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- PDB-4pl8: Structure of rabbit skeletal muscle actin in complex with a hybri... -

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Basic information

Entry
Database: PDB / ID: 4pl8
TitleStructure of rabbit skeletal muscle actin in complex with a hybrid peptide comprising thymosin beta4 and the lysine-rich region of Cordon-Bleu
Components
  • Actin, alpha skeletal muscle
  • Thymosin beta-4,Protein cordon-bleu,Thymosin beta-4
KeywordsCONTRACTILE PROTEIN/STRUCTURAL PROTEIN / CONTRACTILE PROTEIN-STRUCTURAL PROTEIN complex
Function / homology
Function and homology information


positive regulation of proton-transporting ATP synthase activity, rotational mechanism / somite specification / floor plate development / actin filament network formation / terminal web / embryonic axis specification / notochord development / sequestering of actin monomers / digestive tract development / collateral sprouting in absence of injury ...positive regulation of proton-transporting ATP synthase activity, rotational mechanism / somite specification / floor plate development / actin filament network formation / terminal web / embryonic axis specification / notochord development / sequestering of actin monomers / digestive tract development / collateral sprouting in absence of injury / positive regulation of ruffle assembly / positive regulation of dendrite development / positive regulation of endothelial cell chemotaxis / cytoskeletal motor activator activity / positive regulation of ATP biosynthetic process / tropomyosin binding / mesenchyme migration / myosin heavy chain binding / troponin I binding / actin filament bundle / dendritic growth cone / filamentous actin / skeletal muscle thin filament assembly / actin filament bundle assembly / striated muscle thin filament / skeletal muscle myofibril / actin monomer binding / positive regulation of blood vessel endothelial cell migration / skeletal muscle fiber development / axonal growth cone / negative regulation of canonical NF-kappaB signal transduction / stress fiber / titin binding / regulation of cell migration / ruffle / tumor necrosis factor-mediated signaling pathway / actin filament polymerization / protein sequestering activity / liver development / platelet alpha granule lumen / filopodium / neural tube closure / actin filament organization / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / negative regulation of inflammatory response / calcium-dependent protein binding / Platelet degranulation / lamellipodium / cell cortex / cell body / cytoskeleton / hydrolase activity / protein domain specific binding / axon / neuronal cell body / dendrite / calcium ion binding / positive regulation of gene expression / perinuclear region of cytoplasm / enzyme binding / magnesium ion binding / RNA binding / extracellular region / ATP binding / membrane / identical protein binding / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Cordon-bleu, ubiquitin-like domain / Protein cordon-bleu-like / Cordon-bleu ubiquitin-like domain / Thymosin beta-4 family signature. / Beta-thymosin / Beta-thymosin superfamily / Thymosin beta-4 family / Thymosin beta actin-binding motif. / Wiskott Aldrich syndrome homology region 2 / WH2 motif ...Cordon-bleu, ubiquitin-like domain / Protein cordon-bleu-like / Cordon-bleu ubiquitin-like domain / Thymosin beta-4 family signature. / Beta-thymosin / Beta-thymosin superfamily / Thymosin beta-4 family / Thymosin beta actin-binding motif. / Wiskott Aldrich syndrome homology region 2 / WH2 motif / WH2 domain / WH2 domain profile. / ATPase, substrate binding domain, subdomain 4 / Actin; Chain A, domain 4 / ATPase, nucleotide binding domain / Actins signature 1. / Actin, conserved site / Actins signature 2. / Actin/actin-like conserved site / Actins and actin-related proteins signature. / Actin / Actin family / Actin / ATPase, nucleotide binding domain / Nucleotidyltransferase; domain 5 / Alpha-Beta Complex / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
ADENOSINE-5'-TRIPHOSPHATE / Protein cordon-bleu / Thymosin beta-4 / Actin, alpha skeletal muscle
Similarity search - Component
Biological speciesOryctolagus cuniculus (rabbit)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2 Å
AuthorsXue, B. / Robinson, R.C.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2014
Title: Structural basis of thymosin-beta 4/profilin exchange leading to actin filament polymerization.
Authors: Xue, B. / Leyrat, C. / Grimes, J.M. / Robinson, R.C.
History
DepositionMay 16, 2014Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Oct 22, 2014Provider: repository / Type: Initial release
Revision 1.1Nov 12, 2014Group: Database references
Revision 1.2Nov 8, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description / Source and taxonomy
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / citation / database_2 / entity_src_nat / pdbx_database_status / pdbx_entity_src_syn / pdbx_initial_refinement_model / pdbx_struct_assembly / pdbx_struct_conn_angle / pdbx_struct_oper_list / refine_hist / struct_conn
Item: _citation.journal_id_CSD / _database_2.pdbx_DOI ..._citation.journal_id_CSD / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _entity_src_nat.pdbx_alt_source_flag / _pdbx_database_status.pdb_format_compatible / _pdbx_entity_src_syn.pdbx_alt_source_flag / _pdbx_struct_assembly.oligomeric_details / _pdbx_struct_oper_list.symmetry_operation / _struct_conn.pdbx_dist_value / _struct_conn.ptnr2_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Actin, alpha skeletal muscle
H: Thymosin beta-4,Protein cordon-bleu,Thymosin beta-4
B: Actin, alpha skeletal muscle
hetero molecules


