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- PDB-3aqd: Unliganded TRAP -

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Basic information

Entry
Database: PDB / ID: 3aqd
TitleUnliganded TRAP
ComponentsTranscription attenuation protein mtrB
KeywordsRNA BINDING PROTEIN / 11-fold symmetric ring / Control of tryptophan synthesis / Tryptophan and Anti-TRAP
Function / homology
Function and homology information


DNA-templated transcription termination / regulation of DNA-templated transcription / RNA binding / identical protein binding
Similarity search - Function
TRAP-like / Transcription attenuation protein MtrB / Tryptophan RNA-binding attenuator protein domain / Tryptophan RNA-binding attenuator protein / Tryptophan RNA-binding attenuator protein-like domain superfamily / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Transcription attenuation protein MtrB
Similarity search - Component
Biological speciesBacillus stearothermophilus (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.2 Å
AuthorsMalay, A.A.D. / Watanabe, M. / Heddle, J.G. / Tame, J.R.H.
CitationJournal: To be Published
Title: Allostery in TRAP
Authors: Malay, A.A.D. / Watanabe, M. / Heddle, J.G. / Tame, J.R.H.
History
DepositionOct 29, 2010Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Dec 29, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 1, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Transcription attenuation protein mtrB
B: Transcription attenuation protein mtrB
C: Transcription attenuation protein mtrB
D: Transcription attenuation protein mtrB
E: Transcription attenuation protein mtrB
F: Transcription attenuation protein mtrB
G: Transcription attenuation protein mtrB
H: Transcription attenuation protein mtrB
I: Transcription attenuation protein mtrB
J: Transcription attenuation protein mtrB
K: Transcription attenuation protein mtrB
L: Transcription attenuation protein mtrB
M: Transcription attenuation protein mtrB
N: Transcription attenuation protein mtrB
O: Transcription attenuation protein mtrB
P: Transcription attenuation protein mtrB
Q: Transcription attenuation protein mtrB
R: Transcription attenuation protein mtrB
S: Transcription attenuation protein mtrB
T: Transcription attenuation protein mtrB
U: Transcription attenuation protein mtrB
V: Transcription attenuation protein mtrB


Theoretical massNumber of molelcules
Total (without water)181,66222
Polymers181,66222
Non-polymers00
Water1267
1
A: Transcription attenuation protein mtrB
B: Transcription attenuation protein mtrB
C: Transcription attenuation protein mtrB
D: Transcription attenuation protein mtrB
E: Transcription attenuation protein mtrB
F: Transcription attenuation protein mtrB
G: Transcription attenuation protein mtrB
H: Transcription attenuation protein mtrB
I: Transcription attenuation protein mtrB
J: Transcription attenuation protein mtrB
K: Transcription attenuation protein mtrB


Theoretical massNumber of molelcules
Total (without water)90,83111
Polymers90,83111
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area20920 Å2
ΔGint-95 kcal/mol
Surface area28810 Å2
MethodPISA
2
L: Transcription attenuation protein mtrB
M: Transcription attenuation protein mtrB
N: Transcription attenuation protein mtrB
O: Transcription attenuation protein mtrB
P: Transcription attenuation protein mtrB
Q: Transcription attenuation protein mtrB
R: Transcription attenuation protein mtrB
S: Transcription attenuation protein mtrB
T: Transcription attenuation protein mtrB
U: Transcription attenuation protein mtrB
V: Transcription attenuation protein mtrB


Theoretical massNumber of molelcules
Total (without water)90,83111
Polymers90,83111
Non-polymers00
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area20940 Å2
ΔGint-94 kcal/mol
Surface area28590 Å2
MethodPISA
Unit cell
Length a, b, c (Å)68.154, 85.432, 127.444
Angle α, β, γ (deg.)90.00, 95.13, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
51E
61F
71G
81H
91I
101J
111K
121L
131M
141N
151O
161P
171Q
181R
191S
201T
211U
221V

NCS domain segments:

Component-ID: 1 / Ens-ID: 1 / Refine code: 2

Dom-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
1SERSERLYSLYSAA7 - 755 - 73
2SERSERLYSLYSBB7 - 755 - 73
3SERSERGLYGLYCC7 - 745 - 72
4SERSERGLYGLYDD7 - 745 - 72
5SERSERLYSLYSEE7 - 755 - 73
6SERSERGLYGLYFF7 - 745 - 72
7ASNASNGLYGLYGG6 - 744 - 72
8ASNASNGLYGLYHH6 - 744 - 72
9SERSERGLUGLUII7 - 735 - 71
10SERSERGLYGLYJJ7 - 745 - 72
11SERSERGLYGLYKK7 - 745 - 72
12SERSERGLYGLYLL7 - 745 - 72
13SERSERGLYGLYMM7 - 745 - 72
14SERSERGLYGLYNN7 - 745 - 72
15SERSERGLYGLYOO7 - 745 - 72
16SERSERLYSLYSPP7 - 755 - 73
17SERSERGLUGLUQQ7 - 735 - 71
18SERSERGLUGLURR7 - 735 - 71
19ASNASNGLYGLYSS6 - 744 - 72
20SERSERGLYGLYTT7 - 745 - 72
21SERSERLYSLYSUU7 - 755 - 73
22SERSERLYSLYSVV7 - 755 - 73

