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- PDB-5ok6: Ubiquitin specific protease 11 USP11 - peptide F complex -

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Basic information

Entry
Database: PDB / ID: 5ok6
TitleUbiquitin specific protease 11 USP11 - peptide F complex
Components
  • ALA-GLU-GLY-GLU-PHE-TYR-LYS-LEU-LYS-ILE-ARG-THR-PRO-AAR
  • Ubiquitin carboxyl-terminal hydrolase 11
KeywordsPROTEIN BINDING / peptide ligand complex / ubiquitin / protease
Function / homology
Function and homology information


protein deubiquitination / Association of TriC/CCT with target proteins during biosynthesis / transcription corepressor binding / chromosome / ubiquitin-dependent protein catabolic process / ubiquitinyl hydrolase 1 / cysteine-type deubiquitinase activity / Ub-specific processing proteases / cysteine-type endopeptidase activity / proteolysis ...protein deubiquitination / Association of TriC/CCT with target proteins during biosynthesis / transcription corepressor binding / chromosome / ubiquitin-dependent protein catabolic process / ubiquitinyl hydrolase 1 / cysteine-type deubiquitinase activity / Ub-specific processing proteases / cysteine-type endopeptidase activity / proteolysis / nucleoplasm / nucleus / cytosol
Similarity search - Function
Ubiquitin-like domain, USP-type / Ubiquitin-like domain / Peptidase C19, ubiquitin-specific peptidase, DUSP domain / DUSP-like superfamily / DUSP domain / DUSP domain profile. / Domain in ubiquitin-specific proteases. / Ubiquitin carboxyl-terminal hydrolase, C-terminal / Ubiquitin-specific protease C-terminal / Ubiquitin specific protease (USP) domain signature 2. ...Ubiquitin-like domain, USP-type / Ubiquitin-like domain / Peptidase C19, ubiquitin-specific peptidase, DUSP domain / DUSP-like superfamily / DUSP domain / DUSP domain profile. / Domain in ubiquitin-specific proteases. / Ubiquitin carboxyl-terminal hydrolase, C-terminal / Ubiquitin-specific protease C-terminal / Ubiquitin specific protease (USP) domain signature 2. / Ubiquitin specific protease (USP) domain signature 1. / Ubiquitin specific protease, conserved site / Peptidase C19, ubiquitin carboxyl-terminal hydrolase / Ubiquitin carboxyl-terminal hydrolase / Ubiquitin specific protease domain / Ubiquitin specific protease (USP) domain profile. / Papain-like cysteine peptidase superfamily
Similarity search - Domain/homology
Ubiquitin carboxyl-terminal hydrolase / Ubiquitin carboxyl-terminal hydrolase 11
Similarity search - Component
Biological speciesHomo sapiens (human)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.3 Å
AuthorsSpiliotopoulos, A. / Dreveny, I.
Funding support United Kingdom, 1items
OrganizationGrant numberCountry
Biotechnology and Biological Sciences Research CouncilBB/H012656/1 United Kingdom
Citation
Journal: J.Biol.Chem. / Year: 2019
Title: Discovery of peptide ligands targeting a specific ubiquitin-like domain-binding site in the deubiquitinase USP11.
Authors: Spiliotopoulos, A. / Blokpoel Ferreras, L. / Densham, R.M. / Caulton, S.G. / Maddison, B.C. / Morris, J.R. / Dixon, J.E. / Gough, K.C. / Dreveny, I.
#1: Journal: Biochemistry / Year: 2014
Title: Structure and catalytic regulatory function of ubiquitin specific protease 11 N-terminal and ubiquitin-like domains.
Authors: Harper, S. / Gratton, H.E. / Cornaciu, I. / Oberer, M. / Scott, D.J. / Emsley, J. / Dreveny, I.
History
DepositionJul 25, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 8, 2018Provider: repository / Type: Initial release
Revision 1.1Sep 25, 2019Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Jan 17, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Ubiquitin carboxyl-terminal hydrolase 11
B: Ubiquitin carboxyl-terminal hydrolase 11
C: ALA-GLU-GLY-GLU-PHE-TYR-LYS-LEU-LYS-ILE-ARG-THR-PRO-AAR
D: ALA-GLU-GLY-GLU-PHE-TYR-LYS-LEU-LYS-ILE-ARG-THR-PRO-AAR
hetero molecules


