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- PDB-5dif: Crystal Structure of CPEB4 NES Peptide in complex with CRM1-Ran-RanBP1 -

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Basic information

Entry
Database: PDB / ID: 5dif
TitleCrystal Structure of CPEB4 NES Peptide in complex with CRM1-Ran-RanBP1
Components
  • Cytoplasmic polyadenylation element-binding protein 4
  • Exportin-1
  • 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


cellular response to decreased oxygen levels / tRNA re-export from nucleus / Transport of Mature mRNA derived from an Intron-Containing Transcript / pre-miRNA export from nucleus / RNA nuclear export complex / snRNA import into nucleus / Regulation of HSF1-mediated heat shock response / nuclear export signal receptor activity / Transcriptional and post-translational regulation of MITF-M expression and activity / manchette ...cellular response to decreased oxygen levels / tRNA re-export from nucleus / Transport of Mature mRNA derived from an Intron-Containing Transcript / pre-miRNA export from nucleus / RNA nuclear export complex / snRNA import into nucleus / Regulation of HSF1-mediated heat shock response / nuclear export signal receptor activity / Transcriptional and post-translational regulation of MITF-M expression and activity / manchette / cellular response to mineralocorticoid stimulus / translation factor activity, RNA binding / Regulation of cholesterol biosynthesis by SREBP (SREBF) / tRNA export from nucleus / importin-alpha family protein binding / SUMOylation of SUMOylation proteins / protein localization to kinetochore / spindle pole body / Rev-mediated nuclear export of HIV RNA / Nuclear import of Rev protein / U4 snRNA binding / nuclear export / SUMOylation of RNA binding proteins / protein localization to nucleolus / NEP/NS2 Interacts with the Cellular Export Machinery / RNA export from nucleus / tRNA processing in the nucleus / GTP metabolic process / Postmitotic nuclear pore complex (NPC) reformation / SUMOylation of chromatin organization proteins / nuclear import signal receptor activity / MicroRNA (miRNA) biogenesis / DNA metabolic process / MAPK6/MAPK4 signaling / dynein intermediate chain binding / mitotic sister chromatid segregation / ribosomal large subunit export from nucleus / U5 snRNA binding / spermatid development / viral process / U2 snRNA binding / U6 snRNA binding / positive regulation of protein binding / sperm flagellum / nuclear pore / mRNA export from nucleus / U1 snRNA binding / ribosomal subunit export from nucleus / cellular response to glucose starvation / negative regulation of cytoplasmic translation / ribosomal small subunit export from nucleus / centriole / ionotropic glutamate receptor signaling pathway / protein export from nucleus / GTPase activator activity / mRNA regulatory element binding translation repressor activity / response to ischemia / mRNA 3'-UTR binding / mitotic spindle organization / male germ cell nucleus / hippocampus development / cellular response to amino acid stimulus / Transcriptional regulation by small RNAs / G1/S transition of mitotic cell cycle / recycling endosome / kinetochore / positive regulation of protein import into nucleus / small GTPase binding / protein import into nucleus / GDP binding / nuclear envelope / melanosome / mitotic cell cycle / ribosome binding / G protein activity / growth cone / actin cytoskeleton organization / midbody / ubiquitin-dependent protein catabolic process / dendritic spine / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / negative regulation of neuron apoptotic process / neuron projection / postsynaptic density / cadherin binding / protein heterodimerization activity / protein domain specific binding / cell division / GTPase activity / synapse / dendrite / chromatin binding / chromatin / GTP binding / protein-containing complex binding / nucleolus / perinuclear region of cytoplasm / magnesium ion binding / endoplasmic reticulum / protein-containing complex
Similarity search - Function
Cytoplasmic polyadenylation element-binding protein, ZZ domain / Cytoplasmic polyadenylation element-binding protein / CEBP, ZZ domain superfamily / Cytoplasmic polyadenylation element-binding protein ZZ domain / RNA recognition motif / Ran-specific GTPase-activating protein 1, Ran-binding domain / Exportin-1, repeat 3 / Chromosome region maintenance repeat / Exportin-1, repeat 2 / Chromosome region maintenance or exportin repeat ...Cytoplasmic polyadenylation element-binding protein, ZZ domain / Cytoplasmic polyadenylation element-binding protein / CEBP, ZZ domain superfamily / Cytoplasmic polyadenylation element-binding protein ZZ domain / RNA recognition motif / Ran-specific GTPase-activating protein 1, Ran-binding domain / Exportin-1, repeat 3 / Chromosome region maintenance repeat / Exportin-1, repeat 2 / Chromosome region maintenance or exportin repeat / CRM1 / Exportin repeat 2 / CRM1 / Exportin repeat 3 / CRM1 C terminal / Exportin-1, C-terminal / 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 / Ran GTPase / Small GTPase Ran-type domain profile. / Importin-beta N-terminal domain / Importin-beta N-terminal domain / Importin-beta N-terminal domain profile. / 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 / RNA recognition motif / Eukaryotic RNA Recognition Motif (RRM) profile. / RNA recognition motif domain / RNA-binding domain superfamily / Rab subfamily of small GTPases / Armadillo-like helical / Small GTP-binding protein domain / PH-like domain superfamily / Armadillo-type fold / Roll / Nucleotide-binding alpha-beta plait domain superfamily / P-loop containing nucleotide triphosphate hydrolases / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / 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 / Cytoplasmic polyadenylation element-binding protein 4
Similarity search - Component
Biological speciesHomo sapiens (human)
Saccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.092 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 / Other
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 1.6Mar 6, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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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: Cytoplasmic polyadenylation element-binding protein 4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)164,09614
Polymers162,8704
Non-polymers1,22710
Water11,890660
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area12390 Å2
ΔGint-71 kcal/mol
Surface area57640 Å2
MethodPISA
Unit cell
Length a, b, c (Å)105.993, 105.993, 304.063
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number96
Space group name H-MP43212
Components on special symmetry positions
IDModelComponents
11C-1255-

