2ILN

Crystal structure of the Bowman-Birk inhibitor from snail medic seeds in complex with bovine trypsin

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	7.5	298	1.5M lithium sulphate, 0.1M Hepes, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298.0K

Crystal Properties
Matthews coefficient	Solvent content
2.49	50.63

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 54.47	α = 90
b = 54.47	β = 90
c = 180.08	γ = 90

Symmetry
Space Group	P 41

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	MAR CCD 165 mm	Mirrors: Three-segment Pt-coated toroidal	2004-02-05	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	ELETTRA BEAMLINE 5.2R	1.00	ELETTRA	5.2R

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	2	30	95.8	0.093	4	2.4	34060	33730	1	1

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R-Sym I (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
	2	2.05	97.5		0.28	2.4	2.4	2479

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	PDB ENTRY 1D6R	2	25	31992	31992	1680	95.62	0.2348	0.2348	0.23194	0.28686	RANDOM	29.668

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]
2.38			2.38		-4.76

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	40.597
r_dihedral_angle_3_deg	14.799
r_dihedral_angle_4_deg	12.559
r_dihedral_angle_1_deg	6.43
r_scangle_it	2.13
r_scbond_it	1.37
r_angle_refined_deg	1.356
r_mcangle_it	0.967
r_mcbond_it	0.552
r_nbtor_refined	0.301

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	40.597
r_dihedral_angle_3_deg	14.799
r_dihedral_angle_4_deg	12.559
r_dihedral_angle_1_deg	6.43
r_scangle_it	2.13
r_scbond_it	1.37
r_angle_refined_deg	1.356
r_mcangle_it	0.967
r_mcbond_it	0.552
r_nbtor_refined	0.301
r_symmetry_hbond_refined	0.249
r_symmetry_vdw_refined	0.223
r_nbd_refined	0.202
r_xyhbond_nbd_refined	0.173
r_chiral_restr	0.097
r_bond_refined_d	0.009
r_gen_planes_refined	0.004

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	3669
Nucleic Acid Atoms
Solvent Atoms	376
Heterogen Atoms

Software

Software
Software Name	Purpose
REFMAC	refinement
MAR345	data collection
MOSFLM	data reduction
CCP4	data scaling
MOLREP	phasing

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.