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- PDB-4ch2: Low-salt crystal structure of a thrombin-GpIbalpha peptide complex -

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Basic information

Entry
Database: PDB / ID: 4ch2
TitleLow-salt crystal structure of a thrombin-GpIbalpha peptide complex
Components
  • PLATELET GLYCOPROTEIN IB ALPHA CHAIN, RESIDUES 287-300
  • THROMBIN, HEAVY CHAIN
  • THROMBIN, LIGHT CHAIN
KeywordsHYDROLASE/PEPTIDE / HYDROLASE-PEPTIDE COMPLEX
Function / homology
Function and homology information


thrombin-activated receptor activity / glycoprotein Ib-IX-V complex / Enhanced binding of GP1BA variant to VWF multimer:collagen / Defective binding of VWF variant to GPIb:IX:V / positive regulation of leukocyte tethering or rolling / blood coagulation, intrinsic pathway / Defective F9 activation / Platelet Adhesion to exposed collagen / positive regulation of platelet activation / megakaryocyte development ...thrombin-activated receptor activity / glycoprotein Ib-IX-V complex / Enhanced binding of GP1BA variant to VWF multimer:collagen / Defective binding of VWF variant to GPIb:IX:V / positive regulation of leukocyte tethering or rolling / blood coagulation, intrinsic pathway / Defective F9 activation / Platelet Adhesion to exposed collagen / positive regulation of platelet activation / megakaryocyte development / GP1b-IX-V activation signalling / cytolysis by host of symbiont cells / positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway / thrombospondin receptor activity / Defective factor XII causes hereditary angioedema / thrombin-activated receptor signaling pathway / thrombin / neutrophil-mediated killing of gram-negative bacterium / regulation of blood coagulation / Defective F8 cleavage by thrombin / ligand-gated ion channel signaling pathway / Platelet Aggregation (Plug Formation) / negative regulation of astrocyte differentiation / positive regulation of collagen biosynthetic process / negative regulation of platelet activation / negative regulation of blood coagulation / positive regulation of blood coagulation / negative regulation of fibrinolysis / regulation of cytosolic calcium ion concentration / Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus / Gamma-carboxylation of protein precursors / Common Pathway of Fibrin Clot Formation / Removal of aminoterminal propeptides from gamma-carboxylated proteins / fibrinolysis / negative regulation of proteolysis / Intrinsic Pathway of Fibrin Clot Formation / release of sequestered calcium ion into cytosol / negative regulation of cytokine production involved in inflammatory response / extracellular matrix / positive regulation of release of sequestered calcium ion into cytosol / Peptide ligand-binding receptors / Regulation of Complement cascade / acute-phase response / positive regulation of receptor signaling pathway via JAK-STAT / Cell surface interactions at the vascular wall / lipopolysaccharide binding / growth factor activity / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / cell morphogenesis / positive regulation of insulin secretion / platelet activation / positive regulation of protein localization to nucleus / response to wounding / Golgi lumen / antimicrobial humoral immune response mediated by antimicrobial peptide / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / positive regulation of reactive oxygen species metabolic process / blood coagulation / heparin binding / regulation of cell shape / Thrombin signalling through proteinase activated receptors (PARs) / positive regulation of protein phosphorylation / positive regulation of cell growth / : / G alpha (q) signalling events / blood microparticle / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / cell surface receptor signaling pathway / cell adhesion / receptor ligand activity / endoplasmic reticulum lumen / external side of plasma membrane / signaling receptor binding / serine-type endopeptidase activity / positive regulation of cell population proliferation / calcium ion binding / cell surface / proteolysis / extracellular space / extracellular exosome / extracellular region / membrane / plasma membrane
Similarity search - Function
Leucine rich repeat N-terminal domain / Leucine-rich repeat N-terminal domain / Leucine rich repeat N-terminal domain / Cysteine-rich flanking region, C-terminal / Leucine rich repeat C-terminal domain / Leucine-rich repeats, bacterial type / Prothrombin/thrombin / Thrombin light chain / Thrombin light chain domain superfamily / : ...Leucine rich repeat N-terminal domain / Leucine-rich repeat N-terminal domain / Leucine rich repeat N-terminal domain / Cysteine-rich flanking region, C-terminal / Leucine rich repeat C-terminal domain / Leucine-rich repeats, bacterial type / Prothrombin/thrombin / Thrombin light chain / Thrombin light chain domain superfamily / : / Thrombin light chain / Kringle domain / Kringle / Kringle, conserved site / Kringle superfamily / Kringle domain signature. / Kringle domain profile. / Kringle domain / Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain / Gamma-carboxyglutamic acid-rich (GLA) domain / Gamma-carboxyglutamic acid-rich (GLA) domain superfamily / Vitamin K-dependent carboxylation domain. / Gla domain profile. / Domain containing Gla (gamma-carboxyglutamate) residues. / Leucine rich repeat / Leucine-rich repeat, typical subtype / Leucine-rich repeats, typical (most populated) subfamily / Kringle-like fold / Leucine-rich repeat profile. / Leucine-rich repeat / Leucine-rich repeat domain superfamily / Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Serine proteases, trypsin family, histidine active site. / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, serine active site. / Serine proteases, trypsin domain profile. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Trypsin-like serine proteases / Thrombin, subunit H / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
D-Phe-Pro-Arg-CH2Cl / Chem-0G6 / Prothrombin / Platelet glycoprotein Ib alpha chain
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.6 Å
AuthorsLechtenberg, B.C. / Freund, S.M.V. / Huntington, J.A.
CitationJournal: J.Mol.Biol. / Year: 2014
Title: Gpibalpha Interacts Exclusively with Exosite II of Thrombin
Authors: Lechtenberg, B.C. / Freund, S.M.V. / Huntington, J.A.
History
DepositionNov 28, 2013Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 11, 2013Provider: repository / Type: Initial release
Revision 1.1Dec 18, 2013Group: Database references
Revision 1.2Dec 25, 2013Group: Non-polymer description
Revision 1.3Feb 12, 2014Group: Database references
Revision 1.4Dec 20, 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 / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim / 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 / _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_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_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_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _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_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 / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.5Oct 23, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: THROMBIN, LIGHT CHAIN
B: THROMBIN, HEAVY CHAIN
C: THROMBIN, LIGHT CHAIN
D: THROMBIN, HEAVY CHAIN
P: PLATELET GLYCOPROTEIN IB ALPHA CHAIN, RESIDUES 287-300
Q: PLATELET GLYCOPROTEIN IB ALPHA CHAIN, RESIDUES 287-300
hetero molecules


