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- PDB-4u8u: The Crystallographic structure of the giant hemoglobin from Gloss... -

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Basic information

Entry
Database: PDB / ID: 4u8u
TitleThe Crystallographic structure of the giant hemoglobin from Glossoscolex paulistus at 3.2 A resolution.
Components
  • Globin a chain
  • Globin b Chain
  • Globin c Chain
  • Globin d Chain
  • Linker L1
  • Linker L2
  • Linker L3
KeywordsOXYGEN STORAGE/Transport / Erythrocruorins / Glossoscolex paulistus / Giant extracellular hemoglobin / OXYGEN STORAGE-Transport complex
Function / homology
Function and homology information


hemoglobin complex / oxygen carrier activity / oxygen binding / iron ion binding / heme binding / extracellular region / metal ion binding
Similarity search - Function
Lipocalin - #620 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1520 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1530 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1540 / Annelid erythrocruorin linker subunit, C-terminal / Erythrocruorin linker subunit, C-terminal superfamily / Extracellular hemoglobin linker subunit, heterodimerisation domain / Annelid erythrocruorin linker subunit C-terminus / Globin, extracellular / Erythrocruorin ...Lipocalin - #620 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1520 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1530 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1540 / Annelid erythrocruorin linker subunit, C-terminal / Erythrocruorin linker subunit, C-terminal superfamily / Extracellular hemoglobin linker subunit, heterodimerisation domain / Annelid erythrocruorin linker subunit C-terminus / Globin, extracellular / Erythrocruorin / Low-density lipoprotein receptor domain class A / Low-density lipoprotein (LDL) receptor class A, conserved site / LDL-receptor class A (LDLRA) domain signature. / LDL-receptor class A (LDLRA) domain profile. / Low-density lipoprotein receptor domain class A / Low-density lipoprotein (LDL) receptor class A repeat / LDL receptor-like superfamily / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Globin/Protoglobin / Globins / Globin domain profile. / Globin-like / Globin / Globin / Lipocalin / Helix non-globular / Globin-like superfamily / Special / Beta Barrel / Orthogonal Bundle / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
CYANIDE ION / PROTOPORPHYRIN IX CONTAINING FE / Extracellular globin / Extracellular globin / Extracellular globin / Extracellular globin / Linker L1 / Linker L2 / Linker L3
Similarity search - Component
Biological speciesGlossoscolex paulistus (invertebrata)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 3.2 Å
AuthorsBachega, J.F.R. / Maluf, F.V. / Andi, B. / D'Muniz Pereira, H. / Carazzollea, M.F. / Orville, A. / Tabak, M. / Garratt, R.C. / Horjales, E.
CitationJournal: Acta Crystallogr.,Sect.D / Year: 2015
Title: The structure of the giant haemoglobin from Glossoscolex paulistus.
Authors: Ruggiero Bachega, J.F. / Vasconcelos Maluf, F. / Andi, B. / D'Muniz Pereira, H. / Falsarella Carazzollea, M. / Orville, A.M. / Tabak, M. / Brandao-Neto, J. / Garratt, R.C. / Horjales Reboredo, E.
History
DepositionAug 4, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 10, 2015Provider: repository / Type: Initial release
Revision 1.1Jun 17, 2015Group: Structure summary
Revision 1.2Jun 24, 2015Group: Database references
Revision 1.3Sep 7, 2016Group: Derived calculations / Non-polymer description
Revision 1.4Jul 29, 2020Group: Data collection / Derived calculations / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / pdbx_struct_conn_angle / pdbx_struct_oper_list / struct_conn / struct_conn_type / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr2_symmetry / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.ptnr3_symmetry / _pdbx_struct_conn_angle.value / _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.pdbx_role / _struct_conn.pdbx_value_order / _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.ptnr1_symmetry / _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.ptnr2_symmetry / _struct_conn_type.id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.5Dec 27, 2023Group: Data collection / Database references / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Globin a chain
B: Globin b Chain
C: Globin c Chain
D: Globin d Chain
E: Globin a chain
F: Globin b Chain
G: Globin c Chain
H: Globin d Chain
I: Globin a chain
J: Globin b Chain
K: Globin c Chain
L: Globin d Chain
M: Linker L1
N: Linker L2
O: Linker L3
P: Globin a chain
Q: Globin b Chain
R: Globin c Chain
S: Globin d Chain
T: Globin a chain
U: Globin b Chain
V: Globin c Chain
W: Globin d Chain
X: Globin a chain
Y: Globin b Chain
Z: Globin c Chain
a: Globin d Chain
b: Linker L1
c: Linker L2
d: Linker L3
e: Globin a chain
f: Globin b Chain
g: Globin c Chain
h: Globin d Chain
i: Globin a chain
j: Globin b Chain
k: Globin c Chain
l: Globin d Chain
m: Globin a chain
n: Globin b Chain
o: Globin c Chain
p: Globin d Chain
q: Linker L1
r: Linker L2
s: Linker L3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)855,005135
Polymers830,45845
Non-polymers24,54790
Water1086
1
A: Globin a chain
B: Globin b Chain
C: Globin c Chain
D: Globin d Chain
E: Globin a chain
F: Globin b Chain
G: Globin c Chain
H: Globin d Chain
I: Globin a chain
J: Globin b Chain
K: Globin c Chain
L: Globin d Chain
M: Linker L1
N: Linker L2
O: Linker L3
P: Globin a chain
Q: Globin b Chain
R: Globin c Chain
S: Globin d Chain
T: Globin a chain
U: Globin b Chain
V: Globin c Chain
W: Globin d Chain
X: Globin a chain
Y: Globin b Chain
Z: Globin c Chain
a: Globin d Chain
b: Linker L1
c: Linker L2
d: Linker L3
e: Globin a chain
f: Globin b Chain
g: Globin c Chain
h: Globin d Chain
i: Globin a chain
j: Globin b Chain
k: Globin c Chain
l: Globin d Chain
m: Globin a chain
n: Globin b Chain
o: Globin c Chain
p: Globin d Chain
q: Linker L1
r: Linker L2
s: Linker L3
hetero molecules

