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- PDB-1gtn: Structure of the trp RNA-binding attenuation protein (TRAP) bound... -

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Basic information

Entry
Database: PDB / ID: 1gtn
TitleStructure of the trp RNA-binding attenuation protein (TRAP) bound to an RNA molecule containing 11 GAGCC repeats
Components
  • (GAGCC)11G 56-NUCLEOTIDE RNA
  • TRP RNA-BINDING ATTENUATION PROTEIN
KeywordsRNA BINDING PROTEIN/RNA / RNA BINDING PROTEIN-RNA COMPLEX / TRANSCRIPTION ATTENUATION / RNA-BINDING PROTEIN / TRP RNA
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
TRYPTOPHAN / RNA / RNA (> 10) / Transcription attenuation protein MtrB
Similarity search - Component
Biological speciesBACILLUS STEAROTHERMOPHILUS (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å
AuthorsHopcroft, N.H. / Wendt, A.L. / Gollnick, P. / Antson, A.A.
Citation
Journal: Acta Crystallogr.,Sect.D / Year: 2002
Title: Specificity of Trap-RNA Interactions: Crystal Structures of Two Complexes with Different RNA Sequences
Authors: Hopcroft, N.H. / Wendt, A.L. / Gollnick, P. / Antson, A.A.
#1: Journal: Nature / Year: 1999
Title: Structure of the Trp RNA-Binding Attenuation Protein, Trap, Bound to RNA
Authors: Antson, A.A. / Dodson, E.J. / Dodson, G.G. / Greaves, R.B. / Chen, X. / Gollnick, P.
History
DepositionJan 16, 2002Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 5, 2002Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: TRP RNA-BINDING ATTENUATION PROTEIN
B: TRP RNA-BINDING ATTENUATION PROTEIN
C: TRP RNA-BINDING ATTENUATION PROTEIN
D: TRP RNA-BINDING ATTENUATION PROTEIN
E: TRP RNA-BINDING ATTENUATION PROTEIN
F: TRP RNA-BINDING ATTENUATION PROTEIN
G: TRP RNA-BINDING ATTENUATION PROTEIN
H: TRP RNA-BINDING ATTENUATION PROTEIN
I: TRP RNA-BINDING ATTENUATION PROTEIN
J: TRP RNA-BINDING ATTENUATION PROTEIN
K: TRP RNA-BINDING ATTENUATION PROTEIN
L: TRP RNA-BINDING ATTENUATION PROTEIN
M: TRP RNA-BINDING ATTENUATION PROTEIN
N: TRP RNA-BINDING ATTENUATION PROTEIN
O: TRP RNA-BINDING ATTENUATION PROTEIN
P: TRP RNA-BINDING ATTENUATION PROTEIN
Q: TRP RNA-BINDING ATTENUATION PROTEIN
R: TRP RNA-BINDING ATTENUATION PROTEIN
S: TRP RNA-BINDING ATTENUATION PROTEIN
T: TRP RNA-BINDING ATTENUATION PROTEIN
U: TRP RNA-BINDING ATTENUATION PROTEIN
V: TRP RNA-BINDING ATTENUATION PROTEIN
W: (GAGCC)11G 56-NUCLEOTIDE RNA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)204,59046
Polymers199,89223
Non-polymers4,69723
Water1,31573
1
A: TRP RNA-BINDING ATTENUATION PROTEIN
B: TRP RNA-BINDING ATTENUATION PROTEIN
C: TRP RNA-BINDING ATTENUATION PROTEIN
D: TRP RNA-BINDING ATTENUATION PROTEIN
E: TRP RNA-BINDING ATTENUATION PROTEIN
F: TRP RNA-BINDING ATTENUATION PROTEIN
G: TRP RNA-BINDING ATTENUATION PROTEIN
H: TRP RNA-BINDING ATTENUATION PROTEIN
I: TRP RNA-BINDING ATTENUATION PROTEIN
J: TRP RNA-BINDING ATTENUATION PROTEIN
K: TRP RNA-BINDING ATTENUATION PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)93,28223
Polymers90,83111
Non-polymers2,45112
Water19811
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area27860 Å2
ΔGint-115.2 kcal/mol
Surface area35930 Å2
MethodPQS
2
L: TRP RNA-BINDING ATTENUATION PROTEIN
M: TRP RNA-BINDING ATTENUATION PROTEIN
N: TRP RNA-BINDING ATTENUATION PROTEIN
O: TRP RNA-BINDING ATTENUATION PROTEIN
P: TRP RNA-BINDING ATTENUATION PROTEIN
Q: TRP RNA-BINDING ATTENUATION PROTEIN
R: TRP RNA-BINDING ATTENUATION PROTEIN
S: TRP RNA-BINDING ATTENUATION PROTEIN
T: TRP RNA-BINDING ATTENUATION PROTEIN
U: TRP RNA-BINDING ATTENUATION PROTEIN
V: TRP RNA-BINDING ATTENUATION PROTEIN
W: (GAGCC)11G 56-NUCLEOTIDE RNA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)111,30823
Polymers109,06112
Non-polymers2,24611
Water19811
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area39870 Å2
ΔGint-156 kcal/mol
Surface area40530 Å2
MethodPQS
Unit cell
Length a, b, c (Å)145.839, 111.722, 138.715
Angle α, β, γ (deg.)90.00, 117.78, 90.00
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
51E
61F
71G
81H
91I
101J
111K
12L
22M
32N
42O
52P
62Q
72R
82S
92T
102U
112V

