1LV3

Solution NMR Structure of Zinc Finger Protein yacG from Escherichia coli. Northeast Structural Genomics Consortium Target ET92.

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	4D_13C-separated_NOESY	2mM YacG U-15N, 450 mM NaCl, 25 mM Na2HPO4, 10 mM DTT	90% H2O/10% D2O	450 mM salt, 25 mM phosphate buffer	6.5	ambient	298
2	3D_13C-separated_NOESY	2mM YacG U-15N, 450 mM NaCl, 25 mM Na2HPO4, 10 mM DTT	90% H2O/10% D2O	450 mM salt, 25 mM phosphate buffer	6.5	ambient	298
3	3D_15N-separated_NOESY	2mM YacG U-15N, 450 mM NaCl, 25 mM Na2HPO4, 10 mM DTT	90% H2O/10% D2O	450 mM salt, 25 mM phosphate buffer	6.5	ambient	298
4	HNHA	2mM YacG U-15N, 450 mM NaCl, 25 mM Na2HPO4, 10 mM DTT	90% H2O/10% D2O	450 mM salt, 25 mM phosphate buffer	6.5	ambient	298
5	2H_exchange	2mM YacG U-15N, 450 mM NaCl, 25 mM Na2HPO4, 10 mM DTT	90% H2O/10% D2O	450 mM salt, 25 mM phosphate buffer	6.5	ambient	298

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Varian	INOVA	600
2	Varian	INOVA	750
3	Varian	INOVA	800

NMR Refinement
Method	Details	Software
distance geometry and simulated annealing	THE STRUCTURES ARE BASED ON A TOTAL OF 396 RESTRAINTS. SUMMARY OF EXPERIMENTAL CONSTRAINTS: DISTANCE CONSTRAINTS: TOTAL = 367; ZN RESTRAINTS 10; INTRA-RESIDUE [I=J] = 93; SEQUENTIAL [(I-J)=1] = 120; MEDIUM RANGE [1<(I-J)<5] = 52; LONG RANGE [(I-J)>=5] = 86; NUMBER OF DISTANCE CONSTRAINTS PER RESIDUE (RESIDUES 4-40)= 9.8; DIHEDRAL-ANGLE CONSTRAINTS = 29 (16 PHI, 13 PSI); TOTAL HYDROGEN BOND CONSTRAINTS = 6 (2 PER H-BOND); TOTAL NUMBER OF CONSTRAINTS PER RESIDUE (4-40)= 10.6; NUMBER OF LONG RANGE CONSTRAINTS PER RESIDUE = 2.6; NUMBER OF STRUCTURES COMPUTED = 40; NUMBER OF STRUCTURES USED = 20. AVERAGE RESIDUAL CONSTRAINT VIOLATIONS: DISTANCE VIOLATIONS >0.0 ANG = 20. AVERAGE R.M.S. DISTANCE VIOLATION = 0.011 ANG. MAXIMUM NUMBER OF DISTANCE VIOLATIONS 26. AVERAGE DIHEDRAL ANGLE VIOLATIONS: >0 DEG = 0.8; MAX NUMBER OF ANGLE VIOLATION = 2 DEG; AVERAGE R.M.S. ANGLE VIOLATION = 0.11 DEG. RMSD VALUES: BACKBONE ATOMS (N,C,C') OF RESIDUES (4-40) = 0.46 ANG; BACKBONE ATOMS(N,C,C') OF SECONDARY STRUCTURE RESIDUES (6-17, 30-37) = 0.22 ANG; ALL HEAVY ATOMS OF RESIDUES (4-40) = 1.01 ANG; ALL HEAVY ATOMS OF SECONDARY STRUCTURE RESIDUES = 0.77 ANG. PROCHECK USING RESIDUES (4-40): MOST FAVORED REGIONS = 76%; ADDITIONAL ALLOWED REGIONS = 16%; GENEROUSLY ALLOWED REGIONS = 4%; DISALLOWED REGIONS = 4%. PROCHECK USING SECONDARY STRUCTURE RESIDUES (6-17, 30-37): MOST FAVOREDREGIONS = 95%; ADDITIONAL ALLOWED REGIONS = 5%; GENEROUSLY ALLOWED REGIONS =0%; DISALLOWED REGIONS = 0%.	X-PLOR

NMR Ensemble Information
Conformer Selection Criteria	structures with favorable non-bond energy
Conformers Calculated Total Number	40
Conformers Submitted Total Number	20
Representative Model	1 (closest to the average)

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	structure solution	X-PLOR	3.84
2	processing	Felix	98
3	collection	VNMR
4	data analysis	Sparky
5	refinement	X-PLOR	3.84	Brunger, A.T.

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.