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- PDB-5di9: Crystal Structure of hRio2 NES Reverse Mutant Peptide in complex ... -

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Basic information

Entry
Database: PDB / ID: 5di9
TitleCrystal Structure of hRio2 NES Reverse Mutant Peptide in complex with CRM1-Ran-RanBP1
Components
  • Engineered Nuclear Export Signal Peptide (hRio2 NES reverse mutant)
  • Exportin-1Karyopherin
  • GTP-binding nuclear protein Ran
  • Ran-specific GTPase-activating protein 1
KeywordsTRANSPORT PROTEIN / Peptides / HEAT repeat / Nuclear Export signal / Exportin-1 / Nuclear Transport
Function / homology
Function and homology information


MAPK6/MAPK4 signaling / RNA nuclear export complex / nuclear export signal receptor activity / pre-miRNA export from nucleus / snRNA import into nucleus / cellular response to mineralocorticoid stimulus / manchette / Regulation of cholesterol biosynthesis by SREBP (SREBF) / importin-alpha family protein binding / U4 snRNA binding ...MAPK6/MAPK4 signaling / RNA nuclear export complex / nuclear export signal receptor activity / pre-miRNA export from nucleus / snRNA import into nucleus / cellular response to mineralocorticoid stimulus / manchette / Regulation of cholesterol biosynthesis by SREBP (SREBF) / importin-alpha family protein binding / U4 snRNA binding / spindle pole body / RNA export from nucleus / protein localization to kinetochore / nuclear export / protein localization to nucleolus / Rev-mediated nuclear export of HIV RNA / Nuclear import of Rev protein / GTP metabolic process / NEP/NS2 Interacts with the Cellular Export Machinery / tRNA processing in the nucleus / Postmitotic nuclear pore complex (NPC) reformation / MicroRNA (miRNA) biogenesis / nuclear import signal receptor activity / DNA metabolic process / NLS-bearing protein import into nucleus / dynein intermediate chain binding / ribosomal subunit export from nucleus / spermatid development / mitotic sister chromatid segregation / ribosomal small subunit export from nucleus / ribosomal large subunit export from nucleus / U5 snRNA binding / sperm flagellum / U2 snRNA binding / U6 snRNA binding / mRNA export from nucleus / nuclear pore / U1 snRNA binding / protein export from nucleus / centriole / viral process / GTPase activator activity / G protein activity / mitotic spindle organization / male germ cell nucleus / hippocampus development / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / Transcriptional regulation by small RNAs / G1/S transition of mitotic cell cycle / kinetochore / recycling endosome / small GTPase binding / positive regulation of protein import into nucleus / protein import into nucleus / GDP binding / melanosome / mitotic cell cycle / nuclear envelope / positive regulation of protein binding / midbody / ubiquitin-dependent protein catabolic process / actin cytoskeleton organization / cadherin binding / protein heterodimerization activity / cell division / protein domain specific binding / GTPase activity / chromatin binding / chromatin / GTP binding / nucleolus / perinuclear region of cytoplasm / magnesium ion binding / protein-containing complex / RNA binding / extracellular exosome / nucleoplasm / membrane / nucleus / cytosol / cytoplasm
Similarity search - Function