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1115A8 - 73
2115B8 - 73
3115C8 - 73
4115D8 - 73
5115E8 - 73
6115F8 - 73
7115G8 - 73
8115H8 - 73
9115I8 - 73
10115J8 - 73
11115K8 - 73
1214A81
2214B81
3214C81
4214D81
5214E81
6214F81
7214G81
8214H81
9214I81
10214J81
11214K81
1125L6 - 73
2125M6 - 73
3125N6 - 73
4125O6 - 73
5125P6 - 73
6125Q6 - 73
7125R6 - 73
8125S6 - 73
9125T6 - 73
10125U6 - 73
11125V6 - 73
1224L81
2224M81
3224N81
4224O81
5224P81
6224Q81
7224R81
8224S81
9224T81
10224U81
11224V81
1321L101 - 105
2321M101 - 105
3321N101 - 105
4321O101 - 105
5321P101 - 105
6321Q101 - 105
7321R101 - 105
8321S101 - 105
9321T101 - 105
10321U101 - 105
11321V101 - 105

NCS ensembles :
ID
1
2
DetailsBIOMOLECULE 1 IS AN 11 MER WHILST BIOMOLECULE 2 IS A12 MER CONSISTING OF AN 11 MER WITH BOUND RNA CHAIN

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Components

#1: Protein ...
TRP RNA-BINDING ATTENUATION PROTEIN


Mass: 8257.377 Da / Num. of mol.: 22
Source method: isolated from a genetically manipulated source
Details: THE STRUCTURE CONTAINS 2 11-MER MOLECULES (CHAINS A TO K AND L TO V), (RESIDUES 1-75) (SOME N- AND C-TERMINAL RESIDUES MISSING DUE TO DISORDER)
Source: (gene. exp.) BACILLUS STEAROTHERMOPHILUS (bacteria) / Plasmid: PTZSTMTRB / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): SG62052/PGP1-2 / References: UniProt: Q9X6J6
#2: RNA chain (GAGCC)11G 56-NUCLEOTIDE RNA


Mass: 18230.039 Da / Num. of mol.: 1 / Source method: obtained synthetically
#3: Chemical...
ChemComp-TRP / TRYPTOPHAN / Tryptophan


