Arachidonate production from DAG / acylglycerol catabolic process / Acyl chain remodeling of DAG and TAG / acylglycerol lipase / monoacylglycerol catabolic process / triglyceride catabolic process / regulation of endocannabinoid signaling pathway / monoacylglycerol lipase activity / arachidonic acid metabolic process / regulation of sensory perception of pain ...Arachidonate production from DAG / acylglycerol catabolic process / Acyl chain remodeling of DAG and TAG / acylglycerol lipase / monoacylglycerol catabolic process / triglyceride catabolic process / regulation of endocannabinoid signaling pathway / monoacylglycerol lipase activity / arachidonic acid metabolic process / regulation of sensory perception of pain / lysophospholipase activity / Triglyceride catabolism / regulation of signal transduction / lipid metabolic process / fatty acid biosynthetic process / regulation of inflammatory response / inflammatory response / endoplasmic reticulum membrane / protein homodimerization activity / membrane / plasma membrane / cytosol Similarity search - Function
Resolution: 2.2→2.3 Å / % possible obs: 86 % / Redundancy: 4.5 % / Mean I/σ(I) obs: 3.86 / Num. measured obs: 4066 / Rsym value: 0.4 / % possible all: 86.3
-
Processing
Software
Name
Version
Classification
REFMAC
5.2.0019
refinement
ADSC
Quantum
datacollection
XDS
datareduction
XSCALE
datascaling
PHASER
phasing
Refinement
Method to determine structure: MOLECULAR REPLACEMENT Starting model: a partial/incomplete model of PDB entries obtained by other methods Resolution: 2.2→43.02 Å / Cor.coef. Fo:Fc: 0.946 / Cor.coef. Fo:Fc free: 0.928 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.228 / ESU R Free: 0.187 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.22889
1896
5 %
RANDOM
Rwork
0.19207
-
-
-
obs
0.19392
35779
97.93 %
-
all
-
37675
-
-
Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parameters
Biso mean: 31.203 Å2
Baniso -1
Baniso -2
Baniso -3
1-
0.87 Å2
0 Å2
0 Å2
2-
-
-1.35 Å2
0 Å2
3-
-
-
0.48 Å2
Refinement step
Cycle: LAST / Resolution: 2.2→43.02 Å
Protein
Nucleic acid
Ligand
Solvent
Total
Num. atoms
4516
0
12
177
4705
Refine LS restraints
Refine-ID
Type
Dev ideal
Dev ideal target
Number
X-RAY DIFFRACTION
r_bond_refined_d
0.021
0.022
4622
X-RAY DIFFRACTION
r_angle_refined_deg
1.839
1.972
6277
X-RAY DIFFRACTION
r_dihedral_angle_1_deg
6.066
5
580
X-RAY DIFFRACTION
r_dihedral_angle_2_deg
28.037
23.438
192
X-RAY DIFFRACTION
r_dihedral_angle_3_deg
15.03
15
776
X-RAY DIFFRACTION
r_dihedral_angle_4_deg
13.805
15
28
X-RAY DIFFRACTION
r_chiral_restr
0.117
0.2
718
X-RAY DIFFRACTION
r_gen_planes_refined
0.013
0.021
3462
X-RAY DIFFRACTION
r_mcbond_it
1.065
1.5
2900
X-RAY DIFFRACTION
r_mcangle_it
1.93
2
4677
X-RAY DIFFRACTION
r_scbond_it
3.179
3
1722
X-RAY DIFFRACTION
r_scangle_it
4.774
4.5
1600
LS refinement shell
Resolution: 2.2→2.257 Å / Total num. of bins used: 20
Rfactor
Num. reflection
% reflection
Rfree
0.263
142
-
Rwork
0.227
2558
-
obs
-
-
96.5 %
+
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