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- PDB-5wqd: Crystal structure of TRF2 TRFH in complex with an NBS1 peptide -

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Basic information

Entry
Database: PDB / ID: 5wqd
TitleCrystal structure of TRF2 TRFH in complex with an NBS1 peptide
Components
  • Nibrin
  • Telomeric repeat-binding factor 2
KeywordsCELL CYCLE / Telomere / shelterin complex / DNA damage response
Function / homology
Function and homology information


telomere maintenance via telomere trimming / chromosomal region / telomeric 3' overhang formation / axonal transport of messenger ribonucleoprotein complex / negative regulation of beta-galactosidase activity / negative regulation of telomere single strand break repair / negative regulation of telomere maintenance via recombination / telomeric loop formation / Mre11 complex / negative regulation of telomere maintenance ...telomere maintenance via telomere trimming / chromosomal region / telomeric 3' overhang formation / axonal transport of messenger ribonucleoprotein complex / negative regulation of beta-galactosidase activity / negative regulation of telomere single strand break repair / negative regulation of telomere maintenance via recombination / telomeric loop formation / Mre11 complex / negative regulation of telomere maintenance / blastocyst growth / negative regulation of telomere maintenance via semi-conservative replication / negative regulation of exonuclease activity / negative regulation of telomeric D-loop disassembly / protection from non-homologous end joining at telomere / negative regulation of telomere capping / Sensing of DNA Double Strand Breaks / BRCA1-C complex / RNA-templated DNA biosynthetic process / negative regulation of t-circle formation / telomeric D-loop disassembly / t-circle formation / DNA double-strand break processing / shelterin complex / Telomere C-strand synthesis initiation / DNA strand resection involved in replication fork processing / double-stranded telomeric DNA binding / Telomere C-strand (Lagging Strand) Synthesis / regulation of telomere maintenance via telomerase / nuclear inclusion body / homologous recombination / Processive synthesis on the C-strand of the telomere / nuclear telomere cap complex / G-rich strand telomeric DNA binding / positive regulation of telomere maintenance / Polymerase switching on the C-strand of the telomere / isotype switching / HDR through MMEJ (alt-NHEJ) / Removal of the Flap Intermediate from the C-strand / anterograde axonal transport / Impaired BRCA2 binding to PALB2 / telomere capping / mitotic G2/M transition checkpoint / positive regulation of kinase activity / regulation of telomere maintenance / Defective homologous recombination repair (HRR) due to BRCA1 loss of function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function / Homologous DNA Pairing and Strand Exchange / Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA) / regulation of DNA-templated DNA replication initiation / Resolution of D-loop Structures through Holliday Junction Intermediates / DNA duplex unwinding / protein localization to chromosome, telomeric region / negative regulation of telomere maintenance via telomere lengthening / HDR through Single Strand Annealing (SSA) / Impaired BRCA2 binding to RAD51 / telomeric DNA binding / mitotic G2 DNA damage checkpoint signaling / negative regulation of cellular senescence / Presynaptic phase of homologous DNA pairing and strand exchange / negative regulation of telomere maintenance via telomerase / neuromuscular process controlling balance / Telomere Extension By Telomerase / neuroblast proliferation / DNA damage response, signal