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- PDB-4z6a: Crystal Structure of a FVIIa-Trypsin Chimera (YT) in Complex with... -

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Basic information

Entry
Database: PDB / ID: 4z6a
TitleCrystal Structure of a FVIIa-Trypsin Chimera (YT) in Complex with Soluble Tissue Factor
Components
  • (Coagulation factor ...) x 2
  • Tissue factor
KeywordsHYDROLASE / trypsin-fold / protein-protein complex
Function / homology
Function and homology information


activation of plasma proteins involved in acute inflammatory response / activation of blood coagulation via clotting cascade / coagulation factor VIIa / response to Thyroid stimulating hormone / response to astaxanthin / response to thyrotropin-releasing hormone / response to 2,3,7,8-tetrachlorodibenzodioxine / response to carbon dioxide / response to genistein / serine-type peptidase complex ...activation of plasma proteins involved in acute inflammatory response / activation of blood coagulation via clotting cascade / coagulation factor VIIa / response to Thyroid stimulating hormone / response to astaxanthin / response to thyrotropin-releasing hormone / response to 2,3,7,8-tetrachlorodibenzodioxine / response to carbon dioxide / response to genistein / serine-type peptidase complex / response to vitamin K / positive regulation of platelet-derived growth factor receptor signaling pathway / positive regulation of leukocyte chemotaxis / response to thyroxine / NGF-stimulated transcription / response to cholesterol / cytokine receptor activity / response to growth hormone / positive regulation of positive chemotaxis / Extrinsic Pathway of Fibrin Clot Formation / positive regulation of endothelial cell apoptotic process / positive regulation of blood coagulation / animal organ regeneration / positive regulation of TOR signaling / Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus / Gamma-carboxylation of protein precursors / Removal of aminoterminal propeptides from gamma-carboxylated proteins / positive regulation of endothelial cell proliferation / serine-type peptidase activity / BMAL1:CLOCK,NPAS2 activates circadian expression / positive regulation of interleukin-8 production / circadian rhythm / phospholipid binding / protein processing / Golgi lumen / response to estrogen / cytokine-mediated signaling pathway / positive regulation of angiogenesis / blood coagulation / response to estradiol / : / protease binding / vesicle / response to hypoxia / positive regulation of cell migration / endoplasmic reticulum lumen / signaling receptor binding / external side of plasma membrane / serine-type endopeptidase activity / calcium ion binding / positive regulation of gene expression / cell surface / extracellular space / extracellular region / membrane / plasma membrane
Similarity search - Function
Tissue factor / Tissue factor, conserved site / Tissue factor signature. / Interferon/interleukin receptor domain / Interferon-alpha/beta receptor, fibronectin type III / : / Tissue factor / Peptidase S1A, coagulation factor VII/IX/X/C/Z / : / Coagulation factor-like, Gla domain superfamily ...Tissue factor / Tissue factor, conserved site / Tissue factor signature. / Interferon/interleukin receptor domain / Interferon-alpha/beta receptor, fibronectin type III / : / Tissue factor / Peptidase S1A, coagulation factor VII/IX/X/C/Z / : / Coagulation factor-like, Gla domain superfamily / Laminin / Laminin / Coagulation Factor Xa inhibitory site / EGF-like domain / EGF-type aspartate/asparagine hydroxylation site / EGF-like calcium-binding, conserved site / Calcium-binding EGF-like domain signature. / Aspartic acid and asparagine hydroxylation site. / EGF-like calcium-binding