data_5803 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5803 _Entry.Title ; Three-disulfide variant of hen lysozyme: C64A/C80A ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2003-05-19 _Entry.Accession_date 2003-05-20 _Entry.Last_release_date 2004-09-14 _Entry.Original_release_date 2004-09-14 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Atsushi Yokota . . . 5803 2 Kenichi Hirai . . . 5803 3 Hiroyo Miyauchi . . . 5803 4 Yasuo Noda . . . 5803 5 Kyouko Inoue . . . 5803 6 Kazuyuki Akasaka . . . 5803 7 Hideki Tachibana . . . 5803 8 Shin-ichi Segawa . . . 5803 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5803 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 680 5803 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2004-09-14 2003-05-19 original author . 5803 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 5068 'Recombinant hen lysozyme with extra N-terminal Met' 5803 BMRB 5069 'Two-disulfide variant of hen lysozyme: 2SS[6-127, 30-115]' 5803 BMRB 5804 'Three-disulfide variant of hen lysozyme: C76A/C94A' 5803 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5803 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 15157100 _Citation.Full_citation . _Citation.Title ; NMR characterization of three-disulfide variants of lysozyme, C64A/C80A, C76A/C94A, and C30A/C115A--a marginally stable state in folded proteins. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 43 _Citation.Journal_issue 21 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 6663 _Citation.Page_last 6669 _Citation.Year 2004 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Atsushi Yokota . . . 5803 1 2 Kenichi Hirai . . . 5803 1 3 Hiroyo Miyauchi . . . 5803 1 4 Satoshi Iimura . . . 5803 1 5 Yasuo Noda . . . 5803 1 6 Kyouko Inoue . . . 5803 1 7 Kazuyuki Akasaka . . . 5803 1 8 Hideki Tachibana . . . 5803 1 9 Shin-ichi Segawa . . . 5803 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'Lysozyme Variants' 5803 1 NMR 5803 1 'Protein Folding' 5803 1 'Three-Disulfide Intermediate' 5803 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 5803 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10395829 _Citation.Full_citation ; van den Berg B, Chung EW, Robinson CV, Dobson CM. Characterisation of the dominant oxidative folding intermediate of hen lysozyme. J Mol Biol. 1999 Jul 16;290(3):781-96. ; _Citation.Title 'Characterisation of the dominant oxidative folding intermediate of hen lysozyme.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 290 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0022-2836 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 781 _Citation.Page_last 796 _Citation.Year 1999 _Citation.Details ; Reduced denatured lysozyme has been oxidised and refolded at pH values close to neutral in an efficient way by dilution from buffers containing 8.0 M urea, and refolding intermediates were separated by reverse-phase HPLC at pH 2. By using peptic digestion in combination with high-resolution Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometry (MS) and tandem MS/MS the dominant intermediate was identified to be des-[76-94]. This species has three of the four native disulphide bonds, but lacks the Cys76-Cys94 disulphide bond which connects the two folding domains in the native protein. Characterisation of des-[76-94] by 2D1H NMR shows that it has a highly native-like structure. This provides an explanation for the accumulation of this species during refolding as direct oxidation to the fully native protein will be restricted by the burial of Cys94 in the protein interior. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 B 'van den Berg' B. . . 5803 2 2 'E W' Chung E. W. . 5803 2 3 'C V' Robinson C. V. . 5803 2 4 'C M' Dobson C. M. . 5803 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 5803 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 11841203 _Citation.Full_citation ; Noda Y, Yokota A, Horii D, Tominaga T, Tanisaka Y, Tachibana H, Segawa S. NMR structural study of two-disulfide variant of hen lysozyme: 2SS[6-127, 30-115]--a disulfide intermediate with a partly unfolded structure. Biochemistry. 2002 Feb 19;41(7):2130-9. ; _Citation.Title 'NMR structural study of two-disulfide variant of hen lysozyme: 2SS[6-127, 30-115]--a disulfide intermediate with a partly unfolded structure.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 41 _Citation.Journal_issue 7 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0006-2960 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 2130 _Citation.Page_last 2139 _Citation.Year 2002 _Citation.Details ; The 15N-labeled recombinant hen lysozyme and two species of two-disulfide variants, denoted as 2SS[6-127, 30-115] and 2SS[64-80, 76-94], were studied by means of NMR spectroscopy. The former variant contains two disulfide bridges in the alpha-domain, while the latter has one disulfide bridge in the beta-domain and the other one at the interface between two domains. Resonance assignments were performed using 3D TOCSY-HSQC and NOESY-HSQC spectra. The 15N-1H-HSQC spectrum of 2SS[6-127, 30-115] was similar to that of recombinant lysozyme as a whole, although a number of cross-peaks disappeared. On the other hand, the HSQC spectrum of 2SS[64-80, 76-94] was characteristic of unfolded proteins. The structure of 2SS[6-127, 30-115] was thoroughly examined on the basis of NOE contacts determined by NMR spectroscopy. The structure of the alpha-domain was quite similar to that of authentic lysozyme, while the beta-domain was largely unstructured. However, NMR data clearly demonstrated that some residual structures exist in the beta-domain. The beta1 and beta2 strands were maintained stably as an antiparallel beta-sheet. In addition, the residues 55 and 56 were located in the vicinity of the end of the B-helix. Further, the C-helix was properly set with side-chains of I88, V92, K96, and V99 facing toward the hydrophobic core in the alpha-domain. These residual structures inherent in the amino acid sequence were evaluated concerning the folding process of lysozyme. Our experiments imply that the establishment of the backbone conformation ranging from residues 76-99 plays a key role in attaining the cooperativity between two domains required for the folding transition. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Yasuo Noda Y. . . 5803 3 2 Atsushi Yokota A. . . 5803 3 3 Daisuke Horii D. . . 5803 3 4 Takeshi Tominaga T. . . 5803 3 5 Yoshiaki Tanisaka Y. . . 5803 3 6 Hideki Tachibana H. . . 5803 3 7 Shin-ichi Segawa S. . . 5803 3 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_HEWL _Assembly.Sf_category assembly _Assembly.Sf_framecode system_HEWL _Assembly.Entry_ID 5803 _Assembly.ID 1 _Assembly.Name 'hen egg white lysozyme' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'all disulfide bound' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number 3.2.1.17 _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 5803 1 stop_ loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 'hen lysozyme Cys mutants, C64A/C80A' 1 $HEWL . . . native . . . . . 5803 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . 1 CYS 7 7 SG . 1 . 1 CYS 128 128 SG . . . . . . . . . . 5803 1 2 disulfide single . 1 . 1 CYS 31 31 SG . 1 . 1 CYS 116 116 SG . . . . . . . . . . 5803 1 3 disulfide single . 1 . 1 CYS 77 77 SG . 1 . 1 CYS 95 95 SG . . . . . . . . . . 5803 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'hen egg white lysozyme' system 5803 1 HEWL abbreviation 5803 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID Hydrolase(O-Glycosyl) 5803 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_HEWL _Entity.Sf_category entity _Entity.Sf_framecode HEWL _Entity.Entry_ID 5803 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'three-disulfide variant of hen lysozyme' _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; MKVFGRCELAAAMKRHGLDN YRGYSLGNWVCAAKFESNFN TQATNRNTDGSTDYGILQIN SRWWANDGRTPGSRNLCNIP ASALLSSDITASVNCAKKIV SDGNGMNAWVAWRNRCKGTD VQAWIRGCRL ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 130 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all disulfide bound' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 14374 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details ; Hen lysozyme with Cys64 and Cys80 replaced by Ala and three disulfide bridges between Cys6 and Cys127, between Cys30 and Cys115, and between Cys76 and Cys94. ; _Entity.DB_query_date 2008-08-19 _Entity.DB_query_revised_last_date 2008-08-19 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID . . SWISS-PROT P00698 . 'Lysozyme C precursor (1,4-beta-N-acetylmuramidase C) (Allergen Gal d 4) (Allergen Gal d IV)' . . . . . 99.23 147 98.45 98.45 2.46e-68 . . . . 5803 1 . . GenBank AAL69327 . 'egg white lysozyme [Gallus gallus]' . . . . . 99.23 147 98.45 98.45 2.46e-68 . . . . 5803 1 . . GenBank AAA48943 . 'lysozyme (' . . . . . 99.23 147 98.45 98.45 2.46e-68 . . . . 5803 1 . . PDB 8LYZ . 'An X-Ray Study Of The Structure And Binding Properties Of Iodine-Inactivated Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 7LYZ . 'Protein Model Building By The Use Of A Constrained- Restrained Least-Squares Procedure' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 6LYZ . 'Real-Space Refinement Of The Structure Of Hen Egg-White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 6LYT . 'Comparison Of Radiation-Induced Decay And Structure Refinement From X-Ray Data Collected From Lysozyme Crystals At Low And Ambient Temperatures' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 5LYZ . 'Real-Space Refinement Of The Structure Of Hen Egg-White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 5LYT . 'Comparison Of Radiation-Induced Decay And Structure Refinement From X-Ray Data Collected From Lysozyme Crystals At Low And Ambient Temperatures' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 5LYM . 'Studies Of Monoclinic Hen Egg White Lysozyme. Iv. X-Ray Refinement At 1.8 Angstrom Resolution And A Comparison Of The Variable Regions In The Polymorphic Forms' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 4LZT . 'Atomic Resolution Refinement Of Triclinic Hew Lysozyme At 295k' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 4LYZ . 'Real-Space Refinement Of The Structure Of Hen Egg-White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 4LYT . 'Comparison Of Radiation-Induced Decay And Structure Refinement From X-Ray Data Collected From Lysozyme Crystals At Low And Ambient Temperatures' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 4LYO . 'Cross-Linked Chicken Lysozyme Crystal In Neat Acetonitrile, Then Back-Soaked In Water' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 4LYM . 'Crystal Structure Of Low Humidity Tetragonal Lysozyme At 2.1-Angstroms Resolution. Variability In Hydration Shell And Its Structural Consequences' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 3LZT . 'Refinement Of Triclinic Lysozyme At Atomic Resolution' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 3LYZ . 'Real-Space Refinement Of The Structure Of Hen Egg-White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 3LYT . 'Comparison Of Radiation-Induced Decay And Structure Refinement From X-Ray Data Collected From Lysozyme Crystals At Low And Ambient Temperatures' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 3LYO . 'Cross-Linked Chicken Lysozyme Crystal In 95% Acetonitrile- Water' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 3LYM . 'Crystal Structure Of Hen Egg-White Lysozyme At A Hydrostatic Pressure Of 1000 Atmospheres' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 3HFM . 'Structure Of An Antibody-Antigen Complex. Crystal Structure Of The HyHEL-10 Fab-Lysozyme Complex' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 3D9A . 'High Resolution Crystal Structure Structure Of Hyhel10 Fab Complexed To Hen Egg Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 3B6L . 'Crystal Structure Of Lysozyme Folded In Sds And 2-Methyl-2, 4-Pentanediol' . . . . . 