Mass: 44187.148 Da / Num. of mol.: 1 / Fragment: RESIDUES 1-363 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Cell line (production host): High Five / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: Q9BT78
Mass: 18.015 Da / Num. of mol.: 336 / Source method: isolated from a natural source / Formula: H2O
Sequence details
CRYSTALLIZED WITH AN N-TERMINAL STREP(II) FUSION TAG
-
Experimental details
-
Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
-
Sample preparation
Crystal
Density Matthews: 3.03 Å3/Da / Density % sol: 0.59 % / Description: NONE
Crystal grow
Method: vapor diffusion / pH: 7.5 Details: 16 MG/ML PROTEIN IN 50 MM HEPES PH 7.4, 200 MM NACL, 2 MM DTT WAS MIXED EQUALLY WITH 100 MM HEPES PH 7.5, 4.3 M NACL. CRYSTALS WERE GROWN BY VAPOR DIFFUSION
Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 1 Å / Relative weight: 1
Reflection
Resolution: 1.6→32 Å / Num. obs: 69613 / % possible obs: 100 % / Observed criterion σ(I): -3 / Redundancy: 8.4 % / Biso Wilson estimate: 30.58 Å2 / Rmerge(I) obs: 0.05 / Net I/σ(I): 20.3
Reflection shell
Resolution: 1.6→1.61 Å / Redundancy: 8.5 % / Rmerge(I) obs: 1.35 / Mean I/σ(I) obs: 1.4 / % possible all: 100
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Processing
Software
Name
Version
Classification
BUSTER
2.11.5
refinement
XDS
datareduction
XDS
AIMLESS
datascaling
autoSHARP
phasing
Refinement
Method to determine structure: SIRAS Starting model: NONE Resolution: 1.6→31.76 Å / Cor.coef. Fo:Fc: 0.9601 / Cor.coef. Fo:Fc free: 0.9583 / SU R Cruickshank DPI: 0.078 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.069 / SU Rfree Blow DPI: 0.067 / SU Rfree Cruickshank DPI: 0.067 Details: IDEAL-DIST CONTACT TERM CONTACT SETUP. RESIDUE TYPES WITHOUT CCP4 ATOM TYPE IN LIBRARY=NA CL. NUMBER OF ATOMS WITH PROPER CCP4 ATOM TYPE=6343. NUMBER WITH APPROX DEFAULT CCP4 ATOM TYPE=0. ...Details: IDEAL-DIST CONTACT TERM CONTACT SETUP. RESIDUE TYPES WITHOUT CCP4 ATOM TYPE IN LIBRARY=NA CL. NUMBER OF ATOMS WITH PROPER CCP4 ATOM TYPE=6343. NUMBER WITH APPROX DEFAULT CCP4 ATOM TYPE=0. NUMBER TREATED BY BAD NON-BONDED CONTACTS=13. RESIDUES -24 TO -9 OF THE FUSION TAG AND RESIDUE 363 THE C-TERMINUS ARE DISORDERED
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.1929
3564
5.12 %
RANDOM
Rwork
0.1789
-
-
-
obs
0.1796
69593
99.98 %
-
Displacement parameters
Biso mean: 40.76 Å2
Baniso -1
Baniso -2
Baniso -3
1-
-3.7237 Å2
0 Å2
1.488 Å2
2-
-
-0.7194 Å2
0 Å2
3-
-
-
4.4431 Å2
Refine analyze
Luzzati coordinate error obs: 0.237 Å
Refinement step
Cycle: LAST / Resolution: 1.6→31.76 Å
Protein
Nucleic acid
Ligand
Solvent
Total
Num. atoms
2949
0
14
336
3299
Refine LS restraints
Refine-ID
Type
Dev ideal
Number
Restraint function
Weight
X-RAY DIFFRACTION
t_bond_d
0.01
6061
HARMONIC
2
X-RAY DIFFRACTION
t_angle_deg
0.98
10962
HARMONIC
2
X-RAY DIFFRACTION
t_dihedral_angle_d
1391
SINUSOIDAL
2
X-RAY DIFFRACTION
t_incorr_chiral_ct
X-RAY DIFFRACTION
t_pseud_angle
X-RAY DIFFRACTION
t_trig_c_planes
88
HARMONIC
2
X-RAY DIFFRACTION
t_gen_planes
915
HARMONIC
5
X-RAY DIFFRACTION
t_it
6061
HARMONIC
20
X-RAY DIFFRACTION
t_nbd
2
SEMIHARMONIC
5
X-RAY DIFFRACTION
t_omega_torsion
3.05
X-RAY DIFFRACTION
t_other_torsion
13.32
X-RAY DIFFRACTION
t_improper_torsion
X-RAY DIFFRACTION
t_chiral_improper_torsion
404
SEMIHARMONIC
5
X-RAY DIFFRACTION
t_sum_occupancies
8
HARMONIC
1
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
6677
SEMIHARMONIC
4
LS refinement shell
Resolution: 1.6→1.64 Å / Total num. of bins used: 20
Rfactor
Num. reflection
% reflection
Rfree
0.2192
218
4.24 %
Rwork
0.2143
4920
-
all
0.2145
5138
-
obs
-
-
99.98 %
Refinement TLS params.