domain / Calcium-binding EGF-like domain / Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain / Gamma-carboxyglutamic acid-rich (GLA) domain / Gamma-carboxyglutamic acid-rich (GLA) domain superfamily / Vitamin K-dependent carboxylation domain. / Gla domain profile. / Domain containing Gla (gamma-carboxyglutamate) residues. / Epidermal growth factor-like domain. / EGF-like domain profile. / EGF-like domain signature 1. / EGF-like domain signature 2. / EGF-like domain / Fibronectin type III / Fibronectin type III superfamily / Ribbon / Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Serine proteases, trypsin family, histidine active site. / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, serine active site. / Serine proteases, trypsin domain profile. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Trypsin-like serine proteases / Thrombin, subunit H / Immunoglobulin-like fold / Peptidase S1, PA clan, chymotrypsin-like fold / Immunoglobulins / Peptidase S1, PA clan / Beta Barrel / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
D-Phe-Phe-Arg Chloromethylketone / Chem-0Z6 / beta-D-glucopyranose / CITRIC ACID / alpha-L-fucopyranose / Coagulation factor VII / Tissue factor
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.25 Å
Model detailsA human-FVIIa Variant with the 170-loop swapped with that from human-Trypsin, and an additional ...A human-FVIIa Variant with the 170-loop swapped with that from human-Trypsin, and an additional replacement of Tyr170b with Phe
AuthorsSorensen, A.B. / Svensson, L.A. / Gandhi, P.S.
CitationJournal: J.Biol.Chem. / Year: 2016
Title: Molecular Basis of Enhanced Activity in Factor VIIa-Trypsin Variants Conveys Insights into Tissue Factor-mediated Allosteric Regulation of Factor VIIa Activity.
Authors: Sorensen, A.B. / Madsen, J.J. / Svensson, L.A. / Pedersen, A.A. / stergaard, H. / Overgaard, M.T. / Olsen, O.H. / Gandhi, P.S.
History
DepositionApr 4, 2015Deposition site: RCSB / Processing site: PDBE
Revision 1.0Dec 30, 2015Provider: repository / Type: Initial release
Revision 1.1Jan 13, 2016Group: Database references
Revision 1.2Mar 9, 2016Group: Database references
Revision 1.3Dec 21, 2016Group: Non-polymer description
Revision 1.4Jan 17, 2018Group: Data collection / Category: diffrn_source / Item: _diffrn_source.pdbx_synchrotron_site
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / pdbx_struct_conn_angle / struct_conn / struct_site / struct_site_gen
Item: _atom_site.auth_atom_id / _atom_site.label_atom_id ..._atom_site.auth_atom_id / _atom_site.label_atom_id / _chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _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_role / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_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
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Jan 10, 2024Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 3.0Oct 1, 2025Group: Advisory / Atomic model ...Advisory / Atomic model / Derived calculations / Structure summary
Category: atom_site / pdbx_entry_details ...atom_site / pdbx_entry_details / pdbx_modification_feature / pdbx_validate_close_contact / struct_conn
Item: _atom_site.auth_atom_id / _atom_site.label_atom_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
L: Coagulation factor VII
H: Coagulation factor VII
T: Tissue factor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)62,6248
Polymers61,5433
Non-polymers1,0815
Water4,143230
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5770 Å2
ΔGint-15 kcal/mol
Surface area23770 Å2
MethodPISA
Unit cell
Length a, b, c (Å)67.030, 81.700, 124.560
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Coagulation factor ... , 2 types, 2 molecules LH