HOH

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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): BL21(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 / Chromosome region maintenance protein 1 / Karyopherin-124


Mass: 117458.781 Da / Num. of mol.: 1 / Mutation: V441D,D536G,T539C,V540E,K541Q,Y1022C
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 Cytoplasmic polyadenylation element-binding protein 4


Mass: 2130.339 Da / Num. of mol.: 1 / Fragment: Nuclear Export Signal
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CPEB4 / Plasmid: pMal / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q17RY0*PLUS

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Non-polymers , 5 types, 670 molecules

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


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


Mass: 92.094 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C3H8O3
#8: Chemical ChemComp-CL / CHLORIDE ION


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


Mass: 18.015 Da / Num. of mol.: 660 / 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: 2.62 Å3/Da / Density % sol: 53.08 %
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: Nov 24, 2014
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: 2.1→50 Å / Num. obs: 102512 / % possible obs: 99.5 % / Redundancy: 6 % / Biso Wilson estimate: 25.79 Å2 / Rmerge(I) obs: 0.081 / Rpim(I) all: 0.035 / Rrim(I) all: 0.084 / Χ2: 0.886 / Net I/av σ(I): 19.494 / Net I/σ(I): 7.9 / Num. measured all: 619523
Reflection shell

Diffraction-ID: 1 / Rejects: _

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allCC1/2Rpim(I) allΧ2% possible allRrim(I) all
2.1-2.146.10.98750570.6320.4340.874100
2.14-2.186.10.86550840.6750.3790.8861000.947
2.18-2.226.10.75450870.7370.3320.91000.827
2.22-2.266.10.61350600.8070.270.9391000.672
2.26-2.316.10.51650820.8620.2270.9111000.566
2.31-2.376.10.42850690.8960.1880.8991000.47
2.37-2.426.10.36150890.9230.1580.9071000.396
2.42-2.496.10.30550590.9340.1340.9091000.334
2.49-2.566.10.24751030.9540.1080.89899.90.271
2.56-2.656.10.20751240.9680.090.8781000.227
2.65-2.746.10.16751240.9740.0730.8621000.183
2.74-2.856.10.13250780.9840.0570.83899.90.145
2.85-2.986.10.10151280.9890.0430.80699.90.11
2.98-3.146.10.07951450.9920.0340.81699.70.087
3.14-3.336.10.06251440.9940.0260.84999.70.068
3.33-3.5960.05251370.9960.0220.94399.40.057
3.59-3.9560.0551920.9960.0211.18499.30.054
3.95-4.5260.04251590.9950.0181.1498.90.046
4.52-5.75.80.03252240.9970.0140.768980.035
5.7-505.70.02253670.9980.010.51795.40.024

