1OY7

Structure and Function Analysis of Peptide Antagonists of Melanoma Inhibitor of Apoptosis (ML-IAP)

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	5	298	sodium acetate, PEG 300, DTT , pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K

Crystal Properties
Matthews coefficient	Solvent content
3.1	60.05

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 83.878	α = 90
b = 83.878	β = 90
c = 94.34	γ = 120

Symmetry
Space Group	P 32

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	double crystal Si 111 monochromator	2002-05-02	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	SSRL BEAMLINE BL1-5	1.033	SSRL	BL1-5

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (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	2.7	30	99.8	0.141	0.141	8	2.1	20337	20139			53.112

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	R-Sym I (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	2.7	2.8	99.4		0.35	0.35	2	2.1	2035

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	FOURIER SYNTHESIS	THROUGHOUT	PDB ENTRY 1OXN	2.7	20	19324	19096	979	98.82	0.155	0.1553	0.15243	0.21134	copied from test set for 1OXN	44.175

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]
0.66	0.33		0.66		-1

RMS Deviations
Key	Refinement Restraint Deviation
r_scangle_it	6.421
r_mcangle_it	5.379
r_dihedral_angle_1_deg	5.141
r_scbond_it	3.908
r_mcbond_it	3.057
r_angle_refined_deg	1.079
r_nbd_refined	0.21
r_symmetry_vdw_refined	0.18
r_symmetry_hbond_refined	0.18
r_xyhbond_nbd_refined	0.15

RMS Deviations
Key	Refinement Restraint Deviation
r_scangle_it	6.421
r_mcangle_it	5.379
r_dihedral_angle_1_deg	5.141
r_scbond_it	3.908
r_mcbond_it	3.057
r_angle_refined_deg	1.079
r_nbd_refined	0.21
r_symmetry_vdw_refined	0.18
r_symmetry_hbond_refined	0.18
r_xyhbond_nbd_refined	0.15
r_chiral_restr	0.081
r_bond_refined_d	0.008
r_gen_planes_refined	0.004

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	3980
Nucleic Acid Atoms
Solvent Atoms	403
Heterogen Atoms	27

Software

Software
Software Name	Purpose
REFMAC	refinement
HKL-2000	data reduction
SCALEPACK	data scaling
CNS	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.