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- PDB-5vpf: Transcription factor FosB/JunD bZIP domain in complex with cognat... -

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Basic information

Entry
Database: PDB / ID: 5vpf
TitleTranscription factor FosB/JunD bZIP domain in complex with cognate DNA, type-II crystal
Components
  • DNA (5'-D(*CP*GP*TP*CP*GP*GP*TP*GP*AP*CP*TP*CP*AP*CP*CP*GP*AP*CP*G)-3')
  • DNA (5'-D(*CP*GP*TP*CP*GP*GP*TP*GP*AP*GP*TP*CP*AP*CP*CP*GP*AP*CP*G)-3')
  • Protein fosB
  • Transcription factor jun-D
Keywordstranscription/dna / activator protein-1 / basic leucine zipper / bZIP / fos / jun / transcription factor / DNA-binding protein / redox switch / coiled-coil / transcription-dna complex
Function / homology
Function and homology information


transcription factor AP-1 complex / NGF-stimulated transcription / osteoblast development / response to steroid hormone / response to morphine / response to corticosterone / behavioral response to cocaine / positive regulation of osteoblast differentiation / cellular response to hormone stimulus / response to mechanical stimulus ...transcription factor AP-1 complex / NGF-stimulated transcription / osteoblast development / response to steroid hormone / response to morphine / response to corticosterone / behavioral response to cocaine / positive regulation of osteoblast differentiation / cellular response to hormone stimulus / response to mechanical stimulus / response to cAMP / transcription repressor complex / response to amphetamine / cellular response to calcium ion / transcription coregulator binding / response to progesterone / female pregnancy / response to nicotine / RNA polymerase II transcription regulator complex / sequence-specific double-stranded DNA binding / regulation of cell population proliferation / DNA-binding transcription activator activity, RNA polymerase II-specific / gene expression / transcription regulator complex / Estrogen-dependent gene expression / response to ethanol / transcription by RNA polymerase II / DNA-binding transcription factor activity, RNA polymerase II-specific / transcription cis-regulatory region binding / regulation of cell cycle / RNA polymerase II cis-regulatory region sequence-specific DNA binding / response to xenobiotic stimulus / intracellular membrane-bounded organelle / regulation of transcription by RNA polymerase II / chromatin / enzyme binding / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / DNA binding / nucleoplasm / nucleus / cytosol
Similarity search - Function
AP-1 transcription factor / Transcription factor Jun / Jun-like transcription factor / Jun-like transcription factor / bZIP transcription factor / Transcription factor, Skn-1-like, DNA-binding domain superfamily / : / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #170 / Basic-leucine zipper (bZIP) domain signature. / Basic-leucine zipper (bZIP) domain profile. ...AP-1 transcription factor / Transcription factor Jun / Jun-like transcription factor / Jun-like transcription factor / bZIP transcription factor / Transcription factor, Skn-1-like, DNA-binding domain superfamily / : / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #170 / Basic-leucine zipper (bZIP) domain signature. / Basic-leucine zipper (bZIP) domain profile. / basic region leucin zipper / Basic-leucine zipper domain / Basic-leucine zipper domain superfamily / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
PHOSPHATE ION / DNA / DNA (> 10) / Transcription factor JunD / Protein FosB
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.694 Å
AuthorsYin, Z. / Rudenko, G. / Machius, M.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Institute on Drug Abuse (NIH/NIDA)R01 DA040621 United States
Brain and Behavior Research Foundation United States
CitationJournal: Nucleic Acids Res. / Year: 2017
Title: Activator Protein-1: redox switch controlling structure and DNA-binding.
Authors: Yin, Z. / Machius, M. / Nestler, E.J. / Rudenko, G.
History
DepositionMay 4, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 6, 2017Provider: repository / Type: Initial release
Revision 1.1Oct 18, 2017Group: Database references / Category: citation
Item: _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Nov 15, 2017Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3Dec 11, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4Oct 4, 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: Protein fosB
B: Transcription factor jun-D
E: DNA (5'-D(*CP*GP*TP*CP*GP*GP*TP*GP*AP*CP*TP*CP*AP*CP*CP*GP*AP*CP*G)-3')
F: DNA (5'-D(*CP*GP*TP*CP*GP*GP*TP*GP*AP*GP*TP*CP*AP*CP*CP*GP*AP*CP*G)-3')
C: Protein fosB
D: Transcription factor jun-D
G: DNA (5'-D(*CP*GP*TP*CP*GP*GP*TP*GP*AP*CP*TP*CP*AP*CP*CP*GP*AP*CP*G)-3')
H: DNA (5'-D(*CP*GP*TP*CP*GP*GP*TP*GP*AP*GP*TP*CP*AP*CP*CP*GP*AP*CP*G)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,60121
Polymers55,8208
Non-polymers78013
Water1,27971
1
A: Protein fosB
B: Transcription factor jun-D
E: DNA (5'-D(*CP*GP*TP*CP*GP*GP*TP*GP*AP*CP*TP*CP*AP*CP*CP*GP*AP*CP*G)-3')
F: DNA (5'-D(*CP*GP*TP*CP*GP*GP*TP*GP*AP*GP*TP*CP*AP*CP*CP*GP*AP*CP*G)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)28,37713
Polymers27,9104
Non-polymers4669
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8710 Å2
ΔGint-74 kcal/mol
Surface area14840 Å2
MethodPISA
2
C: Protein fosB
D: Transcription factor jun-D
G: DNA (5'-D(*CP*GP*TP*CP*GP*GP*TP*GP*AP*CP*TP*CP*AP*CP*CP*GP*AP*CP*G)-3')
H: DNA (5'-D(*CP*GP*TP*CP*GP*GP*TP*GP*AP*GP*TP*CP*AP*CP*CP*GP*AP*CP*G)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)28,2248
Polymers27,9104
Non-polymers3144
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7370 Å2
ΔGint-59 kcal/mol
Surface area15020 Å2
MethodPISA
Unit cell
Length a, b, c (Å)119.637, 119.637, 249.970
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number178
Space group name H-MP6122
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and ((resid 154 through 158 and (name N...
21(chain C and (resid 154 through 171 or resid 174...
12(chain E and (resid 1 through 9 or resid 11 through 18))
22(chain F and ((resid 23 and (name C4 or name...
32(chain G and (resid 1 through 9 or resid 11 through 18))
42(chain H and ((resid 23 and (name C4 or name...
13(chain B and (resid 267 through 269 or (resid 270...
23(chain D and ((resid 267 through 268 and (name N...

