2H5D

0.9A resolution crystal structure of alpha-lytic protease complexed with a transition state analogue, MeOSuc-Ala-Ala-Pro-Val boronic acid

X-RAY DIFFRACTION

Starting Model(s)

Initial Refinement Model(s)
Type	Source	Accession Code	Details
experimental model	PDB	1P02	SAME PROTEIN BOUND TO MEOSUC-ALA-ALA-PRO-ALA BORONIC ACID AT 0.9A RESOLUTION (UNPUBLISHED DATA, BUT RELATED TO 1P02)

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1		8	298	1.3M LITHIUM SULFATE, 0.02M TRIS, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K, pH 8.00

Crystal Properties
Matthews coefficient	Solvent content
2.44	49.6

Crystal Data

Unit Cell
Length ( ? )	Angle ( ? )
a = 65.768	�� = 90
b = 65.768	�� = 90
c = 79.554	�� = 120

Symmetry
Space Group	P 32 2 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	CCD	ADSC QUANTUM 315		2004-06-19	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	ALS BEAMLINE 8.2.2		ALS	8.2.2

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	0.9	28.5	99.9	0.085	27.9	8.7		147100

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	0.9	0.91	99.5		0.448	4.8	5.9

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Starting model	Resolution (High)	Resolution (Low)	Number Reflections (All)	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	REFINEMENT OF PREVIOUSLY-SOLVED STRUCTURE OF ALPHA-LYTIC PROTEASE BOUND TO MEOSUC-ALA-ALA-PRO-ALA BORONIC ACID	FREE R	SAME PROTEIN BOUND TO MEOSUC-ALA-ALA-PRO-ALA BORONIC ACID AT 0.9A RESOLUTION (UNPUBLISHED DATA, BUT RELATED TO 1P02)	0.9	20	146962	7352	99.9	0.081	0.08		0.091	RANDOM

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]

Coordinate Error
Structure Solution Method	Refinement High Resolution	Refinement Low Resolution
21	1367.28	1784.32

RMS Deviations
Key	Refinement Restraint Deviation
s_approx_iso_adps	0.086
s_zero_chiral_vol	0.081
s_non_zero_chiral_vol	0.07
s_angle_d	0.045
s_similar_adp_cmpnt	0.038
s_from_restr_planes	0.035
s_bond_d	0.016
s_rigid_bond_adp_cmpnt	0.005
s_similar_dist
s_anti_bump_dis_restr

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	1424
Nucleic Acid Atoms
Solvent Atoms	432
Heterogen Atoms	45

Software

Software
Software Name	Purpose
HKL-2000	data collection
SCALEPACK	data scaling
starting	model building
SHELXL-97	refinement
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.