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- PDB-3by7: CRYSTAL STRUCTURE OF A PROTEIN STRUCTURALLY SIMILAR TO SM/LSM-LIK... -

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Basic information

Entry
Database: PDB / ID: 3by7
TitleCRYSTAL STRUCTURE OF A PROTEIN STRUCTURALLY SIMILAR TO SM/LSM-LIKE RNA-BINDING PROTEINS (JCVI_PEP_1096686650277) FROM UNCULTURED MARINE ORGANISM AT 2.60 A RESOLUTION
Componentsuncharacterized protein
KeywordsUNKNOWN FUNCTION / METAGENOMICS / STRUCTURAL GENOMICS / JOINT CENTER FOR STRUCTURAL GENOMICS / JCSG / PROTEIN STRUCTURE INITIATIVE / PSI-2
Function / homologySH3 type barrels. - #100 / SH3 type barrels. / Roll / Mainly Beta
Function and homology information
Biological speciesuncultured marine organism (environmental samples)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.6 Å
AuthorsJoint Center for Structural Genomics (JCSG)
CitationJournal: Proteins / Year: 2009
Title: Crystal structure of a novel Sm-like protein of putative cyanophage origin at 2.60 A resolution.
Authors: Das, D. / Kozbial, P. / Axelrod, H.L. / Miller, M.D. / McMullan, D. / Krishna, S.S. / Abdubek, P. / Acosta, C. / Astakhova, T. / Burra, P. / Carlton, D. / Chen, C. / Chiu, H.J. / Clayton, T. ...Authors: Das, D. / Kozbial, P. / Axelrod, H.L. / Miller, M.D. / McMullan, D. / Krishna, S.S. / Abdubek, P. / Acosta, C. / Astakhova, T. / Burra, P. / Carlton, D. / Chen, C. / Chiu, H.J. / Clayton, T. / Deller, M.C. / Duan, L. / Elias, Y. / Elsliger, M.A. / Ernst, D. / Farr, C. / Feuerhelm, J. / Grzechnik, A. / Grzechnik, S.K. / Hale, J. / Han, G.W. / Jaroszewski, L. / Jin, K.K. / Johnson, H.A. / Klock, H.E. / Knuth, M.W. / Kumar, A. / Marciano, D. / Morse, A.T. / Murphy, K.D. / Nigoghossian, E. / Nopakun, A. / Okach, L. / Oommachen, S. / Paulsen, J. / Puckett, C. / Reyes, R. / Rife, C.L. / Sefcovic, N. / Sudek, S. / Tien, H. / Trame, C. / Trout, C.V. / van den Bedem, H. / Weekes, D. / White, A. / Xu, Q. / Hodgson, K.O. / Wooley, J. / Deacon, A.M. / Godzik, A. / Lesley, S.A. / Wilson, I.A.
History
DepositionJan 15, 2008Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 29, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Oct 25, 2017Group: Author supporting evidence / Refinement description / Category: pdbx_struct_assembly_auth_evidence / software / Item: _software.classification / _software.name
Revision 1.3Jul 24, 2019Group: Data collection / Derived calculations / Refinement description
Category: software / struct_conn
Item: _software.classification / _software.contact_author ..._software.classification / _software.contact_author / _software.contact_author_email / _software.language / _software.location / _software.name / _software.type / _software.version / _struct_conn.pdbx_leaving_atom_flag
Revision 1.4Feb 1, 2023Group: Database references / Category: database_2 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: uncharacterized protein
B: uncharacterized protein
C: uncharacterized protein
D: uncharacterized protein
E: uncharacterized protein


Theoretical massNumber of molelcules
Total (without water)55,7375
Polymers55,7375
Non-polymers00
Water1267
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration, light scattering
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6060 Å2
MethodPISA
Unit cell
Length a, b, c (Å)108.250, 77.180, 71.470
Angle α, β, γ (deg.)90.000, 113.820, 90.000
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
51E
61A
71B
81C
91D
101E
111A
121B
131C
141D
151E
161A
171B
181C
191D
201E
211A
221B
231C
241D
251E
261A
271B
281C
291D
301E
311A
321B
331C
341D
351E
361A
371B
381C
391D
401E
411A
421B
431C
441D
451E
461A
471B
481C
491D
501E
511A
521B
531C
541D
551E
561A
571B
581C
591D
601E
611A
621B
631C
641D
651E