#1: Protein Coagulation factor VII / Proconvertin / Serum prothrombin conversion accelerator / SPCA


Mass: 10500.729 Da / Num. of mol.: 1 / Fragment: UNP residues 108-203
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Tissue: Blood / Gene: F7 / Organ: Kidney / Plasmid: pQMCF-5
Details (production host): Cells were licensed from Icosagen (Estonia)
Cell line (production host): CHOEBNALT85 / Production host: Cricetulus griseus (Chinese hamster) / References: UniProt: P08709, coagulation factor VIIa
#2: Protein Coagulation factor VII / Proconvertin / Serum prothrombin conversion accelerator / SPCA


Mass: 27524.611 Da / Num. of mol.: 1 / Fragment: unp residues 213-465 / Mutation: [169-175] LQQSRKVGDSPN - EASYPGK
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Tissue: Blood / Gene: F7 / Organ: Kidney / Plasmid: pQMCF-5
Details (production host): Cells were licensed from Icosagen (Estonia)
Cell line (production host): CHOEBNALT85 / Production host: Cricetulus griseus (Chinese hamster) / References: UniProt: P08709, coagulation factor VIIa

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Protein , 1 types, 1 molecules T

#3: Protein Tissue factor / TF / Coagulation factor III / Thromboplastin


Mass: 23518.156 Da / Num. of mol.: 1 / Fragment: unp residues 36-242
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Tissue: Blood / Gene: F3 / Plasmid: pET3a / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): Origami 2 / References: UniProt: P13726

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Sugars , 2 types, 2 molecules

#4: Sugar ChemComp-BGC / beta-D-glucopyranose / beta-D-glucose / D-glucose / glucose


Type: D-saccharide, beta linking / Mass: 180.156 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Formula: C6H12O6
IdentifierTypeProgram
DGlcpbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
b-D-glucopyranoseCOMMON NAMEGMML 1.0
b-D-GlcpIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcSNFG CARBOHYDRATE SYMBOLGMML 1.0
#5: Sugar ChemComp-FUC / alpha-L-fucopyranose / alpha-L-fucose / 6-deoxy-alpha-L-galactopyranose / L-fucose / fucose


Type: L-saccharide, alpha linking / Mass: 164.156 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Formula: C6H12O5
IdentifierTypeProgram
LFucpaCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
a-L-fucopyranoseCOMMON NAMEGMML 1.0
a-L-FucpIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
FucSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 4 types, 233 molecules

#6: Chemical ChemComp-0Z6 / D-phenylalanyl-N-[(2S,3S)-6-{[amino(iminio)methyl]amino}-1-chloro-2-hydroxyhexan-3-yl]-L-phenylalaninamide / Proconvertin / Serum prothrombin conversion accelerator / SPCA / FFRCK


Type: peptide-like, Peptide-like / Class: Inhibitor / Mass: 504.045 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Formula: C25H36ClN6O3 / References: D-Phe-Phe-Arg Chloromethylketone
#7: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Ca
#8: Chemical ChemComp-CIT / CITRIC ACID


Mass: 192.124 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H8O7
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 230 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY

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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: 2.78 Å3/Da / Density % sol: 55.76 % / Description: Elongated hexgonal prisms
Crystal growTemperature: 295 K / Method: vapor diffusion, hanging drop / pH: 5.6
Details: 0.1M NaCitrate, 16.6% PEG 3350, 12.5% 1-Propanol, with seeding

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: MAX II / Beamline: I911-3 / Wavelength: 1 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Sep 25, 2013
Details: Rh-coated Si mirrors: M1 collimating mirror, M2 toroidal focusing mirror
RadiationMonochromator: Si (111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.25→29.5155 Å / Num. all: 32043 / Num. obs: 32041 / % possible obs: 97 % / Observed criterion σ(I): -3 / Redundancy: 4.8 % / Biso Wilson estimate: 36.89 Å2 / Rmerge F obs: 0.99 / Rmerge(I) obs: 0.1434 / Rrim(I) all: 0.158 / Χ2: 0.936 / Net I/σ(I): 7.33 / Num. measured all: 155085
Reflection shell

Diffraction-ID: 1 / Rejects: _

Resolution (Å)Highest resolution (Å)Redundancy (%)Rmerge F obsRmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsRrim(I) all% possible all
2.25-2.333.70.2181.4330.646269464034671.69481
2.31-2.370.2681.180.99974450142331.50294
2.37-2.440.390.9641.1910918440142421.22596.4
2.44-2.520.4260.9031.3311211429341941.14597.7
2.52-2.60.6060.6661.7210750412940330.84697.7
2.6-2.690.6750.5152.1910412400739270.65598
2.69-2.790.7750.3992.8610166388338120.50698.2
2.79-2.90.8770.2913.729685370536310.36898
2.9-3.030.920.2274.739383358835300.28798.4
3.03-3.180.9520.1636.318885339333400.20698.4
3.18-3.350.9750.1248.188462322131780.15698.7
3.35-3.560.9870.08710.758101310030480.10998.3
3.56-3.80.9920.06912.997414285428040.08698.2
3.8-4.110.9950.05215.936997268326510.06598.8
4.11-4.50.9960.04319.246416247224350.05498.5
4.5-5.030.9970.0419.995760223021960.0598.5
5.03-5.810.9960.04219.085022195319240.05298.5
5.81-7.120.9970.04318.774274167216460.05498.4
7.12-10.060.9980.02925.023275127412600.03698.9
10.060.9990.02130.1817117066580.02693.2