transduction by p53 class mediator / Packaging Of Telomere Ends / axon cytoplasm / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / positive regulation of protein autophosphorylation / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / Inhibition of DNA recombination at telomere / Meiotic synapsis / telomere maintenance / intrinsic apoptotic signaling pathway / replication fork / meiotic cell cycle / DNA damage checkpoint signaling / male germ cell nucleus / positive regulation of nitric-oxide synthase activity / Nonhomologous End-Joining (NHEJ) / double-strand break repair via homologous recombination / HDR through Homologous Recombination (HRR) / G2/M DNA damage checkpoint / DNA Damage/Telomere Stress Induced Senescence / PML body / Meiotic recombination / double-strand break repair / cellular senescence / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / site of double-strand break / Processing of DNA double-strand break ends / DNA-binding transcription factor binding / in utero embryonic development / Regulation of TP53 Activity through Phosphorylation / damaged DNA binding / chromosome, telomeric region / nuclear body
Similarity search - Function
Nibrin, C-terminal / Nibrin / DNA damage repair protein Nbs1 / DNA damage repair protein Nbs1 / Nibrin, second BRCT domain / Nibrin, second BRCT domain superfamily / Second BRCT domain on Nijmegen syndrome breakage protein / Telomere repeat-binding factor, dimerisation domain / Telomeric repeat-binding factor 2, Rap1-binding domain / Nibrin-related ...Nibrin, C-terminal / Nibrin / DNA damage repair protein Nbs1 / DNA damage repair protein Nbs1 / Nibrin, second BRCT domain / Nibrin, second BRCT domain superfamily / Second BRCT domain on Nijmegen syndrome breakage protein / Telomere repeat-binding factor, dimerisation domain / Telomeric repeat-binding factor 2, Rap1-binding domain / Nibrin-related / Telomeric repeat-binding factor 2 Rap1-binding motif / Telomeric repeat-binding factor 2 / Telomeric repeat-binding factor 1/2 / Telomere repeat-binding factor, dimerisation domain superfamily / Telomere repeat-binding factor, dimerisation domain / Telomere repeat binding factor (TRF) / Myb-type HTH DNA-binding domain profile. / Forkhead associated domain / Forkhead-associated (FHA) domain profile. / FHA domain / Myb domain / Forkhead-associated (FHA) domain / Myb-like DNA-binding domain / SMAD/FHA domain superfamily / BRCA1 C Terminus (BRCT) domain / SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains / SANT/Myb domain / BRCT domain / BRCT domain superfamily / Homeobox-like domain superfamily / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Alpha Horseshoe / Mainly Alpha
Similarity search - Domain/homology
Nibrin / Telomeric repeat-binding factor 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3 Å
AuthorsHu, C. / Chen, Y. / Lei, M.
CitationJournal: Mol. Cell / Year: 2017
Title: NBS1 Phosphorylation Status Dictates Repair Choice of Dysfunctional Telomeres
Authors: Rai, R. / Hu, C. / Broton, C. / Chen, Y. / Lei, M. / Chang, S.
History
DepositionNov 26, 2016Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Mar 8, 2017Provider: repository / Type: Initial release
Revision 1.1Mar 15, 2017Group: Database references
Revision 1.2Nov 8, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
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: Telomeric repeat-binding factor 2
B: Telomeric repeat-binding factor 2
C: Telomeric repeat-binding factor 2
D: Telomeric repeat-binding factor 2
E: Telomeric repeat-binding factor 2
F: Telomeric repeat-binding factor 2
G: Telomeric repeat-binding factor 2
H: Nibrin
I: Nibrin
J: Nibrin
K: Nibrin
L: Nibrin
M: Nibrin
N: Nibrin