99.23 147 98.45 98.45 2.46e-68 . . . . 5803 1 . . PDB 2Z19 . 'Phase Transition Of Monoclinic Lysozyme Crystal Soaked In A Saturated Nacl Solution' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2Z18 . 'Phase Transition Of Monoclinic Lysozyme Crystal Soaked In A 10% Nacl Solution' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2Z12 . 'Structure Of The Transformed Monoclinic Lysozyme By Controlled Dehydration' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2YVB . 'High Resolution X-Ray Crystal Structure Of Tetragonal Hen Egg White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2YSS . 'Crystal Structure Of Humanized Hyhel-10 Fv Mutant(Hq39kw47y)-Hen Lysozyme Complex' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2VB1 . 'Hewl At 0.65 Angstrom Resolution' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2Q0M . 'Tricarbonylmanganese(I)-Lysozyme Complex : A Structurally Characterized Organometallic Protein' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2PC2 . 'Lysozyme Cocrystallized With Tris-Dipicolinate Eu Complex' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2LZT . 'Refinement Of Triclinic Lysozyme. Ii. The Method Of Stereochemically Restrained Least-Squares' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2LZH . 'The Structures Of The Monoclinic And Orthorhombic Forms Of Hen Egg-White Lysozyme At 6 Angstroms Resolution.' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2LYZ . 'Real-Space Refinement Of The Structure Of Hen Egg-White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2LYO . 'Cross-Linked Chicken Lysozyme Crystal In 90% Acetonitrile- Water' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2LYM . 'Crystal Structure Of Hen Egg-White Lysozyme At A Hydrostatic Pressure Of 1000 Atmospheres' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2I6Z . 'X-Ray Diffraction Studies Of Adducts Between Anticancer Platinum Drugs And Hen Egg White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2I26 . 'Crystal Structure Analysis Of The Nurse Shark New Antigen Receptor Ancestral Variable Domain In Complex With Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2I25 . 'Crystal Structure Analysis Of The Nurse Shark New Antigen Receptor Pbla8 Variable Domain In Complex With Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2HUB . 'Structure Of Hen Egg-White Lysozyme Determined From Crystals Grown In Ph 7.5' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2HU3 . 'Parent Structure Of Hen Egg White Lysozyme Grown In Acidic Ph 4.8. Refinement For Comparison With Crosslinked Molecules Of Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2HU1 . 'Crystal Structure Analysis Of Hen Egg White Lyszoyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2HTX . 'Crystal Structure Analysis Of Hen Egg White Lysozyme Crosslinked By Polymerized Glutaraldehyde In Acidic Environment' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2HSO . 'Multipattern Rietveld Refinement With Protein Powder Data: An Approach To Higher Resolution' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2HS9 . 'Multipattern Rietveld Refinement With Protein Powder Data: An Approach To Higher Resolution' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2HS7 . 'Multipattern Rietveld Refinement With Protein Powder Data: An Approach To Higher Resolution' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2H9K . 'Structure Of Hen Egg White Lysozyme Soaked With Ni-Cyclam' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2H9J . 'Structure Of Hen Egg White Lysozyme Soaked With Ni2- Xylylbicyclam' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2G4Q . 'Anomalous Substructure Of Lysozyme At Ph 8.0' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2G4P . 'Anomalous Substructure Of Lysozyme At Ph 4.5' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2FBB . 'Crystal Structure Analysis Of Hexagonal Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2F4G . 'Triclinic Cross-Linked Lysozyme Soaked In Bromoethanol 1m' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2F4A . 'Triclinic Cross-Linked Lysozyme Soaked With Thiourea 1.5m' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2F30 . 'Triclinic Cross-Linked Lysozyme Soaked With 4.5m Urea' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2F2N . 'Triclinic Hen Egg Lysozyme Cross-Linked By Glutaraldehyde' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2EPE . 'Crystal Structure Analysis Of Hen Egg White Lysozyme Grown By Capillary Method' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2EKS . 'Crystal Structure Of Humanized Hyhel-10 Fv-Hen Lysozyme Complex' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2EIZ . 'Crystal Structure Of Humanized Hyhel-10 Fv Mutant(Hw47y)- Hen Lysozyme Complex' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2DQJ . 'Crystal Structure Of Hyhel-10 Fv (Wild-Type) Complexed With Hen Egg Lysozyme At 1.8a Resolution' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2DQI . 'Crystal Structure Of Hyhel-10 Fv Mutant (Ly50a) Complexed With Hen Egg Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2DQH . 'Crystal Structure Of Hyhel-10 Fv Mutant (Hy58a) Complexed With Hen Egg Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2DQG . 'Crystal Structure Of Hyhel-10 Fv Mutant (Hy53f) Complexed With Hen Egg Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2DQF . 'Crystal Structure Of Hyhel-10 Fv Mutant (Y33ay53a) Complexed With Hen Egg Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2DQE . 'Crystal Structure Of Hyhel-10 Fv Mutant (Hy53a) Complexed With Hen Egg Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2DQD . 'Crystal Structure Of Hyhel-10 Fv Mutant (Hy50f) Complexed With Hen Egg Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2DQC . 'Crystal Structure Of Hyhel-10 Fv Mutant(Hy33f) Complexed With Hen Egg Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2D91 . 'Structure Of Hyper-Vil-Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2D6B . 'Novel Bromate Species Trapped Within A Protein Crystal' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2D4K . 'Monoclinic Hen Egg-White Lysozyme Crystallized At 313k' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2D4J . 'Transformed Monoclinic Crystal Of Hen Egg-White Lysozyme From A Heavy Water Solution' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2D4I . 'Monoclinic Hen Egg-White Lysozyme Crystallized At Ph4.5 Form Heavy Water Solution' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2CGI . 'Siras Structure Of Tetragonal Lysosyme Using Derivative Data Collected At The High Energy Remote Holmium Kedge' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2CDS . Lysozyme . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2C8P . 'Lysozyme (60sec) And Uv Laser Excited Fluorescence' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2C8O . 'Lysozyme (1sec) And Uv Lasr Excited Fluorescence' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2BPU . 'The Kedge Holmium Derivative Of Hen Egg-White Lysozyme At High Resolution From Single Wavelength Anomalous Diffraction' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2BLY . 'Hewl After A High Dose X-Ray "burn"' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2BLX . 'Hewl Before A High Dose X-Ray "burn"' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2B5Z . 'Hen Lysozyme Chemically Glycosylated' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2AUB . 'Lysozyme Structure Derived From Thin-Film-Based Crystals' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2A7F . 'On The Routine Use Of Soft X-Rays In Macromolecular Crystallography, Part Iii- The Optimal Data Collection Wavelength' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2A7D . 'On The Routine Use Of Soft X-Rays In Macromolecular Crystallography, Part Iii- The Optimal Data Collection Wavelength' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 2A6U . 'Ph Evolution Of Tetragonal Hewl At 4 Degrees Celcius.' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1ZVY . 'Crystal Structure Of The Vhh D3-L11 In Complex With Hen Egg White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1ZVH . 'Crystal Stucture Of The Vhh Domain D2-L24 In Complex With Hen Egg White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1ZV5 . 'Crystal Structure Of The Variable Domain Of The Camelid Heavy-Chain Antibody D2-L29 In Complex With Hen Egg White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1ZMY . 'Cabbcii-10 Vhh Framework With Cdr Loops Of Cablys3 Grafted On It And In Complex With Hen Egg White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1Z55 . 'Effect Of Alcohols On Protein Hydration' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1YQV . 'The Crystal Structure Of The Antibody Fab Hyhel5 Complex With Lysozyme At 1.7a Resolution' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1YL1 . 'Effect Of Alcohols On Protein Hydration' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1YL0 . 'Effect Of Alcohols On Protein Hydration' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1YKZ . 'Effect Of Alcohols On Protein Hydration' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1YKY . 'Effect Of Alcohols On Protein Hydration' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1YKX . 'Effect Of Alcohols On Protein Hydration' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1YIL . 'Structure Of Hen Egg White Lysozyme Soaked With Cu2- Xylylbicyclam' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1YIK . 'Structure Of Hen Egg White Lysozyme Soaked With Cu-Cyclam' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1XGU . 'Structure For Antibody Hyhel-63 Y33f Mutant Complexed With Hen Egg Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1XGT . 'Structure For Antibody Hyhel-63 Y33l Mutant Complexed With Hen Egg Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1XGR . 'Structure For Antibody Hyhel-63 Y33i Mutant Complexed With Hen Egg Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1XGQ . 'Structure For Antibody Hyhel-63 Y33v Mutant Complexed With Hen Egg Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1XGP . 'Structure For Antibody Hyhel-63 Y33a Mutant Complexed With Hen Egg Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1XFP . 'Crystal Structure Of The Cdr2 Germline Reversion Mutant Of Cab-Lys3 In Complex With Hen Egg White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1XEK . 'The Crystal Structures Of Lysozyme At Very Low Levels Of Hydration' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1XEJ . 'The Crystal Structures Of Lysozyme At Very Low Levels Of Hydration' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1XEI . 'The Crystal Structures Of Lysozyme At Very Low Levels Of Hydration' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1WTN . 'The Structure Of Hew Lysozyme Orthorhombic Crystal Growth Under A High Magnetic Field' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1WTM . 'X-Ray Structure Of Hew Lysozyme Orthorhombic Crystal Formed In The Earth's Magnetic Field' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1W6Z . 'High Energy Tetragonal Lysozyme X-Ray Structure' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1VFB . 'Bound Water Molecules And Conformational Stabilization Help Mediate An Antigen-Antibody Association' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1VED . 'The Crystal Structure Of The Orthorhombic Form Of Hen Egg White Lysozyme At 1.9 Angstroms Resolution In Space' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1VDT . 'The Crystal Structure Of The Tetragonal Form Of Hen Egg White Lysozyme At 1.7 Angstroms Resolution Under Basic Conditions In Space' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1VDS . 'The Crystal Structure Of The Tetragonal Form Of Hen Egg White Lysozyme At 1.6 Angstroms Resolution In Space' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1VDQ . 