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- PDB-6f09: Binary complex of 14-3-3 zeta with ubiquitin specific protease 8 ... -

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Basic information

Entry
Database: PDB / ID: 6f09
TitleBinary complex of 14-3-3 zeta with ubiquitin specific protease 8 (USP8) pSer718 peptide
Components
  • 14-3-3 protein zeta/delta
  • Ubiquitin carboxyl-terminal hydrolase 8
KeywordsSIGNALING PROTEIN / 14-3-3 / Usp8 / phosphosite / binary complex protein-peptide
Function / homology
Function and homology information


negative regulation of lysosomal protein catabolic process / acrosomal membrane / synaptic target recognition / Golgi reassembly / NOTCH4 Activation and Transmission of Signal to the Nucleus / establishment of Golgi localization / regulation of protein catabolic process at postsynapse, modulating synaptic transmission / protein K48-linked deubiquitination / endosome organization / respiratory system process ...negative regulation of lysosomal protein catabolic process / acrosomal membrane / synaptic target recognition / Golgi reassembly / NOTCH4 Activation and Transmission of Signal to the Nucleus / establishment of Golgi localization / regulation of protein catabolic process at postsynapse, modulating synaptic transmission / protein K48-linked deubiquitination / endosome organization / respiratory system process / tube formation / regulation of synapse maturation / Rap1 signalling / K48-linked deubiquitinase activity / negative regulation of protein localization to nucleus / protein K63-linked deubiquitination / KSRP (KHSRP) binds and destabilizes mRNA / K63-linked deubiquitinase activity / positive regulation of amyloid fibril formation / GP1b-IX-V activation signalling / mitotic cytokinesis / Interleukin-3, Interleukin-5 and GM-CSF signaling / Regulation of localization of FOXO transcription factors / protein deubiquitination / Activation of BAD and translocation to mitochondria / phosphoserine residue binding / cellular response to dexamethasone stimulus / regulation of ERK1 and ERK2 cascade / protein targeting / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / SARS-CoV-2 targets host intracellular signalling and regulatory pathways / cellular response to glucose starvation / SARS-CoV-1 targets host intracellular signalling and regulatory pathways / RHO GTPases activate PKNs / negative regulation of TORC1 signaling / ERK1 and ERK2 cascade / Transcriptional and post-translational regulation of MITF-M expression and activity / Regulation of FZD by ubiquitination / Downregulation of ERBB2:ERBB3 signaling / lung development / protein sequestering activity / negative regulation of innate immune response / hippocampal mossy fiber to CA3 synapse / TP53 Regulates Metabolic Genes / Translocation of SLC2A4 (GLUT4) to the plasma membrane / Deactivation of the beta-catenin transactivating complex / Negative regulation of NOTCH4 signaling / Negative regulation of MET activity / cellular response to nerve growth factor stimulus / regulation of protein stability / SH3 domain binding / intracellular protein localization / melanosome / positive regulation of canonical Wnt signaling pathway / regulation of protein localization / midbody / angiogenesis / protein phosphatase binding / blood microparticle / vesicle / DNA-binding transcription factor binding / transmembrane transporter binding / Ras protein signal transduction / ubiquitinyl hydrolase 1 / cysteine-type deubiquitinase activity / early endosome / protein phosphorylation / endosome membrane / Ub-specific processing proteases / postsynaptic density / cadherin binding / protein domain specific binding / cysteine-type endopeptidase activity / focal adhesion / ubiquitin protein ligase binding / protein kinase binding / negative regulation of apoptotic process / glutamatergic synapse / negative regulation of transcription by RNA polymerase II / signal transduction / proteolysis / extracellular space / RNA binding / extracellular exosome / nucleoplasm / identical protein binding / nucleus / plasma membrane / cytoplasm / cytosol
Similarity search - Function
: / USP8 WW domain / USP8 dimerisation domain / USP8 dimerisation domain / : / Rhodanese-like domain / Rhodanese domain profile. / Rhodanese-like domain superfamily / Rhodanese-like domain / Ubiquitin specific protease (USP) domain signature 2. ...: / USP8 WW domain / USP8 dimerisation domain / USP8 dimerisation domain / : / Rhodanese-like domain / Rhodanese domain profile. / Rhodanese-like domain superfamily / Rhodanese-like domain / 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 / 14-3-3 domain / Ubiquitin specific protease domain / Ubiquitin specific protease (USP) domain profile. / Delta-Endotoxin; domain 1 / 14-3-3 proteins signature 2. / 14-3-3 protein, conserved site / 14-3-3 proteins signature 1. / 14-3-3 protein / 14-3-3 homologues / 14-3-3 domain / 14-3-3 domain superfamily / 14-3-3 protein / Papain-like cysteine peptidase superfamily / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
Ubiquitin carboxyl-terminal hydrolase 8 / 14-3-3 protein zeta/delta
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.594 Å
AuthorsCentorrino, F. / Ballone, A. / Ottmann, C. / Guo, S. / Leysen, S.
Funding support Netherlands, 1items
OrganizationGrant numberCountry
H2020 Marie Curie Actions of the European CommissionGrant Agreement 675179 Netherlands
CitationJournal: FEBS Lett. / Year: 2018
Title: Biophysical and structural insight into the USP8/14-3-3 interaction.
Authors: Centorrino, F. / Ballone, A. / Wolter, M. / Ottmann, C.
History
DepositionNov 17, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 7, 2018Provider: repository / Type: Initial release
Revision 1.1Apr 25, 2018Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title
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
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.3Oct 16, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
P: 14-3-3 protein zeta/delta
A: Ubiquitin carboxyl-terminal hydrolase 8
Q: 14-3-3 protein zeta/delta
B: Ubiquitin carboxyl-terminal hydrolase 8
R: 14-3-3 protein zeta/delta
C: Ubiquitin carboxyl-terminal hydrolase 8
S: 14-3-3 protein zeta/delta
D: Ubiquitin carboxyl-terminal hydrolase 8


