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- PDB-4aca: CRYSTAL STRUCTURE OF TRANSLATION ELONGATION FACTOR SELB FROM METH... -

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Basic information

Entry
Database: PDB / ID: 4aca
TitleCRYSTAL STRUCTURE OF TRANSLATION ELONGATION FACTOR SELB FROM METHANOCOCCUS MARIPALUDIS, APO FORM
ComponentsTRANSLATION ELONGATION FACTOR SELB
KeywordsTRANSLATION / SELENOCYSTEINE / SECIS ELEMENT / EF-SEC / SEC-TRNA(SEC)
Function / homology
Function and homology information


selenocysteine incorporation / translation elongation factor activity / GTPase activity / GTP binding / RNA binding / metal ion binding / cytoplasm
Similarity search - Function
: / Archaeal selenocysteine-specific elongation factor, domain III / translation elongation factor selb, chain A, domain 4 / Translation elongation factor, selenocysteine-specific / : / Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal / Translation factors / Translation elongation factor EFTu-like, domain 2 / Elongation factor Tu domain 2 / Elongation Factor Tu (Ef-tu); domain 3 ...: / Archaeal selenocysteine-specific elongation factor, domain III / translation elongation factor selb, chain A, domain 4 / Translation elongation factor, selenocysteine-specific / : / Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal / Translation factors / Translation elongation factor EFTu-like, domain 2 / Elongation factor Tu domain 2 / Elongation Factor Tu (Ef-tu); domain 3 / Ribosomal protein L35A superfamily / Translational (tr)-type GTP-binding domain / Elongation factor Tu GTP binding domain / Translational (tr)-type guanine nucleotide-binding (G) domain profile. / Small GTP-binding protein domain / Thrombin, subunit H / Translation protein, beta-barrel domain superfamily / P-loop containing nucleotide triphosphate hydrolases / Beta Barrel / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
GUANOSINE-5'-MONOPHOSPHATE / Selenocysteine-specific elongation factor
Similarity search - Component
Biological speciesMETHANOCOCCUS MARIPALUDIS (archaea)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 3.15 Å
AuthorsLeibundgut, M. / Frick, C. / Thanbichler, M. / Boeck, A. / Ban, N.
CitationJournal: Embo J. / Year: 2005
Title: Selenocysteine tRNA-Specific Elongation Factor Selb is a Structural Chimaera of Elongation and Initiation Factors.
Authors: Leibundgut, M. / Frick, C. / Thanbichler, M. / Bock, A. / Ban, N.
History
DepositionDec 14, 2011Deposition site: PDBE / Processing site: PDBE
SupersessionNov 7, 2012ID: 1WB2
Revision 1.0Nov 7, 2012Provider: repository / Type: Initial release
Revision 1.1Dec 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_conn / struct_sheet / 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_conn.conn_type_id / _struct_conn.id / _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_sheet.number_strands / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.2Oct 16, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature
Remark 700 SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AF" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AF" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "AG" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BB" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN -7-STRANDED BARREL THIS IS REPRESENTED BY A -6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BD" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN -3-STRANDED BARREL THIS IS REPRESENTED BY A -2-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "CB" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN -1-STRANDED BARREL THIS IS REPRESENTED BY A 0-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "CD" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN -3-STRANDED BARREL THIS IS REPRESENTED BY A -2-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "DF" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN -2-STRANDED BARREL THIS IS REPRESENTED BY A -1-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "DG" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 0-STRANDED BARREL THIS IS REPRESENTED BY A 1-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: TRANSLATION ELONGATION FACTOR SELB
B: TRANSLATION ELONGATION FACTOR SELB
C: TRANSLATION ELONGATION FACTOR SELB
D: TRANSLATION ELONGATION FACTOR SELB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)220,37019
Polymers216,5864
Non-polymers3,78415
Water00
1
A: TRANSLATION ELONGATION FACTOR SELB


Theoretical massNumber of molelcules
Total (without water)54,1471
Polymers54,1471
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: TRANSLATION ELONGATION FACTOR SELB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)55,0945
Polymers54,1471
Non-polymers9484
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: TRANSLATION ELONGATION FACTOR SELB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,98212
Polymers54,1471
Non-polymers2,83611
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
D: TRANSLATION ELONGATION FACTOR SELB


Theoretical massNumber of molelcules
Total (without water)54,1471
Polymers54,1471
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)146.860, 146.860, 297.830
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number151
Space group name H-MP3112

