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- PDB-2yjf: Oligomeric assembly of actin bound to MRTF-A -

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Basic information

Entry
Database: PDB / ID: 2yjf
TitleOligomeric assembly of actin bound to MRTF-A
Components
  • ACTIN, ALPHA SKELETAL MUSCLE
  • MKL/MYOCARDIN-LIKE PROTEIN 1
KeywordsMOTOR PROTEIN
Function / homology
Function and homology information


SUMOylation of transcription cofactors / leucine zipper domain binding / RHO GTPases Activate Formins / smooth muscle cell differentiation / wound healing, spreading of cells / cytoskeletal motor activator activity / tropomyosin binding / myosin heavy chain binding / mesenchyme migration / troponin I binding ...SUMOylation of transcription cofactors / leucine zipper domain binding / RHO GTPases Activate Formins / smooth muscle cell differentiation / wound healing, spreading of cells / cytoskeletal motor activator activity / tropomyosin binding / myosin heavy chain binding / mesenchyme migration / troponin I binding / actin filament bundle / filamentous actin / actin filament bundle assembly / skeletal muscle thin filament assembly / striated muscle thin filament / negative regulation of apoptotic signaling pathway / skeletal muscle myofibril / actin monomer binding / skeletal muscle fiber development / stress fiber / forebrain development / titin binding / actin filament polymerization / filopodium / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / neuron migration / positive regulation of miRNA transcription / neuron projection development / calcium-dependent protein binding / lamellipodium / cell body / actin binding / actin cytoskeleton organization / transcription coactivator activity / molecular adaptor activity / transcription cis-regulatory region binding / hydrolase activity / DNA-binding transcription factor activity / protein domain specific binding / calcium ion binding / positive regulation of gene expression / regulation of transcription by RNA polymerase II / positive regulation of DNA-templated transcription / magnesium ion binding / positive regulation of transcription by RNA polymerase II / nucleoplasm / ATP binding / identical protein binding / nucleus / cytosol / cytoplasm
Similarity search - Function
Cobalamin-dependent Methionine Synthase; domain 2 / Cobalamin-dependent Methionine Synthase; domain 2 - #10 / Helix Hairpins - #2040 / Myocardin-like / RPEL repeat / RPEL repeat / RPEL repeat profile. / Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2 / SAP domain superfamily / SAP domain ...Cobalamin-dependent Methionine Synthase; domain 2 / Cobalamin-dependent Methionine Synthase; domain 2 - #10 / Helix Hairpins - #2040 / Myocardin-like / RPEL repeat / RPEL repeat / RPEL repeat profile. / Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2 / SAP domain superfamily / SAP domain / SAP motif profile. / Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation / SAP domain / ATPase, substrate binding domain, subdomain 4 / Actin; Chain A, domain 4 / Helix Hairpins / 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 / Helix non-globular / Special / ATPase, nucleotide binding domain / Nucleotidyltransferase; domain 5 / Alpha-Beta Complex / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
ADENOSINE-5'-TRIPHOSPHATE / LATRUNCULIN B / Actin, alpha skeletal muscle / Myocardin-related transcription factor A
Similarity search - Component
Biological speciesORYCTOLAGUS CUNICULUS (rabbit)
MUS MUSCULUS (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.5 Å
AuthorsMouilleron, S. / Langer, C.A. / Guettler, S. / McDonald, N.Q. / Treisman, R.
CitationJournal: Sci Signal / Year: 2011
Title: Structure of a pentavalent G-actin*MRTF-A complex reveals how G-actin controls nucleocytoplasmic shuttling of a transcriptional coactivator.
Authors: Mouilleron, S. / Langer, C.A. / Guettler, S. / McDonald, N.Q. / Treisman, R.
History
DepositionMay 19, 2011Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 6, 2011Provider: repository / Type: Initial release
Revision 1.1Nov 16, 2011Group: Database references / Version format compliance
Revision 1.2Oct 3, 2012Group: Derived calculations
Revision 1.3Apr 11, 2018Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.journal_abbrev / _citation.page_first ..._citation.journal_abbrev / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.title / _citation_author.name
Revision 1.4Dec 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 / pdbx_struct_conn_angle / struct_conn / 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 / _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.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_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_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_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: ACTIN, ALPHA SKELETAL MUSCLE
B: ACTIN, ALPHA SKELETAL MUSCLE
C: ACTIN, ALPHA SKELETAL MUSCLE
D: ACTIN, ALPHA SKELETAL MUSCLE
E: ACTIN, ALPHA SKELETAL MUSCLE
M: MKL/MYOCARDIN-LIKE PROTEIN 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)229,83418
Polymers226,3856
Non-polymers3,44812
Water0
1
A: ACTIN, ALPHA SKELETAL MUSCLE
B: ACTIN, ALPHA SKELETAL MUSCLE
C: ACTIN, ALPHA SKELETAL MUSCLE
M: MKL/MYOCARDIN-LIKE PROTEIN 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)144,57712
Polymers142,1914
Non-polymers2,3858
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area12990 Å2
ΔGint-83.8 kcal/mol
Surface area45330 Å2
MethodPISA
2
D: ACTIN, ALPHA SKELETAL MUSCLE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,6283
Polymers42,0971
Non-polymers5312
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
E: ACTIN, ALPHA SKELETAL MUSCLE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,6283
Polymers42,0971
Non-polymers5312
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)182.910, 182.910, 378.281
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number179
Space group name H-MP6522
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
31
41
51
12
22
32
42
52

