1EIB

CRYSTAL STRUCTURE OF CHITINASE A MUTANT D313A COMPLEXED WITH OCTA-N-ACETYLCHITOOCTAOSE (NAG)8.

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	7.2	291	0.75 M CITRATE-NA PH 7.2 AND 20% (V/V) METHANOL , VAPOR DIFFUSION, HANGING DROP, temperature 291K

Crystal Properties
Matthews coefficient	Solvent content
3.2	61.5

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 201.602	α = 90
b = 132.171	β = 90
c = 59.529	γ = 90

Symmetry
Space Group	C 2 2 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	IMAGE PLATE	MARRESEARCH	Rh coated pre-mirror and segmented, bent mirror	1999-04-04	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	EMBL/DESY, HAMBURG BEAMLINE BW7B		EMBL/DESY, HAMBURG	BW7B

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	1.8	10	97.7	0.034	24.4	3.7	71855	71855			20.1

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	1.8	1.86	99		0.147	7.7	3.4	7198

Refinement

Statistics
Diffraction ID	Structure Solution 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	1edq	1.8	10	71821	71821	3612	97.7	0.18	0.18	0.178	0.217	RANDOM	26

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]

RMS Deviations
Key	Refinement Restraint Deviation
p_transverse_tor	24.7
p_staggered_tor	12.6
p_planar_tor	6.6
p_scangle_it	2.65
p_mcangle_it	1.9
p_scbond_it	1.81
p_mcbond_it	1.34
p_multtor_nbd	0.246
p_xyhbond_nbd	0.225
p_singtor_nbd	0.169

RMS Deviations
Key	Refinement Restraint Deviation
p_transverse_tor	24.7
p_staggered_tor	12.6
p_planar_tor	6.6
p_scangle_it	2.65
p_mcangle_it	1.9
p_scbond_it	1.81
p_mcbond_it	1.34
p_multtor_nbd	0.246
p_xyhbond_nbd	0.225
p_singtor_nbd	0.169
p_chiral_restr	0.12
p_planar_d	0.035
p_angle_d	0.026
p_bond_d	0.012
p_plane_restr	0.011
p_hb_or_metal_coord
p_xhyhbond_nbd

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	4134
Nucleic Acid Atoms
Solvent Atoms	863
Heterogen Atoms	113

Software

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

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.