Theoretical massNumber of molelcules
Total (without water)179,20614
Polymers179,20614
Non-polymers00
Water0
1
A: Telomeric repeat-binding factor 2
H: Nibrin


Theoretical massNumber of molelcules
Total (without water)25,6012
Polymers25,6012
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Telomeric repeat-binding factor 2
I: Nibrin


Theoretical massNumber of molelcules
Total (without water)25,6012
Polymers25,6012
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Telomeric repeat-binding factor 2
J: Nibrin


Theoretical massNumber of molelcules
Total (without water)25,6012
Polymers25,6012
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Telomeric repeat-binding factor 2
K: Nibrin


Theoretical massNumber of molelcules
Total (without water)25,6012
Polymers25,6012
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
E: Telomeric repeat-binding factor 2
L: Nibrin


Theoretical massNumber of molelcules
Total (without water)25,6012
Polymers25,6012
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
6
F: Telomeric repeat-binding factor 2
M: Nibrin


Theoretical massNumber of molelcules
Total (without water)25,6012
Polymers25,6012
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
7
G: Telomeric repeat-binding factor 2
N: Nibrin


Theoretical massNumber of molelcules
Total (without water)25,6012
Polymers25,6012
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)144.616, 153.267, 108.029
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP21212

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Components

#1: Protein
Telomeric repeat-binding factor 2 / / TRF2


Mass: 23724.646 Da / Num. of mol.: 7 / Fragment: UNP residues 84-287
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TERF2, TRBF2, TRF2 / Plasmid: PETSumo / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q15554
#2: Protein/peptide
Nibrin / / NBS1


Mass: 1876.247 Da / Num. of mol.: 7 / Fragment: UNP residues 423-438 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: O60934

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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: 3.41 Å3/Da / Density % sol: 63.88 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 / Details: 0.1M MES, 20% PEG8000, 2mM DTT

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.9787 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Mar 9, 2007
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9787 Å / Relative weight: 1
ReflectionResolution: 3→50 Å / Num. obs: 47897 / % possible obs: 96.4 % / Redundancy: 7.5 % / Biso Wilson estimate: 69.1 Å2 / Rmerge(I) obs: 0.08 / Net I/av σ(I): 19.833 / Net I/σ(I): 8.7
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsCC1/2Diffraction-ID% possible all
3-3.053.40.4370.938179.9
3.05-3.1140.4560.869184.9
3.11-3.174.60.4710.892187.2
3.17-3.235.40.3920.915189.2
3.23-3.36.10.3510.943193.2
3.3-3.386.70.2840.964196.1
3.38-3.467.10.2490.977198
3.46-3.567.40.2330.981199.1
3.56-3.667.60.1970.986199.5
3.66-3.787.80.1530.991199.8
3.78-3.9180.1250.994199.6
3.91-4.078.10.1070.9961100
4.07-4.268.40.0820.9971100
4.26-4.488.60.0670.9981100
4.48-4.768.90.0660.9981100
4.76-5.1390.0740.9971100
5.13-5.6490.0820.9971100
5.64-6.4690.0830.9971100
6.46-8.1390.0440.9991100
8.13-508.50.0241199.9

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Phasing

PhasingMethod: molecular replacement
Phasing MRModel details: Phaser MODE: MR_AUTO
Highest resolutionLowest resolution
Rotation7.37 Å48.17 Å
Translation7.37 Å48.17 Å

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Processing

Software
NameVersionClassification
PHENIX(1.11.1_2575: ???)refinement
HKL-2000data collection
HKL-2000data processing
PHASER2.5.6phasing
PDB_EXTRACT3.2data extraction
HKL-2000data reduction
HKL-2000data scaling
HKLdata reduction
HKLdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3BUA

3bua


Resolution: 3→48.171 Å / SU ML: 0.4 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 31.17
RfactorNum. reflection% reflection
Rfree0.2844 2267 4.81 %
Rwork0.2326 --
obs0.2351 47155 96.71 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 210.19 Å2 / Biso mean: 87.734 Å2 / Biso min: 23.9 Å2
Refinement stepCycle: final / Resolution: 3→48.171 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11619 0 0 0 11619
Num. residues----1470
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00311798
X-RAY DIFFRACTIONf_angle_d0.55115913
X-RAY DIFFRACTIONf_chiral_restr0.0351855
X-RAY DIFFRACTIONf_plane_restr0.0042033
X-RAY DIFFRACTIONf_dihedral_angle_d2.3467300
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 16

