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- PDB-5ipm: SigmaS-transcription initiation complex with 4-nt nascent RNA -

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Basic information

Entry
Database: PDB / ID: 5ipm
TitleSigmaS-transcription initiation complex with 4-nt nascent RNA
Components
  • (DNA-directed RNA polymerase subunit ...) x 4
  • RNA polymerase sigma factor RpoS
  • nascent RNA 4-mer
  • synthetic non-template strand DNA (50-MER)
  • synthetic template strand DNA (50-MER)
KeywordsTRANSCRIPTION / TRANSFERASE/DNA/RNA / Transcription initiation / RNA polymerase / general stress sigma factor / pyrophosphate release / TRANSFERASE-DNA-RNA complex
Function / homology
Function and homology information


sigma factor antagonist complex / RNA polymerase complex / response to stress / submerged biofilm formation / cellular response to cell envelope stress / regulation of DNA-templated transcription initiation / sigma factor activity / bacterial-type flagellum assembly / bacterial-type RNA polymerase core enzyme binding / cytosolic DNA-directed RNA polymerase complex ...sigma factor antagonist complex / RNA polymerase complex / response to stress / submerged biofilm formation / cellular response to cell envelope stress / regulation of DNA-templated transcription initiation / sigma factor activity / bacterial-type flagellum assembly / bacterial-type RNA polymerase core enzyme binding / cytosolic DNA-directed RNA polymerase complex / bacterial-type flagellum-dependent cell motility / nitrate assimilation / regulation of DNA-templated transcription elongation / transcription elongation factor complex / transcription antitermination / cell motility / DNA-templated transcription initiation / ribonucleoside binding / DNA-directed RNA polymerase / DNA-directed RNA polymerase activity / response to heat / protein-containing complex assembly / intracellular iron ion homeostasis / protein dimerization activity / response to antibiotic / negative regulation of DNA-templated transcription / magnesium ion binding / DNA binding / zinc ion binding / membrane / cytoplasm / cytosol
Similarity search - Function
RNA polymerase sigma factor RpoS / Sigma-70 factors family signature 1. / : / RNA polymerase sigma-70 region 1.2 / Sigma-70 factor, region 1.2 / RNA polymerase sigma-70 region 3 / Sigma-70 region 3 / Sigma-70 factors family signature 2. / RNA polymerase sigma-70 / RNA polymerase sigma-70 region 4 ...RNA polymerase sigma factor RpoS / Sigma-70 factors family signature 1. / : / RNA polymerase sigma-70 region 1.2 / Sigma-70 factor, region 1.2 / RNA polymerase sigma-70 region 3 / Sigma-70 region 3 / Sigma-70 factors family signature 2. / RNA polymerase sigma-70 / RNA polymerase sigma-70 region 4 / Sigma-70, region 4 / RNA polymerase sigma-70 region 2 / RNA polymerase sigma-70 like domain / Sigma-70 region 2 / RNA polymerase sigma factor, region 2 / RNA polymerase sigma factor, region 3/4-like / DNA-directed RNA polymerase, omega subunit / DNA-directed RNA polymerase, subunit beta-prime, bacterial type / DNA-directed RNA polymerase, beta subunit, external 1 domain superfamily / DNA-directed RNA polymerase, beta subunit, external 1 domain / RNA polymerase beta subunit external 1 domain / RNA polymerase, alpha subunit, C-terminal / Bacterial RNA polymerase, alpha chain C terminal domain / DNA-directed RNA polymerase beta subunit, bacterial-type / DNA-directed RNA polymerase, alpha subunit / DNA-directed RNA polymerase, subunit beta-prime / RNA polymerase Rpb6 / RNA polymerase, subunit omega/Rpo6/RPB6 / RNA polymerase Rpb6 / RNA polymerase Rpb2, domain 2 superfamily / RNA polymerase Rpb1, domain 3 superfamily / RPB6/omega subunit-like superfamily / DNA-directed RNA polymerase, insert domain / DNA-directed RNA polymerase, RpoA/D/Rpb3-type / RNA polymerase Rpb3/RpoA insert domain / RNA polymerase Rpb3/Rpb11 dimerisation domain / RNA polymerases D / RNA polymerase Rpb1, clamp domain superfamily / RNA polymerase Rpb1, domain 3 / RNA polymerase Rpb1, domain 3 / RNA polymerase Rpb1, domain 1 / RNA polymerase Rpb1, domain 1 / RNA polymerase, beta subunit, protrusion / RNA polymerase beta subunit / RNA polymerase, alpha subunit / RNA polymerase Rpb1, domain 5 / RNA polymerase Rpb1, domain 4 / RNA polymerase Rpb1, domain 2 / RNA polymerase Rpb1, domain 5 / RNA polymerase Rpb1, domain 4 / DNA-directed RNA polymerase, insert domain superfamily / RNA polymerase, N-terminal / RNA polymerase Rpb2, domain 2 / RNA polymerase Rpb1, funnel domain superfamily / RNA polymerase Rpb2, domain 2 / RNA polymerase I subunit A N-terminus / RNA polymerase, RBP11-like subunit / RNA polymerase, beta subunit, conserved site / RNA polymerase Rpb2, domain 7 / RNA polymerase Rpb2, domain 3 / RNA polymerase Rpb2, OB-fold / RNA polymerase Rpb2, domain 7 / RNA polymerase Rpb2, domain 3 / RNA polymerases beta chain signature. / DNA-directed RNA polymerase, subunit 2, hybrid-binding domain / DNA-directed RNA polymerase, subunit 2 / DNA-directed RNA polymerase, subunit 2, hybrid-binding domain superfamily / RNA polymerase Rpb2, domain 6 / Winged helix-like DNA-binding domain superfamily
Similarity search - Domain/homology
DNA / DNA (> 10) / RNA / DNA-directed RNA polymerase subunit alpha / DNA-directed RNA polymerase subunit omega / DNA-directed RNA polymerase subunit beta' / DNA-directed RNA polymerase subunit beta / RNA polymerase sigma factor RpoS
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4.2 Å
AuthorsLiu, B. / Zuo, Y. / Steitz, T.A.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2016
Title: Structures of E. coli sigma S-transcription initiation complexes provide new insights into polymerase mechanism.
Authors: Liu, B. / Zuo, Y. / Steitz, T.A.
History
DepositionMar 9, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 30, 2016Provider: repository / Type: Initial release
Revision 1.1Apr 13, 2016Group: Database references
Revision 1.2Jun 22, 2016Group: Database references
Revision 1.3Oct 23, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / citation / database_2 / pdbx_entry_details / pdbx_modification_feature / pdbx_struct_oper_list / struct_conn / struct_conn_type / struct_ncs_dom_lim
Item: _citation.journal_id_CSD / _database_2.pdbx_DOI ..._citation.journal_id_CSD / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_oper_list.symmetry_operation / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_conn_type.id / _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: DNA-directed RNA polymerase subunit alpha
B: DNA-directed RNA polymerase subunit alpha
C: DNA-directed RNA polymerase subunit beta
D: DNA-directed RNA polymerase subunit beta'
E: DNA-directed RNA polymerase subunit omega
F: RNA polymerase sigma factor RpoS
1: synthetic non-template strand DNA (50-MER)
2: synthetic template strand DNA (50-MER)
3: nascent RNA 4-mer
hetero molecules


