data_4943 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4943 _Entry.Title ; 1H Chemical shift Assignments for Lysozymes marketed by Seikagaku and Sigma companies at pH 3.8, 308K ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2001-01-19 _Entry.Accession_date 2001-01-19 _Entry.Last_release_date 2003-05-21 _Entry.Original_release_date 2003-05-21 _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 Jaroslaw Poznanski . . . 4943 2 Yannis Georgalis . . . 4943 3 Lorin Wehr . . . 4943 4 Piotr Zielenkiewicz . . . 4943 5 Wolfram Saenger . . . 4943 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 2 4943 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 964 4943 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 . . 2003-05-21 2001-01-19 original author . 4943 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4943 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Comparison of Two Different Lysozyme Types Under Native and Crystallization Conditions using Two-Dimensional NMR and Dynamic Light Scattering ; _Citation.Status submitted _Citation.Type journal _Citation.Journal_abbrev 'Biophys. Chem.' _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _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 . _Citation.Page_last . _Citation.Year 2002 _Citation.Details ; See reference in the saveframe ref_1. ; 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 Jaroslaw Poznanski . . . 4943 1 2 Yannis Georgalis . . . 4943 1 3 Lorin Wehr . . . 4943 1 4 Piotr Zielenkiewicz . . . 4943 1 5 Wolfram Saenger . . . 4943 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID Lysozyme 4943 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 4943 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 3349024 _Citation.Full_citation ; Redfield C, Dobson CM. Sequential 1H NMR assignments and secondary structure of hen egg white lysozyme in solution. Biochemistry. 1988 Jan 12;27(1):122-36. ; _Citation.Title 'Sequential 1H NMR assignments and secondary structure of hen egg white lysozyme in solution.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 27 _Citation.Journal_issue 1 _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 122 _Citation.Page_last 136 _Citation.Year 1988 _Citation.Details ; Assignments for 1H NMR resonances of 121 of the 129 residues of hen egg white lysozyme have been obtained by sequence-specific methods. Spin systems were identified with phase-sensitive two-dimensional (2-D) correlated spectroscopy and single and double relayed coherence transfer spectroscopy. For key types of amino acid residues, particularly alanine, threonine, valine, and glycine, complete spin systems were identified. For other residues a less complete definition of the spin system was found to be adequate for the purpose of sequential assignment. Sequence-specific assignments were achieved by phase-sensitive 2-D nuclear Overhauser enhancement spectroscopy (NOESY). Exploitation of the wide range of hydrogen exchange rates found in lysozyme was a useful approach to overcoming the problem of spectral overlap. The sequential assignment was built up from 21 peptide segments ranging in length from 2 to 13 residues. The NOESY spectra were also used to provide information about the secondary structure of the protein in solution. Three helical regions and two regions of beta-sheet were identified from the NOESY data; these regions are identical with those found in the X-ray structure of hen lysozyme. Slowly exchanging amides are generally correlated with hydrogen bonding identified in the X-ray structure; a number of exceptions to this general trend were, however, found. The results presented in this paper indicate that highly detailed information can be obtained from 2-D NMR spectra of a protein that is significantly larger than those studied previously. ; 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 C. Redfield C. . . 4943 2 2 C.M. Dobson C. M. . 4943 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 4943 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8520220 _Citation.Full_citation ; Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93. ; _Citation.Title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of biomolecular NMR' _Citation.Journal_volume 6 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0925-2738 _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 277 _Citation.Page_last 293 _Citation.Year 1995 _Citation.Details ; The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks. ; 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 F. Delaglio F. . . 4943 3 2 S. Grzesiek S. . . 4943 3 3 G.W. Vuister G. W. . 4943 3 4 G. Zhu G. . . 4943 3 5 J. Pfeifer J. . . 4943 3 6 A. Bax A. . . 4943 3 stop_ save_ save_ref_3 _Citation.Sf_category citations _Citation.Sf_framecode ref_3 _Citation.Entry_ID 4943 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Bartels,CH; Xia,T-H; Billeter,M; Guntert,P; Wuthrich,K. The program XEASY for computer-supported NMR specreal analysis of biological macromolecules. J. Biomol. NMR 5,1-10(1995) ; _Citation.Title . _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _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 . _Citation.Page_last . _Citation.Year . _Citation.Details . save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_Lysozyme _Assembly.Sf_category assembly _Assembly.Sf_framecode system_Lysozyme _Assembly.Entry_ID 4943 _Assembly.ID 1 _Assembly.Name 'Chicken 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 4943 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 lysozyme 1 $Lysozyme . . . native . . . . . 4943 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 6 6 SG . 1 . 1 CYS 127 127 SG . . . . . . . . . . 4943 1 2 disulfide single . 1 . 1 CYS 30 30 SG . 1 . 1 CYS 115 115 SG . . . . . . . . . . 4943 1 3 disulfide single . 1 . 1 CYS 64 64 SG . 1 . 1 CYS 80 80 SG . . . . . . . . . . 4943 1 4 disulfide single . 1 . 1 CYS 76 76 SG . 1 . 1 CYS 94 94 SG . . . . . . . . . . 4943 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes PDB 1LKS . . . . . 'link to crystal structure. In reported data comparison of lysozyme probes marketed by two distributors' 4943 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'Chicken Egg White Lysozyme' system 4943 1 Lysozyme abbreviation 4943 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'bacteriolytic function' 4943 1 'hydrolysis and transglycosylation' 4943 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Lysozyme _Entity.Sf_category entity _Entity.Sf_framecode Lysozyme _Entity.Entry_ID 4943 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Chicken Egg White 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 ; KVFGRCELAAAMKRHGLDNY RGYSLGNWVCAAKFESNFNT QATNRNTDGSTDYGILQINS RWWCNDGRTPGSRNLCNIPC SALLSSDITASVNCAKKIVS DGNGMNAWVAWRNRCKGTDV QAWIRGCRLDRSR ; _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 133 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all disulfide bound' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 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 1 no BMRB 1093 . lysozyme . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 2 no BMRB 1104 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 3 no BMRB 1105 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 4 no BMRB 11052 . 2SS(6-127_64-80) . . . . . 96.99 130 96.90 96.90 1.01e-84 . . . . 4943 1 5 no BMRB 1650 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 6 no BMRB 1651 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 7 no BMRB 1653 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 8 no BMRB 1770 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 9 no BMRB 1772 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 10 no BMRB 1798 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 11 no BMRB 1799 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 12 no BMRB 1800 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 13 no BMRB 1801 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 14 no BMRB 1802 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 15 no BMRB 1803 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 16 no BMRB 18304 . HEWL . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 17 no BMRB 18305 . HEWL . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 18 no BMRB 1865 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 19 no BMRB 1881 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 20 no BMRB 1882 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 21 no BMRB 1883 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 22 no BMRB 1884 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 23 no BMRB 1975 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 24 no BMRB 1977 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 25 no BMRB 2231 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 26 no BMRB 2446 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 27 no BMRB 2786 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 28 no BMRB 2858 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 29 no BMRB 2917 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 30 no BMRB 2957 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 31 no BMRB 4562 . HEWL . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 32 no BMRB 4831 . lysozyme . . . . . 96.99 129 99.22 100.00 1.71e-87 . . . . 4943 1 33 no BMRB 5068 . metLYZ . . . . . 96.99 130 100.00 100.00 5.85e-88 . . . . 4943 1 34 no BMRB 5069 . 2SS(6-127_30-115) . . . . . 96.99 130 96.90 96.90 1.01e-84 . . . . 4943 1 35 no BMRB 568 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 36 no BMRB 569 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 37 no BMRB 5803 . HEWL . . . . . 96.99 130 98.45 98.45 3.92e-86 . . . . 4943 1 38 no BMRB 5804 . HEWL . . . . . 96.99 130 98.45 98.45 3.92e-86 . . . . 4943 1 39 no BMRB 6415 . C30A/C115A . . . . . 96.99 130 98.45 98.45 3.92e-86 . . . . 4943 1 40 no BMRB 7143 . HEWL . . . . . 96.99 129 99.22 100.00 1.71e-87 . . . . 4943 1 41 no BMRB 7144 . HEWL . . . . . 96.99 129 99.22 100.00 1.71e-87 . . . . 4943 1 42 no BMRB 7159 . 2SS[6-127,_30-115] . . . . . 96.99 129 96.90 96.90 8.61e-85 . . . . 4943 1 43 no BMRB 7160 . metLYZ . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 44 no BMRB 791 . lysozyme . . . . . 96.99 129 99.22 99.22 6.83e-87 . . . . 4943 1 45 no PDB 193L . "The 1.33 A Structure Of Tetragonal Hen Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 46 no PDB 194L . "The 1.40 A Structure Of Spacehab-01 Hen Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 47 no PDB 1A2Y . "Hen Egg White Lysozyme, D18a Mutant, In Complex With Mouse Monoclonal Antibody D1.3" . . . . . 96.99 129 99.22 99.22 6.32e-87 . . . . 4943 1 48 no PDB 1AKI . "The Structure Of The Orthorhombic Form Of Hen Egg-White Lysozyme At 1.5 Angstroms Resolution" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 49 no PDB 1AT5 . "Hen Egg White Lysozyme With A Succinimide Residue" . . . . . 96.99 129 98.45 98.45 5.93e-86 . . . . 4943 1 50 no PDB 1AT6 . "Hen Egg White Lysozyme With A Isoaspartate Residue" . . . . . 96.99 129 99.22 99.22 5.61e-87 . . . . 4943 1 51 no PDB 1AZF . "Chicken Egg White Lysozyme Crystal Grown In Bromide Solution" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 52 no PDB 1B0D . "Structural Effects Of Monovalent Anions On Polymorphic Lysozyme Crystals" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 53 no PDB 1B2K . "Structural Effects Of Monovalent Anions On Polymorphic Lysozyme Crystals" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 54 no PDB 1BGI . "Orthorhombic Lysozyme Crystallized At High Temperature (310k)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 55 no PDB 1BHZ . "Low Temperature Middle Resolution Structure Of Hen Egg White Lysozyme From Masc Data" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 56 no PDB 1BQL . "Structure Of An Anti-Hel Fab Fragment Complexed With Bobwhite Quail Lysozyme" . . . . . 96.99 129 96.90 100.00 1.50e-86 . . . . 4943 1 57 no PDB 1BVK . "Humanized Anti-Lysozyme Fv Complexed With Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 58 no PDB 1BVX . "The 1.8 A Structure Of Gel Grown Tetragonal Hen Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 59 no PDB 1BWH . "The 1.8 A Structure Of Ground Control Grown Tetragonal Hen Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 60 no PDB 1BWI . "The 1.8 A Structure Of Microbatch Oil Drop Grown Tetragonal Hen Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 61 no PDB 1BWJ . "The 1.8 A Structure Of Microgravity Grown Tetragonal Hen Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 62 no PDB 1C08 . "Crystal Structure Of Hyhel-10 Fv-Hen Lysozyme Complex" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 63 no PDB 1C10 . "Crystal Structure Of Hew Lysozyme Under Pressure Of Xenon (8 Bar)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 64 no PDB 1DKJ . "Bobwhite Quail Lysozyme" . . . . . 96.99 129 96.90 100.00 1.50e-86 . . . . 4943 1 65 no PDB 1DKK . "Bobwhite Quail Lysozyme With Nitrate" . . . . . 96.99 129 96.90 100.00 1.50e-86 . . . . 4943 1 66 no PDB 1DPW . "Structure Of Hen Egg-White Lysozyme In Complex With Mpd" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 67 no PDB 1DPX . "Structure Of Hen Egg-White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 68 no PDB 1DQJ . "Crystal Structure Of The Anti-Lysozyme Antibody Hyhel-63 Complexed With Hen Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 69 no PDB 1E8L . "Nmr Solution Structure Of Hen Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 70 no PDB 1F0W . "Crystal Structure Of Orthorhombic Lysozyme Grown At Ph 6.5" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 71 no PDB 1F10 . "Crystal Structure Of Orthorhombic Lysozyme Grown At Ph 6.5 At 88% Relative Humidity" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 72 no PDB 1FDL . "Crystallographic Refinement Of The Three-Dimensional Structure Of The Fab D1.3-Lysozyme Complex At 2.5- Angstroms Resolution" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 73 no PDB 1FLQ . "Hen Egg White Lysozyme Mutant With Alanine Substituted For Glycine" . . . . . 96.99 129 99.22 99.22 2.47e-87 . . . . 4943 1 74 no PDB 1FLU . "Hen Egg White Lysozyme Mutant With Alanine Substituted For Glycine" . . . . . 96.99 129 99.22 99.22 2.47e-87 . . . . 4943 1 75 no PDB 1FLW . "Hen Egg White Lysozyme Mutant With Alanine Substituted For Glycine" . . . . . 96.99 129 99.22 99.22 2.47e-87 . . . . 4943 1 76 no PDB 1FLY . "Hen Egg White Lysozyme Mutant With Alanine Substituted For Glycine" . . . . . 96.99 129 99.22 99.22 2.47e-87 . . . . 4943 1 77 no PDB 1FN5 . "Hen Egg White Lysozyme Mutant With Alanine Substituted For Glycine" . . . . . 96.99 129 99.22 99.22 2.47e-87 . . . . 4943 1 78 no PDB 1G7H . "Crystal Structure Of Hen Egg White Lysozyme (Hel) Complexed With The Mutant Anti-Hel Monoclonal Antibody D1.3(Vlw92a)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 79 no PDB 1G7I . "Crystal Structure Of Hen Egg White Lysozyme (Hel) Complexed With The Mutant Anti-Hel Monoclonal Antibody D1.3 (Vlw92f)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 80 no PDB 1G7J . "Crystal Structure Of Hen Egg White Lysozyme (Hel) Complexed With The Mutant Anti-Hel Monoclonal Antibody D1.3 (Vlw92h)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 81 no PDB 1G7L . "Crystal Structure Of Hen Egg White Lysozyme (Hel) Complexed With The Mutant Anti-Hel Monoclonal Antibody D1.3 (Vlw92s)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 82 no PDB 1G7M . "Crystal Structure Of Hen Egg White Lysozyme (Hel) Complexed With The Mutant Anti-Hel Monoclonal Antibody D1.3 (Vlw92v)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 83 no PDB 1GPQ . "Structure Of Ivy Complexed With Its Target, Hewl" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 84 no PDB 1GWD . "Tri-Iodide Derivative Of Hen Egg-White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 85 no PDB 1GXV . "Solution Structure Of Lysozyme At Low And High Pressure" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 86 no PDB 1GXX . "Solution Structure Of Lysozyme At Low And High Pressure" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 87 no PDB 1H6M . "Covalent Glycosyl-Enzyme Intermediate Of Hen Egg White Lysozyme" . . . . . 96.99 129 99.22 100.00 1.72e-87 . . . . 4943 1 88 no PDB 1H87 . "Gadolinium Derivative Of Tetragonal Hen Egg-White Lysozyme At 1.7 A Resolution" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 89 no PDB 1HC0 . "Structure Of Lysozyme With Periodate" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 90 no PDB 1HEL . "Structural And Thermodynamic Analysis Of Compensating Mutations Within The Core Of Chicken Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 91 no PDB 1HEM . "Structural And Thermodynamic Analysis Of Compensating Mutations Within The Core Of Chicken Egg White Lysozyme" . . . . . 96.99 129 99.22 100.00 1.30e-87 . . . . 4943 1 92 no PDB 1HEN . "Structural And Thermodynamic Analysis Of Compensating Mutations Within The Core Of Chicken Egg White Lysozyme" . . . . . 96.99 129 98.45 100.00 2.03e-87 . . . . 4943 1 93 no PDB 1HEO . "Structural And Thermodynamic Analysis Of Compensating Mutations Within The Core Of Chicken Egg White Lysozyme" . . . . . 96.99 129 99.22 100.00 9.36e-88 . . . . 4943 1 94 no PDB 1HEP . "Structural And Thermodynamic Analysis Of Compensating Mutations Within The Core Of Chicken Egg White Lysozyme" . . . . . 96.99 129 97.67 100.00 6.68e-87 . . . . 4943 1 95 no PDB 1HEQ . "Structural And Thermodynamic Analysis Of Compensating Mutations Within The Core Of Chicken Egg White Lysozyme" . . . . . 96.99 129 98.45 100.00 4.27e-87 . . . . 4943 1 96 no PDB 1HER . "Structural And Thermodynamic Analysis Of Compensating Mutations Within The Core Of Chicken Egg White Lysozyme" . . . . . 96.99 129 99.22 100.00 1.78e-87 . . . . 4943 1 97 no PDB 1HEW . "Refinement Of An Enzyme Complex With Inhibitor Bound At Partial Occupancy. Hen Egg-White Lysozyme And Tri-N-Acetylchitotriose A" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 98 no PDB 1HF4 . "Structural Effects Of Monovalent Anions On Polymorphic Lysozyme Crystals" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 99 no PDB 1HSW . "Lysozyme (Mucopeptide N-Acetylmuramyl Hydrolase)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 100 no PDB 1HSX . "Lysozyme Grown At Basic Ph And Its Low Humidity Variant" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 101 no PDB 1IC4 . "Crystal Structure Of Hyhel-10 Fv Mutant(Hd32a)-Hen Lysozyme Complex" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 102 no PDB 1IC5 . "Crystal Structure Of Hyhel-10 Fv Mutant(Hd99a)-Hen Lysozyme Complex" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 103 no PDB 1IC7 . "Crystal Structure Of Hyhel-10 Fv Mutant(Hd32a99a)-Hen Lysozyme Complex" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 104 no PDB 1IEE . "Structure Of Tetragonal Hen Egg White Lysozyme At 0.94 A From Crystals Grown By The Counter-Diffusion Method" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 105 no PDB 1IO5 . "Hydrogen And Hydration Of Hen Egg-White Lysozyme Determined By Neutron Diffraction" . . . . . 96.24 129 100.00 100.00 3.51e-87 . . . . 