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- PDB-6w9r: Crystal structure of an OTU deubiquitinase from Wolbachia pipient... -

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Basic information

Entry
Database: PDB / ID: 6w9r
TitleCrystal structure of an OTU deubiquitinase from Wolbachia pipientis wMel bound to ubiquitin
Components
  • OTU domain-containing protein wMelOTU
  • Ubiquitin
KeywordsHYDROLASE / Deubiquitinase / Bacterial effector
Function / homology
Function and homology information


Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) / Myoclonic epilepsy of Lafora / FLT3 signaling by CBL mutants / Prevention of phagosomal-lysosomal fusion / IRAK2 mediated activation of TAK1 complex / Alpha-protein kinase 1 signaling pathway / Glycogen synthesis / IRAK1 recruits IKK complex ...Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) / Myoclonic epilepsy of Lafora / FLT3 signaling by CBL mutants / Prevention of phagosomal-lysosomal fusion / IRAK2 mediated activation of TAK1 complex / Alpha-protein kinase 1 signaling pathway / Glycogen synthesis / IRAK1 recruits IKK complex / IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation / Membrane binding and targetting of GAG proteins / Endosomal Sorting Complex Required For Transport (ESCRT) / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Negative regulation of FLT3 / Constitutive Signaling by NOTCH1 HD Domain Mutants / Regulation of FZD by ubiquitination / TICAM1,TRAF6-dependent induction of TAK1 complex / NOTCH2 Activation and Transmission of Signal to the Nucleus / TICAM1-dependent activation of IRF3/IRF7 / APC/C:Cdc20 mediated degradation of Cyclin B / p75NTR recruits signalling complexes / Downregulation of ERBB4 signaling / APC-Cdc20 mediated degradation of Nek2A / PINK1-PRKN Mediated Mitophagy / TRAF6-mediated induction of TAK1 complex within TLR4 complex / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / Pexophagy / Regulation of innate immune responses to cytosolic DNA / InlA-mediated entry of Listeria monocytogenes into host cells / VLDLR internalisation and degradation / Downregulation of ERBB2:ERBB3 signaling / NF-kB is activated and signals survival / NRIF signals cell death from the nucleus / Regulation of PTEN localization / Activated NOTCH1 Transmits Signal to the Nucleus / Regulation of BACH1 activity / Translesion synthesis by REV1 / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Translesion synthesis by POLK / MAP3K8 (TPL2)-dependent MAPK1/3 activation / TICAM1, RIP1-mediated IKK complex recruitment / Downregulation of TGF-beta receptor signaling / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / Translesion synthesis by POLI / Gap-filling DNA repair synthesis and ligation in GG-NER / Josephin domain DUBs / Regulation of activated PAK-2p34 by proteasome mediated degradation / InlB-mediated entry of Listeria monocytogenes into host cell / IKK complex recruitment mediated by RIP1 / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Autodegradation of Cdh1 by Cdh1:APC/C / TNFR1-induced NF-kappa-B signaling pathway / APC/C:Cdc20 mediated degradation of Securin / Asymmetric localization of PCP proteins / TCF