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- PDB-4f52: Structure of a Glomulin-RBX1-CUL1 complex -

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Open data


ID or keywords:

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Basic information

Entry
Database: PDB / ID: 4f52
TitleStructure of a Glomulin-RBX1-CUL1 complex
Components
  • Cullin-1
  • E3 ubiquitin-protein ligase RBX1
  • Glomulin
KeywordsCell Cycle/Ligase/Signaling Protein / Cullin-RING E3 Ligase / Inhibitor / Cell Cycle-Ligase-Signaling Protein complex
Function / homology
Function and homology information


hepatocyte growth factor receptor binding / ubiquitin-protein transferase inhibitor activity / Parkin-FBXW7-Cul1 ubiquitin ligase complex / muscle cell differentiation / regulation of proteasomal ubiquitin-dependent protein catabolic process / negative regulation of beige fat cell differentiation / cullin-RING-type E3 NEDD8 transferase / NEDD8 transferase activity / cullin-RING ubiquitin ligase complex / negative regulation of mitophagy ...hepatocyte growth factor receptor binding / ubiquitin-protein transferase inhibitor activity / Parkin-FBXW7-Cul1 ubiquitin ligase complex / muscle cell differentiation / regulation of proteasomal ubiquitin-dependent protein catabolic process / negative regulation of beige fat cell differentiation / cullin-RING-type E3 NEDD8 transferase / NEDD8 transferase activity / cullin-RING ubiquitin ligase complex / negative regulation of mitophagy / regulation of xenophagy / cellular response to chemical stress / Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling / Cul7-RING ubiquitin ligase complex / regulation of cell cycle process / neural crest cell differentiation / RNA polymerase II transcription initiation surveillance / positive regulation of protein autoubiquitination / protein neddylation / regulation of BMP signaling pathway / NEDD8 ligase activity / regulation of mitophagy / negative regulation of response to oxidative stress / regulation of centrosome duplication / neural tube closure / protein K27-linked ubiquitination / positive regulation of cilium assembly / Cul5-RING ubiquitin ligase complex / ubiquitin-ubiquitin ligase activity / regulation of TOR signaling / ubiquitin-dependent protein catabolic process via the C-end degron rule pathway / Cul2-RING ubiquitin ligase complex / negative regulation of DNA-templated DNA replication / SCF ubiquitin ligase complex / regulation of DNA damage checkpoint / regulation of mitotic cytokinesis / negative regulation of type I interferon production / Cul3-RING ubiquitin ligase complex / regulation of miRNA-mediated gene silencing / SCF-dependent proteasomal ubiquitin-dependent protein catabolic process / regulation of natural killer cell activation / Prolactin receptor signaling / nucleotide-excision repair complex / Cul4-RING E3 ubiquitin ligase complex / regulation of cell cycle phase transition / regulation of stem cell population maintenance / vasculogenesis / ubiquitin ligase complex scaffold activity / negative regulation of adipose tissue development / Cul4B-RING E3 ubiquitin ligase complex / regulation of cellular response to stress / positive regulation of phosphorylation / limb development / Cul4A-RING E3 ubiquitin ligase complex / negative regulation of T cell proliferation / protein monoubiquitination / cullin family protein binding / centrosome duplication / regulation of DNA-templated DNA replication initiation / cilium assembly / intrinsic apoptotic signaling pathway / ribosome-associated ubiquitin-dependent protein catabolic process / positive regulation of interleukin-2 production / negative regulation of insulin receptor signaling pathway / signal transduction in response to DNA damage / protein K63-linked ubiquitination / Nuclear events stimulated by ALK signaling in cancer / regulation of cellular response to insulin stimulus / protein K48-linked ubiquitination / post-translational protein modification / positive regulation of TORC1 signaling / transcription-coupled nucleotide-excision repair / regulation of embryonic development / replication fork processing / cellular response to amino acid stimulus / regulation of mitotic cell cycle / negative regulation of canonical NF-kappaB signal transduction / positive regulation of cytokine production / negative regulation of canonical Wnt signaling pathway / Regulation of BACH1 activity / T cell activation / MAP3K8 (TPL2)-dependent MAPK1/3 activation / site of DNA damage / G1/S transition of mitotic cell cycle / protein processing / epigenetic regulation of gene expression / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / Dectin-1 mediated noncanonical NF-kB signaling / Degradation of DVL / Degradation of CRY and PER proteins / negative regulation of smoothened signaling pathway / nucleotide-excision repair / Iron uptake and transport / regulation of autophagy / Activation of NF-kappaB in B cells / Degradation of GLI1 by the proteasome / Recognition of DNA damage by PCNA-containing replication complex / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / Negative regulation of NOTCH4 signaling
Similarity search - Function
YAP-binding/ALF4/Glomulin / Glomulin/ALF4 / Uncharacterised protein family, YAP/Alf4/glomulin / Cullin; Chain C, Domain 2 / Cullin Repeats / 5 helical Cullin repeat like / Zinc finger, RING-H2-type / RING-H2 zinc finger domain / : / Cullin protein neddylation domain ...YAP-binding/ALF4/Glomulin / Glomulin/ALF4 / Uncharacterised protein family, YAP/Alf4/glomulin / Cullin; Chain C, Domain 2 / Cullin Repeats / 5 helical Cullin repeat like / Zinc finger, RING-H2-type / RING-H2 zinc finger domain / : / Cullin protein neddylation domain / Cullin, conserved site / Cullin family signature. / Cullin, N-terminal / Cullin repeat-like-containing domain superfamily / Cullin protein, neddylation domain / Cullin / Cullin protein neddylation domain / Cullin alpha solenoid domain / Cullin / : / Cullin alpha+beta domain / Cullin homology domain / Cullin homology domain superfamily / Cullin family profile. / Zinc/RING finger domain, C3HC4 (zinc finger) / Herpes Virus-1 / Ribosomal Protein S5; domain 2 / Zinc finger RING-type profile. / Zinc finger, RING-type / Zinc finger, RING/FYVE/PHD-type / Winged helix DNA-binding domain superfamily / Winged helix-like DNA-binding domain superfamily / Up-down Bundle / 2-Layer Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
E3 ubiquitin-protein ligase RBX1 / Cullin-1 / Glomulin
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 3 Å
AuthorsDuda, D.M. / Olszewski, J.L. / Schulman, B.A.
CitationJournal: Mol.Cell / Year: 2012
Title: Structure of a Glomulin-RBX1-CUL1 Complex: Inhibition of a RING E3 Ligase through Masking of Its E2-Binding Surface.
Authors: Duda, D.M. / Olszewski, J.L. / Tron, A.E. / Hammel, M. / Lambert, L.J. / Waddell, M.B. / Mittag, T. / Decaprio, J.A. / Schulman, B.A.
History
DepositionMay 11, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 19, 2012Provider: repository / Type: Initial release
Revision 1.1Feb 28, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / 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 / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _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_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Cullin-1
B: E3 ubiquitin-protein ligase RBX1
C: Cullin-1
D: E3 ubiquitin-protein ligase RBX1
E: Glomulin
F: Glomulin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)226,36212
Polymers225,9706
Non-polymers3926
Water00
1
A: Cullin-1
B: E3 ubiquitin-protein ligase RBX1
E: Glomulin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)113,1816
Polymers112,9853
Non-polymers1963
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7900 Å2
ΔGint-25 kcal/mol
Surface area43300 Å2
MethodPISA
2
C: Cullin-1
D: E3 ubiquitin-protein ligase RBX1
F: Glomulin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)113,1816
Polymers112,9853
Non-polymers1963
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7700 Å2
ΔGint-33 kcal/mol
Surface area41930 Å2
MethodPISA
Unit cell
Length a, b, c (Å)53.333, 193.932, 142.075
Angle α, β, γ (deg.)90.00, 98.81, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein Cullin-1 / CUL-1