'The Crystal Structure Of The Orthorhombic Form Of Hen Egg White Lysozyme At 1.5 Angstroms Resolution' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1VDP . 'The Crystal Structure Of The Monoclinic Form Of Hen Egg White Lysozyme At 1.7 Angstroms Resolution In Space' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1VAU . 'Xenon Derivative Of Hen Egg-White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1VAT . 'Iodine Derivative Of Hen Egg-White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1V7T . 'Triclinic Lysozyme With Low Solvent Content Obtained By Phase Transition' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1V7S . 'Triclinic Hen Lysozyme Crystallized At 313k From A D2o Solution' . . . . . 98.46 129 98.44 98.44 2.03e-67 . . . . 5803 1 . . PDB 1UUZ . 'Ivy:a New Family Of Protein' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1UIH . 'Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1UIG . 'Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1UCO . 'Hen Egg-White Lysozyme, Low Humidity Form' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1UC0 . 'Crystal Structure Of Wild-Type Hen-Egg White Lysozyme Singly Labeled With 2',3'-Epoxypropyl Beta-Glycoside Of N- Acetyllactosamine' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1UA6 . 'Crystal Structure Of Hyhel-10 Fv Mutant Sfsf Complexed With Hen Egg White Lysozyme Complex' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1T6V . 'Crystal Structure Analysis Of The Nurse Shark New Antigen Receptor (Nar) Variable Domain In Complex With Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1T3P . 'Half-Sandwich Arene Ruthenium(Ii)-Enzyme Complex' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1SQ2 . 'Crystal Structure Analysis Of The Nurse Shark New Antigen Receptor (Nar) Variable Domain In Complex With Lyxozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1SFG . 'Binding Of Hexa-N-Acetylchitohexaose: A Powder Diffraction Study' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1SFB . 'Binding Of Penta-N-Acetylchitopentaose To Hew Lysozyme: A Powder Diffraction Study' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1SF7 . 'Binding Of Tetra-N-Acetylchitotetraose To Hew Lysozyme: A Powder Diffraction Study' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1SF6 . 'Binding Of N,N',N"-Triacetylchitotriose To Hew Lysozyme: A Powder Diffraction Study' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1SF4 . 'Binding Of N,N'-Diacetylchitobiose To Hew Lysozyme: A Powder Diffraction Study' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1RJC . 'Crystal Structure Of The Camelid Single Domain Antibody Cab- Lys2 In Complex With Hen Egg White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1RI8 . 'Crystal Structure Of The Camelid Single Domain Antibody 1d2l19 In Complex With Hen Egg White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1RFP . 'Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1RCM . 'Crystal Structure Of A Ubiquitin-Dependent Degradation Substrate: A Three-Disulfide Form Of Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1QTK . 'Crystal Structure Of Hew Lysozyme Under Pressure Of Krypton (55 Bar)' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1QIO . 'Specific Chemical And Structural Damage Caused By Intense Synchrotron Radiation To Hen Egg White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1PS5 . 'Structure Of The Monoclinic C2 Form Of Hen Egg-White Lysozyme At 2.0 Angstroms Resolution' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1P2C . 'Crystal Structure Analysis Of An Anti-Lysozyme Antibody' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1NDM . 'Crystal Structure Of Fab Fragment Of Antibody Hyhel-26 Complexed With Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1N4F . 'Para-Arsanilate Derivative Of Hen Egg-White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1MLC . 'Monoclonal Antibody Fab D44.1 Raised Against Chicken Egg- White Lysozyme Complexed With Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1MEL . 'Crystal Structure Of A Camel Single-Domain Vh Antibody Fragment In Complex With Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LZT . 'Refinement Of Triclinic Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LZN . 'Neutron Structure Of Hen Egg-White Lysozyme' . . . . . 98.46 129 98.44 98.44 2.13e-67 . . . . 5803 1 . . PDB 1LZH . 'The Structures Of The Monoclinic And Orthorhombic Forms Of Hen Egg-White Lysozyme At 6 Angstroms Resolution.' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LZC . 'Dissection Of Protein-Carbohydrate Interactions In Mutant Hen Egg-White Lysozyme Complexes And Their Hydrolytic Activity' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LZB . 'Dissection Of Protein-Carbohydrate Interactions In Mutant Hen Egg-White Lysozyme Complexes And Their Hydrolytic Activity' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LZA . 'Dissection Of Protein-Carbohydrate Interactions In Mutant Hen Egg-White Lysozyme Complexes And Their Hydrolytic Activity' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LZ9 . 'Anomalous Signal Of Solvent Bromines Used For Phasing Of Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LZ8 . 'Lysozyme Phased On Anomalous Signal Of Sulfurs And Chlorines' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LYZ . 'Real-Space Refinement Of The Structure Of Hen Egg-White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LYS . 'X-Ray Structure Of A Monoclinic Form Of Hen Egg-White Lysozyme Crystallized At 313k. Comparison Of Two Independent Molecules' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LYO . 'Cross-Linked Lysozyme Crystal In Neat Water' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LSG . 'Three-Dimensional Structure Of The Platelet Integrin Recognition Segment Of The Fibrinogen Gamma Chain Obtained By Carrier Protein-Driven Crystallization' . . . . . 100.00 144 98.46 98.46 4.48e-69 . . . . 5803 1 . . PDB 1LSF . 'The Influence Of Temperature On Lysozyme Crystals. Structure And Dynamics Of Protein And Water' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LSE . 'The Influence Of Temperature On Lysozyme Crystals. Structure And Dynamics Of Protein And Water' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LSD . 'The Influence Of Temperature On Lysozyme Crystals. Structure And Dynamics Of Protein And Water' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LSC . 'The Influence Of Temperature On Lysozyme Crystals. Structure And Dynamics Of Protein And Water' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LSB . 'The Influence Of Temperature On Lysozyme Crystals. Structure And Dynamics Of Protein And Water' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LSA . 'The Influence Of Temperature On Lysozyme Crystals. Structure And Dynamics Of Protein And Water' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LPI . 'Hew Lysozyme: Trp...Na Cation-Pi Interaction' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LMA . 'Protein Hydration And Water Structure: X-Ray Analysis Of A Closely Packed Protein Crystal With Very Low Solvent Content' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LKS . 'Hen Egg White Lysozyme Nitrate' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LKR . 'Monoclinic Hen Egg White Lysozyme Iodide' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LJK . 'Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 15% Trehalose' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LJJ . 'Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 10% Trehalose' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LJI . 'Crystal Structure Of Monoclinic Lysozyme Grown In Presence 10% Sorbitol' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LJH . 'Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 5% Glycerol' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LJG . 'Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 5% Glycerol' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LJF . 'Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 10% Sucrose' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LJE . 'Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 10% Sucrose' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LJ4 . 'Crystal Structure Of Monoclinic Lysozyme Grown At Ph 4.6' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LJ3 . 'Crystal Structure Of Monoclinic Lysozyme Grown At Ph 4.6' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1LCN . 'Monoclinic Hen Egg White Lysozyme, Thiocyanate Complex' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1KIR . 'Fv Mutant Y(A 50)s (Vl Domain) Of Mouse Monoclonal Antibody D1.3 Complexed With Hen Egg White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1KIQ . 'Fv Mutant Y(B 101)f (Vh Domain) Of Mouse Monoclonal Antibody D1.3 Complexed With Hen Egg White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1KIP . 'Fv Mutant Y(B 32)a (Vh Domain) Of Mouse Monoclonal Antibody D1.3 Complexed With Hen Egg White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1JTT . 'Degenerate Interfaces In Antigen-Antibody Complexes' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1JTO . 'Degenerate Interfaces In Antigen-Antibody Complexes' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1JPO . 'Low Temperature Orthorhombic Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1JJ3 . 'Crystal Structure Of Monoclinic Lysozyme Grown At Ph 4.6' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1JJ1 . 'Crystal Structure Of Orthorhombic Lysozyme Grown At Ph 4.6 In Presence Of 5% Sorbitol' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1JJ0 . 'Crystal Structure Of Tetragonal Lysozyme Grown In Presence Of 30% Sucrose' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1JIY . 'Crystal Structure Of Tetragonal Lysozyme Grown In Presence 20% Sorbitol' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1JIT . 'Crystal Structure Of Tetragonal Lysozyme Grown In Presence 30% Trehalose' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1JIS . 'Crystal Structure Of Tetragonal Lysozyme Grown At Ph 4.6' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1JA7 . 'Binding Of N-Acetylglucosamine To Chicken Egg Lysozyme: A Powder Diffraction Study' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1JA6 . 'Binding Of N-Acetylglucosamine To Chicken Egg Lysozyme: A Powder Diffraction Study' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1JA4 . 'Binding Of N-Acetylglucosamine To Chicken Egg Lysozyme: A Powder Diffraction Study' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1JA2 . 'Binding Of N-Acetylglucosamine To Chicken Egg Lysozyme: A Powder Diffraction Study' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1J1X . 'Crystal Structure Of Hyhel-10 Fv Mutant Ls93a Complexed With Hen Egg White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1J1P . 'Crystal Structure Of Hyhel-10 Fv Mutant Ls91a Complexed With Hen Egg White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1J1O . 'Crystal Structure Of Hyhel-10 Fv Mutant Ly50f Complexed With Hen Egg White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1IO5 . 'Hydrogen And Hydration Of Hen Egg-White Lysozyme Determined By Neutron Diffraction' . . . . . 98.46 129 98.44 98.44 2.13e-67 . . . . 5803 1 . . PDB 1IEE . 'Structure Of Tetragonal Hen Egg White Lysozyme At 0.94 A From Crystals Grown By The Counter-Diffusion Method' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1IC7 . 'Crystal Structure Of Hyhel-10 Fv Mutant(Hd32a99a)-Hen Lysozyme Complex' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1IC5 . 'Crystal Structure Of Hyhel-10 Fv Mutant(Hd99a)-Hen Lysozyme Complex' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1IC4 . 'Crystal Structure Of Hyhel-10 Fv Mutant(Hd32a)-Hen Lysozyme Complex' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1HSX . 'Lysozyme Grown At Basic Ph And Its Low Humidity Variant' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1HSW . 