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3.0001-3.06530.40321000.33362369246982
3.0653-3.13660.39061390.31142434257386
3.1366-3.2150.34341450.29892552269789
3.215-3.30190.31811580.28652659281794
3.3019-3.3990.29831480.26792802295097
3.399-3.50870.32381340.25832825295999
3.5087-3.63410.32241360.24752882301899
3.6341-3.77950.32871360.240528643000100
3.7795-3.95150.30251240.236429073031100
3.9515-4.15970.31691270.227828973024100
4.1597-4.42010.23271320.192529113043100
4.4201-4.76110.25731860.194128563042100
4.7611-5.23970.28841620.217729113073100
5.2397-5.99670.27771530.258929283081100
5.9967-7.55060.29621220.255230093131100
7.5506-48.17760.22941650.196430823247100
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)
12.5146-0.11530.48286.5883-0.85592.77140.16550.1639-0.2397-1.21950.2996-0.14370.4418-0.0149-0.27560.26810.00430.08880.3171-0.04680.419514.347222.4235143.6432
22.07430.22180.41742.5789-1.72772.2375-0.293-0.03560.20590.02310.2481-0.45450.13-0.0614-0.02010.23510.0130.04960.27020.03010.470315.719931.6596146.9679
33.9691-3.2582-0.46984.88071.67681.0069-0.6659-0.88310.69750.87981.3844-1.76540.76760.556-0.05920.35620.02690.02050.7643-0.11950.655318.318745.6595155.461
41.3735-1.02351.03554.54-1.81331.76930.01380.08491.0305-0.3471-0.3037-1.3222-0.4320.4360.04830.3621-0.09050.140.46390.10221.186320.552752.4731142.2794
53.69431.9922-0.81978.6841.16174.0968-0.13781.8484-0.2078-0.97380.3313-0.01380.7618-0.46790.15140.92620.0919-0.04930.8862-0.02640.5848.963220.6237134.5303
60.8426-0.6579-0.27333.2021-0.49833.8496-0.0552-0.042-0.0171-0.2607-0.04690.10590.53-0.11040.04190.2165-0.0612-0.02160.2554-0.00210.42677.234717.9612153.9229
73.38840.37651.67854.1782-0.72453.0325-0.1279-0.4150.25950.56390.09330.5548-0.2819-0.428-0.00550.29480.05150.13390.36490.01760.47511.971816.2761175.5476
80.54640.3197-0.12432.2589-1.87432.551-0.0893-0.1891-0.05460.2313-0.04480.2870.1576-0.30750.14850.32680.06390.06180.39980.03140.49848.86738.6337174.4393
91.3573-0.39350.03314.2134-2.79063.5720.2246-0.63510.07980.21130.0693-0.77631.7329-0.0137-0.16361.01410.3574-0.09590.518-0.01650.605732.1497-6.7963196.5025
101.76531.30160.611.14550.16833.29830.1185-0.00340.2090.0773-0.1823-0.19750.63450.4906-0.01760.60370.2063-0.03590.4550.02260.450732.5471.6557191.2751
113.93230.485-0.075.0106-1.86313.17150.218-0.4278-0.30720.5172-0.1015-0.70390.09141.2745-0.16250.37580.1125-0.05450.7078-0.05210.524238.000211.5135183.3715
125.1172-0.972-0.06170.81730.92081.3163-0.72290.04640.55-0.5909-0.2029-1.61050.91670.3931-0.09940.99470.3420.22691.0658-0.02460.900342.1546-0.5477171.3789
130.75190.02940.73434.5772-1.04574.8255-0.1443-0.03950.1342-0.6710.0002-0.37530.32290.575-0.00150.22140.0460.09810.51630.0480.463433.032615.2921170.3842
147.61972.2929-2.08424.9133-2.75484.4684-0.08490.4144-0.3971-0.3830.5462-0.58530.3151-0.6866-0.37231.49610.1829-0.05940.4943-0.13720.529525.113-15.25192.7086
150.89590.2992-0.18583.28942.54354.339-0.09210.25780.26440.4572-0.14890.34420.78730.16840.20551.0539-0.0224-0.03440.48560.07660.515924.7928-6.2502206.2933