Theoretical massNumber of molelcules
Total (without water)93,1797
Polymers92,0853
Non-polymers1,0954
Water9,566531
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6610 Å2
ΔGint-54 kcal/mol
Surface area29490 Å2
MethodPISA
Unit cell
Length a, b, c (Å)93.640, 93.640, 206.274
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number96
Space group name H-MP43212
Detailsbiological unit is the same as asym.

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Components

#1: Protein Actin, alpha skeletal muscle / / Alpha-actin-1


Mass: 41875.633 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Oryctolagus cuniculus (rabbit) / Tissue: skeletal muscle / References: UniProt: P68135
#2: Protein Thymosin beta-4,Protein cordon-bleu,Thymosin beta-4 / T beta-4 / Fx


Mass: 8333.400 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P62328, UniProt: O75128
#3: Chemical ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE / Adenosine triphosphate


Mass: 507.181 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H16N5O13P3 / Comment: ATP, energy-carrying molecule*YM
#4: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ca
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 531 / Source method: isolated from a natural source / Formula: H2O

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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: 2.46 Å3/Da / Density % sol: 49.9 %
Crystal growTemperature: 288 K / Method: vapor diffusion, sitting drop / pH: 3.5 / Details: 0.1 M citric acid, 15% (w/v) PEG 3350

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSRRC / Beamline: BL13B1 / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Jun 6, 2012 / Details: Quantum-315
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2→20 Å / Num. obs: 62837 / % possible obs: 100 % / Redundancy: 12 % / Rmerge(I) obs: 0.06 / Χ2: 0.96 / Net I/av σ(I): 40.929 / Net I/σ(I): 12.5 / Num. measured all: 751602
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allΧ2Diffraction-ID% possible all
2-2.0711.80.59561730.8111100
2.07-2.1511.90.42261490.851100
2.15-2.2511.90.3162030.899100
2.25-2.3711.90.22961890.913100
2.37-2.5211.90.16362220.931100
2.52-2.7112.10.11362340.966100
2.71-2.9912.20.07562680.97100
2.99-3.4212.30.05363141.071100
3.42-4.311.90.04563991.386100
4.3-2011.80.02866860.789100

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
DENZOdata collection
SCALEPACKdata reduction
PHASER2.1.4phasing
PDB_EXTRACT3.11data extraction
Cootmodel building
PHENIX(phenix.refine: 1.8.4_1496)refinement
PHASERmodel building
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1T44

1t44


Resolution: 2→19.896 Å / Occupancy max: 1 / Occupancy min: 1 / SU ML: 0.17 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 19.28 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.207 3180 5.07 %
Rwork0.171 59549 -
obs0.1728 62729 99.95 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 127.94 Å2 / Biso mean: 31.9416 Å2 / Biso min: 10.58 Å2
Refinement stepCycle: LAST / Resolution: 2→19.896 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5703 0 64 531 6298
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0085886
X-RAY DIFFRACTIONf_angle_d1.1637981
X-RAY DIFFRACTIONf_chiral_restr0.05890
X-RAY DIFFRACTIONf_plane_restr0.0061010
X-RAY DIFFRACTIONf_dihedral_angle_d13.5522195
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 10 / % reflection obs: 100 %