Type: L-peptide linking / Mass: 204.225 Da / Num. of mol.: 23 / Source method: obtained synthetically / Formula: C11H12N2O2
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 73 / 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: 2.5 Å3/Da / Density % sol: 50.4 %
Crystal growpH: 8
Details: 0.2M K-GLUTAMATE, 50MM TRIETHANOLAMINE PH8.0,10MM MGCL2, 8-11% MONOMETHYL PEG 2000,+0.4M KCL AT END, pH 8.00
Crystal grow
*PLUS
pH: 7.8 / Method: vapor diffusion, hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDDetailsChemical formula
115 mg/mlprotein-RNA1drop
270 mMpotassium phosphate1droppH7.8
310 mML-tryptophan1drop
40.2 Mpotassium glutamate1reservoir
550 mMtri-ethanolamine1reservoirpH8.0
610 mM1reservoirMgCl2
78-11 %PEG2000 MME1reservoir

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Data collection

DiffractionMean temperature: 120 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.946
DetectorDate: Feb 15, 1999
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.946 Å / Relative weight: 1
ReflectionResolution: 2.5→20 Å / Num. obs: 65753 / % possible obs: 94.6 % / Redundancy: 1.8 % / Rmerge(I) obs: 0.05 / Net I/σ(I): 13.5
Reflection shellResolution: 2.5→2.59 Å / Redundancy: 1.6 % / Rmerge(I) obs: 0.265 / Mean I/σ(I) obs: 2.4 / % possible all: 77
Reflection
*PLUS
Lowest resolution: 20 Å / Rmerge(I) obs: 0.05
Reflection shell
*PLUS
Highest resolution: 2.5 Å / % possible obs: 77 % / Num. unique obs: 5337