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
PHENIXrefinement
XSCALEJuly 4, 2012 BUILT=20130706data scaling
PHASER2.5.7phasing
PDB_EXTRACT3.15data extraction
XDSMarch 30, 2013data reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: In-House FVIIa-WT:sTF-FFR similar to 1DAN

1dan


Resolution: 2.25→29.513 Å / SU ML: 0.32 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 25.82 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2405 1605 5.01 %Random selection
Rwork0.1882 30436 --
obs0.1907 32041 96.61 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 131.57 Å2 / Biso mean: 48.914 Å2 / Biso min: 15.57 Å2
Refinement stepCycle: final / Resolution: 2.25→29.513 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4209 0 61 230 4500
Biso mean--91.63 38.6 -
Num. residues----545
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0084385
X-RAY DIFFRACTIONf_angle_d0.95976
X-RAY DIFFRACTIONf_chiral_restr0.034673
X-RAY DIFFRACTIONf_plane_restr0.003767
X-RAY DIFFRACTIONf_dihedral_angle_d12.0271560
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 11

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.25-2.32260.36031080.31112258236680
2.3226-2.40560.29961560.28472679283595
2.4056-2.50180.34881500.2792754290498
2.5018-2.61560.29791530.25662760291398
2.6156-2.75340.32691300.23682806293698
2.7534-2.92580.28951710.21832781295299
2.9258-3.15150.25251380.21032816295499
3.1515-3.46820.24191450.17862835298099
3.4682-3.9690.231380.15092864300299
3.969-4.99660.1631470.13192886303399
4.9966-29.51550.20831690.16952997316699
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)DetailsOrigin x (Å)Origin y (Å)Origin z (Å)
15.4945-0.27682.22675.42131.33493.46540.50860.6274-0.7172-0.3789-0.1252-0.07090.45890.2088-0.24140.5540.1526-0.05870.4558-0.09150.5229FVIIa LightChain-3.1362-30.80942.8238
21.17490.9616-0.6233.280.77635.4634-0.36790.3661-0.68-0.1239-0.03090.03780.8514-0.36070.23870.3741-0.08620.04420.328-0.10090.49FVIIa LightChain-19.0576-33.660636.0048
32.5051-0.19220.09223.4209-1.62544.17440.062-0.2876-0.06220.0109-0.034-0.0176-0.02770.10750.02170.23870.03210.0230.2391-0.03030.2824FVIIa HeavyChain-18.7416-13.685552.2195
44.3934-0.0085-0.07793.63440.20612.94770.1012-0.61360.10340.4457-0.04630.2421-0.0642-0.3352-0.04020.2680.01350.05240.2651-0.00270.2199FVIIa HeavyChain-17.2651-13.868159.7693
55.0355-1.53010.87671.43650.41181.5004-0.2396-0.2199-0.12670.28940.252-0.0223-0.02930.22760.02310.32160.054-0.03050.27140.00840.3047FVIIa HeavyChain-5.9343-20.257858.7826
62.4218-0.683-0.77761.77260.56032.8593-0.02640.0344-0.06660.0125-0.03030.00920.04930.06550.06630.18120.0184-0.01720.2490.00450.292FVIIa HeavyChain-13.5081-17.480545.4619
75.09765.4862-2.28486.2269-3.38973.67560.2935-0.11240.2401-0.0651-0.2121-0.2272-0.0720.8744-0.03420.19080.02360.08050.55720.00480.3972FVIIa HeavyChain5.4726-14.086441.7781
83.9081.13820.39073.73771.18843.37090.05070.08150.0251-0.2099-0.0152-0.1576-0.20970.0255-0.02470.23440.0570.00750.23160.02420.3082FVIIa HeavyChain-10.1409-14.452641.8589