A: Globin a chain
B: Globin b Chain
C: Globin c Chain
D: Globin d Chain
E: Globin a chain
F: Globin b Chain
G: Globin c Chain
H: Globin d Chain
I: Globin a chain
J: Globin b Chain
K: Globin c Chain
L: Globin d Chain
M: Linker L1
N: Linker L2
O: Linker L3
P: Globin a chain
Q: Globin b Chain
R: Globin c Chain
S: Globin d Chain
T: Globin a chain
U: Globin b Chain
V: Globin c Chain
W: Globin d Chain
X: Globin a chain
Y: Globin b Chain
Z: Globin c Chain
a: Globin d Chain
b: Linker L1
c: Linker L2
d: Linker L3
e: Globin a chain
f: Globin b Chain
g: Globin c Chain
h: Globin d Chain
i: Globin a chain
j: Globin b Chain
k: Globin c Chain
l: Globin d Chain
m: Globin a chain
n: Globin b Chain
o: Globin c Chain
p: Globin d Chain
q: Linker L1
r: Linker L2
s: Linker L3
hetero molecules

A: Globin a chain
B: Globin b Chain
C: Globin c Chain
D: Globin d Chain
E: Globin a chain
F: Globin b Chain
G: Globin c Chain
H: Globin d Chain
I: Globin a chain
J: Globin b Chain
K: Globin c Chain
L: Globin d Chain
M: Linker L1
N: Linker L2
O: Linker L3
P: Globin a chain
Q: Globin b Chain
R: Globin c Chain
S: Globin d Chain
T: Globin a chain
U: Globin b Chain
V: Globin c Chain
W: Globin d Chain
X: Globin a chain
Y: Globin b Chain
Z: Globin c Chain
a: Globin d Chain
b: Linker L1
c: Linker L2
d: Linker L3
e: Globin a chain
f: Globin b Chain
g: Globin c Chain
h: Globin d Chain
i: Globin a chain
j: Globin b Chain
k: Globin c Chain
l: Globin d Chain
m: Globin a chain
n: Globin b Chain
o: Globin c Chain
p: Globin d Chain
q: Linker L1
r: Linker L2
s: Linker L3
hetero molecules

A: Globin a chain
B: Globin b Chain
C: Globin c Chain
D: Globin d Chain
E: Globin a chain
F: Globin b Chain
G: Globin c Chain
H: Globin d Chain
I: Globin a chain
J: Globin b Chain
K: Globin c Chain
L: Globin d Chain
M: Linker L1
N: Linker L2
O: Linker L3
P: Globin a chain
Q: Globin b Chain
R: Globin c Chain
S: Globin d Chain
T: Globin a chain
U: Globin b Chain
V: Globin c Chain
W: Globin d Chain
X: Globin a chain
Y: Globin b Chain
Z: Globin c Chain
a: Globin d Chain
b: Linker L1
c: Linker L2
d: Linker L3
e: Globin a chain
f: Globin b Chain
g: Globin c Chain
h: Globin d Chain
i: Globin a chain
j: Globin b Chain
k: Globin c Chain
l: Globin d Chain
m: Globin a chain
n: Globin b Chain
o: Globin c Chain
p: Globin d Chain
q: Linker L1
r: Linker L2
s: Linker L3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)3,420,018540
Polymers3,321,831180
Non-polymers98,188360
Water36020
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_655-x+1,-y,z1
crystal symmetry operation3_655-x+1,y,-z1
crystal symmetry operation4_555x,-y,-z1
Buried area529490 Å2
ΔGint-2247 kcal/mol
Surface area1149930 Å2
MethodPISA
Unit cell
Length a, b, c (Å)272.680, 319.900, 333.180
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number23
Space group name H-MI222
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
31
41
51
61
71
81
91
12
22
32
42
52
62
72
82
92
13
23
33
43
53
63
73
83
93
14
24
34
44
54
64
74
84
94
15
25
35
16
26
36
17
27
37

