Mass: 18.015 Da / Num. of mol.: 213 / Source method: isolated from a natural source / Formula: H2O
Sequence details
THE ENTRY CONTAINS AN ENGINEERED FUSION PROTEIN. THE TAND1 AND TAND2 REGION (8-71) OF TAF1 IS ...THE ENTRY CONTAINS AN ENGINEERED FUSION PROTEIN. THE TAND1 AND TAND2 REGION (8-71) OF TAF1 IS COVALENTLY LINKED VIA A PROTEIN LINKER (GGGSGGGSGGGS) TO TBP (61-240) IN ORDER TO ACCOMMODATE THESE IN THE SAME PDB CHAIN AN OFFSET OF 100 HAS BEEN APPLIED TO THE TBP RESIDUE NUMBERING AND SO THIS NOW RUNS FROM 161 TO 340 RATHER THAN 61 TO 240. OTHER_DETAILS: CONSTRUCTS CONTAIN RESIDUE: 8-71 MUTATIONS: G41A AND A42R, WHICH ARE DUE TO A CLONING ARTIFACT, RELATIVE TO THE UNIPROT ENTRY: P46677
-
Experimental details
-
Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
-
Sample preparation
Crystal
Density Matthews: 2.01 Å3/Da / Density % sol: 38.73 % / Description: NONE
Resolution: 1.97→59.54 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.9188 / SU R Cruickshank DPI: 0.159 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.176 / SU Rfree Blow DPI: 0.16 / SU Rfree Cruickshank DPI: 0.154 Details: REFINEMENT NOTE 1: IDEAL-DIST CONTACT SETUP. RESIDUE TYPES WITHOUT CCP4 ATOM TYPE IN LIBRARY=CL CA GOL. NUMBER OF ATOMS WITH PROPER CCP4 ATOM TYPE=2149. NUMBER WITH APPROX DEFAULT CCP4 ATOM ...Details: REFINEMENT NOTE 1: IDEAL-DIST CONTACT SETUP. RESIDUE TYPES WITHOUT CCP4 ATOM TYPE IN LIBRARY=CL CA GOL. NUMBER OF ATOMS WITH PROPER CCP4 ATOM TYPE=2149. NUMBER WITH APPROX DEFAULT CCP4 ATOM TYPE=37. NUMBER TREATED BY BAD NON- BONDED CONTACTS=3.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.223
888
4.97 %
RANDOM
Rwork
0.1644
-
-
-
obs
0.167
17873
99.36 %
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Displacement parameters
Biso mean: 28.39 Å2
Baniso -1
Baniso -2
Baniso -3
1-
-3.2727 Å2
0 Å2
0 Å2
2-
-
2.589 Å2
0 Å2
3-
-
-
0.6836 Å2
Refine analyze
Luzzati coordinate error obs: 0.18 Å
Refinement step
Cycle: LAST / Resolution: 1.97→59.54 Å
Protein
Nucleic acid
Ligand
Solvent
Total
Num. atoms
1851
0
40
213
2104
Refine LS restraints
Refine-ID
Type
Dev ideal
Number
Restraint function
Weight
X-RAY DIFFRACTION
t_bond_d
0.01
2008
HARMONIC
2
X-RAY DIFFRACTION
t_angle_deg
1.02
2710
HARMONIC
2
X-RAY DIFFRACTION
t_dihedral_angle_d
949
SINUSOIDAL
2
X-RAY DIFFRACTION
t_incorr_chiral_ct
X-RAY DIFFRACTION
t_pseud_angle
X-RAY DIFFRACTION
t_trig_c_planes
49
HARMONIC
2
X-RAY DIFFRACTION
t_gen_planes
295
HARMONIC
5
X-RAY DIFFRACTION
t_it
2008
HARMONIC
20
X-RAY DIFFRACTION
t_nbd
2
SEMIHARMONIC
5
X-RAY DIFFRACTION
t_omega_torsion
3.5
X-RAY DIFFRACTION
t_other_torsion
2.63
X-RAY DIFFRACTION
t_improper_torsion
X-RAY DIFFRACTION
t_chiral_improper_torsion
262
SEMIHARMONIC
5
X-RAY DIFFRACTION
t_sum_occupancies
X-RAY DIFFRACTION
t_utility_distance
X-RAY DIFFRACTION
t_utility_angle
X-RAY DIFFRACTION
t_utility_torsion
X-RAY DIFFRACTION
t_ideal_dist_contact
2561
SEMIHARMONIC
4
LS refinement shell
Resolution: 1.97→2.09 Å / Total num. of bins used: 9
Rfactor
Num. reflection
% reflection
Rfree
0.221
127
4.53 %
Rwork
0.1851
2678
-
all
0.1868
2805
-
obs
-
-
99.36 %
+
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