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- PDB-3zng: Ankyrin repeat and SOCS-box protein 9 (ASB9) in complex with Elon... -

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Basic information

Entry
Database: PDB / ID: 3zng
TitleAnkyrin repeat and SOCS-box protein 9 (ASB9) in complex with ElonginB and ElonginC
Components
  • ANKYRIN REPEAT AND SOCS BOX PROTEIN 9
  • TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 1
  • TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 2
KeywordsTRANSCRIPTION / CULLIN-RING LIGASE
Function / homology
Function and homology information


target-directed miRNA degradation / elongin complex / VCB complex / Cul5-RING ubiquitin ligase complex / Cul2-RING ubiquitin ligase complex / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / Tat-mediated elongation of the HIV-1 transcript ...target-directed miRNA degradation / elongin complex / VCB complex / Cul5-RING ubiquitin ligase complex / Cul2-RING ubiquitin ligase complex / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / Formation of HIV elongation complex in the absence of HIV Tat / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / RNA Polymerase II Pre-transcription Events / transcription corepressor binding / transcription initiation at RNA polymerase II promoter / TP53 Regulates Transcription of DNA Repair Genes / transcription elongation by RNA polymerase II / Vif-mediated degradation of APOBEC3G / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / Inactivation of CSF3 (G-CSF) signaling / Evasion by RSV of host interferon responses / Regulation of expression of SLITs and ROBOs / positive regulation of protein catabolic process / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Antigen processing: Ubiquitination & Proteasome degradation / Neddylation / protein-macromolecule adaptor activity / ubiquitin-dependent protein catabolic process / protein-containing complex assembly / intracellular signal transduction / protein ubiquitination / ubiquitin protein ligase binding / regulation of transcription by RNA polymerase II / mitochondrion / nucleoplasm / cytosol
Similarity search - Function
: / Ankyrin repeat and SOCS box protein 9/11, SOCS box domain / SOCS box / SOCS box / SOCS box-like domain superfamily / SOCS box domain / SOCS box domain profile. / SOCS_box / Elongin C; Chain C, domain 1 / Elongin B ...: / Ankyrin repeat and SOCS box protein 9/11, SOCS box domain / SOCS box / SOCS box / SOCS box-like domain superfamily / SOCS box domain / SOCS box domain profile. / SOCS_box / Elongin C; Chain C, domain 1 / Elongin B / Elongin-C / Potassium Channel Kv1.1; Chain A / Potassium Channel Kv1.1; Chain A / Ankyrin repeat-containing domain / S-phase kinase-associated protein 1-like / SKP1 component, POZ domain / Skp1 family, tetramerisation domain / Found in Skp1 protein family / SKP1/BTB/POZ domain superfamily / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / Ankyrin repeats (3 copies) / Ankyrin repeat profile. / Ankyrin repeat region circular profile. / ankyrin repeats / Ankyrin repeat / Ankyrin repeat-containing domain superfamily / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Ubiquitin-like (UB roll) / Alpha Horseshoe / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Ubiquitin-like domain superfamily / Roll / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Elongin-C / Elongin-B / Ankyrin repeat and SOCS box protein 9
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.85 Å
AuthorsThomas, J. / Van Molle, I. / Ciulli, A.
CitationJournal: Biochemistry / Year: 2013
Title: Multimeric Complexes Among Ankyrin-Repeat and Socs-Box Protein 9 (Asb9), Elonginbc, and Cullin 5: Insights Into the Structure and Assembly of Ecs-Type Cullin-Ring E3 Ubiquitin Ligases.
Authors: Thomas, J.C. / Matak-Vinkovic, D. / Van Molle, I. / Ciulli, A.
History
DepositionFeb 14, 2013Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 4, 2013Provider: repository / Type: Initial release
Revision 1.1Dec 25, 2013Group: Database references / Source and taxonomy
Revision 1.2Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _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: ANKYRIN REPEAT AND SOCS BOX PROTEIN 9
B: TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 1
C: TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 2
D: ANKYRIN REPEAT AND SOCS BOX PROTEIN 9
E: TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 1
F: TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)107,1587
Polymers107,0966
Non-polymers621
Water63135
1
A: ANKYRIN REPEAT AND SOCS BOX PROTEIN 9
B: TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 1
C: TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)53,6104
Polymers53,5483
Non-polymers621
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4290 Å2
ΔGint-45.4 kcal/mol
Surface area20210 Å2
MethodPISA
2
D: ANKYRIN REPEAT AND SOCS BOX PROTEIN 9
E: TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 1
F: TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 2


