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- PDB-6w9d: RNF12 RING domain in complex with a Ube2d2~Ub conjugate -

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Basic information

Entry
Database: PDB / ID: 6w9d
TitleRNF12 RING domain in complex with a Ube2d2~Ub conjugate
Components
  • E3 ubiquitin-protein ligase RLIM
  • Ubiquitin-conjugating enzyme E2 D2
  • Ubiquitin
KeywordsLIGASE / RING E3 ligase / Ubiquitin / Ubiquitin conjugating enzyme / X-chromosome inactivation / RING
Function / homology
Function and homology information


random inactivation of X chromosome / (E3-independent) E2 ubiquitin-conjugating enzyme / E2 ubiquitin-conjugating enzyme / ubiquitin conjugating enzyme activity / protein K48-linked ubiquitination / protein autoubiquitination / ubiquitin ligase complex / Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) ...random inactivation of X chromosome / (E3-independent) E2 ubiquitin-conjugating enzyme / E2 ubiquitin-conjugating enzyme / ubiquitin conjugating enzyme activity / protein K48-linked ubiquitination / protein autoubiquitination / ubiquitin ligase 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 / Constitutive Signaling by NOTCH1 HD Domain Mutants / Endosomal Sorting Complex Required For Transport (ESCRT) / NOTCH2 Activation and Transmission of Signal to the Nucleus / 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 / Regulation of FZD by ubiquitination / TICAM1,TRAF6-dependent induction of TAK1 complex / TICAM1-dependent activation of IRF3/IRF7 / APC/C:Cdc20 mediated degradation of Cyclin B / Downregulation of ERBB4 signaling / p75NTR recruits signalling complexes / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / APC-Cdc20 mediated degradation of Nek2A / PINK1-PRKN Mediated Mitophagy / transcription repressor complex / TRAF6-mediated induction of TAK1 complex within TLR4 complex / InlA-mediated entry of Listeria monocytogenes into host cells / Pexophagy / Regulation of innate immune responses to cytosolic DNA / VLDLR internalisation and degradation / Downregulation of ERBB2:ERBB3 signaling / NRIF signals cell death from the nucleus / Activated NOTCH1 Transmits Signal to the Nucleus / Translesion synthesis by REV1 / NF-kB is activated and signals survival / Regulation of PTEN localization / Translesion synthesis by POLK / Regulation of BACH1 activity / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Translesion synthesis by POLI / Gap-filling DNA repair synthesis and ligation in GG-NER / MAP3K8 (TPL2)-dependent MAPK1/3 activation / TICAM1, RIP1-mediated IKK complex recruitment / Downregulation of TGF-beta receptor signaling / Josephin domain DUBs / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / 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 / Regulation of NF-kappa B signaling / NIK-->noncanonical NF-kB signaling / Ubiquitin-dependent degradation of Cyclin D / AUF1 (hnRNP D0) binds and destabilizes mRNA / Negative regulators of DDX58/IFIH1 signaling / TNFR2 non-canonical NF-kB pathway / NOTCH3 Activation and Transmission of Signal to the Nucleus / activated TAK1 mediates p38 MAPK activation / Assembly of the pre-replicative complex / Vpu mediated degradation of CD4 / Deactivation of the beta-catenin transactivating complex / Degradation of DVL / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Recognition of DNA damage by PCNA-containing replication complex / Regulation of signaling by CBL / Dectin-1 mediated noncanonical NF-kB signaling / Hh mutants are degraded by ERAD / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Fanconi Anemia Pathway / Negative regulation of FGFR3 signaling / Termination of translesion DNA synthesis / Peroxisomal protein import / Degradation of AXIN / Downregulation of SMAD2/3:SMAD4 transcriptional activity / Regulation of TNFR1 signaling / Defective CFTR causes cystic fibrosis / Degradation of GLI1 by the proteasome / Activation of NF-kappaB in B cells / Hedgehog ligand biogenesis / Negative regulation of FGFR2 signaling / Negative regulation of FGFR4 signaling / Stabilization of p53
Similarity search - Function
Ring finger domain / Ubiquitin Conjugating Enzyme / Ubiquitin Conjugating Enzyme / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / Ubiquitin-conjugating enzyme E2, catalytic domain homologues / Ubiquitin-conjugating enzyme E2 / Ubiquitin-conjugating enzyme / Ubiquitin-conjugating (UBC) core domain profile. / Ubiquitin-conjugating enzyme/RWD-like ...Ring finger domain / Ubiquitin Conjugating Enzyme / Ubiquitin Conjugating Enzyme / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / Ubiquitin-conjugating enzyme E2, catalytic domain homologues / Ubiquitin-conjugating enzyme E2 / Ubiquitin-conjugating enzyme / Ubiquitin-conjugating (UBC) core domain profile. / Ubiquitin-conjugating enzyme/RWD-like / Zinc/RING finger domain, C3HC4 (zinc finger) / Herpes Virus-1 / Ring finger / Ubiquitin conserved site / Ubiquitin domain / Zinc finger RING-type profile. / Zinc finger, RING-type / Ubiquitin domain signature. / Ubiquitin family / Ubiquitin homologues / Ubiquitin-like domain / Ubiquitin domain profile. / Ubiquitin-like domain superfamily / Zinc finger, RING/FYVE/PHD-type / Roll / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
IODIDE ION / Polyubiquitin-C / Ubiquitin-conjugating enzyme E2 D2 / E3 ubiquitin-protein ligase RLIM
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3.19 Å
AuthorsMiddleton, A.J. / Day, C.L.
Funding support New Zealand, 1items
OrganizationGrant numberCountry
Marsden Fund New Zealand
CitationJournal: J.Mol.Biol. / Year: 2020
Title: The RING Domain of RING Finger 12 Efficiently Builds Degradative Ubiquitin Chains.
Authors: Middleton, A.J. / Zhu, J. / Day, C.L.
History
DepositionMar 22, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 20, 2020Provider: repository / Type: Initial release
Revision 1.1May 27, 2020Group: Database references / Category: citation / citation_author
Item: _citation.pdbx_database_id_PubMed / _citation.title ..._citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID
Revision 1.2Jul 1, 2020Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3Oct 18, 2023Group: 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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Ubiquitin-conjugating enzyme E2 D2
B: E3 ubiquitin-protein ligase RLIM
C: Ubiquitin
D: Ubiquitin-conjugating enzyme E2 D2
E: E3 ubiquitin-protein ligase RLIM
F: Ubiquitin
G: Ubiquitin-conjugating enzyme E2 D2
H: E3 ubiquitin-protein ligase RLIM
I: Ubiquitin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)113,89123
Polymers112,4849
Non-polymers1,40814
Water0
1
A: Ubiquitin-conjugating enzyme E2 D2
B: E3 ubiquitin-protein ligase RLIM
C: Ubiquitin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)37,8797
Polymers37,4953
Non-polymers3854
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
D: Ubiquitin-conjugating enzyme E2 D2
E: E3 ubiquitin-protein ligase RLIM
F: Ubiquitin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,0068
Polymers37,4953
Non-polymers5125
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
G: Ubiquitin-conjugating enzyme E2 D2
H: E3 ubiquitin-protein ligase RLIM
I: Ubiquitin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,0068
Polymers37,4953
Non-polymers5125
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)135.473, 135.473, 51.372
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number144
Space group name H-MP31

