2O0A | pdb_00002o0a

The structure of the C-terminal domain of Vik1 has a motor domain fold but lacks a nucleotide-binding site.

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	5.5	278	100 mM Na/MES/Acetate, pH 5.5, 24 % pentaerythritol ethoxylate (Mr 797), 300 mM NaCl, and 5% ethylene glycol, VAPOR DIFFUSION, HANGING DROP, temperature 278K

Crystal Properties
Matthews coefficient	Solvent content
1.88	34.59

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 46.524	α = 90
b = 70.129	β = 90
c = 79.861	γ = 90

Symmetry
Space Group	P 21 21 21

Diffraction

Diffraction Experiment
ID #	Crystal ID	Scattering Type	Data Collection Temperature	Detector	Detector Type	Details	Collection Date	Monochromator	Protocol
1	1	x-ray	100	CCD	CUSTOM-MADE		2005-11-20	M	MAD
2	1
3	1

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	APS BEAMLINE 19-BM	0.97885, 0.97885, 0.97896, 0.97118	APS	19-BM

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	1.55	50	99.3	0.05	13.3	6.3		38292			28.7

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)
	1.55	1.61	98.8		0.317		5.4	3742

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 (Depositor)	R-Work (DCC)	R-Free (Depositor)	R-Free (DCC)	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	MAD	THROUGHOUT	1.6	50	34969	1759	99.35	0.212	0.21	0.21	0.261	0.26	RANDOM	22.427

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]
1.33			-0.34		-0.99

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	39.195
r_dihedral_angle_4_deg	16.013
r_dihedral_angle_3_deg	13.333
r_dihedral_angle_1_deg	6.035
r_scangle_it	2.407
r_scbond_it	1.617
r_mcangle_it	1.307
r_angle_refined_deg	1.204
r_mcbond_it	0.763
r_nbtor_refined	0.308

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	39.195
r_dihedral_angle_4_deg	16.013
r_dihedral_angle_3_deg	13.333
r_dihedral_angle_1_deg	6.035
r_scangle_it	2.407
r_scbond_it	1.617
r_mcangle_it	1.307
r_angle_refined_deg	1.204
r_mcbond_it	0.763
r_nbtor_refined	0.308
r_symmetry_vdw_refined	0.2
r_nbd_refined	0.195
r_xyhbond_nbd_refined	0.125
r_symmetry_hbond_refined	0.106
r_chiral_restr	0.081
r_bond_refined_d	0.009
r_gen_planes_refined	0.005

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2209
Nucleic Acid Atoms
Solvent Atoms	241
Heterogen Atoms	4

Software

Software
Software Name	Purpose
DENZO	data reduction
SCALEPACK	data scaling
SOLVE	phasing
RESOLVE	phasing
REFMAC	refinement
PDB_EXTRACT	data extraction
HKL-2000	data collection
HKL-2000	data reduction

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.