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Processing

Software
NameVersionClassification
REFMAC5.1.07refinement
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1GTF
Resolution: 2.5→19.84 Å / Cor.coef. Fo:Fc: 0.933 / Cor.coef. Fo:Fc free: 0.914 / SU B: 14.27 / SU ML: 0.294 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.654 / ESU R Free: 0.313 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: THE ASYMMETRIC UNIT CONTAINS TWO PROTEIN MOLECULES, EACH MADE UP OF 11 IDENTICAL POLYPEPTIDE CHAINS. ONE OF THESE 11-MERS HAS THE SINGLE RNA MOLECULE BOUND TO IT. THE PROTEIN CHAINS ARE ...Details: THE ASYMMETRIC UNIT CONTAINS TWO PROTEIN MOLECULES, EACH MADE UP OF 11 IDENTICAL POLYPEPTIDE CHAINS. ONE OF THESE 11-MERS HAS THE SINGLE RNA MOLECULE BOUND TO IT. THE PROTEIN CHAINS ARE DESIGNATED A TO V, AND THE AMINO ACIDS IN EACH CHAIN ARE NUMBERED 1 - 75, ALTHOUGH SOME N- AND C- TERMINAL RESIDUES ARE MISSING FROM THE MODEL DUE TO DISORDER. THE RNA MOLECULE CONSISTS OF 11 GAGCC REPEATS, PLUS ONE FINAL G, WHICH IS ABSENT FROM THE MODEL DUE TO DISORDER. FOR THE PURPOSE OF APPLYING NCS RESTRAINTS, EACH GAGCC REPEAT NEEDED TO BE GIVEN A DIFFERENT CHAIN ID. DUE TO A LACK OF AVAILABLE LETTERS, THIS MEANT THAT EACH GAGCC REPEAT WAS GIVEN THE SAME CHAIN ID AS THE PROTEIN MONOMER TO WHICH IT IS BOUND. THUS, THE RNA IS LABELLED AS RESIDUES 101-105 OF EACH OF THE SUBUNITS L TO V, ALTHOUGH SOME NUCLEOTIDES ARE MISSING DUE TO DISORDER. SIMILARLY, THE TRYPTOPHAN LIGAND BOUND TO EACH OF THE 22 PROTEIN MONOMERS IS LABELLED AS RESIDUE 81 OF THAT CHAIN.
RfactorNum. reflection% reflectionSelection details
Rfree0.273 1312 2 %RANDOM
Rwork0.235 ---
obs0.236 63405 100 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
Refinement stepCycle: LAST / Resolution: 2.5→19.84 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11855 968 345 73 13241
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0180.02113345
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg
X-RAY DIFFRACTIONr_angle_other_deg1.8422.00818072
X-RAY DIFFRACTIONr_dihedral_angle_1_deg
X-RAY DIFFRACTIONr_dihedral_angle_2_deg
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.287152214
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.9941588
X-RAY DIFFRACTIONr_chiral_restr0.1070.22058
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.029541
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2460.24616
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1510.2459
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.3860.255
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.3390.216
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.4581.57584
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.786212139
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it1.20135761
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it1.70645933
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11A10tight positional0.160.3
12B10tight positional0.140.3
13C10tight positional0.220.3
14D10tight positional0.220.3
15E10tight positional0.160.3
16F10tight positional0.210.3
17G10tight positional0.180.3
18H10tight positional0.210.3
19I10tight positional0.170.3
110J10tight positional0.180.3
111K10tight positional0.90.3
21L636tight positional0.180.3
22M636tight positional0.20.3
23N636tight positional0.160.3
24O636tight positional0.210.3
25P636tight positional0.220.3
26Q636tight positional0.170.3
27R636tight positional0.190.3
28S636tight positional0.220.3
29T636tight positional0.190.3
210U636tight positional0.170.3
211V636tight positional0.210.3
11A269medium positional0.10.1
12B269medium positional0.10.1
13C269medium positional0.10.1
14D269medium positional0.10.1
15E269medium positional0.10.1
16F269medium positional0.110.1
17G269medium positional0.10.1
18H269medium positional0.10.1
19I269medium positional0.10.1
110J269medium positional0.110.1
111K269medium positional0.10.1
21L269medium positional0.020.1
22M269medium positional0.020.1
23N269medium positional0.020.1
24O269medium positional0.020.1
25P269medium positional0.020.1
26Q269medium positional0.020.1
27R269medium positional0.020.1
28S269medium positional0.020.1
29T269medium positional0.020.1
210U269medium positional0.020.1
211V269medium positional0.020.1