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Components

#1: Protein Ubiquitin-conjugating enzyme E2 D2 / (E3-independent) E2 ubiquitin-conjugating enzyme D2 / E2 ubiquitin-conjugating enzyme D2 / ...(E3-independent) E2 ubiquitin-conjugating enzyme D2 / E2 ubiquitin-conjugating enzyme D2 / Ubiquitin carrier protein D2 / Ubiquitin-conjugating enzyme E2(17)KB 2 / Ubiquitin-conjugating enzyme E2-17 kDa 2 / Ubiquitin-protein ligase D2 / p53-regulated ubiquitin-conjugating enzyme 1


Mass: 17874.340 Da / Num. of mol.: 3 / Mutation: C21S, S22R, C85K, C107S, C111S
Source method: isolated from a genetically manipulated source
Details: C21, C107, and C111 are mutated to Ser for stability. C85 is mutated to Lys for formation of an isopeptide bond to G76 of ubiquitin. S22 is mutated to Arg
Source: (gene. exp.) Homo sapiens (human) / Gene: UBE2D2, PUBC1, UBC4, UBC5B, UBCH4, UBCH5B / Production host: Escherichia coli (E. coli)
References: UniProt: P62837, E2 ubiquitin-conjugating enzyme, (E3-independent) E2 ubiquitin-conjugating enzyme
#2: Protein E3 ubiquitin-protein ligase RLIM / LIM domain-interacting RING finger protein / RING finger LIM domain-binding protein / R-LIM / RING ...LIM domain-interacting RING finger protein / RING finger LIM domain-binding protein / R-LIM / RING finger protein 12 / RING-type E3 ubiquitin transferase RLIM / Renal carcinoma antigen NY-REN-43 / RNF12