Theoretical massNumber of molelcules
Total (without water)111,6908
Polymers111,6908
Non-polymers00
Water11,620645
1
S: 14-3-3 protein zeta/delta
D: Ubiquitin carboxyl-terminal hydrolase 8

P: 14-3-3 protein zeta/delta
A: Ubiquitin carboxyl-terminal hydrolase 8


Theoretical massNumber of molelcules
Total (without water)55,8454
Polymers55,8454
Non-polymers00
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_665x+1,y+1,z1
2
R: 14-3-3 protein zeta/delta
C: Ubiquitin carboxyl-terminal hydrolase 8

Q: 14-3-3 protein zeta/delta
B: Ubiquitin carboxyl-terminal hydrolase 8


Theoretical massNumber of molelcules
Total (without water)55,8454
Polymers55,8454
Non-polymers00
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_455x-1,y,z1
3
P: 14-3-3 protein zeta/delta
A: Ubiquitin carboxyl-terminal hydrolase 8

S: 14-3-3 protein zeta/delta
D: Ubiquitin carboxyl-terminal hydrolase 8


Theoretical massNumber of molelcules
Total (without water)55,8454
Polymers55,8454
Non-polymers00
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_445x-1,y-1,z1
Buried area4610 Å2
ΔGint-23 kcal/mol
Surface area21860 Å2
MethodPISA
4
Q: 14-3-3 protein zeta/delta
B: Ubiquitin carboxyl-terminal hydrolase 8

R: 14-3-3 protein zeta/delta
C: Ubiquitin carboxyl-terminal hydrolase 8


Theoretical massNumber of molelcules
Total (without water)55,8454
Polymers55,8454
Non-polymers00
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_655x+1,y,z1
Buried area4160 Å2
ΔGint-28 kcal/mol
Surface area21780 Å2
MethodPISA
Unit cell
Length a, b, c (Å)60.379, 64.890, 71.519
Angle α, β, γ (deg.)99.71, 114.22, 108.79
Int Tables number1
Space group name H-MP1

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Components

#1: Protein
14-3-3 protein zeta/delta / Protein kinase C inhibitor protein 1 / KCIP-1


Mass: 26316.764 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: YWHAZ / Production host: Escherichia coli (E. coli) / References: UniProt: P63104
#2: Protein/peptide
Ubiquitin carboxyl-terminal hydrolase 8 / Deubiquitinating enzyme 8 / Ubiquitin isopeptidase Y / hUBPy / Ubiquitin thioesterase 8 / Ubiquitin- ...Deubiquitinating enzyme 8 / Ubiquitin isopeptidase Y / hUBPy / Ubiquitin thioesterase 8 / Ubiquitin-specific-processing protease 8


Mass: 1605.706 Da / Num. of mol.: 4 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P40818, ubiquitinyl hydrolase 1
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 645 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

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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: 2.1 Å3/Da / Density % sol: 41.43 %
Crystal growTemperature: 298.15 K / Method: vapor diffusion, hanging drop / Details: 0.1 M phosphate citrate pH 4.4; 40% PEG 300