Ran-specific GTPase-activating protein 1, Ran-binding domain / Exportin-1, C-terminal / Exportin-1, repeat 3 / Chromosome region maintenance repeat / Exportin-1, repeat 2 / CRM1 C terminal / Chromosome region maintenance or exportin repeat / CRM1 / Exportin repeat 2 / CRM1 / Exportin repeat 3 / CRM1 C terminal ...Ran-specific GTPase-activating protein 1, Ran-binding domain / Exportin-1, C-terminal / Exportin-1, repeat 3 / Chromosome region maintenance repeat / Exportin-1, repeat 2 / CRM1 C terminal / Chromosome region maintenance or exportin repeat / CRM1 / Exportin repeat 2 / CRM1 / Exportin repeat 3 / CRM1 C terminal / Exportin-1/5 / Exportin-1/Importin-beta-like / Exportin 1-like protein / Ran binding protein RanBP1-like / Ran binding domain / RanBP1 domain / Ran binding domain type 1 profile. / Ran-binding domain / small GTPase Ran family profile. / Ran GTPase / Importin-beta N-terminal domain profile. / Importin-beta N-terminal domain / Importin-beta N-terminal domain / Importin-beta, N-terminal domain / Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) / PH-domain like / Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases / Rho (Ras homology) subfamily of Ras-like small GTPases / Ras subfamily of RAS small GTPases / Small GTPase / Ras family / Rab subfamily of small GTPases / Armadillo-like helical / Small GTP-binding protein domain / PH-like domain superfamily / Armadillo-type fold / P-loop containing nucleotide triphosphate hydrolases / Roll / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / Exportin-1 / Ran-specific GTPase-activating protein 1 / GTP-binding nuclear protein Ran
Similarity search - Component
Biological speciesHomo sapiens (human)
Saccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.28 Å
AuthorsFung, H.Y. / Chook, Y.M.
Funding support Hong Kong, United States, 6items
OrganizationGrant numberCountry
Croucher FoundationStudent Scholarship Hong Kong
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM069909 United States
Cancer Prevention and Research Institute of Texas (CPRIT)RP120352 United States
University of Texas SouthwesternEndowed Scholars Program United States
Welch FoundationI-1532 United States
Leukemia & Lymphoma SocietyScholar Award United States
CitationJournal: Elife / Year: 2015
Title: Structural determinants of nuclear export signal orientation in binding to exportin CRM1.
Authors: Fung, H.Y. / Fu, S.C. / Brautigam, C.A. / Chook, Y.M.
History
DepositionAug 31, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 16, 2015Provider: repository / Type: Initial release
Revision 1.1Oct 21, 2015Group: Database references
Revision 1.2Sep 20, 2017Group: Author supporting evidence / Derived calculations / Category: pdbx_audit_support / pdbx_struct_oper_list
Item: _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation
Revision 1.3Sep 27, 2017Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4Apr 24, 2019Group: Author supporting evidence / Data collection / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.5Dec 25, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.6Sep 27, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_conn_type
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_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_ptnr1_label_alt_id / _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_conn_type.id
Revision 1.7Nov 15, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: GTP-binding nuclear protein Ran
B: Ran-specific GTPase-activating protein 1
C: Exportin-1
D: Engineered Nuclear Export Signal Peptide (hRio2 NES reverse mutant)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)164,19712
Polymers163,1824
Non-polymers1,0168
Water6,449358
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area12010 Å2
ΔGint-111 kcal/mol
Surface area57770 Å2
MethodPISA
Unit cell
Length a, b, c (Å)106.692, 106.692, 304.497
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number96
Space group name H-MP43212