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Components

#1: Protein ...
Transcription attenuation protein mtrB / Trp RNA-binding attenuation protein / TRAP / Tryptophan RNA-binding attenuator protein


Mass: 8257.377 Da / Num. of mol.: 22
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacillus stearothermophilus (bacteria) / Gene: mtrB / Production host: Escherichia coli (E. coli) / References: UniProt: Q9X6J6
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 7 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.03 Å3/Da / Density % sol: 39.53 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 25% PEG 400, 0.2M calcium chloride, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Photon Factory / Beamline: BL-17A / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 270 / Detector: CCD
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.1→50 Å / Num. all: 24780 / Num. obs: 23417 / % possible obs: 94.5 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 3.4 % / Rmerge(I) obs: 0.082 / Net I/σ(I): 10.3

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHASERphasing
REFMAC5.5.0109refinement
HKL-2000data reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1QAW
Resolution: 3.2→20 Å / Cor.coef. Fo:Fc: 0.898 / Cor.coef. Fo:Fc free: 0.866 / SU B: 62.6 / SU ML: 0.484 / Cross valid method: THROUGHOUT / ESU R Free: 0.615 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES: WITH TLS ADDED
RfactorNum. reflection% reflectionSelection details
Rfree0.2674 1174 5.1 %RANDOM
Rwork0.2384 ---
obs0.2399 22011 95.94 %-
all-22942 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso max: 130.87 Å2 / Biso mean: 68.0068 Å2 / Biso min: 3.14 Å2
Baniso -1Baniso -2Baniso -3
1--0.31 Å2-0 Å20.07 Å2
2--0.1 Å20 Å2
3---0.22 Å2
Refinement stepCycle: LAST / Resolution: 3.2→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10662 0 0 7 10669
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0120.02110789
X-RAY DIFFRACTIONr_angle_refined_deg1.3211.93114496
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.33751351
X-RAY DIFFRACTIONr_dihedral_angle_2_deg30.85624.318491
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.803151895
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.6551555
X-RAY DIFFRACTIONr_chiral_restr0.0830.21716
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.027865
X-RAY DIFFRACTIONr_mcbond_it1.6491.56783
X-RAY DIFFRACTIONr_mcangle_it3.097210858
X-RAY DIFFRACTIONr_scbond_it2.28634006
X-RAY DIFFRACTIONr_scangle_it4.0224.53638
Refine LS restraints NCS