'Lysozyme (Mucopeptide N-Acetylmuramyl Hydrolase)' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1HF4 . 'Structural Effects Of Monovalent Anions On Polymorphic Lysozyme Crystals' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1HEW . 'Refinement Of An Enzyme Complex With Inhibitor Bound At Partial Occupancy. Hen Egg-White Lysozyme And Tri-N- Acetylchitotriose At 1.75 Angstroms Resolution' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1HEL . 'Structural And Thermodynamic Analysis Of Compensating Mutations Within The Core Of Chicken Egg White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1HC0 . 'Structure Of Lysozyme With Periodate' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1H87 . 'Gadolinium Derivative Of Tetragonal Hen Egg-White Lysozyme At 1.7 A Resolution' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1GXX . 'Solution Structure Of Lysozyme At Low And High Pressure' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1GXV . 'Solution Structure Of Lysozyme At Low And High Pressure' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1GWD . 'Tri-Iodide Derivative Of Hen Egg-White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1GPQ . 'Structure Of Ivy Complexed With Its Target, Hewl' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1G7M . 'Crystal Structure Of Hen Egg White Lysozyme (Hel) Complexed With The Mutant Anti-Hel Monoclonal Antibody D1.3 (Vlw92v)' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1G7L . 'Crystal Structure Of Hen Egg White Lysozyme (Hel) Complexed With The Mutant Anti-Hel Monoclonal Antibody D1.3 (Vlw92s)' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1G7J . 'Crystal Structure Of Hen Egg White Lysozyme (Hel) Complexed With The Mutant Anti-Hel Monoclonal Antibody D1.3 (Vlw92h)' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1G7I . 'Crystal Structure Of Hen Egg White Lysozyme (Hel) Complexed With The Mutant Anti-Hel Monoclonal Antibody D1.3 (Vlw92f)' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1G7H . 'Crystal Structure Of Hen Egg White Lysozyme (Hel) Complexed With The Mutant Anti-Hel Monoclonal Antibody D1.3(Vlw92a)' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1FDL . 'Crystallographic Refinement Of The Three-Dimensional Structure Of The Fab D1.3-Lysozyme Complex At 2.5- Angstroms Resolution' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1F10 . 'Crystal Structure Of Orthorhombic Lysozyme Grown At Ph 6.5 At 88% Relative Humidity' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1F0W . 'Crystal Structure Of Orthorhombic Lysozyme Grown At Ph 6.5' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1E8L . 'Nmr Solution Structure Of Hen Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1DQJ . 'Crystal Structure Of The Anti-Lysozyme Antibody Hyhel-63 Complexed With Hen Egg White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1DPX . 'Structure Of Hen Egg-White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1DPW . 'Structure Of Hen Egg-White Lysozyme In Complex With Mpd' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1C10 . 'Crystal Structure Of Hew Lysozyme Under Pressure Of Xenon (8 Bar)' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1C08 . 'Crystal Structure Of Hyhel-10 Fv-Hen Lysozyme Complex' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1BWJ . 'The 1.8 A Structure Of Microgravity Grown Tetragonal Hen Egg White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1BWI . 'The 1.8 A Structure Of Microbatch Oil Drop Grown Tetragonal Hen Egg White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1BWH . 'The 1.8 A Structure Of Ground Control Grown Tetragonal Hen Egg White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1BVX . 'The 1.8 A Structure Of Gel Grown Tetragonal Hen Egg White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1BVK . 'Humanized Anti-Lysozyme Fv Complexed With Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1BHZ . 'Low Temperature Middle Resolution Structure Of Hen Egg White Lysozyme From Masc Data' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1BGI . 'Orthorhombic Lysozyme Crystallized At High Temperature (310k)' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1B2K . 'Structural Effects Of Monovalent Anions On Polymorphic Lysozyme Crystals' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1B0D . 'Structural Effects Of Monovalent Anions On Polymorphic Lysozyme Crystals' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1AZF . 'Chicken Egg White Lysozyme Crystal Grown In Bromide Solution' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 1AKI . 'The Structure Of The Orthorhombic Form Of Hen Egg-White Lysozyme At 1.5 Angstroms Resolution' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 194L . 'The 1.40 A Structure Of Spacehab-01 Hen Egg White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . PDB 193L . 'The 1.33 A Structure Of Tetragonal Hen Egg White Lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . BMRB 5069 . 'hen egg white lysozyme variant' . . . . . 100.00 130 98.46 98.46 1.21e-68 . . . . 5803 1 . . BMRB 5068 . 'hen egg white lysozyme' . . . . . 100.00 130 98.46 98.46 9.56e-69 . . . . 5803 1 . . BMRB 4943 . 'Chicken Egg White Lysozyme' . . . . . 99.23 133 98.45 98.45 5.52e-68 . . . . 5803 1 . . BMRB 4562 . 'hen egg white lysozyme' . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 . . BMRB 1093 . lysozyme . . . . . 99.23 129 98.45 98.45 5.95e-68 . . . . 5803 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'three-disulfide variant of hen lysozyme' common 5803 1 C64A/C80A variant 5803 1 C64A/C80A abbreviation 5803 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 0 MET . 5803 1 2 1 LYS . 5803 1 3 2 VAL . 5803 1 4 3 PHE . 5803 1 5 4 GLY . 5803 1 6 5 ARG . 5803 1 7 6 CYS . 5803 1 8 7 GLU . 5803 1 9 8 LEU . 5803 1 10 9 ALA . 5803 1 11 10 ALA . 5803 1 12 11 ALA . 5803 1 13 12 MET . 5803 1 14 13 LYS . 5803 1 15 14 ARG . 5803 1 16 15 HIS . 5803 1 17 16 GLY . 5803 1 18 17 LEU . 5803 1 19 18 ASP . 5803 1 20 19 ASN . 5803 1 21 20 TYR . 5803 1 22 21 ARG . 5803 1 23 22 GLY . 5803 1 24 23 TYR . 5803 1 25 24 SER . 5803 1 26 25 LEU . 5803 1 27 26 GLY . 5803 1 28 27 ASN . 5803 1 29 28 TRP . 5803 1 30 29 VAL . 5803 1 31 30 CYS . 5803 1 32 31 ALA . 5803 1 33 32 ALA . 5803 1 34 33 LYS . 5803 1 35 34 PHE . 5803 1 36 35 GLU . 5803 1 37 36 SER . 5803 1 38 37 ASN . 5803 1 39 38 PHE . 5803 1 40 39 ASN . 5803 1 41 40 THR . 5803 1 42 41 GLN . 5803 1 43 42 ALA . 5803 1 44 43 THR . 5803 1 45 44 ASN . 5803 1 46 45 ARG . 5803 1 47 46 ASN . 5803 1 48 47 THR . 5803 1 49 48 ASP . 5803 1 50 49 GLY . 5803 1 51 50 SER . 5803 1 52 51 THR . 5803 1 53 52 ASP . 5803 1 54 53 TYR . 5803 1 55 54 GLY . 5803 1 56 55 ILE . 5803 1 57 56 LEU . 5803 1 58 57 GLN . 5803 1 59 58 ILE . 5803 1 60 59 ASN . 5803 1 61 60 SER . 5803 1 62 61 ARG . 5803 1 63 62 TRP . 5803 1 64 63 TRP . 5803 1 65 64 ALA . 5803 1 66 65 ASN . 5803 1 67 66 ASP . 5803 1 68 67 GLY . 5803 1 69 68 ARG . 5803 1 70 69 THR . 5803 1 71 70 PRO . 5803 1 72 71 GLY . 5803 1 73 72 SER . 5803 1 74 73 ARG . 5803 1 75 74 ASN . 5803 1 76 75 LEU . 5803 1 77 76 CYS . 5803 1 78 77 ASN . 5803 1 79 78 ILE . 5803 1 80 79 PRO . 5803 1 81 80 ALA . 5803 1 82 81 SER . 5803 1 83 82 ALA . 5803 1 84 83 LEU . 5803 1 85 84 LEU . 5803 1 86 85 SER . 5803 1 87 86 SER . 5803 1 88 87 ASP . 5803 1 89 88 ILE . 5803 1 90 89 THR . 5803 1 91 90 ALA . 5803 1 92 91 SER . 5803 1 93 92 VAL . 5803 1 94 93 ASN . 5803 1 95 94 CYS . 5803 1 96 95 ALA . 5803 1 97 96 LYS . 5803 1 98 97 LYS . 5803 1 99 98 ILE . 5803 1 100 99 VAL . 5803 1 101 100 SER . 5803 1 102 101 ASP . 5803 1 103 102 GLY . 5803 1 104 103 ASN . 5803 1 105 104 GLY . 5803 1 106 105 MET . 5803 1 107 106 ASN . 5803 1 108 107 ALA . 5803 1 109 108 TRP . 5803 1 110 109 VAL . 5803 1 111 110 ALA . 5803 1 112 111 TRP . 5803 1 113 112 ARG . 5803 1 114 113 ASN . 5803 1 115 114 ARG . 5803 1 116 115 CYS . 5803 1 117 116 LYS . 5803 1 118 117 GLY . 5803 1 119 118 THR . 5803 1 120 119 ASP . 5803 1 121 120 VAL . 5803 1 122 121 GLN . 5803 1 123 122 ALA . 5803 1 124 123 TRP . 5803 1 125 124 ILE . 5803 1 126 125 ARG . 5803 1 127 126 GLY . 5803 1 128 127 CYS . 5803 1 129 128 ARG . 5803 1 130 129 LEU . 5803 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . MET 1 1 5803 1 . LYS 2 2 5803 1 . VAL 3 3 5803 1 . PHE 4 4 5803 1 . GLY 5 5 5803 1 . ARG 6 6 5803 1 . CYS 7 7 5803 1 . GLU 8 8 5803 1 . LEU 9 9 5803 1 . ALA 10 10 5803 1 . ALA 11 11 5803 1 . ALA 12 12 5803 1 . MET 13 13 5803 1 . LYS 14 14 5803 1 . ARG 15 15 5803 1 . HIS 16 16 5803 1 . GLY 17 17 5803 1 . LEU 18 18 5803 1 . ASP 19 19 5803 1 . ASN 20 20 5803 1 . TYR 21 21 5803 1 . ARG 22 22 5803 1 . GLY 23 23 5803 1 . TYR 24 24 5803 1 . SER 25 25 5803 1 . LEU 26 26 5803 1 . GLY 27 27 5803 1 . ASN 28 28 5803 1 . TRP 29 29 5803 1 . VAL 30 30 5803 1 . CYS 31 31 5803 1 . ALA 32 32 5803 1 . ALA 33 33 5803 1 . LYS 34 34 5803 1 . PHE 35 35 5803 1 . GLU 36 36 5803 1 . SER 37 37 5803 1 . ASN 38 38 5803 1 . PHE 39 39 5803 1 . ASN 40 40 5803 1 . THR 41 41 5803 1 . GLN 42 42 5803 1 . ALA 43 43 5803 1 . THR 44 44 5803 1 . ASN 45 45 5803 1 . ARG 46 46 5803 1 . ASN 47 47 5803 1 . THR 48 48 5803 1 . ASP 49 49 5803 1 . GLY 50 50 5803 1 . SER 51 51 5803 1 . THR 52 52 5803 1 . ASP 53 53 5803 1 . TYR 54 54 5803 1 . GLY 55 55 5803 1 . ILE 56 56 5803 1 . LEU 57 57 5803 1 . GLN 58 58 5803 1 . ILE 59 59 5803 1 . ASN 60 60 5803 1 . SER 61 61 5803 1 . ARG 62 62 5803 1 . TRP 63 63 5803 1 . TRP 64 64 5803 1 . ALA 65 65 5803 1 . ASN 66 66 5803 1 . ASP 67 67 5803 1 . GLY 68 68 5803 1 . ARG 69 69 5803 1 . THR 70 70 5803 1 . PRO 71 71 5803 1 . GLY 72 72 5803 1 . SER 73 73 5803 1 . ARG 74 74 5803 1 . ASN 75 75 5803 1 . LEU 76 76 5803 1 . CYS 77 77 5803 1 . ASN 78 78 5803 1 . ILE 79 79 5803 1 . PRO 80 80 5803 1 . ALA 81 81 5803 1 . SER 82 82 5803 1 . ALA 83 83 5803 1 . LEU 84 84 5803 1 . LEU 85 85 5803 1 . SER 86 86 5803 1 . SER 87 87 5803 1 . ASP 88 88 5803 1 . ILE 89 89 5803 1 . THR 90 90 5803 1 . ALA 91 91 5803 1 . SER 92 92 5803 1 . VAL 93 93 5803 1 . ASN 94 94 5803 1 . CYS 95 95 5803 1 . ALA 96 96 5803 1 . LYS 97 97 5803 1 . LYS 98 98 5803 1 . ILE 99 99 5803 1 . VAL 100 100 5803 1 . SER 101 101 5803 1 . ASP 102 102 5803 1 . GLY 103 103 5803 1 . ASN 104 104 5803 1 . GLY 105 105 5803 1 . MET 106 106 5803 1 . ASN 107 107 5803 1 . ALA 108 108 5803 1 . TRP 109 109 5803 1 . VAL 110 110 5803 1 . ALA 111 111 5803 1 . TRP 112 112 5803 1 . ARG 113 113 5803 1 . ASN 114 114 5803 1 . ARG 115 115 5803 1 . CYS 116 116 5803 1 . LYS 117 117 5803 1 . GLY 118 118 5803 1 . THR 119 119 5803 1 . ASP 120 120 5803 1 . VAL 121 121 5803 1 . GLN 122 122 5803 1 . ALA 123 123 5803 1 . TRP 124 124 5803 1 . ILE 125 125 5803 1 . ARG 126 126 5803 1 . GLY 127 127 5803 1 . CYS 128 128 5803 1 . ARG 129 129 5803 1 . LEU 130 130 5803 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 5803 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $HEWL . 9031 . . 'Gallus gallus' Chicken . . Eukaryota Metazoa Gallus gallus . . . . 'egg white' . . . . . . . . . . . . . . . . 5803 1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Entity_experimental_src_list.Sf_category experimental_source _Entity_experimental_src_list.Sf_framecode experimental_source _Entity_experimental_src_list.Entry_ID 5803 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $HEWL . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli AD18 . . . . . . . . . . . . plasmid . . . . . . . . . 5803 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5803 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'three-disulfide variant of hen lysozyme' [U-15N] . . 1 $HEWL . . . 0.3 1.0 mM . . . . 5803 1 stop_ save_ ####################### # Sample conditions # ####################### save_EX-cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode EX-cond_1 _Sample_condition_list.Entry_ID 5803 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 3.8 0.1 na 5803 1 temperature 298 0.1 K 5803 1 stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Software.Sf_category software _Software.Sf_framecode XWINNMR _Software.Entry_ID 5803 _Software.ID 1 _Software.Name XWINNMR _Software.Version 2.6 _Software.Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 5803 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5803 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 NMR_spectrometer Bruker DRX . 600 . . . 5803 1 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 5803 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 DQF-COSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5803 1 2 NOESY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5803 1 3 HOHAHA . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5803 1 4 '15N 3D-NOESY-HSQC' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5803 1 5 '15N 3D-TOCSY-HSQC' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5803 1 6 '1H-15N HSQC' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5803 1 7 '15N 3D-HSQC-NOESY-HSQC' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5803 1 stop_ save_ save_NMR_spec_expt__0_1 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1 _NMR_spec_expt.Entry_ID 5803 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name DQF-COSY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 5803 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name NOESY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 5803 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name HOHAHA _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_4 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4 _NMR_spec_expt.Entry_ID 5803 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name '15N 3D-NOESY-HSQC' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_5 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_5 _NMR_spec_expt.Entry_ID 5803 _NMR_spec_expt.ID 5 _NMR_spec_expt.Name '15N 3D-TOCSY-HSQC' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_6 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_6 _NMR_spec_expt.Entry_ID 5803 _NMR_spec_expt.ID 6 _NMR_spec_expt.Name '1H-15N HSQC' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_7 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_7 _NMR_spec_expt.Entry_ID 5803 _NMR_spec_expt.ID 7 _NMR_spec_expt.Name '15N 3D-HSQC-NOESY-HSQC' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 5803 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 external direct 1.0 . . . . . . . . . 5803 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_1 _Assigned_chem_shift_list.Entry_ID 5803 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $EX-cond_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 DQF-COSY 1 $sample_1 . 5803 1 2 NOESY 1 $sample_1 . 5803 1 3 HOHAHA 1 $sample_1 . 5803 1 4 '15N 3D-NOESY-HSQC' 1 $sample_1 . 5803 1 5 '15N 3D-TOCSY-HSQC' 1 $sample_1 . 5803 1 6 '1H-15N HSQC' 1 $sample_1 . 5803 1 7 '15N 3D-HSQC-NOESY-HSQC' 1 $sample_1 . 5803 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 2 2 LYS H H 1 8.84 0.02 . 1 . . . . 1 . . . 5803 1 2 . 1 1 2 2 LYS HA H 1 4.37 0.02 . 1 . . . . 1 . . . 5803 1 3 . 1 1 2 2 LYS HB2 H 1 1.75 0.02 . 2 . . . . 1 . . . 5803 1 4 . 1 1 2 2 LYS HB3 H 1 1.50 0.02 . 2 . . . . 1 . . . 5803 1 5 . 1 1 3 3 VAL H H 1 8.87 0.02 . 1 . . . . 2 . . . 5803 1 6 . 1 1 3 3 VAL HA H 1 4.84 0.02 . 1 . . . . 2 . . . 5803 1 7 . 1 1 3 3 VAL HB H 1 2.01 0.02 . 1 . . . . 2 . . . 5803 1 8 . 1 1 3 3 VAL HG11 H 1 1.04 0.02 . 2 . . . . 2 . . . 5803 1 9 . 1 1 3 3 VAL HG12 H 1 1.04 0.02 . 2 . . . . 2 . . . 5803 1 10 . 1 1 3 3 VAL HG13 H 1 1.04 0.02 . 2 . . . . 2 . . . 5803 1 11 . 1 1 3 3 VAL HG21 H 1 0.94 0.02 . 2 . . . . 2 . . . 5803 1 12 . 1 1 3 3 VAL HG22 H 1 0.94 0.02 . 2 . . . . 2 . . . 5803 1 13 . 1 1 3 3 VAL HG23 H 1 0.94 0.02 . 2 . . . . 2 . . . 5803 1 14 . 1 1 4 4 PHE H H 1 8.69 0.02 . 1 . . . . 3 . . . 5803 1 15 . 1 1 4 4 PHE HA H 1 4.26 0.02 . 1 . . . . 3 . . . 5803 1 16 . 1 1 4 4 PHE HB2 H 1 3.19 0.02 . 2 . . . . 3 . . . 5803 1 17 . 1 1 4 4 PHE HB3 H 1 2.67 0.02 . 2 . . . . 3 . . . 5803 1 18 . 1 1 4 4 PHE HD1 H 1 6.97 0.02 . 1 . . . . 3 . . . 5803 1 19 . 1 1 4 4 PHE HD2 H 1 6.97 0.02 . 1 . . . . 3 . . . 5803 1 20 . 1 1 4 4 PHE HE1 H 1 7.20 0.02 . 1 . . . . 3 . . . 5803 1 21 . 1 1 4 4 PHE HE2 H 1 7.20 0.02 . 1 . . . . 3 . . . 5803 1 22 . 1 1 4 4 PHE HZ H 1 7.48 0.02 . 1 . . . . 3 . . . 5803 1 23 . 1 1 5 5 GLY H H 1 8.46 0.02 . 1 . . . . 4 . . . 5803 1 24 . 1 1 5 5 GLY HA2 H 1 4.32 0.02 . 2 . . . . 4 . . . 5803 1 25 . 1 1 5 5 GLY HA3 H 1 3.97 0.02 . 2 . . . . 4 . . . 5803 1 26 . 1 1 6 6 ARG H H 1 8.58 0.02 . 1 . . . . 5 . . . 5803 1 27 . 1 1 6 6 ARG HA H 1 3.36 0.02 . 1 . . . . 5 . . . 5803 1 28 . 1 1 6 6 ARG HB2 H 1 2.08 0.02 . 2 . . . . 5 . . . 5803 1 29 . 1 1 6 6 ARG HD2 H 1 3.87 0.02 . 2 . . . . 5 . . . 5803 1 30 . 1 1 6 6 ARG HE H 1 7.58 0.02 . 1 . . . . 5 . . . 5803 1 31 . 1 1 7 7 CYS H H 1 8.71 0.02 . 1 . . . . 6 . . . 5803 1 32 . 1 1 7 7 CYS HA H 1 4.74 0.02 . 1 . . . . 6 . . . 5803 1 33 . 1 1 7 7 CYS HB2 H 1 3.22 0.02 . 2 . . . . 6 . . . 5803 1 34 . 1 1 7 7 CYS HB3 H 1 2.78 0.02 . 2 . . . . 6 . . . 5803 1 35 . 1 1 8 8 GLU H H 1 8.29 0.02 . 1 . . . . 7 . . . 5803 1 36 . 1 1 8 8 GLU HA H 1 4.10 0.02 . 1 . . . . 7 . . . 5803 1 37 . 1 1 8 8 GLU HB2 H 1 2.30 0.02 . 2 . . . . 7 . . . 5803 1 38 . 1 1 8 8 GLU HG2 H 1 2.34 0.02 . 2 . . . . 7 . . . 5803 1 39 . 1 1 8 8 GLU HG3 H 1 2.52 0.02 . 2 . . . . 7 . . . 5803 1 40 . 1 1 9 9 LEU H H 1 8.65 0.02 . 1 . . . . 8 . . . 5803 1 41 . 1 1 9 9 LEU HA H 1 3.78 0.02 . 1 . . . . 8 . . . 5803 1 42 . 1 1 9 9 LEU HB2 H 1 1.61 0.02 . 2 . . . . 8 . . . 5803 1 43 . 1 1 9 9 LEU HB3 H 1 0.93 0.02 . 2 . . . . 8 . . . 5803 1 44 . 1 1 9 9 LEU HG H 1 1.54 0.02 . 1 . . . . 8 . . . 5803 1 45 . 1 1 9 9 LEU HD11 H 1 0.59 0.02 . 2 . . . . 8 . . . 5803 1 46 . 1 1 9 9 LEU HD12 H 1 0.59 0.02 . 2 . . . . 8 . . . 5803 1 47 . 1 1 9 9 LEU HD13 H 1 0.59 0.02 . 2 . . . . 8 . . . 5803 1 48 . 1 1 9 9 LEU HD21 H 1 -0.02 0.02 . 2 . . . . 8 . . . 5803 1 49 . 1 1 9 9 LEU HD22 H 1 -0.02 0.02 . 2 . . . . 8 . . . 5803 1 50 . 1 1 9 9 LEU HD23 H 1 -0.02 0.02 . 2 . . . . 8 . . . 5803 1 51 . 1 1 10 10 ALA H H 1 8.44 0.02 . 1 . . . . 9 . . . 5803 1 52 . 1 1 10 10 ALA HA H 1 3.60 0.02 . 1 . . . . 9 . . . 5803 1 53 . 1 1 10 10 ALA HB1 H 1 1.57 0.02 . 1 . . . . 9 . . . 5803 1 54 . 1 1 10 10 ALA HB2 H 1 1.57 0.02 . 1 . . . . 9 . . . 5803 1 55 . 1 1 10 10 ALA HB3 H 1 1.57 0.02 . 1 . . . . 9 . . . 5803 1 56 . 1 1 11 11 ALA H H 1 8.18 0.02 . 1 . . . . 10 . . . 5803 1 57 . 1 1 11 11 ALA HA H 1 3.98 0.02 . 1 . . . . 10 . . . 5803 1 58 . 1 1 11 11 ALA HB1 H 1 1.54 0.02 . 1 . . . . 10 . . . 5803 1 59 . 1 1 11 11 ALA HB2 H 1 1.54 0.02 . 1 . . . . 10 . . . 5803 1 60 . 1 1 11 11 ALA HB3 H 1 1.54 0.02 . 1 . . . . 10 . . . 5803 1 61 . 1 1 12 12 ALA H H 1 7.79 0.02 . 1 . . . . 11 . . . 5803 1 62 . 1 1 12 12 ALA HA H 1 4.27 0.02 . 1 . . . . 11 . . . 5803 1 63 . 1 1 12 12 ALA HB1 H 1 1.51 0.02 . 1 . . . . 11 . . . 5803 1 64 . 1 1 12 12 ALA HB2 H 1 1.51 0.02 . 1 . . . . 11 . . . 5803 1 65 . 1 1 12 12 ALA HB3 H 1 1.51 0.02 . 1 . . . . 11 . . . 5803 1 66 . 1 1 13 13 MET H H 1 9.16 0.02 . 1 . . . . 12 . . . 5803 1 67 . 1 1 13 13 MET HA H 1 3.45 0.02 . 1 . . . . 12 . . . 5803 1 68 . 1 1 13 13 MET HB2 H 1 1.91 0.02 . 2 . . . . 12 . . . 5803 1 69 . 1 1 13 13 MET HG2 H 1 2.76 0.02 . 2 . . . . 12 . . . 5803 1 70 . 1 1 13 13 MET HG3 H 1 1.34 0.02 . 2 . . . . 12 . . . 5803 1 71 . 1 1 13 13 MET HE1 H 1 1.66 0.02 . 1 . . . . 12 . . . 5803 1 72 . 1 1 13 13 MET HE2 H 1 1.66 0.02 . 1 . . . . 12 . . . 5803 1 73 . 1 1 13 13 MET HE3 H 1 1.66 0.02 . 1 . . . . 12 . . . 5803 1 74 . 1 1 14 14 LYS H H 1 8.54 0.02 . 1 . . . . 13 . . . 5803 1 75 . 1 1 14 14 LYS HA H 1 3.98 0.02 . 1 . . . . 13 . . . 5803 1 76 . 1 1 14 14 LYS HB2 H 1 2.23 0.02 . 2 . . . . 13 . . . 5803 1 77 . 1 1 14 14 LYS HB3 H 1 1.94 0.02 . 2 . . . . 13 . . . 5803 1 78 . 1 1 14 14 LYS HD2 H 1 1.75 0.02 . 2 . . . . 13 . . . 5803 1 79 . 1 1 14 14 LYS HD3 H 1 3.03 0.02 . 2 . . . . 13 . . . 5803 1 80 . 1 1 15 15 ARG H H 1 8.25 0.02 . 1 . . . . 14 . . . 5803 1 81 . 1 1 15 15 ARG HA H 1 4.13 0.02 . 1 . . . . 14 . . . 5803 1 82 . 1 1 15 15 ARG HB2 H 1 1.98 0.02 . 2 . . . . 14 . . . 5803 1 83 . 1 1 15 15 ARG HG2 H 1 1.58 0.02 . 2 . . . . 14 . . . 5803 1 84 . 1 1 15 15 ARG HD2 H 1 3.15 0.02 . 2 . . . . 14 . . . 5803 1 85 . 1 1 15 15 ARG HE H 1 7.16 0.02 . 1 . . . . 14 . . . 5803 1 86 . 1 1 16 16 HIS H H 1 7.36 0.02 . 1 . . . . 15 . . . 5803 1 87 . 1 1 16 16 HIS HA H 1 4.56 0.02 . 1 . . . . 15 . . . 5803 1 88 . 1 1 16 16 HIS HB2 H 1 3.71 0.02 . 2 . . . . 15 . . . 5803 1 89 . 1 1 16 16 HIS HB3 H 1 2.57 0.02 . 2 . . . . 15 . . . 5803 1 90 . 1 1 16 16 HIS HD2 H 1 7.53 0.02 . 1 . . . . 15 . . . 5803 1 91 . 1 1 16 16 HIS HE1 H 1 8.84 0.02 . 1 . . . . 15 . . . 5803 1 92 . 1 1 17 17 GLY H H 1 7.63 0.02 . 1 . . . . 16 . . . 5803 1 93 . 1 1 17 17 GLY HA2 H 1 3.91 0.02 . 2 . . . . 16 . . . 5803 1 94 . 1 1 17 17 GLY HA3 H 1 4.13 0.02 . 2 . . . . 16 . . . 5803 1 95 . 1 1 18 18 LEU H H 1 7.16 0.02 . 1 . . . . 17 . . . 5803 1 96 . 1 1 18 18 LEU HA H 1 3.93 0.02 . 1 . . . . 17 . . . 5803 1 97 . 1 1 18 18 LEU HB2 H 1 0.74 0.02 . 2 . . . . 17 . . . 5803 1 98 . 1 1 18 18 LEU HB3 H 1 0.27 0.02 . 2 . . . . 17 . . . 5803 1 99 . 1 1 18 18 LEU HG H 1 0.69 0.02 . 1 . . . . 17 . . . 5803 1 100 . 1 1 18 18 LEU HD11 H 1 -0.69 0.02 . 2 . . . . 17 . . . 5803 1 101 . 1 1 18 18 LEU HD12 H 1 -0.69 0.02 . 2 . . . . 17 . . . 5803 1 102 . 1 1 18 18 LEU HD13 H 1 -0.69 0.02 . 2 . . . . 17 . . . 5803 1 103 . 1 1 18 18 LEU HD21 H 1 -0.10 0.02 . 2 . . . . 17 . . . 5803 1 104 . 1 1 18 18 LEU HD22 H 1 -0.10 0.02 . 2 . . . . 17 . . . 5803 1 105 . 1 1 18 18 LEU HD23 H 1 -0.10 0.02 . 2 . . . . 17 . . . 5803 1 106 . 1 1 19 19 ASP H H 1 8.82 0.02 . 1 . . . . 18 . . . 5803 1 107 . 1 1 19 19 ASP HA H 1 4.26 0.02 . 1 . . . . 18 . . . 5803 1 108 . 1 1 19 19 ASP HB2 H 1 3.02 0.02 . 2 . . . . 18 . . . 5803 1 109 . 1 1 19 19 ASP HB3 H 1 2.39 0.02 . 2 . . . . 18 . . . 5803 1 110 . 1 1 20 20 ASN H H 1 8.40 0.02 . 1 . . . . 19 . . . 5803 1 111 . 1 1 20 20 ASN HA H 1 3.96 0.02 . 1 . . . . 19 . . . 5803 1 112 . 1 1 20 20 ASN HB2 H 1 2.85 0.02 . 2 . . . . 19 . . . 5803 1 113 . 1 1 20 20 ASN HB3 H 1 3.06 0.02 . 2 . . . . 19 . . . 5803 1 114 . 1 1 20 20 ASN HD21 H 1 7.47 0.02 . 2 . . . . 19 . . . 5803 1 115 . 1 1 20 20 ASN HD22 H 1 6.63 0.02 . 2 . . . . 19 . . . 5803 1 116 . 1 1 21 21 TYR H H 1 8.13 0.02 . 1 . . . . 20 . . . 5803 1 117 . 1 1 21 21 TYR HA H 1 4.22 0.02 . 1 . . . . 20 . . . 5803 1 118 . 1 1 21 21 TYR HB2 H 1 3.06 0.02 . 2 . . . . 20 . . . 5803 1 119 . 1 1 21 21 TYR HB3 H 1 3.22 0.02 . 2 . . . . 20 . . . 5803 1 120 . 1 1 21 21 TYR HD1 H 1 7.18 0.02 . 1 . . . . 20 . . . 5803 1 121 . 1 1 21 21 TYR HD2 H 1 7.18 0.02 . 1 . . . . 20 . . . 5803 1 122 . 1 1 21 21 TYR HE1 H 1 6.96 0.02 . 1 . . . . 20 . . . 5803 1 123 . 1 1 21 21 TYR HE2 H 1 6.96 0.02 . 1 . . . . 20 . . . 5803 1 124 . 1 1 22 22 ARG H H 1 9.02 0.02 . 1 . . . . 21 . . . 5803 1 125 . 1 1 22 22 ARG HA H 1 3.64 0.02 . 1 . . . . 21 . . . 5803 1 126 . 1 1 22 22 ARG HB2 H 1 1.90 0.02 . 2 . . . . 21 . . . 5803 1 127 . 1 1 22 22 ARG HB3 H 1 2.26 0.02 . 2 . . . . 21 . . . 5803 1 128 . 1 1 22 22 ARG HG2 H 1 1.23 0.02 . 2 . . . . 21 . . . 5803 1 129 . 1 1 22 22 ARG HD2 H 1 3.08 0.02 . 2 . . . . 21 . . . 5803 1 130 . 1 1 22 22 ARG HE H 1 7.16 0.02 . 1 . . . . 21 . . . 5803 1 131 . 1 1 23 23 GLY H H 1 7.62 0.02 . 1 . . . . 22 . . . 5803 1 132 . 1 1 23 23 GLY HA2 H 1 3.88 0.02 . 2 . . . . 22 . . . 5803 1 133 . 1 1 23 23 GLY HA3 H 1 3.49 0.02 . 2 . . . . 22 . . . 5803 1 134 . 1 1 24 24 TYR H H 1 7.68 0.02 . 1 . . . . 23 . . . 5803 1 135 . 1 1 24 24 TYR HA H 1 4.56 0.02 . 1 . . . . 23 . . . 5803 1 136 . 1 1 24 24 TYR HB2 H 1 3.30 0.02 . 2 . . . . 23 . . . 5803 1 137 . 1 1 24 24 TYR HB3 H 1 2.47 0.02 . 2 . . . . 23 . . . 5803 1 138 . 1 1 24 24 TYR HD1 H 1 7.03 0.02 . 1 . . . . 23 . . . 5803 1 139 . 1 1 24 24 TYR HD2 H 1 7.03 0.02 . 1 . . . . 23 . . . 5803 1 140 . 1 1 24 24 TYR HE1 H 1 6.71 0.02 . 1 . . . . 23 . . . 5803 1 141 . 1 1 24 24 TYR HE2 H 1 6.71 0.02 . 1 . . . . 23 . . . 5803 1 142 . 1 1 25 25 SER H H 1 9.08 0.02 . 1 . . . . 24 . . . 5803 1 143 . 1 1 25 25 SER HA H 1 4.51 0.02 . 