Theoretical massNumber of molelcules
Total (without water)441,35612
Polymers441,2019
Non-polymers1553
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area53800 Å2
ΔGint-262 kcal/mol
Surface area151890 Å2
MethodPISA
Unit cell
Length a, b, c (Å)132.752, 151.967, 228.064
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B

NCS domain segments:

Component-ID: _ / Ens-ID: 1 / Beg auth comp-ID: THR / Beg label comp-ID: THR / End auth comp-ID: VAL / End label comp-ID: VAL / Refine code: _ / Auth seq-ID: 6 - 232 / Label seq-ID: 13 - 239

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

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Components

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DNA-directed RNA polymerase subunit ... , 4 types, 5 molecules ABCDE

#1: Protein DNA-directed RNA polymerase subunit alpha / RNAP subunit alpha / RNA polymerase subunit alpha / Transcriptase subunit alpha


Mass: 26899.572 Da / Num. of mol.: 2 / Fragment: UNP residues 1-235
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: rpoA, pez, phs, sez, b3295, JW3257 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P0A7Z4, DNA-directed RNA polymerase
#2: Protein DNA-directed RNA polymerase subunit beta / RNAP subunit beta / RNA polymerase subunit beta / Transcriptase subunit beta


Mass: 150820.875 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli)
Gene: rpoB, groN, nitB, rif, ron, stl, stv, tabD, b3987, JW3950
Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P0A8V2, DNA-directed RNA polymerase
#3: Protein DNA-directed RNA polymerase subunit beta' / RNAP subunit beta' / RNA polymerase subunit beta' / Transcriptase subunit beta'


Mass: 155366.781 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: rpoC, tabB, b3988, JW3951 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P0A8T7, DNA-directed RNA polymerase
#4: Protein DNA-directed RNA polymerase subunit omega / RNAP omega subunit / RNA polymerase omega subunit / Transcriptase subunit omega