Ens-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Dom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A232TIGHT POSITIONAL0.040.05
2B232TIGHT POSITIONAL0.040.05
3C232TIGHT POSITIONAL0.050.05
4D232TIGHT POSITIONAL0.040.05
5E232TIGHT POSITIONAL0.040.05
6F232TIGHT POSITIONAL0.040.05
7G232TIGHT POSITIONAL0.030.05
8H232TIGHT POSITIONAL0.040.05
9I232TIGHT POSITIONAL0.030.05
10J232TIGHT POSITIONAL0.040.05
11K232TIGHT POSITIONAL0.030.05
12L232TIGHT POSITIONAL0.040.05
13M232TIGHT POSITIONAL0.040.05
14N232TIGHT POSITIONAL0.040.05
15O232TIGHT POSITIONAL0.030.05
16P232TIGHT POSITIONAL0.030.05
17Q232TIGHT POSITIONAL0.030.05
18R232TIGHT POSITIONAL0.030.05
19S232TIGHT POSITIONAL0.040.05
20T232TIGHT POSITIONAL0.040.05
21U232TIGHT POSITIONAL0.050.05
22V232TIGHT POSITIONAL0.040.05
1A182MEDIUM POSITIONAL0.050.5
2B182MEDIUM POSITIONAL0.040.5
3C182MEDIUM POSITIONAL0.040.5
4D182MEDIUM POSITIONAL0.040.5
5E182MEDIUM POSITIONAL0.040.5
6F182MEDIUM POSITIONAL0.040.5
7G182MEDIUM POSITIONAL0.040.5
8H182MEDIUM POSITIONAL0.050.5
9I182MEDIUM POSITIONAL0.030.5
10J182MEDIUM POSITIONAL0.040.5
11K182MEDIUM POSITIONAL0.040.5
12L182MEDIUM POSITIONAL0.040.5
13M182MEDIUM POSITIONAL0.040.5
14N182MEDIUM POSITIONAL0.050.5
15O182MEDIUM POSITIONAL0.040.5
16P182MEDIUM POSITIONAL0.040.5
17Q182MEDIUM POSITIONAL0.040.5
18R182MEDIUM POSITIONAL0.040.5
19S182MEDIUM POSITIONAL0.040.5
20T182MEDIUM POSITIONAL0.040.5
21U182MEDIUM POSITIONAL0.040.5
22V182MEDIUM POSITIONAL0.040.5
1A232TIGHT THERMAL0.070.5
2B232TIGHT THERMAL0.130.5
3C232TIGHT THERMAL0.160.5
4D232TIGHT THERMAL0.120.5
5E232TIGHT THERMAL0.060.5
6F232TIGHT THERMAL0.070.5
7G232TIGHT THERMAL0.080.5
8H232TIGHT THERMAL0.080.5
9I232TIGHT THERMAL0.080.5
10J232TIGHT THERMAL0.110.5
11K232TIGHT THERMAL0.090.5
12L232TIGHT THERMAL0.070.5
13M232TIGHT THERMAL0.070.5
14N232TIGHT THERMAL0.090.5
15O232TIGHT THERMAL0.090.5
16P232TIGHT THERMAL0.090.5
17Q232TIGHT THERMAL0.080.5
18R232TIGHT THERMAL0.090.5
19S232TIGHT THERMAL0.060.5
20T232TIGHT THERMAL0.10.5
21U232TIGHT THERMAL0.150.5
22V232TIGHT THERMAL0.140.5
1A182MEDIUM THERMAL0.072
2B182MEDIUM THERMAL0.132
3C182MEDIUM THERMAL0.152
4D182MEDIUM THERMAL0.122
5E182MEDIUM THERMAL0.062
6F182MEDIUM THERMAL0.072
7G182MEDIUM THERMAL0.072
8H182MEDIUM THERMAL0.072
9I182MEDIUM THERMAL0.092
10J182MEDIUM THERMAL0.12
11K182MEDIUM THERMAL0.082
12L182MEDIUM THERMAL0.072
13M182MEDIUM THERMAL0.072
14N182MEDIUM THERMAL0.092
15O182MEDIUM THERMAL0.092
16P182MEDIUM THERMAL0.082
17Q182MEDIUM THERMAL0.092
18R182MEDIUM THERMAL0.092
19S182MEDIUM THERMAL0.062
20T182MEDIUM THERMAL0.092
21U182MEDIUM THERMAL0.142
22V182MEDIUM THERMAL0.132
LS refinement shellResolution: 3.2→3.281 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.292 73 -
Rwork0.3 1410 -
all-1483 -
obs--85.08 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
10.2184-0.14730.44270.7403-0.07781.05640.01870.24610.074-0.0781-0.0597-0.32140.03030.4630.0410.31070.00440.04770.3620.03020.28630.064.703-34.962
20.1889-0.16490.35790.6153-0.05211.01240.007-0.067-0.02890.0201-0.04730.2842-0.0502-0.42520.04030.32620.0290.00310.3598-0.0130.2925-28.4286.066-27.9
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A7 - 75
2X-RAY DIFFRACTION1B7 - 75
3X-RAY DIFFRACTION1C7 - 74
4X-RAY DIFFRACTION1D7 - 74
5X-RAY DIFFRACTION1E7 - 75
6X-RAY DIFFRACTION1F7 - 74
7X-RAY DIFFRACTION1G6 - 74
8X-RAY DIFFRACTION1H6 - 74
9X-RAY DIFFRACTION1I7 - 73
10X-RAY DIFFRACTION1J7 - 74
11X-RAY DIFFRACTION1K7 - 74
12X-RAY DIFFRACTION2L7 - 74
13X-RAY DIFFRACTION2M7 - 74
14X-RAY DIFFRACTION2N7 - 74
15X-RAY DIFFRACTION2O7 - 74
16X-RAY DIFFRACTION2P7 - 75
17X-RAY DIFFRACTION2Q7 - 73
18X-RAY DIFFRACTION2R7 - 73
19X-RAY DIFFRACTION2S6 - 74
20X-RAY DIFFRACTION2T7 - 74
21X-RAY DIFFRACTION2U7 - 75
22X-RAY DIFFRACTION2V7 - 75

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