Mass: 11043.381 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RLIM, RNF12 / Production host: Escherichia coli (E. coli)
References: UniProt: Q9NVW2, RING-type E3 ubiquitin transferase
#3: Protein Ubiquitin /


Mass: 8576.831 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Details: Linked to Ube2d2 via isopeptide bond between G76 of ubiquitin and Lys85 of Ube2d2
Source: (gene. exp.) Homo sapiens (human) / Gene: UBC / Production host: Escherichia coli (E. coli) / References: UniProt: P0CG48
#4: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Zn
#5: Chemical
ChemComp-IOD / IODIDE ION / Iodide


Mass: 126.904 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: I
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: 2.42 Å3/Da / Density % sol: 49.17 % / Description: Needles
Crystal growTemperature: 289 K / Method: vapor diffusion, hanging drop / pH: 7.5 / Details: 15-20% PEG 3350, 200-400 mM NaI

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.9537 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Oct 28, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9537 Å / Relative weight: 1
ReflectionResolution: 3.189→47.06 Å / Num. obs: 17289 / % possible obs: 98.3 % / Redundancy: 2.3 % / Biso Wilson estimate: 90.34 Å2 / CC1/2: 0.995 / Rmerge(I) obs: 0.088 / Rpim(I) all: 0.071 / Rrim(I) all: 0.114 / Net I/σ(I): 8.2
Reflection shellResolution: 3.19→3.41 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.638 / Num. unique obs: 3172 / CC1/2: 0.52 / Rpim(I) all: 0.514 / Rrim(I) all: 0.827 / % possible all: 99

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
PHENIX1.13_2998refinement
XDSdata reduction
Aimless0.5.28data scaling
PHASERphasing
PDB_EXTRACT3.25data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1UBQ