Theoretical massNumber of molelcules
Total (without water)53,5483
Polymers53,5483
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4350 Å2
ΔGint-43.4 kcal/mol
Surface area20490 Å2
MethodPISA
Unit cell
Length a, b, c (Å)114.110, 103.130, 109.900
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212

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Components

#1: Protein ANKYRIN REPEAT AND SOCS BOX PROTEIN 9 / ASB-9 / ASB9


Mass: 29425.727 Da / Num. of mol.: 2 / Fragment: RESIDUES 35-294
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q96DX5
#2: Protein TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 1 / ELONGIN 15 KDA SUBUNIT / ELONGIN-C / ELOC / RNA POLYMERASE II TRANSCRIPTION FACTOR SIII SUBUNIT C / ...ELONGIN 15 KDA SUBUNIT / ELONGIN-C / ELOC / RNA POLYMERASE II TRANSCRIPTION FACTOR SIII SUBUNIT C / SIII P15 / ELONGINC


Mass: 10974.616 Da / Num. of mol.: 2 / Fragment: RESIDUES 17-112
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q15369
#3: Protein TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 2 / ELONGIN 18 KDA SUBUNIT / ELONGIN-B / ELOB / RNA POLYMERASE II TRANSCRIPTION FACTOR SIII SUBUNIT B / ...ELONGIN 18 KDA SUBUNIT / ELONGIN-B / ELOB / RNA POLYMERASE II TRANSCRIPTION FACTOR SIII SUBUNIT B / SIII P18 / ELONGINB


Mass: 13147.781 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q15370
#4: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6O2
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 35 / Source method: isolated from a natural source / Formula: H2O
Sequence detailsRESIDUES 34-294 ONLY. SEQUENCE CONTAINS ADDITIONAL RESIDUES AENLYFQ AT C-TERMINUS LEFT OVER FROM ...RESIDUES 34-294 ONLY. SEQUENCE CONTAINS ADDITIONAL RESIDUES AENLYFQ AT C-TERMINUS LEFT OVER FROM CLEAVAGE OF HIS6 AND FLAG TAGS RESIDUES 17-112 ONLY. SEQUENCE CONTAINS ADDITIONAL M RESIDUE AT N-TERMINUS.

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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: 3.05 Å3/Da / Density % sol: 59.7 % / Description: NONE
Crystal growDetails: 0.1 M BIS-TRIS PROPANE, PH 6.7, 0.2 M SODIUM MALONATE, 22% PEG 3350, 10% ETHYLENE GLYCOL

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I24 / Wavelength: 0.97879
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Sep 22, 2012 / Details: MIRRORS
RadiationMonochromator: DOUBLE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97879 Å / Relative weight: 1
ReflectionResolution: 2.85→50.64 Å / Num. obs: 30887 / % possible obs: 99.8 % / Observed criterion σ(I): 3 / Redundancy: 11.4 % / Biso Wilson estimate: 72.51 Å2 / Rmerge(I) obs: 0.12 / Net I/σ(I): 14.2
Reflection shellResolution: 2.85→2.92 Å / Redundancy: 10.7 % / Rmerge(I) obs: 0.91 / Mean I/σ(I) obs: 2.8 / % possible all: 99.6