Theoretical massNumber of molelcules
Total (without water)57,2487
Polymers57,0324
Non-polymers2163
Water11,692649
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A: Ubiquitin carboxyl-terminal hydrolase 11
D: ALA-GLU-GLY-GLU-PHE-TYR-LYS-LEU-LYS-ILE-ARG-THR-PRO-AAR
hetero molecules


Theoretical massNumber of molelcules
Total (without water)28,6083
Polymers28,5162
Non-polymers921
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2040 Å2
ΔGint-8 kcal/mol
Surface area13430 Å2
MethodPISA
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B: Ubiquitin carboxyl-terminal hydrolase 11
C: ALA-GLU-GLY-GLU-PHE-TYR-LYS-LEU-LYS-ILE-ARG-THR-PRO-AAR
hetero molecules


Theoretical massNumber of molelcules
Total (without water)28,6404
Polymers28,5162
Non-polymers1242
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1620 Å2
ΔGint-9 kcal/mol
Surface area13120 Å2
MethodPISA
Unit cell
Length a, b, c (Å)65.770, 45.510, 100.610
Angle α, β, γ (deg.)90.000, 102.680, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain C and (resid 3 through 11 or resid 13 through 14))
21(chain D and (resid 3 through 11 or resid 13 through 14))
12(chain A and (resid 32 through 36 or resid 38...
22(chain B and (resid 32 through 36 or resid 38...

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111GLYGLYARGARG(chain C and (resid 3 through 11 or resid 13 through 14))CC3 - 113 - 11
121PROPROAARAAR(chain C and (resid 3 through 11 or resid 13 through 14))CC13 - 1413 - 14
211GLYGLYARGARG(chain D and (resid 3 through 11 or resid 13 through 14))DD3 - 113 - 11
221PROPROAARAAR(chain D and (resid 3 through 11 or resid 13 through 14))DD13 - 1413 - 14
112LEULEUASPASP(chain A and (resid 32 through 36 or resid 38...AA32 - 3610 - 14
122GLNGLNGLYGLY(chain A and (resid 32 through 36 or resid 38...AA38 - 4816 - 26
132GLUGLULEULEU(chain A and (resid 32 through 36 or resid 38...AA50 - 6128 - 39
142LYSLYSLYSLYS(chain A and (resid 32 through 36 or resid 38...AA6442
152TRPTRPTRPTRP(chain A and (resid 32 through 36 or resid 38...AA6644
162LYSLYSTRPTRP(chain A and (resid 32 through 36 or resid 38...AA68 - 7046 - 48
172ALAALAASPASP(chain A and (resid 32 through 36 or resid 38...AA72 - 7850 - 56
182ASPASPGLYGLY(chain A and (resid 32 through 36 or resid 38...AA80 - 8658 - 64
192ILEILELYSLYS(chain A and (resid 32 through 36 or resid 38...AA88 - 10366 - 81
1102GLYGLYGLYGLY(chain A and (resid 32 through 36 or resid 38...AA105 - 10983 - 87
1112ASPASPVALVAL(chain A and (resid 32 through 36 or resid 38...AA111 - 12489 - 102
1122TRPTRPPROPRO(chain A and (resid 32 through 36 or resid 38...AA126 - 134104 - 112
1132ILEILEVALVAL(chain A and (resid 32 through 36 or resid 38...AA136 - 159114 - 137
1142HISHISVALVAL(chain A and (resid 32 through 36 or resid 38...AA161 - 170139 - 148
1152PHEPHEGLUGLU(chain A and (resid 32 through 36 or resid 38...AA172 - 195150 - 173
1162THRTHRTHRTHR(chain A and (resid 32 through 36 or resid 38...AA197 - 214175 - 192
1172ILEILEGLUGLU(chain A and (resid 32 through 36 or resid 38...AA216 - 246194 - 224
212LEULEUASPASP(chain B and (resid 32 through 36 or resid 38...BB32 - 3610 - 14
222GLNGLNGLYGLY(chain B and (resid 32 through 36 or resid 38...BB38 - 4816 - 26
232GLUGLULEULEU(chain B and (resid 32 through 36 or resid 38...BB50 - 6128 - 39
242LYSLYSLYSLYS(chain B and (resid 32 through 36 or resid 38...BB6442
252TRPTRPTRPTRP(chain B and (resid 32 through 36 or resid 38...BB6644
262LYSLYSTRPTRP(chain B and (resid 32 through 36 or resid 38...BB68 - 7046 - 48
272ALAALAASPASP(chain B and (resid 32 through 36 or resid 38...BB72 - 7850 - 56
282ASPASPGLYGLY(chain B and (resid 32 through 36 or resid 38...BB80 - 8658 - 64
292ILEILELYSLYS(chain B and (resid 32 through 36 or resid 38...BB88 - 10366 - 81
2102GLYGLYGLYGLY(chain B and (resid 32 through 36 or resid 38...BB105 - 10983 - 87
2112ASPASPVALVAL(chain B and (resid 32 through 36 or resid 38...BB111 - 12489 - 102
2122TRPTRPPROPRO(chain B and (resid 32 through 36 or resid 38...BB126 - 134104 - 112
2132ILEILEVALVAL(chain B and (resid 32 through 36 or resid 38...BB136 - 159114 - 137
2142HISHISVALVAL(chain B and (resid 32 through 36 or resid 38...BB161 - 170139 - 148
2152PHEPHEGLUGLU(chain B and (resid 32 through 36 or resid 38...BB172 - 195150 - 173
2162THRTHRTHRTHR(chain B and (resid 32 through 36 or resid 38...BB197 - 214175 - 192
2172ILEILEGLUGLU(chain B and (resid 32 through 36 or resid 38...BB216 - 246194 - 224