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Sep 7, 2017
RadiationProtocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.594→61.137 Å / Num. obs: 107299 / % possible obs: 91.5 % / Redundancy: 3.3 % / Biso Wilson estimate: 20.1 Å2 / Rmerge(I) obs: 0.062 / Rpim(I) all: 0.062 / Rrim(I) all: 0.088 / Net I/σ(I): 1.84
Reflection shellResolution: 1.594→1.62 Å

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Processing

Software
NameVersionClassification
PHENIX(1.12_2829: ???)refinement
iMOSFLMdata reduction
Aimlessdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4HKC

4hkc


Resolution: 1.594→61.137 Å / SU ML: 0.21 / Cross valid method: NONE / σ(F): 1.96 / Phase error: 22.56
RfactorNum. reflection% reflection
Rfree0.2247 5241 4.89 %
Rwork0.18 --
obs0.1822 107251 91.49 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 1.594→61.137 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7352 0 0 645 7997
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.017447
X-RAY DIFFRACTIONf_angle_d1.01110041
X-RAY DIFFRACTIONf_dihedral_angle_d13.074589
X-RAY DIFFRACTIONf_chiral_restr0.051132
X-RAY DIFFRACTIONf_plane_restr0.0071295
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.594-1.61210.31211620.27773315X-RAY DIFFRACTION90
1.6121-1.63110.31192050.26383446X-RAY DIFFRACTION92
1.6311-1.6510.30241690.2483320X-RAY DIFFRACTION91
1.651-1.67190.26031850.23753356X-RAY DIFFRACTION91
1.6719-1.69390.26911950.22563380X-RAY DIFFRACTION91
1.6939-1.71710.2581890.23183311X-RAY DIFFRACTION90
1.7171-1.74160.27921640.21223366X-RAY DIFFRACTION89
1.7416-1.76760.26731610.21533262X-RAY DIFFRACTION89
1.7676-1.79520.27931680.21543285X-RAY DIFFRACTION88
1.7952-1.82470.23451520.20743122X-RAY DIFFRACTION83
1.8247-1.85610.27971640.20733446X-RAY DIFFRACTION93
1.8561-1.88990.23611760.20243436X-RAY DIFFRACTION92
1.8899-1.92620.22861700.19913460X-RAY DIFFRACTION93
1.9262-1.96560.23911750.20133430X-RAY DIFFRACTION92
1.9656-2.00830.24761750.18883431X-RAY DIFFRACTION92
2.0083-2.0550.24181710.193403X-RAY DIFFRACTION92
2.055-2.10640.22371640.1783397X-RAY DIFFRACTION91
2.1064-2.16340.23751820.17043263X-RAY DIFFRACTION88
2.1634-2.2270.20351880.17353289X-RAY DIFFRACTION89
2.227-2.29890.22091770.16563503X-RAY DIFFRACTION94
2.2989-2.38110.21422020.1633482X-RAY DIFFRACTION94
2.3811-2.47640.25561680.16663463X-RAY DIFFRACTION93
2.4764-2.58910.1852040.17443489X-RAY DIFFRACTION93
2.5891-2.72560.2271720.17313367X-RAY DIFFRACTION91
2.7256-2.89640.21481630.17193327X-RAY DIFFRACTION89
2.8964-3.120.2261760.18153562X-RAY DIFFRACTION96
3.12-3.4340.21681670.17043542X-RAY DIFFRACTION95
3.434-3.93080.19731660.15833487X-RAY DIFFRACTION94
3.9308-4.95210.18861540.15493496X-RAY DIFFRACTION93
4.9521-61.18210.23161770.19253574X-RAY DIFFRACTION96
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)
10.1966-0.23430.36040.83670.0391.09660.0604-0.31440.83190.0208-0.05290.2725-0.1161-0.5013-0.02850.09270.08730.03140.192-0.06140.4724-21.87854.877-5.032
21.15741.09980.84380.76470.28780.5003-0.1111-0.02020.0963-0.20210.04680.10520.00090.0519-0.10830.137-0.00890.00620.1081-0.01090.1491-4.506-4.3712-10.6732