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 3ZKJ

3zkj


Resolution: 2.85→50.638 Å / SU ML: 0.37 / σ(F): 1.33 / Phase error: 26.14 / Stereochemistry target values: MLHL
RfactorNum. reflection% reflection
Rfree0.2416 1549 5.1 %
Rwork0.1946 --
obs0.1969 30665 99.09 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.85→50.638 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6468 0 4 35 6507
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0096634
X-RAY DIFFRACTIONf_angle_d1.1859026
X-RAY DIFFRACTIONf_dihedral_angle_d14.0342374
X-RAY DIFFRACTIONf_chiral_restr0.0631045
X-RAY DIFFRACTIONf_plane_restr0.0081173
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.8501-2.94210.32381260.30732580X-RAY DIFFRACTION98
2.9421-3.04720.41051150.28032628X-RAY DIFFRACTION98
3.0472-3.16920.35061440.27732575X-RAY DIFFRACTION99
3.1692-3.31340.29041400.2532589X-RAY DIFFRACTION99
3.3134-3.48810.27161510.21522617X-RAY DIFFRACTION99
3.4881-3.70660.25961420.19642630X-RAY DIFFRACTION99
3.7066-3.99260.27811300.17812645X-RAY DIFFRACTION100
3.9926-4.39420.20841500.15722664X-RAY DIFFRACTION99
4.3942-5.02960.19661480.15112646X-RAY DIFFRACTION100
5.0296-6.33480.23821510.19482713X-RAY DIFFRACTION100
6.3348-50.64570.20071520.18832829X-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)
12.833-0.72322.15832.8498-0.58485.00580.0171-0.1620.0195-0.0496-0.2570.5296-0.0642-0.24980.20320.3648-0.0497-0.13550.4521-0.00280.7096-53.44122.2767-9.0556
24.1702-0.88652.48982.07710.19851.7687-0.0937-0.23670.03330.0692-0.2335-0.0128-0.42030.44140.18750.384-0.0858-0.07550.5020.04970.6359-44.221921.21592.8723
32.9652-2.22312.08315.7905-1.32073.3733-0.0456-0.2047-0.2780.35820.10310.58520.2738-0.3036-0.04620.457-0.05280.09130.38310.06320.5165-35.206110.61913.7568
44.73790.9670.57794.62711.03562.0283-0.4055-0.2795-0.47980.07020.2309-0.02860.5343-0.34170.15490.5437-0.03360.13870.40790.04710.3697-22.607311.698921.5695
54.7391.68191.53030.811.64416.2518-0.0879-1.32180.18590.4904-0.4113-0.54760.38840.20930.58190.69950.1115-0.24340.73050.13930.9099-0.497214.868539.3285
67.786-8.3303-0.42189.6062-0.70252.0219-0.49040.0082-0.27650.26690.16360.29160.5420.6611-0.08850.6090.00380.11810.67580.16220.68061.50649.447229.074
74.3714-3.68270.41074.4369-1.6641.36130.1861-0.40960.29670.6111-0.0336-1.52480.29941.24280.26090.65450.0721-0.38580.94660.04250.88873.368819.000933.2326
84.11041.0888-0.91512.246-2.1874.3109-0.2023-0.9213-0.82590.39650.06680.0762-0.4864-0.11160.06280.57740.1166-0.10010.60780.21460.7095-10.180514.508236.2605
93.9814-0.60280.840.2826-0.09280.6252-0.4348-0.746-1.99910.86350.62731.3510.0554-0.6065-0.44460.8170.16320.19420.78730.43061.0041-20.1468.516135.9816
109.7784-2.93050.82698.0804-2.766810.0033-0.49610.2258-0.60550.7166-0.0671-0.7107-0.41240.2360.27610.34580.0286-0.05150.42580.04160.5241-9.524919.826726.9593