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111CHAIN A AND (RESSEQ 7:23 OR RESSEQ 28:35 OR RESSEQ...
211CHAIN E AND (RESSEQ 7:23 OR RESSEQ 28:35 OR RESSEQ...
311CHAIN B AND (RESSEQ 7:23 OR RESSEQ 28:35 OR RESSEQ...
411CHAIN C AND (RESSEQ 27:35 OR RESSEQ 51:56 OR RESSEQ...
511CHAIN D AND (RESSEQ 7:23 OR RESSEQ 27:35 OR RESSEQ...
112CHAIN A AND (RESSEQ 7:23 OR RESSEQ 28:35 OR RESSEQ...
212CHAIN E AND (RESSEQ 7:23 OR RESSEQ 28:35 OR RESSEQ...
312CHAIN B AND (RESSEQ 7:23 OR RESSEQ 28:35 OR RESSEQ...
412CHAIN C AND (RESSEQ 27:35 OR RESSEQ 51:56 OR RESSEQ...
512CHAIN D AND (RESSEQ 7:23 OR RESSEQ 27:35 OR RESSEQ...

NCS ensembles :
ID
1
2

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Components

#1: Protein
ACTIN, ALPHA SKELETAL MUSCLE / / ALPHA-ACTIN-1


Mass: 42096.953 Da / Num. of mol.: 5
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) ORYCTOLAGUS CUNICULUS (rabbit) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / Variant (production host): ROSETTA PLYSS / References: UniProt: P68135
#2: Protein MKL/MYOCARDIN-LIKE PROTEIN 1 / BASIC SAP COILED-COIL TRANSCRIPTION ACTIVATOR / MEGAKARYOBLASTIC LEUKEMIA 1 PROTEIN HOMOLOG / ...BASIC SAP COILED-COIL TRANSCRIPTION ACTIVATOR / MEGAKARYOBLASTIC LEUKEMIA 1 PROTEIN HOMOLOG / MYOCARDIN-RELATED TRANSCRIPTION FACTOR A / MRTF-A


Mass: 15900.372 Da / Num. of mol.: 1 / Fragment: RPEL DOMAIN, RESIDUES 16-142 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) MUS MUSCULUS (house mouse) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / Variant (production host): ROSETTA PLYSS / References: UniProt: Q8K4J6
#3: Chemical ChemComp-LAB / LATRUNCULIN B / Latrunculin