1ubq


Resolution: 3.19→47.058 Å / SU ML: 0.47 / Cross valid method: THROUGHOUT / σ(F): 1.96 / Phase error: 29.19
RfactorNum. reflection% reflection
Rfree0.2806 829 4.8 %
Rwork0.2217 --
obs0.2245 17276 98.25 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 204.8 Å2 / Biso mean: 95.3047 Å2 / Biso min: 45.9 Å2
Refinement stepCycle: final / Resolution: 3.19→47.058 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6858 0 14 0 6872
Biso mean--91.91 --
Num. residues----854
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0027010
X-RAY DIFFRACTIONf_angle_d0.5279495
X-RAY DIFFRACTIONf_dihedral_angle_d3.4294322
X-RAY DIFFRACTIONf_chiral_restr0.0411062
X-RAY DIFFRACTIONf_plane_restr0.0041220
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
3.19-3.38870.3681380.3231278499
3.3887-3.65020.37551370.2651275499
3.6502-4.01740.29251420.2359276199
4.0174-4.59830.24691440.1984275799
4.5983-5.79160.26171240.211273598
5.7916-47.0580.26151440.201265695
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)
110.11572.76176.26098.4275-2.31179.1280.29751.662-0.1452-0.58470.20180.1368-0.23491.4071-0.37910.675-0.04030.12730.7721-0.02550.6994140.1618143.883531.2734
27.3671.51362.46514.769-1.12925.26640.061-0.1355-0.02080.1996-0.03220.25490.3883-0.0312-0.16550.63540.03840.0540.48310.04110.4627127.7091139.232236.6098
36.77152.0815-1.36029.5828-7.85022.9878-0.35650.0472-0.746-0.84361.3960.61431.603-1.5565-1.10960.9133-0.2022-0.03190.6755-0.02050.7096112.2679134.769332.0376
42.5018-4.8258-6.21276.45794.01574.38870.5242-0.45950.2531.47470.0671-1.2111-0.2639-0.9099-1.14821.35780.2362-0.4271.490.04020.8806154.2089133.75958.184
55.9811-2.7852.31134.9212-2.16142.76250.56790.0718-1.9077-0.85140.0926-0.11952.09680.9958-0.4440.950.1219-0.21030.8464-0.10090.864153.8001133.018946.6939
62.01197.55265.89272.03241.93321.93290.485-0.3572-0.9846-1.63131.4675-2.0212.16320.2032-1.85151.55840.1917-0.19180.7263-0.00750.889149.9166131.117548.8579
77.3636-2.47240.76021.84842.95253.5065-0.4714-1.387-0.51231.23850.47970.145-0.5755-0.3922-0.35480.9727-0.1389-0.07521.34090.20520.6951142.7829135.078553.1417
80.55812.04011.68246.11685.71895.41760.4965-0.2716-1.34210.0985-0.2123-1.05040.00730.0234-0.1081.3098-0.0449-0.17830.68690.01211.2058137.5123115.812235.701
99.4723-0.4645-2.28646.16181.70845.21310.8982-0.67790.1265-0.0839-0.06390.26970.30360.1499-0.80050.9342-0.00350.00550.73120.00330.8002130.8936118.716838.8743
104.3218-1.4043-4.00528.03555.74067.10790.40430.49150.5230.62240.1277-1.02040.1071-0.4856-0.53560.82570.0416-0.04630.72520.13580.9649132.9489118.400430.3195
112.6947-7.3475-6.15723.37212.26852.9852-0.5216-1.867-0.29571.46860.3308-0.01860.91930.61570.17610.9742-0.020.04210.94890.02650.751181.6412117.173962.0568
124.1915-4.2019-2.12897.69711.7194.9786-0.1084-0.42430.18090.09770.2565-0.1299-0.55730.6558-0.13180.5994-0.10570.03530.61550.02320.416180.2341131.259257.2573
138.6861.91-1.81935.55890.037510.15990.3909-0.06120.58170.3909-0.1229-0.1171-1.76220.29880.12511.1325-0.23350.02210.789-0.04870.702577.6636147.755461.4264
149.0821-2.10315.98332.3718-5.81676.0341-0.00751.092-1.1907-0.83380.33150.2484-0.17242.0557-0.67661.23060.15570.07950.9883-0.15130.776794.3459112.253136.9512
152.5507-6.0175-1.03412.56995.86273.9081-0.1399-1.3938-1.3989-0.24010.98970.53260.4014-0.0144-0.850.75630.1112-0.15890.77540.07141.082994.4253108.039948.0505
161.88728.19876.5332.0363-1.10888.07730.1010.0003-0.4223-2.77210.1437-2.98651.02174.0554-0.50780.7536-0.0850.29241.4828-0.28181.148298.3353115.636242.0973
179.7245-4.75455.71627.72941.53087.7112-0.00740.32040.8725-2.5092-0.5271-0.45020.1186-0.16930.58991.186-0.05250.07370.74170.02990.709190.2299119.908940.3106
188.3767-5.6570.10166.8416-3.60084.90180.12710.3734-1.9411-0.65430.0656-0.36752.4822-1.7712-0.17310.899-0.3771-0.06391.2377-0.22280.7368103.3583127.39955.5765
