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- PDB-2xvt: Structure of the extracellular domain of human RAMP2 -

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Basic information

Entry
Database: PDB / ID: 2xvt
TitleStructure of the extracellular domain of human RAMP2
ComponentsRECEPTOR ACTIVITY-MODIFYING PROTEIN 2
KeywordsMEMBRANE PROTEIN / TRANSMEMBRANE / RECEPTOR TRANSPORT / PROTEIN-TRAFFICKING / GPCR / CRLR / CGRP / ADRENOMEDULIN
Function / homology
Function and homology information


basement membrane assembly / vascular associated smooth muscle cell development / adrenomedullin binding / adrenomedullin receptor activity / adrenomedullin receptor complex / adrenomedullin receptor signaling pathway / Calcitonin-like ligand receptors / positive regulation of vasculogenesis / bicellular tight junction assembly / regulation of G protein-coupled receptor signaling pathway ...basement membrane assembly / vascular associated smooth muscle cell development / adrenomedullin binding / adrenomedullin receptor activity / adrenomedullin receptor complex / adrenomedullin receptor signaling pathway / Calcitonin-like ligand receptors / positive regulation of vasculogenesis / bicellular tight junction assembly / regulation of G protein-coupled receptor signaling pathway / adherens junction assembly / negative regulation of vascular permeability / sprouting angiogenesis / cellular response to vascular endothelial growth factor stimulus / vasculogenesis / coreceptor activity / negative regulation of endothelial cell apoptotic process / clathrin-coated pit / cellular response to hormone stimulus / protein localization to plasma membrane / intracellular protein transport / adenylate cyclase-activating G protein-coupled receptor signaling pathway / receptor internalization / regulation of blood pressure / positive regulation of angiogenesis / calcium ion transport / protein transport / heart development / G alpha (s) signalling events / angiogenesis / lysosome / receptor complex / G protein-coupled receptor signaling pathway / positive regulation of gene expression / cell surface / plasma membrane / cytoplasm
Similarity search - Function
Receptor activity modifying family / Receptor activity modifying protein / RAMP domain superfamily / Receptor activity modifying family / DNA polymerase; domain 1 / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Receptor activity-modifying protein 2
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.05 Å
AuthorsQuigley, A. / Pike, A.C.W. / Burgess-Brown, N. / Krojer, T. / Shrestha, L. / Goubin, S. / Kim, J. / Das, S. / Muniz, J.R.C. / Canning, P. ...Quigley, A. / Pike, A.C.W. / Burgess-Brown, N. / Krojer, T. / Shrestha, L. / Goubin, S. / Kim, J. / Das, S. / Muniz, J.R.C. / Canning, P. / Chaikuad, A. / Vollmar, M. / von Delft, F. / Arrowsmith, C.H. / Weigelt, J. / Edwards, A.M. / Bountra, C. / Barr, A.J. / Carpenter, E.P.
CitationJournal: To be Published
Title: Structure of the Extracellular Domain of Human Ramp2
Authors: Quigley, A. / Pike, A.C.W. / Burgess-Brown, N. / Krojer, T. / Shrestha, L. / Goubin, S. / Kim, J. / Das, S. / Muniz, J.R.C. / Canning, P. / Chaikuad, A. / Vollmar, M. / von Delft, F. / ...Authors: Quigley, A. / Pike, A.C.W. / Burgess-Brown, N. / Krojer, T. / Shrestha, L. / Goubin, S. / Kim, J. / Das, S. / Muniz, J.R.C. / Canning, P. / Chaikuad, A. / Vollmar, M. / von Delft, F. / Arrowsmith, C.H. / Weigelt, J. / Edwards, A.M. / Bountra, C. / Barr, A.J. / Carpenter, E.P.
History
DepositionOct 31, 2010Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 29, 2010Provider: repository / Type: Initial release
Revision 1.1Mar 6, 2013Group: Data collection
Revision 1.2Dec 10, 2014Group: Data collection / Version format compliance
Revision 1.3Jan 24, 2018Group: Database references / Category: citation_author / Item: _citation_author.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: RECEPTOR ACTIVITY-MODIFYING PROTEIN 2
B: RECEPTOR ACTIVITY-MODIFYING PROTEIN 2
C: RECEPTOR ACTIVITY-MODIFYING PROTEIN 2
D: RECEPTOR ACTIVITY-MODIFYING PROTEIN 2
E: RECEPTOR ACTIVITY-MODIFYING PROTEIN 2
F: RECEPTOR ACTIVITY-MODIFYING PROTEIN 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)65,3599
Polymers65,2396
Non-polymers1203
Water4,107228
1
D: RECEPTOR ACTIVITY-MODIFYING PROTEIN 2
E: RECEPTOR ACTIVITY-MODIFYING PROTEIN 2
F: RECEPTOR ACTIVITY-MODIFYING PROTEIN 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,7005
Polymers32,6193
Non-polymers802
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4110 Å2
ΔGint-41.4 kcal/mol
Surface area11940 Å2
MethodPISA
2
A: RECEPTOR ACTIVITY-MODIFYING PROTEIN 2
B: RECEPTOR ACTIVITY-MODIFYING PROTEIN 2
C: RECEPTOR ACTIVITY-MODIFYING PROTEIN 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,6604
Polymers32,6193
Non-polymers401
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4090 Å2
ΔGint-35.1 kcal/mol
Surface area11840 Å2
MethodPISA
3
A: RECEPTOR ACTIVITY-MODIFYING PROTEIN 2