Mass: 32470.072 Da / Num. of mol.: 2
Fragment: C-terminal domain, delta WHB domain, UNP residues 411-690
Mutation: L421E, V451E, V452K, Y455K
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CUL1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q13616
#2: Protein E3 ubiquitin-protein ligase RBX1 / Protein ZYP / RING finger protein 75 / RING-box protein 1 / Rbx1 / Regulator of cullins 1


Mass: 12089.677 Da / Num. of mol.: 2 / Fragment: UNP residues 5-108
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RBX1, RNF75, ROC1 / Production host: Escherichia coli (E. coli)
References: UniProt: P62877, Ligases; Forming carbon-nitrogen bonds; Acid-amino-acid ligases (peptide synthases)
#3: Protein Glomulin / FK506-binding protein-associated protein / FAP / FKBP-associated protein


Mass: 68425.125 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: GLMN, FAP48, FAP68, VMGLOM / Production host: Escherichia coli (E. coli) / References: UniProt: Q92990
#4: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Zn

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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: 3.21 Å3/Da / Density % sol: 61.72 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 18-21% PEG3350, 0.3-0.45M ammonium citrate, 10mM DTT, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.97949 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Jun 22, 2011
RadiationMonochromator: Cryo-cooled double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97949 Å / Relative weight: 1
ReflectionResolution: 3→50 Å / Num. obs: 56830 / % possible obs: 99.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0
Reflection shellResolution: 3→3.11 Å / % possible all: 99.1