dependent signaling in response to WNT / SCF-beta-TrCP mediated degradation of Emi1 / AUF1 (hnRNP D0) binds and destabilizes mRNA / NIK-->noncanonical NF-kB signaling / Ubiquitin-dependent degradation of Cyclin D / Regulation of NF-kappa B signaling / TNFR2 non-canonical NF-kB pathway / activated TAK1 mediates p38 MAPK activation / Assembly of the pre-replicative complex / Vpu mediated degradation of CD4 / NOTCH3 Activation and Transmission of Signal to the Nucleus / Negative regulators of DDX58/IFIH1 signaling / Deactivation of the beta-catenin transactivating complex / Degradation of DVL / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Regulation of signaling by CBL / Dectin-1 mediated noncanonical NF-kB signaling / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Fanconi Anemia Pathway / Negative regulation of FGFR3 signaling / Hh mutants are degraded by ERAD / Recognition of DNA damage by PCNA-containing replication complex / Peroxisomal protein import / Degradation of AXIN / Downregulation of SMAD2/3:SMAD4 transcriptional activity / Degradation of GLI1 by the proteasome / Activation of NF-kappaB in B cells / Regulation of TNFR1 signaling / Negative regulation of FGFR2 signaling / Termination of translesion DNA synthesis / Negative regulation of FGFR4 signaling / Hedgehog ligand biogenesis / Defective CFTR causes cystic fibrosis / Stabilization of p53 / EGFR downregulation / Negative regulation of NOTCH4 signaling / Negative regulation of FGFR1 signaling / Iron uptake and transport / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / G2/M Checkpoints / SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription / Vif-mediated degradation of APOBEC3G
Similarity search - Function
OTU domain / OTU domain profile. / Ubiquitin domain signature. / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Ubiquitin-like domain superfamily
Similarity search - Domain/homology
CITRATE ANION / Polyubiquitin-C / OTU domain-containing protein
Similarity search - Component
Biological speciesHomo sapiens (human)
Wolbachia pipientis wMel (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.82 Å
AuthorsSchubert, A.F. / Pruneda, J.N. / Komander, D.
Funding support United Kingdom, European Union, 2items
OrganizationGrant numberCountry
Medical Research Council (MRC, United Kingdom)U105192732 United Kingdom
European Research Council (ERC)309456European Union
CitationJournal: Embo J. / Year: 2020
Title: Identification and characterization of diverse OTU deubiquitinases in bacteria.
Authors: Schubert, A.F. / Nguyen, J.V. / Franklin, T.G. / Geurink, P.P. / Roberts, C.G. / Sanderson, D.J. / Miller, L.N. / Ovaa, H. / Hofmann, K. / Pruneda, J.N. / Komander, D.
History
DepositionMar 23, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 1, 2020Provider: repository / Type: Initial release
Revision 1.1Aug 12, 2020Group: Database references / Category: citation / Item: _citation.journal_volume
Revision 1.2Oct 18, 2023Group: Author supporting evidence / Data collection ...Author supporting evidence / Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_audit_support / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_audit_support.country