Method: refined / Refine-ID: X-RAY DIFFRACTION
ID
L11 (°2)
L12 (°2)
L13 (°2)
L22 (°2)
L23 (°2)
L33 (°2)
S11 (Å °)
S12 (Å °)
S13 (Å °)
S21 (Å °)
S22 (Å °)
S23 (Å °)
S31 (Å °)
S32 (Å °)
S33 (Å °)
T11 (Å2)
T12 (Å2)
T13 (Å2)
T22 (Å2)
T23 (Å2)
T33 (Å2)
Origin x (Å)
Origin y (Å)
Origin z (Å)
1
10.1499
2.1574
-3.1244
0.5517
-1.692
-1.7275
-0.3696
0.621
0.0978
-0.007
0.506
-0.1589
0.1507
0.308
-0.1364
-0.2772
-0.1327
-0.0523
0.4966
-0.3254
-0.1892
-19.9205
6.4234
55.5244
2
7.8993
-0.7512
-1.0346
2.082
0.9422
5.7616
-0.2441
1.208
-0.0727
-0.1704
-0.3541
0.2295
0.0893
-1.3656
0.5981
-0.3057
-0.0474
-0.0585
0.2819
-0.2091
-0.1775
-10.2168
11.2808
57.2824
3
2.7754
-1.2874
-1.8168
1.5331
2.5145
6.7653
-0.1717
0.2992
-0.1017
-0.0606
-0.2517
0.2075
-0.1157
-0.695
0.4233
-0.1225
-0.0047
-0.0157
0.0156
-0.061
-0.0705
-6.0354
14.2962
69.1575
4
4.8186
-1.3322
-1.1315
2.8657
3.3876
6.9981
-0.0337
0.0542
-0.2172
0.0033
-0.0538
0.1256
0.2389
-0.1083
0.0875
-0.0435
0.034
-0.0052
-0.0652
-0.0264
-0.0866
-0.3907
16.323
81.1286
5
1.3508
0.2096
-0.0518
2.2145
0.9737
3.3501
0.0164
0.093
-0.125
-0.0846
0.0556
-0.1368
-0.1355
0.1727
-0.072
-0.0154
0.0006
-0.0038
-0.0249
-0.0323
-0.0407
5.6218
21.9538
87.4059
6
2.4531
1.7227
-1.4634
2.1249
-1.0469
2.5632
-0.1103
0.2045
-0.1444
-0.1398
0.0612
-0.1371
0.2448
0.0217
0.0491
-0.0193
0.0081
0.0103
-0.0748
-0.007
-0.0559
9.9626
32.6874
93.8427
7
1.6344
0.0823
-0.8913
1.0566
0.644
4.7554
0.1409
-0.0739
0.1772
-0.0118
-0.0001
-0.0233
-0.3908
0.2084
-0.1408
0.013
-0.0194
0.0119
-0.0659
-0.0012
-0.0357
9.9873
43.8118
103.8637
8
1.3748
0.7866
0.9275
1.8822
1.0998
5.5047
0.1845
-0.1614
0.1904
0.3097
-0.1561
0.2566
0.0143
-0.4681
-0.0285
-0.0661
0.0084
0.0562
-0.0726
-0.0192
-0.0485
-0.6564
40.9426
112.3003
9
4.0016
1.294
0.7251
0.6455
0.196
2.232
0.1003
-0.1042
0.2241
0.6169
-0.2138
0.177
0.6493
-0.3649
0.1136
0.0987
-0.0928
0.0592
-0.0632
-0.0533
-0.0404
0.1034
36.5604
126.8592
10
2.897
0.8354
2.7073
6.8727
3.5662
2.2841
0.166
-0.5213
-0.248
0.8264
0.0053
-0.2823
0.3164
0.0152
-0.1713
0.2597
-0.0404
-0.0046
-0.0989
0.0157
-0.069
6.0786
31.717
130.1022
Refinement TLS group
ID
Refine-ID
Refine TLS-ID
Selection details
1
X-RAY DIFFRACTION
1
{A|-8 - 18}
2
X-RAY DIFFRACTION
2
{A|19 - 58}
3
X-RAY DIFFRACTION
3
{A|59 - 116}
4
X-RAY DIFFRACTION
4
{A|117 - 140}
5
X-RAY DIFFRACTION
5
{A|141 - 180}
6
X-RAY DIFFRACTION
6
{A|181 - 218}
7
X-RAY DIFFRACTION
7
{A|219 - 268}
8
X-RAY DIFFRACTION
8
{A|269 - 315}
9
X-RAY DIFFRACTION
9
{A|316 - 344}
10
X-RAY DIFFRACTION
10
{A|345 - 362}
+
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