Theoretical massNumber of molelcules
Total (without water)72,94714
Polymers71,6256
Non-polymers1,3228
Water8,521473
1
A: THROMBIN, LIGHT CHAIN
B: THROMBIN, HEAVY CHAIN
P: PLATELET GLYCOPROTEIN IB ALPHA CHAIN, RESIDUES 287-300
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,4747
Polymers35,8123
Non-polymers6614
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5240 Å2
ΔGint-19.4 kcal/mol
Surface area15360 Å2
MethodPISA
2
C: THROMBIN, LIGHT CHAIN
D: THROMBIN, HEAVY CHAIN
Q: PLATELET GLYCOPROTEIN IB ALPHA CHAIN, RESIDUES 287-300
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,4747
Polymers35,8123
Non-polymers6614
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4970 Å2
ΔGint-18.4 kcal/mol
Surface area14890 Å2
MethodPISA
Unit cell
Length a, b, c (Å)149.570, 50.560, 76.280
Angle α, β, γ (deg.)90.00, 97.15, 90.00
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11B-2196-

HOH

Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21C
12B
22D

NCS domain segments:

Component-ID: _ / Refine code: _

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11GLUGLUSERSERAA290 - 3156 - 31
21GLUGLUSERSERCC290 - 3156 - 31
12ILEILEGLYGLYBB321 - 5781 - 258
22ILEILEGLYGLYDD321 - 5781 - 258