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
M: Ubiquitin
N: Ubiquitin
O: Ubiquitin
P: Ubiquitin
Q: Ubiquitin
R: Ubiquitin
S: Ubiquitin
T: Ubiquitin
U: Ubiquitin
V: Ubiquitin
W: Ubiquitin
X: Ubiquitin
A: OTU domain-containing protein wMelOTU
B: OTU domain-containing protein wMelOTU
C: OTU domain-containing protein wMelOTU
D: OTU domain-containing protein wMelOTU
E: OTU domain-containing protein wMelOTU
F: OTU domain-containing protein wMelOTU
G: OTU domain-containing protein wMelOTU
H: OTU domain-containing protein wMelOTU
I: OTU domain-containing protein wMelOTU
J: OTU domain-containing protein wMelOTU
K: OTU domain-containing protein wMelOTU
L: OTU domain-containing protein wMelOTU
hetero molecules


Theoretical massNumber of molelcules
Total (without water)335,41136
Polymers333,14124
Non-polymers2,26912
Water65,4123631
1
M: Ubiquitin
A: OTU domain-containing protein wMelOTU
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,9513
Polymers27,7622
Non-polymers1891
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3660 Å2
ΔGint-5 kcal/mol
Surface area10760 Å2
MethodPISA
2
N: Ubiquitin
B: OTU domain-containing protein wMelOTU
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,9513
Polymers27,7622
Non-polymers1891
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3610 Å2
ΔGint-6 kcal/mol
Surface area10630 Å2
MethodPISA
3
O: Ubiquitin
F: OTU domain-containing protein wMelOTU
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,9513
Polymers27,7622
Non-polymers1891
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3560 Å2
ΔGint-8 kcal/mol
Surface area10790 Å2
MethodPISA
4
P: Ubiquitin
D: OTU domain-containing protein wMelOTU
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,9513
Polymers27,7622
Non-polymers1891
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3560 Å2
ΔGint-7 kcal/mol
Surface area10980 Å2
MethodPISA
5
Q: Ubiquitin
I: OTU domain-containing protein wMelOTU
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,9513
Polymers27,7622
Non-polymers1891
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3630 Å2
ΔGint-7 kcal/mol
Surface area10680 Å2
MethodPISA
6
R: Ubiquitin
J: OTU domain-containing protein wMelOTU
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,9513
Polymers27,7622
Non-polymers1891
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3590 Å2
ΔGint-6 kcal/mol
Surface area10660 Å2
MethodPISA
7
S: Ubiquitin
E: OTU domain-containing protein wMelOTU
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,9513
Polymers27,7622
Non-polymers1891
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3610 Å2
ΔGint-5 kcal/mol
Surface area10680 Å2
MethodPISA
8
T: Ubiquitin
C: OTU domain-containing protein wMelOTU
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,9513
Polymers27,7622
Non-polymers1891
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3650 Å2
ΔGint-6 kcal/mol
Surface area10500 Å2
MethodPISA
9
U: Ubiquitin
K: OTU domain-containing protein wMelOTU
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,9513
Polymers27,7622
Non-polymers1891
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3630 Å2
ΔGint-5 kcal/mol
Surface area10510 Å2
MethodPISA
10
V: Ubiquitin
L: OTU domain-containing protein wMelOTU
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,9513
Polymers27,7622
Non-polymers1891
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3620 Å2
ΔGint-6 kcal/mol
Surface area10640 Å2
MethodPISA
11
W: Ubiquitin
G: OTU domain-containing protein wMelOTU
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,9513
Polymers27,7622
Non-polymers1891
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3500 Å2
ΔGint-8 kcal/mol
Surface area10630 Å2
MethodPISA
12
X: Ubiquitin
H: OTU domain-containing protein wMelOTU
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,9513
Polymers27,7622
Non-polymers1891
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3600 Å2
ΔGint-6 kcal/mol
Surface area10570 Å2
MethodPISA
Unit cell
Length a, b, c (Å)136.925, 78.203, 280.425
Angle α, β, γ (deg.)90.000, 91.570, 90.000
Int Tables number5
Space group name H-MC121

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Components

#1: Protein
Ubiquitin


Mass: 8701.014 Da / Num. of mol.: 12
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UBC / Production host: Escherichia coli (E. coli) / References: UniProt: P0CG48
#2: Protein
OTU domain-containing protein wMelOTU


Mass: 19060.771 Da / Num. of mol.: 12
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Wolbachia pipientis wMel (bacteria) / Gene: WD_0443 / Production host: Escherichia coli (E. coli) / References: UniProt: Q73HU7
#3: Chemical
ChemComp-FLC / CITRATE ANION


Mass: 189.100 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C6H5O7
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 3631 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN

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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: 2.26 Å3/Da / Density % sol: 45.48 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / Details: 20% PEG 6K, 0.1 M citrate pH 4.6

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.96861 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: May 9, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.96861 Å / Relative weight: 1
ReflectionResolution: 1.82→27.29 Å / Num. obs: 247996 / % possible obs: 98.3 % / Redundancy: 7.8 % / CC1/2: 0.997 / Rmerge(I) obs: 0.147 / Rpim(I) all: 0.056 / Rrim(I) all: 0.157 / Net I/σ(I): 9.4
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. measured allNum. unique obsCC1/2Rpim(I) allRrim(I) allNet I/σ(I) obs% possible all
1.85-1.887.70.92493464121700.8490.3540.992.897.2
10.13-27.297.80.0591212015610.9980.0220.06318.494.8

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
PHENIX1.17.1_3660refinement
XDSJan 10, 2014data reduction
Aimless0.2.8data scaling
PHASERphasing
PDB_EXTRACT3.25data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1UBQ, 6W9O