Mass: 10118.352 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: rpoZ, b3649, JW3624 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P0A800, DNA-directed RNA polymerase

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DNA chain , 2 types, 2 molecules 12

#6: DNA chain synthetic non-template strand DNA (50-MER)


Mass: 15329.811 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)
#7: DNA chain synthetic template strand DNA (50-MER)


Mass: 15547.958 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)

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Protein / RNA chain , 2 types, 2 molecules F3

#5: Protein RNA polymerase sigma factor RpoS / Sigma S / Sigma-38


Mass: 38777.602 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: rpoS, appR, katF, nur, otsX, sigS, b2741, JW5437 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P13445
#8: RNA chain nascent RNA 4-mer


Mass: 1440.785 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)

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Non-polymers , 2 types, 3 molecules

#9: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#10: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg

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Details

Has protein modificationY

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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: 2.61 Å3/Da / Density % sol: 52.82 %
Crystal growTemperature: 295 K / Method: vapor diffusion, sitting drop / pH: 7.8 / Details: PEG3350, sodium chloride, HEPES

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-E / Wavelength: 0.979 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Nov 26, 2014
RadiationMonochromator: single crystal Si(220) side bounce / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979 Å / Relative weight: 1
ReflectionResolution: 4.2→126.464 Å / Num. obs: 32692 / % possible obs: 99.9 % / Redundancy: 7.7 % / Net I/σ(I): 8.44
Reflection shellHighest resolution: 4.2 Å

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Processing

Software
NameVersionClassification
REFMAC5.8.0123refinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 4.2→126.46 Å / Cor.coef. Fo:Fc: 0.928 / Cor.coef. Fo:Fc free: 0.889 / SU B: 371.28 / SU ML: 1.82 / Cross valid method: THROUGHOUT / ESU R Free: 1.328 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.33005 1651 4.8 %RANDOM
Rwork0.27042 ---
obs0.27337 32692 99.88 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 284.432 Å2
Baniso -1Baniso -2Baniso -3
1-10.18 Å20 Å20 Å2
2--10.03 Å20 Å2
3----20.21 Å2
Refinement stepCycle: LAST / Resolution: 4.2→126.46 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms27572 1452 3 0 29027
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.01929598
X-RAY DIFFRACTIONr_bond_other_d0.0020.0228286
X-RAY DIFFRACTIONr_angle_refined_deg1.4241.93240273
X-RAY DIFFRACTIONr_angle_other_deg0.838365096
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.55553505
X-RAY DIFFRACTIONr_dihedral_angle_2_deg23.74124.0641319
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.488155172
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.86815263
X-RAY DIFFRACTIONr_chiral_restr0.0750.24517
X-RAY DIFFRACTIONr_gen_planes_refined0.0250.02132440
X-RAY DIFFRACTIONr_gen_planes_other0.020.026440
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it10.19521.55314053
X-RAY DIFFRACTIONr_mcbond_other10.19421.55314052
X-RAY DIFFRACTIONr_mcangle_it16.85336.35117547
X-RAY DIFFRACTIONr_mcangle_other16.85336.35117548
X-RAY DIFFRACTIONr_scbond_it10.77122.79615545
X-RAY DIFFRACTIONr_scbond_other10.77222.79515544
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other17.88738.16622727
X-RAY DIFFRACTIONr_long_range_B_refined28.70456.398132913
X-RAY DIFFRACTIONr_long_range_B_other28.70456.397132912
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Ens-ID: 1 / Number: 27606 / Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Rms dev position: 0.06 Å / Weight position: 0.05