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain A and ((resid 154 through 158 and (name N...A154 - 158
121(chain A and ((resid 154 through 158 and (name N...A152 - 218
131(chain A and ((resid 154 through 158 and (name N...A152 - 218
141(chain A and ((resid 154 through 158 and (name N...A152 - 218
151(chain A and ((resid 154 through 158 and (name N...A152 - 218
211(chain C and (resid 154 through 171 or resid 174...C154 - 171
221(chain C and (resid 154 through 171 or resid 174...C174 - 181
231(chain C and (resid 154 through 171 or resid 174...C183 - 198
241(chain C and (resid 154 through 171 or resid 174...C200 - 217
112(chain E and (resid 1 through 9 or resid 11 through 18))E0
212(chain F and ((resid 23 and (name C4 or name...F23
222(chain F and ((resid 23 and (name C4 or name...F1 - 19
232(chain F and ((resid 23 and (name C4 or name...F1 - 19
242(chain F and ((resid 23 and (name C4 or name...F1 - 19
252(chain F and ((resid 23 and (name C4 or name...F1 - 19
262(chain F and ((resid 23 and (name C4 or name...F1 - 19
272(chain F and ((resid 23 and (name C4 or name...F1 - 19
282(chain F and ((resid 23 and (name C4 or name...F1 - 19
292(chain F and ((resid 23 and (name C4 or name...F1 - 19
2102(chain F and ((resid 23 and (name C4 or name...F1 - 19
2112(chain F and ((resid 23 and (name C4 or name...F1 - 19
2122(chain F and ((resid 23 and (name C4 or name...F1 - 19
2132(chain F and ((resid 23 and (name C4 or name...F1 - 19
2142(chain F and ((resid 23 and (name C4 or name...F1 - 19
312(chain G and (resid 1 through 9 or resid 11 through 18))G0
412(chain H and ((resid 23 and (name C4 or name...H23
422(chain H and ((resid 23 and (name C4 or name...H1 - 19
432(chain H and ((resid 23 and (name C4 or name...H1 - 19
442(chain H and ((resid 23 and (name C4 or name...H1 - 19
452(chain H and ((resid 23 and (name C4 or name...H1 - 19
462(chain H and ((resid 23 and (name C4 or name...H1 - 19
472(chain H and ((resid 23 and (name C4 or name...H1 - 19
482(chain H and ((resid 23 and (name C4 or name...H1 - 19
492(chain H and ((resid 23 and (name C4 or name...H1 - 19
4102(chain H and ((resid 23 and (name C4 or name...H1 - 19
4112(chain H and ((resid 23 and (name C4 or name...H1 - 19
4122(chain H and ((resid 23 and (name C4 or name...H1 - 19
4132(chain H and ((resid 23 and (name C4 or name...H1 - 19
4142(chain H and ((resid 23 and (name C4 or name...H1 - 19
113(chain B and (resid 267 through 269 or (resid 270...B267 - 269
123(chain B and (resid 267 through 269 or (resid 270...B270 - 271
133(chain B and (resid 267 through 269 or (resid 270...B266 - 332
143(chain B and (resid 267 through 269 or (resid 270...B266 - 332
153(chain B and (resid 267 through 269 or (resid 270...B266 - 332
163(chain B and (resid 267 through 269 or (resid 270...B266 - 332
213(chain D and ((resid 267 through 268 and (name N...D267 - 268
223(chain D and ((resid 267 through 268 and (name N...D267 - 331
233(chain D and ((resid 267 through 268 and (name N...D267 - 331
243(chain D and ((resid 267 through 268 and (name N...D267 - 331
253(chain D and ((resid 267 through 268 and (name N...D267 - 331