Theoretical massNumber of molelcules
Total (without water)10,8731
Polymers10,8731
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
B: RECEPTOR ACTIVITY-MODIFYING PROTEIN 2


Theoretical massNumber of molelcules
Total (without water)10,8731
Polymers10,8731
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
C: RECEPTOR ACTIVITY-MODIFYING PROTEIN 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)10,9132
Polymers10,8731
Non-polymers401
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
6
D: RECEPTOR ACTIVITY-MODIFYING PROTEIN 2


Theoretical massNumber of molelcules
Total (without water)10,8731
Polymers10,8731
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
7
E: RECEPTOR ACTIVITY-MODIFYING PROTEIN 2


Theoretical massNumber of molelcules
Total (without water)10,8731
Polymers10,8731
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
8
F: RECEPTOR ACTIVITY-MODIFYING PROTEIN 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)10,9533
Polymers10,8731
Non-polymers802
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)59.759, 90.984, 92.056
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
31C
41D
51E
61F
12A
22B
32C
42D
52E
62F
13A
23B
33C
43D
53E
63F
14A
24B
34C
44D
54E
64F
15A
25B
35C
45D
55E
65F
16A
26B
36C
46D
56E
66F
17A
27B
37C
47D
57E
67F
18A
28B
38C
48D
58E
68F
19A
29B
39C
49D
59E
69F
110A
210B
310C
410D
510E
610F
111A
211B
311C
411D
511E
611F

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1112A61 - 69
2112B61 - 69
3112C61 - 69
4112D61 - 69
5112E61 - 69
6112F61 - 69
1125A70 - 71
2125B70 - 71
3125C70 - 71
4125D70 - 71
5125E70 - 71
6125F70 - 71
1132A72 - 76
2132B72 - 76
3132C72 - 76
4132D72 - 76
5132E72 - 76
6132F72 - 76
1146A77 - 80
2146B77 - 80
3146C77 - 80
4146D77 - 80
5146E77 - 80
6146F77 - 80
1152A81 - 87
2152B81 - 87
3152C81 - 87
4152D81 - 87
5152E81 - 87
6152F81 - 87
1164A105 - 110
2164B105 - 110
3164C105 - 110
4164D105 - 110
5164E105 - 110
6164F105 - 110
1172A111 - 117
2172B111 - 117
3172C111 - 117
4172D111 - 117
5172E111 - 117
6172F111 - 117
1183A119 - 128
2183B119 - 128
3183C119 - 128
4183D119 - 128
5183E119 - 128
6183F119 - 128
1196A129 - 132
2196B129 - 132
3196C129 - 132
4196D129 - 132
5196E129 - 132
6196F129 - 132
11103A88 - 95
21103B88 - 95
31103C88 - 95
41103D88 - 95
51103E88 - 95
61103F88 - 95
11113A96 - 104
21113B96 - 104
31113C96 - 104
41113D96 - 104
51113E96 - 104
61113F96 - 104

