5HZN

Structure of NVP-AEW541 in complex with IGF-1R kinase

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	6.25	293	25% PEG8000, 0.1M MES PH6.25, 0.2 M AMMONIUM SULFATE, 4% GLYCEROL

Crystal Properties
Matthews coefficient	Solvent content
2.97	58.63

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 111.435	α = 90
b = 190.045	β = 90.22
c = 155.488	γ = 90

Symmetry
Space Group	C 1 2 1

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		2003-06-16	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	SLS BEAMLINE X06SA	0.97779	SLS	X06SA

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	2.2	40	90.9	0.078	9.8	3.5		147785

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	2.2	2.28	78.5		0.413

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Resolution (High)	Resolution (Low)	Number Reflections (Observed)	Number Reflections (R-Free)	Percent Reflections (Observed)	R-Factor (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	MOLECULAR REPLACEMENT	THROUGHOUT	2.2	30	140330	7403	90.62	0.1952	0.194	0.2178	RANDOM	45.611

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]
-1.08		0.05	2.95		-1.86

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	33.32
r_dihedral_angle_4_deg	21.621
r_dihedral_angle_3_deg	15.003
r_dihedral_angle_1_deg	6.148
r_scangle_it	3.445
r_scbond_it	2.227
r_angle_refined_deg	1.786
r_mcangle_it	1.712
r_mcbond_it	1.072
r_symmetry_vdw_refined	0.221

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	33.32
r_dihedral_angle_4_deg	21.621
r_dihedral_angle_3_deg	15.003
r_dihedral_angle_1_deg	6.148
r_scangle_it	3.445
r_scbond_it	2.227
r_angle_refined_deg	1.786
r_mcangle_it	1.712
r_mcbond_it	1.072
r_symmetry_vdw_refined	0.221
r_nbd_refined	0.2
r_xyhbond_nbd_refined	0.146
r_symmetry_hbond_refined	0.146
r_chiral_restr	0.083
r_bond_refined_d	0.013
r_gen_planes_refined	0.005

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	18975
Nucleic Acid Atoms
Solvent Atoms	551
Heterogen Atoms	380

Software

Software
Software Name	Purpose
DENZO	data reduction
SCALEPACK	data scaling
REFMAC	refinement
PDB_EXTRACT	data extraction
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.