4943 1 106 no PDB 1IOQ . "Stabilization Of Hen Egg White Lysozyme By A Cavity-Filling Mutation" . . . . . 96.99 129 98.45 98.45 1.20e-86 . . . . 4943 1 107 no PDB 1IOR . "Stabilization Of Hen Egg White Lysozyme By A Cavity-Filling Mutation" . . . . . 96.99 129 98.45 99.22 6.32e-87 . . . . 4943 1 108 no PDB 1IOS . "Stabilization Of Hen Egg White Lysozyme By A Cavity-Filling Mutation" . . . . . 96.99 129 99.22 99.22 3.83e-87 . . . . 4943 1 109 no PDB 1IOT . "Stabilization Of Hen Egg White Lysozyme By A Cavity-Filling Mutation" . . . . . 96.99 129 99.22 100.00 2.08e-87 . . . . 4943 1 110 no PDB 1IR7 . "Im Mutant Of Lysozyme" . . . . . 96.99 129 99.22 100.00 1.65e-87 . . . . 4943 1 111 no PDB 1IR8 . "Im Mutant Of Lysozyme" . . . . . 96.99 129 99.22 100.00 1.65e-87 . . . . 4943 1 112 no PDB 1IR9 . "Im Mutant Of Lysozyme" . . . . . 96.99 129 99.22 100.00 1.65e-87 . . . . 4943 1 113 no PDB 1J1O . "Crystal Structure Of Hyhel-10 Fv Mutant Ly50f Complexed With Hen Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 114 no PDB 1J1P . "Crystal Structure Of Hyhel-10 Fv Mutant Ls91a Complexed With Hen Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 115 no PDB 1J1X . "Crystal Structure Of Hyhel-10 Fv Mutant Ls93a Complexed With Hen Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 116 no PDB 1JA2 . "Binding Of N-Acetylglucosamine To Chicken Egg Lysozyme: A Powder Diffraction Study" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 117 no PDB 1JA4 . "Binding Of N-Acetylglucosamine To Chicken Egg Lysozyme: A Powder Diffraction Study" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 118 no PDB 1JA6 . "Binding Of N-Acetylglucosamine To Chicken Egg Lysozyme: A Powder Diffraction Study" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 119 no PDB 1JA7 . "Binding Of N-Acetylglucosamine To Chicken Egg Lysozyme: A Powder Diffraction Study" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 120 no PDB 1JIS . "Crystal Structure Of Tetragonal Lysozyme Grown At Ph 4.6" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 121 no PDB 1JIT . "Crystal Structure Of Tetragonal Lysozyme Grown In Presence 30% Trehalose" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 122 no PDB 1JIY . "Crystal Structure Of Tetragonal Lysozyme Grown In Presence 20% Sorbitol" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 123 no PDB 1JJ0 . "Crystal Structure Of Tetragonal Lysozyme Grown In Presence Of 30% Sucrose" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 124 no PDB 1JJ1 . "Crystal Structure Of Orthorhombic Lysozyme Grown At Ph 4.6 In Presence Of 5% Sorbitol" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 125 no PDB 1JJ3 . "Crystal Structure Of Monoclinic Lysozyme Grown At Ph 4.6" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 126 no PDB 1JPO . "Low Temperature Orthorhombic Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 127 no PDB 1JTO . "Degenerate Interfaces In Antigen-Antibody Complexes" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 128 no PDB 1JTT . "Degenerate Interfaces In Antigen-Antibody Complexes" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 129 no PDB 1KIP . "Fv Mutant Y(B 32)a (Vh Domain) Of Mouse Monoclonal Antibody D1.3 Complexed With Hen Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 130 no PDB 1KIQ . "Fv Mutant Y(B 101)f (Vh Domain) Of Mouse Monoclonal Antibody D1.3 Complexed With Hen Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 131 no PDB 1KIR . "Fv Mutant Y(A 50)s (Vl Domain) Of Mouse Monoclonal Antibody D1.3 Complexed With Hen Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 132 no PDB 1KXW . "Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains" . . . . . 96.99 129 99.22 100.00 1.92e-87 . . . . 4943 1 133 no PDB 1KXX . "Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains" . . . . . 96.99 129 98.45 100.00 1.29e-86 . . . . 4943 1 134 no PDB 1KXY . "Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains" . . . . . 96.99 129 99.22 100.00 2.76e-87 . . . . 4943 1 135 no PDB 1LCN . "Monoclinic Hen Egg White Lysozyme, Thiocyanate Complex" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 136 no PDB 1LJ3 . "Crystal Structure Of Monoclinic Lysozyme Grown At Ph 4.6" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 137 no PDB 1LJ4 . "Crystal Structure Of Monoclinic Lysozyme Grown At Ph 4.6" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 138 no PDB 1LJE . "Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 10% Sucrose" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 139 no PDB 1LJF . "Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 10% Sucrose" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 140 no PDB 1LJG . "Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 5% Glycerol" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 141 no PDB 1LJH . "Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 5% Glycerol" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 142 no PDB 1LJI . "Crystal Structure Of Monoclinic Lysozyme Grown In Presence 10% Sorbitol" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 143 no PDB 1LJJ . "Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 10% Trehalose" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 144 no PDB 1LJK . "Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 15% Trehalose" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 145 no PDB 1LKR . "Monoclinic Hen Egg White Lysozyme Iodide" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 146 no PDB 1LKS . "Hen Egg White Lysozyme Nitrate" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 147 no PDB 1LMA . "Protein Hydration And Water Structure: X-Ray Analysis Of A Closely Packed Protein Crystal With Very Low Solvent Content" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 148 no PDB 1LPI . "Hew Lysozyme: Trp...Na Cation-Pi Interaction" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 149 no PDB 1LSA . "The Influence Of Temperature On Lysozyme Crystals. Structure And Dynamics Of Protein And Water" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 150 no PDB 1LSB . "The Influence Of Temperature On Lysozyme Crystals. Structure And Dynamics Of Protein And Water" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 151 no PDB 1LSC . "The Influence Of Temperature On Lysozyme Crystals. Structure And Dynamics Of Protein And Water" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 152 no PDB 1LSD . "The Influence Of Temperature On Lysozyme Crystals. Structure And Dynamics Of Protein And Water" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 153 no PDB 1LSE . "The Influence Of Temperature On Lysozyme Crystals. Structure And Dynamics Of Protein And Water" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 154 no PDB 1LSF . "The Influence Of Temperature On Lysozyme Crystals. Structure And Dynamics Of Protein And Water" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 155 no PDB 1LSG . "Three-Dimensional Structure Of The Platelet Integrin Recognition Segment Of The Fibrinogen Gamma Chain Obtained By Carrier Prot" . . . . . 100.00 144 96.99 97.74 1.28e-88 . . . . 4943 1 156 no PDB 1LSM . "Thermal Stability Determinants Of Chicken Egg-White Lysozyme Core Mutants: Hydrophobicity, Packing Volume And Conserved Buried " . . . . . 96.99 129 97.67 99.22 1.97e-86 . . . . 4943 1 157 no PDB 1LSN . "Thermal Stability Determinants Of Chicken Egg-White Lysozyme Core Mutants: Hydrophobicity, Packing Volume And Conserved Buried " . . . . . 96.99 129 98.45 100.00 7.13e-87 . . . . 4943 1 158 no PDB 1LSY . "Crystal Structure Of The Mutant D52s Hen Egg White Lysozyme With An Oligosaccharide Product" . . . . . 96.99 147 99.22 99.22 2.89e-87 . . . . 4943 1 159 no PDB 1LSZ . "Crystal Structure Of The Mutant D52s Hen Egg White Lysozyme With An Oligosaccharide Product" . . . . . 96.99 147 99.22 99.22 2.89e-87 . . . . 4943 1 160 no PDB 1LYO . "Cross-Linked Lysozyme Crystal In Neat Water" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 161 no PDB 1LYS . "X-Ray Structure Of A Monoclinic Form Of Hen Egg-White Lysozyme Crystallized At 313k. Comparison Of Two Independent Molecules" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 162 no PDB 1LYZ . "Real-Space Refinement Of The Structure Of Hen Egg-White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 163 no PDB 1LZ8 . "Lysozyme Phased On Anomalous Signal Of Sulfurs And Chlorines" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 164 no PDB 1LZ9 . "Anomalous Signal Of Solvent Bromines Used For Phasing Of Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 165 no PDB 1LZA . "Dissection Of Protein-Carbohydrate Interactions In Mutant Hen Egg-White Lysozyme Complexes And Their Hydrolytic Activity" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 166 no PDB 1LZB . "Dissection Of Protein-Carbohydrate Interactions In Mutant Hen Egg- White Lysozyme Complexes And Their Hydrolytic Activity" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 167 no PDB 1LZC . "Dissection Of Protein-Carbohydrate Interactions In Mutant Hen Egg- White Lysozyme Complexes And Their Hydrolytic Activity" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 168 no PDB 1LZD . "Dissection Of Protein-Carbohydrate Interactions In Mutant Hen Egg-White Lysozyme Complexes And Their Hydrolytic Activity" . . . . . 96.99 129 99.22 100.00 3.58e-87 . . . . 4943 1 169 no PDB 1LZE . "Dissection Of Protein-Carbohydrate Interactions In Mutant Hen Egg- White Lysozyme Complexes And Their Hydrolytic Activity" . . . . . 96.99 129 99.22 100.00 3.58e-87 . . . . 4943 1 170 no PDB 1LZG . "Dissection Of Protein-Carbohydrate Interactions In Mutant Hen Egg- White Lysozyme Complexes And Their Hydrolytic Activity" . . . . . 96.99 129 99.22 100.00 4.66e-87 . . . . 4943 1 171 no PDB 1LZH . "The Structures Of The Monoclinic And Orthorhombic Forms Of Hen Egg-White Lysozyme At 6 Angstroms Resolution." . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 172 no PDB 1LZN . "Neutron Structure Of Hen Egg-White Lysozyme" . . . . . 96.24 129 100.00 100.00 3.51e-87 . . . . 4943 1 173 no PDB 1LZT . "Refinement Of Triclinic Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 174 no PDB 1MEL . "Crystal Structure Of A Camel Single-Domain Vh Antibody Fragment In Complex With Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 175 no PDB 1MLC . "Monoclonal Antibody Fab D44.1 Raised Against Chicken Egg- White Lysozyme Complexed With Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 176 no PDB 1N4F . "Para-Arsanilate Derivative Of Hen Egg-White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 177 no PDB 1NBY . "Crystal Structure Of Hyhel-63 Complexed With Hel Mutant K96a" . . . . . 96.99 129 99.22 99.22 4.32e-87 . . . . 4943 1 178 no PDB 1NBZ . "Crystal Structure Of Hyhel-63 Complexed With Hel Mutant K97a" . . . . . 96.99 129 99.22 99.22 4.32e-87 . . . . 4943 1 179 no PDB 1NDG . "Crystal Structure Of Fab Fragment Of Antibody Hyhel-8 Complexed With Its Antigen Lysozyme" . . . . . 96.99 129 99.22 99.22 5.37e-87 . . . . 4943 1 180 no PDB 1NDM . "Crystal Structure Of Fab Fragment Of Antibody Hyhel-26 Complexed With Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 181 no PDB 1P2C . "Crystal Structure Analysis Of An Anti-Lysozyme Antibody" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 182 no PDB 1PS5 . "Structure Of The Monoclinic C2 Form Of Hen Egg-White Lysozyme At 2.0 Angstroms Resolution" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 183 no PDB 1QIO . "Specific Chemical And Structural Damage Caused By Intense Synchrotron Radiation To Hen Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 184 no PDB 1QTK . "Crystal Structure Of Hew Lysozyme Under Pressure Of Krypton (55 Bar)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 185 no PDB 1RCM . "Crystal Structure Of A Ubiquitin-Dependent Degradation Substrate: A Three-Disulfide Form Of Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 186 no PDB 1RFP . "Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 187 no PDB 1RI8 . "Crystal Structure Of The Camelid Single Domain Antibody 1d2l19 In Complex With Hen Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 188 no PDB 1RJC . "Crystal Structure Of The Camelid Single Domain Antibody Cab-Lys2 In Complex With Hen Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 189 no PDB 1SF4 . "Binding Of N,n'-diacetylchitobiose To Hew Lysozyme: A Powder Diffraction Study" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 190 no PDB 1SF6 . ; Binding Of N,N',N"-Triacetylchitotriose To Hew Lysozyme: A Powder Diffraction Study ; . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 191 no PDB 1SF7 . "Binding Of Tetra-N-Acetylchitotetraose To Hew Lysozyme: A Powder Diffraction Study" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 192 no PDB 1SFB . "Binding Of Penta-N-Acetylchitopentaose To Hew Lysozyme: A Powder Diffraction Study" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 193 no PDB 1SFG . "Binding Of Hexa-N-Acetylchitohexaose: A Powder Diffraction Study" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 194 no PDB 1SQ2 . "Crystal Structure Analysis Of The Nurse Shark New Antigen Receptor (nar) Variable Domain In Complex With Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 195 no PDB 1T3P . "Half-Sandwich Arene Ruthenium(Ii)-Enzyme Complex" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 196 no PDB 1T6V . "Crystal Structure Analysis Of The Nurse Shark New Antigen Receptor (nar) Variable Domain In Complex With Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 197 no PDB 1UA6 . "Crystal Structure Of Hyhel-10 Fv Mutant Sfsf Complexed With Hen Egg White Lysozyme Complex" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 198 no PDB 1UC0 . "Crystal Structure Of Wild-Type Hen-Egg White Lysozyme Singly Labeled With 2',3'-Epoxypropyl Beta-Glycoside Of N-Acetyllactosami" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 199 no PDB 1UCO . "Hen Egg-White Lysozyme, Low Humidity Form" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 200 no PDB 1UIA . "Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains" . . . . . 96.99 127 98.45 98.45 7.00e-84 . . . . 4943 1 201 no PDB 1UIB . "Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains" . . . . . 96.99 127 98.45 98.45 7.00e-84 . . . . 4943 1 202 no PDB 1UIC . "Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains" . . . . . 96.99 129 99.22 99.22 1.57e-86 . . . . 4943 1 203 no PDB 1UID . "Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains" . . . . . 96.99 129 99.22 99.22 1.42e-86 . . . . 4943 1 204 no PDB 1UIE . "Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains" . . . . . 96.99 129 99.22 99.22 2.24e-86 . . . . 4943 1 205 no PDB 1UIF . "Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains" . . . . . 96.99 129 99.22 99.22 2.15e-86 . . . . 4943 1 206 no PDB 1UIG . "Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 207 no PDB 1UIH . "Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 208 no PDB 1UUZ . "Ivy:a New Family Of Protein" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 209 no PDB 1V7S . "Triclinic Hen Lysozyme Crystallized At 313k From A D2o Solution" . . . . . 96.24 129 100.00 100.00 2.64e-87 . . . . 4943 1 210 no PDB 1V7T . "Triclinic Lysozyme With Low Solvent Content Obtained By Phase Transition" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 211 no PDB 1VAT . "Iodine Derivative Of Hen Egg-White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 212 no PDB 1VAU . "Xenon Derivative Of Hen Egg-White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 213 no PDB 1VDP . "The Crystal Structure Of The Monoclinic Form Of Hen Egg White Lysozyme At 1.7 Angstroms Resolution In Space" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 214 no PDB 1VDQ . "The Crystal Structure Of The Orthorhombic Form Of Hen Egg White Lysozyme At 1.5 Angstroms Resolution" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 215 no PDB 1VDS . "The Crystal Structure Of The Tetragonal Form Of Hen Egg White Lysozyme At 1.6 Angstroms Resolution In Space" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 216 no PDB 1VDT . "The Crystal Structure Of The Tetragonal Form Of Hen Egg White Lysozyme At 1.7 Angstroms Resolution Under Basic Conditions In Sp" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 217 no PDB 1VED . "The Crystal Structure Of The Orthorhombic Form Of Hen Egg White Lysozyme At 1.9 Angstroms Resolution In Space" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 218 no PDB 1VFB . "Bound Water Molecules And Conformational Stabilization Help Mediate An Antigen-Antibody Association" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 219 no PDB 1W6Z . "High Energy Tetragonal Lysozyme X-ray Structure" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 220 no PDB 1WTM . "X-Ray Structure Of Hew Lysozyme Orthorhombic Crystal Formed In The Earth's Magnetic Field" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 221 no PDB 1WTN . "The Structure Of Hew Lysozyme Orthorhombic Crystal Growth Under A High Magnetic Field" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 222 no PDB 1XEI . "The Crystal Structures Of Lysozyme At Very Low Levels Of Hydration" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 223 no PDB 1XEJ . "The Crystal Structures Of Lysozyme At Very Low Levels Of Hydration" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 224 no PDB 1XEK . "The Crystal Structures Of Lysozyme At Very Low Levels Of Hydration" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 225 no PDB 1XFP . "Crystal Structure Of The Cdr2 Germline Reversion Mutant Of Cab-lys3 In Complex With Hen Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 226 no PDB 1XGP . "Structure For Antibody Hyhel-63 Y33a Mutant Complexed With Hen Egg Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 227 no PDB 1XGQ . "Structure For Antibody Hyhel-63 Y33v Mutant Complexed With Hen Egg Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 228 no PDB 1XGR . "Structure For Antibody Hyhel-63 Y33i Mutant Complexed With Hen Egg Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 229 no PDB 1XGT . "Structure For Antibody Hyhel-63 Y33l Mutant Complexed With Hen Egg Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 230 no PDB 1XGU . "Structure For Antibody Hyhel-63 Y33f Mutant Complexed With Hen Egg Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 231 no PDB 1YIK . "Structure Of Hen Egg White Lysozyme Soaked With Cu-Cyclam" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 232 no PDB 1YIL . "Structure Of Hen Egg White Lysozyme Soaked With Cu2- Xylylbicyclam" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 233 no PDB 1YKX . "Effect Of Alcohols On Protein Hydration" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 234 no PDB 1YKY . "Effect Of Alcohols On Protein Hydration" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 235 no PDB 1YKZ . "Effect Of Alcohols On Protein Hydration" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 236 no PDB 1YL0 . "Effect Of Alcohols On Protein Hydration" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 237 no PDB 1YL1 . "Effect Of Alcohols On Protein Hydration" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 238 no PDB 1YQV . "The Crystal Structure Of The Antibody Fab Hyhel5 Complex With Lysozyme At 1.7a Resolution" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 239 no PDB 1Z55 . "Effect Of Alcohols On Protein Hydration" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 240 no PDB 1ZMY . "Cabbcii-10 Vhh Framework With Cdr Loops Of Cablys3 Grafted On It And In Complex With Hen Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 241 no PDB 1ZV5 . "Crystal Structure Of The Variable Domain Of The Camelid Heavy-Chain Antibody D2-L29 In Complex With Hen Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 242 no PDB 1ZVH . "Crystal Stucture Of The Vhh Domain D2-L24 In Complex With Hen Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 243 no PDB 1ZVY . "Crystal Structure Of The Vhh D3-l11 In Complex With Hen Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 244 no PDB 2A6U . "Ph Evolution Of Tetragonal Hewl At 4 Degrees Celcius." . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 245 no PDB 2A7D . "On The Routine Use Of Soft X-Rays In Macromolecular Crystallography, Part Iii- The Optimal Data Collection Wavelength" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 246 no PDB 2A7F . "On The Routine Use Of Soft X-Rays In Macromolecular Crystallography, Part Iii- The Optimal Data Collection Wavelength" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 247 no PDB 2AUB . "Lysozyme Structure Derived From Thin-Film-Based Crystals" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 248 no PDB 2B5Z . "Hen Lysozyme Chemically Glycosylated" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 249 no PDB 2BLX . 'Hewl Before A High Dose X-Ray "burn"' . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 250 no PDB 2BLY . 'Hewl After A High Dose X-Ray "burn"' . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 251 no PDB 2BPU . "The Kedge Holmium Derivative Of Hen Egg-White Lysozyme At High Resolution From Single Wavelength Anomalous Diffraction" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 252 no PDB 2C8O . "Lysozyme (1sec) And Uv Lasr Excited Fluorescence" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 253 no PDB 2C8P . "Lysozyme (60sec) And Uv Laser Excited Fluorescence" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 254 no PDB 2CDS . Lysozyme . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 255 no PDB 2CGI . "Siras Structure Of Tetragonal Lysosyme Using Derivative Data Collected At The High Energy Remote Holmium Kedge" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 256 no PDB 2D4I . "Monoclinic Hen Egg-White Lysozyme Crystallized At Ph4.5 Form Heavy Water Solution" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 257 no PDB 2D4J . "Transformed Monoclinic Crystal Of Hen Egg-White Lysozyme From A Heavy Water Solution" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 258 no PDB 2D4K . "Monoclinic Hen Egg-White Lysozyme Crystallized At 313k" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 259 no PDB 2D6B . "Novel Bromate Species Trapped Within A Protein Crystal" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 260 no PDB 2D91 . "Structure Of Hyper-Vil-Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 261 no PDB 2DQC . "Crystal Structure Of Hyhel-10 Fv Mutant(Hy33f) Complexed With Hen Egg Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 262 no PDB 2DQD . "Crystal Structure Of Hyhel-10 Fv Mutant (Hy50f) Complexed With Hen Egg Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 263 no PDB 2DQE . "Crystal Structure Of Hyhel-10 Fv Mutant (Hy53a) Complexed With Hen Egg Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 264 no PDB 2DQF . "Crystal Structure Of Hyhel-10 Fv Mutant (Y33ay53a) Complexed With Hen Egg Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 265 no PDB 2DQG . "Crystal Structure Of Hyhel-10 Fv Mutant (Hy53f) Complexed With Hen Egg Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 266 no PDB 2DQH . "Crystal Structure Of Hyhel-10 Fv Mutant (Hy58a) Complexed With Hen Egg Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 267 no PDB 2DQI . "Crystal Structure Of Hyhel-10 Fv Mutant (Ly50a) Complexed With Hen Egg Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 268 no PDB 2DQJ . "Crystal Structure Of Hyhel-10 Fv (Wild-Type) Complexed With Hen Egg Lysozyme At 1.8a Resolution" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 269 no PDB 2EIZ . "Crystal Structure Of Humanized Hyhel-10 Fv Mutant(hw47y)-hen Lysozyme Complex" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 270 no PDB 2EKS . "Crystal Structure Of Humanized Hyhel-10 Fv-Hen Lysozyme Complex" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 271 no PDB 2EPE . "Crystal Structure Analysis Of Hen Egg White Lysozyme Grown By Capillary Method" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 272 no PDB 2F2N . "Triclinic Hen Egg Lysozyme Cross-linked By Glutaraldehyde" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 273 no PDB 2F30 . "Triclinic Cross-Linked Lysozyme Soaked With 4.5m Urea" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 274 no PDB 2F4A . "Triclinic Cross-linked Lysozyme Soaked With Thiourea 1.5m" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 275 no PDB 2F4G . "Triclinic Cross-Linked Lysozyme Soaked In Bromoethanol 1m" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 276 no PDB 2FBB . "Crystal Structure Analysis Of Hexagonal Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 277 no PDB 2G4P . "Anomalous Substructure Of Lysozyme At Ph 4.5" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 278 no PDB 2G4Q . "Anomalous Substructure Of Lysozyme At Ph 8.0" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 279 no PDB 2H9J . "Structure Of Hen Egg White Lysozyme Soaked With Ni2- Xylylbicyclam" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 280 no PDB 2H9K . "Structure Of Hen Egg White Lysozyme Soaked With Ni-Cyclam" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 281 no PDB 2HS7 . "Multipattern Rietveld Refinement With Protein Powder Data: An Approach To Higher Resolution" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 282 no PDB 2HS9 . "Multipattern Rietveld Refinement With Protein Powder Data: An Approach To Higher Resolution" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 283 no PDB 2HSO . "Multipattern Rietveld Refinement With Protein Powder Data: An Approach To Higher Resolution" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 284 no PDB 2HTX . "Crystal Structure Analysis Of Hen Egg White Lysozyme Crosslinked By Polymerized Glutaraldehyde In Acidic Environment" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 285 no PDB 2HU1 . "Crystal Structure Analysis Of Hen Egg White Lyszoyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 286 no PDB 2HU3 . "Parent Structure Of Hen Egg White Lysozyme Grown In Acidic Ph 4.8. Refinement For Comparison With Crosslinked Molecules Of Lyso" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 287 no PDB 2HUB . "Structure Of Hen Egg-White Lysozyme Determined From Crystals Grown In Ph 7.5" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 288 no PDB 2I25 . "Crystal Structure Analysis Of The Nurse Shark New Antigen Receptor Pbla8 Variable Domain In Complex With Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 289 no PDB 2I26 . "Crystal Structure Analysis Of The Nurse Shark New Antigen Receptor Ancestral Variable Domain In Complex With Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 290 no PDB 2I6Z . "X-Ray Diffraction Studies Of Adducts Between Anticancer Platinum Drugs And Hen Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 291 no PDB 2IFF . "Structure Of An Antibody-Lysozyme Complex: Effect Of A Conservative Mutation" . . . . . 96.99 129 99.22 100.00 1.33e-87 . . . . 4943 1 292 no PDB 2LYM . "Crystal Structure Of Hen Egg-White Lysozyme At A Hydrostatic Pressure Of 1000 Atmospheres" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 293 no PDB 2LYO . "Cross-Linked Chicken Lysozyme Crystal In 90% Acetonitrile- Water" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 294 no PDB 2LYZ . "Real-Space Refinement Of The Structure Of Hen Egg-White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 295 no PDB 2LZH . "The Structures Of The Monoclinic And Orthorhombic Forms Of Hen Egg-White Lysozyme At 6 Angstroms Resolution." . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 296 no PDB 2LZT . "Refinement Of Triclinic Lysozyme. Ii. The Method Of Stereochemically Restrained Least-Squares" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 297 no PDB 2PC2 . "Lysozyme Cocrystallized With Tris-Dipicolinate Eu Complex" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 298 no PDB 2Q0M . "Tricarbonylmanganese(I)-Lysozyme Complex : A Structurally Characterized Organometallic Protein" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 299 no PDB 2VB1 . "Hewl At 0.65 Angstrom Resolution" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 300 no PDB 2W1L . "The Interdependence Of Wavelength, Redundancy And Dose In Sulfur Sad Experiments: 0.979 A Wavelength 991 Images Data" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 301 no PDB 2W1M . "The Interdependence Of Wavelength, Redundancy And Dose In Sulfur Sad Experiments: 2.070 A Wavelength With 2theta 30 Degrees Dat" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 302 no PDB 2W1X . "The Interdependence Of Wavelength, Redundancy And Dose In Sulfur Sad Experiments: 1.284 A Wavelength 360 Images Data" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 303 no PDB 2W1Y . "The Interdependence Of Wavelength, Redundancy And Dose In Sulfur Sad Experiments: 1.540 A Wavelength 180 Images Data" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 304 no PDB 2WAR . "Hen Egg White Lysozyme E35q Chitopentaose Complex" . . . . . 96.99 129 99.22 100.00 1.72e-87 . . . . 4943 1 305 no PDB 2X0A . "Mpd-Lysozyme Structure At 55.5 Kev Using A Trixxel Csi-Asi Based Digital Imager And The New Esrf U22 Undulator Source At Id15" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 306 no PDB 2XBR . "Raman Crystallography Of Hen White Egg Lysozyme - Low X-Ray Dose (0.2 Mgy)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 307 no PDB 2XBS . "Raman Crystallography Of Hen White Egg Lysozyme - High X- Ray Dose (16 Mgy)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 308 no PDB 2XJW . "Lysozyme-Co Releasing Molecule Adduct" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 309 no PDB 2XTH . "K2ptbr6 Binding To Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 310 no PDB 2YBH . "Nitrate X-Ray Induced Reduction On Hewl Crystals (2.31 Mgy)." . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 311 no PDB 2YBI . "Nitrate X-Ray Induced Reduction On Hewl Crystals (6.62 Mgy)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 312 no PDB 2YBJ . "Nitrate X-Ray Induced Reduction On Hewl Crystals (12.31 Mgy)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 313 no PDB 2YBL . "Nitrate X-Ray Induced Reduction On Hewl Crystals (17.9 Mgy)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 314 no PDB 2YBM . "Nitrate X-Ray Induced Reduction On Hewl Crystals (23.3 Mgy)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 315 no PDB 2YBN . "Nitrate X-Ray Induced Reduction On Hewl Crystals (28.6 Mgy)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 316 no PDB 2YDG . "Ascorbate Co-Crystallized Hewl." . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 317 no PDB 2YSS . "Crystal Structure Of Humanized Hyhel-10 Fv Mutant(Hq39kw47y)-Hen Lysozyme Complex" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 318 no PDB 2YVB . "High Resolution X-ray Crystal Structure Of Tetragonal Hen Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 319 no PDB 2Z12 . "Structure Of The Transformed Monoclinic Lysozyme By Controlled Dehydration" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 320 no PDB 2Z18 . "Phase Transition Of Monoclinic Lysozyme Crystal Soaked In A 10% Nacl Solution" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 321 no PDB 2Z19 . "Phase Transition Of Monoclinic Lysozyme Crystal Soaked In A Saturated Nacl Solution" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 322 no PDB 2ZNW . "Crystal Structure Of Scfv10 In Complex With Hen Egg Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 323 no PDB 2ZNX . "5-fluorotryptophan Incorporated Scfv10 Complexed To Hen Egg Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 324 no PDB 2ZQ3 . "The Crystal Structure Of The Orthorhombic Form Of Hen Egg White Lysozyme At 1.6 Angstroms Resolution" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 325 no PDB 2ZQ4 . "The Crystal Structure Of The Orthorhombic Form Of Hen Egg White Lysozyme At 2.0 Angstroms Resolution" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 326 no PDB 2ZYP . "X-Ray Structure Of Hen Egg-White Lysozyme With Poly(Allyl Amine)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 327 no PDB 3A34 . "Effect Of Ariginine On Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 328 no PDB 3A3Q . "Structure Of N59d Hen Egg-white Lysozyme In Complex With (glcnac)3" . . . . . 96.99 129 99.22 100.00 1.92e-87 . . . . 4943 1 329 no PDB 3A3R . "Structure Of N59d Hen Egg-white Lysozyme" . . . . . 96.99 129 99.22 100.00 1.92e-87 . . . . 4943 1 330 no PDB 3A67 . "Crystal Structure Of Hyhel-10 Fv Mutant Ln31d Complexed With White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 331 no PDB 3A6B . "Crystal Structure Of Hyhel-10 Fv Mutant Ln32d Complexed With White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 332 no PDB 3A6C . "Crystal Structure Of Hyhel-10 Fv Mutant Ln92d Complexed With White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 333 no PDB 3A8Z . "Crystal Structure Of Hen Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 334 no PDB 3A90 . "Crystal Structure Of Hen Egg White Lysozyme Soaked With 1mm Rhcl3" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 335 no PDB 3A91 . "Crystal Structure Of Hen Egg White Lysozyme Soaked With 5mm Rhcl3" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 336 no PDB 3A92 . "Crystal Structure Of Hen Egg White Lysozyme Soaked With 10mm Rhcl3" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 337 no PDB 3A93 . "Crystal Structure Of Hen Egg White Lysozyme Soaked With 30mm Rhcl3" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 338 no PDB 3A94 . "Crystal Structure Of Hen Egg White Lysozyme Soaked With 100mm Rhcl3" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 339 no PDB 3A95 . "Crystal Structure Of Hen Egg White Lysozyme Soaked With 100mm Rhcl3 At Ph3.8" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 340 no PDB 3A96 . "Crystal Structure Of Hen Egg White Lysozyme Soaked With 100mm Rhcl3 At Ph2.2" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 341 no PDB 3AGG . "X-Ray Analysis Of Lysozyme In The Absence Of Arg" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 342 no PDB 3AGH . "X-Ray Analysis Of Lysozyme In The Presence Of 200 Mm Arg" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 343 no PDB 3AGI . "High Resolution X-Ray Analysis Of Arg-Lysozyme Complex In The Presence Of 500 Mm Arg" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 344 no PDB 3AJN . "Structural Basis Of Glycine Amide On Suppression Of Protein Aggregation By High Resolution X-Ray Analysis" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 345 no PDB 3ATN . "Glycine Ethyl Ester Shielding On The Aromatic Surfaces Of Lysozyme: Implication For Suppression Of Protein Aggregation" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 346 no PDB 3ATO . "Glycine Ethyl Ester Shielding On The Aromatic Surfaces Of Lysozyme: Implication For Suppression Of Protein Aggregation" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 347 no PDB 3AW6 . "Crystal Structure Of Tetragonal Hen Egg White Lysozyme At 84.2% Relative Humidity" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 348 no PDB 3AW7 . "Crystal Structure Of Tetragonal Hen Egg White Lysozyme At 71.9% Relative Humidity" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 349 no PDB 3AZ4 . "Crystal Structure Of Co/o-hewl" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 350 no PDB 3AZ5 . "Crystal Structure Of Pt/o-hewl" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 351 no PDB 3AZ6 . "Crystal Structure Of Co/t-hewl" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 352 no PDB 3AZ7 . "Crystal Structure Of Pt/t-hewl" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 353 no PDB 3B6L . "Crystal Structure Of Lysozyme Folded In Sds And 2-Methyl-2, 4-Pentanediol" . . . . . 96.99 147 100.00 100.00 3.59e-88 . . . . 4943 1 354 no PDB 3B72 . "Crystal Structure Of Lysozyme Folded In Sds And 2-Methyl-2, 4-Pentanediol" . . . . . 96.99 147 100.00 100.00 3.59e-88 . . . . 4943 1 355 no PDB 3D9A . "High Resolution Crystal Structure Structure Of Hyhel10 Fab Complexed To Hen Egg Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 356 no PDB 3E3D . "Structure Of Hen Egg White Lysozyme With The Magic Triangle I3c" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 357 no PDB 3EMS . "Effect Of Ariginine On Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 358 no PDB 3EXD . "Sulfur-Sad Phased Hewl Crystal" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 359 no PDB 3F6Z . "Crystal Structure Of Pseudomonas Aeruginosa Mlic In Complex With Hen Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 360 no PDB 3G3A . "Structure Of A Lamprey Variable Lymphocyte Receptor In Complex With A Protein Antigen" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 361 no PDB 3G3B . "Structure Of A Lamprey Variable Lymphocyte Receptor Mutant In Complex With A Protein Antigen" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 362 no PDB 3HFM . "Structure Of An Antibody-Antigen Complex. Crystal Structure Of The HyHEL-10 Fab-Lysozyme Complex" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 363 no PDB 3IJU . "Chicken Egg White Lysozyme By Highly Ordered Apa (Anodic Porous Alumina) Nanotemplate Crystallization Method" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 364 no PDB 3IJV . "Chicken Egg White Lysozyme By Classical Hanging Drop Vapour Diffusion Method" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 365 no PDB 3J4G . "Structure Of Lysozyme Solved By Microed To 2.9 A" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 366 no PDB 3J6K . "2.5a Structure Of Lysozyme Solved By Microed" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 367 no PDB 3KAM . "Hen Egg White Lysozyme Derivatized With Rhenium(I) Diaquatricarbonyl Cation" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 368 no PDB 3LYM . "Crystal Structure Of Hen Egg-White Lysozyme At A Hydrostatic Pressure Of 1000 Atmospheres" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 369 no PDB 3LYO . "Cross-Linked Chicken Lysozyme Crystal In 95% Acetonitrile- Water" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 370 no PDB 3LYT . "Comparison Of Radiation-Induced Decay And Structure Refinement From X-Ray Data Collected From Lysozyme Crystals At Low And Ambi" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 371 no PDB 3LYZ . "Real-Space Refinement Of The Structure Of Hen Egg-White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 372 no PDB 3LZT . "Refinement Of Triclinic Lysozyme At Atomic Resolution" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 373 no PDB 3M18 . "Crystal Structure Of Variable Lymphocyte Receptor Vlra.R2.1 In Complex With Hen Egg Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 374 no PDB 3M3U . "Effect Of Temperature On Tryptophan Fluorescence In Lysozyme Crystals" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 375 no PDB 3N9A . "Mite-Y Lysozyme: Vegemite" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 376 no PDB 3N9C . "Mite-Y Lysozyme: Marmite" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 377 no PDB 3N9E . "Mite-Y Lysozyme: Promite" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 378 no PDB 3OJP . "D52n Mutant Of Hen Egg White Lysozyme (Hewl)" . . . . . 