NCS ensembles :
ID
1
2
3

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Components

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Protein , 2 types, 4 molecules ACBD

#1: Protein Protein fosB / G0/G1 switch regulatory protein 3


Mass: 8267.290 Da / Num. of mol.: 2 / Fragment: unp residues 153-219
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FOSB, G0S3 / Plasmid: pET21-NESG / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta 2 (DE3) / References: UniProt: P53539
#2: Protein Transcription factor jun-D


Mass: 7989.425 Da / Num. of mol.: 2 / Fragment: unp residues 266-332
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: JUND / Plasmid: pET21a / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta 2 (DE3) / References: UniProt: P17535

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DNA chain , 2 types, 4 molecules EGFH

#3: DNA chain DNA (5'-D(*CP*GP*TP*CP*GP*GP*TP*GP*AP*CP*TP*CP*AP*CP*CP*GP*AP*CP*G)-3')


Mass: 5806.749 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human)
#4: DNA chain DNA (5'-D(*CP*GP*TP*CP*GP*GP*TP*GP*AP*GP*TP*CP*AP*CP*CP*GP*AP*CP*G)-3')


Mass: 5846.772 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human)

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Non-polymers , 5 types, 84 molecules

#5: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C2H6O2
#6: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#7: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Na
#8: Chemical ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: PO4
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 71 / 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: 4.63 Å3/Da / Density % sol: 73.41 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.5 / Details: 0.9 M Na2HPO4