113.26040.32331.99322.35411.46632.2335-0.4145-0.4382-0.40251.36760.45810.3514-0.2129-1.0761-0.31511.30920.4767-0.31871.07820.18640.5608-7.869914.461949.3557
122.5856-1.08580.52843.0505-1.1991.338-0.3743-0.9583-0.46630.619-0.0299-0.62160.70671.01810.26381.91280.6971-0.57361.11740.11180.5543-1.935110.384256.5866
133.1767-0.95952.26881.5141-1.29452.81620.1048-0.1293-0.29160.7498-0.0732-0.42930.65591.39041.12891.43770.0596-0.38381.56970.87380.18651.123915.341659.1659
140.3827-0.7432-0.45871.4951.36245.0747-0.4814-0.8345-0.0970.7932-0.90940.7110.3177-0.20040.09721.1260.26590.0571.38430.15990.6461-16.167816.195150.1331
153.61520.45771.75813.26450.22725.7072-0.2395-0.37150.20270.47770.4046-0.4175-1.4253-0.33260.1510.89140.0762-0.11860.6864-0.12250.8192-14.618831.300331.5691
163.8846-3.1371-2.00266.1339-3.55618.47260.00040.1416-1.4368-0.1734-0.04050.89190.4648-1.34990.27350.47390.006-0.23990.5345-0.15180.8093-24.1475-12.08975.7633
173.2120.49851.33212.7134-0.63025.60520.06630.199-0.1352-0.03510.0417-0.21580.0270.1345-0.17680.51320.0726-0.07970.3933-0.04050.5554-19.1143-5.3774-3.3019
184.3749-0.90270.75844.152-1.2161.4922-0.03980.2612-0.1879-0.4122-0.0050.33420.05630.18860.05490.69710.0688-0.07770.7253-0.07730.4495-32.85429.0614-23.2093
192.41320.5181-1.23751.8392-1.53481.5890.2535-0.0310.0195-0.3104-0.0492-0.0866-0.2991-0.0356-0.1850.85470.02170.01450.7566-0.11490.4075-30.072523.3788-28.8212
201.9777-0.80220.96722.3012-1.05192.29180.7492-0.44270.4164-1.0153-0.5406-0.6236-1.0829-0.3021-0.25091.69630.0780.14170.8654-0.17970.5242-28.533639.2129-51.6363
213.5357-0.7988-0.29613.01050.19790.0686-0.0122-0.67170.04470.03840.1835-0.3815-1.2884-0.6639-0.04481.47830.04140.12910.871-0.16630.3868-28.526735.7977-45.5463
223.0899-1.3529-2.88782.7289-0.0194.36530.28660.2584-0.0122-0.2021-0.11170.3495-0.4288-1.73950.24641.0764-0.00930.08671.4977-0.33990.3407-33.311420.6914-44.9037
233.4312-2.0012.22127.5785-2.25584.0239-0.6522-0.1062-0.10910.60040.03690.1815-0.9344-0.13130.59181.3669-0.10340.15750.8645-0.16990.5575-23.351433.1858-36.9103
246.70846.147-1.25899.6456-1.30383.81110.9508-0.64060.43351.0693-0.47360.1352-1.4325-1.0642-0.28751.10390.17420.07010.8582-0.1070.4509-25.536629.4394-58.9916
251.6685-0.98421.29233.45592.0253.7525-0.2712-0.6250.637-0.20340.5830.0897-0.927-0.9294-0.2151.59230.12780.09150.67760.00350.4383-24.339634.6327-57.9076
263.40420.4365-0.90913.61930.46921.57310.49840.84730.0573-0.4815-0.44790.1916-1.7298-2.1486-0.07671.38010.42510.06010.9778-0.08880.4963-27.42133.3007-69.5772
272.00823.00570.65419.09240.08076.40910.2902-0.7950.3490.4753-0.0138-0.7241-0.46050.4263-0.44410.64060.01190.09160.8849-0.220.5938-19.56324.4121-70.3637