96.99 129 99.22 100.00 2.76e-87 . . . . 4943 1 379 no PDB 3OK0 . "E35a Mutant Of Hen Egg White Lysozyme (Hewl)" . . . . . 96.99 129 99.22 99.22 5.67e-87 . . . . 4943 1 380 no PDB 3P4Z . "Time-Dependent And Protein-Directed In Situ Growth Of Gold Nanoparticles In A Single Crystal Of Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 381 no PDB 3P64 . "Time-Dependent And Protein-Directed In Situ Growth Of Gold Nanoparticles In A Single Crystal Of Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 382 no PDB 3P65 . "Time-Dependent And Protein-Directed In Situ Growth Of Gold Nanoparticles In A Single Crystal Of Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 383 no PDB 3P66 . "Time-Dependent And Protein-Directed In Situ Growth Of Gold Nanoparticles In A Single Crystal Of Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 384 no PDB 3P68 . "Time-Dependent And Protein-Directed In Situ Growth Of Gold Nanoparticles In A Single Crystal Of Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 385 no PDB 3QE8 . "Crystal Structure Analysis Of Lysozyme-Bound Fac-[re(Co)3(H2o)(Im)]+" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 386 no PDB 3QNG . "Crystal Structure Analysis Of Lysozyme-Bound Fac-[re(Co)3(L-Serine)]" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 387 no PDB 3QY4 . "Crystallization And In Situ Data Collection Of Lysozyme Using The Crystal Former" . . . . . 96.24 129 99.22 99.22 2.01e-86 . . . . 4943 1 388 no PDB 3RNX . "Crystal Structure Of Lysozyme In 30% Ethanol" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 389 no PDB 3RT5 . "Lysozyme In 30% Propanol" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 390 no PDB 3RU5 . "Silver Metallated Hen Egg White Lysozyme At 1.35 A" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 391 no PDB 3RW8 . "Crystal Structure Of Lysozyme In 40% Ethanol" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 392 no PDB 3RZ4 . "Hen Egg-White Lysozyme In Hepes Buffer At Ph 7.5" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 393 no PDB 3SP3 . "Lysozyme In 20% Sucrose" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 394 no PDB 3T6U . "Crystal Structure Of Lysozyme In 40% Sucrose" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 395 no PDB 3TMU . "X-Ray Radiation Damage To Hewl Crystals Soaked In 100mm Sodium Nitrate (Undosed)" . . . . . 96.99 147 100.00 100.00 3.59e-88 . . . . 4943 1 396 no PDB 3TMV . "X-Ray Radiation Damage To Hewl Crystals Soaked In 100mm Sodium Nitrate (Dose0.12mgy)" . . . . . 96.99 147 100.00 100.00 3.59e-88 . . . . 4943 1 397 no PDB 3TMW . "X-Ray Radiation Damage To Hewl Crystals Soaked In 100mm Sodium Nitrate (Undosed)" . . . . . 96.99 147 100.00 100.00 3.59e-88 . . . . 4943 1 398 no PDB 3TMX . "X-Ray Radiation Damage To Hewl Crystals Soaked In 100mm Sodium Nitrate (Dose1.9mgy)" . . . . . 96.99 147 100.00 100.00 3.59e-88 . . . . 4943 1 399 no PDB 3TXB . "Hewl Co-crystallization With Cisplatin In Aqueous Media With Glycerol As The Cryoprotectant" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 400 no PDB 3TXD . "Hewl Co-crystallization With Carboplatin In Aqueous Media With Glycerol As The Cryoprotectant" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 401 no PDB 3TXE . "Hewl Co-crystallization With Carboplatin In Aqueous Media With Paratone As The Cryoprotectant" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 402 no PDB 3TXF . "Hewl Co-crystallization With Cisplatin In Dmso Media With Glycerol As The Cryoprotectant" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 403 no PDB 3TXG . "Hewl Co-crystallization With Cisplatin In Dmso Media With Paratone As The Cryoprotectant" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 404 no PDB 3TXH . "Hewl Co-crystallization With Carboplatin In Dmso Media With Glycerol As The Cryoprotectant" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 405 no PDB 3TXI . "Hewl Co-crystallization With Carboplatin In Dmso Media With Paratone As The Cryoprotectant" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 406 no PDB 3TXJ . "Hewl Co-crystallization With Nag With Silicone Oil As The Cryoprotectant" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 407 no PDB 3TXK . "Hewl Co-crystallization With Cisplatin In Dmso Media With Paratone As The Cryoprotectant At Ph 6.5" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 408 no PDB 3ULR . "Lysozyme Contamination Facilitates Crystallization Of A Hetero- Trimericcortactin:arg:lysozyme Complex" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 409 no PDB 3VFX . "Lysozyme Dimer" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 410 no PDB 3W6A . "Crystal Structure Of Cross-linked Tetragonal Hen Egg White Lysozyme Soaked Wiht 5mm [ru(benzene)cl2]2" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 411 no PDB 3WL2 . "Monoclinic Lysozyme At 0.96 A Resolution" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 412 no PDB 3WMK . "Crystal Structure Of Hen Egg-white Lysozyme In Ph 4.5 Sodium Acetatewith 1m Nacl At 277k" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 413 no PDB 3WPJ . "Spatiotemporal Development Of Soaked Protein Crystal; Native" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 414 no PDB 3WPK . "Spatiotemporal Development Of Soaked Protein Crystal; 750 Sec" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 415 no PDB 3WPL . "Spatiotemporal Development Of Soaked Protein Crystal; 2510 Sec" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 416 no PDB 3WU7 . "Spatiotemporal Development Of Soaked Protein Crystal; Derivative 250 Sec" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 417 no PDB 3WU8 . "Spatiotemporal Development Of Soaked Protein Crystal; Derivative 1080 Sec" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 418 no PDB 3WU9 . "Spatiotemporal Development Of Soaked Protein Crystal; Derivative 1580 Sec" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 419 no PDB 3WUA . "Spatiotemporal Development Of Soaked Protein Crystal; Derivative 3610 Sec" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 420 no PDB 3WUL . "Crystal Structure Of Hen Egg-white Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 421 no PDB 3WUM . "Crystal Structure Of Hen Egg-white Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 422 no PDB 3WXT . "Crystal Structure Of Hen Egg-white Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 423 no PDB 3WXU . "Crystal Structure Of Hen Egg-white Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 424 no PDB 3ZEK . "Hen Egg-White Lysozyme Structure Determined At Room Temperature By In-Situ Diffraction In Chipx" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 425 no PDB 3ZVQ . "Crystal Structure Of Proteolyzed Lysozyme" . . . . . 52.63 70 100.00 100.00 2.54e-43 . . . . 4943 1 426 no PDB 4A7D . "X-Ray Crystal Structure Of Hewl Flash-Cooled At High Pressure" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 427 no PDB 4A8A . "Asymmetric Cryo-Em Reconstruction Of E. Coli Degq 12-Mer In Complex With Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 428 no PDB 4A8B . "Symmetrized Cryo-Em Reconstruction Of E. Coli Degq 12-Mer In Complex With Lysozymes" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 429 no PDB 4AGA . "Hofmeister Effects Of Ionic Liquids In Protein Crystallization: Direct And Water-Mediated Interactions" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 430 no PDB 4AXT . "Crystal Structure Of Hen Egg White Lysozyme From An Auto Harvested Crystal, Control Experiment" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 431 no PDB 4B0D . "Crystal Structure Of Hen Egg White Lysozyme From An Auto Harvested Crystal" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 432 no PDB 4B1A . "Crystal Structure Of Lysozyme With Keggin Molecule" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 433 no PDB 4B49 . "1.15 A Structure Of Lysozyme Crystallized Without 2-Methyl- 2,4-Pentanediol" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 434 no PDB 4B4E . "1.00 A Structure Of Lysozyme Crystallized With (r)-2-methyl-2,4-pentanediol" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 435 no PDB 4B4I . "1.20 A Structure Of Lysozyme Crystallized With (S)-2-Methyl-2,4-Pentanediol" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 436 no PDB 4B4J . "1.25 A Structure Of Lysozyme Crystallized With (rs)-2-methyl-2,4-pentanediol" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 437 no PDB 4BAD . "Hen Egg-White Lysozyme Structure In Complex With The Europium Tris-Hydroxymethyltriazoledipicolinate Complex At 1.35 A Resoluti" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 438 no PDB 4BAF . "Hen Egg-white Lysozyme Structure In Complex With The Europium Tris-hydroxyethyltriazoledipicolinate Complex At 1.51 A Resolutio" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 439 no PDB 4BAP . "Hen Egg-White Lysozyme Structure In Complex With The Europium Tris-Hydroxyethylcholinetriazoledipicolinate Complex At 1.21 A Re" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 440 no PDB 4BS7 . "Hen Egg-white Lysozyme Structure Determined At Room Temperature By In-situ Diffraction And Sad Phasing In Chipx" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 441 no PDB 4C3W . "Vanadium(iv)-picolinate Complexed With Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 442 no PDB 4CJ2 . "Crystal Structure Of Hewl In Complex With Affitin H4" . . . . . 96.99 147 100.00 100.00 3.59e-88 . . . . 4943 1 443 no PDB 4D9Z . "Lysozyme At 318k" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 444 no PDB 4DC4 . "Lysozyme Trimer" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 445 no PDB 4DD0 . "Eval Processed Hewl, Cisplatin Aqueous Glycerol" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 446 no PDB 4DD1 . "Eval Processed Hewl, Cisplatin Aqueous Paratone" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 447 no PDB 4DD2 . "Eval Processed Hewl, Carboplatin Aqueous Glycerol" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 448 no PDB 4DD3 . "Eval Processed Hewl, Carboplatin Aqueous Paratone" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 449 no PDB 4DD4 . "Eval Processed Hewl, Cisplatin Dmso Glycerol" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 450 no PDB 4DD6 . "Eval Processed Hewl, Cisplatin Dmso Paratone" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 451 no PDB 4DD7 . "Eval Processed Hewl, Carboplatin Dmso Glycerol" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 452 no PDB 4DD9 . "Eval Processed Hewl, Carboplatin Dmso Paratone" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 453 no PDB 4DDA . "Eval Processed Hewl, Nag" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 454 no PDB 4DDB . "Eval Processed Hewl, Cisplatin Dmso Paratone Ph 6.5" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 455 no PDB 4DDC . "Eval Processed Hewl, Cisplatin Dmso Nag Silicone Oil" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 456 no PDB 4DT3 . "Crystal Structure Of Zinc-charged Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 457 no PDB 4E3U . "Crystal Structure Of Hen Egg White Lysozyme Cryoprotected In Proline" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 458 no PDB 4EOF . "Lysozyme In The Presence Of Arginine" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 459 no PDB 4ET8 . "Hen Egg-White Lysozyme Solved From 40 Fs Free-Electron Laser Pulse Data" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 460 no PDB 4ET9 . "Hen Egg-White Lysozyme Solved From 5 Fs Free-Electron Laser Pulse Data" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 461 no PDB 4ETA . "Lysozyme, Room Temperature, 400 Kgy Dose" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 462 no PDB 4ETB . "Lysozyme, Room Temperature, 200 Kgy Dose" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 463 no PDB 4ETC . "Lysozyme, Room Temperature, 24 Kgy Dose" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 464 no PDB 4ETD . "Lysozyme, Room-Temperature, Rotating Anode, 0.0026 Mgy" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 465 no PDB 4ETE . "Lysozyme, Room-Temperature, Rotating Anode, 0.0021 Mgy" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 466 no PDB 4FJR . "Mode Of Interaction Of Merocyanine 540 With Hew Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 467 no PDB 4G49 . "Room Temperature X-ray Diffraction Of Cisplatin Binding To Hewl In Aqueous Media After 15 Months Of Crystal Storage" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 468 no PDB 4G4A . "Room Temperature X-ray Diffraction Studies Of Cisplatin Binding To Hewl In Dmso Media After 14 Months Of Crystal Storage" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 469 no PDB 4G4B . "Room Temperature X-ray Diffraction Study Of Cisplatin Binding To Hewl In Dmso Media With Nag After 7 Months Of Crystal Storage" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 470 no PDB 4G4C . "Room Temperature X-ray Diffraction Study Of Carboplatin Binding To Hewl In Dmso Media After 13 Months Of Crystal Storage" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 471 no PDB 4G4H . "100k X-ray Diffraction Study Of Carboplatin Binding To Hewl In Dmso Media After 13 Months Of Crystal Storage" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 472 no PDB 4GCB . "100k X-ray Diffraction Study Of A 6-fold Molar Excess Of A Cisplatin/carboplatin Mixture Binding To Hewl" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 473 no PDB 4GCC . "Room Temperature X-ray Diffraction Study Of A 6-fold Molar Excess Of A Cisplatin/carboplatin Mixture Binding To Hewl, Dataset 1" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 474 no PDB 4GCD . "Room Temperature X-ray Diffraction Study Of A 6-fold Molar Excess Of A Cisplatin/carboplatin Mixture Binding To Hewl, Dataset 2" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 475 no PDB 4GCE . "Room Temperature X-ray Diffraction Study Of A 6-fold Molar Excess Of A Cisplatin/carboplatin Mixture Binding To Hewl, Dataset 3" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 476 no PDB 4GCF . "Room Temperature X-ray Diffraction Study Of A 6-fold Molar Excess Of A Cisplatin/carboplatin Mixture Binding To Hewl, Dataset 4" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 477 no PDB 4GLA . "Obody Nl8 Bound To Hen Egg-white Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 478 no PDB 4GLV . "Obody Am3l09 Bound To Hen Egg-white Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 479 no PDB 4GN3 . "Obody Am1l10 Bound To Hen Egg-white Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 480 no PDB 4GN4 . "Obody Am2ep06 Bound To Hen Egg-white Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 481 no PDB 4GN5 . "Obody Am3l15 Bound To Hen Egg-white Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 482 no PDB 4H1P . "Use Of Europium For Sad Phasing At The Cu K Alpha Wavelength" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 483 no PDB 4H8X . "Radiation Damage Study Of Lysozyme - 0.07 Mgy" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 484 no PDB 4H8Y . "Radiation Damage Study Of Lysozyme- 0.14 Mgy" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 485 no PDB 4H8Z . "Radiation Damage Study Of Lysozyme - 0.21 Mgy" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 486 no PDB 4H90 . "Radiation Damage Study Of Lysozyme - 0.28 Mgy" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 487 no PDB 4H91 . "Radiation Damage Study Of Lysozyme - 0.35 Mgy" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 488 no PDB 4H92 . "Radiation Damage Study Of Lysozyme- 0.42 Mgy" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 489 no PDB 4H93 . "Radiation Damage Study Of Lysozyme - 0.49 Mgy" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 490 no PDB 4H94 . "Radiation Damage In Lysozyme - 0.56 Mgy" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 491 no PDB 4H9A . "Radiation Damage Study Of Lysozyme - 0.63 Mgy" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 492 no PDB 4H9B . "Radiation Damage Study Of Lysozyme - 0.70 Mgy" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 493 no PDB 4H9C . "Radiation Damage Study Of Lysozyme - 0.77 Mgy" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 494 no PDB 4H9E . "Radiation Damage Study Of Lysozyme - 0.84 Mgy" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 495 no PDB 4H9F . "Radiation Damage Study Of Lysozyme - 0.91 Mgy" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 496 no PDB 4H9H . "Radiation Damage Study Of Lysozyme - 0.98 Mgy" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 497 no PDB 4H9I . "Radiation Damage Study Of Lysozyme - 1.05 Mgy" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 498 no PDB 4HP0 . "Crystal Structure Of Hen Egg White Lysozyme In Complex With Gn3-m" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 499 no PDB 4HPI . "Crystal Structure Of Hen Egg White Lysozyme Complex With Gn2-m" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 500 no PDB 4HSF . "Lysozyme With Arginine At 318k" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 501 no PDB 4HTK . "Mitigation Of X-ray Damage In Macromolecular Crystallography By Submicrometer Line Focusing; Total Dose 2.17 X 10e+12 X-ray Pho" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 502 no PDB 4HTN . "Mitigation Of X-ray Damage In Macromolecular Crystallography By Submicrometer Line Focusing; Total Dose 1.32 X 10e+12 X-ray Pho" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 503 no PDB 4HTQ . "Mitigation Of X-ray Damage In Macromolecular Crystallography By Submicrometer Line Focusing; Total Dose 6.70 X 10e+11 X-ray Pho" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 504 no PDB 4HV1 . "Laser-induced Microfragmentation Of Lysozyme Crystals Allows X-ray Nanodiffraction Characterization Of Individual Domains (lb4)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 505 no PDB 4HV2 . "Laser-induced Microfragmentation Of Lysozyme Crystals Allows X-ray Nanodiffraction Characterization Of Individual Domains (lb5)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 506 no PDB 4I8S . "Hen Lysozyme Protein Crystallization Via Standard Hanging Drop Vapor Diffusion" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 507 no PDB 4IAS . "Hew Lysozyme By Langmuir- Blodgett Modified Vapour Diffusion" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 508 no PDB 4IAT . "Hew Lysozyme By Langmuir- Blodgett Modified Vapour