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all
1.9995-2.07090.26062980.200858596157
2.0709-2.15370.22113220.187358246146
2.1537-2.25160.25343240.199258776201
2.2516-2.37010.22543230.194158636186
2.3701-2.51840.21013270.181158906217
2.5184-2.71240.21993120.172959116223
2.7124-2.98450.18653260.171259376263
2.9845-3.41450.2153200.170659816301
3.4145-4.29480.18973150.152860736388
4.2948-19.89650.18823130.160463346647
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)
10.5412-0.2920.09430.40690.08490.0926-0.007-0.0906-0.141-0.0171-0.0246-0.33510.43150.106-0.02170.36590.02760.04790.09540.02430.1992-16.72060.276818.3934
20.75640.3171-0.00781.06370.49240.9360.0471-0.1734-0.32660.5428-0.0563-1.04980.21430.7429-0.04470.34750.0017-0.15420.33170.07110.3219-9.29947.15829.5214
30.2846-0.0344-0.04290.1323-0.05430.03430.04-1.132-0.161.00660.0007-0.0667-0.021-0.1032-0.00580.60820.0025-0.10010.49320.04660.4249-9.086310.957834.8697
40.2514-0.13560.00160.1922-0.070.4685-0.0553-0.21050.4940.30790.0254-0.4077-0.16340.4789-0.01640.2079-0.0253-0.03160.21590.00110.279-10.679717.477720.8493
50.6783-0.1371-0.09540.21660.04960.0170.0393-0.32490.01190.4066-0.0867-0.39070.40180.4803-0.00220.40510.0705-0.03930.26660.09810.2911-5.90762.077721.8527
60.2180.19580.0190.20790.11490.27580.12520.12010.1909-0.2709-0.1581-0.41180.17880.2130.00030.23520.0470.07560.16290.03950.2432-12.17928.807811.1806
70.09270.036-0.00120.14850.07810.1558-0.0445-0.08260.18790.02830.1425-0.45470.10180.07320.00240.26890.05170.01980.21830.0680.2726-4.04929.127610.6316
80.5083-0.0518-0.13020.45-0.25420.6167-0.02410.10820.0591-0.059-0.0486-0.0720.0979-0.0511-0.00010.1813-0.01320.02920.12910.00040.137-26.109312.51510.717
91.0611-0.3569-0.51320.53890.23530.5882-0.0021-0.52510.08440.50880.1849-0.13190.15540.40840.01850.331-0.01470.00670.2148-0.01390.1564-29.13319.464939.1857
100.789-1.3167-1.66434.01843.03393.56350.3511-0.5149-0.08450.37990.1862-0.78560.02710.96490.40730.3539-0.05320.01780.35230.03380.216-26.089111.485839.6066
110.0834-0.0976-0.09150.157-0.07450.6053-0.08010.01230.0682-0.01350.12770.4135-0.1639-0.425-0.00160.1726-0.01830.03550.2524-0.02580.2487-46.525718.480234.4899
120.3111-0.03910.06560.0565-0.04390.0358-0.0026-0.92030.01350.5134-0.0358-0.00190.1637-0.0733-0.00840.45460.02590.01240.50410.13690.3325-35.85468.696746.8548
130.1749-0.02130.07410.1036-0.01710.04110.0806-0.25890.03770.26720.09540.0796-0.0668-0.03970.01530.1682-0.02470.03690.1819-0.01050.1243-36.533920.452232.692
140.6006-0.13310.05970.11620.08420.1113-0.0113-0.19870.49150.04780.0541-0.0092-0.7228-0.107-0.00840.2928-0.01940.01130.2049-0.00410.2089-34.636424.80319.9698
150.4259-0.09890.05750.1489-0.07620.0415-0.05180.63970.2616-0.4974-0.02350.1581-0.0893-0.5286-0.01070.2494-0.03030.0290.3059-0.00690.1996-38.331419.83294.489
160.12190.0588-0.09070.16750.06310.2789-0.03220.0975-0.08710.0233-0.01640.20950.1504-0.2556-0.00150.1996-0.0450.02190.2311-0.02370.1764-40.762312.469116.9093
170.01030.0011-0.00720.0357-0.00180.0044-0.1423-0.1469-0.2558-0.04810.0191-0.01630.3578-0.07010.00070.3938-0.04450.03090.15950.02940.2521-28.6512.670222.1219
183.4821-0.49270.58470.7401-0.56880.5485-0.00940.2666-0.4494-0.2819-0.1539-0.25910.32970.05230.13030.3267-0.0360.07680.1292-0.01430.1545-20.943-1.21368.7756