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11

NCS oper:
IDCodeMatrixVector
1given(-0.47561, 0.73733, -0.47972), (-0.85187, -0.25008, 0.4602), (0.21935, 0.62753, 0.74705)76.90105, 73.44485, -24.33546
2given(-0.492, -0.852, 0.177), (0.715, -0.28, 0.641), (-0.497, 0.442, 0.747)106.11459, -21.31891, 22.70615
3given(0.482, -0.732, 0.481), (-0.85, -0.257, 0.46), (-0.213, -0.631, -0.746)16.38894, 73.23527, 70.09725
4given(-1, 0.008, 0.018), (0.008, 1, -0.01), (-0.019, -0.01, -1)93.41971, -0.67687, 47.44164
5given(0.485, 0.856, -0.179), (0.732, -0.285, 0.619), (0.479, -0.432, -0.764)-11.76748, -22.21119, 24.33679

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Components

#1: Protein
RECEPTOR ACTIVITY-MODIFYING PROTEIN 2 / CALCITONIN-RECEPTOR-LIKE RECEPTOR ACTIVITY-MODIFYING PROTEIN 2 / CRLR ACTIVITY-MODIFYING PROTEIN 2 / RAMP2


Mass: 10873.156 Da / Num. of mol.: 6 / Fragment: EXTRACELLULAR DOMAIN, RESIDUES 48-139
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PNIC28-BSA4 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): R3-PRARE2 / References: UniProt: O60895
#2: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Ca
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 228 / 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: 2

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Sample preparation

CrystalDensity Matthews: 1.75 Å3/Da / Density % sol: 35.87 % / Description: NONE
Crystal growpH: 7.5
Details: 0.1M CALCIUM CHLORIDE, 26% PEG MONOMETHYLETHER 350, 0.1M HEPES PH 7.5

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Data collection

Diffraction
IDMean temperature (K)Crystal-ID
11001
21001
Diffraction source
SourceSiteBeamlineIDWavelengthWavelength (Å)
SYNCHROTRONDiamond I0210.9795
SYNCHROTRONDiamond I0420.9803, 0.9806, 0.9763
Detector
TypeIDDetectorDateDetails
ADSC CCD1CCDAug 11, 2010NULL: NULL
ADSC CCD2CCD
Radiation
IDProtocolMonochromatic (M) / Laue (L)Scattering typeWavelength-ID
1SINGLE WAVELENGTHMx-ray1
2MADMx-ray1
Radiation wavelength
IDWavelength (Å)Relative weight
10.97951
20.98031
30.98061
40.97631
ReflectionResolution: 2.05→50.13 Å / Num. obs: 32252 / % possible obs: 99.7 % / Observed criterion σ(I): 0 / Redundancy: 6.7 % / Biso Wilson estimate: 22.244 Å2 / Rmerge(I) obs: 0.16 / Net I/σ(I): 7.8
Reflection shellResolution: 2.05→2.16 Å / Redundancy: 4.6 % / Rmerge(I) obs: 0.77 / Mean I/σ(I) obs: 2 / % possible all: 98.2

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Processing

Software
NameVersionClassification
REFMAC5.5.0110refinement
MOSFLMdata reduction
SCALAdata scaling
autoSHARPphasing
RefinementMethod to determine structure: MAD
Starting model: NONE

Resolution: 2.05→64.71 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.934 / SU B: 10.876 / SU ML: 0.143 / Cross valid method: THROUGHOUT / ESU R: 0.226 / ESU R Free: 0.19 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.24636 1627 5.1 %RANDOM
Rwork0.1969 ---
obs0.19944 30525 99.74 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å
Displacement parametersBiso mean: 21.316 Å2
Baniso -1Baniso -2Baniso -3
1--1.74 Å20 Å20 Å2
2--2.04 Å20 Å2
3----0.3 Å2
Refinement stepCycle: LAST / Resolution: 2.05→64.71 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3924 0 3 228 4155
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0160.0214092
X-RAY DIFFRACTIONr_bond_other_d0.0010.022724
X-RAY DIFFRACTIONr_angle_refined_deg1.5591.9065579
X-RAY DIFFRACTIONr_angle_other_deg1.4773.0076551
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.215463
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.65824.103234
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.00715629
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.591521
X-RAY DIFFRACTIONr_chiral_restr0.1050.2564
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.0214560
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02911
X-RAY DIFFRACTIONr_nbd_refined0.2240.2859
X-RAY DIFFRACTIONr_nbd_other0.170.22640
X-RAY DIFFRACTIONr_nbtor_refined0.1930.21986
X-RAY DIFFRACTIONr_nbtor_other0.090.21840
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1870.2199
X-RAY DIFFRACTIONr_xyhbond_nbd_other0.0220.21
X-RAY DIFFRACTIONr_metal_ion_refined0.1620.212
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.20.224
X-RAY DIFFRACTIONr_symmetry_vdw_other0.1830.255
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1450.218
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it2.36532359
X-RAY DIFFRACTIONr_mcbond_other0.8443912
X-RAY DIFFRACTIONr_mcangle_it3.33253831
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it5.46381733
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it6.767111748
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 / Weight position: 10