Diffusion" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 509 no PDB 4II8 . "Lysozyme With Benzyl Alcohol" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 510 no PDB 4J1A . "X-ray Structure Of The Adduct Between Hen Egg White Lysozyme And Aziru (green Crystal)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 511 no PDB 4J1B . "X-ray Structure Of The Adduct Between Hen Egg White Lysozyme And Aziru (black Crystal)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 512 no PDB 4J7V . "Crystal Structure Of Cross-linked Hen Egg White Lysozyme Soaked With 5mm [ru(benzene)cl2]2" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 513 no PDB 4KXI . "Crystallographic Study Of The Complex Of Ni(ii) Schiff Base Complex And Hew Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 514 no PDB 4LFP . "X-ray Structure Of The Adduct Between Hen Egg White Lysozyme And A Homoleptic Gold(i) Complex With The Saccharynate Ligand" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 515 no PDB 4LFX . "X-ray Structure Of The Adduct Between Hen Egg White Lysozyme And Auoxo6, A Dinuclear Gold(iii) Complex With -dioxo Bridges Link" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 516 no PDB 4LGK . "X-ray Structure Of The Adduct Between Hen Egg White Lysozyme And Au2phen, A Dinuclear Gold(iii) Complex With -dioxo Bridges Lin" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 517 no PDB 4LT0 . "Hewl Co-crystallized With Carboplatin In Non-nacl Conditions: Crystal 1 Processed Using The Eval Software Package" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 518 no PDB 4LT1 . "Hewl Co-crystallised With Carboplatin In Non-nacl Conditions: Crystal 1 Processed Using The Xds Software Package" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 519 no PDB 4LT2 . "Hewl Co-crystallized With Carboplatin In Non-nacl Conditions: Crystal 2 Processed Using The Eval Software Package" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 520 no PDB 4LT3 . "Hewl Co-crystallized With Carboplatin In Non-nacl Conditions: Crystal 2 Processed Using The Xds Software Package" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 521 no PDB 4LYM . "Crystal Structure Of Low Humidity Tetragonal Lysozyme At 2.1-Angstroms Resolution. Variability In Hydration Shell And Its Struc" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 522 no PDB 4LYO . "Cross-Linked Chicken Lysozyme Crystal In Neat Acetonitrile, Then Back-Soaked In Water" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 523 no PDB 4LYT . "Comparison Of Radiation-Induced Decay And Structure Refinement From X-Ray Data Collected From Lysozyme Crystals At Low And Ambi" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 524 no PDB 4LYZ . "Real-Space Refinement Of The Structure Of Hen Egg-White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 525 no PDB 4LZT . "Atomic Resolution Refinement Of Triclinic Hew Lysozyme At 295k" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 526 no PDB 4M4O . "Crystal Structure Of The Aptamer Mine-lysozyme Complex" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 527 no PDB 4M6D . "Crystal Structure Of The Aptamer Minf-lysozyme Complex." . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 528 no PDB 4MR1 . "X-ray Structure Of The Adduct Between Hen Egg White Lysozyme And Cis- Diamminediiodoplatinum(ii)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 529 no PDB 4MWK . "Triclinic Hewl Co-crystallised With Cisplatin, Studied At A Data Collection Temperature Of 150k" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 530 no PDB 4MWM . "Triclinic Hewl Co-crystallised With Cisplatin, Studied At A Data Collection Temperature Of 200k" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 531 no PDB 4MWN . "Triclinic Hewl Co-crystallised With Cisplatin, Studied At A Data Collection Temperature Of 294k" . . . . . 96.99 130 100.00 100.00 5.08e-88 . . . . 4943 1 532 no PDB 4N1C . "Structural Evidence For Antigen Receptor Evolution" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 533 no PDB 4N1E . "Structural Evidence For Antigen Receptor Evolution" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 534 no PDB 4N5R . "Hen Egg-white Lysozyme Phased Using Free-electron Laser Data" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 535 no PDB 4N8Z . "In Situ Lysozyme Crystallized On A Mitegen Micromesh With Benzamidine Ligand" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 536 no PDB 4NEB . "Previously De-ionized Hew Lysozyme Batch Crystallized In 0.5 M Mncl2" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 537 no PDB 4NFV . "Previously De-ionized Hew Lysozyme Batch Crystallized In 1.1 M Mncl2" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 538 no PDB 4NG1 . "Previously De-ionized Hew Lysozyme Batch Crystallized In 1.9 M Cscl" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 539 no PDB 4NG8 . "Dialyzed Hew Lysozyme Batch Crystallized In 1.9 M Cscl And Collected At 100 K." . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 540 no PDB 4NGI . "Previously De-ionized Hew Lysozyme Crystallized In 1.0 M Rbcl And Collected At 125k" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 541 no PDB 4NGJ . "Dialyzed Hew Lysozyme Batch Crystallized In 1.0 M Rbcl And Collected At 100 K" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 542 no PDB 4NGK . "Previously De-ionized Hew Lysozyme Batch Crystallized In 0.2 M Cocl2" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 543 no PDB 4NGL . "Previously De-ionized Hew Lysozyme Batch Crystallized In 0.6 M Cocl2" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 544 no PDB 4NGO . "Previously De-ionized Hew Lysozyme Batch Crystallized In 1.0 M Cocl2" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 545 no PDB 4NGV . "Previously De-ionized Hew Lysozyme Batch Crystallized In 0.5 M Ybcl3" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 546 no PDB 4NGW . "Dialyzed Hew Lysozyme Batch Crystallized In 0.5 M Ybcl3 And Collected At 100 K" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 547 no PDB 4NGY . "Dialyzed Hew Lysozyme Batch Crystallized In 0.75 M Ybcl3 And Collected At 100 K" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 548 no PDB 4NGZ . "Previously De-ionized Hew Lysozyme Crystallized In 0.5 M Ybcl3/30% (v/v) Glycerol And Collected At 125k" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 549 no PDB 4NHI . "Crystal Structure Of Hen Egg-white Lysozyme In Tris Buffer At Ph 7.5 With Magnesium Formate" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 550 no PDB 4NHP . "X-ray Structure Of The Complex Between The Hen Egg White Lysozyme And Pentachlorocarbonyliridate (iii) (4 Days)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 551 no PDB 4NHQ . "X-ray Structure Of The Complex Between Hen Egg White Lysozyme And Pentachlorocarbonyliridate(iii) (5 Days)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 552 no PDB 4NHS . "X-ray Structure Of The Complex Between Hen Egg White Lysozyme And Pentachlorocarbonyliridate(iii) (9 Days)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 553 no PDB 4NHT . "X-ray Structure Of The Complex Between Hen Egg White Lysozyme And Pentachlorocarbonyliridate(iii) (6 Days)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 554 no PDB 4NIJ . "X-ray Structure Of The Complex Between Hen Egg White Lysozyme And Pentachlorocarbonyliridate(iii) (30 Days)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 555 no PDB 4NSF . "Carboplatin Binding To Hewl In Nabr Crystallisation Conditions Studied At An X-ray Wavelength Of 0.9163a" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 556 no PDB 4NSG . "Carboplatin Binding To Hewl In Nabr Crystallisation Conditions Studied At An X-ray Wavelength Of 1.5418a" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 557 no PDB 4NSH . "Carboplatin Binding To Hewl In 0.2m Nh4so4, 0.1m Naac In 25% Peg 4000 At Ph 4.6" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 558 no PDB 4NSI . "Carboplatin Binding To Hewl In 20% Propanol, 20% Peg 4000 At Ph5.6" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 559 no PDB 4NSJ . "Carboplatin Binding To Hewl In 2m Nh4formate, 0.1m Hepes At Ph 7.5" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 560 no PDB 4NWE . "Lysozyme Under 30 Bar Pressure Of Nitrous Oxide" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 561 no PDB 4NWH . "Lysozyme Under 30 Bar Pressure Of Xenon" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 562 no PDB 4NY5 . "X-ray Structure Of The Adduct Formed Between Hen Egg White Lysozyme And Nami-a" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 563 no PDB 4O34 . "Room Temperature Macromolecular Serial Crystallography Using Synchrotron Radiation" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 564 no PDB 4OOO . "X-ray Structure Of The Lysozyme Derivative Of Tetrakis(acetato) Chlorido Diruthenium(ii,iii) Complex" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 565 no PDB 4OOT . "X-ray Structure Of The Protein-gold Adduct Formed Upon Reaction Of Aubipic With Hen Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 566 no PDB 4OW9 . "Cisplatin Binding To Hewl Under Sodium Iodide Crystallisation Conditions" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 567 no PDB 4OWA . "Carboplatin Binding To Hewl Under Sodium Iodide Crystallisation Conditions" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 568 no PDB 4OWB . "Cisplatin Binding To Hewl Under Sodium Bromide Crystallisation Conditions" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 569 no PDB 4OWC . "Pti6 Binding To Hewl" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 570 no PDB 4OWE . "Ptcl6 Binding To Hewl" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 571 no PDB 4OWH . "Ptbr6 Binding To Hewl" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 572 no PDB 4OXE . "Carboplatin Binding To Triclinic Hewl Studied At A Data Collection Temperature Of 200k" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 573 no PDB 4P2E . "Acoustic Transfer Of Protein Crystals From Agar Pedestals To Micromeshes For High Throughput Screening Of Heavy Atom Derivative" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 574 no PDB 4PHI . "Crystal Structure Of Hewl With Hexatungstotellurate(vi)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 575 no PDB 4PPO . "First Crystal Structure For An Oxaliplatin-protein Complex" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 576 no PDB 4PRQ . "Crystal Structure Of Hen Egg-white Lysozyme In Complex With Sclx4 At 1.72 A Resolution" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 577 no PDB 4QEQ . "High Resolution Structure Of Egg White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 578 no PDB 4QGZ . "X-ray Structure Of The Adduct Formed Between Hen Egg White Lysozyme And Trans-dimethylamine Methylamine Dichlorido Platinum(ii)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 579 no PDB 4QY9 . "X-ray Structure Of The Adduct Between Hen Egg White Lysozyme And Auoxo3, A Cytotoxic Gold(iii) Compound" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 580 no PDB 4RDS . "Lysozyme Crystallized With Red Food Coloring Dye" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 581 no PDB 4TUN . "Crystal Structure Of Chicken Egg White Lysozyme Adduct With Organophosphorus Pesticide Monochrotophos" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 582 no PDB 4TWS . "Gadolinium Derivative Of Tetragonal Hen Egg-whote Lysozyme At 1.45 A Resolution" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 583 no PDB 4UWN . "Lysozyme Soaked With A Ruthenium Based Corm With A Methione Oxide Ligand (complex 6b)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 584 no PDB 4UWU . "Lysozyme Soaked With A Ruthenium Based Corm With A Pyridine Ligand (complex 7)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 585 no PDB 4UWV . "Lysozyme Soaked With A Ruthenium Based Corm With A Pyridine Ligand (complex 8)" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 586 no PDB 4W94 . "Crystal Structure Of Cross-linked Tetragonal Hen Egg White Lysozyme Soaked With 5mm [ru(co)3cl2]2" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 587 no PDB 4W96 . "Crystal Structure Of Cross-linked Tetragonal Hen Egg White Lysozyme Soaked With 5mm [ru(co)3cl2]2 Followed By The Reaction In D" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 588 no PDB 4XAD . "Crystal Structure Of Hen Egg White Lysozyme In Complex With Galf- Glcnac" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 589 no PDB 5LYM . "Studies Of Monoclinic Hen Egg White Lysozyme. Iv. X-Ray Refinement At 1.8 Angstrom Resolution And A Comparison Of The Variable " . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 590 no PDB 5LYT . "Comparison Of Radiation-Induced Decay And Structure Refinement From X-Ray Data Collected From Lysozyme Crystals At Low And Ambi" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 591 no PDB 5LYZ . "Real-Space Refinement Of The Structure Of Hen Egg-White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 592 no PDB 6LYT . "Comparison Of Radiation-Induced Decay And Structure Refinement From X-Ray Data Collected From Lysozyme Crystals At Low And Ambi" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 593 no PDB 6LYZ . "Real-Space Refinement Of The Structure Of Hen Egg-White Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 594 no PDB 7LYZ . "Protein Model Building By The Use Of A Constrained- Restrained Least-Squares Procedure" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 595 no PDB 8LYZ . "An X-Ray Study Of The Structure And Binding Properties Of Iodine-Inactivated Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 596 no PDB 9LYZ . "X-Ray Crystallography Of The Binding Of The Bacterial Cell Wall Trisaccharide Nam-Nag-Nam To Lysozyme" . . . . . 96.99 129 100.00 100.00 5.98e-88 . . . . 4943 1 597 no EMBL CAA23711 . "unnamed protein product [Gallus gallus]" . . . . . 96.99 147 98.45 99.22 5.87e-87 . . . . 4943 1 598 no GB AAA48943 . "lysozyme ( [Gallus gallus]" . . . . . 96.99 147 100.00 100.00 3.59e-88 . . . . 4943 1 599 no GB AAL69327 . "egg white lysozyme [Gallus gallus]" . . . . . 96.99 147 100.00 100.00 3.59e-88 . . . . 4943 1 600 no GB ACL81571 . "lysozyme [Gallus gallus]" . . . . . 96.99 147 99.22 99.22 6.69e-87 . . . . 4943 1 601 no GB ACL81572 . "lysozyme [Gallus gallus]" . . . . . 96.99 147 99.22 99.22 6.69e-87 . . . . 4943 1 602 no GB ACL81573 . "lysozyme [Gallus gallus]" . . . . . 96.99 147 98.45 98.45 2.22e-86 . . . . 4943 1 603 no PRF 630460A . "lysozyme [Gallus gallus]" . . . . . 96.99 129 99.22 100.00 1.92e-87 . . . . 4943 1 604 no REF NP_990612 . "lysozyme C precursor [Gallus gallus]" . . . . . 96.99 147 98.45 99.22 5.87e-87 . . . . 4943 1 605 no SP P00698 . "RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; AltName: Full=Allergen Gal d IV; AltName: Allergen=Gal d" . . . . . 96.99 147 100.00 100.00 3.59e-88 . . . . 4943 1 606 no SP P00699 . "RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C [Callipepla californica]" . . . . . 96.99 129 96.90 99.22 3.33e-86 . . . . 4943 1 607 no SP P00700 . "RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C [Colinus virginianus]" . . . . . 96.99 129 96.90 100.00 1.50e-86 . . . . 4943 1 608 no SP Q7LZP9 . "RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C [Lophophorus impejanus]" . . . . . 96.99 129 96.90 97.67 1.69e-84 . . . . 4943 1 609 no SP Q7LZQ0 . "RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C [Catreus wallichii]" . . . . . 96.99 129 96.90 97.67 1.69e-84 . . . . 4943 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Chicken Egg White Lysozyme' common 4943 1 Lysozyme abbreviation 4943 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 . LYS . 4943 1 2 . VAL . 4943 1 3 . PHE . 4943 1 4 . GLY . 4943 1 5 . ARG . 4943 1 6 . CYS . 4943 1 7 . GLU . 4943 1 8 . LEU . 4943 1 9 . ALA . 4943 1 10 . ALA . 4943 1 11 . ALA . 4943 1 12 . MET . 4943 1 13 . LYS . 4943 1 14 . ARG . 4943 1 15 . HIS . 4943 1 16 . GLY . 4943 1 17 . LEU . 4943 1 18 . ASP . 4943 1 19 . ASN . 4943 1 20 . TYR . 4943 1 21 . ARG . 4943 1 22 . GLY . 4943 1 23 . TYR . 4943 1 24 . SER . 4943 1 25 . LEU . 4943 1 26 . GLY . 4943 1 27 . ASN . 4943 1 28 . TRP . 4943 1 29 . VAL . 4943 1 30 . CYS . 4943 1 31 . ALA . 4943 1 32 . ALA . 4943 1 33 . LYS . 4943 1 34 . PHE . 4943 1 35 . GLU . 4943 1 36 . SER . 4943 1 37 . ASN . 4943 1 38 . PHE . 4943 1 39 . ASN . 4943 1 40 . THR . 4943 1 41 . GLN . 4943 1 42 . ALA . 4943 1 43 . THR . 4943 1 44 . ASN . 4943 1 45 . ARG . 4943 1 46 . ASN . 4943 1 47 . THR . 4943 1 48 . ASP . 4943 1 49 . GLY . 4943 1 50 . SER . 4943 1 51 . THR . 4943 1 52 . ASP . 4943 1 53 . TYR . 4943 1 54 . GLY . 4943 1 55 . ILE . 4943 1 56 . LEU . 4943 1 57 . GLN . 4943 1 58 . ILE . 4943 1 59 . ASN . 4943 1 60 . SER . 4943 1 61 . ARG . 4943 1 62 . TRP . 4943 1 63 . TRP . 4943 1 64 . CYS . 4943 1 65 . ASN . 4943 1 66 . ASP . 4943 1 67 . GLY . 4943 1 68 . ARG . 4943 1 69 . THR . 4943 1 70 . PRO . 4943 1 71 . GLY . 4943 1 72 . SER . 4943 1 73 . ARG . 4943 1 74 . ASN . 4943 1 75 . LEU . 4943 1 76 . CYS . 4943 1 77 . ASN . 4943 1 78 . ILE . 4943 1 79 . PRO . 4943 1 80 . CYS . 4943 1 81 . SER . 4943 1 82 . ALA . 4943 1 83 . LEU . 4943 1 84 . LEU . 4943 1 85 . SER . 4943 1 86 . SER . 4943 1 87 . ASP . 4943 1 88 . ILE . 4943 1 89 . THR . 4943 1 90 . ALA . 4943 1 91 . SER . 4943 1 92 . VAL . 4943 1 93 . ASN . 4943 1 94 . CYS . 4943 1 95 . ALA . 4943 1 96 . LYS . 4943 1 97 . LYS . 4943 1 98 . ILE . 4943 1 99 . VAL . 4943 1 100 . SER . 4943 1 101 . ASP . 4943 1 102 . GLY . 4943 1 103 . ASN . 4943 1 104 . GLY . 4943 1 105 . MET . 4943 1 106 . ASN . 4943 1 107 . ALA . 4943 1 108 . TRP . 4943 1 109 . VAL . 4943 1 110 . ALA . 4943 1 111 . TRP . 4943 1 112 . ARG . 4943 1 113 . ASN . 4943 1 114 . ARG . 4943 1 115 . CYS . 4943 1 116 . LYS . 4943 1 117 . GLY . 4943 1 118 . THR . 4943 1 119 . ASP . 4943 1 120 . VAL . 4943 1 121 . GLN . 4943 1 122 . ALA . 4943 1 123 . TRP . 4943 1 124 . ILE . 4943 1 125 . ARG . 4943 1 126 . GLY . 4943 1 127 . CYS . 4943 1 128 . ARG . 4943 1 129 . LEU . 4943 1 130 . ASP . 4943 1 131 . ARG . 4943 1 132 . SER . 4943 1 133 . ARG . 