190.8773-0.0039-0.60150.3911-0.29280.6377-0.00330.6142-0.1685-0.16290.00210.27950.3373-0.32-0.04770.29430.08040.09270.29790.0740.2888-8.38362.40740.9681
200.4342-0.55380.15410.9285-0.43980.34140.17490.2143-0.3752-0.43030.02930.35950.1344-0.28280.02010.31460.06360.04850.34480.06890.2988-6.374310.31720.6257
210.7944-0.2065-0.48260.47480.0040.69120.04680.90380.1556-0.410.07410.25270.0733-0.5005-0.51810.14560.0492-0.08550.64140.23850.1529-18.420822.6341-26.6197
220.1093-0.09350.02821.00030.74760.6614-0.16930.22130.2011-0.2284-0.09390.6265-0.5111-0.2139-0.21090.44920.0705-0.07370.86980.43660.8382-21.815640.9096-25.1244
230.16510.03030.03060.00650.01490.2119-0.0590.01820.43140.09470.16440.2037-0.2451-0.24130.20230.28950.19280.12920.31490.22440.4903-16.841834.228-13.6594
240.87890.14070.34590.1976-0.20840.55040.0730.72780.4616-0.3104-0.01310.3268-0.2157-0.42860.4409-0.09240.3208-0.1430.89420.48090.4361-27.533328.6542-24.2798
250.62820.16770.15031.0538-0.06720.2040.13330.18850.24760.1169-0.06320.2965-0.0171-0.59260.20790.08490.04530.00330.40840.08770.2519-21.035421.8745-14.1121
260.04190.07380.05041.0340.12570.0820.0807-0.0660.49170.2237-0.02220.2274-0.0562-0.42080.08080.12160.10580.09170.4650.17890.3414-28.446624.5661-11.9825
270.82490.103-0.01740.19740.33610.71330.03850.13940.05550.03820.03130.02630.1121-0.11730.00020.12690.00290.00310.21740.05950.1724-8.084717.7364-13.6094
280.1680.1895-0.10410.29680.04760.37040.2414-0.0570.33030.45720.06870.4162-0.4492-0.00920.02460.21670.03430.04890.21790.05830.33631.009739.9034-23.0478
291.31250.48340.39290.473-0.30631.1592-0.1665-0.25420.9721-0.15850.14750.1732-0.2499-0.3132-0.06210.22340.0082-0.0430.30960.09740.44292.229637.2262-31.5687
301.49330.00470.01540.7237-0.47540.3088-0.0850.8753-0.2482-0.9044-0.024-0.29910.3753-0.102-0.01240.34760.03940.0880.3820.0760.440116.054135.1769-36.1178
310.7526-0.49190.3030.3198-0.20.12330.14760.35910.5608-0.3961-0.03350.286-0.3352-0.3386-0.00410.6263-0.0512-0.17431.03340.2970.7079-0.131642.8031-42.5137
320.20550.0011-0.03920.1356-0.15590.27530.04960.04630.31210.09710.08120.1213-0.3830.0360.00210.1765-0.01520.0290.16340.04940.24328.27636.3867-24.3211
331.8339-0.2144-0.04680.2722-0.37250.99020.1052-0.43650.81210.566-0.1318-0.1606-0.91120.0379-0.00060.2979-0.02970.00890.2265-0.01050.26876.777730.4703-12.8089
340.42410.1599-0.24220.9727-0.10720.14360.0217-0.3726-0.27390.4359-0.0504-0.33540.20850.4788-0.04040.1980.0509-0.00450.26520.05630.19876.233914.9719-7.1014
350.05-0.05230.10450.63430.651.1169-0.08250.18530.2763-0.14950.2029-0.12670.10740.18530.17630.126-0.01330.00950.24630.08220.22090.069820.3648-22.0638
360.1426-0.0321-0.01210.01090.03970.1299-0.0088-0.0548-0.1627-0.01320.1140.07430.10420.14890.00020.14290.01630.02440.23590.05260.214311.676920.5536-19.7143
370.0438-0.05650.10080.2729-0.20460.2771-0.05510.2311-0.2343-0.22750.08750.22410.5275-0.02230.00670.26070.04030.00720.3344-0.01110.23762.577715.4593-24.2543
381.092-0.876-1.01720.70010.82150.9665-0.08650.5756-0.52540.0109-0.26950.17350.5072-0.3052-0.16780.2088-0.0689-0.01310.36390.00380.2232-14.875513.5076-22.5896
390.9085-0.06010.39510.13520.10730.97050.06250.1101-0.40450.28480.19140.27210.4821-0.26190.09380.2725-0.0330.06220.39170.04590.3071-29.533913.7615-9.5232
