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- PDB-4nnj: Crystal structure of Uba1 in complex with ubiquitin-AMP and thioe... -

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Basic information

Entry
Database: PDB / ID: 4nnj
TitleCrystal structure of Uba1 in complex with ubiquitin-AMP and thioesterified ubiquitin
Components
  • Uba1
  • Ubiquitin-activating enzyme E1 1
KeywordsPROTEIN BINDING / ubiquitin activating enzyme (E1) / Uba1 / ubiquitin / acyladenylate / ubiquitin thioester / Ubiquitin activation / AMP / thioesterified Ub
Function / homology
Function and homology information


Josephin domain DUBs / RAS processing / Regulation of PTEN localization / ER Quality Control Compartment (ERQC) / UCH proteinases / Interleukin-1 signaling / Aggrephagy / Pexophagy / PINK1-PRKN Mediated Mitophagy / Regulation of pyruvate metabolism ...Josephin domain DUBs / RAS processing / Regulation of PTEN localization / ER Quality Control Compartment (ERQC) / UCH proteinases / Interleukin-1 signaling / Aggrephagy / Pexophagy / PINK1-PRKN Mediated Mitophagy / Regulation of pyruvate metabolism / Peroxisomal protein import / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Metalloprotease DUBs / E1 ubiquitin-activating enzyme / Endosomal Sorting Complex Required For Transport (ESCRT) / ubiquitin activating enzyme activity / E3 ubiquitin ligases ubiquitinate target proteins / Translesion synthesis by REV1 / Translesion synthesis by POLK / Translesion synthesis by POLI / Translesion Synthesis by POLH / Termination of translesion DNA synthesis / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / Negative regulators of DDX58/IFIH1 signaling / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / Regulation of PTEN stability and activity / CDK-mediated phosphorylation and removal of Cdc6 / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / KEAP1-NFE2L2 pathway / Neddylation / Formation of TC-NER Pre-Incision Complex / Orc1 removal from chromatin / MAPK6/MAPK4 signaling / SRP-dependent cotranslational protein targeting to membrane / GTP hydrolysis and joining of the 60S ribosomal subunit / Gap-filling DNA repair synthesis and ligation in TC-NER / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / Formation of a pool of free 40S subunits / Antigen processing: Ubiquitination & Proteasome degradation / L13a-mediated translational silencing of Ceruloplasmin expression / Dual incision in TC-NER / Ub-specific processing proteases / modification-dependent protein catabolic process / protein tag activity / peroxisome / ubiquitin-dependent protein catabolic process / protein ubiquitination / DNA damage response / ubiquitin protein ligase binding / ATP binding / nucleus / cytoplasm / cytosol
Similarity search - Function
Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 2 / Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1 / Ubiquitin-activating enzyme E1, SCCH domain / Ubiquitin-activating enzyme E1, UFD domain / Ubiquitin-activating enzyme E1, FCCH domain / Ubiquitin-activating enzyme E1, conserved site / Ubiquitin-activating enzyme signature 1. / Ubiquitin-activating enzyme E1 / Ubiquitin-activating enzyme E1, C-terminal / Ubiquitin-activating enzyme E1, FCCH domain ...Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 2 / Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1 / Ubiquitin-activating enzyme E1, SCCH domain / Ubiquitin-activating enzyme E1, UFD domain / Ubiquitin-activating enzyme E1, FCCH domain / Ubiquitin-activating enzyme E1, conserved site / Ubiquitin-activating enzyme signature 1. / Ubiquitin-activating enzyme E1 / Ubiquitin-activating enzyme E1, C-terminal / Ubiquitin-activating enzyme E1, FCCH domain / Ubiquitin-activating enzyme E1, four-helix bundle / Ubiquitin-activating enzyme E1, C-terminal domain superfamily / Ubiquitin-activating enzyme E1, SCCH domain / Ubiquitin-activating enzyme E1, FCCH domain superfamily / Ubiquitin fold domain / Ubiquitin-activating enzyme E1 FCCH domain / Ubiquitin-activating enzyme E1 four-helix bundle / Ubiquitin-activating enzyme e1 C-terminal domain / Ubiquitin-activating enzyme, SCCH domain / Ubiquitin-activating enzyme, SCCH domain / Ubiquitin-activating enzyme E1, Cys active site / Ubiquitin-activating enzyme active site. / Ubiquitin/SUMO-activating enzyme E1-like / Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1 / ThiF/MoeB/HesA family / THIF-type NAD/FAD binding fold / ThiF family / Ubiquitin-activating enzyme / Structural Genomics Hypothetical 15.5 Kd Protein In mrcA-pckA Intergenic Region; Chain A / Elongation Factor Tu (Ef-tu); domain 3 / FAD/NAD(P)-binding domain / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / 3-Layer(bba) Sandwich / : / Ubiquitin domain signature. / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin-like (UB roll) / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Arc Repressor Mutant, subunit A / NAD(P)-binding Rossmann-like Domain / Ubiquitin-like domain superfamily / Roll / Beta Barrel / Rossmann fold / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
ADENOSINE MONOPHOSPHATE / Polyubiquitin / Ubiquitin-activating enzyme E1 1
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsSchaefer, A. / Schindelin, H.
CitationJournal: Acta Crystallogr.,Sect.D / Year: 2014
Title: Structure of the ubiquitin-activating enzyme loaded with two ubiquitin molecules.
Authors: Schafer, A. / Kuhn, M. / Schindelin, H.
History
DepositionNov 18, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 7, 2014Provider: repository / Type: Initial release
Revision 1.1Sep 24, 2014Group: Database references
Revision 1.2Sep 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
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
A: Ubiquitin-activating enzyme E1 1
B: Uba1
C: Ubiquitin-activating enzyme E1 1
D: Uba1
E: Uba1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)262,75340
Polymers259,0045
Non-polymers3,74935
Water18,3751020
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)73.040, 195.651, 230.629
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP22121

