5DDW

Crystal structure of aminotransferase CrmG from Actinoalloteichus sp. WH1-2216-6 in complex with the PMP external aldimine adduct with Caerulomycin M

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	8.5	293	0.2M Sodium acetate, 0.1M TRIS pH 8.5, 32% PEG3350, 2% glycerol

Crystal Properties
Matthews coefficient	Solvent content
2.39	48.6

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 83.788	α = 106.63
b = 83.687	β = 109.09
c = 88.052	γ = 95.07

Symmetry
Space Group	P 1

Diffraction

Diffraction Experiment
ID #	Crystal ID	Scattering Type	Data Collection Temperature	Detector	Detector Type	Details	Collection Date	Monochromator	Protocol
1	1	x-ray	100	PIXEL	DECTRIS PILATUS 6M		2015-06-22	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	SSRF BEAMLINE BL19U1	0.9785	SSRF	BL19U1

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (Observed)	Rpim I (All)	CC (Half)	Net I Over Average Sigma (I)	Redundancy	Number Reflections (All)	Number Reflections (Observed)	Observed Criterion Sigma (F)	Observed Criterion Sigma (I)	B (Isotropic) From Wilson Plot
1	2.3	49.25	92.2	0.152	0.074	0.988	8.1	4.6		86965

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	Rpim I (All)	CC (Half)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	2.3	2.34	87.5		0.555	0.296	0.76	2.5	4	4115

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Resolution (High)	Resolution (Low)	Number Reflections (Observed)	Number Reflections (R-Free)	Percent Reflections (Observed)	R-Factor (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	MOLECULAR REPLACEMENT	THROUGHOUT	2.3	49.25	82633	4323	92.21	0.2001	0.198	0.2393	RANDOM	27.183

Temperature Factor Modeling
Anisotropic B[1][1]	Anisotropic B[1][2]	Anisotropic B[1][3]	Anisotropic B[2][2]	Anisotropic B[2][3]	Anisotropic B[3][3]
0.32	0.15	0.08	0.1	-0.22	-0.22

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	34.374
r_dihedral_angle_4_deg	22.126
r_dihedral_angle_3_deg	17.754
r_dihedral_angle_1_deg	7.83
r_mcangle_it	4.51
r_mcbond_it	3.052
r_mcbond_other	3.052
r_angle_refined_deg	0.703
r_angle_other_deg	0.611
r_chiral_restr	0.065

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	34.374
r_dihedral_angle_4_deg	22.126
r_dihedral_angle_3_deg	17.754
r_dihedral_angle_1_deg	7.83
r_mcangle_it	4.51
r_mcbond_it	3.052
r_mcbond_other	3.052
r_angle_refined_deg	0.703
r_angle_other_deg	0.611
r_chiral_restr	0.065
r_bond_refined_d	0.014
r_gen_planes_refined	0.014
r_gen_planes_other	0.008
r_bond_other_d	0.004

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	15813
Nucleic Acid Atoms
Solvent Atoms	417
Heterogen Atoms	150

Software

Software
Software Name	Purpose
Aimless	data scaling
REFMAC	refinement
PDB_EXTRACT	data extraction
Aimless	data reduction
MOLREP	phasing

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.