NCS domain segments:

Ens-ID: 1

Dom-IDComponent-IDBeg label comp-IDEnd label comp-IDRefine codeAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11LYSASN5AA2 - 33 - 4
21LYSASN5BB2 - 33 - 4
31LYSASN5CC2 - 33 - 4
41LYSASN5DD2 - 33 - 4
51ASNASN5EE34
62ILEMSE2AA4 - 75 - 8
72ILEMSE2BB4 - 75 - 8
82ILEMSE2CC4 - 75 - 8
92ILEMSE2DD4 - 75 - 8
102ILEMSE2EE4 - 75 - 8
113ARGARG3AA89
123ARGARG3BB89
133ARGARG3CC89
143ARGARG3DD89
153ARGARG3EE89
164LEUGLN2AA9 - 3810 - 39
174LEUGLN2BB9 - 3810 - 39
184LEUALA2CC9 - 3910 - 40
194LEUGLN2DD9 - 3810 - 39
204LEUMSE2EE9 - 3710 - 38
215VALGLN5AA45 - 4646 - 47
225VALGLN5BB45 - 4646 - 47
235VALGLN5CC45 - 4646 - 47
245VALGLN5DD45 - 4646 - 47
255VALGLN5EE45 - 4646 - 47
266LEUILE2AA47 - 6948 - 70
276LEUILE2BB47 - 6948 - 70
286LEUILE2CC47 - 6948 - 70
296LEUILE2DD47 - 6948 - 70
306LEUILE2EE47 - 6948 - 70
317THRTHR5AA7071
327THRTHR5BB7071
337THRTHR5CC7071
347THRTHR5DD7071
357THRTHR5EE7071
368ILEASP2AA71 - 7672 - 77
378ILEASP2BB71 - 7672 - 77
388ILEASP2CC71 - 7672 - 77
398ILEASP2DD71 - 7672 - 77
408ILEASP2EE71 - 7672 - 77
419ASPASP5AA7778
429ASPASP5BB7778
439ASPASP5CC7778
449ASPASP5DD7778
459ASPASP5EE7778
4610ILELYS2AA78 - 8079 - 81
4710ILELYS2BB78 - 8079 - 81
4810ILELYS2CC78 - 8079 - 81
4910ILELYS2DD78 - 8079 - 81
5010ILELYS2EE78 - 8079 - 81
5111SERSER3AA8182
5211SERSER3BB8182
5311SERSER3CC8182
5411SERSER3DD8182
5511SERSER3EE8182
5612TYRSER2AA82 - 8483 - 85
5712TYRSER2BB82 - 8483 - 85
5812TYRSER2CC82 - 8483 - 85
5912TYRSER2DD82 - 8483 - 85
6012TYRSER2EE82 - 8483 - 85
6113HISTHR5AA85 - 8686 - 87
6213HISTHR5BB85 - 8686 - 87
6313HISTHR5CC85 - 8686 - 87
6413HISTHR5DD85 - 8686 - 87
6513HISHIS5EE8586
DetailsTHIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 5 CHAINS FORMING A PENTAMER AS JUDGED BY CRYSTAL PACKING ANALYSIS. SIZE EXCLUSION CHROMATOGRAPHY WITH STATIC LIGHT SCATTERING SUPPORTS THE ASSIGNMENT OF A PENTAMER AS THE SIGNIFICANT OLIGOMERIZATION STATE IN SOLUTION.