161.6477-1.33630.76691.0019-0.68982.9366-0.4308-0.18270.34070.33950.0464-0.1452-0.17280.4577-0.04630.60030.13870.02140.60580.00260.327532.63623.3985210.2122
170.2597-0.14680.03170.3110.13610.0832-0.09920.258-0.8806-0.0777-0.02810.64670.0263-0.8526-0.0940.9313-0.080.17350.66180.05740.531816.0893-1.2255202.6972
183.2796-0.50761.13291.9572-0.293.83680.2246-0.37180.01170.04260.02220.21160.4037-0.6426-0.03120.67090.07830.07160.69410.01580.359221.10567.9441218.6191
192.71960.79590.66543.067-0.38112.9532-0.3244-0.47310.41450.0313-0.01550.088-0.0156-0.1091-0.00630.60940.16950.14210.6557-0.13360.45923.871216.0921229.9709
201.6883-1.06180.77751.1285-0.54061.7972-0.2842-0.45510.15540.51580.0760.40890.08170.03620.06230.84260.04730.13670.795-0.1630.527428.411619.4234238.0042
210.2282-0.8614-1.10015.56543.57093.4087-0.073-0.1749-0.24150.09990.14570.4531.27620.2518-0.05881.330.20510.01110.6510.06480.615129.4769-7.1017217.9972
221.8621-0.13020.89471.6591.37972.44620.11030.0489-0.0540.10330.0139-0.22360.58510.9364-0.12480.64570.1347-0.06111.0829-0.01080.518654.396212.2905136.9695
230.5327-0.0608-1.10313.34520.90953.21940.11470.2957-0.0645-0.36970.0466-0.6498-0.0230.9907-0.14610.58330.10270.0710.9834-0.11740.586754.38419.1362116.9024
240.735-0.19050.1364.91141.03822.83870.14760.04670.34650.646-0.30560.365-0.32210.90.10460.7211-0.1734-0.04030.9460.05710.45848.603727.6396147.0652
251.2326-1.54080.46623.05931.6132.1739-0.3369-0.03480.28040.7610.018-0.13480.01110.2170.20160.9417-0.1933-0.12050.79690.0540.671550.058244.099153.4416
261.0549-1.1766-0.01812.334-1.40611.728-1.0078-0.61680.02932.44670.6037-0.0954-0.7621-0.080.32411.58040.4930.3621-0.2169-0.46230.146467.58933.6948198.0035
272.1835-0.1960.25456.8065-0.66860.8916-0.22810.5269-0.04880.63630.32660.99820.1911-0.3333-0.10540.401-0.08220.11960.49560.01080.697364.441511.8112185.3163
281.06040.47730.51130.42020.12860.2949-0.425-0.3737-0.65240.5969-0.34281.64750.2005-1.04360.77460.85620.57031.00230.6617-0.63612.416353.313124.8072192.1227
293.75431.02280.06966.40210.55285.5044-0.18780.98650.5627-0.2240.61931.2547-0.4588-0.4156-0.35730.512-0.0589-0.16230.5850.23160.799164.885630.1742176.5841
300.10730.0797-0.11470.0863-0.25010.48130.3349-0.28650.54860.726-0.02470.2337-0.0207-0.21880.71472.92130.14880.78950.3051-0.61320.365669.91611.1338205.2383
311.88640.94860.23982.3154-0.38714.6846-0.409-0.789-0.42921.5869-0.063-0.90340.09061.65840.01610.60730.06810.02090.72780.00190.908220.561234.7311154.9028
322.2381-1.5064-0.94943.0575-0.87971.5083-0.042-0.12230.54160.0706-0.00930.9852-0.1774-1.51230.03520.42920.0646-0.05390.66940.030.7394-0.693625.7758164.5116
333.2528-0.5058-0.05673.9911-0.16584.38230.35541.24450.10950.3281-0.8904-0.8566-0.07780.26080.16080.7564-0.0833-0.1080.71390.22280.652936.857510.8798192.5247
344.31850.51080.23096.5112-0.37416.0405-0.39770.16440.70561.78340.80650.9212-1.09180.17560.17270.70870.00250.09410.6922-0.08760.47422.27511.6577209.9904