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Components

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Protein , 3 types, 3 molecules ABC

#1: Protein GTP-binding nuclear protein Ran / Androgen receptor-associated protein 24 / GTPase Ran / Ras-like protein TC4 / Ras-related nuclear protein


Mass: 26758.564 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RAN, ARA24, OK/SW-cl.81 / Plasmid: pET15 / Production host: Escherichia coli (E. coli) / Strain (production host): BL219(DE3) / References: UniProt: P62826
#2: Protein Ran-specific GTPase-activating protein 1 / Chromosome stability protein 20 / Perinuclear array-localized protein / Ran-binding protein 1 / RANBP1


Mass: 16521.867 Da / Num. of mol.: 1 / Fragment: RanDB1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Strain: ATCC 204508 / S288c / Gene: YRB1, CST20, HTN1, SFO1, YDR002W, YD8119.08 / Plasmid: pGex4T3 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P41920
#3: Protein Exportin-1 / Karyopherin / Chromosome region maintenance protein 1 / Karyopherin-124


Mass: 117458.781 Da / Num. of mol.: 1
Mutation: V441D,D536G,T539C,V540E,K541Q,Y1022C, delta 377-413
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c / Gene: CRM1, KAP124, XPO1, YGR218W, G8514 / Plasmid: pGex4T3 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P30822

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Protein/peptide , 1 types, 1 molecules D

#4: Protein/peptide Engineered Nuclear Export Signal Peptide (hRio2 NES reverse mutant)


Mass: 2442.496 Da / Num. of mol.: 1 / Fragment: Nuclear Export Signal
Source method: isolated from a genetically manipulated source
Details: Engineered mutant sequence of CPEPB4 NES / Source: (gene. exp.) Homo sapiens (human) / Gene: CPEB4 / Plasmid: pMal / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)

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Non-polymers , 6 types, 366 molecules

#5: Chemical ChemComp-GNP / PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / 5'-Guanylyl imidodiphosphate


Mass: 522.196 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H17N6O13P3
Comment: GppNHp, GMPPNP, energy-carrying molecule analogue*YM
#6: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#7: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C3H8O3
#8: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn
#9: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#10: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 358 / 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: 2.66 Å3/Da / Density % sol: 53.67 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.4
Details: 17% PEG3350, 100mM Bis-Tris pH6.4, 200mM NH4NO3, 10mM Spermine HCl

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Data collection

DiffractionMean temperature: 93 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.9795 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Feb 20, 2015
RadiationMonochromator: Rosenbaum-Rock high-resolution double-crystal monochromator
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.28→50 Å / Num. obs: 127043 / % possible obs: 98 % / Redundancy: 7 % / Biso Wilson estimate: 28.49 Å2 / Rmerge(I) obs: 0.09 / Rpim(I) all: 0.035 / Rrim(I) all: 0.092 / Χ2: 0.899 / Net I/av σ(I): 22.5 / Net I/σ(I): 8.3 / Num. measured all: 557247
Reflection shell

Diffraction-ID: 1 / Rejects: 0

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allCC1/2Rpim(I) allΧ2% possible allRrim(I) all
2.28-2.3270.97139740.7760.3860.92199.2
2.32-2.366.90.82739590.80.330.91499.10.892
2.36-2.4170.71839480.8550.2850.92199.20.774
2.41-2.4670.63539270.8890.2520.909990.685
2.46-2.5170.5439770.9120.2140.892990.582
2.51-2.5770.45139650.9380.1780.89698.90.486
2.57-2.6370.38339670.9510.1520.89198.80.413
2.63-2.770.33239760.9610.1310.89798.80.358
2.7-2.7870.26839850.9680.1060.86798.70.289
2.78-2.8770.21439590.9810.0840.85798.60.231
2.87-2.9870.17639780.9860.0690.85498.50.19
2.98-3.0970.1439760.990.0550.8698.30.15
3.09-3.247.10.10739790.9930.0420.86398.10.115
3.24-3.4170.08739660.9940.0340.9297.90.094
3.41-3.6270.07339820.9940.0291.05897.60.079
3.62-3.970.06639740.9950.0261.24797.40.071
3.9-4.2970.05239980.9970.021.12996.90.056
4.29-4.916.80.03940060.9980.0150.93696.60.042
4.91-6.1970.03240470.9990.0130.62196.20.035
6.19-506.70.02541840.9990.010.52493.40.027

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Processing

Software
NameVersionClassification
PHENIXrefinement
HKL-2000data scaling
PDB_EXTRACT3.15data extraction
Cootmodel building
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4HB2