1ubq

6w9o


Resolution: 1.82→27.29 Å / SU ML: 0.19 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 23.47
RfactorNum. reflection% reflection
Rfree0.2081 12296 5.03 %
Rwork0.1664 --
obs0.1685 244560 92.24 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 114.34 Å2 / Biso mean: 24.3795 Å2 / Biso min: 6.36 Å2
Refinement stepCycle: final / Resolution: 1.82→27.29 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms22609 0 156 3646 26411
Biso mean--29.67 34.48 -
Num. residues----2858
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.82-1.840.30464170.2427889830695
1.84-1.860.29294120.22987935834795
1.86-1.890.27844210.22417867828894
1.89-1.910.23793890.21347915830494
1.91-1.930.25643940.20887878827295
1.93-1.960.25734300.20377908833895
1.96-1.990.2614190.19227868828795
1.99-2.020.24553980.18387984838294
2.02-2.050.25734030.18867864826795
2.05-2.080.22434200.18037934835495
2.08-2.120.22493990.17287925832494
2.12-2.160.21254140.16897864827894
2.16-2.20.21464180.16297869828794
2.2-2.240.20464530.16297800825393
2.24-2.290.20744320.15977753818593
2.29-2.350.23124240.15927757818193
2.35-2.40.22664010.16397759816092
2.4-2.470.2254130.17137825823893
2.47-2.540.24653950.1737796819193
2.54-2.620.2293820.16967782816493
2.62-2.720.21714420.16557737817992
2.72-2.830.20384040.1587707811192
2.83-2.960.21443850.16317651803691
2.96-3.110.19644010.15697647804891
3.11-3.310.19354040.15077596800090
3.31-3.560.18664370.15257506794389
3.56-3.920.16573680.1427535790389
3.92-4.480.15624180.14067382780088
4.48-5.640.17544140.15287293770786
5.64-27.290.18483890.16957038742781
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)
11.3101-0.11470.53192.663-1.00341.39740.06890.03890.27220.0213-0.08910.2278-0.1547-0.03310.01770.10180.00430.010.0911-0.0060.1533-19.0794-3.748173.2665
21.3710.11960.34582.24440.19680.66660.0517-0.05780.18270.1246-0.1313-0.2312-0.07940.04540.06480.0674-0.0028-0.00280.11960.01230.151313.2418-0.7217136.6414
31.9452-0.3882-0.35251.3984-0.13441.3369-0.01350.22880.1203-0.0931-0.0752-0.24110.05510.18310.06970.0810.00260.01430.1270.04480.1516-31.3135-2.831451.3939
41.9411-0.2344-0.51531.4587-0.0511.46590.01310.13120.0567-0.1031-0.0062-0.30180.00010.2071-0.03430.07750.00180.0210.15280.01810.1601-33.11490.525121.6116
51.31940.01480.50492.8825-0.69291.4728-0.09060.03150.34970.0543-0.10180.0867-0.22430.02870.15470.19360.0036-0.07780.1349-0.01280.2477-16.9961-6.73083.3681
61.24170.13010.44061.67640.1140.95490.01040.00650.22180.0938-0.1306-0.2417-0.10660.06610.09760.0753-0.0009-0.02910.11340.02780.18315.208-3.916566.3252
73.00310.4528-0.45412.116-0.08571.6629-0.0672-0.33190.15120.08290.00680.46430.0201-0.3560.03710.16350.0175-0.00370.2295-0.03810.209728.9243-5.156518.4606
82.7517-0.0382-0.30731.65520.07071.4367-0.1435-0.33970.13410.10030.06370.36640.0581-0.22040.06640.09960.00990.00690.1499-0.02360.153727.0361-2.389188.1238
90.24180.02520.30270.0803-0.12720.7855-0.07310.1035-0.4382-0.2128-0.2822-0.6538-0.01690.88380.20240.17210.08160.09440.44390.26360.564120.77117.654545.0544
101.7408-0.17640.4481.1196-0.5931.0947-0.0410.0153-0.293-0.0016-0.0306-0.24370.06420.22170.040.08820.01710.03530.15040.03910.204319.016110.982115.4665
111.222-0.09690.58381.03280.03031.36460.2239-0.0449-0.6488-0.86840.07380.37570.9073-0.3391-0.11810.6555-0.1237-0.22260.1602-0.03110.316-21.61184.82327.4706
121.06170.44280.35162.27150.98721.2787-0.05770.1376-0.4186-0.1715-0.03310.09580.2141-0.17120.05340.1946-0.03530.00760.1243-0.04790.2587-23.20887.573697.1491