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)
11A54tight positional0.09
12B54tight positional0.09
13C54tight positional0.1
14D54tight positional0.09
15E54tight positional0.08
16F54tight positional0.08
31A30tight positional0.16
32B30tight positional0.07
33C30tight positional0.09
34D30tight positional0.11
35E30tight positional0.09
36F30tight positional0.12
51A42tight positional0.09
52B42tight positional0.09
53C42tight positional0.13
54D42tight positional0.11
55E42tight positional0.12
56F42tight positional0.09
71A40tight positional0.09
72B40tight positional0.09
73C40tight positional0.09
74D40tight positional0.06
75E40tight positional0.07
76F40tight positional0.1
81A60tight positional0.09
82B60tight positional0.09
83C60tight positional0.13
84D60tight positional0.14
85E60tight positional0.1
86F60tight positional0.11
101A47tight positional0.11
102B47tight positional0.12
103C47tight positional0.14
104D47tight positional0.12
105E47tight positional0.12
106F47tight positional0.19
111A54tight positional0.08
112B54tight positional0.08
113C54tight positional0.08
114D54tight positional0.14
115E54tight positional0.09
116F54tight positional0.09
11A78medium positional0.19
12B78medium positional0.18
13C78medium positional0.21
14D78medium positional0.25
15E78medium positional0.18
16F78medium positional0.18
21A12medium positional0.54
22B12medium positional0.29
23C12medium positional0.31
24D12medium positional0.25
25E12medium positional0.58
26F12medium positional0.33
31A41medium positional0.28
32B41medium positional0.18
33C41medium positional0.17
34D41medium positional0.15
35E41medium positional0.19
36F41medium positional0.18
51A58medium positional0.22
52B58medium positional0.19
53C58medium positional0.23
54D58medium positional0.19
55E58medium positional0.2
56F58medium positional0.19
61A75medium positional0.26
62B75medium positional0.17
63C75medium positional0.18
64D75medium positional0.24
65E75medium positional0.22
66F75medium positional0.2
71A55medium positional0.14
72B55medium positional0.13
73C55medium positional0.15
74D55medium positional0.16
75E55medium positional0.15
76F55medium positional0.23
21A16loose positional1.31
22B16loose positional0.62
23C16loose positional0.63
24D16loose positional0.66
25E16loose positional1.22
26F16loose positional0.64
41A54loose positional0.26
42B54loose positional0.23
43C54loose positional0.46
44D54loose positional0.25
45E54loose positional0.27
46F54loose positional0.39
81A91loose positional0.38
82B91loose positional0.45
83C91loose positional0.56
84D91loose positional0.44
85E91loose positional0.42
86F91loose positional0.55
91A40loose positional0.5
92B40loose positional0.23
93C40loose positional0.25
94D40loose positional0.25
95E40loose positional0.55
96F40loose positional0.26
101A61loose positional0.63
102B61loose positional0.73
103C61loose positional0.64
104D61loose positional0.68
105E61loose positional0.6
106F61loose positional0.81
111A77loose positional0.14
112B77loose positional0.21
113C77loose positional0.17
114D77loose positional0.23
115E77loose positional0.15
116F77loose positional0.19
11A54tight thermal1.87
12B54tight thermal1.57
13C54tight thermal1.64
14D54tight thermal1.59
15E54tight thermal1.38
16F54tight thermal1.41
31A30tight thermal3.54
32B30tight thermal1.77
33C30tight thermal2.89
34D30tight thermal2.03
35E30tight thermal3.18
36F30tight thermal2.71
51A42tight thermal1.67
52B42tight thermal1.65
53C42tight thermal1.81
54D42tight thermal1.18
55E42tight thermal1.27
56F42tight thermal1.54
71A40tight thermal1.46
72B40tight thermal1.8
73C40tight thermal1.63