4hb2


Resolution: 2.28→37.721 Å / SU ML: 0.22 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 22.44 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2115 3179 2.5 %Random selection
Rwork0.1683 123864 --
obs0.1694 127043 82.82 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 155.93 Å2 / Biso mean: 43.9482 Å2 / Biso min: 14.35 Å2
Refinement stepCycle: final / Resolution: 2.28→37.721 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10876 0 59 358 11293
Biso mean--46.41 35.44 -
Num. residues----1347
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00611243
X-RAY DIFFRACTIONf_angle_d0.83515214
X-RAY DIFFRACTIONf_chiral_restr0.0321730
X-RAY DIFFRACTIONf_plane_restr0.0031934
X-RAY DIFFRACTIONf_dihedral_angle_d13.2494202
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 23

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.2786-2.31260.2764860.24743267335350
2.3126-2.34870.2935860.23293340342652
2.3487-2.38720.2811890.23493481357053
2.3872-2.42840.2303920.22793607369955
2.4284-2.47250.2531960.223709380557
2.4725-2.52010.26111000.2114011411162
2.5201-2.57150.27011130.20464301441466
2.5715-2.62740.24971290.20514671480072
2.6274-2.68850.22181280.20845289541781
2.6885-2.75570.27641580.20495932609091
2.7557-2.83020.2441490.21136273642296
2.8302-2.91350.23891660.20236381654798
2.9135-3.00750.27141620.19326405656799
3.0075-3.11490.20861640.19436371653598
3.1149-3.23960.27741680.18866399656798
3.2396-3.38690.2051630.18146360652398
3.3869-3.56540.211650.17166411657698
3.5654-3.78860.18681660.15236309647597
3.7886-4.08080.17031590.14336305646497
4.0808-4.49080.17421560.12366278643497
4.4908-5.13930.16011660.11796288645497
5.1393-6.46960.21781570.15136295645297
6.4696-37.72650.18121610.13956181634295
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)
12.1792-0.84440.80722.14581.5235.7302-0.25950.23970.0524-0.28290.2785-0.5268-0.41520.4633-0.04740.1736-0.02410.00680.2771-0.07440.36267.960844.497437.9198
22.0016-1.927-0.15182.60221.1921.48660.01950.5517-0.1773-0.69180.0408-0.3757-0.26360.4027-0.08830.2745-0.08110.13610.4452-0.14340.39337.24846.49925.2007
31.2671-0.8157-0.05844.61680.70842.47010.1290.12940.0576-0.09850.2134-0.8685-0.54350.6305-0.34430.2326-0.10870.06820.367-0.12640.514311.771953.095538.1109
42.0295-1.0146-0.36731.0669-0.38130.63390.05090.3052-0.3680.00150.0267-0.53250.08220.3252-0.08340.14310.0268-0.03170.2959-0.11660.54518.118737.280437.2095
51.0173-0.3544-0.23922.7464-1.08093.770.02450.126-0.4033-0.18990.0418-0.20280.34320.068-0.04510.13480.0375-0.00420.2134-0.07330.3393-1.558434.165538.7031
61.08080.0273-1.46863.223-0.81153.79170.00130.1038-0.0288-0.10610.0460.0528-0.0256-0.4455-0.03510.15880.0211-0.0140.2492-0.06630.257-6.935542.979338.418
72.18810.24520.88413.18910.61574.150.02340.02180.2891-0.2332-0.0142-0.0605-0.89060.0278-0.00320.34410.00050.02540.2516-0.03620.31580.599556.658638.9399
84.61190.6502-0.264.08380.20753.3048-0.19250.6476-0.2114-0.76970.5101-0.89540.27020.0138-0.24350.8215-0.60520.19181.191-0.31080.638220.03373.817320.4525
