1M46

CRYSTAL STRUCTURE OF MLC1P BOUND TO IQ4 OF MYO2P, A CLASS V MYOSIN

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	5.6	293	ammonium sulfate, potassium/sodium tartrate, sodium citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystal Properties
Matthews coefficient	Solvent content
2.21	44.25

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 48.504	α = 90
b = 121.504	β = 90
c = 29.082	γ = 90

Symmetry
Space Group	P 21 21 2

Diffraction

Diffraction Experiment
ID #	Crystal ID	Scattering Type	Data Collection Temperature	Detector	Detector Type	Details	Collection Date	Monochromator	Protocol
1	1	x-ray	293	IMAGE PLATE	MARRESEARCH	Charles Supper Double Mirror X-ray Focusing System	2000-07-01	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	ROTATING ANODE	RIGAKU RUH3R	1.5418

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (Observed)	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	2.103	45	99.7	0.075	15	10.4	10540	10540		-3

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
	2.103	2.18	98.5		0.36	4.2

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Resolution (High)	Resolution (Low)	Number Reflections (All)	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, Based on another structure of a mutant of MLC1P bound to IQ4 that crystallized in a different space group and was determined in the lab by the se-met mad method	THROUGHOUT	2.103	40	10035	10035	504	99.2	0.2013	0.19901	0.23895	RANDOM	36.784

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]
-0.56			0.24		0.32

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_3_deg	13.496
r_scangle_it	7.574
r_scbond_it	4.446
r_dihedral_angle_1_deg	3.993
r_mcangle_it	2.933
r_angle_refined_deg	1.817
r_mcbond_it	1.542
r_nbd_refined	0.227
r_symmetry_vdw_refined	0.226
r_xyhbond_nbd_refined	0.183

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_3_deg	13.496
r_scangle_it	7.574
r_scbond_it	4.446
r_dihedral_angle_1_deg	3.993
r_mcangle_it	2.933
r_angle_refined_deg	1.817
r_mcbond_it	1.542
r_nbd_refined	0.227
r_symmetry_vdw_refined	0.226
r_xyhbond_nbd_refined	0.183
r_symmetry_hbond_refined	0.149
r_chiral_restr	0.141
r_bond_refined_d	0.022
r_gen_planes_refined	0.009

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	1388
Nucleic Acid Atoms
Solvent Atoms	81
Heterogen Atoms

Software

Software
Software Name	Purpose
HKL-2000	data collection
SCALEPACK	data scaling
AMoRE	phasing
REFMAC	refinement
HKL-2000	data reduction

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.