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Components

#1: Protein
uncharacterized protein


Mass: 11147.415 Da / Num. of mol.: 5
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) uncultured marine organism (environmental samples)
Gene: Synthetic gene: The gene product was based on JCVI_PEP_1096686650277 from the Sorcerer II Global Ocean Sampling experiment
Plasmid: SpeedET / Production host: Escherichia coli (E. coli) / Strain (production host): HK100
#2: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 7 / Source method: isolated from a natural source / Formula: H2O
Sequence details1. THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED ...1. THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE FOLLOWED BY THE TARGET SEQUENCE. 2. THE SEQUENCE OF THIS PROTEIN WAS NOT AVAILABLE AT THE UNIPROT KNOWLEDGEBASE (UNIPROTKB) DATABASE AT THE TIME OF DEPOSITION. THE SEQUENCE INFORMATION IS AVAILABLE AT THE J. CRAIG VENTER INSTITUTE WITH ACCESSION CODE JCVI_PEP_1096686650277, FROM THE UNIPROT ARCHIVE (UNIPARC) UNDER ACCESSION ID UPI000148A153 AND FROM THE UNIPROT METAGENOMIC AND ENVIRONMENTAL SEQUENCES (UNIMES) DATABASE UNDER ACCESSION ID MES00005880000.

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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: 2.45 Å3/Da / Density % sol: 49.8 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 7.3
Details: NANODROP, 0.2M Ca Acetate, 20.0% PEG 3350, No Buffer pH 7.3, VAPOR DIFFUSION, SITTING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 0.95373, 0.97957, 0.97942
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Aug 19, 2007 / Details: Adjustable focusing mirrors in K-B geometry
RadiationMonochromator: Si(111) double crystal / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
IDWavelength (Å)Relative weight
10.953731
20.979571
30.979421
ReflectionResolution: 2.6→27.057 Å / Num. obs: 16122 / % possible obs: 95.7 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 58.562 Å2 / Rmerge(I) obs: 0.047 / Net I/σ(I): 9.46
Reflection shell
Resolution (Å)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. unique obsDiffraction-ID% possible all
2.6-2.690.4041.819182946192.4
2.69-2.80.3672.120723203196.2
2.8-2.930.322.521093225196.5
2.93-3.080.191419863068196.5
3.08-3.270.1545.420093111196.6
3.27-3.520.0768.420453151197
3.52-3.880.05711.420693257196.8
3.88-4.430.03515.619723104196.6
4.43-5.570.02820.820303164196.5
5.57-27.0570.02122.619823047191.6

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Phasing

PhasingMethod: MAD

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Processing

Software
NameVersionClassificationNB
REFMAC5.2.0019refinement
PHENIXrefinement
SHELXphasing
MolProbity3beta29model building
XSCALEdata scaling
PDB_EXTRACT3data extraction
MAR345CCDdata collection
XDSdata reduction
SHELXDphasing
autoSHARPphasing
RefinementMethod to determine structure: MAD / Resolution: 2.6→27.057 Å / Cor.coef. Fo:Fc: 0.935 / Cor.coef. Fo:Fc free: 0.897 / SU B: 36.405 / SU ML: 0.331 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.616 / ESU R Free: 0.339
Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES
Details: 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE ...Details: 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 3. ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY.
RfactorNum. reflection% reflectionSelection details
Rfree0.285 825 5.1 %RANDOM
Rwork0.235 ---
obs0.238 16120 96.58 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 32.898 Å2
Baniso -1Baniso -2Baniso -3
1--0.18 Å20 Å2-0.3 Å2
2--4.18 Å20 Å2
3----4.25 Å2
Refinement stepCycle: LAST / Resolution: 2.6→27.057 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3024 0 0 7 3031
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0130.0223068
X-RAY DIFFRACTIONr_bond_other_d0.0050.021944
X-RAY DIFFRACTIONr_angle_refined_deg1.2471.9734184
X-RAY DIFFRACTIONr_angle_other_deg0.87134873
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.425395
X-RAY DIFFRACTIONr_dihedral_angle_2_deg42.75826.66793
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.68415529
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.625153
X-RAY DIFFRACTIONr_chiral_restr0.0720.2543
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.023256
X-RAY DIFFRACTIONr_gen_planes_other0.0020.02486
X-RAY DIFFRACTIONr_nbd_refined0.1980.2551
X-RAY DIFFRACTIONr_nbd_other0.1920.21927
X-RAY DIFFRACTIONr_nbtor_refined0.1750.21507
X-RAY DIFFRACTIONr_nbtor_other0.0830.21687
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1620.261
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1250.27
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2330.215
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2420.22
X-RAY DIFFRACTIONr_mcbond_it0.7852.52174
X-RAY DIFFRACTIONr_mcbond_other0.2682.5797
X-RAY DIFFRACTIONr_mcangle_it1.02743327
X-RAY DIFFRACTIONr_scbond_it2.38161131
X-RAY DIFFRACTIONr_scangle_it3.7478857
Refine LS restraints NCS