NCS ensembles :
ID
1
2

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Components

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Protein/peptide , 2 types, 4 molecules ACPQ

#1: Protein/peptide THROMBIN, LIGHT CHAIN / COAGULATION FACTOR II


Mass: 4096.534 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PET23 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): STAR, PLYSS / References: UniProt: P00734, thrombin
#3: Protein/peptide PLATELET GLYCOPROTEIN IB ALPHA CHAIN, RESIDUES 287-300 / GP-IB ALPHA / GPIB-ALPHA / GPIBA / GLYCOPROTEIN IBALPHA / ANTIGEN CD42B-ALPHA / GPIBALPHA PEPTIDE


Mass: 1935.584 Da / Num. of mol.: 2 / Fragment: C-TERMINAL FRAGMENT OF GPIBALPHA, 271-284 / Source method: obtained synthetically / Details: ALL THREE TYROSINE RESIDUES ARE PHOSPHORYLATED / Source: (synth.) HOMO SAPIENS (human) / References: UniProt: P07359

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Protein , 1 types, 2 molecules BD

#2: Protein THROMBIN, HEAVY CHAIN


Mass: 29780.219 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PET23 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): STAR, PLYSS / References: UniProt: P00734, thrombin

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Non-polymers , 4 types, 481 molecules

#4: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C3H8O3
#5: Chemical ChemComp-0G6 / D-phenylalanyl-N-[(2S,3S)-6-{[amino(iminio)methyl]amino}-1-chloro-2-hydroxyhexan-3-yl]-L-prolinamide / PPACK


Type: peptide-like, Peptide-like / Class: Inhibitor / Mass: 453.986 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C21H34ClN6O3 / References: D-Phe-Pro-Arg-CH2Cl
#6: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Na
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 473 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY
Nonpolymer detailsDEOXY-CHLOROMETHYL-ARGININE (ACL): MODIFIED BY REACTION WITH CATALYTIC HIS AND SER

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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: 2.15 Å3/Da / Density % sol: 42.82 % / Description: NONE
Crystal growpH: 7.4 / Details: 50 MM SODIUM FORMATE, 16% PEG-3350, pH 7.4

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.8
DetectorType: ADSC CCD / Detector: CCD / Date: Apr 29, 2010
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.8 Å / Relative weight: 1
ReflectionResolution: 1.6→41.2 Å / Num. obs: 72363 / % possible obs: 96.8 % / Observed criterion σ(I): 0 / Redundancy: 2.5 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 9.6
Reflection shellResolution: 1.6→1.69 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.5 / Mean I/σ(I) obs: 1.8 / % possible all: 98.4

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Processing

Software
NameVersionClassification
REFMAC5.7.0029refinement
MOSFLMdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1PPB