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Components

#1: Protein
TRANSLATION ELONGATION FACTOR SELB / MJ0495-LIKE PROTEIN


Mass: 54146.504 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) METHANOCOCCUS MARIPALUDIS (archaea) / Strain: JJ / Description: GERMAN COLLECTION OF MICROORGANISMS (DSM 2067) / Plasmid: PT7-7 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): ROSETTA / References: UniProt: Q8J307
#2: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: SO4
#3: Chemical
ChemComp-DXC / (3ALPHA,5BETA,12ALPHA)-3,12-DIHYDROXYCHOLAN-24-OIC ACID / DEOXYCHOLIC ACID


Mass: 392.572 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C24H40O4 / Comment: detergent*YM
#4: Chemical ChemComp-5GP / GUANOSINE-5'-MONOPHOSPHATE


Mass: 363.221 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H14N5O8P
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: 4.3 Å3/Da / Density % sol: 71 %
Description: THE INCREASED MERGING R VALUE IN THE HIGHEST RESOLUTION SHELL OF 1.64 IS DUE TO ANISOTROPY OF THE DATA
Crystal growDetails: 10 MM KCL,20 MM TRIS/HCL (PH 7.5),40 MM MGSO4,2 MM DTT,3 MM GDP,1.8 - 2.0 M AMMONIUM SULFATE,100 MM SODIUM CITRATE (PH 6.0),1 MM DEOXYCHOLIC ACID

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1
DetectorType: MARRESEARCH / Detector: CCD / Date: Dec 19, 2003
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.15→50 Å / Num. obs: 124004 / % possible obs: 99.7 % / Observed criterion σ(I): -3 / Redundancy: 8.7 % / Biso Wilson estimate: 97.09 Å2 / Rmerge(I) obs: 0.11 / Net I/σ(I): 15.23
Reflection shellResolution: 3.15→3.34 Å / Redundancy: 8.3 % / Rmerge(I) obs: 1.64 / Mean I/σ(I) obs: 1.71 / % possible all: 99.7

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE: 1.8_1069)refinement
XDSdata reduction
XSCALEdata scaling
CNSphasing
RefinementMethod to determine structure: SAD
Starting model: 4AC9