4943 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 . LYS 1 1 4943 1 . VAL 2 2 4943 1 . PHE 3 3 4943 1 . GLY 4 4 4943 1 . ARG 5 5 4943 1 . CYS 6 6 4943 1 . GLU 7 7 4943 1 . LEU 8 8 4943 1 . ALA 9 9 4943 1 . ALA 10 10 4943 1 . ALA 11 11 4943 1 . MET 12 12 4943 1 . LYS 13 13 4943 1 . ARG 14 14 4943 1 . HIS 15 15 4943 1 . GLY 16 16 4943 1 . LEU 17 17 4943 1 . ASP 18 18 4943 1 . ASN 19 19 4943 1 . TYR 20 20 4943 1 . ARG 21 21 4943 1 . GLY 22 22 4943 1 . TYR 23 23 4943 1 . SER 24 24 4943 1 . LEU 25 25 4943 1 . GLY 26 26 4943 1 . ASN 27 27 4943 1 . TRP 28 28 4943 1 . VAL 29 29 4943 1 . CYS 30 30 4943 1 . ALA 31 31 4943 1 . ALA 32 32 4943 1 . LYS 33 33 4943 1 . PHE 34 34 4943 1 . GLU 35 35 4943 1 . SER 36 36 4943 1 . ASN 37 37 4943 1 . PHE 38 38 4943 1 . ASN 39 39 4943 1 . THR 40 40 4943 1 . GLN 41 41 4943 1 . ALA 42 42 4943 1 . THR 43 43 4943 1 . ASN 44 44 4943 1 . ARG 45 45 4943 1 . ASN 46 46 4943 1 . THR 47 47 4943 1 . ASP 48 48 4943 1 . GLY 49 49 4943 1 . SER 50 50 4943 1 . THR 51 51 4943 1 . ASP 52 52 4943 1 . TYR 53 53 4943 1 . GLY 54 54 4943 1 . ILE 55 55 4943 1 . LEU 56 56 4943 1 . GLN 57 57 4943 1 . ILE 58 58 4943 1 . ASN 59 59 4943 1 . SER 60 60 4943 1 . ARG 61 61 4943 1 . TRP 62 62 4943 1 . TRP 63 63 4943 1 . CYS 64 64 4943 1 . ASN 65 65 4943 1 . ASP 66 66 4943 1 . GLY 67 67 4943 1 . ARG 68 68 4943 1 . THR 69 69 4943 1 . PRO 70 70 4943 1 . GLY 71 71 4943 1 . SER 72 72 4943 1 . ARG 73 73 4943 1 . ASN 74 74 4943 1 . LEU 75 75 4943 1 . CYS 76 76 4943 1 . ASN 77 77 4943 1 . ILE 78 78 4943 1 . PRO 79 79 4943 1 . CYS 80 80 4943 1 . SER 81 81 4943 1 . ALA 82 82 4943 1 . LEU 83 83 4943 1 . LEU 84 84 4943 1 . SER 85 85 4943 1 . SER 86 86 4943 1 . ASP 87 87 4943 1 . ILE 88 88 4943 1 . THR 89 89 4943 1 . ALA 90 90 4943 1 . SER 91 91 4943 1 . VAL 92 92 4943 1 . ASN 93 93 4943 1 . CYS 94 94 4943 1 . ALA 95 95 4943 1 . LYS 96 96 4943 1 . LYS 97 97 4943 1 . ILE 98 98 4943 1 . VAL 99 99 4943 1 . SER 100 100 4943 1 . ASP 101 101 4943 1 . GLY 102 102 4943 1 . ASN 103 103 4943 1 . GLY 104 104 4943 1 . MET 105 105 4943 1 . ASN 106 106 4943 1 . ALA 107 107 4943 1 . TRP 108 108 4943 1 . VAL 109 109 4943 1 . ALA 110 110 4943 1 . TRP 111 111 4943 1 . ARG 112 112 4943 1 . ASN 113 113 4943 1 . ARG 114 114 4943 1 . CYS 115 115 4943 1 . LYS 116 116 4943 1 . GLY 117 117 4943 1 . THR 118 118 4943 1 . ASP 119 119 4943 1 . VAL 120 120 4943 1 . GLN 121 121 4943 1 . ALA 122 122 4943 1 . TRP 123 123 4943 1 . ILE 124 124 4943 1 . ARG 125 125 4943 1 . GLY 126 126 4943 1 . CYS 127 127 4943 1 . ARG 128 128 4943 1 . LEU 129 129 4943 1 . ASP 130 130 4943 1 . ARG 131 131 4943 1 . SER 132 132 4943 1 . ARG 133 133 4943 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 4943 _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 $Lysozyme . 9031 organism . 'Gallus gallus' Chicken . . Eukaryota Metazoa Gallus gallus . . . 'egg white' . . . . . . . . . . . . . . . . . 4943 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 4943 _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 $Lysozyme . vendor . . . . . . . . . . . . . . . . . . . . . . . . Sigma . 'Lot nr. 57H7045' . . 4943 1 2 1 $Lysozyme . vendor . . . . . . . . . . . . . . . . . . . . . . . . Seikagaku . 'Lot nr. E94Z06' . . 4943 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_A _Sample.Sf_category sample _Sample.Sf_framecode sample_A _Sample.Entry_ID 4943 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details 'Lysozyme marketed by Sigma' _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 'Chicken Egg White Lysozyme' . . . 1 $Lysozyme . . 10 . . mM . . . . 4943 1 stop_ save_ save_sample_B _Sample.Sf_category sample _Sample.Sf_framecode sample_B _Sample.Entry_ID 4943 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details 'Lysozyme marketed by Seikagaku' _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 'Chicken Egg White Lysozyme' . . . 1 $Lysozyme . . 10 . . mM . . . . 4943 2 stop_ save_ ####################### # Sample conditions # ####################### save_cond _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode cond _Sample_condition_list.Entry_ID 4943 _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 n/a 4943 1 temperature 308 1 K 4943 1 stop_ save_ ############################ # Computer software used # ############################ save_nmrpipe _Software.Sf_category software _Software.Sf_framecode nmrpipe _Software.Entry_ID 4943 _Software.ID 1 _Software.Name nmrpipe _Software.Version 1.7 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data processing' 4943 1 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 3 $ref_2 4943 1 stop_ save_ save_XEasy _Software.Sf_category software _Software.Sf_framecode XEasy _Software.Entry_ID 4943 _Software.ID 2 _Software.Name XEasy _Software.Version 1.3.11 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'peak assignment' 4943 2 'sequential assignment' 4943 2 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 4 $ref_3 4943 2 stop_ 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 4943 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model 'Unity Plus' _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4943 _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 Varian 'Unity Plus' . 500 . . . 4943 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 4943 _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 '1H-1H TOCSY' . . . . . . . . . . . . . . . . 1 $cond . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4943 1 2 '1H-1H NOESY' . . . . . . . . . . . . . . . . 1 $cond . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4943 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 4943 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name '1H-1H TOCSY' _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 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _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 4943 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name '1H-1H 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 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _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 4943 _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 internal direct 1.0 . . . . . . . . . 4943 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_Sigma _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode Sigma _Assigned_chem_shift_list.Entry_ID 4943 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $cond _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 '1H-1H TOCSY' 1 $sample_A . 4943 1 2 '1H-1H NOESY' 1 $sample_A . 4943 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 VAL H H 1 8.96 0.01 . 1 . . . . . . . . 4943 1 2 . 1 1 2 2 VAL HA H 1 4.98 0.01 . 1 . . . . . . . . 4943 1 3 . 1 1 2 2 VAL HB H 1 2.02 0.01 . 1 . . . . . . . . 4943 1 4 . 1 1 3 3 PHE H H 1 8.89 0.01 . 1 . . . . . . . . 4943 1 5 . 1 1 3 3 PHE HA H 1 4.23 0.01 . 1 . . . . . . . . 4943 1 6 . 1 1 3 3 PHE HB2 H 1 3.18 0.01 . 2 . . . . . . . . 4943 1 7 . 1 1 3 3 PHE HB3 H 1 2.69 0.01 . 2 . . . . . . . . 4943 1 8 . 1 1 4 4 GLY H H 1 8.51 0.01 . 1 . . . . . . . . 4943 1 9 . 1 1 4 4 GLY HA2 H 1 4.28 0.01 . 2 . . . . . . . . 4943 1 10 . 1 1 4 4 GLY HA3 H 1 3.89 0.01 . 2 . . . . . . . . 4943 1 11 . 1 1 5 5 ARG H H 1 8.57 0.01 . 1 . . . . . . . . 4943 1 12 . 1 1 5 5 ARG HA H 1 3.39 0.01 . 1 . . . . . . . . 4943 1 13 . 1 1 6 6 CYS H H 1 8.61 0.01 . 1 . . . . . . . . 4943 1 14 . 1 1 6 6 CYS HA H 1 4.74 0.01 . 1 . . . . . . . . 4943 1 15 . 1 1 6 6 CYS HB2 H 1 3.24 0.01 . 2 . . . . . . . . 4943 1 16 . 1 1 6 6 CYS HB3 H 1 2.81 0.01 . 2 . . . . . . . . 4943 1 17 . 1 1 7 7 GLU H H 1 8.13 0.01 . 1 . . . . . . . . 4943 1 18 . 1 1 7 7 GLU HA H 1 4.12 0.01 . 1 . . . . . . . . 4943 1 19 . 1 1 7 7 GLU HB2 H 1 2.33 0.01 . 2 . . . . . . . . 4943 1 20 . 1 1 7 7 GLU HB3 H 1 2.19 0.01 . 2 . . . . . . . . 4943 1 21 . 1 1 8 8 LEU H H 1 8.63 0.01 . 1 . . . . . . . . 4943 1 22 . 1 1 8 8 LEU HA H 1 3.77 0.01 . 1 . . . . . . . . 4943 1 23 . 1 1 8 8 LEU HB2 H 1 1.58 0.01 . 2 . . . . . . . . 4943 1 24 . 1 1 8 8 LEU HB3 H 1 0.93 0.01 . 2 . . . . . . . . 4943 1 25 . 1 1 9 9 ALA H H 1 8.40 0.01 . 1 . . . . . . . . 4943 1 26 . 1 1 9 9 ALA HA H 1 3.61 0.01 . 1 . . . . . . . . 4943 1 27 . 1 1 9 9 ALA HB1 H 1 1.57 0.01 . 1 . . . . . . . . 4943 1 28 . 1 1 9 9 ALA HB2 H 1 1.57 0.01 . 1 . . . . . . . . 4943 1 29 . 1 1 9 9 ALA HB3 H 1 1.57 0.01 . 1 . . . . . . . . 4943 1 30 . 1 1 10 10 ALA H H 1 8.17 0.01 . 1 . . . . . . . . 4943 1 31 . 1 1 10 10 ALA HA H 1 3.99 0.01 . 1 . . . . . . . . 4943 1 32 . 1 1 10 10 ALA HB1 H 1 1.56 0.01 . 1 . . . . . . . . 4943 1 33 . 1 1 10 10 ALA HB2 H 1 1.56 0.01 . 1 . . . . . . . . 4943 1 34 . 1 1 10 10 ALA HB3 H 1 1.56 0.01 . 1 . . . . . . . . 4943 1 35 . 1 1 11 11 ALA H H 1 7.78 0.01 . 1 . . . . . . . . 4943 1 36 . 1 1 11 11 ALA HA H 1 4.29 0.01 . 1 . . . . . . . . 4943 1 37 . 1 1 11 11 ALA HB1 H 1 1.53 0.01 . 1 . . . . . . . . 4943 1 38 . 1 1 11 11 ALA HB2 H 1 1.53 0.01 . 1 . . . . . . . . 4943 1 39 . 1 1 11 11 ALA HB3 H 1 1.53 0.01 . 1 . . . . . . . . 4943 1 40 . 1 1 12 12 MET H H 1 9.10 0.01 . 1 . . . . . . . . 4943 1 41 . 1 1 12 12 MET HA H 1 3.47 0.01 . 1 . . . . . . . . 4943 1 42 . 1 1 12 12 MET HB2 H 1 1.57 0.01 . 2 . . . . . . . . 4943 1 43 . 1 1 12 12 MET HB3 H 1 1.89 0.01 . 2 . . . . . . . . 4943 1 44 . 1 1 13 13 LYS H H 1 8.54 0.01 . 1 . . . . . . . . 4943 1 45 . 1 1 13 13 LYS HA H 1 3.98 0.01 . 1 . . . . . . . . 4943 1 46 . 1 1 13 13 LYS HB2 H 1 2.21 0.01 . 2 . . . . . . . . 4943 1 47 . 1 1 13 13 LYS HB3 H 1 1.95 0.01 . 2 . . . . . . . . 4943 1 48 . 1 1 14 14 ARG H H 1 8.23 0.01 . 1 . . . . . . . . 4943 1 49 . 1 1 14 14 ARG HA H 1 4.14 0.01 . 1 . . . . . . . . 4943 1 50 . 1 1 14 14 ARG HB2 H 1 1.97 0.01 . 2 . . . . . . . . 4943 1 51 . 1 1 14 14 ARG HB3 H 1 1.84 0.01 . 2 . . . . . . . . 4943 1 52 . 1 1 15 15 HIS H H 1 7.33 0.01 . 1 . . . . . . . . 4943 1 53 . 1 1 15 15 HIS HA H 1 4.54 0.01 . 1 . . . . . . . . 4943 1 54 . 1 1 15 15 HIS HB2 H 1 3.71 0.01 . 2 . . . . . . . . 4943 1 55 . 1 1 15 15 HIS HB3 H 1 2.58 0.01 . 2 . . . . . . . . 4943 1 56 . 1 1 16 16 GLY H H 1 7.63 0.01 . 1 . . . . . . . . 4943 1 57 . 1 1 16 16 GLY HA2 H 1 4.12 0.01 . 2 . . . . . . . . 4943 1 58 . 1 1 16 16 GLY HA3 H 1 3.92 0.01 . 2 . . . . . . . . 4943 1 59 . 1 1 17 17 LEU H H 1 7.14 0.01 . 1 . . . . . . . . 4943 1 60 . 1 1 17 17 LEU HA H 1 3.94 0.01 . 1 . . . . . . . . 4943 1 61 . 1 1 17 17 LEU HB2 H 1 0.72 0.01 . 2 . . . . . . . . 4943 1 62 . 1 1 17 17 LEU HB3 H 1 0.28 0.01 . 2 . . . . . . . . 4943 1 63 . 1 1 18 18 ASP H H 1 8.72 0.01 . 1 . . . . . . . . 4943 1 64 . 1 1 18 18 ASP HA H 1 4.27 0.01 . 1 . . . . . . . . 4943 1 65 . 1 1 18 18 ASP HB2 H 1 3.02 0.01 . 2 . . . . . . . . 4943 1 66 . 1 1 18 18 ASP HB3 H 1 2.39 0.01 . 2 . . . . . . . . 4943 1 67 . 1 1 19 19 ASN H H 1 8.37 0.01 . 1 . . . . . . . . 4943 1 68 . 1 1 19 19 ASN HA H 1 3.98 0.01 . 1 . . . . . . . . 4943 1 69 . 1 1 19 19 ASN HB2 H 1 3.06 0.01 . 2 . . . . . . . . 4943 1 70 . 1 1 19 19 ASN HB3 H 1 2.85 0.01 . 2 . . . . . . . . 4943 1 71 . 1 1 20 20 TYR H H 1 8.10 0.01 . 1 . . . . . . . . 4943 1 72 . 1 1 20 20 TYR HA H 1 4.25 0.01 . 1 . . . . . . . . 4943 1 73 . 1 1 20 20 TYR HB2 H 1 3.23 0.01 . 2 . . . . . . . . 4943 1 74 . 1 1 20 20 TYR HB3 H 1 3.06 0.01 . 2 . . . . . . . . 4943 1 75 . 1 1 21 21 ARG H H 1 8.94 0.01 . 1 . . . . . . . . 4943 1 76 . 1 1 21 21 ARG HA H 1 3.64 0.01 . 1 . . . . . . . . 4943 1 77 . 1 1 21 21 ARG HB2 H 1 2.24 0.01 . 2 . . . . . . . . 4943 1 78 . 1 1 21 21 ARG HB3 H 1 1.88 0.01 . 2 . . . . . . . . 4943 1 79 . 1 1 22 22 GLY H H 1 7.54 0.01 . 1 . . . . . . . . 4943 1 80 . 1 1 22 22 GLY HA2 H 1 3.87 0.01 . 2 . . . . . . . . 4943 1 81 . 1 1 22 22 GLY HA3 H 1 3.50 0.01 . 2 . . . . . . . . 4943 1 82 . 1 1 23 23 TYR H H 1 7.67 0.01 . 1 . . . . . . . . 4943 1 83 . 1 1 23 23 TYR HA H 1 4.57 0.01 . 1 . . . . . . . . 4943 1 84 . 1 1 23 23 TYR HB2 H 1 3.31 0.01 . 2 . . . . . . . . 4943 1 85 . 1 1 23 23 TYR HB3 H 1 2.50 0.01 . 2 . . . . . . . . 4943 1 86 . 1 1 24 24 SER H H 1 8.99 0.01 . 1 . . . . . . . . 4943 1 87 . 1 1 24 24 SER HA H 1 4.54 0.01 . 1 . . . . . . . . 4943 1 88 . 1 1 25 25 LEU H H 1 9.03 0.01 . 1 . . . . . . . . 4943 1 89 . 1 1 25 25 LEU HA H 1 4.41 0.01 . 1 . . . . . . . . 4943 1 90 . 1 1 26 26 GLY H H 1 9.59 0.01 . 1 . . . . . . . . 4943 1 91 . 1 1 26 26 GLY HA2 H 1 4.20 0.01 . 2 . . . . . . . . 4943 1 92 . 1 1 26 26 GLY HA3 H 1 3.68 0.01 . 2 . . . . . . . . 4943 1 93 . 1 1 27 27 ASN H H 1 8.19 0.01 . 1 . . . . . . . . 4943 1 94 . 1 1 27 27 ASN HA H 1 4.21 0.01 . 1 . . . . . . . . 4943 1 95 . 1 1 27 27 ASN HB2 H 1 2.89 0.01 . 2 . . . . . . . . 4943 1 96 . 1 1 27 27 ASN HB3 H 1 2.33 0.01 . 2 . . . . . . . . 4943 1 97 . 1 1 28 28 TRP H H 1 7.19 0.01 . 1 . . . . . . . . 4943 1 98 . 1 1 28 28 TRP HA H 1 3.77 0.01 . 1 . . . . . . . . 4943 1 99 . 1 1 28 28 TRP HB2 H 1 3.27 0.01 . 2 . . . . . . . . 4943 1 100 . 1 1 28 28 TRP HB3 H 1 3.21 0.01 . 2 . . . . . . . . 4943 1 101 . 1 1 29 29 VAL H H 1 7.56 0.01 . 1 . . . . . . . . 4943 1 102 . 1 1 29 29 VAL HA H 1 3.45 0.01 . 1 . . . . . . . . 4943 1 103 . 1 1 29 29 VAL HB H 1 1.95 0.01 . 1 . . . . . . . . 4943 1 104 . 1 1 30 30 CYS H H 1 8.02 0.01 . 1 . . . . . . . . 4943 1 105 . 1 1 30 30 CYS HA H 1 2.51 0.01 . 1 . . . . . . . . 4943 1 106 . 1 1 30 30 CYS HB2 H 1 2.92 0.01 . 2 . . . . . . . . 4943 1 107 . 1 1 30 30 CYS HB3 H 1 2.63 0.01 . 2 . . . . . . . . 4943 1 108 . 1 1 31 31 ALA H H 1 8.12 0.01 . 1 . . . . . . . . 4943 1 109 . 1 1 31 31 ALA HA H 1 3.72 0.01 . 1 . . . . . . . . 4943 1 110 . 1 1 31 31 ALA HB1 H 1 1.01 0.01 . 1 . . . . . . . . 4943 1 111 . 1 1 31 31 ALA HB2 H 1 1.01 0.01 . 1 . . . . . . . . 4943 1 112 . 1 1 31 31 ALA HB3 H 1 1.01 0.01 . 1 . . . . . . . . 4943 1 113 . 1 1 32 32 ALA H H 1 7.59 0.01 . 1 . . . . . . . . 4943 1 114 . 1 1 32 32 ALA HA H 1 4.03 0.01 . 1 . . . . . . . . 4943 1 115 . 1 1 32 32 ALA HB1 H 1 1.32 0.01 . 1 . . . . . . . . 4943 1 116 . 1 1 32 32 ALA HB2 H 1 1.32 0.01 . 1 . . . . . . . . 4943 1 117 . 1 1 32 32 ALA HB3 H 1 1.32 0.01 . 1 . . . . . . . . 4943 1 118 . 1 1 33 33 LYS H H 1 7.95 0.01 . 1 . . . . . . . . 4943 1 119 . 1 1 33 33 LYS HA H 1 2.58 0.01 . 1 . . . . . . . . 4943 1 120 . 1 1 34 34 PHE H H 1 7.35 0.01 . 1 . . . . . . . . 4943 1 121 . 1 1 34 34 PHE HA H 1 4.32 0.01 . 1 . . . . . . . . 4943 1 122 . 1 1 34 34 PHE HB2 H 1 3.19 0.01 . 2 . . . . . . . . 4943 1 123 . 1 1 34 34 PHE HB3 H 1 2.29 0.01 . 2 . . . . . . . . 4943 1 124 . 1 1 35 35 GLU H H 1 8.59 0.01 . 1 . . . . . . . . 4943 1 125 . 1 1 35 35 GLU HA H 1 4.46 0.01 . 1 . . . . . . . . 4943 1 126 . 1 1 35 35 GLU HB2 H 1 2.03 0.01 . 2 . . . . . . . . 4943 1 127 . 1 1 35 35 GLU HB3 H 1 1.77 0.01 . 2 . . . . . . . . 4943 1 128 . 1 1 36 36 SER H H 1 7.93 0.01 . 1 . . . . . . . . 4943 1 129 . 1 1 36 36 SER HA H 1 4.58 0.01 . 1 . . . . . . . . 4943 1 130 . 1 1 36 36 SER HB2 H 1 4.48 0.01 . 2 . . . . . . . . 4943 1 131 . 1 1 36 36 SER HB3 H 1 3.56 0.01 . 2 . . . . . . . . 4943 1 132 . 1 1 37 37 ASN H H 1 8.14 0.01 . 1 . . . . . . . . 4943 1 133 . 1 1 37 37 ASN HA H 1 4.49 0.01 . 1 . . . . . . . . 4943 1 134 . 1 1 37 37 ASN HB2 H 1 3.32 0.01 . 2 . . . . . . . . 4943 1 135 . 1 1 37 37 ASN HB3 H 1 2.49 0.01 . 2 . . . . . . . . 4943 1 136 . 1 1 38 38 PHE H H 1 7.36 0.01 . 1 . . . . . . . . 4943 1 137 . 1 1 38 38 PHE HA H 1 3.87 0.01 . 1 . . . . . . . . 4943 1 138 . 1 1 38 38 PHE HB3 H 1 3.63 0.01 . 2 . . . . . . . . 4943 1 139 . 1 1 39 39 ASN H H 1 7.41 0.01 . 1 . . . . . . . . 4943 1 140 . 1 1 39 39 ASN HA H 1 5.42 0.01 . 1 . . . . . . . . 4943 1 141 . 1 1 39 39 ASN HB2 H 1 3.48 0.01 . 2 . . . . . . . . 4943 1 142 . 1 1 39 39 ASN HB3 H 1 2.85 0.01 . 2 . . . . . . . . 4943 1 143 . 1 1 40 40 THR H H 1 9.37 0.01 . 1 . . . . . . . . 4943 1 144 . 1 1 40 40 THR HA H 1 4.07 0.01 . 1 . . . . . . . . 4943 1 145 . 1 1 40 40 THR HB H 1 4.68 0.01 . 1 . . . . . . . . 4943 1 146 . 1 1 41 41 GLN H H 1 7.91 0.01 . 1 . . . . . . . . 4943 1 147 . 1 1 41 41 GLN HA H 1 4.45 0.01 . 1 . . . . . . . . 4943 1 148 . 1 1 41 41 GLN HB2 H 1 2.46 0.01 . 2 . . . . . . . . 4943 1 149 . 1 1 41 41 GLN HB3 H 1 1.90 0.01 . 2 . . . . . . . . 4943 1 150 . 1 1 42 42 ALA H H 1 6.85 0.01 . 1 . . . . . . . . 4943 1 151 . 1 1 42 42 ALA HA H 1 4.15 0.01 . 1 . . . . . . . . 4943 1 152 . 1 1 42 42 ALA HB1 H 1 1.36 0.01 . 1 . . . . . . . . 4943 1 153 . 1 1 42 42 ALA HB2 H 1 1.36 0.01 . 1 . . . . . . . . 4943 1 154 . 1 1 42 42 ALA HB3 H 1 1.36 0.01 . 1 . . . . . . . . 4943 1 155 . 1 1 43 43 THR H H 1 8.26 0.01 . 1 . . . . . . . . 4943 1 156 . 1 1 43 43 THR HA H 1 5.16 0.01 . 1 . . . . . . . . 4943 1 157 . 1 1 43 43 THR HB H 1 3.73 0.01 . 1 . . . . . . . . 4943 1 158 . 1 1 44 44 ASN H H 1 8.16 0.01 . 1 . . . . . . . . 4943 1 159 . 1 1 44 44 ASN HA H 1 5.01 0.01 . 1 . . . . . . . . 4943 1 160 . 1 1 44 44 ASN HB2 H 1 2.73 0.01 . 1 . . . . . . . . 4943 1 161 . 1 1 44 44 ASN HB3 H 1 2.73 0.01 . 1 . . . . . . . . 4943 1 162 . 1 1 45 45 ARG H H 1 8.83 0.01 . 1 . . . . . . . . 4943 1 163 . 1 1 45 45 ARG HA H 1 4.51 0.01 . 1 . . . . . . . . 4943 1 164 . 1 1 45 45 ARG HB2 H 1 1.71 0.01 . 2 . . . . . . . . 4943 1 165 . 1 1 45 45 ARG HB3 H 1 1.67 0.01 . 2 . . . . . . . . 4943 1 166 . 1 1 46 46 ASN H H 1 8.89 0.01 . 1 . . . . . . . . 4943 1 167 . 1 1 46 46 ASN HA H 1 5.13 0.01 . 1 . . . . . . . . 4943 1 168 . 1 1 46 46 ASN HB2 H 1 2.88 0.01 . 1 . . . . . . . . 4943 1 169 . 1 1 46 46 ASN HB3 H 1 2.88 0.01 . 1 . . . . . . . . 4943 1 170 . 1 1 47 47 THR H H 1 8.81 0.01 . 1 . . . . . . . . 4943 1 171 . 1 1 47 47 THR HA H 1 4.38 0.01 . 1 . . . . . . . . 4943 1 172 . 1 1 47 47 THR HB H 1 4.12 0.01 . 1 . . . . . . . . 4943 1 173 . 1 1 48 48 ASP H H 1 7.82 0.01 . 1 . . . . . . . . 4943 1 174 . 1 1 48 48 ASP HA H 1 4.59 0.01 . 1 . . . . . . . . 4943 1 175 . 1 1 48 48 ASP HB2 H 1 3.10 0.01 . 2 . . . . . . . . 4943 1 176 . 1 1 48 48 ASP HB3 H 1 2.67 0.01 . 2 . . . . . . . . 4943 1 177 . 1 1 49 49 GLY H H 1 7.88 0.01 . 1 . . . . . . . . 4943 1 178 . 1 1 49 49 GLY HA2 H 1 3.73 0.01 . 2 . . . . . . . . 4943 1 179 . 1 1 49 49 GLY HA3 H 1 4.42 0.01 . 2 . . . . . . . . 4943 1 180 . 1 1 50 50 SER H H 1 8.29 0.01 . 1 . . . . . . . . 4943 1 181 . 1 1 50 50 SER HA H 1 4.57 0.01 . 1 . . . . . . . . 4943 1 182 . 1 1 50 50 SER HB2 H 1 4.24 0.01 . 2 . . . . . . . . 4943 1 183 . 1 1 50 50 SER HB3 H 1 3.76 0.01 . 2 . . . . . . . . 4943 1 184 . 1 1 51 51 THR H H 1 9.16 0.01 . 1 . . . . . . . . 4943 1 185 . 1 1 51 51 THR HA H 1 4.93 0.01 . 1 . . . . . . . . 4943 1 186 . 1 1 51 51 THR HB H 1 3.77 0.01 . 1 . . . . . . . . 4943 1 187 . 1 1 52 52 ASP H H 1 8.80 0.01 . 1 . . . . . . . . 4943 1 188 . 1 1 52 52 ASP HA H 1 5.20 0.01 . 1 . . . . . . . . 4943 1 189 . 1 1 52 52 ASP HB2 H 1 2.61 0.01 . 2 . . . . . . . . 4943 1 190 . 1 1 52 52 ASP HB3 H 1 2.02 0.01 . 2 . . . . . . . . 4943 1 191 . 1 1 53 53 TYR H H 1 9.02 0.01 . 1 . . . . . . . . 4943 1 192 . 1 1 53 53 TYR HA H 1 4.77 0.01 . 1 . . . . . . . . 4943 1 193 . 1 1 53 53 TYR HB2 H 1 2.97 0.01 . 2 . . . . . . . . 4943 1 194 . 1 1 53 53 TYR HB3 H 1 2.65 0.01 . 2 . . . . . . . . 4943 1 195 . 1 1 54 54 GLY H H 1 9.04 0.01 . 1 . . . . . . . . 4943 1 196 . 1 1 54 54 GLY HA2 H 1 4.41 0.01 . 2 . . . . . . . . 4943 1 197 . 1 1 54 54 GLY HA3 H 1 4.32 0.01 . 2 . . . . . . . . 4943 1 198 . 1 1 55 55 ILE H H 1 9.26 0.01 . 1 . . . . . . . . 4943 1 199 . 1 1 55 55 ILE HA H 1 4.30 0.01 . 1 . . . . . . . . 4943 1 200 . 1 1 55 55 ILE HB H 1 1.65 0.01 . 1 . . . . . . . . 4943 1 201 . 1 1 56 56 LEU H H 1 8.89 0.01 . 1 . . . . . . . . 4943 1 202 . 1 1 56 56 LEU HA H 1 4.41 0.01 . 1 . . . . . . . . 4943 1 203 . 1 1 56 56 LEU HB2 H 1 1.74 0.01 . 2 . . . . . . . . 4943 1 204 . 1 1 56 56 LEU HB3 H 1 1.48 0.01 . 2 . . . . . . . . 4943 1 205 . 1 1 57 57 GLN H H 1 7.90 0.01 . 1 . . . . . . . . 4943 1 206 . 1 1 57 57 GLN HA H 1 3.38 0.01 . 1 . . . . . . . . 4943 1 207 . 1 1 57 57 GLN HB2 H 1 2.23 0.01 . 2 . . . . . . . . 4943 1 208 . 1 1 57 57 GLN HB3 H 1 2.16 0.01 . 2 . . . . . . . . 4943 1 209 . 1 1 58 58 ILE H H 1 7.71 0.01 . 1 . . . . . . . . 4943 1 210 . 1 1 58 58 ILE HA H 1 4.04 0.01 . 1 . . . . . . . . 4943 1 211 . 1 1 58 58 ILE HB H 1 1.85 0.01 . 1 . . . . . . . . 4943 1 212 . 1 1 59 59 ASN H H 1 8.56 0.01 . 1 . . . . . . . . 4943 1 213 . 1 1 59 59 ASN HA H 1 5.65 0.01 . 1 . . . . . . . . 4943 1 214 . 1 1 59 59 ASN HB2 H 1 3.43 0.01 . 2 . . . . . . . . 4943 1 215 . 1 1 59 59 ASN HB3 H 1 3.03 0.01 . 2 . . . . . . . . 4943 1 216 . 1 1 60 60 SER H H 1 9.18 0.01 . 1 . . . . . . . . 4943 1 217 . 1 1 60 60 SER HA H 1 5.17 0.01 . 1 . . . . . . . . 4943 1 218 . 1 1 60 60 SER HB2 H 1 4.43 0.01 . 