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111chain 'C' and (resseq 1:151 )
211chain 'G' and (resseq 1:151 )
311chain 'K' and (resseq 1:151 )
411chain 'R' and (resseq 1:151 )
511chain 'V' and (resseq 1:151 )
611chain 'Z' and (resseq 1:151 )
711chain 'g' and (resseq 1:151 )
811chain 'k' and (resseq 1:151 )
911chain 'o' and (resseq 1:151 )
112chain 'A' and (resseq 2:148 )
212chain 'E' and (resseq 2:148 )
312chain 'I' and (resseq 2:148 )
412chain 'P' and (resseq 2:148 )
512chain 'T' and (resseq 2:148 )
612chain 'X' and (resseq 2:148 )
712chain 'e' and (resseq 2:148 )
812chain 'i' and (resseq 2:148 )
912chain 'm' and (resseq 2:148 )
113chain 'B' and (resseq 1:142 )
213chain 'F' and (resseq 1:142 )
313chain 'J' and (resseq 1:142 )
413chain 'Q' and (resseq 1:142 )
513chain 'U' and (resseq 1:142 )
613chain 'Y' and (resseq 1:142 )
713chain 'f' and (resseq 1:142 )
813chain 'j' and (resseq 1:142 )
913chain 'n' and (resseq 1:142 )
114chain 'D' and (resseq 1:141 )
214chain 'H' and (resseq 1:141 )
314chain 'L' and (resseq 1:141 )
414chain 'S' and (resseq 1:141 )
514chain 'W' and (resseq 1:141 )
614chain 'a' and (resseq 1:141 )
714chain 'h' and (resseq 1:141 )
814chain 'l' and (resseq 1:141 )
914chain 'p' and (resseq 1:141 )
115chain 'M' and (resseq 4:225 )
215chain 'b' and (resseq 4:225 )
315chain 'q' and (resseq 4:225 )
116chain 'N' and (resseq 18:236 )
216chain 'c' and (resseq 18:236 )
316chain 'r' and (resseq 18:236 )
117chain 'O' and (resseq 6:218 )
217chain 'd' and (resseq 6:218 )
317chain 's' and (resseq 6:218 )

NCS ensembles :
ID
1
2
3
4
5
6
7

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Components

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Protein , 7 types, 45 molecules AEIPTXeimBFJQUYfjnCGKRVZgkoDHL...

#1: Protein
Globin a chain


Mass: 17235.375 Da / Num. of mol.: 9 / Source method: isolated from a natural source / Source: (natural) Glossoscolex paulistus (invertebrata) / References: UniProt: A0A0M3KKX5*PLUS
#2: Protein
Globin b Chain


Mass: 16248.312 Da / Num. of mol.: 9 / Source method: isolated from a natural source / Source: (natural) Glossoscolex paulistus (invertebrata) / References: UniProt: A0A0M3KKX6*PLUS
#3: Protein
Globin c Chain


Mass: 16943.453 Da / Num. of mol.: 9 / Source method: isolated from a natural source / Source: (natural) Glossoscolex paulistus (invertebrata) / References: UniProt: A0A0M3KKX7*PLUS
#4: Protein
Globin d Chain


Mass: 16124.284 Da / Num. of mol.: 9 / Source method: isolated from a natural source / Source: (natural) Glossoscolex paulistus (invertebrata) / References: UniProt: A0A0M3KKX8*PLUS
#5: Protein Linker L1


Mass: 25654.531 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Glossoscolex paulistus (invertebrata) / References: UniProt: A0A0M3KKX9*PLUS
#6: Protein Linker L2


Mass: 26777.207 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Glossoscolex paulistus (invertebrata) / References: UniProt: A0A0M3KKY0*PLUS
#7: Protein Linker L3


Mass: 24733.217 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Glossoscolex paulistus (invertebrata) / References: UniProt: A0A0M3KKY1*PLUS

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Sugars , 1 types, 3 molecules

#12: Sugar ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 5 types, 93 molecules

#8: Chemical...
ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME


Mass: 616.487 Da / Num. of mol.: 36 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#9: Chemical...
ChemComp-CYN / CYANIDE ION


Mass: 26.017 Da / Num. of mol.: 36 / Source method: obtained synthetically / Formula: CN
#10: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: Ca
#11: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Zn
#13: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 6 / 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: 4.37 Å3/Da / Density % sol: 71.88 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.5 / Details: PEG8000 10%, CaCl2 2.5 mM, TRIS 50 mM