4ac9


Resolution: 3.15→19.971 Å / SU ML: 0.36 / σ(F): 0.75 / Phase error: 23.33 / Stereochemistry target values: ML
Details: A FOBS OVER SIGMA_FOBS CUTOFF OF 0.75 WAS APPLIED OWING TO ANISOTROPY OF THE DATA. THE MODEL WAS REFINED AGAINST ANOMALOUSLY SCALED DATA
RfactorNum. reflection% reflection
Rfree0.2148 4525 4.2 %
Rwork0.1725 --
obs0.1743 107556 86.86 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 169.71 Å2
Refinement stepCycle: LAST / Resolution: 3.15→19.971 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14274 0 255 0 14529
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00714730
X-RAY DIFFRACTIONf_angle_d1.12619892
X-RAY DIFFRACTIONf_dihedral_angle_d15.5855632
X-RAY DIFFRACTIONf_chiral_restr0.0692409
X-RAY DIFFRACTIONf_plane_restr0.0042448
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.1501-3.18580.40361150.36352517X-RAY DIFFRACTION62
3.1858-3.22310.36911310.30672643X-RAY DIFFRACTION68
3.2231-3.26220.31841290.29092900X-RAY DIFFRACTION73
3.2622-3.30340.37041160.27132824X-RAY DIFFRACTION73
3.3034-3.34660.31280.26192901X-RAY DIFFRACTION72
3.3466-3.39220.3211310.24862897X-RAY DIFFRACTION75
3.3922-3.44050.24481310.23923097X-RAY DIFFRACTION78
3.4405-3.49160.24091250.22763101X-RAY DIFFRACTION78
3.4916-3.54580.3151410.21613029X-RAY DIFFRACTION78
3.5458-3.60360.25631510.20533138X-RAY DIFFRACTION80
3.6036-3.66540.26131330.19013286X-RAY DIFFRACTION81
3.6654-3.73160.21671500.18313335X-RAY DIFFRACTION85
3.7316-3.80290.24591480.17293446X-RAY DIFFRACTION87
3.8029-3.880.18421400.16723476X-RAY DIFFRACTION87
3.88-3.96370.19521570.16223457X-RAY DIFFRACTION88
3.9637-4.05520.22421540.15143563X-RAY DIFFRACTION90
4.0552-4.15570.16951630.1513541X-RAY DIFFRACTION90
4.1557-4.2670.1741630.13523645X-RAY DIFFRACTION92
4.267-4.39130.16331580.12773687X-RAY DIFFRACTION94
4.3913-4.53140.16931690.12853799X-RAY DIFFRACTION95
4.5314-4.69140.16841640.11693757X-RAY DIFFRACTION96
4.6914-4.87660.15861740.12373837X-RAY DIFFRACTION96
4.8766-5.0950.18931670.13453843X-RAY DIFFRACTION97
5.095-5.35870.18181700.14823858X-RAY DIFFRACTION98
5.3587-5.68720.25541650.16583859X-RAY DIFFRACTION97
5.6872-6.11460.24441720.17863916X-RAY DIFFRACTION98
6.1146-6.70860.22371720.18763897X-RAY DIFFRACTION99
6.7086-7.63160.24581720.17653889X-RAY DIFFRACTION99
7.6316-9.44270.18181690.16413958X-RAY DIFFRACTION100
9.4427-19.9710.21611670.19913935X-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)
14.7595-1.0227-0.89294.8292.39176.2115-0.3049-0.8151-0.17390.50170.07470.65110.3543-0.81530.2190.5681-0.08870.04591.4554-0.01080.688728.5856-36.9742-50.7538
24.4853-0.54762.36644.6897-2.1843.0431-0.20150.11890.3583-0.01040.29030.4633-0.573-0.5999-0.10211.10170.4457-0.00510.8887-0.0020.802143.9561-13.2844-9.3441
34.6662-0.359-1.56562.2978-1.78019.0408-0.05450.6089-0.1434-0.40190.11010.07640.286-0.4195-0.0560.64490.0526-0.09230.5857-0.04750.483469.0466-49.765924.2115
40.9464-1.6086-0.36287.6722-1.97762.7523-0.4819-0.3180.60380.13420.57831.2656-1.0959-0.7483-0.1482.61680.8414-0.15941.5754-0.13321.833530.912915.7594-17.8984
55.4283-0.9726-3.91837.26574.02999.0082-0.4622-2.38460.53920.95130.3006-0.36080.3756-2.02930.01121.26520.3288-0.20863.1737-0.44571.010118.7031-24.9215-27.6263
67.92181.6733-0.80086.5428-0.10915.8456-0.1523-0.84790.13390.50550.11960.1216-0.6594-0.17980.06510.82050.2761-0.05520.70820.00970.445458.6308-27.50848.5266
77.166-1.23090.77758.97991.41178.89310.13860.20670.3081-0.58920.0542-0.8845-0.46091.4348-0.23420.536-0.07880.13610.81710.05170.537192.6648-46.298111.8378
83.5822-1.80310.73853.81770.4012.4012-0.0497-0.16490.1655-0.39430.2167-0.1047-1.8858-0.2354-0.01673.41960.6417-0.15841.45730.05011.883939.255232.1233-36.0882
97.1458-2.2117-0.13475.0417-0.00820.8362-0.2599-0.21810.0163-0.4634-0.45910.52530.234-1.48190.69071.0660.2113-0.06933.0849-0.51241.39990.5589-27.8985-51.7495
107.92832.0058-4.47077.4194-0.52095.50060.30340.4772-0.2357-1.35710.32511.70530.0513-2.3961-0.55041.1555-0.0325-0.3421.75220.31981.119730.2709-37.40111.5745
113.63410.3139-1.28742.6942-1.94075.1456-0.018-0.4342-0.1430.2165-0.2286-0.3693-0.43530.76280.23660.53560.0511-0.06340.9746-0.00370.608494.4427-53.396441.9177