1 . . . . . . . . 4943 1 219 . 1 1 60 60 SER HB3 H 1 4.43 0.01 . 1 . . . . . . . . 4943 1 220 . 1 1 61 61 ARG H H 1 8.77 0.01 . 1 . . . . . . . . 4943 1 221 . 1 1 61 61 ARG HA H 1 4.11 0.01 . 1 . . . . . . . . 4943 1 222 . 1 1 61 61 ARG HB2 H 1 1.71 0.01 . 2 . . . . . . . . 4943 1 223 . 1 1 61 61 ARG HB3 H 1 1.46 0.01 . 2 . . . . . . . . 4943 1 224 . 1 1 62 62 TRP H H 1 7.13 0.01 . 1 . . . . . . . . 4943 1 225 . 1 1 62 62 TRP HA H 1 4.41 0.01 . 1 . . . . . . . . 4943 1 226 . 1 1 62 62 TRP HB2 H 1 1.84 0.01 . 1 . . . . . . . . 4943 1 227 . 1 1 62 62 TRP HB3 H 1 1.84 0.01 . 1 . . . . . . . . 4943 1 228 . 1 1 63 63 TRP H H 1 7.44 0.01 . 1 . . . . . . . . 4943 1 229 . 1 1 63 63 TRP HA H 1 4.99 0.01 . 1 . . . . . . . . 4943 1 230 . 1 1 63 63 TRP HB2 H 1 3.44 0.01 . 2 . . . . . . . . 4943 1 231 . 1 1 63 63 TRP HB3 H 1 3.36 0.01 . 2 . . . . . . . . 4943 1 232 . 1 1 64 64 CYS H H 1 7.59 0.01 . 1 . . . . . . . . 4943 1 233 . 1 1 64 64 CYS HA H 1 5.83 0.01 . 1 . . . . . . . . 4943 1 234 . 1 1 64 64 CYS HB2 H 1 3.06 0.01 . 2 . . . . . . . . 4943 1 235 . 1 1 64 64 CYS HB3 H 1 2.56 0.01 . 2 . . . . . . . . 4943 1 236 . 1 1 65 65 ASN H H 1 8.27 0.01 . 1 . . . . . . . . 4943 1 237 . 1 1 65 65 ASN HA H 1 5.53 0.01 . 1 . . . . . . . . 4943 1 238 . 1 1 65 65 ASN HB2 H 1 2.85 0.01 . 2 . . . . . . . . 4943 1 239 . 1 1 65 65 ASN HB3 H 1 2.47 0.01 . 2 . . . . . . . . 4943 1 240 . 1 1 66 66 ASP H H 1 9.69 0.01 . 1 . . . . . . . . 4943 1 241 . 1 1 66 66 ASP HA H 1 4.99 0.01 . 1 . . . . . . . . 4943 1 242 . 1 1 66 66 ASP HB2 H 1 3.29 0.01 . 2 . . . . . . . . 4943 1 243 . 1 1 66 66 ASP HB3 H 1 2.25 0.01 . 2 . . . . . . . . 4943 1 244 . 1 1 67 67 GLY H H 1 8.34 0.01 . 1 . . . . . . . . 4943 1 245 . 1 1 67 67 GLY HA2 H 1 4.15 0.01 . 2 . . . . . . . . 4943 1 246 . 1 1 67 67 GLY HA3 H 1 3.86 0.01 . 2 . . . . . . . . 4943 1 247 . 1 1 68 68 ARG H H 1 8.08 0.01 . 1 . . . . . . . . 4943 1 248 . 1 1 68 68 ARG HA H 1 4.78 0.01 . 1 . . . . . . . . 4943 1 249 . 1 1 68 68 ARG HB2 H 1 1.84 0.01 . 1 . . . . . . . . 4943 1 250 . 1 1 68 68 ARG HB3 H 1 1.84 0.01 . 1 . . . . . . . . 4943 1 251 . 1 1 69 69 THR H H 1 8.19 0.01 . 1 . . . . . . . . 4943 1 252 . 1 1 69 69 THR HA H 1 4.61 0.01 . 1 . . . . . . . . 4943 1 253 . 1 1 69 69 THR HB H 1 4.19 0.01 . 1 . . . . . . . . 4943 1 254 . 1 1 70 70 PRO HA H 1 4.32 0.01 . 1 . . . . . . . . 4943 1 255 . 1 1 70 70 PRO HB2 H 1 2.30 0.01 . 2 . . . . . . . . 4943 1 256 . 1 1 70 70 PRO HB3 H 1 2.12 0.01 . 2 . . . . . . . . 4943 1 257 . 1 1 71 71 GLY H H 1 8.70 0.01 . 1 . . . . . . . . 4943 1 258 . 1 1 71 71 GLY HA2 H 1 3.82 0.01 . 2 . . . . . . . . 4943 1 259 . 1 1 71 71 GLY HA3 H 1 3.67 0.01 . 2 . . . . . . . . 4943 1 260 . 1 1 72 72 SER H H 1 7.30 0.01 . 1 . . . . . . . . 4943 1 261 . 1 1 72 72 SER HA H 1 4.56 0.01 . 1 . . . . . . . . 4943 1 262 . 1 1 72 72 SER HB2 H 1 4.25 0.01 . 2 . . . . . . . . 4943 1 263 . 1 1 72 72 SER HB3 H 1 3.77 0.01 . 2 . . . . . . . . 4943 1 264 . 1 1 73 73 ARG H H 1 8.02 0.01 . 1 . . . . . . . . 4943 1 265 . 1 1 73 73 ARG HA H 1 4.23 0.01 . 1 . . . . . . . . 4943 1 266 . 1 1 73 73 ARG HB2 H 1 1.67 0.01 . 2 . . . . . . . . 4943 1 267 . 1 1 73 73 ARG HB3 H 1 1.54 0.01 . 2 . . . . . . . . 4943 1 268 . 1 1 74 74 ASN H H 1 8.20 0.01 . 1 . . . . . . . . 4943 1 269 . 1 1 74 74 ASN HA H 1 3.76 0.01 . 1 . . . . . . . . 4943 1 270 . 1 1 74 74 ASN HB2 H 1 3.09 0.01 . 2 . . . . . . . . 4943 1 271 . 1 1 74 74 ASN HB3 H 1 2.01 0.01 . 2 . . . . . . . . 4943 1 272 . 1 1 75 75 LEU H H 1 9.03 0.01 . 1 . . . . . . . . 4943 1 273 . 1 1 75 75 LEU HA H 1 4.10 0.01 . 1 . . . . . . . . 4943 1 274 . 1 1 75 75 LEU HB2 H 1 2.12 0.01 . 2 . . . . . . . . 4943 1 275 . 1 1 75 75 LEU HB3 H 1 1.48 0.01 . 2 . . . . . . . . 4943 1 276 . 1 1 76 76 CYS H H 1 9.48 0.01 . 1 . . . . . . . . 4943 1 277 . 1 1 76 76 CYS HA H 1 4.46 0.01 . 1 . . . . . . . . 4943 1 278 . 1 1 76 76 CYS HB2 H 1 3.69 0.01 . 1 . . . . . . . . 4943 1 279 . 1 1 76 76 CYS HB3 H 1 3.69 0.01 . 1 . . . . . . . . 4943 1 280 . 1 1 77 77 ASN H H 1 8.05 0.01 . 1 . . . . . . . . 4943 1 281 . 1 1 77 77 ASN HA H 1 4.22 0.01 . 1 . . . . . . . . 4943 1 282 . 1 1 77 77 ASN HB2 H 1 3.18 0.01 . 2 . . . . . . . . 4943 1 283 . 1 1 77 77 ASN HB3 H 1 2.51 0.01 . 2 . . . . . . . . 4943 1 284 . 1 1 78 78 ILE H H 1 8.80 0.01 . 1 . . . . . . . . 4943 1 285 . 1 1 78 78 ILE HA H 1 4.99 0.01 . 1 . . . . . . . . 4943 1 286 . 1 1 78 78 ILE HB H 1 1.71 0.01 . 1 . . . . . . . . 4943 1 287 . 1 1 79 79 PRO HA H 1 5.18 0.01 . 1 . . . . . . . . 4943 1 288 . 1 1 79 79 PRO HB2 H 1 2.37 0.01 . 2 . . . . . . . . 4943 1 289 . 1 1 79 79 PRO HB3 H 1 2.02 0.01 . 2 . . . . . . . . 4943 1 290 . 1 1 80 80 CYS H H 1 8.25 0.01 . 1 . . . . . . . . 4943 1 291 . 1 1 80 80 CYS HA H 1 3.90 0.01 . 1 . . . . . . . . 4943 1 292 . 1 1 80 80 CYS HB2 H 1 1.74 0.01 . 2 . . . . . . . . 4943 1 293 . 1 1 80 80 CYS HB3 H 1 1.31 0.01 . 2 . . . . . . . . 4943 1 294 . 1 1 81 81 SER H H 1 8.58 0.01 . 1 . . . . . . . . 4943 1 295 . 1 1 81 81 SER HA H 1 3.80 0.01 . 1 . . . . . . . . 4943 1 296 . 1 1 81 81 SER HB2 H 1 3.90 0.01 . 1 . . . . . . . . 4943 1 297 . 1 1 81 81 SER HB3 H 1 3.90 0.01 . 1 . . . . . . . . 4943 1 298 . 1 1 82 82 ALA H H 1 7.61 0.01 . 1 . . . . . . . . 4943 1 299 . 1 1 82 82 ALA HA H 1 4.24 0.01 . 1 . . . . . . . . 4943 1 300 . 1 1 82 82 ALA HB1 H 1 1.50 0.01 . 1 . . . . . . . . 4943 1 301 . 1 1 82 82 ALA HB2 H 1 1.50 0.01 . 1 . . . . . . . . 4943 1 302 . 1 1 82 82 ALA HB3 H 1 1.50 0.01 . 1 . . . . . . . . 4943 1 303 . 1 1 83 83 LEU H H 1 7.86 0.01 . 1 . . . . . . . . 4943 1 304 . 1 1 83 83 LEU HA H 1 4.25 0.01 . 1 . . . . . . . . 4943 1 305 . 1 1 83 83 LEU HB2 H 1 2.09 0.01 . 2 . . . . . . . . 4943 1 306 . 1 1 83 83 LEU HB3 H 1 1.66 0.01 . 2 . . . . . . . . 4943 1 307 . 1 1 84 84 LEU H H 1 7.13 0.01 . 1 . . . . . . . . 4943 1 308 . 1 1 84 84 LEU HA H 1 5.11 0.01 . 1 . . . . . . . . 4943 1 309 . 1 1 84 84 LEU HB2 H 1 1.90 0.01 . 2 . . . . . . . . 4943 1 310 . 1 1 84 84 LEU HB3 H 1 1.71 0.01 . 2 . . . . . . . . 4943 1 311 . 1 1 85 85 SER H H 1 6.84 0.01 . 1 . . . . . . . . 4943 1 312 . 1 1 85 85 SER HA H 1 4.50 0.01 . 1 . . . . . . . . 4943 1 313 . 1 1 85 85 SER HB2 H 1 4.15 0.01 . 2 . . . . . . . . 4943 1 314 . 1 1 85 85 SER HB3 H 1 3.87 0.01 . 2 . . . . . . . . 4943 1 315 . 1 1 86 86 SER H H 1 8.51 0.01 . 1 . . . . . . . . 4943 1 316 . 1 1 86 86 SER HA H 1 4.28 0.01 . 1 . . . . . . . . 4943 1 317 . 1 1 86 86 SER HB2 H 1 3.92 0.01 . 2 . . . . . . . . 4943 1 318 . 1 1 86 86 SER HB3 H 1 3.87 0.01 . 2 . . . . . . . . 4943 1 319 . 1 1 87 87 ASP H H 1 8.16 0.01 . 1 . . . . . . . . 4943 1 320 . 1 1 87 87 ASP HA H 1 4.93 0.01 . 1 . . . . . . . . 4943 1 321 . 1 1 87 87 ASP HB2 H 1 2.95 0.01 . 2 . . . . . . . . 4943 1 322 . 1 1 87 87 ASP HB3 H 1 2.65 0.01 . 2 . . . . . . . . 4943 1 323 . 1 1 88 88 ILE H H 1 8.12 0.01 . 1 . . . . . . . . 4943 1 324 . 1 1 88 88 ILE HA H 1 4.65 0.01 . 1 . . . . . . . . 4943 1 325 . 1 1 88 88 ILE HB H 1 1.85 0.01 . 1 . . . . . . . . 4943 1 326 . 1 1 89 89 THR H H 1 8.36 0.01 . 1 . . . . . . . . 4943 1 327 . 1 1 89 89 THR HA H 1 3.06 0.01 . 1 . . . . . . . . 4943 1 328 . 1 1 89 89 THR HB H 1 3.98 0.01 . 1 . . . . . . . . 4943 1 329 . 1 1 90 90 ALA H H 1 9.11 0.01 . 1 . . . . . . . . 4943 1 330 . 1 1 90 90 ALA HA H 1 4.09 0.01 . 1 . . . . . . . . 4943 1 331 . 1 1 90 90 ALA HB1 H 1 1.35 0.01 . 1 . . . . . . . . 4943 1 332 . 1 1 90 90 ALA HB2 H 1 1.35 0.01 . 1 . . . . . . . . 4943 1 333 . 1 1 90 90 ALA HB3 H 1 1.35 0.01 . 1 . . . . . . . . 4943 1 334 . 1 1 91 91 SER H H 1 7.79 0.01 . 1 . . . . . . . . 4943 1 335 . 1 1 91 91 SER HA H 1 4.09 0.01 . 1 . . . . . . . . 4943 1 336 . 1 1 91 91 SER HB2 H 1 4.00 0.01 . 2 . . . . . . . . 4943 1 337 . 1 1 91 91 SER HB3 H 1 3.49 0.01 . 2 . . . . . . . . 4943 1 338 . 1 1 92 92 VAL H H 1 8.38 0.01 . 1 . . . . . . . . 4943 1 339 . 1 1 92 92 VAL HA H 1 3.14 0.01 . 1 . . . . . . . . 4943 1 340 . 1 1 92 92 VAL HB H 1 1.91 0.01 . 1 . . . . . . . . 4943 1 341 . 1 1 93 93 ASN H H 1 8.65 0.01 . 1 . . . . . . . . 4943 1 342 . 1 1 93 93 ASN HA H 1 4.28 0.01 . 1 . . . . . . . . 4943 1 343 . 1 1 93 93 ASN HB2 H 1 2.89 0.01 . 2 . . . . . . . . 4943 1 344 . 1 1 93 93 ASN HB3 H 1 2.78 0.01 . 2 . . . . . . . . 4943 1 345 . 1 1 94 94 CYS H H 1 7.90 0.01 . 1 . . . . . . . . 4943 1 346 . 1 1 94 94 CYS HA H 1 5.00 0.01 . 1 . . . . . . . . 4943 1 347 . 1 1 94 94 CYS HB2 H 1 3.38 0.01 . 2 . . . . . . . . 4943 1 348 . 1 1 94 94 CYS HB3 H 1 2.71 0.01 . 2 . . . . . . . . 4943 1 349 . 1 1 95 95 ALA H H 1 8.70 0.01 . 1 . . . . . . . . 4943 1 350 . 1 1 95 95 ALA HA H 1 4.11 0.01 . 1 . . . . . . . . 4943 1 351 . 1 1 95 95 ALA HB1 H 1 1.53 0.01 . 1 . . . . . . . . 4943 1 352 . 1 1 95 95 ALA HB2 H 1 1.53 0.01 . 1 . . . . . . . . 4943 1 353 . 1 1 95 95 ALA HB3 H 1 1.53 0.01 . 1 . . . . . . . . 4943 1 354 . 1 1 96 96 LYS H H 1 8.02 0.01 . 1 . . . . . . . . 4943 1 355 . 1 1 96 96 LYS HA H 1 3.73 0.01 . 1 . . . . . . . . 4943 1 356 . 1 1 96 96 LYS HB2 H 1 1.68 0.01 . 1 . . . . . . . . 4943 1 357 . 1 1 96 96 LYS HB3 H 1 1.68 0.01 . 1 . . . . . . . . 4943 1 358 . 1 1 97 97 LYS H H 1 7.24 0.01 . 1 . . . . . . . . 4943 1 359 . 1 1 97 97 LYS HA H 1 4.16 0.01 . 1 . . . . . . . . 4943 1 360 . 1 1 97 97 LYS HB2 H 1 2.22 0.01 . 2 . . . . . . . . 4943 1 361 . 1 1 97 97 LYS HB3 H 1 2.16 0.01 . 2 . . . . . . . . 4943 1 362 . 1 1 98 98 ILE H H 1 7.98 0.01 . 1 . . . . . . . . 4943 1 363 . 1 1 98 98 ILE HA H 1 2.80 0.01 . 1 . . . . . . . . 4943 1 364 . 1 1 98 98 ILE HB H 1 1.50 0.01 . 1 . . . . . . . . 4943 1 365 . 1 1 99 99 VAL H H 1 8.25 0.01 . 1 . . . . . . . . 4943 1 366 . 1 1 99 99 VAL HA H 1 3.90 0.01 . 1 . . . . . . . . 4943 1 367 . 1 1 99 99 VAL HB H 1 2.42 0.01 . 1 . . . . . . . . 4943 1 368 . 1 1 100 100 SER H H 1 7.67 0.01 . 1 . . . . . . . . 4943 1 369 . 1 1 100 100 SER HA H 1 4.45 0.01 . 1 . . . . . . . . 4943 1 370 . 1 1 100 100 SER HB2 H 1 4.19 0.01 . 2 . . . . . . . . 4943 1 371 . 1 1 100 100 SER HB3 H 1 4.10 0.01 . 2 . . . . . . . . 4943 1 372 . 1 1 101 101 ASP H H 1 8.01 0.01 . 1 . . . . . . . . 4943 1 373 . 1 1 101 101 ASP HA H 1 4.79 0.01 . 1 . . . . . . . . 4943 1 374 . 1 1 101 101 ASP HB2 H 1 3.06 0.01 . 1 . . . . . . . . 4943 1 375 . 1 1 101 101 ASP HB3 H 1 3.06 0.01 . 1 . . . . . . . . 4943 1 376 . 1 1 102 102 GLY H H 1 8.18 0.01 . 1 . . . . . . . . 4943 1 377 . 1 1 102 102 GLY HA2 H 1 4.10 0.01 . 2 . . . . . . . . 4943 1 378 . 1 1 102 102 GLY HA3 H 1 3.99 0.01 . 2 . . . . . . . . 4943 1 379 . 1 1 103 103 ASN H H 1 8.19 0.01 . 1 . . . . . . . . 4943 1 380 . 1 1 103 103 ASN HA H 1 4.95 0.01 . 1 . . . . . . . . 4943 1 381 . 1 1 103 103 ASN HB2 H 1 2.80 0.01 . 2 . . . . . . . . 4943 1 382 . 1 1 103 103 ASN HB3 H 1 2.72 0.01 . 2 . . . . . . . . 4943 1 383 . 1 1 104 104 GLY H H 1 8.22 0.01 . 1 . . . . . . . . 4943 1 384 . 1 1 104 104 GLY HA2 H 1 4.24 0.01 . 2 . . . . . . . . 4943 1 385 . 1 1 104 104 GLY HA3 H 1 4.08 0.01 . 2 . . . . . . . . 4943 1 386 . 1 1 105 105 MET H H 1 7.08 0.01 . 1 . . . . . . . . 4943 1 387 . 1 1 105 105 MET HA H 1 3.83 0.01 . 1 . . . . . . . . 4943 1 388 . 1 1 105 105 MET HB2 H 1 0.43 0.01 . 2 . . . . . . . . 4943 1 389 . 1 1 105 105 MET HB3 H 1 -0.99 0.01 . 2 . . . . . . . . 4943 1 390 . 1 1 106 106 ASN H H 1 7.65 0.01 . 1 . . . . . . . . 4943 1 391 . 1 1 106 106 ASN HA H 1 4.46 0.01 . 1 . . . . . . . . 4943 1 392 . 1 1 106 106 ASN HB2 H 1 3.04 0.01 . 2 . . . . . . . . 4943 1 393 . 1 1 106 106 ASN HB3 H 1 2.81 0.01 . 2 . . . . . . . . 4943 1 394 . 1 1 107 107 ALA H H 1 6.78 0.01 . 1 . . . . . . . . 4943 1 395 . 1 1 107 107 ALA HA H 1 3.85 0.01 . 1 . . . . . . . . 4943 1 396 . 1 1 107 107 ALA HB1 H 1 0.62 0.01 . 1 . . . . . . . . 4943 1 397 . 1 1 107 107 ALA HB2 H 1 0.62 0.01 . 1 . . . . . . . . 4943 1 398 . 1 1 107 107 ALA HB3 H 1 0.62 0.01 . 1 . . . . . . . . 4943 1 399 . 1 1 108 108 TRP H H 1 7.87 0.01 . 1 . . . . . . . . 4943 1 400 . 1 1 108 108 TRP HA H 1 4.70 0.01 . 1 . . . . . . . . 4943 1 401 . 1 1 108 108 TRP HB2 H 1 3.36 0.01 . 2 . . . . . . . . 4943 1 402 . 1 1 108 108 TRP HB3 H 1 3.27 0.01 . 2 . . . . . . . . 4943 1 403 . 1 1 109 109 VAL H H 1 8.94 0.01 . 1 . . . . . . . . 4943 1 404 . 1 1 109 109 VAL HA H 1 3.64 0.01 . 1 . . . . . . . . 4943 1 405 . 1 1 109 109 VAL HB H 1 2.17 0.01 . 1 . . . . . . . . 4943 1 406 . 1 1 110 110 ALA H H 1 8.04 0.01 . 1 . . . . . . . . 4943 1 407 . 1 1 110 110 ALA HA H 1 4.27 0.01 . 1 . . . . . . . . 4943 1 408 . 1 1 110 110 ALA HB1 H 1 1.33 0.01 . 1 . . . . . . . . 4943 1 409 . 1 1 110 110 ALA HB2 H 1 1.33 0.01 . 1 . . . . . . . . 4943 1 410 . 1 1 110 110 ALA HB3 H 1 1.33 0.01 . 1 . . . . . . . . 4943 1 411 . 1 1 111 111 TRP H H 1 7.25 0.01 . 1 . . . . . . . . 4943 1 412 . 1 1 111 111 TRP HA H 1 3.73 0.01 . 1 . . . . . . . . 4943 1 413 . 1 1 111 111 TRP HB2 H 1 4.07 0.01 . 2 . . . . . . . . 4943 1 414 . 1 1 111 111 TRP HB3 H 1 2.79 0.01 . 2 . . . . . . . . 4943 1 415 . 1 1 112 112 ARG H H 1 8.25 0.01 . 1 . . . . . . . . 4943 1 416 . 1 1 112 112 ARG HA H 1 3.39 0.01 . 1 . . . . . . . . 4943 1 417 . 1 1 112 112 ARG HB2 H 1 2.13 0.01 . 2 . . . . . . . . 4943 1 418 . 1 1 112 112 ARG HB3 H 1 2.00 0.01 . 2 . . . . . . . . 4943 1 419 . 1 1 113 113 ASN H H 1 7.97 0.01 . 1 . . . . . . . . 4943 1 420 . 1 1 113 113 ASN HA H 1 4.53 0.01 . 1 . . . . . . . . 4943 1 421 . 1 1 113 113 ASN HB2 H 1 2.68 0.01 . 1 . . . . . . . . 4943 1 422 . 1 1 113 113 ASN HB3 H 1 2.68 0.01 . 1 . . . . . . . . 4943 1 423 . 1 1 114 114 ARG H H 1 7.66 0.01 . 1 . . . . . . . . 4943 1 424 . 1 1 114 114 ARG HA H 1 4.32 0.01 . 1 . . . . . . . . 4943 1 425 . 1 1 114 114 ARG HB2 H 1 1.20 0.01 . 2 . . . . . . . . 4943 1 426 . 1 1 114 114 ARG HB3 H 1 0.62 0.01 . 2 . . . . . . . . 4943 1 427 . 1 1 115 115 CYS H H 1 7.34 0.01 . 1 . . . . . . . . 4943 1 428 . 1 1 115 115 CYS HA H 1 4.54 0.01 . 1 . . . . . . . . 4943 1 429 . 1 1 115 115 CYS HB2 H 1 2.61 0.01 . 2 . . . . . . . . 4943 1 430 . 1 1 115 115 CYS HB3 H 1 2.48 0.01 . 2 . . . . . . . . 4943 1 431 . 1 1 116 116 LYS H H 1 7.06 0.01 . 1 . . . . . . . . 4943 1 432 . 1 1 116 116 LYS HA H 1 3.45 0.01 . 1 . . . . . . . . 4943 1 433 . 1 1 116 116 LYS HB2 H 1 -0.18 0.01 . 2 . . . . . . . . 4943 1 434 . 1 1 116 116 LYS HB3 H 1 1.23 0.01 . 2 . . . . . . . . 4943 1 435 . 1 1 117 117 GLY H H 1 8.70 0.01 . 1 . . . . . . . . 4943 1 436 . 1 1 117 117 GLY HA2 H 1 4.13 0.01 . 2 . . . . . . . . 4943 1 437 . 1 1 117 117 GLY HA3 H 1 3.81 0.01 . 2 . . . . . . . . 4943 1 438 . 1 1 118 118 THR H H 1 7.65 0.01 . 1 . . . . . . . . 4943 1 439 . 1 1 118 118 THR HA H 1 4.76 0.01 . 1 . . . . . . . . 4943 1 440 . 1 1 118 118 THR HB H 1 4.32 0.01 . 1 . . . . . . . . 4943 1 441 . 1 1 119 119 ASP H H 1 8.65 0.01 . 1 . . . . . . . . 4943 1 442 . 1 1 119 119 ASP HA H 1 5.00 0.01 . 1 . . . . . . . . 4943 1 443 . 1 1 119 119 ASP HB2 H 1 2.95 0.01 . 2 . . . . . . . . 4943 1 444 . 1 1 119 119 ASP HB3 H 1 2.73 0.01 . 2 . . . . . . . . 4943 1 445 . 1 1 120 120 VAL H H 1 8.13 0.01 . 1 . . . . . . . . 4943 1 446 . 1 1 120 120 VAL HA H 1 4.36 0.01 . 1 . . . . . . . . 4943 1 447 . 1 1 120 120 VAL HB H 1 2.18 0.01 . 1 . . . . . . . . 4943 1 448 . 1 1 121 121 GLN H H 1 8.45 0.01 . 1 . . . . . . . . 4943 1 449 . 1 1 121 121 GLN HA H 1 4.34 0.01 . 1 . . . . . . . . 4943 1 450 . 1 1 121 121 GLN HB2 H 1 2.27 0.01 . 2 . . . . . . . . 4943 1 451 . 1 1 121 121 GLN HB3 H 1 2.19 0.01 . 2 . . . . . . . . 4943 1 452 . 1 1 122 122 ALA H H 1 7.71 0.01 . 1 . . . . . . . . 4943 1 453 . 1 1 122 122 ALA HA H 1 3.83 0.01 . 1 . . . . . . . . 4943 1 454 . 1 1 122 122 ALA HB1 H 1 1.17 0.01 . 1 . . . . . . . . 4943 1 455 . 1 1 122 122 ALA HB2 H 1 1.17 0.01 . 1 . . . . . . . . 4943 1 456 . 1 1 122 122 ALA HB3 H 1 1.17 0.01 . 1 . . . . . . . . 4943 1 457 . 1 1 123 123 TRP H H 1 7.59 0.01 . 1 . . . . . . . . 4943 1 458 . 1 1 123 123 TRP HA H 1 4.12 0.01 . 1 . . . . . . . . 4943 1 459 . 1 1 123 123 TRP HB2 H 1 3.51 0.01 . 2 . . . . . . . . 4943 1 460 . 1 1 123 123 TRP HB3 H 1 3.41 0.01 . 2 . . . . . . . . 4943 1 461 . 1 1 124 124 ILE H H 1 7.56 0.01 . 1 . . . . . . . . 4943 1 462 . 1 1 124 124 ILE HA H 1 4.74 0.01 . 1 . . . . . . . . 4943 1 463 . 1 1 124 124 ILE HB H 1 2.22 0.01 . 1 . . . . . . . . 4943 1 464 . 1 1 125 125 ARG H H 1 7.33 0.01 . 1 . . . . . . . . 4943 1 465 . 1 1 125 125 ARG HA H 1 4.17 0.01 . 1 . . . . . . . . 4943 1 466 . 1 1 125 125 ARG HB2 H 1 1.82 0.01 . 2 . . . . . . . . 4943 1 467 . 1 1 125 125 ARG HB3 H 1 1.78 0.01 . 2 . . . . . . . . 4943 1 468 . 1 1 126 126 GLY H H 1 9.13 0.01 . 1 . . . . . . . . 4943 1 469 . 1 1 126 126 GLY HA2 H 1 4.31 0.01 . 2 . . . . . . . . 4943 1 470 . 1 1 126 126 GLY HA3 H 1 3.76 0.01 . 2 . . . . . . . . 4943 1 471 . 1 1 127 127 CYS H H 1 7.47 0.01 . 1 . . . . . . . . 4943 1 472 . 1 1 127 127 CYS HA H 1 4.93 0.01 . 1 . . . . . . . . 4943 1 473 . 1 1 127 127 CYS HB2 H 1 3.08 0.01 . 2 . . . . . . . . 4943 1 474 . 1 1 127 127 CYS HB3 H 1 2.65 0.01 . 2 . . . . . . . . 4943 1 475 . 1 1 128 128 ARG H H 1 8.90 0.01 . 1 . . . . . . . . 4943 1 476 . 1 1 128 128 ARG HA H 1 4.37 0.01 . 1 . . . . . . . . 4943 1 477 . 1 1 128 128 ARG HB2 H 1 1.87 0.01 . 2 . . . . . . . . 4943 1 478 . 1 1 128 128 ARG HB3 H 1 1.79 0.01 . 2 . . . . . . . . 4943 1 479 . 1 1 129 129 LEU H H 1 7.94 0.01 . 1 . . . . . . . . 4943 1 480 . 1 1 129 129 LEU HA H 1 4.29 0.01 . 1 . . . . . . . . 4943 1 481 . 1 1 129 129 LEU HB2 H 1 1.66 0.01 . 2 . . . . . . . . 4943 1 482 . 1 1 129 129 LEU HB3 H 1 1.46 0.01 . 2 . . . . . . . . 4943 1 stop_ save_ save_Seikagaku _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode Seikagaku _Assigned_chem_shift_list.Entry_ID 4943 _Assigned_chem_shift_list.ID 2 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $cond _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 . . 2 $sample_B . 4943 2 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 VAL H H 1 8.96 0.01 . 1 . . . . . . . . 4943 2 2 . 1 1 2 2 VAL HA H 1 4.98 0.01 . 1 . . . . . . . . 4943 2 3 . 1 1 2 2 VAL HB H 1 2.01 0.01 . 1 . . . . . . . . 4943 2 4 . 1 1 3 3 PHE H H 1 8.89 0.01 . 1 . . . . . . . . 4943 2 5 . 1 1 3 3 PHE HA H 1 4.22 0.01 . 1 . . . . . . . . 4943 2 6 . 1 1 3 3 PHE HB2 H 1 3.17 0.01 . 2 . . . . . . . . 4943 2 7 . 1 1 3 3 PHE HB3 H 1 2.69 0.01 . 2 . . . . . . . . 4943 2 8 . 1 1 4 4 GLY H H 1 8.50 0.01 . 1 . . . . . . . . 4943 2 9 . 1 1 4 4 GLY HA2 H 1 4.28 0.01 . 2 . . . . . . . . 4943 2 10 . 1 1 4 4 GLY HA3 H 1 3.89 0.01 . 2 . . . . . . . . 4943 2 11 . 1 1 5 5 ARG H H 1 8.56 0.01 . 1 . . . . . . . . 4943 2 12 . 1 1 5 5 ARG HA H 1 3.38 0.01 . 1 . . . . . . . . 4943 2 13 . 1 1 6 6 CYS H H 1 8.60 0.01 . 1 . . . . . . . . 4943 2 14 . 1 1 6 6 CYS HA H 1 4.74 0.01 . 1 . . . . . . . . 4943 2 15 . 1 1 6 6 CYS HB2 H 1 3.23 0.01 . 2 . . . . . . . . 4943 2 16 . 1 1 6 6 CYS HB3 H 1 2.79 0.01 . 2 . . . . . . . . 4943 2 17 . 1 1 7 7 GLU H H 1 8.11 0.01 . 1 . . . . . . . . 4943 2 18 . 1 1 7 7 GLU HA H 1 4.12 0.01 . 1 . . . . . . . . 4943 2 19 . 1 1 7 7 GLU HB2 H 1 2.33 0.01 . 2 . . . . . . . . 4943 2 20 . 1 1 7 7 GLU HB3 H 1 2.19 0.01 . 2 . . . . . . . . 4943 2 21 . 1 1 8 8 LEU H H 1 8.62 0.01 . 1 . . . . . . . . 4943 2 22 . 1 1 8 8 LEU HA H 1 3.78 0.01 . 1 . . . . . . . . 4943 2 23 . 1 1 8 8 LEU HB2 H 1 1.59 0.01 . 2 . . . . . . . . 4943 2 24 . 1 1 8 8 LEU HB3 H 1 0.93 0.01 . 2 . . . . . . . . 4943 2 25 . 1 1 9 9 ALA H H 1 8.39 0.01 . 1 . . . . . . . . 4943 2 26 . 1 1 9 9 ALA HA H 1 3.61 0.01 . 1 . . . . . . . . 4943 2 27 . 1 1 9 9 ALA HB1 H 1 1.57 0.01 . 1 . . . . . . . . 4943 2 28 . 1 1 9 9 ALA HB2 H 1 1.57 0.01 . 1 . . . . . . . . 