NCS ensembles :
ID
1
2

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Components

#1: Protein Ubiquitin carboxyl-terminal hydrolase 11 / Ubiquitin specific peptidase 11 / isoform CRA_b


Mass: 26804.859 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: USP11, hCG_17279 / Production host: Escherichia coli (E. coli) / References: UniProt: G5E9A6, UniProt: P51784*PLUS
#2: Protein/peptide ALA-GLU-GLY-GLU-PHE-TYR-LYS-LEU-LYS-ILE-ARG-THR-PRO-AAR


Mass: 1711.016 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)
#3: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#4: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H6O2
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 649 / 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: 2.58 Å3/Da / Density % sol: 52.25 %
Crystal growTemperature: 283.15 K / Method: vapor diffusion, sitting drop / Details: 0.01M tri-sodium citrate, 16% PEG6000

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I02 / Wavelength: 0.97949 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Oct 5, 2013
RadiationMonochromator: double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97949 Å / Relative weight: 1
ReflectionResolution: 1.3→49.01 Å / Num. obs: 140611 / % possible obs: 98.3 % / Redundancy: 4.1 % / Biso Wilson estimate: 13.76 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.051 / Rpim(I) all: 0.028 / Rrim(I) all: 0.058 / Net I/σ(I): 16 / Num. measured all: 578764 / Scaling rejects: 0
Reflection shell

Diffraction-ID: 1 / Redundancy: 4.1 %

Resolution (Å)Rmerge(I) obsCC1/2Rpim(I) allRrim(I) all% possible all
1.3-1.330.6240.7620.3450.71696.6
5.81-49.010.0290.9980.0160.03398.5

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Processing

Software
NameVersionClassification
Aimless0.1.29data scaling
PHENIX1.11.1_2575refinement
PDB_EXTRACT3.22data extraction
XDSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4MEL