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHENIX(phenix.autosol)model building
PHENIX(phenix.refine: 1.7.1_743)refinement
HKL-2000data reduction
HKL-2000data scaling
PHENIXphasing
RefinementMethod to determine structure: SAD / Resolution: 3→37.39 Å / SU ML: 1.15 / σ(F): 0 / Phase error: 33.11 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.289 2831 5.04 %
Rwork0.219 --
obs0.222 56192 98.8 %
all-56192 -
Solvent computationShrinkage radii: 0.83 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 74.26 Å2 / ksol: 0.32 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--8.4955 Å20 Å2-4.0719 Å2
2--23.2586 Å20 Å2
3----14.7631 Å2
Refinement stepCycle: LAST / Resolution: 3→37.39 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13891 0 6 0 13897
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0114154
X-RAY DIFFRACTIONf_angle_d1.30619089
X-RAY DIFFRACTIONf_dihedral_angle_d20.9195322
X-RAY DIFFRACTIONf_chiral_restr0.0852198
X-RAY DIFFRACTIONf_plane_restr0.0052389
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3-3.05280.47011360.37392526X-RAY DIFFRACTION95
3.0528-3.10830.38311270.3482705X-RAY DIFFRACTION99
3.1083-3.16810.42531560.33262651X-RAY DIFFRACTION99
3.1681-3.23270.39681410.32282666X-RAY DIFFRACTION100
3.2327-3.3030.38421520.28592706X-RAY DIFFRACTION99
3.303-3.37970.381460.26062627X-RAY DIFFRACTION99
3.3797-3.46420.34251480.24592656X-RAY DIFFRACTION100
3.4642-3.55780.32221340.23062710X-RAY DIFFRACTION99
3.5578-3.66240.31251260.23352683X-RAY DIFFRACTION100
3.6624-3.78050.30131360.22722695X-RAY DIFFRACTION99
3.7805-3.91550.27951460.2192635X-RAY DIFFRACTION99
3.9155-4.07210.29381410.21012723X-RAY DIFFRACTION99
4.0721-4.25720.29651330.20092655X-RAY DIFFRACTION99
4.2572-4.48130.27831420.17922712X-RAY DIFFRACTION99
4.4813-4.76150.21671640.16822638X-RAY DIFFRACTION100
4.7615-5.12830.27711350.17942699X-RAY DIFFRACTION99
5.1283-5.64280.27711280.22962683X-RAY DIFFRACTION99
5.6428-6.45570.2991370.24342711X-RAY DIFFRACTION99
6.4557-8.11980.26231340.2122668X-RAY DIFFRACTION98
8.1198-37.3860.24491690.18972612X-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)
17.61564.23052.87784.75123.51376.71080.56530.4054-1.58211.58580.32920.15831.8941-0.3112-0.47851.57460.0364-0.24660.65480.15161.2022-4.9977-59.33834.8443
27.75863.638-0.53929.23030.03223.84470.4023-0.1184-1.5386-0.36370.2808-0.16291.20520.0719-0.55680.76060.1298-0.3150.58580.13350.49484.1855-43.93311.0378
30.1997-0.7448-0.30676.85523.10958.64970.23250.35940.2756-0.577-0.5297-0.1568-0.6263-0.38680.24250.48230.00770.04640.38730.09030.47274.8633-26.98867.0144
44.16620.6908-2.22972.92340.09276.28320.17360.22950.06470.0424-0.0491-0.0489-0.62360.2518-0.06480.23560.0442-0.00510.47430.08080.4394-0.0512-24.587818.5534
57.80920.0612-1.21915.39730.01086.01690.5609-0.631-0.20780.4465-0.6360.50770.2173-1.02890.03860.430.02620.05760.73430.11750.3251-6.5907-28.431831.4491
63.2557-0.2122-0.75633.3871-0.06492.64390.25250.26970.16870.0408-0.510.03430.61530.60860.24120.2606-0.01360.12140.7234-0.00390.36284.8382-23.58353.292
75.5022-2.252-0.11856.59151.25093.1247-0.79451.65321.6296-0.4946-0.6631-0.41030.05270.26250.85750.87050.8302-0.04271.33290.83250.7921-2.5747-5.4228-20.063
84.4441-4.3956-4.13914.34294.08763.8513-1.36060.46181.2988-1.8247-0.0126-2.4109-1.86191.66781.60921.3729-0.2572-0.16130.93570.37251.6736-4.2915.5397-25.9785
99.31421.47631.89624.6655-1.87837.4680.52911.4440.6094-0.8602-1.0001-0.3809-0.41211.96310.18930.6255-0.00750.131.43810.51771.042110.2127-3.7935-18.1766
106.4248-4.28817.13764.6716-4.14428.1552-0.2372-1.12370.0398-0.3437-0.3225-0.8055-0.4581.52080.89190.80630.02960.0951.97810.41720.882317.7411-6.5326-18.7155
119.2548-5.0033-6.11595.9784.21938.0071-0.88230.15441.21690.36190.7864-0.55910.1233-0.5314-0.57661.2887-0.0426-0.17891.09220.18210.996321.8421-7.378266.2163
128.3097-6.77630.6969.40742.13181.67060.09580.27661.02870.12160.2625-0.4827-0.63520.0697-0.42881.21380.11010.1471.11470.13850.657329.0861-20.583570.8416
131.0863.1251.32929.33333.27064.7274-0.3723-0.7099-0.51650.64490.8230.04920.30190.8428-0.37560.60080.29040.0861.05610.15980.436634.5681-40.493266.0267
