SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 30-STRANDED BARREL THIS IS REPRESENTED BY A 31-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.
PROTEINHFQ / HOST FACTOR-I PROTEIN / HF-I / HFQ PROTEIN
Mass: 8257.572 Da / Num. of mol.: 6 / Fragment: RESIDUES 1-72 Source method: isolated from a genetically manipulated source Details: THE SEQUENCE IS PRECEDED BY A GA TAG REMAINING FROM THE PURIFICATION TAG. Source: (gene. exp.) SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHIMURIUM (bacteria) Strain: LT2 / Plasmid: PET M60 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3)GOLD / References: UniProt: P0A1R0
Resolution: 1.15→18.84 Å / SU ML: 0.12 / σ(F): 1.99 / Phase error: 21.88 / Stereochemistry target values: ML Details: HYDROGENS WERE REFINED IN THE RIDING POSITIONS. B FACTORS WERE REFINED ANISOTROPICALLY FOR NON-HYDROGEN ATOMS. THE FOLLOWING RESIDUES WERE MODELED AS DOUBLE CONFORMATIONS. CHAIN A, RESIDUES ...Details: HYDROGENS WERE REFINED IN THE RIDING POSITIONS. B FACTORS WERE REFINED ANISOTROPICALLY FOR NON-HYDROGEN ATOMS. THE FOLLOWING RESIDUES WERE MODELED AS DOUBLE CONFORMATIONS. CHAIN A, RESIDUES 60, 66. CHAIN B, RESIDUES 17, 19, 36, 38, 60, 66. CHAIN C, RESIDUES 17, 38, 60, 61, 66. CHAIN D, RESIDUES 13, 36. CHAIN E, RESIDUES 36, 66. CHAIN F, RESIDUE 61.THE FOLLOWING RESIDUES ARE DISORDERED. CHAIN A, RESIDUES 1 TO 5, 71 TO 72. CHAIN B, RESIDUES 1 TO 6, 72. CHAIN C, RESIDUES 1 TO 3, 72. CHAIN D, RESIDUES 1 TO 3, 72. CHAIN E, RESIDUES 1 TO 3, 72. CHAIN F, RESIDUES 1 TO 5, 72.
Rfactor
Num. reflection
% reflection
Rfree
0.2076
6171
5 %
Rwork
0.1682
-
-
obs
0.1701
123284
98 %
Solvent computation
Shrinkage radii: 0.89 Å / VDW probe radii: 1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 45.557 Å2 / ksol: 0.461 e/Å3
Displacement parameters
Biso mean: 15.6 Å2
Baniso -1
Baniso -2
Baniso -3
1-
0.3713 Å2
0 Å2
0 Å2
2-
-
0.3713 Å2
0 Å2
3-
-
-
-0.7426 Å2
Refinement step
Cycle: LAST / Resolution: 1.15→18.84 Å
Protein
Nucleic acid
Ligand
Solvent
Total
Num. atoms
3203
0
0
376
3579
Refine LS restraints
Refine-ID
Type
Dev ideal
Number
X-RAY DIFFRACTION
f_bond_d
0.015
3423
X-RAY DIFFRACTION
f_angle_d
1.614
4665
X-RAY DIFFRACTION
f_dihedral_angle_d
13.238
1313
X-RAY DIFFRACTION
f_chiral_restr
0.093
546
X-RAY DIFFRACTION
f_plane_restr
0.008
602
LS refinement shell
Resolution (Å)
Rfactor Rfree
Num. reflection Rfree
Rfactor Rwork
Num. reflection Rwork
Refine-ID
% reflection obs (%)
1.15-1.1911
0.2972
577
0.2446
11634
X-RAY DIFFRACTION
97
1.1911-1.2388
0.2753
642
0.2311
11717
X-RAY DIFFRACTION
98
1.2388-1.2952
0.2549
622
0.2104
11826
X-RAY DIFFRACTION
99
1.2952-1.3634
0.2472
639
0.1918
11847
X-RAY DIFFRACTION
99
1.3634-1.4488
0.2262
636
0.174
11760
X-RAY DIFFRACTION
99
1.4488-1.5606
0.2047
630
0.1559
11819
X-RAY DIFFRACTION
99
1.5606-1.7176
0.1998
625
0.1445
11725
X-RAY DIFFRACTION
98
1.7176-1.9659
0.1734
625
0.137
11735
X-RAY DIFFRACTION
98
1.9659-2.4759
0.1659
569
0.1373
11668
X-RAY DIFFRACTION
97
2.4759-18.8425
0.2028
606
0.1722
11382
X-RAY DIFFRACTION
95
+
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