74D40tight thermal1.54
75E40tight thermal1.24
76F40tight thermal1.4
81A60tight thermal1.93
82B60tight thermal1.24
83C60tight thermal1.8
84D60tight thermal2.03
85E60tight thermal1.81
86F60tight thermal1.28
101A47tight thermal1.62
102B47tight thermal1.8
103C47tight thermal1.53
104D47tight thermal1.63
105E47tight thermal1.41
106F47tight thermal2.22
111A54tight thermal1.49
112B54tight thermal1.29
113C54tight thermal1.46
114D54tight thermal1.67
115E54tight thermal1.56
116F54tight thermal1.34
11A78medium thermal3.16
12B78medium thermal3.77
13C78medium thermal3.69
14D78medium thermal3.1
15E78medium thermal3.2
16F78medium thermal2.71
21A12medium thermal4
22B12medium thermal1.55
23C12medium thermal1.67
24D12medium thermal3.09
25E12medium thermal2.57
26F12medium thermal2.04
31A41medium thermal4.42
32B41medium thermal1.99
33C41medium thermal3.41
34D41medium thermal2.97
35E41medium thermal4.19
36F41medium thermal3.23
51A58medium thermal2.15
52B58medium thermal2.18
53C58medium thermal2.29
54D58medium thermal2.01
55E58medium thermal2.8
56F58medium thermal2.45
61A75medium thermal2.36
62B75medium thermal2.55
63C75medium thermal2.5
64D75medium thermal2.72
65E75medium thermal3.43
66F75medium thermal2.87
71A55medium thermal1.83
72B55medium thermal1.7
73C55medium thermal1.79
74D55medium thermal1.86
75E55medium thermal1.02
76F55medium thermal1.46
21A16loose thermal4.23
22B16loose thermal5.98
23C16loose thermal2.44
24D16loose thermal4.21
25E16loose thermal4.31
26F16loose thermal4.04
41A54loose thermal2.4
42B54loose thermal3.09
43C54loose thermal3.1
44D54loose thermal2.77
45E54loose thermal3.04
46F54loose thermal3.03
81A91loose thermal2.3
82B91loose thermal2.55
83C91loose thermal2.02
84D91loose thermal2.63
85E91loose thermal2.19
86F91loose thermal2.33
91A40loose thermal3.87
92B40loose thermal2.21
93C40loose thermal3.21
94D40loose thermal1.85
95E40loose thermal4.26
96F40loose thermal3.24
101A61loose thermal2.53
102B61loose thermal4.44
103C61loose thermal4.7
104D61loose thermal4.29
105E61loose thermal2.58
106F61loose thermal2.99
111A77loose thermal2.11
112B77loose thermal2.18
113C77loose thermal2.09
114D77loose thermal2.62
115E77loose thermal2.36
116F77loose thermal2.25
LS refinement shellResolution: 2.049→2.103 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.339 127 -
Rwork0.322 2192 -
obs--98.72 %
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)
13.26290.2950.278910.7463-1.6483.7402-0.0301-0.1603-0.28650.10870.0257-0.72550.00720.23310.00440.004-0.0113-0.01130.16280.02140.10472.142521.797313.6465
25.1786-0.73652.58691.3971-0.95785.9878-0.0366-0.0946-0.2053-0.01630.0385-0.0360.1627-0.092-0.00190.0703-0.04410.01210.10270.0310.073951.784713.089715.1465
35.29731.1941-1.48562.8738-0.82362.7030.1430.00090.38920.04470.01420.2455-0.2321-0.1224-0.15720.09480.0236-0.0020.10270.01210.047555.047533.03846.5274
45.72440.16512.36361.3960.34354.8104-0.05880.2062-0.21120.00110.06050.07380.1693-0.0005-0.00170.08470.03260.02010.0929-0.0180.058542.006112.565430.8212
53.5622-1.0252-0.199111.32432.22653.3861-0.0720.1178-0.3269-0.06570.01660.9268-0.0102-0.24540.05540.00540.0144-0.00840.199-0.01260.130121.625621.670632.1642
65.8905-1.3334-3.1733.09340.90913.77450.1652-0.03530.5002-0.01010.0383-0.3079-0.20380.055-0.20350.101-0.0133-0.01730.062-0.01280.086538.750832.993639.2865
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A58 - 135
2X-RAY DIFFRACTION2B58 - 135
3X-RAY DIFFRACTION3C58 - 136
4X-RAY DIFFRACTION4D57 - 135
5X-RAY DIFFRACTION5E58 - 134
6X-RAY DIFFRACTION6F58 - 136

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