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

Dom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A413TIGHT POSITIONAL0.030.05
2B413TIGHT POSITIONAL0.040.05
3C413TIGHT POSITIONAL0.030.05
4D413TIGHT POSITIONAL0.030.05
5E413TIGHT POSITIONAL0.030.05
1A424MEDIUM POSITIONAL0.230.5
2B424MEDIUM POSITIONAL0.370.5
3C424MEDIUM POSITIONAL0.240.5
4D424MEDIUM POSITIONAL0.280.5
5E424MEDIUM POSITIONAL0.230.5
1A40LOOSE POSITIONAL0.595
2B40LOOSE POSITIONAL1.175
3C40LOOSE POSITIONAL0.735
4D40LOOSE POSITIONAL0.675
5E40LOOSE POSITIONAL0.875
1A413TIGHT THERMAL0.060.5
2B413TIGHT THERMAL0.060.5
3C413TIGHT THERMAL0.060.5
4D413TIGHT THERMAL0.060.5
5E413TIGHT THERMAL0.040.5
1A424MEDIUM THERMAL0.552
2B424MEDIUM THERMAL0.592
3C424MEDIUM THERMAL0.532
4D424MEDIUM THERMAL0.462
5E424MEDIUM THERMAL0.372
1A40LOOSE THERMAL1.1210
2B40LOOSE THERMAL2.3510
3C40LOOSE THERMAL1.1710
4D40LOOSE THERMAL2.1510
5E40LOOSE THERMAL2.1710
LS refinement shellResolution: 2.6→2.667 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.367 59 -
Rwork0.365 1120 -
all-1179 -
obs--94.09 %
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)
18.5346-0.3198-3.03855.92612.19476.98620.14450.32240.60420.1944-0.02620.3556-0.7899-1.0617-0.11830.07160.1415-0.04160.07480.07750.1339-69.044441.436211.2369
22.89040.1050.07044.42541.07229.81490.2829-0.65780.30670.1306-0.2738-0.2933-0.48391.0906-0.0090.0363-0.2539-0.02780.32-0.07930.0915-48.194538.66820.0615
37.23330.5126-1.39735.4258-1.16814.8179-0.25950.2741-0.0959-0.13670.04120.42070.4408-1.4430.21840.2037-0.3944-0.02460.454-0.17280.1216-78.040221.24787.4305
45.84830.35622.24914.2232-0.35564.7359-0.2747-0.5854-0.45910.38040.2204-0.07920.63181.01780.05430.30880.51320.03450.43990.2510.1147-43.891516.47522.524
55.2511-0.61471.6584.3283-1.44972.5506-0.3119-0.5812-0.90670.0162-0.23260.31421.47590.16240.54450.7895-0.11630.2070.17750.00610.3439-62.61175.826613.6023
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
1X-RAY DIFFRACTION1AA2 - 863 - 87
2X-RAY DIFFRACTION2BB2 - 873 - 88
3X-RAY DIFFRACTION3CC2 - 873 - 88
4X-RAY DIFFRACTION4DD2 - 903 - 91
5X-RAY DIFFRACTION5EE3 - 854 - 86

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