1ppb


Resolution: 1.6→37.1 Å / Cor.coef. Fo:Fc: 0.968 / Cor.coef. Fo:Fc free: 0.956 / SU B: 3.027 / SU ML: 0.055 / Cross valid method: THROUGHOUT / ESU R: 0.086 / ESU R Free: 0.087 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES WITH TLS ADDED. DISORDERED REGIONS AND SIDE CHAINS ARE NOT MODELED.
RfactorNum. reflection% reflectionSelection details
Rfree0.1873 3646 5 %RANDOM
Rwork0.15452 ---
obs0.15616 68655 96.48 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 16.614 Å2
Baniso -1Baniso -2Baniso -3
1-0.22 Å20 Å2-0.14 Å2
2--0.05 Å20 Å2
3----0.24 Å2
Refinement stepCycle: LAST / Resolution: 1.6→37.1 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4685 0 86 473 5244
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.020.0195076
X-RAY DIFFRACTIONr_bond_other_d0.0080.024691
X-RAY DIFFRACTIONr_angle_refined_deg2.0671.9876910
X-RAY DIFFRACTIONr_angle_other_deg1.4113.00310786
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.1645618
X-RAY DIFFRACTIONr_dihedral_angle_2_deg32.74223.451226
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.10415825
X-RAY DIFFRACTIONr_dihedral_angle_4_deg12.6321538
X-RAY DIFFRACTIONr_chiral_restr0.1280.2714
X-RAY DIFFRACTIONr_gen_planes_refined0.0130.0215722
X-RAY DIFFRACTIONr_gen_planes_other
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_it
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it
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 / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A10700.12
12C10700.12
21B149300.11
22D149300.11
LS refinement shellResolution: 1.6→1.641 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.275 279 -
Rwork0.251 5178 -
obs--98.54 %
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)
112.081-1.3833.84990.2311-1.06036.6807-0.11160.23460.79640.0515-0.0164-0.0908-0.4865-0.03510.1280.1321-0.01030.05250.02880.04650.1562-13.8176-3.5863-1.0791
24.63620.34361.4022.5614-0.21551.1410.0483-0.02150.15890.078-0.0611-0.3395-0.05850.19930.01290.0328-0.0152-0.00390.0611-0.01250.1205-2.8041-9.989710.274
35.58693.89543.39248.08854.60434.86230.00910.1875-0.10070.04540.084-0.51490.20980.2761-0.0930.03550.0265-0.01180.02860.00320.0861-5.0029-23.68798.8133
40.96440.4264-0.12010.92290.13180.56810.0305-0.16390.2330.1143-0.02940.0404-0.0035-0.0665-0.00120.0711-0.0006-0.00210.0689-0.03990.0723-25.9455-9.544815.365
52.10.47250.09361.51010.19760.85070.0532-0.12460.2960.1292-0.0421-0.0258-0.0525-0.0461-0.01110.06960.00750.00480.0198-0.01260.0492-24.0107-6.653511.6069
61.2933-0.0127-0.06320.7916-0.16170.71590.01880.039-0.0385-0.0184-0.0274-0.03840.0496-0.01940.00860.0731-0.0016-0.0040.0343-0.00750.0052-21.1877-22.07137.6016
74.169-2.05882.62372.3793-1.685112.2662-0.2183-0.25730.33920.37180.1121-0.1433-0.51740.25140.10620.1131-0.01240.0220.08-0.02680.0628-70.3917-1.452135.1707
86.4202-0.3975-1.69674.52540.46955.17850.00390.18420.0342-0.00870.06260.349-0.1869-0.247-0.06660.03450.0410.00760.06220.00560.0466-78.822-2.258228.6664
91.4403-0.73230.32517.7792-3.79845.6582-0.05490.0987-0.2549-0.10260.13870.39080.2093-0.2191-0.08380.0242-0.00640.00640.0465-0.0240.0821-77.8921-17.218429.4283
101.2868-0.6637-0.33020.89050.10540.84680.06550.06610.0945-0.0887-0.041-0.1112-0.03540.0511-0.02450.060800.01360.045900.0149-55.2053-7.509423.642
111.0025-0.1831-0.07890.6428-0.05210.64140.00210.0135-0.0729-0.0043-0.0192-0.0271-0.00150.05640.01710.04890.00430.00520.0351-0.01160.0142-58.3389-11.788827.2603
121.3935-0.069-0.05530.6408-0.03480.65390.0117-0.0371-0.19270.0119-0.01680.04930.06680.04220.00510.04750.00480.00840.02050.00010.0323-61.1954-17.19530.8095
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A285 - 292
2X-RAY DIFFRACTION2A293 - 304
3X-RAY DIFFRACTION3A305 - 316
4X-RAY DIFFRACTION4B321 - 384
5X-RAY DIFFRACTION5B385 - 440
6X-RAY DIFFRACTION6B441 - 578
7X-RAY DIFFRACTION7C290 - 297
8X-RAY DIFFRACTION8C298 - 305
9X-RAY DIFFRACTION9C306 - 318
10X-RAY DIFFRACTION10D321 - 373
11X-RAY DIFFRACTION11D374 - 510
12X-RAY DIFFRACTION12D511 - 578

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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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