95.09311.3112-0.85911.7514-1.26171.91940.5156-0.01410.3294-0.620.2853-1.0466-0.16580.7118-0.70230.7424-0.16540.20921.1263-0.31090.743818.772862.71244.5044
104.1604-0.72180.69195.30170.29973.0298-0.1641-0.12610.09020.07290.31180.30080.1551-0.2846-0.12570.3838-0.13530.1140.4362-0.09840.5148-1.501656.414212.0608
110.96550.52490.10830.8028-0.50620.6216-0.10080.04320.06870.11680.0102-0.3045-0.26580.30420.07750.9675-0.2504-0.03050.5864-0.05290.70043.44680.75946.6365
123.3643-0.18450.43825.03410.34412.67880.03650.0261-0.15840.28270.07710.0775-0.28570.6512-0.07740.4299-0.16090.13950.4647-0.01050.35666.945863.246517.37
130.59450.47140.12971.1730.05380.0418-0.1070.05650.1171-0.0232-0.00170.2281-1.01530.77210.10.7646-0.34140.18070.4779-0.0230.43877.476471.381319.573
142.76572.14470.12053.0881.38861.1917-0.16570.05820.2291-0.4130.17210.1041-1.01390.71150.04350.656-0.27870.11760.5495-0.04020.45117.864371.415913.8068
151.518-0.1122-0.06881.76850.42990.994-0.1242-0.13060.01060.55710.2434-0.76260.34790.3687-0.02630.25160.1315-0.24950.3438-0.07170.60359.994324.882253.1037
162.0351-0.82510.62582.2542-0.48253.0385-0.00610.0055-0.07990.08090.05840.0394-0.0008-0.2417-0.05380.1717-0.0008-0.00360.2261-0.06290.1301-22.843747.136754.8582
171.2152-0.42180.2341.7124-0.00493.37140.23140.05510.229-0.21-0.0489-0.0924-0.7695-0.3868-0.14150.49440.17690.06420.37490.01880.2449-34.10466.753426.1686
182.8382-1.3174-0.55511.84850.44231.83760.03470.21530.1282-0.25890.0991-0.0232-0.3579-0.1605-0.14250.30360.04320.03990.30760.02180.1533-22.35651.2526-1.1383
190.8541-0.82170.98331.4739-1.76712.72080.14840.0797-0.3198-0.1390.0970.28110.18440.0082-0.21390.19110.01410.02320.2501-0.09190.3284-8.825117.542614.5434
204.21862.0506-1.27365.5361-1.57124.69040.0556-0.07490.6318-0.48180.18050.5672-0.7589-0.2746-0.25490.95490.35360.05170.57280.06930.4429-38.971475.974728.4107
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 9 through 22 )A0
2X-RAY DIFFRACTION2chain 'A' and (resid 23 through 44 )A0
3X-RAY DIFFRACTION3chain 'A' and (resid 45 through 66 )A0
4X-RAY DIFFRACTION4chain 'A' and (resid 67 through 91 )A0
5X-RAY DIFFRACTION5chain 'A' and (resid 92 through 111 )A0
6X-RAY DIFFRACTION6chain 'A' and (resid 112 through 148 )A0
7X-RAY DIFFRACTION7chain 'A' and (resid 149 through 179 )A0
8X-RAY DIFFRACTION8chain 'A' and (resid 180 through 190 )A0
9X-RAY DIFFRACTION9chain 'A' and (resid 191 through 206 )A0
10X-RAY DIFFRACTION10chain 'A' and (resid 207 through 216 )A0
11X-RAY DIFFRACTION11chain 'B' and (resid 65 through 82 )B0
12X-RAY DIFFRACTION12chain 'B' and (resid 83 through 106 )B0
13X-RAY DIFFRACTION13chain 'B' and (resid 107 through 154 )B0
14X-RAY DIFFRACTION14chain 'B' and (resid 155 through 200 )B0
15X-RAY DIFFRACTION15chain 'C' and (resid 0 through 245 )C0
16X-RAY DIFFRACTION16chain 'C' and (resid 246 through 495 )C0
17X-RAY DIFFRACTION17chain 'C' and (resid 496 through 637 )C0
18X-RAY DIFFRACTION18chain 'C' and (resid 638 through 808 )C0
19X-RAY DIFFRACTION19chain 'C' and (resid 809 through 1052 )C0
20X-RAY DIFFRACTION20chain 'D' and (resid 5 through 20 )D0

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