1 . . . . 24 . . . 5803 1 144 . 1 1 25 25 SER HB2 H 1 4.21 0.02 . 2 . . . . 24 . . . 5803 1 145 . 1 1 25 25 SER HB3 H 1 4.37 0.02 . 2 . . . . 24 . . . 5803 1 146 . 1 1 26 26 LEU H H 1 9.13 0.02 . 1 . . . . 25 . . . 5803 1 147 . 1 1 26 26 LEU HA H 1 4.39 0.02 . 1 . . . . 25 . . . 5803 1 148 . 1 1 26 26 LEU HB2 H 1 1.63 0.02 . 2 . . . . 25 . . . 5803 1 149 . 1 1 26 26 LEU HG H 1 1.60 0.02 . 1 . . . . 25 . . . 5803 1 150 . 1 1 26 26 LEU HD11 H 1 0.87 0.02 . 2 . . . . 25 . . . 5803 1 151 . 1 1 26 26 LEU HD12 H 1 0.87 0.02 . 2 . . . . 25 . . . 5803 1 152 . 1 1 26 26 LEU HD13 H 1 0.87 0.02 . 2 . . . . 25 . . . 5803 1 153 . 1 1 26 26 LEU HD21 H 1 1.00 0.02 . 2 . . . . 25 . . . 5803 1 154 . 1 1 26 26 LEU HD22 H 1 1.00 0.02 . 2 . . . . 25 . . . 5803 1 155 . 1 1 26 26 LEU HD23 H 1 1.00 0.02 . 2 . . . . 25 . . . 5803 1 156 . 1 1 27 27 GLY H H 1 9.65 0.02 . 1 . . . . 26 . . . 5803 1 157 . 1 1 27 27 GLY HA2 H 1 4.19 0.02 . 2 . . . . 26 . . . 5803 1 158 . 1 1 27 27 GLY HA3 H 1 3.67 0.02 . 2 . . . . 26 . . . 5803 1 159 . 1 1 28 28 ASN H H 1 8.20 0.02 . 1 . . . . 27 . . . 5803 1 160 . 1 1 28 28 ASN HA H 1 4.18 0.02 . 1 . . . . 27 . . . 5803 1 161 . 1 1 28 28 ASN HB2 H 1 2.88 0.02 . 2 . . . . 27 . . . 5803 1 162 . 1 1 28 28 ASN HB3 H 1 2.29 0.02 . 2 . . . . 27 . . . 5803 1 163 . 1 1 28 28 ASN HD21 H 1 7.78 0.02 . 2 . . . . 27 . . . 5803 1 164 . 1 1 29 29 TRP H H 1 7.19 0.02 . 1 . . . . 28 . . . 5803 1 165 . 1 1 29 29 TRP HA H 1 3.76 0.02 . 1 . . . . 28 . . . 5803 1 166 . 1 1 29 29 TRP HB2 H 1 3.26 0.02 . 2 . . . . 28 . . . 5803 1 167 . 1 1 29 29 TRP HD1 H 1 7.27 0.02 . 1 . . . . 28 . . . 5803 1 168 . 1 1 29 29 TRP HE1 H 1 9.33 0.02 . 1 . . . . 28 . . . 5803 1 169 . 1 1 29 29 TRP HE3 H 1 6.66 0.02 . 1 . . . . 28 . . . 5803 1 170 . 1 1 29 29 TRP HZ2 H 1 7.42 0.02 . 1 . . . . 28 . . . 5803 1 171 . 1 1 29 29 TRP HZ3 H 1 6.06 0.02 . 1 . . . . 28 . . . 5803 1 172 . 1 1 29 29 TRP HH2 H 1 6.72 0.02 . 1 . . . . 28 . . . 5803 1 173 . 1 1 30 30 VAL H H 1 7.58 0.02 . 1 . . . . 29 . . . 5803 1 174 . 1 1 30 30 VAL HA H 1 3.45 0.02 . 1 . . . . 29 . . . 5803 1 175 . 1 1 30 30 VAL HB H 1 1.95 0.02 . 1 . . . . 29 . . . 5803 1 176 . 1 1 30 30 VAL HG11 H 1 1.27 0.02 . 2 . . . . 29 . . . 5803 1 177 . 1 1 30 30 VAL HG12 H 1 1.27 0.02 . 2 . . . . 29 . . . 5803 1 178 . 1 1 30 30 VAL HG13 H 1 1.27 0.02 . 2 . . . . 29 . . . 5803 1 179 . 1 1 30 30 VAL HG21 H 1 0.94 0.02 . 2 . . . . 29 . . . 5803 1 180 . 1 1 30 30 VAL HG22 H 1 0.94 0.02 . 2 . . . . 29 . . . 5803 1 181 . 1 1 30 30 VAL HG23 H 1 0.94 0.02 . 2 . . . . 29 . . . 5803 1 182 . 1 1 31 31 CYS H H 1 8.06 0.02 . 1 . . . . 30 . . . 5803 1 183 . 1 1 31 31 CYS HA H 1 2.51 0.02 . 1 . . . . 30 . . . 5803 1 184 . 1 1 31 31 CYS HB2 H 1 2.95 0.02 . 2 . . . . 30 . . . 5803 1 185 . 1 1 31 31 CYS HB3 H 1 2.63 0.02 . 2 . . . . 30 . . . 5803 1 186 . 1 1 32 32 ALA H H 1 8.15 0.02 . 1 . . . . 31 . . . 5803 1 187 . 1 1 32 32 ALA HA H 1 3.71 0.02 . 1 . . . . 31 . . . 5803 1 188 . 1 1 32 32 ALA HB1 H 1 1.02 0.02 . 1 . . . . 31 . . . 5803 1 189 . 1 1 32 32 ALA HB2 H 1 1.02 0.02 . 1 . . . . 31 . . . 5803 1 190 . 1 1 32 32 ALA HB3 H 1 1.02 0.02 . 1 . . . . 31 . . . 5803 1 191 . 1 1 33 33 ALA H H 1 7.60 0.02 . 1 . . . . 32 . . . 5803 1 192 . 1 1 33 33 ALA HA H 1 4.05 0.02 . 1 . . . . 32 . . . 5803 1 193 . 1 1 33 33 ALA HB1 H 1 1.32 0.02 . 1 . . . . 32 . . . 5803 1 194 . 1 1 33 33 ALA HB2 H 1 1.32 0.02 . 1 . . . . 32 . . . 5803 1 195 . 1 1 33 33 ALA HB3 H 1 1.32 0.02 . 1 . . . . 32 . . . 5803 1 196 . 1 1 34 34 LYS H H 1 7.99 0.02 . 1 . . . . 33 . . . 5803 1 197 . 1 1 34 34 LYS HA H 1 2.54 0.02 . 1 . . . . 33 . . . 5803 1 198 . 1 1 34 34 LYS HB2 H 1 1.08 0.02 . 2 . . . . 33 . . . 5803 1 199 . 1 1 34 34 LYS HG2 H 1 0.44 0.02 . 2 . . . . 33 . . . 5803 1 200 . 1 1 34 34 LYS HG3 H 1 -0.48 0.02 . 2 . . . . 33 . . . 5803 1 201 . 1 1 34 34 LYS HD2 H 1 0.71 0.02 . 2 . . . . 33 . . . 5803 1 202 . 1 1 34 34 LYS HD3 H 1 0.61 0.02 . 2 . . . . 33 . . . 5803 1 203 . 1 1 34 34 LYS HE2 H 1 2.67 0.02 . 2 . . . . 33 . . . 5803 1 204 . 1 1 34 34 LYS HE3 H 1 2.32 0.02 . 2 . . . . 33 . . . 5803 1 205 . 1 1 34 34 LYS HZ1 H 1 7.33 0.02 . 1 . . . . 33 . . . 5803 1 206 . 1 1 34 34 LYS HZ2 H 1 7.33 0.02 . 1 . . . . 33 . . . 5803 1 207 . 1 1 34 34 LYS HZ3 H 1 7.33 0.02 . 1 . . . . 33 . . . 5803 1 208 . 1 1 35 35 PHE H H 1 7.41 0.02 . 1 . . . . 34 . . . 5803 1 209 . 1 1 35 35 PHE HA H 1 4.32 0.02 . 1 . . . . 34 . . . 5803 1 210 . 1 1 35 35 PHE HB2 H 1 2.30 0.02 . 2 . . . . 34 . . . 5803 1 211 . 1 1 35 35 PHE HB3 H 1 3.18 0.02 . 2 . . . . 34 . . . 5803 1 212 . 1 1 35 35 PHE HD1 H 1 7.23 0.02 . 1 . . . . 34 . . . 5803 1 213 . 1 1 35 35 PHE HD2 H 1 7.23 0.02 . 1 . . . . 34 . . . 5803 1 214 . 1 1 35 35 PHE HE1 H 1 7.37 0.02 . 1 . . . . 34 . . . 5803 1 215 . 1 1 35 35 PHE HE2 H 1 7.37 0.02 . 1 . . . . 34 . . . 5803 1 216 . 1 1 35 35 PHE HZ H 1 7.51 0.02 . 1 . . . . 34 . . . 5803 1 217 . 1 1 36 36 GLU H H 1 8.64 0.02 . 1 . . . . 35 . . . 5803 1 218 . 1 1 36 36 GLU HA H 1 4.47 0.02 . 1 . . . . 35 . . . 5803 1 219 . 1 1 36 36 GLU HB2 H 1 2.07 0.02 . 2 . . . . 35 . . . 5803 1 220 . 1 1 37 37 SER H H 1 8.07 0.02 . 1 . . . . 36 . . . 5803 1 221 . 1 1 37 37 SER HA H 1 4.57 0.02 . 1 . . . . 36 . . . 5803 1 222 . 1 1 37 37 SER HB2 H 1 4.46 0.02 . 2 . . . . 36 . . . 5803 1 223 . 1 1 37 37 SER HB3 H 1 3.59 0.02 . 2 . . . . 36 . . . 5803 1 224 . 1 1 38 38 ASN H H 1 8.17 0.02 . 1 . . . . 37 . . . 5803 1 225 . 1 1 38 38 ASN HA H 1 4.53 0.02 . 1 . . . . 37 . . . 5803 1 226 . 1 1 38 38 ASN HB2 H 1 3.30 0.02 . 2 . . . . 37 . . . 5803 1 227 . 1 1 38 38 ASN HB3 H 1 2.47 0.02 . 2 . . . . 37 . . . 5803 1 228 . 1 1 38 38 ASN HD21 H 1 7.39 0.02 . 2 . . . . 37 . . . 5803 1 229 . 1 1 38 38 ASN HD22 H 1 6.72 0.02 . 2 . . . . 37 . . . 5803 1 230 . 1 1 39 39 PHE H H 1 7.37 0.02 . 1 . . . . 38 . . . 5803 1 231 . 1 1 39 39 PHE HA H 1 3.88 0.02 . 1 . . . . 38 . . . 5803 1 232 . 1 1 39 39 PHE HB2 H 1 3.61 0.02 . 2 . . . . 38 . . . 5803 1 233 . 1 1 39 39 PHE HD1 H 1 6.96 0.02 . 1 . . . . 38 . . . 5803 1 234 . 1 1 39 39 PHE HD2 H 1 6.96 0.02 . 1 . . . . 38 . . . 5803 1 235 . 1 1 39 39 PHE HE1 H 1 7.41 0.02 . 1 . . . . 38 . . . 5803 1 236 . 1 1 39 39 PHE HE2 H 1 7.41 0.02 . 1 . . . . 38 . . . 5803 1 237 . 1 1 39 39 PHE HZ H 1 6.97 0.02 . 1 . . . . 38 . . . 5803 1 238 . 1 1 40 40 ASN H H 1 7.60 0.02 . 1 . . . . 39 . . . 5803 1 239 . 1 1 40 40 ASN HA H 1 4.98 0.02 . 1 . . . . 39 . . . 5803 1 240 . 1 1 40 40 ASN HB2 H 1 3.45 0.02 . 2 . . . . 39 . . . 5803 1 241 . 1 1 40 40 ASN HB3 H 1 2.97 0.02 . 2 . . . . 39 . . . 5803 1 242 . 1 1 40 40 ASN HD21 H 1 7.63 0.02 . 2 . . . . 39 . . . 5803 1 243 . 1 1 40 40 ASN HD22 H 1 7.03 0.02 . 2 . . . . 39 . . . 5803 1 244 . 1 1 42 42 GLN H H 1 8.09 0.02 . 1 . . . . 41 . . . 5803 1 245 . 1 1 42 42 GLN HA H 1 4.54 0.02 . 1 . . . . 41 . . . 5803 1 246 . 1 1 42 42 GLN HB2 H 1 2.48 0.02 . 2 . . . . 41 . . . 5803 1 247 . 1 1 42 42 GLN HB3 H 1 1.90 0.02 . 2 . . . . 41 . . . 5803 1 248 . 1 1 42 42 GLN HE21 H 1 7.64 0.02 . 2 . . . . 41 . . . 5803 1 249 . 1 1 42 42 GLN HE22 H 1 6.90 0.02 . 2 . . . . 41 . . . 5803 1 250 . 1 1 43 43 ALA H H 1 6.87 0.02 . 1 . . . . 42 . . . 5803 1 251 . 1 1 43 43 ALA HA H 1 4.14 0.02 . 1 . . . . 42 . . . 5803 1 252 . 1 1 43 43 ALA HB1 H 1 1.36 0.02 . 1 . . . . 42 . . . 5803 1 253 . 1 1 43 43 ALA HB2 H 1 1.36 0.02 . 1 . . . . 42 . . . 5803 1 254 . 1 1 43 43 ALA HB3 H 1 1.36 0.02 . 1 . . . . 42 . . . 5803 1 255 . 1 1 44 44 THR H H 1 8.44 0.02 . 1 . . . . 43 . . . 5803 1 256 . 1 1 44 44 THR HA H 1 5.14 0.02 . 1 . . . . 43 . . . 5803 1 257 . 1 1 44 44 THR HB H 1 3.73 0.02 . 1 . . . . 43 . . . 5803 1 258 . 1 1 44 44 THR HG21 H 1 1.08 0.02 . 1 . . . . 43 . . . 5803 1 259 . 1 1 44 44 THR HG22 H 1 1.08 0.02 . 1 . . . . 43 . . . 5803 1 260 . 1 1 44 44 THR HG23 H 1 1.08 0.02 . 1 . . . . 43 . . . 5803 1 261 . 1 1 45 45 ASN H H 1 8.21 0.02 . 1 . . . . 44 . . . 5803 1 262 . 1 1 45 45 ASN HA H 1 5.03 0.02 . 1 . . . . 44 . . . 5803 1 263 . 1 1 45 45 ASN HB2 H 1 2.66 0.02 . 2 . . . . 44 . . . 5803 1 264 . 1 1 45 45 ASN HD21 H 1 7.43 0.02 . 2 . . . . 44 . . . 5803 1 265 . 1 1 45 45 ASN HD22 H 1 6.92 0.02 . 2 . . . . 44 . . . 5803 1 266 . 1 1 46 46 ARG H H 1 8.93 0.02 . 1 . . . . 45 . . . 5803 1 267 . 1 1 46 46 ARG HA H 1 4.55 0.02 . 1 . . . . 45 . . . 5803 1 268 . 1 1 46 46 ARG HB2 H 1 1.69 0.02 . 2 . . . . 45 . . . 5803 1 269 . 1 1 46 46 ARG HB3 H 1 1.84 0.02 . 2 . . . . 45 . . . 5803 1 270 . 1 1 46 46 ARG HD2 H 1 3.16 0.02 . 2 . . . . 45 . . . 5803 1 271 . 1 1 46 46 ARG HE H 1 7.12 0.02 . 1 . . . . 45 . . . 5803 1 272 . 1 1 47 47 ASN H H 1 8.88 0.02 . 1 . . . . 46 . . . 5803 1 273 . 1 1 47 47 ASN HA H 1 5.11 0.02 . 1 . . . . 46 . . . 5803 1 274 . 1 1 47 47 ASN HB2 H 1 2.80 0.02 . 2 . . . . 46 . . . 5803 1 275 . 1 1 47 47 ASN HB3 H 1 2.88 0.02 . 2 . . . . 46 . . . 5803 1 276 . 1 1 47 47 ASN HD21 H 1 6.88 0.02 . 2 . . . . 46 . . . 5803 1 277 . 1 1 48 48 THR H H 1 8.88 0.02 . 1 . . . . 47 . . . 5803 1 278 . 1 1 48 48 THR HA H 1 4.09 0.02 . 1 . . . . 47 . . . 5803 1 279 . 1 1 48 48 THR HB H 1 4.37 0.02 . 1 . . . . 47 . . . 5803 1 280 . 1 1 48 48 THR HG21 H 1 1.34 0.02 . 1 . . . . 47 . . . 5803 1 281 . 1 1 48 48 THR HG22 H 1 1.34 0.02 . 1 . . . . 47 . . . 5803 1 282 . 1 1 48 48 THR HG23 H 1 1.34 0.02 . 1 . . . . 47 . . . 5803 1 283 . 1 1 49 49 ASP H H 1 7.85 0.02 . 1 . . . . 48 . . . 5803 1 284 . 1 1 49 49 ASP HA H 1 4.57 0.02 . 1 . . . . 48 . . . 5803 1 285 . 1 1 49 49 ASP HB2 H 1 2.65 0.02 . 2 . . . . 48 . . . 5803 1 286 . 1 1 49 49 ASP HB3 H 1 3.08 0.02 . 2 . . . . 48 . . . 5803 1 287 . 1 1 50 50 GLY H H 1 7.93 0.02 . 1 . . . . 49 . . . 5803 1 288 . 1 1 50 50 GLY HA2 H 1 4.40 0.02 . 2 . . . . 49 . . . 5803 1 289 . 1 1 50 50 GLY HA3 H 1 3.73 0.02 . 2 . . . . 49 . . . 5803 1 290 . 1 1 51 51 SER H H 1 8.27 0.02 . 1 . . . . 50 . . . 5803 1 291 . 1 1 51 51 SER HA H 1 4.63 0.02 . 1 . . . . 50 . . . 5803 1 292 . 1 1 51 51 SER HB2 H 1 3.76 0.02 . 2 . . . . 50 . . . 5803 1 293 . 1 1 51 51 SER HB3 H 1 4.19 0.02 . 2 . . . . 50 . . . 5803 1 294 . 1 1 52 52 THR H H 1 9.18 0.02 . 1 . . . . 51 . . . 5803 1 295 . 1 1 52 52 THR HA H 1 4.96 0.02 . 1 . . . . 51 . . . 5803 1 296 . 1 1 52 52 THR HG21 H 1 0.31 0.02 . 1 . . . . 51 . . . 5803 1 297 . 1 1 52 52 THR HG22 H 1 0.31 0.02 . 1 . . . . 51 . . . 5803 1 298 . 1 1 52 52 THR HG23 H 1 0.31 0.02 . 1 . . . . 51 . . . 5803 1 299 . 1 1 53 53 ASP HA H 1 5.26 0.02 . 1 . . . . 52 . . . 5803 1 300 . 1 1 53 53 ASP HB2 H 1 2.61 0.02 . 2 . . . . 52 . . . 5803 1 301 . 1 1 53 53 ASP HB3 H 1 2.02 0.02 . 2 . . . . 52 . . . 5803 1 302 . 1 1 54 54 TYR HA H 1 4.90 0.02 . 1 . . . . 53 . . . 5803 1 303 . 1 1 54 54 TYR HB2 H 1 2.66 0.02 . 2 . . . . 53 . . . 5803 1 304 . 1 1 54 54 TYR HD1 H 1 7.10 0.02 . 1 . . . . 53 . . . 5803 1 305 . 1 1 54 54 TYR HD2 H 1 7.10 0.02 . 1 . . . . 53 . . . 5803 1 306 . 1 1 54 54 TYR HE1 H 1 6.79 0.02 . 1 . . . . 53 . . . 5803 1 307 . 1 1 54 54 TYR HE2 H 1 6.79 0.02 . 1 . . . . 53 . . . 5803 1 308 . 1 1 55 55 GLY H H 1 9.19 0.02 . 1 . . . . 54 . . . 5803 1 309 . 1 1 55 55 GLY HA2 H 1 4.55 0.02 . 2 . . . . 54 . . . 5803 1 310 . 1 1 55 55 GLY HA3 H 1 4.14 0.02 . 2 . . . . 54 . . . 5803 1 311 . 1 1 56 56 ILE H H 1 9.48 0.02 . 1 . . . . 55 . . . 5803 1 312 . 1 1 56 56 ILE HA H 1 4.29 0.02 . 1 . . . . 55 . . . 5803 1 313 . 1 1 56 56 ILE HB H 1 1.63 0.02 . 1 . . . . 55 . . . 5803 1 314 . 1 1 56 56 ILE HG12 H 1 1.08 0.02 . 2 . . . . 55 . . . 5803 1 315 . 1 1 56 56 ILE HG13 H 1 1.48 0.02 . 2 . . . . 55 . . . 5803 1 316 . 1 1 56 56 ILE HG21 H 1 0.91 0.02 . 1 . . . . 55 . . . 5803 1 317 . 1 1 56 56 ILE HG22 H 1 0.91 0.02 . 1 . . . . 55 . . . 5803 1 318 . 1 1 56 56 ILE HG23 H 1 0.91 0.02 . 1 . . . . 55 . . . 5803 1 319 . 1 1 56 56 ILE HD11 H 1 0.75 0.02 . 1 . . . . 55 . . . 5803 1 320 . 1 1 56 56 ILE HD12 H 1 0.75 0.02 . 1 . . . . 55 . . . 5803 1 321 . 1 1 56 56 ILE HD13 H 1 0.75 0.02 . 1 . . . . 55 . . . 5803 1 322 . 1 1 57 57 LEU H H 1 9.00 0.02 . 1 . . . . 56 . . . 5803 1 323 . 1 1 57 57 LEU HA H 1 4.45 0.02 . 1 . . . . 56 . . . 5803 1 324 . 1 1 57 57 LEU HB2 H 1 1.75 0.02 . 2 . . . . 56 . . . 5803 1 325 . 1 1 57 57 LEU HB3 H 1 1.52 0.02 . 2 . . . . 56 . . . 