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.979 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 16, 2016
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979 Å / Relative weight: 1
ReflectionResolution: 2.7→50 Å / Num. obs: 30141 / % possible obs: 99.9 % / Redundancy: 15.7 % / Biso Wilson estimate: 40.66 Å2 / Rmerge(I) obs: 0.107 / Rpim(I) all: 0.029 / Rrim(I) all: 0.111 / Χ2: 0.97 / Net I/σ(I): 8.8 / Num. measured all: 473877
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allCC1/2Rpim(I) allRrim(I) allΧ2% possible all
2.7-2.7515.51.75214690.7030.4621.8130.919100
2.75-2.814.41.44514660.7630.3951.4990.916100
2.8-2.8515.91.2214790.8560.3171.2610.966100
2.85-2.9116.60.99914730.9060.2531.0310.93399.9
2.91-2.9716.60.7714680.940.1950.7950.947100
2.97-3.0416.60.614670.9740.1510.6190.94899.9
3.04-3.1216.40.40414700.990.1030.4180.99699.9
3.12-3.2160.23814930.9960.0610.2461.00399.9
3.2-3.315.80.16914800.9980.0450.1751.04999.9
3.3-3.414.70.14114930.9970.0370.1461.044100
3.4-3.5215.30.11614940.9980.030.121.042100
3.52-3.6616.60.12214790.9970.030.1261.003100
3.66-3.8316.40.11514970.9970.0290.1181.034100
3.83-4.0316.20.09115120.9980.0230.0940.98499.9
4.03-4.2915.90.08115200.9980.020.0840.941100
4.29-4.6214.50.07815190.9970.020.0810.904100
4.62-5.0816.50.07315150.9980.0180.0750.888100
5.08-5.81160.07115500.9980.0180.0730.88699.9
5.81-7.3214.50.07415820.9960.020.0760.89699.8
7.32-5014.10.0817150.9710.0240.0841.10699.2

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Processing

Software
NameVersionClassification
PHENIX1.11.1_2575refinement
SCALEPACKdata scaling
PDB_EXTRACT3.22data extraction
DENZOdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1fos