Mass: 395.513 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C20H29NO5S / Comment: toxin*YM
#4: Chemical
ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE / Adenosine triphosphate


Mass: 507.181 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C10H16N5O13P3 / Comment: ATP, energy-carrying molecule*YM
#5: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Mg
Compound detailsENGINEERED RESIDUE IN CHAIN M, GLY 114 TO GLU ENGINEERED RESIDUE IN CHAIN M, PRO 115 TO ARG

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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: 4.02 Å3/Da / Density % sol: 69.45 % / Description: NONE
Crystal growpH: 5.3 / Details: pH 5.3

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.934
DetectorType: ADSC CCD / Detector: CCD / Date: Feb 8, 2009
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.934 Å / Relative weight: 1
ReflectionResolution: 3.5→45 Å / Num. obs: 47726 / % possible obs: 99.6 % / Observed criterion σ(I): 2 / Redundancy: 5.3 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 7.1
Reflection shellResolution: 3.5→3.69 Å / Redundancy: 5.1 % / Rmerge(I) obs: 0.39 / Mean I/σ(I) obs: 2 / % possible all: 99.6

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2V52

2v52


Resolution: 3.5→46.525 Å / SU ML: 0.38 / σ(F): 0 / Phase error: 25.86 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2722 2342 5.1 %
Rwork0.2379 --
obs0.2396 46151 96.34 %
Solvent computationShrinkage radii: 0.83 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 106.344 Å2 / ksol: 0.307 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-10.1626 Å20 Å20 Å2
2--10.1626 Å20 Å2
3----20.3252 Å2
Refinement stepCycle: LAST / Resolution: 3.5→46.525 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13058 0 214 0 13272
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01114115
X-RAY DIFFRACTIONf_angle_d1.02318551
X-RAY DIFFRACTIONf_dihedral_angle_d20.4064783
X-RAY DIFFRACTIONf_chiral_restr0.0642168
X-RAY DIFFRACTIONf_plane_restr0.0042402
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A1176X-RAY DIFFRACTIONPOSITIONAL
12E1176X-RAY DIFFRACTIONPOSITIONAL0.027
13B1208X-RAY DIFFRACTIONPOSITIONAL0.031
14C1108X-RAY DIFFRACTIONPOSITIONAL0.036
15D1212X-RAY DIFFRACTIONPOSITIONAL0.035
21A910X-RAY DIFFRACTIONPOSITIONAL
22E910X-RAY DIFFRACTIONPOSITIONAL0.034
23B1268X-RAY DIFFRACTIONPOSITIONAL0.035
24C1158X-RAY DIFFRACTIONPOSITIONAL0.04
25D1259X-RAY DIFFRACTIONPOSITIONAL0.038
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.5-3.57140.38671400.34172407X-RAY DIFFRACTION92
3.5714-3.6490.38281200.30872430X-RAY DIFFRACTION93
3.649-3.73390.33531430.29162443X-RAY DIFFRACTION94
3.7339-3.82720.30061380.25852442X-RAY DIFFRACTION94
3.8272-3.93070.2781340.2392521X-RAY DIFFRACTION96
3.9307-4.04630.25271560.22072502X-RAY DIFFRACTION95