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Components

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Protein , 2 types, 5 molecules ACBDE

#1: Protein Ubiquitin-activating enzyme E1 1


Mass: 116304.914 Da / Num. of mol.: 2 / Fragment: UNP residues 9-1024
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Strain: ATCC 204508 / S288c / Gene: UBA1, YKL210W / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)RIL / References: UniProt: P22515
#2: Protein Uba1 / Ubiquitin


Mass: 8798.001 Da / Num. of mol.: 3 / Fragment: UNP residues 1-76
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Strain: ATCC 204508 / S288c / Gene: SCD2, UBI4, YLL039C / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)RIL / References: UniProt: P0CG63

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Non-polymers , 4 types, 1055 molecules

#3: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: SO4
#4: Chemical...
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 29 / Source method: obtained synthetically / Formula: C3H8O3
#5: Chemical ChemComp-AMP / ADENOSINE MONOPHOSPHATE


Mass: 347.221 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H14N5O7P / Comment: AMP*YM
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1020 / Source method: isolated from a natural source / Formula: H2O

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Details

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: 3.18 Å3/Da / Density % sol: 61.34 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6
Details: 15% (w/v) polyethylene glycol 3350, 100mM lithium sulfate and 100mM BisTris, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-2 / Wavelength: 0.873 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Jan 1, 2012
RadiationMonochromator: horizontally diffracting monochromator Si(111)
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.873 Å / Relative weight: 1
ReflectionResolution: 2.4→90 Å / Num. obs: 128882 / % possible obs: 98.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 5 % / Biso Wilson estimate: 40.06 Å2 / Rmerge(I) obs: 0.093 / Net I/σ(I): 11.7
Reflection shellResolution: 2.4→2.53 Å / Redundancy: 3.2 % / Rmerge(I) obs: 0.01124 / Mean I/σ(I) obs: 1 / Num. unique all: 17394 / % possible all: 93.4

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Processing

Software
NameVersionClassification
MxCuBEdata collection
EDNAdata collection
PHASERphasing
PHENIX(phenix.refine: 1.8_1069)refinement
XDSdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3CMM

