THE FINAL STRUCTURES ARE BASED ON A TOTAL
OF 1022 CONFORMATIONALLY-RESTRICTING NOE-DERIVED DISTANCE
CONSTRAINTS, 68 DIHEDRAL ANGLE CONSTRAINTS, AND 48 HYDROGEN
BOND CONSTRAINTS (25.9 CONSTRAINTS PER RESIDUE, 4.4 LONG RANGE
CONSTRAINTS PER RESIDUE, COMPUTED FOR RESIDUES 1 TO 48 BY PSVS 1.3).
STRUCTURE DETERMINATION WAS PERFORMED ITERATIVELY USING CYANA 2.1.
THE 20 STRUCTURES OUT OF 100 WITH THE LOWEST TARGET FUNCTION WERE
FURTHER REFINED BY RESTRAINED MOLECULAR DYNAMICS/ENERGY
MINIMIZATION IN EXPLICIT WATER (CNS) WITH PARAM19.

THE PROTEIN IS MONOMERIC BY STATIC LIGHT SCATTERING.
THE STRUCTURE WAS DETERMINED USING TRIPLE RESONANCE NMR
SPECTROSCOPY. AUTOMATED BACKBONE ASSIGNMENTS WERE MADE USING
AUTOASSIGN, AND THE SIDE CHAIN ASSIGNMENTS WERE COMPLETED
MANUALLY. AUTOMATIC NOESY ASSIGNMENTS WERE DETERMINED USING
CYANA 2.1. DIHEDRAL ANGLE CONSTRAINTS WERE OBTAINED FROM
TALOS. HYDROGEN BOND CONSTRAINTS WERE DETERMINED USING BOTH
AUTOSTRUCTURE AND CYANA, AND WERE APPLIED ONLY IN THE FINAL
REFINEMENT STAGE (CNS) OF THE STRUCTURE DETERMINATION.
COMPLETENESS OF NMR ASSIGNMENTS (EXCLUDING C-TERMINAL
HHHHHH): BACKBONE, 98.8%, SIDE CHAIN, 96.9%, AROMATICS, 100%,
STEREOSPECIFIC METHYL, 100%, STEREOSPECIFIC SIDE CHAIN NH2:
100%. FINAL STRUCTURE QUALITY FACTORS (FOR RESIDUES 1 TO 48,
PSVS 1.3), WHERE ORDERED RESIDUES [S(PHI) + S(PSI) > 1.8]
COMPRISE: 2-38: (A) RMSD (ORDERED RESIDUES): BB, 0.4, HEAVY
ATOM, 0.9. (B) RAMACHANDRAN STATISTICS FOR ORDERED RESIDUES:
MOST FAVORED, 98.6%, ADDITIONALLY ALLOWED, 1.4%, GENEROUSLY
ALLOWED, 0.0%, DISALLOWED, 0.0%. (C) PROCHECK SCORES FOR
ORDERED RESIDUES (RAW/Z-): PHI-PSI, 0.53/2.40, ALL, 0.50/2.96.
(D) MOLPROBITY CLASH SCORE (RAW/Z-): 15.44/-1.12. (E) RPF
SCORES FOR GOODNESS OF FIT TO NOESY DATA (RESIDUES 1-48):
RECALL, 0.988, PRECISION, 0.944, F-MEASURE, 0.966, DP-SCORE,
0.822. (F) NUMBER OF CLOSE CONTACTS PER 20 MODELS: NONE. THE C-
TERMINAL HIS TAG RESIDUES OF THE PROTEIN (HHHHHH) WERE NOT
INCLUDED IN THE STRUCTURE CALCULATIONS AND HAVE BEEN OMITTED
FROM THIS DEPOSITION. COORDINATES FOR THE FOLLOWING RESIDUES
ARE NOT WELL DETERMINED [S(PHI) + S(PSI) < 1.8]: 1,39-48.

separate tube (no insert) not similar to the experimental sample tube

Solution NMR structure of the SOS response protein YnzC from Bacillus subtilis.

residues 1-46 of ynzC from Bacillus subtilis
C-terminal LEHHHHHH purification tag starting at residue 47.

Solution Nmr Structure Of The Upf0291 Protein Ynzc From Bacillus Subtilis. Northeast Structural Genomics Target Sr384

Solution Nmr Structure Of The Folded N-Terminal Fragment Of Upf0291 Protein Ynzc From Bacillus Subtilis. Northeast Structural G

hypothetical protein BSNT_08369 [Bacillus subtilis subsp. natto BEST195]

hypothetical protein BEST7613_3509 [Synechocystis sp. PCC 6803]

hypothetical protein BEST7003_1815 [Bacillus subtilis BEST7003]

hypothetical protein BSMD_034710 [Bacillus subtilis Miyagi-4]

conserved hypothetical protein [Bacillus subtilis subsp. subtilis str. 168]

hypothetical protein BSUBE1_1771 [Bacillus subtilis E1]

hypothetical protein BS49_19830 [Bacillus subtilis]

hypothetical protein BS34A_19820 [Bacillus sp.]

Uncharacterized protein conserved in bacteria [Streptococcus pneumoniae]

hypothetical protein BSn5_00270 [Bacillus subtilis BSn5]

conserved hypothetical protein [Bacillus subtilis subsp. spizizenii TU-B-10]

hypothetical protein I33_2000 [Bacillus subtilis subsp. subtilis str. RO-NN-1]

hypothetical protein MY9_1953 [Bacillus sp. JS]

hypothetical protein BSU17880 [Bacillus subtilis subsp. subtilis str. 168]

MULTISPECIES: hypothetical protein [Bacillus]

hypothetical protein [Bacillus vallismortis]

MULTISPECIES: hypothetical protein [Bacillales]

Solution NMR structure of the folded N-terminal fragment of UPF0291 protein ynzC from Bacillus subtilis. Northeast Structural Genomics target SR384-1-46.

2D 1H-13C HSQC stereospecific Leu/Val methyl

Northeast Structural Genomics Consortium

Chen, Arendall, Headd, Keedy, Immormino, Kapral, Murray, Richardson JS, Richardson DC

Zimmerman, Moseley, Kulikowski and Montelione

Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax

Tejero, Snyder, Mao, Aramini and Montelione

Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Thornton