1M4B

Crystal Structure of Human Interleukin-2 K43C Covalently Modified at C43 with 2-[2-(2-Cyclohexyl-2-guanidino-acetylamino)-acetylamino]-N-(3-mercapto-propyl)-propionamide

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	7	298	pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystal Properties
Matthews coefficient	Solvent content
2.04	39.61

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 98.488	α = 90
b = 35.102	β = 97.52
c = 36.642	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	IMAGE PLATE	RIGAKU RAXIS IV	mirror	2000-12-18	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	ROTATING ANODE	RIGAKU	1.5418

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	2.13	10	97.5	0.067	0.067	12.7	4.9	6926	6926			33

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)
	2.13	2.21	78		0.34	0.34	6.7	3.8	558

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	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	2.15	10	6490	6490	320	99.37	0.24686	0.24686	0.24505	0.28584	RANDOM	36.291

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]
-0.76		-1.3	0.92		-0.5

RMS Deviations
Key	Refinement Restraint Deviation
r_scangle_it	5.652
r_mcangle_it	5.481
r_scbond_it	3.558
r_mcbond_it	3.189
r_dihedral_angle_1_deg	1.92
r_angle_refined_deg	0.771
r_symmetry_hbond_refined	0.527
r_symmetry_vdw_refined	0.27
r_nbd_refined	0.224
r_xyhbond_nbd_refined	0.169

RMS Deviations
Key	Refinement Restraint Deviation
r_scangle_it	5.652
r_mcangle_it	5.481
r_scbond_it	3.558
r_mcbond_it	3.189
r_dihedral_angle_1_deg	1.92
r_angle_refined_deg	0.771
r_symmetry_hbond_refined	0.527
r_symmetry_vdw_refined	0.27
r_nbd_refined	0.224
r_xyhbond_nbd_refined	0.169
r_chiral_restr	0.059
r_bond_refined_d	0.004
r_gen_planes_refined	0.002

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	944
Nucleic Acid Atoms
Solvent Atoms	19
Heterogen Atoms	27

Software

Software
Software Name	Purpose
d*TREK	data reduction
AMoRE	phasing
REFMAC	refinement
d*TREK	data scaling

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.