5803 1 326 . 1 1 57 57 LEU HG H 1 1.21 0.02 . 1 . . . . 56 . . . 5803 1 327 . 1 1 57 57 LEU HD11 H 1 0.52 0.02 . 2 . . . . 56 . . . 5803 1 328 . 1 1 57 57 LEU HD12 H 1 0.52 0.02 . 2 . . . . 56 . . . 5803 1 329 . 1 1 57 57 LEU HD13 H 1 0.52 0.02 . 2 . . . . 56 . . . 5803 1 330 . 1 1 57 57 LEU HD21 H 1 0.33 0.02 . 2 . . . . 56 . . . 5803 1 331 . 1 1 57 57 LEU HD22 H 1 0.33 0.02 . 2 . . . . 56 . . . 5803 1 332 . 1 1 57 57 LEU HD23 H 1 0.33 0.02 . 2 . . . . 56 . . . 5803 1 333 . 1 1 58 58 GLN H H 1 8.01 0.02 . 1 . . . . 57 . . . 5803 1 334 . 1 1 58 58 GLN HA H 1 3.38 0.02 . 1 . . . . 57 . . . 5803 1 335 . 1 1 58 58 GLN HB2 H 1 2.01 0.02 . 2 . . . . 57 . . . 5803 1 336 . 1 1 58 58 GLN HB3 H 1 2.22 0.02 . 2 . . . . 57 . . . 5803 1 337 . 1 1 58 58 GLN HE21 H 1 5.26 0.02 . 2 . . . . 57 . . . 5803 1 338 . 1 1 59 59 ILE HB H 1 1.74 0.02 . 1 . . . . 58 . . . 5803 1 339 . 1 1 59 59 ILE HG21 H 1 0.87 0.02 . 1 . . . . 58 . . . 5803 1 340 . 1 1 59 59 ILE HG22 H 1 0.87 0.02 . 1 . . . . 58 . . . 5803 1 341 . 1 1 59 59 ILE HG23 H 1 0.87 0.02 . 1 . . . . 58 . . . 5803 1 342 . 1 1 60 60 ASN HA H 1 5.53 0.02 . 1 . . . . 59 . . . 5803 1 343 . 1 1 60 60 ASN HB2 H 1 3.07 0.02 . 2 . . . . 59 . . . 5803 1 344 . 1 1 60 60 ASN HB3 H 1 3.41 0.02 . 2 . . . . 59 . . . 5803 1 345 . 1 1 61 61 SER H H 1 9.09 0.02 . 1 . . . . 60 . . . 5803 1 346 . 1 1 61 61 SER HA H 1 5.13 0.02 . 1 . . . . 60 . . . 5803 1 347 . 1 1 62 62 ARG H H 1 8.64 0.02 . 1 . . . . 61 . . . 5803 1 348 . 1 1 62 62 ARG HA H 1 4.04 0.02 . 1 . . . . 61 . . . 5803 1 349 . 1 1 62 62 ARG HB2 H 1 1.63 0.02 . 2 . . . . 61 . . . 5803 1 350 . 1 1 62 62 ARG HB3 H 1 1.46 0.02 . 2 . . . . 61 . . . 5803 1 351 . 1 1 63 63 TRP H H 1 7.21 0.02 . 1 . . . . 62 . . . 5803 1 352 . 1 1 63 63 TRP HA H 1 4.40 0.02 . 1 . . . . 62 . . . 5803 1 353 . 1 1 63 63 TRP HB2 H 1 1.91 0.02 . 2 . . . . 62 . . . 5803 1 354 . 1 1 63 63 TRP HD1 H 1 6.99 0.02 . 1 . . . . 62 . . . 5803 1 355 . 1 1 63 63 TRP HE1 H 1 10.15 0.02 . 1 . . . . 62 . . . 5803 1 356 . 1 1 63 63 TRP HZ2 H 1 7.41 0.02 . 1 . . . . 62 . . . 5803 1 357 . 1 1 64 64 TRP HD1 H 1 6.99 0.02 . 1 . . . . 63 . . . 5803 1 358 . 1 1 64 64 TRP HE1 H 1 10.15 0.02 . 1 . . . . 63 . . . 5803 1 359 . 1 1 64 64 TRP HZ2 H 1 7.41 0.02 . 1 . . . . 63 . . . 5803 1 360 . 1 1 68 68 GLY H H 1 8.33 0.02 . 1 . . . . 67 . . . 5803 1 361 . 1 1 68 68 GLY HA2 H 1 4.03 0.02 . 2 . . . . 67 . . . 5803 1 362 . 1 1 69 69 ARG H H 1 8.14 0.02 . 1 . . . . 68 . . . 5803 1 363 . 1 1 69 69 ARG HA H 1 4.78 0.02 . 1 . . . . 68 . . . 5803 1 364 . 1 1 69 69 ARG HB2 H 1 1.80 0.02 . 2 . . . . 68 . . . 5803 1 365 . 1 1 69 69 ARG HG2 H 1 1.50 0.02 . 2 . . . . 68 . . . 5803 1 366 . 1 1 70 70 THR HA H 1 4.61 0.02 . 1 . . . . 69 . . . 5803 1 367 . 1 1 70 70 THR HB H 1 4.16 0.02 . 1 . . . . 69 . . . 5803 1 368 . 1 1 71 71 PRO HB2 H 1 1.88 0.02 . 2 . . . . 70 . . . 5803 1 369 . 1 1 71 71 PRO HB3 H 1 2.30 0.02 . 2 . . . . 70 . . . 5803 1 370 . 1 1 72 72 GLY H H 1 8.76 0.02 . 1 . . . . 71 . . . 5803 1 371 . 1 1 72 72 GLY HA2 H 1 3.83 0.02 . 2 . . . . 71 . . . 5803 1 372 . 1 1 74 74 ARG H H 1 8.37 0.02 . 1 . . . . 73 . . . 5803 1 373 . 1 1 74 74 ARG HA H 1 4.30 0.02 . 1 . . . . 73 . . . 5803 1 374 . 1 1 74 74 ARG HB2 H 1 1.76 0.02 . 2 . . . . 73 . . . 5803 1 375 . 1 1 74 74 ARG HG2 H 1 1.57 0.02 . 2 . . . . 73 . . . 5803 1 376 . 1 1 74 74 ARG HG3 H 1 1.36 0.02 . 2 . . . . 73 . . . 5803 1 377 . 1 1 74 74 ARG HD2 H 1 2.76 0.02 . 2 . . . . 73 . . . 5803 1 378 . 1 1 75 75 ASN HA H 1 3.76 0.02 . 1 . . . . 74 . . . 5803 1 379 . 1 1 75 75 ASN HB2 H 1 2.02 0.02 . 2 . . . . 74 . . . 5803 1 380 . 1 1 78 78 ASN HD21 H 1 7.48 0.02 . 2 . . . . 77 . . . 5803 1 381 . 1 1 78 78 ASN HD22 H 1 6.81 0.02 . 2 . . . . 77 . . . 5803 1 382 . 1 1 79 79 ILE HG12 H 1 1.08 0.02 . 2 . . . . 78 . . . 5803 1 383 . 1 1 79 79 ILE HG13 H 1 1.40 0.02 . 2 . . . . 78 . . . 5803 1 384 . 1 1 79 79 ILE HG21 H 1 0.85 0.02 . 1 . . . . 78 . . . 5803 1 385 . 1 1 79 79 ILE HG22 H 1 0.85 0.02 . 1 . . . . 78 . . . 5803 1 386 . 1 1 79 79 ILE HG23 H 1 0.85 0.02 . 1 . . . . 78 . . . 5803 1 387 . 1 1 83 83 ALA H H 1 7.59 0.02 . 1 . . . . 82 . . . 5803 1 388 . 1 1 83 83 ALA HA H 1 4.24 0.02 . 1 . . . . 82 . . . 5803 1 389 . 1 1 83 83 ALA HB1 H 1 1.44 0.02 . 1 . . . . 82 . . . 5803 1 390 . 1 1 83 83 ALA HB2 H 1 1.44 0.02 . 1 . . . . 82 . . . 5803 1 391 . 1 1 83 83 ALA HB3 H 1 1.44 0.02 . 1 . . . . 82 . . . 5803 1 392 . 1 1 85 85 LEU H H 1 7.02 0.02 . 1 . . . . 84 . . . 5803 1 393 . 1 1 85 85 LEU HA H 1 4.98 0.02 . 1 . . . . 84 . . . 5803 1 394 . 1 1 85 85 LEU HB2 H 1 1.91 0.02 . 2 . . . . 84 . . . 5803 1 395 . 1 1 85 85 LEU HB3 H 1 1.76 0.02 . 2 . . . . 84 . . . 5803 1 396 . 1 1 85 85 LEU HG H 1 1.68 0.02 . 1 . . . . 84 . . . 5803 1 397 . 1 1 85 85 LEU HD11 H 1 0.86 0.02 . 2 . . . . 84 . . . 5803 1 398 . 1 1 85 85 LEU HD12 H 1 0.86 0.02 . 2 . . . . 84 . . . 5803 1 399 . 1 1 85 85 LEU HD13 H 1 0.86 0.02 . 2 . . . . 84 . . . 5803 1 400 . 1 1 85 85 LEU HD21 H 1 0.93 0.02 . 2 . . . . 84 . . . 5803 1 401 . 1 1 85 85 LEU HD22 H 1 0.93 0.02 . 2 . . . . 84 . . . 5803 1 402 . 1 1 85 85 LEU HD23 H 1 0.93 0.02 . 2 . . . . 84 . . . 5803 1 403 . 1 1 86 86 SER H H 1 6.69 0.02 . 1 . . . . 85 . . . 5803 1 404 . 1 1 86 86 SER HA H 1 4.46 0.02 . 1 . . . . 85 . . . 5803 1 405 . 1 1 86 86 SER HB2 H 1 3.89 0.02 . 2 . . . . 85 . . . 5803 1 406 . 1 1 87 87 SER H H 1 8.44 0.02 . 1 . . . . 86 . . . 5803 1 407 . 1 1 87 87 SER HA H 1 4.21 0.02 . 1 . . . . 86 . . . 5803 1 408 . 1 1 87 87 SER HB2 H 1 3.82 0.02 . 2 . . . . 86 . . . 5803 1 409 . 1 1 87 87 SER HB3 H 1 3.91 0.02 . 2 . . . . 86 . . . 5803 1 410 . 1 1 88 88 ASP H H 1 8.23 0.02 . 1 . . . . 87 . . . 5803 1 411 . 1 1 88 88 ASP HA H 1 4.92 0.02 . 1 . . . . 87 . . . 5803 1 412 . 1 1 88 88 ASP HB2 H 1 2.96 0.02 . 2 . . . . 87 . . . 5803 1 413 . 1 1 88 88 ASP HB3 H 1 2.63 0.02 . 2 . . . . 87 . . . 5803 1 414 . 1 1 89 89 ILE H H 1 8.07 0.02 . 1 . . . . 88 . . . 5803 1 415 . 1 1 89 89 ILE HA H 1 4.69 0.02 . 1 . . . . 88 . . . 5803 1 416 . 1 1 89 89 ILE HB H 1 1.82 0.02 . 1 . . . . 88 . . . 5803 1 417 . 1 1 89 89 ILE HG12 H 1 0.33 0.02 . 2 . . . . 88 . . . 5803 1 418 . 1 1 89 89 ILE HG13 H 1 1.14 0.02 . 2 . . . . 88 . . . 5803 1 419 . 1 1 89 89 ILE HG21 H 1 0.78 0.02 . 1 . . . . 88 . . . 5803 1 420 . 1 1 89 89 ILE HG22 H 1 0.78 0.02 . 1 . . . . 88 . . . 5803 1 421 . 1 1 89 89 ILE HG23 H 1 0.78 0.02 . 1 . . . . 88 . . . 5803 1 422 . 1 1 89 89 ILE HD11 H 1 0.18 0.02 . 1 . . . . 88 . . . 5803 1 423 . 1 1 89 89 ILE HD12 H 1 0.18 0.02 . 1 . . . . 88 . . . 5803 1 424 . 1 1 89 89 ILE HD13 H 1 0.18 0.02 . 1 . . . . 88 . . . 5803 1 425 . 1 1 90 90 THR H H 1 8.38 0.02 . 1 . . . . 89 . . . 5803 1 426 . 1 1 90 90 THR HA H 1 3.04 0.02 . 1 . . . . 89 . . . 5803 1 427 . 1 1 90 90 THR HB H 1 4.03 0.02 . 1 . . . . 89 . . . 5803 1 428 . 1 1 90 90 THR HG21 H 1 1.15 0.02 . 1 . . . . 89 . . . 5803 1 429 . 1 1 90 90 THR HG22 H 1 1.15 0.02 . 1 . . . . 89 . . . 5803 1 430 . 1 1 90 90 THR HG23 H 1 1.15 0.02 . 1 . . . . 89 . . . 5803 1 431 . 1 1 91 91 ALA H H 1 9.11 0.02 . 1 . . . . 90 . . . 5803 1 432 . 1 1 91 91 ALA HA H 1 4.08 0.02 . 1 . . . . 90 . . . 5803 1 433 . 1 1 91 91 ALA HB1 H 1 1.33 0.02 . 1 . . . . 90 . . . 5803 1 434 . 1 1 91 91 ALA HB2 H 1 1.33 0.02 . 1 . . . . 90 . . . 5803 1 435 . 1 1 91 91 ALA HB3 H 1 1.33 0.02 . 1 . . . . 90 . . . 5803 1 436 . 1 1 92 92 SER H H 1 7.85 0.02 . 1 . . . . 91 . . . 5803 1 437 . 1 1 92 92 SER HA H 1 3.98 0.02 . 1 . . . . 91 . . . 5803 1 438 . 1 1 92 92 SER HB2 H 1 3.97 0.02 . 2 . . . . 91 . . . 5803 1 439 . 1 1 92 92 SER HB3 H 1 3.47 0.02 . 2 . . . . 91 . . . 5803 1 440 . 1 1 93 93 VAL H H 1 8.38 0.02 . 1 . . . . 92 . . . 5803 1 441 . 1 1 93 93 VAL HA H 1 3.12 0.02 . 1 . . . . 92 . . . 5803 1 442 . 1 1 93 93 VAL HB H 1 1.88 0.02 . 1 . . . . 92 . . . 5803 1 443 . 1 1 93 93 VAL HG11 H 1 0.48 0.02 . 2 . . . . 92 . . . 5803 1 444 . 1 1 93 93 VAL HG12 H 1 0.48 0.02 . 2 . . . . 92 . . . 5803 1 445 . 1 1 93 93 VAL HG13 H 1 0.48 0.02 . 2 . . . . 92 . . . 5803 1 446 . 1 1 93 93 VAL HG21 H 1 0.59 0.02 . 2 . . . . 92 . . . 5803 1 447 . 1 1 93 93 VAL HG22 H 1 0.59 0.02 . 2 . . . . 92 . . . 5803 1 448 . 1 1 93 93 VAL HG23 H 1 0.59 0.02 . 2 . . . . 92 . . . 5803 1 449 . 1 1 94 94 ASN H H 1 8.70 0.02 . 1 . . . . 93 . . . 5803 1 450 . 1 1 94 94 ASN HA H 1 4.27 0.02 . 1 . . . . 93 . . . 5803 1 451 . 1 1 94 94 ASN HB2 H 1 2.92 0.02 . 2 . . . . 93 . . . 5803 1 452 . 1 1 94 94 ASN HB3 H 1 2.75 0.02 . 2 . . . . 93 . . . 5803 1 453 . 1 1 94 94 ASN HD21 H 1 7.66 0.02 . 2 . . . . 93 . . . 5803 1 454 . 1 1 94 94 ASN HD22 H 1 6.99 0.02 . 2 . . . . 93 . . . 5803 1 455 . 1 1 95 95 CYS H H 1 8.03 0.02 . 1 . . . . 94 . . . 5803 1 456 . 1 1 95 95 CYS HA H 1 5.07 0.02 . 1 . . . . 94 . . . 5803 1 457 . 1 1 95 95 CYS HB2 H 1 3.34 0.02 . 2 . . . . 94 . . . 5803 1 458 . 1 1 95 95 CYS HB3 H 1 2.75 0.02 . 2 . . . . 94 . . . 5803 1 459 . 1 1 96 96 ALA H H 1 8.69 0.02 . 1 . . . . 95 . . . 5803 1 460 . 1 1 96 96 ALA HA H 1 4.13 0.02 . 1 . . . . 95 . . . 5803 1 461 . 1 1 96 96 ALA HB1 H 1 1.55 0.02 . 1 . . . . 95 . . . 5803 1 462 . 1 1 96 96 ALA HB2 H 1 1.55 0.02 . 1 . . . . 95 . . . 5803 1 463 . 1 1 96 96 ALA HB3 H 1 1.55 0.02 . 1 . . . . 95 . . . 5803 1 464 . 1 1 97 97 LYS HA H 1 3.71 0.02 . 1 . . . . 96 . . . 5803 1 465 . 1 1 97 97 LYS HB2 H 1 1.68 0.02 . 2 . . . . 96 . . . 5803 1 466 . 1 1 97 97 LYS HB3 H 1 1.12 0.02 . 2 . . . . 96 . . . 5803 1 467 . 1 1 97 97 LYS HG2 H 1 -0.47 0.02 . 2 . . . . 96 . . . 5803 1 468 . 1 1 97 97 LYS HD2 H 1 1.26 0.02 . 2 . . . . 96 . . . 5803 1 469 . 1 1 97 97 LYS HE2 H 1 2.07 0.02 . 2 . . . . 96 . . . 5803 1 470 . 1 1 97 97 LYS HE3 H 1 2.15 0.02 . 2 . . . . 96 . . . 5803 1 471 . 1 1 98 98 LYS H H 1 7.24 0.02 . 1 . . . . 97 . . . 5803 1 472 . 1 1 98 98 LYS HA H 1 4.14 0.02 . 1 . . . . 97 . . . 5803 1 473 . 1 1 98 98 LYS HB2 H 1 2.15 0.02 . 2 . . . . 97 . . . 5803 1 474 . 1 1 99 99 ILE H H 1 8.11 0.02 . 1 . . . . 98 . . . 5803 1 475 . 1 1 99 99 ILE HA H 1 2.79 0.02 . 1 . . . . 98 . . . 5803 1 476 . 1 1 99 99 ILE HB H 1 1.49 0.02 . 1 . . . . 98 . . . 5803 1 477 . 1 1 99 99 ILE HG12 H 1 -2.04 0.02 . 2 . . . . 98 . . . 5803 1 478 . 1 1 99 99 ILE HG13 H 1 0.68 0.02 . 2 . . . . 98 . . . 5803 1 479 . 1 1 99 99 ILE HG21 H 1 -0.25 0.02 . 1 . . . . 98 . . . 5803 1 480 . 1 1 99 99 ILE HG22 H 1 -0.25 0.02 . 1 . . . . 98 . . . 5803 1 481 . 1 1 99 99 ILE HG23 H 1 -0.25 0.02 . 1 . . . . 98 . . . 5803 1 482 . 1 1 99 99 ILE HD11 H 1 0.00 0.02 . 1 . . . . 98 . . . 5803 1 483 . 1 1 99 99 ILE HD12 H 1 0.00 0.02 . 1 . . . . 98 . . . 5803 1 484 . 1 1 99 99 ILE HD13 H 1 0.00 0.02 . 1 . . . . 98 . . . 5803 1 485 . 1 1 100 100 VAL HA H 1 3.91 0.02 . 1 . . . . 99 . . . 5803 1 486 . 1 1 100 100 VAL HB H 1 2.45 0.02 . 1 . . . . 99 . . . 5803 1 487 . 1 1 100 100 VAL HG11 H 1 1.17 0.02 . 2 . . . . 99 . . . 5803 1 488 . 1 1 100 100 VAL HG12 H 1 1.17 0.02 . 2 . . . . 99 . . . 5803 1 489 . 1 1 100 100 VAL HG13 H 1 1.17 0.02 . 2 . . . . 99 . . . 5803 1 490 . 1 1 100 100 VAL HG21 H 1 1.36 0.02 . 2 . . . . 99 . . . 5803 1 491 . 1 1 100 100 VAL HG22 H 1 1.36 0.02 . 2 . . . . 99 . . . 5803 1 492 . 1 1 100 100 VAL HG23 H 1 1.36 0.02 . 2 . . . . 99 . . . 5803 1 493 . 1 1 101 101 SER H H 1 7.69 0.02 . 1 . . . . 100 . . . 5803 1 494 . 1 1 101 101 SER HA H 1 4.48 0.02 . 1 . . . . 100 . . . 5803 1 495 . 1 1 101 101 SER HB2 H 1 4.08 0.02 . 2 . . . . 100 . . . 5803 1 496 . 1 1 102 102 ASP H H 1 7.97 0.02 . 1 . . . . 101 . . . 5803 1 497 . 1 1 102 102 ASP HA H 1 4.76 0.02 . 1 . . . . 101 . . . 5803 1 498 . 1 1 102 102 ASP HB2 H 1 3.04 0.02 . 2 . . . . 101 . . . 5803 1 499 . 1 1 103 103 GLY H H 1 8.20 0.02 . 1 . . . . 102 . . . 5803 1 500 . 1 1 103 103 GLY HA2 H 1 3.95 0.02 . 2 . . . . 102 . . . 5803 1 501 . 1 1 103 103 GLY HA3 H 1 4.24 0.02 . 2 . . . . 102 . . . 5803 1 502 . 1 1 104 104 ASN H H 1 8.16 0.02 . 1 . . . . 103 . . . 5803 1 503 . 1 1 104 104 ASN HA H 1 4.99 0.02 . 1 . . . . 103 . . . 5803 1 504 . 1 1 104 104 ASN HB2 H 1 2.71 0.02 . 2 . . . . 103 . . . 5803 1 505 . 1 1 104 104 ASN HB3 H 1 2.81 0.02 . 2 . . . . 103 . . . 5803 1 506 . 1 1 105 105 GLY H H 1 8.32 0.02 . 1 . . . . 104 . . . 5803 1 507 . 