1fos


Resolution: 2.694→48.593 Å / SU ML: 0.32 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 26.28 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2481 1999 7.31 %
Rwork0.2101 25338 -
obs0.2129 27337 90.86 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 159.18 Å2 / Biso mean: 50.9589 Å2 / Biso min: 11.59 Å2
Refinement stepCycle: final / Resolution: 2.694→48.593 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2115 1523 93 71 3802
Biso mean--63.83 29.29 -
Num. residues----339
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0063938
X-RAY DIFFRACTIONf_angle_d0.7925591
X-RAY DIFFRACTIONf_chiral_restr0.04635
X-RAY DIFFRACTIONf_plane_restr0.004460
X-RAY DIFFRACTIONf_dihedral_angle_d21.7582227
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A636X-RAY DIFFRACTION13.405TORSIONAL
12C636X-RAY DIFFRACTION13.405TORSIONAL
21E706X-RAY DIFFRACTION13.405TORSIONAL
22F706X-RAY DIFFRACTION13.405TORSIONAL
23G706X-RAY DIFFRACTION13.405TORSIONAL
24H706X-RAY DIFFRACTION13.405TORSIONAL
31B662X-RAY DIFFRACTION13.405TORSIONAL
32D662X-RAY DIFFRACTION13.405TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.6936-2.76090.3264990.27631261136065
2.7609-2.83560.26981110.28471397150872
2.8356-2.9190.3281180.27921497161577
2.919-3.01320.34131250.27121580170581
3.0132-3.12090.29661320.25761697182987
3.1209-3.24580.26161430.22381803194692
3.2458-3.39350.23761500.20631903205397
3.3935-3.57230.26581560.194519662122100
3.5723-3.79610.25271540.209219662120100
3.7961-4.0890.23771580.173519892147100
4.089-4.50030.22011580.177120082166100
4.5003-5.15080.23931590.191820252184100
5.1508-6.48710.23871630.215820522215100
6.4871-48.60080.21141730.21032194236799
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)
10.63530.5130.54220.63340.490.4624-0.14080.3101-0.0047-0.15680.2003-0.05910.0462-0.04820.04560.1565-0.0812-0.11670.277-0.0370.2006-12.88968.263-35.607
22.55623.8348-1.1346.5279-2.18191.03650.03340.19820.11320.16520.05660.1045-0.05030.0182-0.08520.23720.0022-0.11520.2257-0.01270.1298-8.81569.169-27.691
38.30172.8092-3.75992.85980.76495.00860.02250.1539-0.39820.14110.25961.1122-0.19-1.3655-0.29520.33310.2221-0.1260.788-0.0720.9369-46.08755.685-32.149
41.75660.8767-0.09370.6659-0.26860.2245-0.13230.3424-0.3498-0.0316-0.0568-0.10190.01560.0505-0.27120.23930.0334-0.08360.3547-0.10530.1853-17.95543.296-28.585
54.1899-0.22061.98051.65290.29413.1734-0.11590.4175-0.49010.07420.03250.00870.15760.18990.10230.18540.02410.01520.3435-0.03130.1929-13.63639.393-28.835
66.1985-1.5196-2.85585.54873.38652.7554-0.1352-0.7260.13540.80490.00150.9647-0.0473-0.71370.12660.4440.1320.12710.43510.0830.3412-35.84648.307-25.5
70.393-0.39040.10380.6077-0.15130.038-0.3091-0.46830.36480.49480.2658-0.2839-0.1134-0.03520.13050.5620.3695-0.04080.632-0.02980.6373-42.39263.105-29.099
81.19122.4452-0.76695.3524-1.79780.94390.0395-0.2404-0.27950.3258-0.0987-0.34690.15510.16450.08120.35870.1217-0.15690.32030.08380.466827.5250.679-6.103
94.13053.7240.73194.21230.45060.4568-0.20210.2246-0.3107-0.13430.239-0.5756-0.01160.1293-0.00110.24670.0739-0.06080.2984-0.06390.542324.51950.268-13.832
100.13510.11180.18750.316-0.12950.623-0.02120.0429-0.34430.01830.0112-0.31050.39620.2404-0.02320.84390.577-0.01941.00480.02091.506731.78712.387-6.615
110.8601-0.76480.32750.9593-0.86451.3032-0.1597-0.11370.35430.0886-0.1496-0.49680.03020.48140.14020.37820.2145-0.08880.54920.04070.895720.62225.306-11.898
124.6275-3.7042-1.0763.3950.55560.467-0.5827-0.5207-0.410.75810.2958-0.2130.46980.05060.28010.44840.1302-0.00310.3090.04730.3882-0.48433.814-6.864
130.8262-1.2211-0.05812.2412-0.69311.38550.02870.064-0.7860.2616-0.03310.09330.31490.12270.010.40360.1499-0.00910.31190.02510.48291.93232.496-8.146
141.5261-0.0239-0.690.00110.01180.31180.08260.1801-0.27050.0905-0.067-0.45360.36640.61290.09260.60010.4158-0.03580.80480.02831.193927.94817.715-11.055
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 152:218 )A152 - 218
2X-RAY DIFFRACTION2( CHAIN B AND RESID 266:332 )B266 - 332
3X-RAY DIFFRACTION3( CHAIN E AND RESID 1:5 )E1 - 5
4X-RAY DIFFRACTION4( CHAIN E AND RESID 6:19 )E6 - 19
5X-RAY DIFFRACTION5( CHAIN F AND RESID 1:10 )F1 - 10
6X-RAY DIFFRACTION6( CHAIN F AND RESID 11:15 )F11 - 15
7X-RAY DIFFRACTION7( CHAIN F AND RESID 16:19 )F16 - 19
8X-RAY DIFFRACTION8( CHAIN C AND RESID 154:217 )C154 - 217
9X-RAY DIFFRACTION9( CHAIN D AND RESID 267:331 )D267 - 331
10X-RAY DIFFRACTION10( CHAIN G AND RESID 1:5 )G1 - 5
11X-RAY DIFFRACTION11( CHAIN G AND RESID 6:10 )G6 - 10
12X-RAY DIFFRACTION12( CHAIN G AND RESID 11:19 )G11 - 19
13X-RAY DIFFRACTION13( CHAIN H AND RESID 1:10 )H1 - 10
14X-RAY DIFFRACTION14( CHAIN H AND RESID 11:19 )H11 - 19

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