143.0655-0.0111.11594.5185-1.66143.624-0.1938-0.26710.36960.1690.3907-0.14240.7061.1791-0.10230.28650.2666-0.01181.14240.14030.263229.6801-42.324654.9165
155.91780.45590.99544.8463-0.17446.08150.2694-0.2011-0.0903-0.3185-0.13430.62010.0439-0.2307-0.14040.3727-0.0068-0.03580.77960.23430.36719.1994-40.738144.4833
160.62190.956-1.19362.1863-1.77492.95950.33710.36520.05290.7742-0.81240.446-1.0071-0.10790.21460.58170.3017-0.22751.5202-0.0487-0.377230.8003-43.012171.549
173.45154.0556-4.4528.8712-1.25249.25720.2178-1.0513-0.13410.8312-0.40830.139-0.15761.38950.42580.93780.1712-0.12120.90310.07480.675727.4586-60.241897.7184
186.84532.4245-0.39266.20384.85845.62480.0652-0.9603-0.48871.4266-0.4555-1.3903-0.1923-0.7740.28111.30370.6765-0.06911.14630.38610.962333.8591-65.02792.7091
197.0936.6133-1.06736.4923-2.35886.086-0.69751.1594-1.5912-1.50130.0027-0.90321.77752.82830.66370.91560.64950.10351.77860.17830.670940.239-63.45887.6148
204.95855.7297-5.07316.6324-5.86095.1843-0.5117-0.2232-0.71650.2174-0.5570.4545-1.17443.2161.10871.48950.2335-0.17731.65820.04440.610544.0394-58.071293.3824
216.21352.2252-1.8762.2497-0.27555.855-0.6525-2.2184-1.68681.2240.33250.1004-0.2858-0.0758-0.05441.02410.0774-0.1650.83890.63151.3801-7.2199-93.8273-12.3245
226.739-1.0274-0.14312.71551.59095.85920.02120.34280.0758-1.69430.10060.4903-0.04710.2750.08081.12920.1927-0.19320.38970.18931.0864-9.1781-83.8969-22.1501
236.562-1.706-0.36758.5738-0.86444.70480.38250.638-1.0363-0.2535-0.25520.61490.61590.0054-0.15820.73980.1358-0.16080.54320.00780.4714-19.3255-59.5612-23.1339
242.70331.94650.05594.60212.8582.8936-0.1508-0.17870.3493-0.3546-0.1360.7962-0.033-0.32090.33120.29830.14060.01490.4663-0.04370.3338-17.5458-24.9387-17.0549
257.9704-2.28623.40243.7348-1.30126.0035-0.4193-0.3241.2060.0585-0.19020.0574-0.38590.04630.53930.4044-0.10510.02380.2897-0.03710.70773.1063-5.7019-1.3375
261.37582.49440.02148.727-2.22412.5413-0.48620.28860.36180.58810.7660.1186-0.09010.3797-0.10791.1980.2081-0.20620.8982-0.00040.80998.560919.325189.1051
272.3331-0.64570.30122.5739-0.04632.9895-0.1661-0.42180.0103-0.33690.03980.0183-0.7292-0.26170.12471.5410.55070.121.00110.18670.56236.2815-8.981595.9794
283.0815-0.8019-1.53344.3231.34375.09970.27790.6010.0978-0.034-0.08130.3704-0.7908-1.3184-0.13380.59090.2865-0.070.688-0.07660.34598.7127-37.265290.7243
298.90570.87273.9854.36652.24282.56290.11532.4978-0.875-1.4319-0.50010.7386-0.9673-0.39530.25160.3763-0.1407-0.380.8742-0.13870.856913.998-57.504876.4892
307.36982.6703-3.26442.4547-1.82235.7227-0.59770.8968-1.1356-0.25490.1755-0.1751.09110.13450.44740.7670.2099-0.00590.666-0.23870.644929.4696-61.662377.0463
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(CHAIN A AND RESID 420:455 )
2X-RAY DIFFRACTION2(CHAIN A AND RESID 458:531 )
3X-RAY DIFFRACTION3(CHAIN A AND RESID 532:569 )
4X-RAY DIFFRACTION4(CHAIN A AND RESID 570:644 )
5X-RAY DIFFRACTION5(CHAIN A AND RESID 645:689 )
6X-RAY DIFFRACTION6(CHAIN B AND RESID 20:44 )
7X-RAY DIFFRACTION7(CHAIN B AND RESID 45:58 )
8X-RAY DIFFRACTION8(CHAIN B AND RESID 59:66 )
9X-RAY DIFFRACTION9(CHAIN B AND RESID 68:96 )
10X-RAY DIFFRACTION10(CHAIN B AND RESID 97:104 )
11X-RAY DIFFRACTION11(CHAIN C AND RESID 419:456 )
12X-RAY DIFFRACTION12(CHAIN C AND RESID 461:522 )
13X-RAY DIFFRACTION13(CHAIN C AND RESID 523:569 )
14X-RAY DIFFRACTION14(CHAIN C AND RESID 570:624 )
15X-RAY DIFFRACTION15(CHAIN C AND RESID 625:688 )
16X-RAY DIFFRACTION16(CHAIN D AND RESID 21:45 )
17X-RAY DIFFRACTION17(CHAIN D AND RESID 46:80 )
18X-RAY DIFFRACTION18(CHAIN D AND RESID 81:87 )
19X-RAY DIFFRACTION19(CHAIN D AND RESID 88:96 )
20X-RAY DIFFRACTION20(CHAIN D AND RESID 97:104 )
21X-RAY DIFFRACTION21(CHAIN E AND RESID 1:38 )
22X-RAY DIFFRACTION22(CHAIN E AND RESID 39:110 )
23X-RAY DIFFRACTION23(CHAIN E AND RESID 111:284 )
24X-RAY DIFFRACTION24(CHAIN E AND RESID 285:452 )
25X-RAY DIFFRACTION25(CHAIN E AND RESID 453:583 )
26X-RAY DIFFRACTION26(CHAIN F AND RESID 1:143 )
27X-RAY DIFFRACTION27(CHAIN F AND RESID 144:259 )
28X-RAY DIFFRACTION28(CHAIN F AND RESID 279:432 )
29X-RAY DIFFRACTION29(CHAIN F AND RESID 439:464 )
30X-RAY DIFFRACTION30(CHAIN F AND RESID 465:583 )

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