4mel


Resolution: 1.3→49.007 Å / SU ML: 0.12 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 17.51
RfactorNum. reflection% reflection
Rfree0.1779 7056 5.02 %
Rwork0.1571 --
obs0.1582 140596 98.3 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 100.41 Å2 / Biso mean: 20.2142 Å2 / Biso min: 7.79 Å2
Refinement stepCycle: final / Resolution: 1.3→49.007 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3795 0 14 649 4458
Biso mean--18.32 32.44 -
Num. residues----462
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0154140
X-RAY DIFFRACTIONf_angle_d1.3465659
X-RAY DIFFRACTIONf_chiral_restr0.102586
X-RAY DIFFRACTIONf_plane_restr0.011749
X-RAY DIFFRACTIONf_dihedral_angle_d19.2231551
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11C102X-RAY DIFFRACTION6.185TORSIONAL
12D102X-RAY DIFFRACTION6.185TORSIONAL
21A1775X-RAY DIFFRACTION6.185TORSIONAL
22B1775X-RAY DIFFRACTION6.185TORSIONAL
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 (%)
1.3-1.31480.26912520.25894356460897
1.3148-1.33020.25692260.24824317454396
1.3302-1.34650.25232370.24154352458997
1.3465-1.36350.25452040.22954414461898
1.3635-1.38150.21862200.22014396461696
1.3815-1.40040.24292310.21084372460398
1.4004-1.42040.24691990.214399459896
1.4204-1.44160.22452390.20814363460298
1.4416-1.46410.222390.20334395463497
1.4641-1.48810.22362700.1984353462398
1.4881-1.51380.20792170.18174413463096
1.5138-1.54130.19032510.17294340459198
1.5413-1.5710.20562370.16684379461696
1.571-1.6030.17262190.15564446466598
1.603-1.63790.17762370.14764345458297
1.6379-1.6760.15832260.15414498472498
1.676-1.71790.18212280.15254387461598
1.7179-1.76440.17012670.14814479474699
1.7644-1.81630.17532310.15145094740100
1.8163-1.87490.18372400.14964499473999
1.8749-1.94190.18092380.14744491472999
1.9419-2.01970.16362270.144345314758100
2.0197-2.11160.1562420.141945354777100
2.1116-2.22290.16382460.139545034749100
2.2229-2.36220.17472280.146545544782100
2.3622-2.54460.16362300.15445484778100
2.5446-2.80060.16662370.155345374774100
2.8006-3.20580.17472150.154446224837100
3.2058-4.03870.17842410.145345694810100
4.0387-49.04180.15932820.14764638492099
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)
14.9388-0.53611.80776.2618-0.37317.47930.135-0.4436-0.50630.3383-0.02480.13310.57190.307-0.04260.18650.0604-0.00390.22190.03220.132180.0033-4.074545.1528
26.02590.03554.52891.61240.93777.2969-0.10190.318-0.21430.03290.0898-0.05080.46150.5694-0.01420.22480.04170.03680.1346-0.02410.111377.7372-3.524128.0258
33.34840.4053.48240.78771.47777.8723-0.1158-0.01440.23-0.0376-0.0771-0.0536-0.23080.22110.17010.11250.00380.00880.10420.01890.060472.74775.763340.2672
41.2068-0.31660.87090.3762-0.56452.7453-0.0218-0.1749-0.03440.06520.02160.0523-0.0473-0.0654-0.00470.10370.00490.01040.0883-0.00060.068667.46753.970840.5257
53.551-0.1062-0.53832.94080.09516.1553-0.15740.1343-0.1327-0.2237-0.03010.00350.2002-0.08320.13460.10090.01590.00030.05410.00570.076665.3042-0.13828.7327
63.74350.95441.97960.68980.42761.37770.0128-0.1141-0.050.04420.02220.0170.0996-0.1-0.0330.144-0.0094-0.00370.07220.01510.053348.3598-1.869915.7963
72.09460.04080.16072.3822-0.34652.6083-0.00240.0144-0.1025-0.11480.00710.03450.1944-0.10360.01440.1181-0.0136-0.02270.08230.00460.0543.3322-1.60727.1099
84.6901-0.23872.42130.6736-1.39194.41440.02740.32720.0572-0.0259-0.0666-0.0640.00290.35770.04390.142-0.02450.00350.0880.00920.081854.41383.48277.7783