351.15960.35370.7724.72991.43992.6602-0.42420.5030.3371-0.4497-0.40730.2231-0.55950.96660.59760.40290.2789-0.37252.14190.2230.385357.911121.6758127.8962
361.7378-1.41230.85431.3588-1.50373.2666-1.42080.37450.15610.6072-1.37531.06660.4834-0.20490.5580.996-0.1520.40550.99890.04340.948845.704732.9562140.301
372.45661.00811.62585.560.06471.23740.4034-0.2923-0.8184-0.8709-0.53731.31750.2899-0.63670.07081.13530.28220.34720.92990.13070.880662.51586.5021181.6692
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 44 through 69 )A44 - 69
2X-RAY DIFFRACTION2chain 'A' and (resid 70 through 111 )A70 - 111
3X-RAY DIFFRACTION3chain 'A' and (resid 112 through 127 )A112 - 127
4X-RAY DIFFRACTION4chain 'A' and (resid 128 through 227 )A128 - 227
5X-RAY DIFFRACTION5chain 'A' and (resid 228 through 245 )A228 - 245
6X-RAY DIFFRACTION6chain 'B' and (resid 43 through 95 )B43 - 95
7X-RAY DIFFRACTION7chain 'B' and (resid 96 through 185 )B96 - 185
8X-RAY DIFFRACTION8chain 'B' and (resid 186 through 244 )B186 - 244
9X-RAY DIFFRACTION9chain 'C' and (resid 42 through 69 )C42 - 69
10X-RAY DIFFRACTION10chain 'C' and (resid 70 through 111 )C70 - 111
11X-RAY DIFFRACTION11chain 'C' and (resid 112 through 143 )C112 - 143
12X-RAY DIFFRACTION12chain 'C' and (resid 144 through 153 )C144 - 153
13X-RAY DIFFRACTION13chain 'C' and (resid 154 through 228 )C154 - 228
14X-RAY DIFFRACTION14chain 'C' and (resid 229 through 245 )C229 - 245
15X-RAY DIFFRACTION15chain 'D' and (resid 43 through 69 )D43 - 69
16X-RAY DIFFRACTION16chain 'D' and (resid 70 through 86 )D70 - 86
17X-RAY DIFFRACTION17chain 'D' and (resid 87 through 94 )D87 - 94
18X-RAY DIFFRACTION18chain 'D' and (resid 95 through 146 )D95 - 146
19X-RAY DIFFRACTION19chain 'D' and (resid 147 through 182 )D147 - 182
20X-RAY DIFFRACTION20chain 'D' and (resid 183 through 213 )D183 - 213
21X-RAY DIFFRACTION21chain 'D' and (resid 214 through 245 )D214 - 245
22X-RAY DIFFRACTION22chain 'E' and (resid 46 through 111 )E46 - 111
23X-RAY DIFFRACTION23chain 'E' and (resid 112 through 243 )E112 - 243
24X-RAY DIFFRACTION24chain 'F' and (resid 43 through 127 )F43 - 127
25X-RAY DIFFRACTION25chain 'F' and (resid 128 through 244 )F128 - 244
26X-RAY DIFFRACTION26chain 'G' and (resid 43 through 69 )G43 - 69
27X-RAY DIFFRACTION27chain 'G' and (resid 70 through 142 )G70 - 142
28X-RAY DIFFRACTION28chain 'G' and (resid 143 through 153 )G143 - 153
29X-RAY DIFFRACTION29chain 'G' and (resid 154 through 227 )G154 - 227
30X-RAY DIFFRACTION30chain 'G' and (resid 228 through 241 )G228 - 241
31X-RAY DIFFRACTION31chain 'H' and (resid 425 through 436 )H425 - 436
32X-RAY DIFFRACTION32chain 'I' and (resid 424 through 436 )I424 - 436
33X-RAY DIFFRACTION33chain 'J' and (resid 427 through 436 )J427 - 436
34X-RAY DIFFRACTION34chain 'K' and (resid 427 through 436 )K427 - 436
35X-RAY DIFFRACTION35chain 'L' and (resid 427 through 436 )L427 - 436
36X-RAY DIFFRACTION36chain 'M' and (resid 429 through 435 )M429 - 435
37X-RAY DIFFRACTION37chain 'N' and (resid 427 through 435 )N427 - 435

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