4.0463-4.17680.25691180.21542548X-RAY DIFFRACTION96
4.1768-4.3260.21731300.20472559X-RAY DIFFRACTION97
4.326-4.4990.23081190.19162579X-RAY DIFFRACTION97
4.499-4.70360.21991380.19652602X-RAY DIFFRACTION98
4.7036-4.95130.26611460.21032614X-RAY DIFFRACTION98
4.9513-5.26110.25041500.21462601X-RAY DIFFRACTION98
5.2611-5.66670.23061250.24632638X-RAY DIFFRACTION98
5.6667-6.23580.29581440.25942662X-RAY DIFFRACTION99
6.2358-7.13530.29431470.27182683X-RAY DIFFRACTION99
7.1353-8.97910.24311400.20322751X-RAY DIFFRACTION99
8.9791-46.5290.29321540.26212827X-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)
12.89480.8314-1.06946.7208-2.25633.39220.22210.37820.3342-0.8775-0.2954-0.3675-0.49620.45150.05381.2072-0.60410.42280.6111-0.0810.6859-11.6603-21.35124.9533
20.3713-0.73630.42251.4655-0.83260.4754-0.6276-0.18350.70131.1312-0.0340.7157-1.02270.3096-0.01630.9451-0.2264-0.04930.671-0.11611.6292-29.8451-12.661318.7718
34.60721.15071.09823.2936-0.55443.25520.11910.3511-0.1398-1.1127-0.05540.03350.27920.0920.00381.2512-0.30680.32150.6501-0.19040.7796-17.7479-44.887920.0468
42.42770.666-0.70261.46380.26221.9972-0.13670.69910.0495-1.41620.25691.70420.1617-1.59460.01741.3531-0.4496-0.23451.15360.01431.5525-40.9247-38.47817.251
53.13960.84881.1193.41151.32772.230.056-0.3366-0.91780.3445-0.15581.27020.7887-0.7569-0.09391.4389-0.03880.57040.73630.36791.71230.7188-69.84373.008
62.62340.03941.69054.3593-1.15524.5565-0.1982-0.5045-0.1140.7719-0.2258-0.1202-0.09090.2391-0.00061.37720.23630.47160.85610.17240.969820.3675-56.790410.3873
71.063-0.01281.17980.9961-0.46971.7132-0.3403-1.1182-0.14441.19940.02430.456-0.1845-0.092-0.2792.29450.11430.96821.48190.22850.283911.1975-55.65832.8766
81.87150.03450.96091.84291.64591.8979-0.9889-0.80960.12230.82860.3573-0.5227-0.66410.22460.0011.54440.3758-0.21731.56880.30681.143752.8847-58.47253.3219
91.23120.23760.52960.04560.1020.2283-0.0293-0.8389-0.61130.3172-0.84360.2404-0.081-0.8685-0.03622.2470.71330.03341.4991-0.62562.226840.0004-40.08840.214
103.6911-0.77850.01092.8446-0.17092.9836-0.0861-0.1674-0.53660.31510.0363-0.11270.05890.5399-0.06531.01090.620.35170.65810.26651.159547.456-68.6489-17.7709
114.1346-0.3181-0.46574.7902-2.23314.7960.12610.1841-0.3198-0.01270.03990.3013-0.30880.14590.00280.87020.17320.17330.51620.04610.815632.2984-50.2802-23.0644
123.93330.4141.09823.9247-0.22644.6342-0.0017-0.2430.2650.6346-0.1258-0.2224-0.71210.4069-0.01231.58130.30910.49190.45410.09120.77476.3226-23.6941-5.7737
130.0145-0.02250.06140.3286-0.01730.23910.14620.5162-0.71280.1783-0.61680.4315-1.5453-0.5564-0.01171.55910.31330.39060.9808-0.20311.2787-4.091-6.6166-10.3552
143.30361.57360.85514.4687-1.6233.71720.1908-0.0601-0.1420.02080.2450.64920.2201-0.5682-01.1860.21810.34350.99960.00981.1249-9.6916-38.3025-17.3769