3cmm


Resolution: 2.4→48.647 Å / SU ML: 0.29 / Isotropic thermal model: Isotropic / σ(F): 0 / Phase error: 21.23 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.2012 1430 1.11 %random
Rwork0.1636 ---
all0.1641 130301 --
obs0.1641 128871 98.01 %-
Solvent computationShrinkage radii: 0.8 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 48.5 Å2
Refine analyzeLuzzati sigma a free: 0.29 Å
Refinement stepCycle: LAST / Resolution: 2.4→48.647 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17708 0 240 1020 18968
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01118322
X-RAY DIFFRACTIONf_angle_d1.35224738
X-RAY DIFFRACTIONf_dihedral_angle_d16.0546869
X-RAY DIFFRACTIONf_chiral_restr0.072757
X-RAY DIFFRACTIONf_plane_restr0.0063211
LS refinement shell
Resolution (Å)Rfactor RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.4-2.44360.31390.311411386X-RAY DIFFRACTION87
2.4436-2.49060.32810.298911945X-RAY DIFFRACTION92
2.4906-2.54150.3080.29112279X-RAY DIFFRACTION94
2.5415-2.59670.28060.271912710X-RAY DIFFRACTION98
2.5967-2.65710.2780.245612842X-RAY DIFFRACTION100
2.6571-2.72360.26690.227513056X-RAY DIFFRACTION100
2.7236-2.79720.28110.209412950X-RAY DIFFRACTION100
2.7972-2.87950.25730.198612981X-RAY DIFFRACTION100
2.8795-2.97240.21020.192212944X-RAY DIFFRACTION100
2.9724-3.07870.28280.188412965X-RAY DIFFRACTION100
3.0787-3.20190.21250.179412991X-RAY DIFFRACTION100
3.2019-3.34760.23220.166412917X-RAY DIFFRACTION100
3.3476-3.5240.23570.156112914X-RAY DIFFRACTION100
3.524-3.74480.1990.142212883X-RAY DIFFRACTION99
3.7448-4.03380.14380.126912921X-RAY DIFFRACTION99
4.0338-4.43950.14270.109512781X-RAY DIFFRACTION98
4.4395-5.08130.13970.106212767X-RAY DIFFRACTION98
5.0813-6.39960.14630.140712873X-RAY DIFFRACTION99
6.3996-48.65690.17560.144212871X-RAY DIFFRACTION99
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)
11.0349-0.28280.13861.43550.13791.5071-0.0143-0.0765-0.0935-0.15190.05840.36630.046-0.3064-0.03260.2124-0.0135-0.0570.31460.03840.4024-24.845624.4568-42.4785
20.42930.91010.35964.34160.88851.0137-0.04010.0634-0.0063-0.19470.0446-0.1992-0.14440.18530.02670.2285-0.00010.01140.38930.02660.3095-0.429344.0596-45.9013
30.6597-0.03040.23960.92850.20520.86890.0177-0.1179-0.20510.12470.06060.09040.1953-0.0309-0.08570.25470.03770.00880.31170.05010.3322-8.63318.6776-28.3216
41.34670.5843-0.66851.9567-0.58413.13110.0037-0.52320.03090.2326-0.0769-0.1684-0.35410.28140.08530.4380.06650.00330.4621-0.03530.2811-10.47762.5795-4.647
50.1389-0.0880.03790.66690.15780.9037-0.0405-0.1185-0.07760.18820.07260.04050.01240.0317-0.01640.19710.00140.01010.30330.00880.2446-5.503233.5398-22.5825
62.21740.22032.22841.4759-0.84634.3537-0.0089-0.2814-0.02290.33280.31250.2806-0.4064-0.5104-0.27190.50220.18410.01290.43830.03150.389117.969915.09642.7543
73.06280.2888-2.57530.0254-0.23882.17360.20360.9691-0.2683-0.5181-0.0929-0.5665-0.35180.3359-0.01090.39860.04690.1930.72650.03170.569517.283434.2124-45.9338