30.98910.4380.58331.10920.28110.821-0.0383-0.0397-0.0508-0.07020.01290.0414-0.09690.0329-0.00070.1303-0.00160.0210.10230.00760.11554.57515.031.3345
40.31170.24220.26210.92350.37350.5201-0.1308-0.4357-0.25340.5107-0.07070.16810.27520.0887-0.04620.23020.00810.03650.21070.04670.18092.7165-3.571816.4938
50.1855-0.00980.09140.0203-0.00090.03560.1732-0.0926-0.1125-0.17430.10190.15440.1425-0.34480.01980.1471-0.02460.02850.20960.05650.1915-2.418-5.15275.2241
60.26570.19180.02690.20880.03960.01710.0136-0.08830.72580.21620.1060.54490.1085-0.374-0.10570.22940.0410.10080.3495-0.02990.2827-3.5141-19.678236.962
70.3196-0.14080.24130.464-0.11120.17110.00510.0592-0.0920.4197-0.01370.1221-0.1805-0.23550.08140.1590.00520.05340.25590.01160.1967-1.5659-26.750933.9679
80.24990.34580.2211.009-0.17070.36680.04840.1596-0.0284-0.2124-0.03330.1366-0.127-0.18720.00040.13390.0136-0.01520.2025-0.00850.16816.752-29.306421.5637
90.014-0.01720.01980.0103-0.01380.0183-0.129-0.0419-0.1636-0.1016-0.32810.1442-0.08410.149-0.00020.3662-0.10320.06620.45430.04310.45230.4401-37.333612.8943
100.16590.2080.21130.24570.10270.41320.2093-0.1632-0.49050.0146-0.03-0.0593-0.06590.00410.01450.14630.011-0.01050.2110.0310.233911.2156-37.535725.734
110.4123-0.0539-0.41620.3346-0.04691.20290.2754-0.3772-0.4170.03680.14120.08730.018-0.04950.33870.1520.0039-0.0460.24740.03230.2937-3.9708-37.746821.9565
120.12220.0144-0.0580.0479-0.04970.20280.36610.3789-0.542-0.2759-0.07450.07580.1961-0.05750.00870.2327-0.0099-0.06180.2268-0.00620.4091-8.1289-41.947614.5991
130.0611-0.15520.16560.3432-0.37450.3577-0.01190.0615-0.1685-0.00560.0902-0.06580.0980.07860.0470.16660.0073-0.03490.2486-0.07220.2008-6.4504-33.43659.9207
140.65060.31170.1850.1608-0.06620.2766-0.04350.16160.05420.00810.16710.0110.19850.08060.0390.19320.0144-0.01080.2553-0.02040.1786-13.0177-27.494.6808
150.20120.15510.05040.1689-0.04990.0732-0.02380.13140.2629-0.0212-0.05290.1011-0.0530.0976-0.00270.1945-0.03330.00190.2901-0.00230.1665-4.8692-23.73695.2022
160.0385-0.02450.04250.0598-0.05420.0513-0.05190.08090.17960.18240.21980.0905-0.2773-0.02420.00650.2571-0.00210.01750.3117-0.00860.2019-0.385-25.263513.8206
170.66491.0667-0.20871.3125-0.14830.1805-0.12280.0614-0.1055-0.01510.1541-0.15640.0276-0.01140.0060.15780.02210.00570.1731-0.02940.1396-36.4587-18.497227.8905
180.12810.05490.06810.5963-0.25810.16270.0481-0.20650.340.3508-0.0280.0295-0.04440.06480.00770.27320.03090.02970.2205-0.01430.1576-47.895-12.421640.7862
191.5758-0.0896-0.28711.1909-0.29670.5179-0.0902-0.03240.19020.16130.0713-0.2589-0.18660.0653-0.00260.1832-0.0023-0.03290.1626-0.02340.1746-31.25310.526629.1398
200.74540.8296-0.09891.0251-0.10530.1568-0.1460.5917-0.0506-0.30240.27340.0858-0.15-0.69260.19660.25110.0329-0.01780.33310.02520.1709-38.87361.842815.9044
210.11640.1116-0.0890.1102-0.08810.08820.05720.58920.1370.12720.02160.24390.2543-0.23650.00190.22290.0009-0.01550.33360.00980.1645-42.3878-2.904923.6585
220.0672-0.04290.00890.1636-0.08580.045-0.05140.3039-0.23830.079-0.0206-0.16690.30070.0176-0.00510.1848-0.01850.0390.2334-0.08550.30233.875936.9263-20.8151
230.00610.0634-0.00990.1101-0.03410.0721-0.09890.2495-0.032-0.06190.127-0.19260.02270.2124-0.00610.2232-0.03270.02570.1825-0.030.18426.33738.2557-21.6814
