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- PDB-7dq6: Crystal structure of HitB in complex with (S)-beta-3-Br-phenylala... -

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Basic information

Entry
Database: PDB / ID: 7dq6
TitleCrystal structure of HitB in complex with (S)-beta-3-Br-phenylalanine sulfamoyladenosine
ComponentsPutative ATP-dependent b-aminoacyl-ACP synthetase
KeywordsLIGASE / Hitachimycin / Polyketide biosynthesis / ATP binding / Adenylation
Function / homology
Function and homology information


AMP-binding / ANL, N-terminal domain / AMP-binding enzyme, C-terminal domain / AMP-binding enzyme C-terminal domain / AMP-binding, conserved site / Putative AMP-binding domain signature. / AMP-dependent synthetase/ligase / AMP-binding enzyme, C-terminal domain superfamily / AMP-binding enzyme
Similarity search - Domain/homology
Chem-HFR / Putative ATP-dependent b-aminoacyl-ACP synthetase
Similarity search - Component
Biological speciesEmbleya scabrispora (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å
AuthorsKudo, F. / Takahashi, S. / Miyanaga, A. / Nakazawa, Y. / Eguchi, T.
CitationJournal: Acs Chem.Biol. / Year: 2021
Title: Mutational Biosynthesis of Hitachimycin Analogs Controlled by the beta-Amino Acid-Selective Adenylation Enzyme HitB.
Authors: Kudo, F. / Takahashi, S. / Miyanaga, A. / Nakazawa, Y. / Nishino, K. / Hayakawa, Y. / Kawamura, K. / Ishikawa, F. / Tanabe, G. / Iwai, N. / Nagumo, Y. / Usui, T. / Eguchi, T.
History
DepositionDec 22, 2020Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Mar 3, 2021Provider: repository / Type: Initial release
Revision 1.1Mar 31, 2021Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.2Nov 29, 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

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Assembly

Deposited unit
A: Putative ATP-dependent b-aminoacyl-ACP synthetase
B: Putative ATP-dependent b-aminoacyl-ACP synthetase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)120,5746
Polymers119,3492
Non-polymers1,2254
Water1,11762
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3970 Å2
ΔGint-20 kcal/mol
Surface area37360 Å2
MethodPISA
Unit cell
Length a, b, c (Å)67.965, 96.693, 166.414
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B

NCS domain segments:

Component-ID: 0 / Ens-ID: 1 / Beg auth comp-ID: ARG / Beg label comp-ID: ARG / End auth comp-ID: ARG / End label comp-ID: ARG / Refine code: 0 / Auth seq-ID: 9 - 528 / Label seq-ID: 25 - 544

Dom-IDAuth asym-IDLabel asym-ID
1AA
2BB

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Components

#1: Protein Putative ATP-dependent b-aminoacyl-ACP synthetase


Mass: 59674.695 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Embleya scabrispora (bacteria) / Gene: hitB / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: A0A0F7R6G7
#2: Chemical ChemComp-HFR / [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl N-[(3S)-3-azanyl-3-(3-bromophenyl)propanoyl]sulfamate


Mass: 572.390 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C19H22BrN7O7S / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ca
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 62 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

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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: 2.29 Å3/Da / Density % sol: 46.31 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / Details: PEG 400, calcium acetate, sodium acetate

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Photon Factory / Beamline: BL-5A / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Dec 10, 2019
RadiationMonochromator: Numerical link type Si(111) double crystal monochromator
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.6→50 Å / Num. obs: 34560 / % possible obs: 99.9 % / Redundancy: 6.6 % / CC1/2: 0.999 / Rmerge(I) obs: 0.089 / Net I/σ(I): 17.5
Reflection shellResolution: 2.6→2.72 Å / Redundancy: 6.4 % / Rmerge(I) obs: 0.804 / Mean I/σ(I) obs: 2.5 / Num. unique obs: 4167 / CC1/2: 0.861 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.8.0238refinement
PDB_EXTRACT3.25data extraction
XDSdata reduction
Aimlessdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 7DQ5

7dq5


Resolution: 2.6→48.39 Å / Cor.coef. Fo:Fc: 0.944 / Cor.coef. Fo:Fc free: 0.905 / SU B: 32.333 / SU ML: 0.31 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.734 / ESU R Free: 0.333 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: U VALUES : WITH TLS ADDED HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.2698 1679 4.9 %RANDOM
Rwork0.2121 ---
obs0.215 32819 99.92 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 125.7 Å2 / Biso mean: 63.691 Å2 / Biso min: 28 Å2
Baniso -1Baniso -2Baniso -3
1--1.74 Å20 Å20 Å2
2--4.12 Å20 Å2
3----2.38 Å2
Refinement stepCycle: final / Resolution: 2.6→48.39 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7026 0 72 62 7160
Biso mean--51.86 48.81 -
Num. residues----917
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.0137251
X-RAY DIFFRACTIONr_bond_other_d0.0030.0176915
X-RAY DIFFRACTIONr_angle_refined_deg1.5171.6649882
X-RAY DIFFRACTIONr_angle_other_deg1.2381.58315872
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.995905
X-RAY DIFFRACTIONr_dihedral_angle_2_deg29.41519.027411
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.153151095
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.5671592
X-RAY DIFFRACTIONr_chiral_restr0.0650.2941
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.028182
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021664
Refine LS restraints NCS

Ens-ID: 1 / Number: 13129 / Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Rms dev position: 0.09 Å / Weight position: 0.05

Dom-IDAuth asym-ID
1A
2B
LS refinement shellResolution: 2.6→2.668 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.346 123 -
Rwork0.329 2376 -
all-2499 -
obs--100 %
Refinement TLS params.

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

IDL11 (°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)
10.3118-0.0340.13550.1820.20770.57770.04270.0729-0.05020.0356-0.0580.0043-0.01640.05860.01530.13550.00720.00890.45810.01070.0245.545-23.266-14.819
20.39380.2243-0.1890.6501-0.11431.019-0.04270.0885-0.0158-0.2033-0.02170.0943-0.0607-0.13740.06440.16470.1088-0.05470.5068-0.06430.0291-13.192-26.677-51.148
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A9 - 602
2X-RAY DIFFRACTION2B9 - 602

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