82.011-4.19520.24546.22790.75494.4825-0.14640.58370.2967-0.419-0.1217-1.0579-0.49211.00640.03040.2866-0.02360.0290.55250.03410.557214.246335.7998-40.9683
96.4226-3.89760.36064.22181.0565.7110.227-0.16390.19890.2961-0.3395-1.0081-0.40270.8080.0750.2647-0.0701-0.11290.48470.02520.651516.644637.2737-32.0398
106.2833.34551.25667.07382.60146.95180.11910.3698-0.34480.2538-0.3392-0.80580.07250.40050.21480.18420.0199-0.03990.47480.090.381610.607825.9234-34.6972
114.0332.0448-4.13884.6086-3.2434.98050.0647-0.2921-1.14940.0057-0.0914-0.73880.73630.93750.2450.34180.252-0.03910.66820.09460.933620.786623.9589-34.9318
120.96982.2883-1.75045.8979-5.01844.7054-0.19821.54720.1575-1.6969-0.0034-1.47140.54320.81860.10950.5148-0.05950.13630.7216-0.0050.541815.128128.1714-46.2117
133.68153.2283-2.77492.8901-2.39342.15150.2446-0.69930.9770.3746-0.08110.1099-0.38270.005-0.49260.28880.0892-0.05180.3788-0.03730.2733-0.300131.2781-26.6934
140.7997-0.26080.00820.9214-0.11110.9813-0.1055-0.09720.00990.05760.15380.0934-0.1534-0.0506-0.0560.30380.0203-0.0040.26180.04440.2543-30.183170.7943-49.611
150.428-0.05130.1451.23850.39750.73360.06580.1842-0.1048-0.30340.077-0.0360.0391-0.0178-0.15580.3518-0.0142-0.03560.38110.01260.2637-29.380847.4191-77.67
161.0902-0.24770.57021.2986-1.32195.58240.06680.1196-0.11760.05140.11910.1882-0.0284-0.4638-0.15150.36540.02030.05320.40650.07850.3883-36.100989.829-95.8506
175.12323.7012-3.76285.1285-2.57883.76130.1599-0.93681.34120.7437-0.0054-0.4432-0.56550.79310.00130.3784-0.0979-0.09070.6156-0.12530.7693-3.588277.1094-61.0941
185.9818-4.16923.20574.8150.34676.52-0.2944-0.5450.2350.42660.287-0.29690.61190.15970.00150.38380.04170.03040.43580.0040.3193-9.053469.5788-61.7712
193.12081.4554-1.23940.6937-0.69081.3184-0.25990.4375-0.26020.0962-0.2314-1.6329-0.93421.20070.51830.5304-0.17350.12820.47550.20551.2148-0.155584.5112-68.8825
202.74561.73512.48113.0762-1.49147.02470.36550.82450.7519-1.09070.3442-1.1687-0.6510.8488-0.40150.5029-0.05110.24620.57950.05860.5667-6.372475.1799-72.8721
215.63681.7059-1.19666.97590.45243.42440.19160.64160.4349-0.7929-0.3246-0.1898-0.4671-0.12220.04510.4238-0.05320.06430.40910.10980.3201-14.916679.4044-70.2825
223.4826-3.28093.54193.3485-2.28747.7793-0.4104-0.27381.7950.33460.0594-1.174-1.35231.21520.5060.5839-0.17240.00220.565-0.08230.9013-6.058286.4619-62.3757
235.72071.0929-3.56143.1991-2.30984.50530.10420.3938-0.3849-0.20350.1764-0.19520.13290.1064-0.2470.35820.0152-0.01750.15960.02580.2735-22.057371.0211-65.6991
244.71425.5515-4.49696.5359-5.27954.6676-0.8104-0.0198-0.6933-0.07580.6848-0.88480.6767-0.06490.13090.5844-0.05870.19120.8027-0.28331.070311.389552.6548-80.5777
251.36550.98320.47767.6787-4.98664.2432-0.25730.924-0.7214-1.33540.6139-2.09480.15250.9548-0.13680.7604-0.29860.28560.9007-0.48810.849314.300253.0473-84.8933
263.49644.1790.21826.91262.11691.81190.04960.95150.0692-1.44360.7916-1.30850.52791.8023-0.88030.7269-0.26610.18080.8681-0.23010.919819.025866.1099-83.7608