92.23911.7199-2.1856.5797-5.80887.9988-0.05910.0711-0.1888-0.1019-0.0694-0.5690.310.22580.08780.15850.0702-0.03280.26850.01980.3006FVIIa HeavyChain-4.3633-19.737647.1008
106.442.97683.7718.64932.54082.29750.7255-0.6853-0.34651.1267-0.1008-0.65370.6184-1.0422-0.47890.5412-0.0078-0.07910.51280.13780.4723FVIIa HeavyChain-4.1785-28.765663.0722
114.8936-4.76414.17288.8895-5.69084.18140.05410.2350.98670.184-0.1934-0.99560.32471.0790.1760.520.16690.02690.7595-0.05020.4639Tissue Factor12.5561-23.444124.6854
123.4692-1.30772.73082.9733-1.06926.4241-0.1875-0.0956-0.0057-0.2167-0.0043-0.13840.10670.47130.20860.44710.12260.09520.55920.04730.3362Tissue Factor4.3756-22.678113.2547
132.67-0.54090.91142.3746-1.59186.11930.05360.0522-0.0197-0.1609-0.00850.030.30150.0409-0.03610.26660.06040.02350.274-0.02070.3066Tissue Factor-3.6666-23.358919.4047
143.3803-4.36830.96566.98771.7358.4812-0.054-0.2792-0.68370.1430.46120.17210.02070.1879-0.41760.32960.10490.03690.50030.05640.5266Tissue Factor2.8747-25.752826.2348
152.9686-1.07123.42081.6763-2.22625.49930.10280.34430.0715-0.2368-0.07920.07130.0540.6136-0.08780.33150.0433-0.00050.27050.04630.2793Tissue Factor-4.5781-14.12830.7085
165.0337-1.84821.7686.3357-4.33193.40420.27220.1748-0.4359-0.4247-0.46220.74340.3015-0.42370.05010.59230.138-0.09580.4979-0.0130.4358Tissue Factor-13.8921-17.65571.1272
176.8239-0.0734-1.60114.5771-2.1892.19210.08130.67340.1481-0.2528-0.1898-0.53380.10250.32070.14550.42230.1174-0.05690.5111-0.01910.4585Tissue Factor-5.0792-5.2673-15.8415
184.3909-1.01570.52513.1473-0.49052.45230.13840.57960.1068-0.2963-0.1034-0.38830.39781.0241-0.02580.55180.2143-0.01370.42810.02930.4319Tissue Factor-2.1697-8.9778-12.4035
Refinement TLS group
IDRefine-IDRefine TLS-IDSelectionSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1allchain 'L' and (resid 48 through 86 )L48 - 86
2X-RAY DIFFRACTION2chain 'L' and (resid 87 through 143 )L87 - 143
3X-RAY DIFFRACTION3chain 'H' and (resid 16 through 50 )H16 - 50
4X-RAY DIFFRACTION4chain 'H' and (resid 51 through 80 )H51 - 80
5X-RAY DIFFRACTION5chain 'H' and (resid 81 through 103 )H81 - 103
6X-RAY DIFFRACTION6chain 'H' and (resid 104 through 167 )H104 - 167
7X-RAY DIFFRACTION7chain 'H' and (resid 168 through 179 )H168 - 179
8X-RAY DIFFRACTION8chain 'H' and (resid 180 through 215 )H180 - 215
9X-RAY DIFFRACTION9chain 'H' and (resid 216 through 243 )H216 - 243
10X-RAY DIFFRACTION10chain 'H' and (resid 244 through 257 )H244 - 257
11X-RAY DIFFRACTION11chain 'T' and (resid 4 through 12 )T4 - 12
12X-RAY DIFFRACTION12chain 'T' and (resid 13 through 31 )T13 - 31
13X-RAY DIFFRACTION13chain 'T' and (resid 32 through 70 )T32 - 70
14X-RAY DIFFRACTION14chain 'T' and (resid 71 through 83 )T71 - 83
15X-RAY DIFFRACTION15chain 'T' and (resid 90 through 127 )T90 - 127
16X-RAY DIFFRACTION16chain 'T' and (resid 128 through 150 )T128 - 150
17X-RAY DIFFRACTION17chain 'T' and (resid 151 through 178 )T151 - 178
18X-RAY DIFFRACTION18chain 'T' and (resid 179 through 210 )T179 - 210

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