Experiment: 1P1R

X-RAY DIFFRACTION

Starting Model(s)

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

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1		7	277	MPD, 50 mM ammonium tris-[(hydroxymethyl)methyl]-2-aminosulfonate buffer, 0.25 mM EDTA, pH 7.0, dialysis, temperature 277K

Crystal Properties
Matthews coefficient	Solvent content
2.14	41.95

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 50.095	α = 90
b = 180.34	β = 106.36
c = 87	γ = 90

Symmetry
Space Group	P 1 21 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	MARRESEARCH		2001-12-09	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	APS BEAMLINE 17-ID	1.00	APS	17-ID

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	1.57	20	94.29	0.047	0.047	32.9	3.3	191371	191371	1		24.3

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R-Sym I (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
	1.57	1.63	79		0.2	5.2	2.8	16092

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Starting model	Resolution (High)	Resolution (Low)	Cut-off Sigma (I)	Number Reflections (All)	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	PDB ENTRY 1HLD	1.57	20	1	191371	191371	1159	94.29	0.1527	0.15243	0.19991	RANDOM	19.166

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]
1.96		0.08	-1.75		-0.17

RMS Deviations
Key	Refinement Restraint Deviation
r_sphericity_bonded	6.339
r_dihedral_angle_1_deg	5.932
r_sphericity_free	5.824
r_scangle_it	5.009
r_scbond_it	3.344
r_mcangle_it	2.094
r_angle_refined_deg	1.469
r_mcbond_it	1.319
r_rigid_bond_restr	1.301
r_nbd_refined	0.198

RMS Deviations
Key	Refinement Restraint Deviation
r_sphericity_bonded	6.339
r_dihedral_angle_1_deg	5.932
r_sphericity_free	5.824
r_scangle_it	5.009
r_scbond_it	3.344
r_mcangle_it	2.094
r_angle_refined_deg	1.469
r_mcbond_it	1.319
r_rigid_bond_restr	1.301
r_nbd_refined	0.198
r_symmetry_vdw_refined	0.18
r_symmetry_hbond_refined	0.141
r_xyhbond_nbd_refined	0.1
r_chiral_restr	0.096
r_bond_refined_d	0.014
r_gen_planes_refined	0.007

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	11140
Nucleic Acid Atoms
Solvent Atoms	1249
Heterogen Atoms	224

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.