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Data collection

DiffractionMean temperature: 103 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X26C / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Jul 8, 2009
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.2→50 Å / Num. obs: 237062 / % possible obs: 99.8 % / Redundancy: 4.7 % / Rmerge(I) obs: 0.112 / Net I/σ(I): 11.2
Reflection shellResolution: 3.2→3.37 Å / Redundancy: 4.2 % / Rmerge(I) obs: 0.5 / Mean I/σ(I) obs: 3.1 / % possible all: 99.2

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Processing

SoftwareName: PHENIX / Version: (phenix.refine: 1.8.1_1168) / Classification: refinement
RefinementResolution: 3.2→49.655 Å / SU ML: 0.41 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 24.12 / Stereochemistry target values: MLHL
RfactorNum. reflection% reflection
Rfree0.2352 11879 5.02 %
Rwork0.2155 --
obs0.2165 236866 99.68 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3.2→49.655 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms57480 0 1677 6 59163
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01260944
X-RAY DIFFRACTIONf_angle_d0.96282807
X-RAY DIFFRACTIONf_dihedral_angle_d15.55821561
X-RAY DIFFRACTIONf_chiral_restr0.0678523
X-RAY DIFFRACTIONf_plane_restr0.00310623
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11C1180X-RAY DIFFRACTIONPOSITIONAL
12G1180X-RAY DIFFRACTIONPOSITIONAL0.019
13K1180X-RAY DIFFRACTIONPOSITIONAL0.019
14R1180X-RAY DIFFRACTIONPOSITIONAL0.015
15V1180X-RAY DIFFRACTIONPOSITIONAL0.02
16Z1180X-RAY DIFFRACTIONPOSITIONAL0.02
17G1180X-RAY DIFFRACTIONPOSITIONAL0.014
18K1180X-RAY DIFFRACTIONPOSITIONAL0.019
19O1180X-RAY DIFFRACTIONPOSITIONAL0.02
21A1187X-RAY DIFFRACTIONPOSITIONAL
22E1187X-RAY DIFFRACTIONPOSITIONAL0.025
23I1187X-RAY DIFFRACTIONPOSITIONAL0.044
24P1187X-RAY DIFFRACTIONPOSITIONAL0.014
25T1187X-RAY DIFFRACTIONPOSITIONAL0.045
26X1187X-RAY DIFFRACTIONPOSITIONAL0.023
27E1187X-RAY DIFFRACTIONPOSITIONAL0.013
28I1187X-RAY DIFFRACTIONPOSITIONAL0.027
29M1187X-RAY DIFFRACTIONPOSITIONAL0.025
31B1148X-RAY DIFFRACTIONPOSITIONAL
32F1148X-RAY DIFFRACTIONPOSITIONAL0.021
33J1148X-RAY DIFFRACTIONPOSITIONAL0.022
34Q1148X-RAY DIFFRACTIONPOSITIONAL0.015
35U1148X-RAY DIFFRACTIONPOSITIONAL0.02
36Y1148X-RAY DIFFRACTIONPOSITIONAL0.023
37F1148X-RAY DIFFRACTIONPOSITIONAL0.015
38J1148X-RAY DIFFRACTIONPOSITIONAL0.021
39N1148X-RAY DIFFRACTIONPOSITIONAL0.022
41D1140X-RAY DIFFRACTIONPOSITIONAL
42H1140X-RAY DIFFRACTIONPOSITIONAL0.019
43L1140X-RAY DIFFRACTIONPOSITIONAL0.019
44S1140X-RAY DIFFRACTIONPOSITIONAL0.014
45W1140X-RAY DIFFRACTIONPOSITIONAL0.038
46A1140X-RAY DIFFRACTIONPOSITIONAL0.018
47H1140X-RAY DIFFRACTIONPOSITIONAL0.013
48L1140X-RAY DIFFRACTIONPOSITIONAL0.019
49P1140X-RAY DIFFRACTIONPOSITIONAL0.018
51M1754X-RAY DIFFRACTIONPOSITIONAL
52B1754X-RAY DIFFRACTIONPOSITIONAL0.064
53Q1754X-RAY DIFFRACTIONPOSITIONAL0.064
61N1713X-RAY DIFFRACTIONPOSITIONAL
62C1713X-RAY DIFFRACTIONPOSITIONAL0.016
63R1713X-RAY DIFFRACTIONPOSITIONAL0.086
71O1686X-RAY DIFFRACTIONPOSITIONAL
72D1686X-RAY DIFFRACTIONPOSITIONAL0.016
73S1686X-RAY DIFFRACTIONPOSITIONAL0.016
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.2-3.23640.42214270.4097379X-RAY DIFFRACTION99
3.2364-3.27440.3643960.35997396X-RAY DIFFRACTION99
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