11A253loose positional0.632
12B253loose positional0.562
13C253loose positional0.812
14D253loose positional0.682
15E253loose positional0.722
16F253loose positional0.972
17G253loose positional0.482
18H253loose positional0.512
19I253loose positional0.592
110J253loose positional0.472
111K253loose positional0.442
21L253loose positional0.052
22M253loose positional0.052
23N253loose positional0.062
24O253loose positional0.052
25P253loose positional0.052
26Q253loose positional0.062
27R253loose positional0.042
28S253loose positional0.042
29T253loose positional0.052
210U253loose positional0.042
211V253loose positional0.042
11A10tight thermal0.481
12B10tight thermal0.41
13C10tight thermal0.671
14D10tight thermal0.231
15E10tight thermal0.381
16F10tight thermal0.551
17G10tight thermal0.611
18H10tight thermal0.181
19I10tight thermal0.431
110J10tight thermal0.361
111K10tight thermal0.341
21L636tight thermal2.21
22M636tight thermal2.021
23N636tight thermal2.581
24O636tight thermal1.551
25P636tight thermal1.971
26Q636tight thermal2.371
27R636tight thermal2.471
28S636tight thermal1.351
29T636tight thermal2.091
210U636tight thermal1.911
211V636tight thermal1.861
11A269medium thermal0.271
12B269medium thermal0.261
13C269medium thermal0.271
14D269medium thermal0.251
15E269medium thermal0.31
16F269medium thermal0.281
17G269medium thermal0.321
18H269medium thermal0.281
19I269medium thermal0.271
110J269medium thermal0.281
111K269medium thermal0.261
21L269medium thermal2.511
22M269medium thermal2.441
23N269medium thermal2.51
24O269medium thermal2.391
25P269medium thermal2.621
26Q269medium thermal2.541
27R269medium thermal2.711
28S269medium thermal2.541
29T269medium thermal2.511
210U269medium thermal2.531
211V269medium thermal2.471
11A253loose thermal0.391
12B253loose thermal0.351
13C253loose thermal0.381
14D253loose thermal0.371
15E253loose thermal0.381
16F253loose thermal0.421
17G253loose thermal0.491
18H253loose thermal0.421
19I253loose thermal0.351
110J253loose thermal0.411
111K253loose thermal0.361
21L253loose thermal3.081
22M253loose thermal2.931
23N253loose thermal3.081
24O253loose thermal3.041
25P253loose thermal3.061
26Q253loose thermal3.231
27R253loose thermal3.481
28S253loose thermal3.231
29T253loose thermal2.951
210U253loose thermal3.191
211V253loose thermal31
LS refinement shellResolution: 2.5→2.56 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.376 72
Rwork0.334 3795
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)
10.5535-0.0765-0.620.70530.07742.4044-0.01440.0867-0.0091-0.4004-0.0719-0.15030.18830.15710.08640.26060.05230.00410.1789-0.00370.296257.14460.075814.1041
20.6707-0.0236-0.66110.77850.00492.542-0.02620.088-0.0277-0.2031-0.0319-0.0640.12490.06230.05810.0178-0.0011-0.07280.206-0.00670.297546.3265-0.02544.9895
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A7 - 74
2X-RAY DIFFRACTION1A81 - 181
3X-RAY DIFFRACTION1B6 - 74
4X-RAY DIFFRACTION1B81
5X-RAY DIFFRACTION1C6 - 74
6X-RAY DIFFRACTION1C81
7X-RAY DIFFRACTION1D7 - 75
8X-RAY DIFFRACTION1D81
9X-RAY DIFFRACTION1E7 - 74
10X-RAY DIFFRACTION1E81
11X-RAY DIFFRACTION1F7 - 75
12X-RAY DIFFRACTION1F81
13X-RAY DIFFRACTION1G6 - 75
14X-RAY DIFFRACTION1G81
15X-RAY DIFFRACTION1H7 - 75
16X-RAY DIFFRACTION1H81
17X-RAY DIFFRACTION1I7 - 75
18X-RAY DIFFRACTION1I81
19X-RAY DIFFRACTION1J7 - 74
20X-RAY DIFFRACTION1J81
21X-RAY DIFFRACTION1K7 - 75
22X-RAY DIFFRACTION1K81
23X-RAY DIFFRACTION2L5 - 74
24X-RAY DIFFRACTION2L81
25X-RAY DIFFRACTION2M5 - 75
26X-RAY DIFFRACTION2M81
27X-RAY DIFFRACTION2N5 - 74
28X-RAY DIFFRACTION2N81
29X-RAY DIFFRACTION2O5 - 75
30X-RAY DIFFRACTION2O81
31X-RAY DIFFRACTION2P5 - 74
32X-RAY DIFFRACTION2P81
33X-RAY DIFFRACTION2Q5 - 74
34X-RAY DIFFRACTION2Q81
35X-RAY DIFFRACTION2R5 - 74
36X-RAY DIFFRACTION2R81
37X-RAY DIFFRACTION2S5 - 74
38X-RAY DIFFRACTION2S81
39X-RAY DIFFRACTION2T5 - 74
40X-RAY DIFFRACTION2T81
41X-RAY DIFFRACTION2U5 - 74
42X-RAY DIFFRACTION2U81
43X-RAY DIFFRACTION2V5 - 74
44X-RAY DIFFRACTION2V81
Refinement
*PLUS
Lowest resolution: 20 Å / Rfactor obs: 0.235 / Rfactor Rfree: 0.273 / Rfactor Rwork: 0.235
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONr_bond_d0.0190.02
X-RAY DIFFRACTIONr_angle_d
X-RAY DIFFRACTIONr_angle_deg22

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