1Y1K

Crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 T58A mutant

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	4.6	277	sodium citrate, isopropanol, PEG 2000, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystal Properties
Matthews coefficient	Solvent content
3.4	63.2

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 94.053	α = 90
b = 94.053	β = 90
c = 187.375	γ = 120

Symmetry
Space Group	P 65 2 2

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 4		2002-10-26	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	ALS BEAMLINE 8.3.1	1.000	ALS	8.3.1

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (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	1.56	81.65	99.5	0.07	13.9	5.6	69911	69911		-3

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	1TM3	1.56	81.65	69911	66395	3516	99.5	0.16532	0.16532	0.16428	0.1848	inherited from 1TM3	18.283

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]
0.27	0.14		0.27		-0.41

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_1_deg	5.72
r_scangle_it	4.52
r_scbond_it	2.752
r_angle_refined_deg	1.865
r_mcangle_it	1.657
r_mcbond_it	0.98
r_symmetry_vdw_refined	0.439
r_symmetry_hbond_refined	0.238
r_nbd_refined	0.21
r_xyhbond_nbd_refined	0.18

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_1_deg	5.72
r_scangle_it	4.52
r_scbond_it	2.752
r_angle_refined_deg	1.865
r_mcangle_it	1.657
r_mcbond_it	0.98
r_symmetry_vdw_refined	0.439
r_symmetry_hbond_refined	0.238
r_nbd_refined	0.21
r_xyhbond_nbd_refined	0.18
r_chiral_restr	0.136
r_metal_ion_refined	0.062
r_bond_refined_d	0.02
r_gen_planes_refined	0.008

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2563
Nucleic Acid Atoms
Solvent Atoms	499
Heterogen Atoms	81

Software

Software
Software Name	Purpose
MOSFLM	data reduction
SCALA	data scaling
TRUNCATE	data reduction
EPMR	phasing
REFMAC	refinement
CCP4	data scaling
TRUNCATE	data scaling

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.