125.97044.14211.67134.82751.39880.3008-0.5384-0.09390.949-0.44420.1878-1.38-1.29920.53280.20092.5495-0.094-0.36941.0988-0.11431.834261.674515.2012-25.3802
133.9871-0.39875.25834.75940.18747.7521-0.2182-1.11320.40730.6727-0.074-0.4042-0.88240.41180.13761.22610.0319-0.13082.9763-0.17171.4777-24.7078-22.2235-76.3271
144.67175.01580.14625.5152-1.27099.0345-0.21570.79843.3062-0.50810.22733.01270.5342-2.44240.27061.6984-0.051-0.38532.37220.34062.8337-1.6357-50.2538-1.0039
158.12440.32444.3873.6641-1.44413.3178-0.1284-0.7027-0.20590.8791-0.0062-1.08020.00910.60220.20411.26190.2115-0.19331.5510.05751.0838111.4139-55.199374.1354
160.28241.0851-0.70689.5372-2.95391.15710.7438-0.9607-0.68690.7093-0.5522-2.2262-0.37370.40770.01432.9238-0.74940.03492.28180.01373.061996.22447.2948-16.0299
177.2855.49085.1158.87652.7363.8581-0.2551-1.75620.42042.0889-0.138-1.5053-0.68543.2270.37392.46640.3205-1.72482.2137-0.18383.714929.9325-21.866-14.5501
184.53863.93620.62923.93362.18525.269-0.46410.61450.7347-0.10020.0723-0.0901-0.030.57260.07352.2755-0.837-0.78151.43920.66671.662475.4009-24.93164.6598
194.9713-2.7733-2.67754.09824.60486.45250.7911-1.9478-1.73731.0301-1.01271.46851.7174-1.31340.15211.4023-0.40070.38820.77960.14711.034670.2211-61.946840.548
201.2276-0.76130.82661.30191.00583.325-1.07561.4331-1.0317-0.971.63840.40782.2469-2.3652-0.28341.3232-0.4441-0.49721.1708-0.0520.985448.5637-56.857827.3154
213.10491.0992.71064.56643.2894.42140.36910.81130.5459-1.0116-0.43630.7575-0.7507-1.19210.07380.8894-0.09780.27341.1587-0.02730.7149.3205-49.859330.7146
222.00082.71632.35295.9251-3.56943.74510.2534-0.6616-1.12580.144-0.6258-0.5158-0.2231-0.02070.17091.59890.12920.00950.53650.02370.470779.6033-58.602953.7515
23222.00012-4.68751.04956.9543-18.32495.712125.0875-7.3879-8.6646-9.6317-40.10710.41422.9085-0.3543-0.18092.7867-0.11321.146549.1643-36.3987-10.4585
244.25444.37394.75076.35944.92895.30592.683-39.584-21.232611.12386.498546.3611.2068-28.7284-9.17651.65270.28060.49412.61790.42153.038172.925-38.2114.7923
252.36051.72861.70012.29022.15812.0384-2.5365-3.05248.25592.09550.51076.3773-6.4487-22.36132.00411.58280.0235-0.69021.95240.07781.368679.7485-49.374543.7393
2621.99992.0001222-4.35711.12084.933727.31795.7845-5.29940.3605-1.3346-1.44531.87510.1491-0.26821.81270.42111.009976.0447-45.180547.0063
274.74292.2207-4.84391.0396-2.26784.947-1.0345-1.6813-22.549913.3552-5.6788-28.67319.9039-5.72956.70651.5675-0.0171-0.14192.0669-0.06312.1581113.4932-54.524358.0203
281.99992.00012.0001221.999914.47719.6961-5.9239-20.8272-8.03838.247831.33125.4274-6.42452.43650.6551-0.93132.38840.89582.282572.6255-66.795232.6662
2921.99992.00011.9999226.67714.8118-21.7096-11.7227-4.70225.7756-4.317915.7275-2.03391.74080.64550.4911.55360.41461.870490.2302-65.301254.5192
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1((CHAIN A AND RESID 0:179))
2X-RAY DIFFRACTION2((CHAIN B AND RESID 1:179))
3X-RAY DIFFRACTION3((CHAIN C AND RESID -2:179))
4X-RAY DIFFRACTION4(CHAIN D AND RESID 2:179)
5X-RAY DIFFRACTION5(CHAIN A AND RESID 180:270)
6X-RAY DIFFRACTION6((CHAIN B AND RESID 180:270) OR (CHAIN B AND RESID 1473))
7X-RAY DIFFRACTION7((CHAIN C AND RESID 180:270) OR (CHAIN C AND RESID 1475))
8X-RAY DIFFRACTION8(CHAIN D AND RESID 180:270)
9X-RAY DIFFRACTION9(CHAIN A AND RESID 271:388)
10X-RAY DIFFRACTION10(CHAIN B AND RESID 271:388)
11X-RAY DIFFRACTION11(CHAIN C AND RESID 271:388)
12X-RAY DIFFRACTION12(CHAIN D AND RESID 271:388)
13X-RAY DIFFRACTION13(CHAIN A AND RESID 389:468)
14X-RAY DIFFRACTION14(CHAIN B AND RESID 389:468)
15X-RAY DIFFRACTION15(CHAIN C AND RESID 389:468)
16X-RAY DIFFRACTION16(CHAIN D AND RESID 389:468)
17X-RAY DIFFRACTION17(CHAIN B AND RESID 1474)
18X-RAY DIFFRACTION18(CHAIN C AND RESID 1476)
19X-RAY DIFFRACTION19(CHAIN C AND RESID 1477)
20X-RAY DIFFRACTION20(CHAIN C AND RESID 1478)
21X-RAY DIFFRACTION21(CHAIN C AND RESID 1479)
22X-RAY DIFFRACTION22(CHAIN C AND RESID 1480)
23X-RAY DIFFRACTION23(CHAIN B AND RESID 1471)
24X-RAY DIFFRACTION24(CHAIN B AND RESID 1472)
25X-RAY DIFFRACTION25(CHAIN C AND RESID 1471)
26X-RAY DIFFRACTION26(CHAIN C AND RESID 1472)
27X-RAY DIFFRACTION27(CHAIN C AND RESID 1473)
28X-RAY DIFFRACTION28(CHAIN C AND RESID 1474)
29X-RAY DIFFRACTION29(CHAIN C AND RESID 1481)

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