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Processing

Software
NameVersionClassification
PHENIXrefinement
HKL-2000data collection
HKL-2000data scaling
PDB_EXTRACT3.15data extraction
HKL-3000data reduction
PHENIXphasing
RefinementResolution: 2.092→40.193 Å / SU ML: 0.21 / Cross valid method: FREE R-VALUE / σ(F): 1.45 / Phase error: 20.69 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2084 4920 4.99 %Random selection
Rwork0.1697 93739 --
obs0.1716 98659 95.74 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 183.11 Å2 / Biso mean: 39.751 Å2 / Biso min: 10.44 Å2
Refinement stepCycle: final / Resolution: 2.092→40.193 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10905 0 76 660 11641
Biso mean--50.33 36.52 -
Num. residues----1351
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00311565
X-RAY DIFFRACTIONf_angle_d0.68915688
X-RAY DIFFRACTIONf_chiral_restr0.0281780
X-RAY DIFFRACTIONf_plane_restr0.0032003
X-RAY DIFFRACTIONf_dihedral_angle_d12.8524347
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.092-2.11580.2703820.23811793187555
2.1158-2.14070.30651430.23262172231569
2.1407-2.16680.26231180.22962608272680
2.1668-2.19420.26521410.23132903304491
2.1942-2.22310.28781430.2183122326596
2.2231-2.25350.24621690.21123173334298
2.2535-2.28570.25621660.20443136330299
2.2857-2.31980.22971670.195732343401100
2.3198-2.35610.23571510.201332433394100
2.3561-2.39470.22571660.194332133379100
2.3947-2.4360.25051380.192432213359100
2.436-2.48030.25681800.185632073387100
2.4803-2.5280.22821620.183632553417100
2.528-2.57950.23211610.179432353396100
2.5795-2.63560.23841840.181332133397100
2.6356-2.69690.23111800.181132253405100
2.6969-2.76440.2131680.179832313399100
2.7644-2.83910.22121480.188632713419100
2.8391-2.92260.22141840.190232343418100
2.9226-3.01690.24091780.189132453423100
3.0169-3.12470.22681800.189732503430100
3.1247-3.24970.23881630.179532633426100
3.2497-3.39760.22551890.173832323421100
3.3976-3.57660.20441730.16423266343999
3.5766-3.80050.17681980.1533250344899
3.8005-4.09370.1721900.13783259344999
4.0937-4.50520.17751690.12353276344599
4.5052-5.15590.14841880.12083279346798
5.1559-6.49150.16621760.15693310348697
6.4915-40.20070.17841650.15073420358594
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)
12.2219-0.73841.65032.23531.06994.15510.0178-0.1090.2098-0.06230.0867-0.4366-0.37040.53660.07750.1093-0.1090.02060.2796-0.09570.28468.753145.658938.0989
21.338-0.31790.17681.95130.37061.13650.03420.22350.0289-0.30460.1722-0.4319-0.45110.4411-0.17280.2073-0.11060.08270.2752-0.05080.29449.466649.738231.4023
31.7964-0.5853-0.00490.8846-0.28010.98870.05580.0491-0.17860.09140.0536-0.47050.0740.3109-0.12070.0877-0.0232-0.01070.2259-0.06230.37957.944837.05536.5281
41.8241-1.19560.83313.037-1.40645.40840.02870.1547-0.4055-0.24910.0772-0.08740.5020.0526-0.10130.1101-0.00990.01690.1461-0.05340.2617-2.629334.241537.3382
51.2045-0.154-1.36992.3422-0.34761.7930.04640.0395-0.0735-0.10860.01660.1390.0233-0.3152-0.04130.11530.0018-0.0190.172-0.04090.2314-6.288342.368438.3493
61.71770.45280.47332.21520.16551.82650.06420.02370.4001-0.03350.03250.0285-0.68170.1493-0.11710.2753-0.03770.03940.1757-0.01810.27560.453956.559838.6589