Dom-IDAuth asym-ID
1A
2B
LS refinement shellResolution: 4.2→4.309 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.508 133 -
Rwork0.51 2350 -
obs--99.64 %
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)
18.66992.5089-1.84066.334-0.95779.78270.1667-0.1863-1.2989-0.03090.1222-0.43030.41381.3541-0.2890.38330.1975-0.17190.31590.22842.01081.089-18.2884.878
212.07220.644-1.67730.4298-0.19451.8992-0.1481-0.5324-0.9907-0.04340.14660.05471.3856-0.53260.00151.3766-0.3663-0.14290.4940.63291.9177-32.887-32.0968.42
39.58115.9101-2.63586.9006-7.547611.89260.267-0.1141-0.13480.55470.14140.0632-0.83670.4626-0.40840.395-0.1053-0.10351.6073-0.15221.798829.6712.8551.396
48.0319-0.26521.10850.90730.69842.7179-0.3772-0.86510.43110.20950.264-0.0467-0.428-0.19280.11320.20920.1539-0.09030.24330.2071.3226-30.5238.3620.025
53.792-0.79311.20446.4687-2.04554.7165-0.00991.3999-0.1637-0.7039-0.0115-0.4312-0.29071.31250.02130.1445-0.1435-0.0040.8207-0.37631.4271-18.3011.757-41.279
64.63461.80890.78812.482-2.81797.02270.5107-0.7357-1.14780.2250.59330.06860.9545-2.4857-1.1040.9863-0.5702-0.48011.01570.57383.1012-60.898-30.081-3.432
79.49150.8555-3.95636.9223.99824.5264-0.3983-0.37010.7714-0.25350.94560.26480.16020.6181-0.54731.72590.1161-0.24461.145-0.34662.4744-31.728-47.496-51.333
811.816-2.054.66682.6514-1.26823.84710.2931-0.2282-0.7549-0.448-0.12040.5850.2296-1.1267-0.17270.4548-0.13570.04310.78110.14551.1534-77.942-3.646-17.192
99.49852.19792.20548.6961-3.27899.7466-0.1420.2038-1.1984-0.7860.2728-0.1760.75520.0058-0.13080.22740.13690.02750.20090.01251.1285-71.50129.32-29.634
109.55071.78383.75792.49693.49446.4724-0.1637-0.48981.20480.01780.0150.1214-1.3003-0.26230.14871.28060.125-0.08450.21590.15611.2644-74.12762.62-28.889
114.512.3664-1.78093.03450.41421.80441.05361.0283-0.326-0.7587-0.7154-0.7492-1.7153-1.1133-0.33822.50010.2353-0.14521.78720.49882.4061-29.34449.563-52.48
124.685-0.26640.32312.5052-0.45272.57010.29630.3174-0.7877-0.4012-0.18060.9395-0.3072-0.6133-0.11570.6944-0.0075-0.44820.4855-0.67022.1501-64.315-2.928-54.216
131.0478-2.28731.55897.1759-2.8222.7807-0.520.23580.34120.67270.3403-0.0015-0.64380.19920.17972.3207-0.1968-0.17971.58160.12533.0946-28.33852.546-28.321
145.2789-4.63257.038310.6797-0.049215.1781-0.4629-0.806-0.91421.5596-0.22452.83340.2873-1.58330.68740.9002-0.4665-0.12261.3646-0.14681.9482-40.673-2.466-24.288
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A6 - 51
2X-RAY DIFFRACTION1A179 - 235
3X-RAY DIFFRACTION1B6 - 51
4X-RAY DIFFRACTION1B179 - 233
5X-RAY DIFFRACTION2A52 - 178
6X-RAY DIFFRACTION3B52 - 178
7X-RAY DIFFRACTION4C3 - 28
8X-RAY DIFFRACTION4C146 - 152
9X-RAY DIFFRACTION4C445 - 455
10X-RAY DIFFRACTION4C517 - 831
11X-RAY DIFFRACTION4C1057 - 1241
12X-RAY DIFFRACTION4D501 - 790
13X-RAY DIFFRACTION5C1242 - 1320
14X-RAY DIFFRACTION5D343 - 500
15X-RAY DIFFRACTION5D791 - 938
16X-RAY DIFFRACTION5D1132 - 1153
17X-RAY DIFFRACTION5D1213 - 1317
18X-RAY DIFFRACTION5D1345 - 1376
19X-RAY DIFFRACTION5D1502 - 1503
20X-RAY DIFFRACTION5E2 - 80
21X-RAY DIFFRACTION5F220 - 244
22X-RAY DIFFRACTION6C832 - 891
23X-RAY DIFFRACTION6C912 - 1056
24X-RAY DIFFRACTION7C892 - 911
25X-RAY DIFFRACTION7F245 - 329
26X-RAY DIFFRACTION8C29 - 145
27X-RAY DIFFRACTION8C456 - 516
28X-RAY DIFFRACTION9C153 - 226
29X-RAY DIFFRACTION9C337 - 444
30X-RAY DIFFRACTION9143 - 50
31X-RAY DIFFRACTION10C227 - 336
32X-RAY DIFFRACTION11D1154 - 1212
33X-RAY DIFFRACTION12C1321 - 1342
34X-RAY DIFFRACTION12D15 - 342
35X-RAY DIFFRACTION12D1318 - 1344
36X-RAY DIFFRACTION12D1501
37X-RAY DIFFRACTION12F53 - 219
38X-RAY DIFFRACTION12127 - 42
39X-RAY DIFFRACTION12222 - 36
40X-RAY DIFFRACTION12151 - 59
41X-RAY DIFFRACTION1224 - 12
42X-RAY DIFFRACTION13D939 - 1131
43X-RAY DIFFRACTION14213 - 21
44X-RAY DIFFRACTION14314 - 17

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Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

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