1 1 105 105 GLY HA2 H 1 4.11 0.02 . 2 . . . . 104 . . . 5803 1 508 . 1 1 105 105 GLY HA3 H 1 4.26 0.02 . 2 . . . . 104 . . . 5803 1 509 . 1 1 106 106 MET H H 1 7.17 0.02 . 1 . . . . 105 . . . 5803 1 510 . 1 1 106 106 MET HA H 1 3.87 0.02 . 1 . . . . 105 . . . 5803 1 511 . 1 1 106 106 MET HB2 H 1 -1.03 0.02 . 2 . . . . 105 . . . 5803 1 512 . 1 1 106 106 MET HB3 H 1 0.45 0.02 . 2 . . . . 105 . . . 5803 1 513 . 1 1 106 106 MET HG2 H 1 0.51 0.02 . 2 . . . . 105 . . . 5803 1 514 . 1 1 106 106 MET HG3 H 1 -0.06 0.02 . 2 . . . . 105 . . . 5803 1 515 . 1 1 106 106 MET HE1 H 1 -0.07 0.02 . 1 . . . . 105 . . . 5803 1 516 . 1 1 106 106 MET HE2 H 1 -0.07 0.02 . 1 . . . . 105 . . . 5803 1 517 . 1 1 106 106 MET HE3 H 1 -0.07 0.02 . 1 . . . . 105 . . . 5803 1 518 . 1 1 107 107 ASN H H 1 7.71 0.02 . 1 . . . . 106 . . . 5803 1 519 . 1 1 107 107 ASN HA H 1 4.48 0.02 . 1 . . . . 106 . . . 5803 1 520 . 1 1 107 107 ASN HB2 H 1 3.06 0.02 . 2 . . . . 106 . . . 5803 1 521 . 1 1 107 107 ASN HB3 H 1 2.82 0.02 . 2 . . . . 106 . . . 5803 1 522 . 1 1 107 107 ASN HD21 H 1 7.57 0.02 . 2 . . . . 106 . . . 5803 1 523 . 1 1 107 107 ASN HD22 H 1 7.18 0.02 . 2 . . . . 106 . . . 5803 1 524 . 1 1 108 108 ALA H H 1 6.75 0.02 . 1 . . . . 107 . . . 5803 1 525 . 1 1 108 108 ALA HA H 1 3.85 0.02 . 1 . . . . 107 . . . 5803 1 526 . 1 1 108 108 ALA HB1 H 1 0.63 0.02 . 1 . . . . 107 . . . 5803 1 527 . 1 1 108 108 ALA HB2 H 1 0.63 0.02 . 1 . . . . 107 . . . 5803 1 528 . 1 1 108 108 ALA HB3 H 1 0.63 0.02 . 1 . . . . 107 . . . 5803 1 529 . 1 1 109 109 TRP H H 1 7.93 0.02 . 1 . . . . 108 . . . 5803 1 530 . 1 1 109 109 TRP HA H 1 4.66 0.02 . 1 . . . . 108 . . . 5803 1 531 . 1 1 109 109 TRP HB2 H 1 3.37 0.02 . 2 . . . . 108 . . . 5803 1 532 . 1 1 109 109 TRP HB3 H 1 3.27 0.02 . 2 . . . . 108 . . . 5803 1 533 . 1 1 109 109 TRP HD1 H 1 7.07 0.02 . 1 . . . . 108 . . . 5803 1 534 . 1 1 109 109 TRP HE1 H 1 10.04 0.02 . 1 . . . . 108 . . . 5803 1 535 . 1 1 109 109 TRP HE3 H 1 7.37 0.02 . 1 . . . . 108 . . . 5803 1 536 . 1 1 109 109 TRP HZ2 H 1 6.94 0.02 . 1 . . . . 108 . . . 5803 1 537 . 1 1 109 109 TRP HZ3 H 1 6.52 0.02 . 1 . . . . 108 . . . 5803 1 538 . 1 1 109 109 TRP HH2 H 1 7.28 0.02 . 1 . . . . 108 . . . 5803 1 539 . 1 1 110 110 VAL H H 1 8.98 0.02 . 1 . . . . 109 . . . 5803 1 540 . 1 1 110 110 VAL HA H 1 3.62 0.02 . 1 . . . . 109 . . . 5803 1 541 . 1 1 110 110 VAL HB H 1 2.16 0.02 . 1 . . . . 109 . . . 5803 1 542 . 1 1 110 110 VAL HG11 H 1 1.03 0.02 . 2 . . . . 109 . . . 5803 1 543 . 1 1 110 110 VAL HG12 H 1 1.03 0.02 . 2 . . . . 109 . . . 5803 1 544 . 1 1 110 110 VAL HG13 H 1 1.03 0.02 . 2 . . . . 109 . . . 5803 1 545 . 1 1 110 110 VAL HG21 H 1 1.12 0.02 . 2 . . . . 109 . . . 5803 1 546 . 1 1 110 110 VAL HG22 H 1 1.12 0.02 . 2 . . . . 109 . . . 5803 1 547 . 1 1 110 110 VAL HG23 H 1 1.12 0.02 . 2 . . . . 109 . . . 5803 1 548 . 1 1 111 111 ALA H H 1 8.02 0.02 . 1 . . . . 110 . . . 5803 1 549 . 1 1 111 111 ALA HA H 1 4.27 0.02 . 1 . . . . 110 . . . 5803 1 550 . 1 1 111 111 ALA HB1 H 1 1.32 0.02 . 1 . . . . 110 . . . 5803 1 551 . 1 1 111 111 ALA HB2 H 1 1.32 0.02 . 1 . . . . 110 . . . 5803 1 552 . 1 1 111 111 ALA HB3 H 1 1.32 0.02 . 1 . . . . 110 . . . 5803 1 553 . 1 1 112 112 TRP H H 1 7.24 0.02 . 1 . . . . 111 . . . 5803 1 554 . 1 1 112 112 TRP HA H 1 3.72 0.02 . 1 . . . . 111 . . . 5803 1 555 . 1 1 112 112 TRP HB2 H 1 4.08 0.02 . 2 . . . . 111 . . . 5803 1 556 . 1 1 112 112 TRP HB3 H 1 2.78 0.02 . 2 . . . . 111 . . . 5803 1 557 . 1 1 112 112 TRP HD1 H 1 7.03 0.02 . 1 . . . . 111 . . . 5803 1 558 . 1 1 112 112 TRP HE1 H 1 10.43 0.02 . 1 . . . . 111 . . . 5803 1 559 . 1 1 112 112 TRP HE3 H 1 7.28 0.02 . 1 . . . . 111 . . . 5803 1 560 . 1 1 112 112 TRP HZ2 H 1 7.51 0.02 . 1 . . . . 111 . . . 5803 1 561 . 1 1 112 112 TRP HZ3 H 1 7.04 0.02 . 1 . . . . 111 . . . 5803 1 562 . 1 1 112 112 TRP HH2 H 1 7.37 0.02 . 1 . . . . 111 . . . 5803 1 563 . 1 1 113 113 ARG H H 1 8.30 0.02 . 1 . . . . 112 . . . 5803 1 564 . 1 1 113 113 ARG HA H 1 3.38 0.02 . 1 . . . . 112 . . . 5803 1 565 . 1 1 113 113 ARG HB2 H 1 1.99 0.02 . 2 . . . . 112 . . . 5803 1 566 . 1 1 113 113 ARG HB3 H 1 2.12 0.02 . 2 . . . . 112 . . . 5803 1 567 . 1 1 113 113 ARG HG2 H 1 1.82 0.02 . 2 . . . . 112 . . . 5803 1 568 . 1 1 113 113 ARG HD2 H 1 3.36 0.02 . 2 . . . . 112 . . . 5803 1 569 . 1 1 113 113 ARG HD3 H 1 3.46 0.02 . 2 . . . . 112 . . . 5803 1 570 . 1 1 113 113 ARG HE H 1 7.32 0.02 . 1 . . . . 112 . . . 5803 1 571 . 1 1 114 114 ASN H H 1 8.01 0.02 . 1 . . . . 113 . . . 5803 1 572 . 1 1 114 114 ASN HA H 1 4.50 0.02 . 1 . . . . 113 . . . 5803 1 573 . 1 1 114 114 ASN HB2 H 1 2.68 0.02 . 2 . . . . 113 . . . 5803 1 574 . 1 1 114 114 ASN HD21 H 1 7.63 0.02 . 2 . . . . 113 . . . 5803 1 575 . 1 1 114 114 ASN HD22 H 1 6.92 0.02 . 2 . . . . 113 . . . 5803 1 576 . 1 1 115 115 ARG H H 1 7.67 0.02 . 1 . . . . 114 . . . 5803 1 577 . 1 1 115 115 ARG HA H 1 4.32 0.02 . 1 . . . . 114 . . . 5803 1 578 . 1 1 115 115 ARG HB2 H 1 1.18 0.02 . 2 . . . . 114 . . . 5803 1 579 . 1 1 115 115 ARG HB3 H 1 0.57 0.02 . 2 . . . . 114 . . . 5803 1 580 . 1 1 115 115 ARG HG2 H 1 1.08 0.02 . 2 . . . . 114 . . . 5803 1 581 . 1 1 115 115 ARG HG3 H 1 1.02 0.02 . 2 . . . . 114 . . . 5803 1 582 . 1 1 115 115 ARG HD2 H 1 2.64 0.02 . 2 . . . . 114 . . . 5803 1 583 . 1 1 115 115 ARG HD3 H 1 2.77 0.02 . 2 . . . . 114 . . . 5803 1 584 . 1 1 115 115 ARG HE H 1 7.03 0.02 . 1 . . . . 114 . . . 5803 1 585 . 1 1 116 116 CYS H H 1 7.37 0.02 . 1 . . . . 115 . . . 5803 1 586 . 1 1 116 116 CYS HA H 1 4.52 0.02 . 1 . . . . 115 . . . 5803 1 587 . 1 1 116 116 CYS HB2 H 1 2.47 0.02 . 2 . . . . 115 . . . 5803 1 588 . 1 1 116 116 CYS HB3 H 1 2.61 0.02 . 2 . . . . 115 . . . 5803 1 589 . 1 1 117 117 LYS H H 1 7.08 0.02 . 1 . . . . 116 . . . 5803 1 590 . 1 1 117 117 LYS HA H 1 3.45 0.02 . 1 . . . . 116 . . . 5803 1 591 . 1 1 117 117 LYS HB2 H 1 1.24 0.02 . 2 . . . . 116 . . . 5803 1 592 . 1 1 117 117 LYS HB3 H 1 -0.23 0.02 . 2 . . . . 116 . . . 5803 1 593 . 1 1 117 117 LYS HG2 H 1 1.06 0.02 . 2 . . . . 116 . . . 5803 1 594 . 1 1 117 117 LYS HG3 H 1 1.68 0.02 . 2 . . . . 116 . . . 5803 1 595 . 1 1 117 117 LYS HD2 H 1 1.55 0.02 . 2 . . . . 116 . . . 5803 1 596 . 1 1 117 117 LYS HE2 H 1 3.09 0.02 . 2 . . . . 116 . . . 5803 1 597 . 1 1 118 118 GLY H H 1 8.75 0.02 . 1 . . . . 117 . . . 5803 1 598 . 1 1 118 118 GLY HA2 H 1 4.13 0.02 . 2 . . . . 117 . . . 5803 1 599 . 1 1 118 118 GLY HA3 H 1 3.81 0.02 . 2 . . . . 117 . . . 5803 1 600 . 1 1 119 119 THR H H 1 7.68 0.02 . 1 . . . . 118 . . . 5803 1 601 . 1 1 119 119 THR HA H 1 4.75 0.02 . 1 . . . . 118 . . . 5803 1 602 . 1 1 119 119 THR HB H 1 4.31 0.02 . 1 . . . . 118 . . . 5803 1 603 . 1 1 119 119 THR HG21 H 1 0.95 0.02 . 1 . . . . 118 . . . 5803 1 604 . 1 1 119 119 THR HG22 H 1 0.95 0.02 . 1 . . . . 118 . . . 5803 1 605 . 1 1 119 119 THR HG23 H 1 0.95 0.02 . 1 . . . . 118 . . . 5803 1 606 . 1 1 120 120 ASP H H 1 8.74 0.02 . 1 . . . . 119 . . . 5803 1 607 . 1 1 120 120 ASP HA H 1 5.00 0.02 . 1 . . . . 119 . . . 5803 1 608 . 1 1 120 120 ASP HB2 H 1 2.74 0.02 . 2 . . . . 119 . . . 5803 1 609 . 1 1 120 120 ASP HB3 H 1 2.95 0.02 . 2 . . . . 119 . . . 5803 1 610 . 1 1 121 121 VAL H H 1 8.17 0.02 . 1 . . . . 120 . . . 5803 1 611 . 1 1 121 121 VAL HA H 1 4.36 0.02 . 1 . . . . 120 . . . 5803 1 612 . 1 1 121 121 VAL HB H 1 2.16 0.02 . 1 . . . . 120 . . . 5803 1 613 . 1 1 121 121 VAL HG11 H 1 1.08 0.02 . 2 . . . . 120 . . . 5803 1 614 . 1 1 121 121 VAL HG12 H 1 1.08 0.02 . 2 . . . . 120 . . . 5803 1 615 . 1 1 121 121 VAL HG13 H 1 1.08 0.02 . 2 . . . . 120 . . . 5803 1 616 . 1 1 121 121 VAL HG21 H 1 1.12 0.02 . 2 . . . . 120 . . . 5803 1 617 . 1 1 121 121 VAL HG22 H 1 1.12 0.02 . 2 . . . . 120 . . . 5803 1 618 . 1 1 121 121 VAL HG23 H 1 1.12 0.02 . 2 . . . . 120 . . . 5803 1 619 . 1 1 122 122 GLN H H 1 8.50 0.02 . 1 . . . . 121 . . . 5803 1 620 . 1 1 122 122 GLN HA H 1 4.34 0.02 . 1 . . . . 121 . . . 5803 1 621 . 1 1 122 122 GLN HB2 H 1 2.20 0.02 . 2 . . . . 121 . . . 5803 1 622 . 1 1 122 122 GLN HB3 H 1 2.25 0.02 . 2 . . . . 121 . . . 5803 1 623 . 1 1 122 122 GLN HG2 H 1 2.52 0.02 . 2 . . . . 121 . . . 5803 1 624 . 1 1 122 122 GLN HE21 H 1 7.74 0.02 . 2 . . . . 121 . . . 5803 1 625 . 1 1 122 122 GLN HE22 H 1 6.96 0.02 . 2 . . . . 121 . . . 5803 1 626 . 1 1 123 123 ALA H H 1 7.72 0.02 . 1 . . . . 122 . . . 5803 1 627 . 1 1 123 123 ALA HA H 1 3.81 0.02 . 1 . . . . 122 . . . 5803 1 628 . 1 1 123 123 ALA HB1 H 1 1.17 0.02 . 1 . . . . 122 . . . 5803 1 629 . 1 1 123 123 ALA HB2 H 1 1.17 0.02 . 1 . . . . 122 . . . 5803 1 630 . 1 1 123 123 ALA HB3 H 1 1.17 0.02 . 1 . . . . 122 . . . 5803 1 631 . 1 1 124 124 TRP H H 1 7.62 0.02 . 1 . . . . 123 . . . 5803 1 632 . 1 1 124 124 TRP HA H 1 4.11 0.02 . 1 . . . . 123 . . . 5803 1 633 . 1 1 124 124 TRP HB2 H 1 3.41 0.02 . 2 . . . . 123 . . . 5803 1 634 . 1 1 124 124 TRP HD1 H 1 7.55 0.02 . 1 . . . . 123 . . . 5803 1 635 . 1 1 124 124 TRP HE1 H 1 10.79 0.02 . 1 . . . . 123 . . . 5803 1 636 . 1 1 124 124 TRP HE3 H 1 7.50 0.02 . 1 . . . . 123 . . . 5803 1 637 . 1 1 124 124 TRP HZ2 H 1 7.78 0.02 . 1 . . . . 123 . . . 5803 1 638 . 1 1 124 124 TRP HZ3 H 1 7.13 0.02 . 1 . . . . 123 . . . 5803 1 639 . 1 1 124 124 TRP HH2 H 1 7.11 0.02 . 1 . . . . 123 . . . 5803 1 640 . 1 1 125 125 ILE H H 1 7.56 0.02 . 1 . . . . 124 . . . 5803 1 641 . 1 1 125 125 ILE HA H 1 4.74 0.02 . 1 . . . . 124 . . . 5803 1 642 . 1 1 125 125 ILE HB H 1 2.22 0.02 . 1 . . . . 124 . . . 5803 1 643 . 1 1 125 125 ILE HG12 H 1 1.24 0.02 . 2 . . . . 124 . . . 5803 1 644 . 1 1 125 125 ILE HG13 H 1 1.44 0.02 . 2 . . . . 124 . . . 5803 1 645 . 1 1 125 125 ILE HG21 H 1 0.82 0.02 . 1 . . . . 124 . . . 5803 1 646 . 1 1 125 125 ILE HG22 H 1 0.82 0.02 . 1 . . . . 124 . . . 5803 1 647 . 1 1 125 125 ILE HG23 H 1 0.82 0.02 . 1 . . . . 124 . . . 5803 1 648 . 1 1 125 125 ILE HD11 H 1 0.95 0.02 . 1 . . . . 124 . . . 5803 1 649 . 1 1 125 125 ILE HD12 H 1 0.95 0.02 . 1 . . . . 124 . . . 5803 1 650 . 1 1 125 125 ILE HD13 H 1 0.95 0.02 . 1 . . . . 124 . . . 5803 1 651 . 1 1 126 126 ARG H H 1 7.33 0.02 . 1 . . . . 125 . . . 5803 1 652 . 1 1 126 126 ARG HA H 1 4.16 0.02 . 1 . . . . 125 . . . 5803 1 653 . 1 1 126 126 ARG HB2 H 1 1.81 0.02 . 2 . . . . 125 . . . 5803 1 654 . 1 1 126 126 ARG HB3 H 1 2.00 0.02 . 2 . . . . 125 . . . 5803 1 655 . 1 1 126 126 ARG HD2 H 1 3.15 0.02 . 2 . . . . 125 . . . 5803 1 656 . 1 1 126 126 ARG HD3 H 1 3.20 0.02 . 2 . . . . 125 . . . 5803 1 657 . 1 1 126 126 ARG HE H 1 7.34 0.02 . 1 . . . . 125 . . . 5803 1 658 . 1 1 127 127 GLY H H 1 9.20 0.02 . 1 . . . . 126 . . . 5803 1 659 . 1 1 127 127 GLY HA2 H 1 4.31 0.02 . 2 . . . . 126 . . . 5803 1 660 . 1 1 127 127 GLY HA3 H 1 3.74 0.02 . 2 . . . . 126 . . . 5803 1 661 . 1 1 128 128 CYS H H 1 7.46 0.02 . 1 . . . . 127 . . . 5803 1 662 . 1 1 128 128 CYS HA H 1 4.92 0.02 . 1 . . . . 127 . . . 5803 1 663 . 1 1 128 128 CYS HB2 H 1 3.09 0.02 . 2 . . . . 127 . . . 5803 1 664 . 1 1 128 128 CYS HB3 H 1 2.62 0.02 . 2 . . . . 127 . . . 5803 1 665 . 1 1 129 129 ARG H H 1 8.98 0.02 . 1 . . . . 128 . . . 5803 1 666 . 1 1 129 129 ARG HA H 1 4.36 0.02 . 1 . . . . 128 . . . 5803 1 667 . 1 1 129 129 ARG HB2 H 1 1.77 0.02 . 2 . . . . 128 . . . 5803 1 668 . 1 1 129 129 ARG HD2 H 1 3.21 0.02 . 2 . . . . 128 . . . 5803 1 669 . 1 1 129 129 ARG HE H 1 7.17 0.02 . 1 . . . . 128 . . . 5803 1 670 . 1 1 130 130 LEU H H 1 8.03 0.02 . 1 . . . . 129 . . . 5803 1 671 . 1 1 130 130 LEU HA H 1 4.28 0.02 . 1 . . . . 129 . . . 5803 1 672 . 1 1 130 130 LEU HB2 H 1 1.66 0.02 . 2 . . . . 129 . . . 5803 1 673 . 1 1 130 130 LEU HB3 H 1 1.46 0.02 . 2 . . . . 129 . . . 5803 1 674 . 1 1 130 130 LEU HG H 1 1.40 0.02 . 1 . . . . 129 . . . 5803 1 675 . 1 1 130 130 LEU HD11 H 1 0.73 0.02 . 2 . . . . 129 . . . 5803 1 676 . 1 1 130 130 LEU HD12 H 1 0.73 0.02 . 2 . . . . 129 . . . 5803 1 677 . 1 1 130 130 LEU HD13 H 1 0.73 0.02 . 2 . . . . 129 . . . 5803 1 678 . 1 1 130 130 LEU HD21 H 1 0.85 0.02 . 2 . . . . 129 . . . 5803 1 679 . 1 1 130 130 LEU HD22 H 1 0.85 0.02 . 2 . . . . 129 . . . 5803 1 680 . 1 1 130 130 LEU HD23 H 1 0.85 0.02 . 2 . . . . 129 . . . 5803 1 stop_ save_