275.4277-1.19991.16035.6442.68161.85510.21571.18060.2608-1.79860.1014-0.05380.04510.2806-0.51051.0842-0.32050.08321.1908-0.01090.44139.648360.6621-89.12
284.4843-4.1078-2.74477.82552.61765.79160.45170.84-0.1235-1.3786-0.45721.46160.3493-1.72760.18610.8933-0.3452-0.09071.181-0.04030.88261.593359.8764-87.0373
299.6965.4443-1.31158.5478-3.04914.43650.1803-0.1190.97451.5575-0.38021.195-0.051-0.470.23160.7653-0.04820.09580.57140.0050.59387.176166.6286-76.887
303.02994.9002-0.31688.71951.49249.0572-0.18630.7941-0.79420.07190.6491-1.48480.14810.5749-0.14470.5238-0.03680.09480.6342-0.02240.664716.764362.9285-75.1492
312.8054-1.5243-4.00772.13862.07365.7345-0.46241.2055-1.0082-0.2240.43870.35810.0904-0.50250.06250.5102-0.02120.21280.8834-0.02710.74956.059255.8815-78.1204
325.74632.808-2.83566.2105-4.7983.9121-0.67410.82340.626-0.92390.30532.8351-0.1798-0.38620.18430.974-0.1742-0.00851.42690.27332.0101-8.030157.5267-84.4906
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 11:166 )A11 - 166
2X-RAY DIFFRACTION2( CHAIN A AND RESID 167:306 )A167 - 306
3X-RAY DIFFRACTION3( CHAIN A AND RESID 307:624 )A307 - 624
4X-RAY DIFFRACTION4( CHAIN A AND RESID 625:811 )A625 - 811
5X-RAY DIFFRACTION5( CHAIN A AND RESID 812:925 )A812 - 925
6X-RAY DIFFRACTION6( CHAIN A AND RESID 926:1024 )A926 - 1024
7X-RAY DIFFRACTION7( CHAIN B AND RESID -1:6 )B-1 - 6
8X-RAY DIFFRACTION8( CHAIN B AND RESID 7:22 )B7 - 22
9X-RAY DIFFRACTION9( CHAIN B AND RESID 23:40 )B23 - 40
10X-RAY DIFFRACTION10( CHAIN B AND RESID 41:50 )B41 - 50
11X-RAY DIFFRACTION11( CHAIN B AND RESID 51:59 )B51 - 59
12X-RAY DIFFRACTION12( CHAIN B AND RESID 60:68 )B60 - 68
13X-RAY DIFFRACTION13( CHAIN B AND ( RESID 69:76 OR RESID 101:101 ) )B69 - 76
14X-RAY DIFFRACTION13( CHAIN B AND ( RESID 69:76 OR RESID 101:101 ) )B101
15X-RAY DIFFRACTION14( CHAIN C AND RESID 11:545 )C11 - 545
16X-RAY DIFFRACTION15( CHAIN C AND RESID 546:909 )C546 - 909
17X-RAY DIFFRACTION16( CHAIN C AND RESID 910:1024 )C910 - 1024
18X-RAY DIFFRACTION17( CHAIN D AND RESID 0:7 )D0 - 7
19X-RAY DIFFRACTION18( CHAIN D AND RESID 8:16 )D8 - 16
20X-RAY DIFFRACTION19( CHAIN D AND RESID 17:22 )D17 - 22
21X-RAY DIFFRACTION20( CHAIN D AND RESID 23:34 )D23 - 34
22X-RAY DIFFRACTION21( CHAIN D AND RESID 35:55 )D35 - 55
23X-RAY DIFFRACTION22( CHAIN D AND RESID 56:65 )D56 - 65
24X-RAY DIFFRACTION23( CHAIN D AND ( RESID 66:76 OR RESID 101:101 ) )D66 - 76
25X-RAY DIFFRACTION23( CHAIN D AND ( RESID 66:76 OR RESID 101:101 ) )D101
26X-RAY DIFFRACTION24( CHAIN E AND RESID 0:11 )E0 - 11
27X-RAY DIFFRACTION25( CHAIN E AND RESID 12:17 )E12 - 17
28X-RAY DIFFRACTION26( CHAIN E AND RESID 18:22 )E18 - 22
29X-RAY DIFFRACTION27( CHAIN E AND RESID 23:34 )E23 - 34
30X-RAY DIFFRACTION28( CHAIN E AND RESID 35:44 )E35 - 44
31X-RAY DIFFRACTION29( CHAIN E AND RESID 45:56 )E45 - 56
32X-RAY DIFFRACTION30( CHAIN E AND RESID 57:65 )E57 - 65
33X-RAY DIFFRACTION31( CHAIN E AND RESID 66:71 )E66 - 71
34X-RAY DIFFRACTION32( CHAIN E AND RESID 72:76 )E72 - 76

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