1OS2

Ternary enzyme-product-inhibitor complexes of human MMP12

X-RAY DIFFRACTION

Starting Model(s)

Initial Refinement Model(s)
Type	Source	Accession Code	Details
experimental model	PDB	1JK3

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	8	298	Tris, PEG6000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K

Crystal Properties
Matthews coefficient	Solvent content
2.71	54.28

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 123.839	α = 90
b = 123.839	β = 90
c = 69.73	γ = 120

Symmetry
Space Group	P 31

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	MARRESEARCH	Si (111) mirrors	2002-12-09	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	ESRF BEAMLINE ID13	0.9322	ESRF	ID13

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (Observed)	R Sym 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	2.15	107	99.9	0.076	0.076	7.3	7.2	64964	64964			34

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	R-Sym I (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
	2.15	2.27	99.9		0.078	0.078	1.9	4.6	9418

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Starting model	Resolution (High)	Resolution (Low)	Number Reflections (All)	Number Reflections (Observed)	Number Reflections (R-Free)	Percent Reflections (Observed)	R-Factor (All)	R-Factor (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	MOLECULAR REPLACEMENT	THROUGHOUT	1JK3	2.15	69.01	61741	61741	3296	100	0.21455	0.21455	0.21153	0.27099	RANDOM	36.148

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]
-0.02	-0.01		-0.02		0.02

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_1_deg	9.963
r_scangle_it	6.14
r_scbond_it	4.425
r_angle_refined_deg	2.763
r_mcangle_it	2.718
r_mcbond_it	1.667
r_metal_ion_refined	0.482
r_symmetry_vdw_refined	0.452
r_nbd_refined	0.312
r_chiral_restr	0.233

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_1_deg	9.963
r_scangle_it	6.14
r_scbond_it	4.425
r_angle_refined_deg	2.763
r_mcangle_it	2.718
r_mcbond_it	1.667
r_metal_ion_refined	0.482
r_symmetry_vdw_refined	0.452
r_nbd_refined	0.312
r_chiral_restr	0.233
r_bond_refined_d	0.035
r_gen_planes_refined	0.014

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	7770
Nucleic Acid Atoms
Solvent Atoms	308
Heterogen Atoms	54

Software

Software
Software Name	Purpose
REFMAC	refinement
MOSFLM	data reduction
CCP4	data scaling
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.