284.2278-1.69590.23841.62650.97811.23620.2247-0.0118-0.48850.1975-0.68920.23530.5707-1.0819-0.12030.6624-0.05850.03740.7058-0.05380.3832-27.515118.803-64.3715
297.2452-1.3837-6.272.3301-0.39398.6076-0.0366-1.2867-0.74761.19750.51590.29760.3663-0.4095-0.29130.93770.15650.15851.04230.01730.5861-27.232921.839-53.1564
301.4332-0.179-1.53180.8417-0.54252.29180.5612-0.33270.5116-0.42030.0369-0.2522-0.71550.3650.53171.7628-0.07890.38710.6453-0.20730.1715-20.107832.4518-64.2
311.692.43462.56563.79163.93594.43570.1645-1.22151.0383-1.3873-0.59640.6674-2.68230.66520.87731.85-0.01350.13171.07440.01340.6989-13.522138.6698-71.2663
321.3210.55241.66890.76951.8344.50340.0453-0.07310.4386-0.18990.0305-0.0959-1.62260.2275-0.17911.6241-0.20760.18051.1269-0.18970.3076-13.282134.6019-53.328
333.77291.00780.39065.62891.11183.8195-0.11110.0105-0.08030.04180.14050.3624-0.24771.1898-0.01870.7805-0.06290.02920.9955-0.05620.6758-10.416925.0519-33.7316
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A AND (RESID 37 THROUGH 104 )
2X-RAY DIFFRACTION2CHAIN A AND (RESID 105 THROUGH 136 )
3X-RAY DIFFRACTION3CHAIN A AND (RESID 137 THROUGH 220 )
4X-RAY DIFFRACTION4CHAIN A AND (RESID 221 THROUGH 294 )
5X-RAY DIFFRACTION5CHAIN B AND (RESID 18 THROUGH 38 )
6X-RAY DIFFRACTION6CHAIN B AND (RESID 39 THROUGH 45 )
7X-RAY DIFFRACTION7CHAIN B AND (RESID 46 THROUGH 66 )
8X-RAY DIFFRACTION8CHAIN B AND (RESID 67 THROUGH 82 )
9X-RAY DIFFRACTION9CHAIN B AND (RESID 83 THROUGH 96 )
10X-RAY DIFFRACTION10CHAIN B AND (RESID 97 THROUGH 112 )
11X-RAY DIFFRACTION11CHAIN C AND (RESID 2 THROUGH 23 )
12X-RAY DIFFRACTION12CHAIN C AND (RESID 24 THROUGH 35 )
13X-RAY DIFFRACTION13CHAIN C AND (RESID 36 THROUGH 46 )
14X-RAY DIFFRACTION14CHAIN C AND (RESID 47 THROUGH 75 )
15X-RAY DIFFRACTION15CHAIN C AND (RESID 91 THROUGH 105 )
16X-RAY DIFFRACTION16CHAIN D AND (RESID 36 THROUGH 48 )
17X-RAY DIFFRACTION17CHAIN D AND (RESID 49 THROUGH 136 )
18X-RAY DIFFRACTION18CHAIN D AND (RESID 137 THROUGH 234 )
19X-RAY DIFFRACTION19CHAIN D AND (RESID 235 THROUGH 294 )
20X-RAY DIFFRACTION20CHAIN E AND (RESID 18 THROUGH 38 )
21X-RAY DIFFRACTION21CHAIN E AND (RESID 39 THROUGH 83 )
22X-RAY DIFFRACTION22CHAIN E AND (RESID 84 THROUGH 96 )
23X-RAY DIFFRACTION23CHAIN E AND (RESID 97 THROUGH 112 )
24X-RAY DIFFRACTION24CHAIN F AND (RESID 2 THROUGH 9 )
25X-RAY DIFFRACTION25CHAIN F AND (RESID 10 THROUGH 18 )
26X-RAY DIFFRACTION26CHAIN F AND (RESID 19 THROUGH 45 )
27X-RAY DIFFRACTION27CHAIN F AND (RESID 46 THROUGH 55 )
28X-RAY DIFFRACTION28CHAIN F AND (RESID 56 THROUGH 65 )
29X-RAY DIFFRACTION29CHAIN F AND (RESID 66 THROUGH 72 )
30X-RAY DIFFRACTION30CHAIN F AND (RESID 73 THROUGH 79 )
31X-RAY DIFFRACTION31CHAIN F AND (RESID 80 THROUGH 89 )
32X-RAY DIFFRACTION32CHAIN F AND (RESID 90 THROUGH 94 )
33X-RAY DIFFRACTION33CHAIN F AND (RESID 95 THROUGH 106 )

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