1Z32

Structure-function relationships in human salivary alpha-amylase: Role of aromatic residues

X-RAY DIFFRACTION

Starting Model(s)

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

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	9		MPD 40%, pH 9.0, VAPOR DIFFUSION, HANGING DROP

Crystal Properties
Matthews coefficient	Solvent content
2.17	42.85

Crystal Data

Unit Cell
Length ( ? )	Angle ( ? )
a = 51.657	�� = 90
b = 73.513	�� = 90
c = 134.362	�� = 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	ADSC QUANTUM 4		2002-04-01	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	CHESS BEAMLINE F1	0.91	CHESS	F1

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	1.6	42	90	0.059	29	3	59813	58813			20

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)
	1.6	1.66	94		0.21	8	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	1smd	1.6	19.84	58813	58813	3140	90.74	0.1919	0.1725	0.17144	0.1919	RANDOM	20.396

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]
-0.01					0.01

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_1_deg	5.965
r_scangle_it	2.481
r_scbond_it	1.571
r_angle_refined_deg	1.153
r_mcangle_it	1.024
r_mcbond_it	0.543
r_nbd_refined	0.195
r_symmetry_vdw_refined	0.157
r_symmetry_hbond_refined	0.133
r_xyhbond_nbd_refined	0.106

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_1_deg	5.965
r_scangle_it	2.481
r_scbond_it	1.571
r_angle_refined_deg	1.153
r_mcangle_it	1.024
r_mcbond_it	0.543
r_nbd_refined	0.195
r_symmetry_vdw_refined	0.157
r_symmetry_hbond_refined	0.133
r_xyhbond_nbd_refined	0.106
r_chiral_restr	0.087
r_metal_ion_refined	0.034
r_bond_refined_d	0.008
r_gen_planes_refined	0.005

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	3942
Nucleic Acid Atoms
Solvent Atoms	339
Heterogen Atoms	34

Software

Software
Software Name	Purpose
REFMAC	refinement
DENZO	data reduction
SCALEPACK	data scaling
AMoRE	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.