92.71081.68451.11694.46351.51092.50710.01850.17890.0391-0.31550.02360.32110.0904-0.1557-0.07580.1223-0.0051-0.0210.09510.00690.095439.15770.72532.1924
106.36780.8756-3.04338.53980.09872.2269-0.0193-0.36890.52850.29520.23310.072-0.2173-0.0675-0.22830.15480.0273-0.00670.2034-0.03190.129582.3712-14.472816.328
116.7862-2.3974-0.94338.08960.52517.00760.1351-0.06380.3562-0.05390.0963-0.749-0.05240.9164-0.21760.22950.0146-0.00920.236-0.0620.181772.8634-15.11129.0767
124.9454-0.4033-3.82560.17710.15483.0949-0.1662-0.1137-0.1781-0.0060.02740.00890.08280.20220.11250.14750.00560.00380.1029-0.00730.069175.6061-22.512112.7659
132.92171.6877-0.63942.9027-0.6681.2892-0.04580.14160.0891-0.19450.08690.17620.0229-0.0151-0.02840.12520.0135-0.00310.0686-0.02220.073563.6912-21.597116.3195
143.6434-0.0156-0.93870.10640.00490.2304-0.0576-0.10450.00090.00690.036-0.0151-0.0285-0.0480.0210.15280.01540.00020.0746-0.01380.089254.8509-18.792824.6654
153.0210.156-0.21.1656-0.20232.508-0.03020.02750.0487-0.00850.05230.0256-0.0288-0.0014-0.0190.1110.01830.01760.08670.00220.054339.0963-14.855428.9585
165.33670.7314-0.330.8604-1.22412.2505-0.0435-0.5573-0.25120.1096-0.0725-0.10230.12360.24260.08770.17690.04930.02170.18370.04790.111942.3673-21.543737.0062
173.0301-2.2471-1.62524.380.80913.1997-0.05880.0648-0.23510.1243-0.00920.48360.0731-0.5220.03590.11170.00460.00510.2051-0.00240.107626.974-17.423733.0716
182.7239-3.76233.37477.8585-6.15035.01290.05480.2067-0.2439-0.3527-0.17770.01460.2-0.36130.17490.1584-0.0322-0.00810.2393-0.03350.138924.416-22.13924.1639
197.4465-5.19145.50046.9836-4.15494.2145-0.058-0.8269-0.38290.32990.34170.11210.897-0.7676-0.25510.3102-0.04560.02410.26220.04390.192730.1912-28.936836.5851
206.841-0.98723.80858.4717-2.81552.7382-0.3427-0.78280.26490.60040.24650.5214-0.432-0.73270.07930.21540.0647-0.01880.1828-0.00680.167934.24727.61717.18
219.13142.2915-4.91047.1041.17087.17090.20480.59010.2444-0.52210.0293-0.3959-0.7073-0.0677-0.19930.25290.0104-0.02910.13780.0330.187544.941511.91571.4213
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 29 through 43 )A29 - 43
2X-RAY DIFFRACTION2chain 'A' and (resid 44 through 57 )A44 - 57
3X-RAY DIFFRACTION3chain 'A' and (resid 58 through 74 )A58 - 74
4X-RAY DIFFRACTION4chain 'A' and (resid 75 through 127 )A75 - 127
5X-RAY DIFFRACTION5chain 'A' and (resid 128 through 150 )A128 - 150
6X-RAY DIFFRACTION6chain 'A' and (resid 151 through 188 )A151 - 188
7X-RAY DIFFRACTION7chain 'A' and (resid 189 through 207 )A189 - 207
8X-RAY DIFFRACTION8chain 'A' and (resid 208 through 226 )A208 - 226
9X-RAY DIFFRACTION9chain 'A' and (resid 227 through 247 )A227 - 247
10X-RAY DIFFRACTION10chain 'B' and (resid 31 through 43 )B31 - 43
11X-RAY DIFFRACTION11chain 'B' and (resid 44 through 57 )B44 - 57
12X-RAY DIFFRACTION12chain 'B' and (resid 58 through 90 )B58 - 90
13X-RAY DIFFRACTION13chain 'B' and (resid 91 through 127 )B91 - 127
14X-RAY DIFFRACTION14chain 'B' and (resid 128 through 162 )B128 - 162
15X-RAY DIFFRACTION15chain 'B' and (resid 163 through 207 )B163 - 207
16X-RAY DIFFRACTION16chain 'B' and (resid 208 through 226 )B208 - 226
17X-RAY DIFFRACTION17chain 'B' and (resid 227 through 247 )B227 - 247
18X-RAY DIFFRACTION18chain 'C' and (resid 1 through 7 )C1 - 7
19X-RAY DIFFRACTION19chain 'C' and (resid 8 through 13 )C8 - 13
20X-RAY DIFFRACTION20chain 'D' and (resid 3 through 7 )D3 - 7
21X-RAY DIFFRACTION21chain 'D' and (resid 8 through 13 )D8 - 13

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