152.1273-0.50031.37270.4816-0.87661.74180.32760.17550.74630.2307-0.11121.8423-0.519-1.75270.06321.20590.56070.33291.92090.09311.8449-25.6349-20.8626-16.5278
162.48820.23362.29591.8057-0.64782.53190.660.9132-2.02880.0445-0.69380.41760.85830.7672-0.01272.13020.60040.30320.96720.10652.192226.9885-96.03091.2502
171.006-0.8096-0.15021.1347-0.22331.32430.131-1.0504-0.30330.4838-0.0272-0.57511.15020.0087-0.00032.16750.2637-0.0032.0830.84941.778335.1072-88.079221.9576
181.94760.25640.63461.7850.4140.2766-0.1421-1.7487-0.60471.3467-0.08760.36241.3325-0.5311-0.66373.0795-0.17330.67262.68530.90121.772616.8383-95.681634.3433
191.0438-0.9005-0.35130.79240.34110.70320.19520.3127-0.1931-0.0891-0.5982-0.44120.04470.68880.05431.2298-0.30280.55150.94380.12940.9405-3.2002-39.101726.3419
201.7293-0.49211.14981.5806-0.7240.87870.42030.4883-0.5016-0.9694-0.04340.05760.0874-0.2563-0.05981.5410.39250.45820.51710.36560.98929.6672-53.7694-5.8275
210.0872-0.2190.24480.5529-0.6270.70560.45450.51290.4699-0.5152-0.03590.31431.76030.51220.19891.7850.38030.01470.93480.27811.44225.6717-71.3336-2.8548
220.19710.1911-0.07950.2550.01720.1557-0.2884-0.663-1.0710.83310.1562-0.4525-0.8422-0.03510.01191.79170.39690.29811.00980.42191.537337.6537-77.35423.3536
230.65260.345-0.43271.12440.47111.7152-0.4096-0.1189-0.54290.0602-0.3947-0.55490.16440.0257-0.19731.3080.83680.26061.85570.32142.329263.5921-78.0459-8.4466
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A AND (RESID 5:32 OR RESID 70:144 OR RESID 338:375)
2X-RAY DIFFRACTION2CHAIN A AND (RESID 33:69)
3X-RAY DIFFRACTION3CHAIN A AND (RESID 145:180 OR RESID 270:337)
4X-RAY DIFFRACTION4CHAIN A AND (RESID 181:269)
5X-RAY DIFFRACTION5CHAIN B AND (RESID 5:33 OR RESID 70:144 OR RESID 338:375)
6X-RAY DIFFRACTION6CHAIN B AND (RESID 145:180 OR RESID 270:337)
7X-RAY DIFFRACTION7CHAIN B AND (RESID 181:269)
8X-RAY DIFFRACTION8CHAIN C AND (RESID 5:33 OR RESID 69:144 OR RESID 338:375)
9X-RAY DIFFRACTION9CHAIN C AND (RESID 34:68)
10X-RAY DIFFRACTION10CHAIN C AND (RESID 145:180 OR RESID 270:337)
11X-RAY DIFFRACTION11CHAIN C AND (RESID 181:269)
12X-RAY DIFFRACTION12CHAIN D AND (RESID 5:32 OR RESID 70:144 OR RESID 338:375)
13X-RAY DIFFRACTION13CHAIN D AND (RESID 33:69)
14X-RAY DIFFRACTION14CHAIN D AND (RESID 145:180 OR RESID 270:337)
15X-RAY DIFFRACTION15CHAIN D AND (RESID 181:269)
16X-RAY DIFFRACTION16CHAIN E AND (RESID 5:32 OR RESID 70:144 OR RESID 338:375)
17X-RAY DIFFRACTION17CHAIN E AND (RESID 145:180 OR RESID 270:337)
18X-RAY DIFFRACTION18CHAIN E AND (RESID 181:269)
19X-RAY DIFFRACTION19CHAIN M AND (RESID 63:102)
20X-RAY DIFFRACTION20CHAIN M AND (RESID 103:134)
21X-RAY DIFFRACTION21CHAIN M AND (RESID 135:143)
22X-RAY DIFFRACTION22CHAIN M AND (RESID 144:167)
23X-RAY DIFFRACTION23CHAIN M AND (RESID 168:183)

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