71.5354-1.5979-2.14552.40362.29913.37990.0440.4681-0.0015-0.31940.0992-0.6855-0.13550.0214-0.11340.6798-0.49450.10620.9728-0.10570.49720.830172.80517.4106
84.04755.1599-1.72587.2392-1.42761.69740.20910.18620.5422-0.21120.4266-0.8702-0.14730.7258-0.49860.5465-0.2160.15710.8321-0.21840.616917.38361.98254.171
92.3292-0.88020.32615.50851.31764.3183-0.33920.0986-0.29110.37950.13480.62290.0499-0.20990.1790.3229-0.08430.06190.3851-0.08360.5907-0.928656.238911.0339
100.5142-0.2742-1.53940.20680.94344.82430.0099-0.0882-0.05220.01750.01630.0098-0.31520.2023-0.0880.8554-0.18740.14040.52450.02460.71311.83882.383750.8635
112.16610.68920.59192.63630.01121.44330.0074-0.02580.08940.2945-0.05220.2493-0.48790.45490.0660.4343-0.16470.10220.3125-0.00410.34396.927567.930620.9519
121.85441.41050.272.79331.18550.6032-0.10390.18750.0608-0.45980.11130.087-0.9560.45520.0460.5372-0.28870.06940.3509-0.00040.36177.244670.588612.0675
131.02390.2108-0.01631.32330.14140.8858-0.0603-0.105-0.00580.42480.3052-0.66730.37720.6940.05720.06960.1257-0.15950.4577-0.13610.56317.579425.121348.7188
141.4099-0.665-0.22982.90971.51951.885-0.1103-0.2207-0.03080.39890.02640.1060.1843-0.03090.07050.25030.0337-0.00650.20470.02080.2271-7.692426.427760.7317
151.9865-0.46390.66961.6766-0.37242.82870.04250.0855-0.07470.03560.0582-0.00490.0517-0.1001-0.07880.09230.0010.00620.1229-0.05020.139-22.645646.988554.3974
160.901-0.06960.03640.7292-0.24143.63340.4066-0.03270.366-0.15370.1322-0.0285-2.0274-0.98950.23980.52280.45070.10670.33860.14770.2418-33.590163.780821.3721
171.0826-0.83370.26311.8051-0.37491.27340.00960.0955-0.0406-0.04230.09670.018-0.0473-0.0493-0.09420.0980.00470.0180.2417-0.02220.1347-15.888539.38950.5944
181.3968-0.7870.90891.4791-0.89372.72480.12320.0139-0.3034-0.21570.05560.23850.2374-0.0891-0.12370.1409-0.0007-0.01630.1825-0.03990.2882-6.975210.199120.4419
192.44190.1615-0.9264.0530.44450.97550.1348-0.01110.49220.06890.20290.0322-0.3529-0.2141-0.14541.18870.67160.15910.6419-0.02550.5344-39.237675.69827.3951
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 8 through 22 )A0
2X-RAY DIFFRACTION2chain 'A' and (resid 23 through 66 )A0
3X-RAY DIFFRACTION3chain 'A' and (resid 67 through 91 )A0
4X-RAY DIFFRACTION4chain 'A' and (resid 92 through 109 )A0
5X-RAY DIFFRACTION5chain 'A' and (resid 110 through 148 )A0
6X-RAY DIFFRACTION6chain 'A' and (resid 149 through 179 )A0
7X-RAY DIFFRACTION7chain 'A' and (resid 180 through 193 )A0
8X-RAY DIFFRACTION8chain 'A' and (resid 194 through 205 )A0
9X-RAY DIFFRACTION9chain 'A' and (resid 206 through 216 )A0
10X-RAY DIFFRACTION10chain 'B' and (resid 63 through 82 )B0
11X-RAY DIFFRACTION11chain 'B' and (resid 83 through 139 )B0
12X-RAY DIFFRACTION12chain 'B' and (resid 140 through 200 )B0
13X-RAY DIFFRACTION13chain 'C' and (resid -1 through 167 )C0
14X-RAY DIFFRACTION14chain 'C' and (resid 168 through 268 )C0
15X-RAY DIFFRACTION15chain 'C' and (resid 269 through 478 )C0
16X-RAY DIFFRACTION16chain 'C' and (resid 479 through 692 )C0
17X-RAY DIFFRACTION17chain 'C' and (resid 693 through 897 )C0
18X-RAY DIFFRACTION18chain 'C' and (resid 898 through 1053 )C0
19X-RAY DIFFRACTION19chain 'D' and (resid 379 through 393 )D0

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