240.44390.42510.17490.4859-0.0360.2247-0.0172-0.1091-0.04550.21820.05710.06630.06030.06570.00010.1698-0.0040.00440.14270.00940.136816.894144.2971-10.1307
250.19470.0831-0.15820.1886-0.17140.23270.06170.05910.0783-0.1774-0.07810.3633-0.0572-0.1668-0.0020.19760.0088-0.00220.15510.04090.208910.414652.2726-14.7672
260.60140.007-0.55830.1881-0.20570.5645-0.03730.04110.0065-0.21980.16720.13160.1341-0.02840.08790.2142-0.014-0.03390.13330.01250.130411.836232.9501-17.7322
270.0209-0.1009-0.18820.08650.04150.4471-0.04690.0688-0.1279-0.35760.12750.50660.168-0.151-0.19430.227-0.0413-0.08240.16090.02190.19754.326628.0926-14.6465
280.41140.5368-0.23850.7922-0.6280.5823-0.0526-0.0712-0.0528-0.01050.00570.08210.01560.0429-0.00770.13840.00440.0040.1260.01470.129711.210423.6483-2.6392
290.16820.12150.18490.1459-0.00020.2532-0.0862-0.0454-0.02020.13280.0943-0.20390.03510.1975-00.2063-0.0157-0.00750.2059-00.136412.803130.02974.3161
301.0947-0.1906-1.20191.04460.37461.3489-0.21160.21550.11550.0782-0.1714-0.0084-0.05970.0527-0.29070.2264-0.0634-0.13890.22550.02150.223212.679138.33640.4132
310.0221-0.0004-0.00050.03020.02920.008-0.27990.0423-0.02810.2136-0.3624-0.33710.40010.4723-0.05480.22610.01460.03110.6006-0.04080.45923.180830.1818-7.0053
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'P' and (resid 2 through 15 )
2X-RAY DIFFRACTION2chain 'P' and (resid 16 through 103 )
3X-RAY DIFFRACTION3chain 'P' and (resid 104 through 184 )
4X-RAY DIFFRACTION4chain 'P' and (resid 185 through 230 )
5X-RAY DIFFRACTION5chain 'A' and (resid 1009 through 1015 )
6X-RAY DIFFRACTION6chain 'Q' and (resid 2 through 15 )
7X-RAY DIFFRACTION7chain 'Q' and (resid 16 through 37 )
8X-RAY DIFFRACTION8chain 'Q' and (resid 38 through 68 )
9X-RAY DIFFRACTION9chain 'Q' and (resid 69 through 76 )
10X-RAY DIFFRACTION10chain 'Q' and (resid 77 through 103 )
11X-RAY DIFFRACTION11chain 'Q' and (resid 104 through 137 )
12X-RAY DIFFRACTION12chain 'Q' and (resid 138 through 159 )
13X-RAY DIFFRACTION13chain 'Q' and (resid 160 through 184 )
14X-RAY DIFFRACTION14chain 'Q' and (resid 185 through 210 )
15X-RAY DIFFRACTION15chain 'Q' and (resid 211 through 229 )
16X-RAY DIFFRACTION16chain 'B' and (resid 1008 through 1016 )
17X-RAY DIFFRACTION17chain 'R' and (resid 2 through 68 )
18X-RAY DIFFRACTION18chain 'R' and (resid 69 through 103 )
19X-RAY DIFFRACTION19chain 'R' and (resid 104 through 207 )
20X-RAY DIFFRACTION20chain 'R' and (resid 208 through 230 )
21X-RAY DIFFRACTION21chain 'C' and (resid 1008 through 1013 )
22X-RAY DIFFRACTION22chain 'S' and (resid 2 through 15 )
23X-RAY DIFFRACTION23chain 'S' and (resid 16 through 37 )
24X-RAY DIFFRACTION24chain 'S' and (resid 38 through 69 )
25X-RAY DIFFRACTION25chain 'S' and (resid 70 through 103 )
26X-RAY DIFFRACTION26chain 'S' and (resid 104 through 137 )
27X-RAY DIFFRACTION27chain 'S' and (resid 138 through 159 )
28X-RAY DIFFRACTION28chain 'S' and (resid 160 through 213 )
29X-RAY DIFFRACTION29chain 'S' and (resid 214 through 230 )
30X-RAY DIFFRACTION30chain 'D' and (resid 1008 through 1010 )
31X-RAY DIFFRACTION31chain 'D' and (resid 1012 through 1017 )

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