400.0828-0.14340.05630.249-0.10020.04130.20610.2613-0.5533-0.19360.0624-0.27410.52930.3819-0.00140.4039-0.07340.01890.48830.00930.3962-23.193815.8049-4.8731
410.0132-0.0057-0.0320.02460.02580.08620.02030.08550.0157-0.01620.0298-0.07430.01560.0508-0.00010.7048-0.11480.11490.4853-0.04540.4874-26.41241.1871-2.0961
420.0426-0.1343-0.03780.6473-0.00540.11190.11440.1538-0.2317-0.19550.08990.13770.1916-0.168-0.0030.5675-0.0164-0.07410.2978-0.09010.3946-29.9237-2.35792.053
430.5409-0.17210.16160.055-0.05150.05010.0047-0.0588-0.63270.09510.08520.120.2716-0.04670.00720.7262-0.15930.09570.1230.02020.4102-27.1274-9.347312.8213
440.1030.0608-0.0830.0332-0.04790.0696-0.0519-0.2670.10120.1760.0964-0.332-0.02750.10570.00210.9614-0.25470.03910.63820.0150.622-19.2385-4.154128.7006
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain A and resid 5:27)A5 - 27
2X-RAY DIFFRACTION2(chain A and resid 28:53)A28 - 53
3X-RAY DIFFRACTION3(chain A and resid 54:70)A54 - 70
4X-RAY DIFFRACTION4(chain A and resid 71:81)A71 - 81
5X-RAY DIFFRACTION5(chain A and resid 82:98)A82 - 98
6X-RAY DIFFRACTION6(chain A and resid 99:115)A99 - 115
7X-RAY DIFFRACTION7(chain A and resid 116:129)A116 - 129
8X-RAY DIFFRACTION8(chain A and resid 130:180)A130 - 180
9X-RAY DIFFRACTION9(chain A and resid 181:199)A181 - 199
10X-RAY DIFFRACTION10(chain A and resid 200:217)A200 - 217
11X-RAY DIFFRACTION11(chain A and resid 218:233)A218 - 233
12X-RAY DIFFRACTION12(chain A and resid 234:249)A234 - 249
13X-RAY DIFFRACTION13(chain A and resid 250:268)A250 - 268
14X-RAY DIFFRACTION14(chain A and resid 269:278)A269 - 278
15X-RAY DIFFRACTION15(chain A and resid 279:292)A279 - 292
16X-RAY DIFFRACTION16(chain A and resid 293:333)A293 - 333
17X-RAY DIFFRACTION17(chain A and resid 334:337)A334 - 337
18X-RAY DIFFRACTION18(chain A and resid 338:353)A338 - 353
19X-RAY DIFFRACTION19(chain A and resid 354:361)A354 - 361
20X-RAY DIFFRACTION20(chain A and resid 362:374)A362 - 374
21X-RAY DIFFRACTION21(chain B and resid 6:33)B6 - 33
22X-RAY DIFFRACTION22(chain B and resid 34:69)B34 - 69
23X-RAY DIFFRACTION23(chain B and resid 70:79)B70 - 79
24X-RAY DIFFRACTION24(chain B and resid 80:98)B80 - 98
25X-RAY DIFFRACTION25(chain B and resid 99:115)B99 - 115
26X-RAY DIFFRACTION26(chain B and resid 116:128)B116 - 128
27X-RAY DIFFRACTION27(chain B and resid 129:175)B129 - 175
28X-RAY DIFFRACTION28(chain B and resid 176:197)B176 - 197
29X-RAY DIFFRACTION29(chain B and resid 198:224)B198 - 224
30X-RAY DIFFRACTION30(chain B and resid 225:238)B225 - 238
31X-RAY DIFFRACTION31(chain B and resid 239:250)B239 - 250
32X-RAY DIFFRACTION32(chain B and resid 251:268)B251 - 268
33X-RAY DIFFRACTION33(chain B and resid 269:278)B269 - 278
34X-RAY DIFFRACTION34(chain B and resid 279:294)B279 - 294
35X-RAY DIFFRACTION35(chain B and resid 295:305)B295 - 305
36X-RAY DIFFRACTION36(chain B and resid 306:325)B306 - 325
37X-RAY DIFFRACTION37(chain B and resid 326:335)B326 - 335
38X-RAY DIFFRACTION38(chain B and resid 336:352)B336 - 352
39X-RAY DIFFRACTION39(chain B and resid 353:367)B353 - 367
40X-RAY DIFFRACTION40(chain B and resid 368:374)B368 - 374
41X-RAY DIFFRACTION41(chain H and resid 34:36)H34 - 36
42X-RAY DIFFRACTION42(chain H and resid 37:41)H37 - 41
43X-RAY DIFFRACTION43(chain H and resid 42:49)H42 - 49
44X-RAY DIFFRACTION44(chain H and resid 50:55)H50 - 55

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