131.01340.2119-0.13231.2864-0.67310.99790.1195-0.10450.05540.2647-0.1663-0.142-0.16740.17930.0240.1552-0.0561-0.03420.1213-0.01740.1009-10.319-16.933188.7279
141.0699-0.22220.07860.9850.0291.07650.07130.0587-0.0017-0.1652-0.08120.0574-0.0037-0.06890.00040.09060.0228-0.01450.10380.00950.08843.9397-14.2748121.4627
151.15190.3446-0.26781.4756-0.31941.1838-0.0930.1188-0.1451-0.19390.0797-0.08070.1484-0.0401-0.00350.1199-0.0139-0.0010.0872-0.03380.103243.9442-3.797173.8452
160.52230.0437-0.31991.22660.08851.1739-0.0797-0.0115-0.07160.0720.03010.0330.1418-0.01740.04560.07360.00890.01050.11750.02740.1221-49.6252-0.5404136.6895
171.31020.1249-0.0151.5809-0.28111.3534-0.04760.0924-0.1447-0.22460.0292-0.09050.1361-0.03050.00290.18180.0109-0.00810.1092-0.0370.118745.6746-6.68283.8701
181.1106-0.0819-0.24731.77870.0711.3323-0.0656-0.0393-0.1460.1940.00030.06990.1553-0.0840.03540.1004-0.00730.01830.11480.04340.1239-47.6988-3.847466.441
191.8165-0.13190.61181.4239-0.49681.8029-0.0143-0.36670.02570.02840.03070.104-0.0929-0.3316-0.0190.14740.0112-0.00440.2053-0.00990.0851-16.15820.559942.2559
201.1951-0.08110.11551.0133-0.19451.58860.0157-0.1814-0.0306-0.02580.01340.1058-0.0498-0.2051-0.01570.06980.00010.01580.10720.00460.0867-18.325223.4122112.1558
211.32150.1922-0.02631.0682-0.29971.61870.0695-0.09550.06960.2138-0.1511-0.1571-0.20140.30650.05830.2294-0.0191-0.08110.196-0.02310.1752-8.3965-20.134318.7573
221.0454-0.23590.12251.15950.08141.12380.06520.15740.0149-0.1519-0.10520.06360.007-0.10710.02150.08350.0156-0.0190.11760.01440.09615.9548-17.64251.3539
231.43080.3222-0.12211.8042-0.45681.6450.00110.1572-0.0663-0.3045-0.228-0.4042-0.13810.50940.16330.31250.00430.09230.29840.10510.222613.675321.163428.9685
241.2670.12160.15071.3542-0.29171.5364-0.05470.18920.0025-0.2373-0.0453-0.1835-0.0840.28740.03420.1617-0.01110.08890.15990.03720.111612.036624.623999.2651
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain 'M' and resid 1 through 76)M1 - 76
2X-RAY DIFFRACTION2(chain 'N' and resid 1 through 76)N1 - 76
3X-RAY DIFFRACTION3(chain 'O' and resid 1 through 76)O1 - 76
4X-RAY DIFFRACTION4(chain 'P' and resid 1 through 76)P1 - 76
5X-RAY DIFFRACTION5(chain 'Q' and resid 1 through 76)Q1 - 76
6X-RAY DIFFRACTION6(chain 'R' and resid 1 through 76)R1 - 76
7X-RAY DIFFRACTION7(chain 'S' and resid 1 through 76)S1 - 76
8X-RAY DIFFRACTION8(chain 'T' and resid 1 through 76)T1 - 76
9X-RAY DIFFRACTION9(chain 'U' and resid 1 through 76)U1 - 76
10X-RAY DIFFRACTION10(chain 'V' and resid 1 through 76)V1 - 76
11X-RAY DIFFRACTION11(chain 'W' and resid 1 through 76)W1 - 76
12X-RAY DIFFRACTION12(chain 'X' and resid 1 through 76)X1 - 76
13X-RAY DIFFRACTION13(chain 'A' and resid 39 through 200)A39 - 200
14X-RAY DIFFRACTION14(chain 'B' and resid 38 through 200)B38 - 200
15X-RAY DIFFRACTION15(chain 'C' and resid 38 through 200)C38 - 200
16X-RAY DIFFRACTION16(chain 'D' and resid 40 through 201)D40 - 201
17X-RAY DIFFRACTION17(chain 'E' and resid 39 through 200)E39 - 200
18X-RAY DIFFRACTION18(chain 'F' and resid 40 through 200)F40 - 200
19X-RAY DIFFRACTION19(chain 'G' and resid 39 through 201)G39 - 201
20X-RAY DIFFRACTION20(chain 'H' and resid 39 through 200)H39 - 200
21X-RAY DIFFRACTION21(chain 'I' and resid 40 through 200)I40 - 200
22X-RAY DIFFRACTION22(chain 'J' and resid 38 through 200)J38 - 200
23X-RAY DIFFRACTION23(chain 'K' and resid 40 through 200)K40 - 200
24X-RAY DIFFRACTION24(chain 'L' and resid 38 through 200)L38 - 200

+
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