199.455-1.5376-0.4448.0014-3.92822.0807-0.5808-0.09731.29242.6395-1.1549-1.3442-0.63430.91281.48581.7857-0.83090.09121.83-0.39041.3826109.5541138.77259.9943
202.5877-1.587-5.72968.8603-0.56758.1218-0.73051.32760.76620.45170.01630.90880.42850.24160.67020.9243-0.26190.00831.5785-0.19571.218499.7434137.885155.8738
216.3914-1.5564.10811.2015-0.25646.08870.9709-3.4032-0.28770.3749-0.21850.2569-0.1455-0.7143-0.86061.0583-0.62270.19641.7165-0.28281.3248103.9674133.335664.9305
222.98675.1145-4.96927.64296.8752.0263-0.73520.56070.7457-0.5179-0.47911.27750.7338-2.04151.42260.8739-0.09050.00131.0068-0.01550.8567118.131474.559965.5327
233.83172.87130.27327.8527-4.58126.2973-0.47180.1216-0.2319-1.39180.19920.090.6266-0.57380.33180.8569-0.0136-0.00980.8218-0.23210.7435123.531685.846261.5603
245.96442.1293-2.22537.8698-4.37273.8835-0.1425-0.01090.33920.20130.0364-0.0976-0.2246-0.11190.0450.44920.0665-0.06440.5074-0.0330.4966122.020790.365570.4683
257.1723-0.3564-0.55165.87643.42363.32740.69460.63370.8994-0.6526-0.45470.7024-1.9097-1.2113-0.21520.76610.2377-0.10360.67270.03990.8186121.4529107.407565.2678
268.83673.88870.38532.0366-4.05457.5886-0.37131.27140.33640.97461.5491.32090.7065-1.2137-1.1791.6293-0.29410.27461.63130.03570.7754115.165975.409195.9686
279.0972-1.41533.99839.1842-2.01741.99192.1088-0.6053-1.94530.45190.57711.4104-4.1006-0.4807-2.25891.3757-0.95630.63040.8560.06110.8504104.189364.41582.7744
287.53560.0165-3.25317.7712-1.20777.11590.2728-0.0055-0.25440.3783-0.00420.49760.2054-0.4628-0.19760.4529-0.0257-0.0750.4453-0.00650.605110.322773.115183.0617
298.99920.1994-2.43248.4654.8998.2974-0.18640.46420.4652-0.6188-0.48380.6666-0.4173-0.64840.38430.77880.23740.03371.13260.12030.658396.187191.206972.3608
302.4731-1.90881.6179.6731-7.30531.9875-0.03790.84120.9521-0.1006-1.364-1.0987-1.5344-0.81481.31051.15030.26150.02851.32820.11281.0966102.196197.0765.1613
319.81840.364.89728.53741.6564.59420.90760.88920.4977-0.3333-0.01941.18570.51460.7154-0.47940.84480.04510.12231.23010.06860.9236100.419889.114666.224
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain A and resid 2:36)A2 - 36
2X-RAY DIFFRACTION2(chain A and resid 37:110)A37 - 110
3X-RAY DIFFRACTION3(chain A and resid 111:149)A111 - 149
4X-RAY DIFFRACTION4(chain B and resid 550:565)B550 - 565
5X-RAY DIFFRACTION5(chain B and resid 566:589)B566 - 589
6X-RAY DIFFRACTION6(chain B and resid 590:593)B590 - 593
7X-RAY DIFFRACTION7(chain B and resid 594:614)B594 - 614
8X-RAY DIFFRACTION8(chain C and resid 1:25)C1 - 25
9X-RAY DIFFRACTION9(chain C and resid 26:50)C26 - 50
10X-RAY DIFFRACTION10(chain C and resid 51:72)C51 - 72
11X-RAY DIFFRACTION11(chain D and resid 2:32)D2 - 32
12X-RAY DIFFRACTION12(chain D and resid 33:112)D33 - 112
13X-RAY DIFFRACTION13(chain D and resid 113:149)D113 - 149
14X-RAY DIFFRACTION14(chain E and resid 545:568)E545 - 568
15X-RAY DIFFRACTION15(chain E and resid 569:584)E569 - 584
16X-RAY DIFFRACTION16(chain E and resid 585:594)E585 - 594
17X-RAY DIFFRACTION17(chain E and resid 595:614)E595 - 614
18X-RAY DIFFRACTION18(chain F and resid 1:15)F1 - 15
19X-RAY DIFFRACTION19(chain F and resid 16:26)F16 - 26
20X-RAY DIFFRACTION20(chain F and resid 27:53)F27 - 53
21X-RAY DIFFRACTION21(chain F and resid 54:70)F54 - 70
22X-RAY DIFFRACTION22(chain G and resid 1:19)G1 - 19
23X-RAY DIFFRACTION23(chain G and resid 20:44)G20 - 44
24X-RAY DIFFRACTION24(chain G and resid 45:111)G45 - 111
25X-RAY DIFFRACTION25(chain G and resid 112:148)G112 - 148
26X-RAY DIFFRACTION26(chain H and resid 545:555)H545 - 555
27X-RAY DIFFRACTION27(chain H and resid 556:568)H556 - 568
28X-RAY DIFFRACTION28(chain H and resid 569:614)H569 - 614
29X-RAY DIFFRACTION29(chain I and resid 1:37)I1 - 37
30X-RAY DIFFRACTION30(chain I and resid 38:59)I38 - 59
31X-RAY DIFFRACTION31(chain I and resid 60:72)I60 - 72

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