43.8362539878 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.093 / Net I/σ(I): 13.7
Reflection shell
Resolution: 2.09→2.16 Å / Redundancy: 5.6 % / Rmerge(I) obs: 1.1 / Mean I/σ(I) obs: 1.1 / Num. unique obs: 9944 / CC1/2: 0.73 / % possible all: 98.4
-
Processing
Software
Name
Version
Classification
PHENIX
1.12_2829
refinement
Aimless
1.12_2829
datascaling
PHENIX
phasing
XDS
datareduction
Coot
modelbuilding
Refinement
Method to determine structure: SAD / Resolution: 2.09762493085→47.6384909553 Å / SU ML: 0.281412881549 / Cross valid method: THROUGHOUT / σ(F): 0.360717156976 / Phase error: 31.4403924482
Rfactor
Num. reflection
% reflection
Rfree
0.249329110804
2049
5.0032964618 %
Rwork
0.228564071678
-
-
obs
0.22961406499
40953
99.5333576376 %
Solvent computation
Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parameters
Biso mean: 51.9849979618 Å2
Refinement step
Cycle: LAST / Resolution: 2.09762493085→47.6384909553 Å
Protein
Nucleic acid
Ligand
Solvent
Total
Num. atoms
2076
0
6
74
2156
Refine LS restraints
Refine-ID
Type
Dev ideal
Number
X-RAY DIFFRACTION
f_bond_d
0.00889166363015
2133
X-RAY DIFFRACTION
f_angle_d
0.953075500496
2890
X-RAY DIFFRACTION
f_chiral_restr
0.290988541613
308
X-RAY DIFFRACTION
f_plane_restr
0.0052816449021
370
X-RAY DIFFRACTION
f_dihedral_angle_d
22.0427649872
777
LS refinement shell
Resolution (Å)
Rfactor Rfree
Num. reflection Rfree
Rfactor Rwork
Num. reflection Rwork
Refine-ID
% reflection obs (%)
2.0976-2.1464
0.339561060626
118
0.359188774491
2520
X-RAY DIFFRACTION
96.242247355
2.1464-2.2001
0.429172341276
137
0.357147146876
2596
X-RAY DIFFRACTION
99.4541484716
2.2001-2.2596
0.362775315843
116
0.346351450143
2604
X-RAY DIFFRACTION
99.1615020051
2.2596-2.3261
0.433628316844
131
0.316357362288
2601
X-RAY DIFFRACTION
98.8780311256
2.3261-2.4011
0.329031893152
126
0.317255257238
2584
X-RAY DIFFRACTION
99.7056659308
2.4011-2.487
0.319466843057
167
0.294782622689
2585
X-RAY DIFFRACTION
99.891107078
2.487-2.5865
0.35254831006
140
0.299751321923
2629
X-RAY DIFFRACTION
100
2.5865-2.7042
0.236786253844
141
0.280729503231
2566
X-RAY DIFFRACTION
99.9630723781
2.7042-2.8468
0.335419632359
144
0.264875329891
2593
X-RAY DIFFRACTION
99.9634769905
2.8468-3.0251
0.255377736014
148
0.252922437418
2594
X-RAY DIFFRACTION
100
3.0251-3.2586
0.279455172176
140
0.243464394683
2597
X-RAY DIFFRACTION
99.9634769905
3.2586-3.5865
0.252521693826
154
0.215940177404
2592
X-RAY DIFFRACTION
99.9272197962
3.5865-4.1052
0.193787365158
120
0.191945469514
2622
X-RAY DIFFRACTION
100
4.1052-5.1711
0.168158408892
118
0.171341384536
2637
X-RAY DIFFRACTION
100
5.1711-47.6508
0.215311476066
149
0.196982947345
2584
X-RAY DIFFRACTION
99.8538545853
+
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