4943 2 29 . 1 1 9 9 ALA HB3 H 1 1.57 0.01 . 1 . . . . . . . . 4943 2 30 . 1 1 10 10 ALA H H 1 8.16 0.01 . 1 . . . . . . . . 4943 2 31 . 1 1 10 10 ALA HA H 1 3.99 0.01 . 1 . . . . . . . . 4943 2 32 . 1 1 10 10 ALA HB1 H 1 1.55 0.01 . 1 . . . . . . . . 4943 2 33 . 1 1 10 10 ALA HB2 H 1 1.55 0.01 . 1 . . . . . . . . 4943 2 34 . 1 1 10 10 ALA HB3 H 1 1.55 0.01 . 1 . . . . . . . . 4943 2 35 . 1 1 11 11 ALA H H 1 7.77 0.01 . 1 . . . . . . . . 4943 2 36 . 1 1 11 11 ALA HA H 1 4.27 0.01 . 1 . . . . . . . . 4943 2 37 . 1 1 11 11 ALA HB1 H 1 1.52 0.01 . 1 . . . . . . . . 4943 2 38 . 1 1 11 11 ALA HB2 H 1 1.52 0.01 . 1 . . . . . . . . 4943 2 39 . 1 1 11 11 ALA HB3 H 1 1.52 0.01 . 1 . . . . . . . . 4943 2 40 . 1 1 12 12 MET H H 1 9.07 0.01 . 1 . . . . . . . . 4943 2 41 . 1 1 12 12 MET HA H 1 3.48 0.01 . 1 . . . . . . . . 4943 2 42 . 1 1 12 12 MET HB2 H 1 1.57 0.01 . 2 . . . . . . . . 4943 2 43 . 1 1 12 12 MET HB3 H 1 1.89 0.01 . 2 . . . . . . . . 4943 2 44 . 1 1 13 13 LYS H H 1 8.53 0.01 . 1 . . . . . . . . 4943 2 45 . 1 1 13 13 LYS HA H 1 3.98 0.01 . 1 . . . . . . . . 4943 2 46 . 1 1 13 13 LYS HB2 H 1 2.20 0.01 . 2 . . . . . . . . 4943 2 47 . 1 1 13 13 LYS HB3 H 1 1.94 0.01 . 2 . . . . . . . . 4943 2 48 . 1 1 14 14 ARG H H 1 8.19 0.01 . 1 . . . . . . . . 4943 2 49 . 1 1 14 14 ARG HA H 1 4.12 0.01 . 1 . . . . . . . . 4943 2 50 . 1 1 14 14 ARG HB2 H 1 1.95 0.01 . 2 . . . . . . . . 4943 2 51 . 1 1 14 14 ARG HB3 H 1 1.84 0.01 . 2 . . . . . . . . 4943 2 52 . 1 1 15 15 HIS H H 1 7.33 0.01 . 1 . . . . . . . . 4943 2 53 . 1 1 15 15 HIS HA H 1 4.54 0.01 . 1 . . . . . . . . 4943 2 54 . 1 1 15 15 HIS HB2 H 1 3.67 0.01 . 2 . . . . . . . . 4943 2 55 . 1 1 15 15 HIS HB3 H 1 2.57 0.01 . 2 . . . . . . . . 4943 2 56 . 1 1 16 16 GLY H H 1 7.64 0.01 . 1 . . . . . . . . 4943 2 57 . 1 1 16 16 GLY HA2 H 1 4.11 0.01 . 2 . . . . . . . . 4943 2 58 . 1 1 16 16 GLY HA3 H 1 3.92 0.01 . 2 . . . . . . . . 4943 2 59 . 1 1 17 17 LEU H H 1 7.14 0.01 . 1 . . . . . . . . 4943 2 60 . 1 1 17 17 LEU HA H 1 3.92 0.01 . 1 . . . . . . . . 4943 2 61 . 1 1 17 17 LEU HB2 H 1 0.72 0.01 . 2 . . . . . . . . 4943 2 62 . 1 1 17 17 LEU HB3 H 1 0.25 0.01 . 2 . . . . . . . . 4943 2 63 . 1 1 18 18 ASP H H 1 8.72 0.01 . 1 . . . . . . . . 4943 2 64 . 1 1 18 18 ASP HA H 1 4.27 0.01 . 1 . . . . . . . . 4943 2 65 . 1 1 18 18 ASP HB2 H 1 3.02 0.01 . 2 . . . . . . . . 4943 2 66 . 1 1 18 18 ASP HB3 H 1 2.38 0.01 . 2 . . . . . . . . 4943 2 67 . 1 1 19 19 ASN H H 1 8.39 0.01 . 1 . . . . . . . . 4943 2 68 . 1 1 19 19 ASN HA H 1 3.98 0.01 . 1 . . . . . . . . 4943 2 69 . 1 1 19 19 ASN HB2 H 1 3.05 0.01 . 2 . . . . . . . . 4943 2 70 . 1 1 19 19 ASN HB3 H 1 2.85 0.01 . 2 . . . . . . . . 4943 2 71 . 1 1 20 20 TYR H H 1 8.11 0.01 . 1 . . . . . . . . 4943 2 72 . 1 1 20 20 TYR HA H 1 4.25 0.01 . 1 . . . . . . . . 4943 2 73 . 1 1 20 20 TYR HB2 H 1 3.23 0.01 . 2 . . . . . . . . 4943 2 74 . 1 1 20 20 TYR HB3 H 1 3.06 0.01 . 2 . . . . . . . . 4943 2 75 . 1 1 21 21 ARG H H 1 8.94 0.01 . 1 . . . . . . . . 4943 2 76 . 1 1 21 21 ARG HA H 1 3.63 0.01 . 1 . . . . . . . . 4943 2 77 . 1 1 21 21 ARG HB2 H 1 2.23 0.01 . 2 . . . . . . . . 4943 2 78 . 1 1 21 21 ARG HB3 H 1 1.88 0.01 . 2 . . . . . . . . 4943 2 79 . 1 1 22 22 GLY H H 1 7.54 0.01 . 1 . . . . . . . . 4943 2 80 . 1 1 22 22 GLY HA2 H 1 3.87 0.01 . 2 . . . . . . . . 4943 2 81 . 1 1 22 22 GLY HA3 H 1 3.50 0.01 . 2 . . . . . . . . 4943 2 82 . 1 1 23 23 TYR H H 1 7.67 0.01 . 1 . . . . . . . . 4943 2 83 . 1 1 23 23 TYR HA H 1 4.57 0.01 . 1 . . . . . . . . 4943 2 84 . 1 1 23 23 TYR HB2 H 1 3.31 0.01 . 2 . . . . . . . . 4943 2 85 . 1 1 23 23 TYR HB3 H 1 2.50 0.01 . 2 . . . . . . . . 4943 2 86 . 1 1 24 24 SER H H 1 9.00 0.01 . 1 . . . . . . . . 4943 2 87 . 1 1 24 24 SER HA H 1 4.54 0.01 . 1 . . . . . . . . 4943 2 88 . 1 1 25 25 LEU H H 1 9.03 0.01 . 1 . . . . . . . . 4943 2 89 . 1 1 25 25 LEU HA H 1 4.41 0.01 . 1 . . . . . . . . 4943 2 90 . 1 1 26 26 GLY H H 1 9.60 0.01 . 1 . . . . . . . . 4943 2 91 . 1 1 26 26 GLY HA2 H 1 4.19 0.01 . 2 . . . . . . . . 4943 2 92 . 1 1 26 26 GLY HA3 H 1 3.67 0.01 . 2 . . . . . . . . 4943 2 93 . 1 1 27 27 ASN H H 1 8.20 0.01 . 1 . . . . . . . . 4943 2 94 . 1 1 27 27 ASN HA H 1 4.21 0.01 . 1 . . . . . . . . 4943 2 95 . 1 1 27 27 ASN HB2 H 1 2.88 0.01 . 2 . . . . . . . . 4943 2 96 . 1 1 27 27 ASN HB3 H 1 2.32 0.01 . 2 . . . . . . . . 4943 2 97 . 1 1 28 28 TRP H H 1 7.19 0.01 . 1 . . . . . . . . 4943 2 98 . 1 1 28 28 TRP HA H 1 3.76 0.01 . 1 . . . . . . . . 4943 2 99 . 1 1 28 28 TRP HB2 H 1 3.27 0.01 . 2 . . . . . . . . 4943 2 100 . 1 1 28 28 TRP HB3 H 1 3.21 0.01 . 2 . . . . . . . . 4943 2 101 . 1 1 29 29 VAL H H 1 7.55 0.01 . 1 . . . . . . . . 4943 2 102 . 1 1 29 29 VAL HA H 1 3.45 0.01 . 1 . . . . . . . . 4943 2 103 . 1 1 29 29 VAL HB H 1 1.95 0.01 . 1 . . . . . . . . 4943 2 104 . 1 1 30 30 CYS H H 1 8.03 0.01 . 1 . . . . . . . . 4943 2 105 . 1 1 30 30 CYS HA H 1 2.51 0.01 . 1 . . . . . . . . 4943 2 106 . 1 1 30 30 CYS HB2 H 1 2.92 0.01 . 2 . . . . . . . . 4943 2 107 . 1 1 30 30 CYS HB3 H 1 2.63 0.01 . 2 . . . . . . . . 4943 2 108 . 1 1 31 31 ALA H H 1 8.12 0.01 . 1 . . . . . . . . 4943 2 109 . 1 1 31 31 ALA HA H 1 3.72 0.01 . 1 . . . . . . . . 4943 2 110 . 1 1 31 31 ALA HB1 H 1 1.01 0.01 . 1 . . . . . . . . 4943 2 111 . 1 1 31 31 ALA HB2 H 1 1.01 0.01 . 1 . . . . . . . . 4943 2 112 . 1 1 31 31 ALA HB3 H 1 1.01 0.01 . 1 . . . . . . . . 4943 2 113 . 1 1 32 32 ALA H H 1 7.58 0.01 . 1 . . . . . . . . 4943 2 114 . 1 1 32 32 ALA HA H 1 4.02 0.01 . 1 . . . . . . . . 4943 2 115 . 1 1 32 32 ALA HB1 H 1 1.32 0.01 . 1 . . . . . . . . 4943 2 116 . 1 1 32 32 ALA HB2 H 1 1.32 0.01 . 1 . . . . . . . . 4943 2 117 . 1 1 32 32 ALA HB3 H 1 1.32 0.01 . 1 . . . . . . . . 4943 2 118 . 1 1 33 33 LYS H H 1 7.94 0.01 . 1 . . . . . . . . 4943 2 119 . 1 1 33 33 LYS HA H 1 2.57 0.01 . 1 . . . . . . . . 4943 2 120 . 1 1 34 34 PHE H H 1 7.35 0.01 . 1 . . . . . . . . 4943 2 121 . 1 1 34 34 PHE HA H 1 4.32 0.01 . 1 . . . . . . . . 4943 2 122 . 1 1 34 34 PHE HB2 H 1 3.19 0.01 . 2 . . . . . . . . 4943 2 123 . 1 1 34 34 PHE HB3 H 1 2.29 0.01 . 2 . . . . . . . . 4943 2 124 . 1 1 35 35 GLU H H 1 8.60 0.01 . 1 . . . . . . . . 4943 2 125 . 1 1 35 35 GLU HA H 1 4.45 0.01 . 1 . . . . . . . . 4943 2 126 . 1 1 35 35 GLU HB2 H 1 2.03 0.01 . 2 . . . . . . . . 4943 2 127 . 1 1 35 35 GLU HB3 H 1 1.77 0.01 . 2 . . . . . . . . 4943 2 128 . 1 1 36 36 SER H H 1 7.92 0.01 . 1 . . . . . . . . 4943 2 129 . 1 1 36 36 SER HA H 1 4.57 0.01 . 1 . . . . . . . . 4943 2 130 . 1 1 36 36 SER HB2 H 1 4.48 0.01 . 2 . . . . . . . . 4943 2 131 . 1 1 36 36 SER HB3 H 1 3.56 0.01 . 2 . . . . . . . . 4943 2 132 . 1 1 37 37 ASN H H 1 8.13 0.01 . 1 . . . . . . . . 4943 2 133 . 1 1 37 37 ASN HA H 1 4.50 0.01 . 1 . . . . . . . . 4943 2 134 . 1 1 37 37 ASN HB2 H 1 3.32 0.01 . 2 . . . . . . . . 4943 2 135 . 1 1 37 37 ASN HB3 H 1 2.49 0.01 . 2 . . . . . . . . 4943 2 136 . 1 1 38 38 PHE H H 1 7.36 0.01 . 1 . . . . . . . . 4943 2 137 . 1 1 38 38 PHE HA H 1 3.87 0.01 . 1 . . . . . . . . 4943 2 138 . 1 1 38 38 PHE HB3 H 1 3.63 0.01 . 2 . . . . . . . . 4943 2 139 . 1 1 39 39 ASN H H 1 7.41 0.01 . 1 . . . . . . . . 4943 2 140 . 1 1 39 39 ASN HA H 1 5.42 0.01 . 1 . . . . . . . . 4943 2 141 . 1 1 39 39 ASN HB2 H 1 3.48 0.01 . 2 . . . . . . . . 4943 2 142 . 1 1 39 39 ASN HB3 H 1 2.85 0.01 . 2 . . . . . . . . 4943 2 143 . 1 1 40 40 THR H H 1 9.37 0.01 . 1 . . . . . . . . 4943 2 144 . 1 1 40 40 THR HA H 1 4.07 0.01 . 1 . . . . . . . . 4943 2 145 . 1 1 40 40 THR HB H 1 4.68 0.01 . 1 . . . . . . . . 4943 2 146 . 1 1 41 41 GLN H H 1 7.90 0.01 . 1 . . . . . . . . 4943 2 147 . 1 1 41 41 GLN HA H 1 4.44 0.01 . 1 . . . . . . . . 4943 2 148 . 1 1 41 41 GLN HB2 H 1 2.45 0.01 . 2 . . . . . . . . 4943 2 149 . 1 1 41 41 GLN HB3 H 1 1.90 0.01 . 2 . . . . . . . . 4943 2 150 . 1 1 42 42 ALA H H 1 6.85 0.01 . 1 . . . . . . . . 4943 2 151 . 1 1 42 42 ALA HA H 1 4.16 0.01 . 1 . . . . . . . . 4943 2 152 . 1 1 42 42 ALA HB1 H 1 1.35 0.01 . 1 . . . . . . . . 4943 2 153 . 1 1 42 42 ALA HB2 H 1 1.35 0.01 . 1 . . . . . . . . 4943 2 154 . 1 1 42 42 ALA HB3 H 1 1.35 0.01 . 1 . . . . . . . . 4943 2 155 . 1 1 43 43 THR H H 1 8.24 0.01 . 1 . . . . . . . . 4943 2 156 . 1 1 43 43 THR HA H 1 5.16 0.01 . 1 . . . . . . . . 4943 2 157 . 1 1 43 43 THR HB H 1 3.73 0.01 . 1 . . . . . . . . 4943 2 158 . 1 1 44 44 ASN H H 1 8.17 0.01 . 1 . . . . . . . . 4943 2 159 . 1 1 44 44 ASN HA H 1 5.00 0.01 . 1 . . . . . . . . 4943 2 160 . 1 1 44 44 ASN HB2 H 1 2.77 0.01 . 2 . . . . . . . . 4943 2 161 . 1 1 44 44 ASN HB3 H 1 2.72 0.01 . 2 . . . . . . . . 4943 2 162 . 1 1 45 45 ARG H H 1 8.81 0.01 . 1 . . . . . . . . 4943 2 163 . 1 1 45 45 ARG HA H 1 4.51 0.01 . 1 . . . . . . . . 4943 2 164 . 1 1 45 45 ARG HB2 H 1 1.71 0.01 . 2 . . . . . . . . 4943 2 165 . 1 1 45 45 ARG HB3 H 1 1.64 0.01 . 2 . . . . . . . . 4943 2 166 . 1 1 46 46 ASN H H 1 8.89 0.01 . 1 . . . . . . . . 4943 2 167 . 1 1 46 46 ASN HA H 1 5.13 0.01 . 1 . . . . . . . . 4943 2 168 . 1 1 46 46 ASN HB2 H 1 2.87 0.01 . 1 . . . . . . . . 4943 2 169 . 1 1 46 46 ASN HB3 H 1 2.87 0.01 . 1 . . . . . . . . 4943 2 170 . 1 1 47 47 THR H H 1 8.82 0.01 . 1 . . . . . . . . 4943 2 171 . 1 1 47 47 THR HA H 1 4.38 0.01 . 1 . . . . . . . . 4943 2 172 . 1 1 47 47 THR HB H 1 4.12 0.01 . 1 . . . . . . . . 4943 2 173 . 1 1 48 48 ASP H H 1 7.82 0.01 . 1 . . . . . . . . 4943 2 174 . 1 1 48 48 ASP HA H 1 4.58 0.01 . 1 . . . . . . . . 4943 2 175 . 1 1 48 48 ASP HB2 H 1 3.09 0.01 . 2 . . . . . . . . 4943 2 176 . 1 1 48 48 ASP HB3 H 1 2.67 0.01 . 2 . . . . . . . . 4943 2 177 . 1 1 49 49 GLY H H 1 7.88 0.01 . 1 . . . . . . . . 4943 2 178 . 1 1 49 49 GLY HA2 H 1 3.73 0.01 . 2 . . . . . . . . 4943 2 179 . 1 1 49 49 GLY HA3 H 1 4.42 0.01 . 2 . . . . . . . . 4943 2 180 . 1 1 50 50 SER H H 1 8.29 0.01 . 1 . . . . . . . . 4943 2 181 . 1 1 50 50 SER HA H 1 4.57 0.01 . 1 . . . . . . . . 4943 2 182 . 1 1 50 50 SER HB2 H 1 4.24 0.01 . 2 . . . . . . . . 4943 2 183 . 1 1 50 50 SER HB3 H 1 3.76 0.01 . 2 . . . . . . . . 4943 2 184 . 1 1 51 51 THR H H 1 9.16 0.01 . 1 . . . . . . . . 4943 2 185 . 1 1 51 51 THR HA H 1 4.93 0.01 . 1 . . . . . . . . 4943 2 186 . 1 1 51 51 THR HB H 1 3.77 0.01 . 1 . . . . . . . . 4943 2 187 . 1 1 52 52 ASP H H 1 8.80 0.01 . 1 . . . . . . . . 4943 2 188 . 1 1 52 52 ASP HA H 1 5.20 0.01 . 1 . . . . . . . . 4943 2 189 . 1 1 52 52 ASP HB2 H 1 2.57 0.01 . 2 . . . . . . . . 4943 2 190 . 1 1 52 52 ASP HB3 H 1 2.00 0.01 . 2 . . . . . . . . 4943 2 191 . 1 1 53 53 TYR H H 1 9.02 0.01 . 1 . . . . . . . . 4943 2 192 . 1 1 53 53 TYR HA H 1 4.77 0.01 . 1 . . . . . . . . 4943 2 193 . 1 1 53 53 TYR HB2 H 1 2.97 0.01 . 2 . . . . . . . . 4943 2 194 . 1 1 53 53 TYR HB3 H 1 2.65 0.01 . 2 . . . . . . . . 4943 2 195 . 1 1 54 54 GLY H H 1 9.03 0.01 . 1 . . . . . . . . 4943 2 196 . 1 1 54 54 GLY HA2 H 1 4.40 0.01 . 2 . . . . . . . . 4943 2 197 . 1 1 54 54 GLY HA3 H 1 4.31 0.01 . 2 . . . . . . . . 4943 2 198 . 1 1 55 55 ILE H H 1 9.24 0.01 . 1 . . . . . . . . 4943 2 199 . 1 1 55 55 ILE HA H 1 4.29 0.01 . 1 . . . . . . . . 4943 2 200 . 1 1 55 55 ILE HB H 1 1.64 0.01 . 1 . . . . . . . . 4943 2 201 . 1 1 56 56 LEU H H 1 8.89 0.01 . 1 . . . . . . . . 4943 2 202 . 1 1 56 56 LEU HA H 1 4.41 0.01 . 1 . . . . . . . . 4943 2 203 . 1 1 56 56 LEU HB2 H 1 1.73 0.01 . 2 . . . . . . . . 4943 2 204 . 1 1 56 56 LEU HB3 H 1 1.46 0.01 . 2 . . . . . . . . 4943 2 205 . 1 1 57 57 GLN H H 1 7.91 0.01 . 1 . . . . . . . . 4943 2 206 . 1 1 57 57 GLN HA H 1 3.37 0.01 . 1 . . . . . . . . 4943 2 207 . 1 1 57 57 GLN HB2 H 1 2.23 0.01 . 2 . . . . . . . . 4943 2 208 . 1 1 57 57 GLN HB3 H 1 2.16 0.01 . 2 . . . . . . . . 4943 2 209 . 1 1 58 58 ILE H H 1 7.72 0.01 . 1 . . . . . . . . 4943 2 210 . 1 1 58 58 ILE HA H 1 4.05 0.01 . 1 . . . . . . . . 4943 2 211 . 1 1 58 58 ILE HB H 1 1.85 0.01 . 1 . . . . . . . . 4943 2 212 . 1 1 59 59 ASN H H 1 8.58 0.01 . 1 . . . . . . . . 4943 2 213 . 1 1 59 59 ASN HA H 1 5.64 0.01 . 1 . . . . . . . . 4943 2 214 . 1 1 59 59 ASN HB2 H 1 3.46 0.01 . 2 . . . . . . . . 4943 2 215 . 1 1 59 59 ASN HB3 H 1 3.00 0.01 . 2 . . . . . . . . 4943 2 216 . 1 1 60 60 SER H H 1 9.18 0.01 . 1 . . . . . . . . 4943 2 217 . 1 1 60 60 SER HA H 1 5.16 0.01 . 1 . . . . . . . . 4943 2 218 . 1 1 60 60 SER HB2 H 1 4.42 0.01 . 1 . . . . . . . . 4943 2 219 . 1 1 60 60 SER HB3 H 1 4.42 0.01 . 1 . . . . . . . . 4943 2 220 . 1 1 61 61 ARG H H 1 8.75 0.01 . 1 . . . . . . . . 4943 2 221 . 1 1 61 61 ARG HA H 1 4.10 0.01 . 1 . . . . . . . . 4943 2 222 . 1 1 61 61 ARG HB2 H 1 1.71 0.01 . 2 . . . . . . . . 4943 2 223 . 1 1 61 61 ARG HB3 H 1 1.45 0.01 . 2 . . . . . . . . 4943 2 224 . 1 1 62 62 TRP H H 1 7.13 0.01 . 1 . . . . . . . . 4943 2 225 . 1 1 62 62 TRP HA H 1 4.41 0.01 . 1 . . . . . . . . 4943 2 226 . 1 1 62 62 TRP HB2 H 1 1.84 0.01 . 1 . . . . . . . . 4943 2 227 . 1 1 62 62 TRP HB3 H 1 1.84 0.01 . 1 . . . . . . . . 4943 2 228 . 1 1 63 63 TRP H H 1 7.45 0.01 . 1 . . . . . . . . 4943 2 229 . 1 1 63 63 TRP HA H 1 4.99 0.01 . 1 . . . . . . . . 4943 2 230 . 1 1 63 63 TRP HB2 H 1 3.44 0.01 . 2 . . . . . . . . 4943 2 231 . 1 1 63 63 TRP HB3 H 1 3.35 0.01 . 2 . . . . . . . . 4943 2 232 . 1 1 64 64 CYS H H 1 7.59 0.01 . 1 . . . . . . . . 4943 2 233 . 1 1 64 64 CYS HA H 1 5.83 0.01 . 1 . . . . . . . . 4943 2 234 . 1 1 64 64 CYS HB2 H 1 3.05 0.01 . 2 . . . . . . . . 4943 2 235 . 1 1 64 64 CYS HB3 H 1 2.54 0.01 . 2 . . . . . . . . 4943 2 236 . 1 1 65 65 ASN H H 1 8.27 0.01 . 1 . . . . . . . . 4943 2 237 . 1 1 65 65 ASN HA H 1 5.53 0.01 . 1 . . . . . . . . 4943 2 238 . 1 1 65 65 ASN HB2 H 1 2.84 0.01 . 2 . . . . . . . . 4943 2 239 . 1 1 65 65 ASN HB3 H 1 2.46 0.01 . 2 . . . . . . . . 4943 2 240 . 1 1 66 66 ASP H H 1 9.70 0.01 . 1 . . . . . . . . 4943 2 241 . 1 1 66 66 ASP HA H 1 4.99 0.01 . 1 . . . . . . . . 4943 2 242 . 1 1 66 66 ASP HB2 H 1 3.29 0.01 . 2 . . . . . . . . 4943 2 243 . 1 1 66 66 ASP HB3 H 1 2.23 0.01 . 2 . . . . . . . . 4943 2 244 . 1 1 67 67 GLY H H 1 8.33 0.01 . 1 . . . . . . . . 4943 2 245 . 1 1 67 67 GLY HA2 H 1 4.15 0.01 . 2 . . . . . . . . 4943 2 246 . 1 1 67 67 GLY HA3 H 1 3.85 0.01 . 2 . . . . . . . . 4943 2 247 . 1 1 68 68 ARG H H 1 8.07 0.01 . 1 . . . . . . . . 4943 2 248 . 1 1 68 68 ARG HA H 1 4.77 0.01 . 1 . . . . . . . . 4943 2 249 . 1 1 68 68 ARG HB2 H 1 1.83 0.01 . 1 . . . . . . . . 4943 2 250 . 1 1 68 68 ARG HB3 H 1 1.83 0.01 . 1 . . . . . . . . 4943 2 251 . 1 1 69 69 THR H H 1 8.19 0.01 . 1 . . . . . . . . 4943 2 252 . 1 1 69 69 THR HA H 1 4.60 0.01 . 1 . . . . . . . . 4943 2 253 . 1 1 69 69 THR HB H 1 4.18 0.01 . 1 . . . . . . . . 4943 2 254 . 1 1 70 70 PRO HA H 1 4.32 0.01 . 1 . . . . . . . . 4943 2 255 . 1 1 70 70 PRO HB2 H 1 2.30 0.01 . 2 . . . . . . . . 4943 2 256 . 1 1 70 70 PRO HB3 H 1 2.12 0.01 . 2 . . . . . . . . 4943 2 257 . 1 1 71 71 GLY H H 1 8.69 0.01 . 1 . . . . . . . . 4943 2 258 . 1 1 71 71 GLY HA2 H 1 3.83 0.01 . 2 . . . . . . . . 4943 2 259 . 1 1 71 71 GLY HA3 H 1 3.67 0.01 . 2 . . . . . . . . 4943 2 260 . 1 1 72 72 SER H H 1 7.29 0.01 . 1 . . . . . . . . 4943 2 261 . 1 1 72 72 SER HA H 1 4.56 0.01 . 1 . . . . . . . . 4943 2 262 . 1 1 72 72 SER HB2 H 1 4.25 0.01 . 2 . . . . . . . . 4943 2 263 . 1 1 72 72 SER HB3 H 1 3.77 0.01 . 2 . . . . . . . . 4943 2 264 . 1 1 73 73 ARG H H 1 8.03 0.01 . 1 . . . . . . . . 4943 2 265 . 1 1 73 73 ARG HA H 1 4.23 0.01 . 1 . . . . . . . . 4943 2 266 . 1 1 73 73 ARG HB2 H 1 1.67 0.01 . 2 . . . . . . . . 4943 2 267 . 1 1 73 73 ARG HB3 H 1 1.53 0.01 . 2 . . . . . . . . 4943 2 268 . 1 1 74 74 ASN H H 1 8.20 0.01 . 1 . . . . . . . . 4943 2 269 . 1 1 74 74 ASN HA H 1 3.75 0.01 . 1 . . . . . . . . 4943 2 270 . 1 1 74 74 ASN HB2 H 1 3.08 0.01 . 2 . . . . . . . . 4943 2 271 . 1 1 74 74 ASN HB3 H 1 2.00 0.01 . 2 . . . . . . . . 4943 2 272 . 1 1 75 75 LEU H H 1 9.03 0.01 . 1 . . . . . . . . 4943 2 273 . 1 1 75 75 LEU HA H 1 4.09 0.01 . 1 . . . . . . . . 4943 2 274 . 1 1 75 75 LEU HB2 H 1 2.12 0.01 . 2 . . . . . . . . 4943 2 275 . 1 1 75 75 LEU HB3 H 1 1.48 0.01 . 2 . . . . . . . . 4943 2 276 . 1 1 76 76 CYS H H 1 9.48 0.01 . 1 . . . . . . . . 4943 2 277 . 1 1 76 76 CYS HA H 1 4.46 0.01 . 1 . . . . . . . . 4943 2 278 . 1 1 76 76 CYS HB2 H 1 3.67 0.01 . 1 . . . . . . . . 4943 2 279 . 1 1 76 76 CYS HB3 H 1 3.67 0.01 . 1 . . . . . . . . 4943 2 280 . 1 1 77 77 ASN H H 1 8.04 0.01 . 1 . . . . . . . . 4943 2 281 . 1 1 77 77 ASN HA H 1 4.22 0.01 . 1 . . . . . . . . 4943 2 282 . 1 1 77 77 ASN HB2 H 1 3.18 0.01 . 2 . . . . . . . . 4943 2 283 . 1 1 77 77 ASN HB3 H 1 2.50 0.01 . 2 . . . . . . . . 4943 2 284 . 1 1 78 78 ILE H H 1 8.79 0.01 . 1 . . . . . . . . 4943 2 285 . 1 1 78 78 ILE HA H 1 4.99 0.01 . 1 . . . . . . . . 4943 2 286 . 1 1 78 78 ILE HB H 1 1.70 0.01 . 1 . . . . . . . . 4943 2 287 . 1 1 79 79 PRO HA H 1 5.18 0.01 . 1 . . . . . . . . 4943 2 288 . 1 1 79 79 PRO HB2 H 1 2.37 0.01 . 2 . . . . . . . . 4943 2 289 . 1 1 79 79 PRO HB3 H 1 2.01 0.01 . 2 . . . . . . . . 4943 2 290 . 1 1 80 80 CYS H H 1 8.26 0.01 . 1 . . . . . . . . 4943 2 291 . 1 1 80 80 CYS HA H 1 3.89 0.01 . 1 . . . . . . . . 4943 2 292 . 1 1 80 80 CYS HB2 H 1 1.73 0.01 . 2 . . . . . . . . 4943 2 293 . 1 1 80 80 CYS HB3 H 1 1.31 0.01 . 2 . . . . . . . . 4943 2 294 . 1 1 81 81 SER H H 1 8.58 0.01 . 1 . . . . . . . . 4943 2 295 . 1 1 81 81 SER HA H 1 3.79 0.01 . 1 . . . . . . . . 4943 2 296 . 1 1 81 81 SER HB2 H 1 3.90 0.01 . 1 . . . . . . . . 4943 2 297 . 1 1 81 81 SER HB3 H 1 3.90 0.01 . 1 . . . . . . . . 4943 2 298 . 1 1 82 82 ALA H H 1 7.61 0.01 . 1 . . . . . . . . 4943 2 299 . 1 1 82 82 ALA HA H 1 4.24 0.01 . 1 . . . . . . . . 4943 2 300 . 1 1 82 82 ALA HB1 H 1 1.50 0.01 . 1 . . . . . . . . 4943 2 301 . 1 1 82 82 ALA HB2 H 1 1.50 0.01 . 1 . . . . . . . . 4943 2 302 . 1 1 82 82 ALA HB3 H 1 1.50 0.01 . 1 . . . . . . . . 4943 2 303 . 1 1 83 83 LEU H H 1 7.85 0.01 . 1 . . . . . . . . 4943 2 304 . 1 1 83 83 LEU HA H 1 4.25 0.01 . 1 . . . . . . . . 4943 2 305 . 1 1 83 83 LEU HB2 H 1 2.08 0.01 . 2 . . . . . . . . 4943 2 306 . 1 1 83 83 LEU HB3 H 1 1.66 0.01 . 2 . . . . . . . . 4943 2 307 . 1 1 84 84 LEU H H 1 7.12 0.01 . 1 . . . . . . . . 4943 2 308 . 1 1 84 84 LEU HA H 1 5.10 0.01 . 1 . . . . . . . . 4943 2 309 . 1 1 84 84 LEU HB2 H 1 1.90 0.01 . 2 . . . . . . . . 4943 2 310 . 1 1 84 84 LEU HB3 H 1 1.70 0.01 . 2 . . . . . . . . 4943 2 311 . 1 1 85 85 SER H H 1 6.84 0.01 . 1 . . . . . . . . 4943 2 312 . 1 1 85 85 SER HA H 1 4.50 0.01 . 1 . . . . . . . . 4943 2 313 . 1 1 85 85 SER HB2 H 1 4.15 0.01 . 2 . . . . . . . . 4943 2 314 . 1 1 85 85 SER HB3 H 1 3.87 0.01 . 2 . . . . . . . . 4943 2 315 . 1 1 86 86 SER H H 1 8.50 0.01 . 1 . . . . . . . . 4943 2 316 . 1 1 86 86 SER HA H 1 4.28 0.01 . 1 . . . . . . . . 4943 2 317 . 1 1 86 86 SER HB2 H 1 3.92 0.01 . 2 . . . . . . . . 4943 2 318 . 1 1 86 86 SER HB3 H 1 3.86 0.01 . 2 . . . . . . . . 4943 2 319 . 1 1 87 87 ASP H H 1 8.16 0.01 . 1 . . . . . . . . 4943 2 320 . 1 1 87 87 ASP HA H 1 4.93 0.01 . 1 . . . . . . . . 4943 2 321 . 1 1 87 87 ASP HB2 H 1 2.93 0.01 . 2 . . . . . . . . 4943 2 322 . 1 1 87 87 ASP HB3 H 1 2.65 0.01 . 2 . . . . . . . . 4943 2 323 . 1 1 88 88 ILE H H 1 8.10 0.01 . 1 . . . . . . . . 4943 2 324 . 1 1 88 88 ILE HA H 1 4.65 0.01 . 1 . . . . . . . . 4943 2 325 . 1 1 88 88 ILE HB H 1 1.85 0.01 . 1 . . . . . . . . 4943 2 326 . 1 1 89 89 THR H H 1 8.35 0.01 . 1 . . . . . . . . 4943 2 327 . 1 1 89 89 THR HA H 1 3.05 0.01 . 1 . . . . . . . . 4943 2 328 . 1 1 89 89 THR HB H 1 3.98 0.01 . 1 . . . . . . . . 4943 2 329 . 1 1 90 90 ALA H H 1 9.10 0.01 . 1 . . . . . . . . 4943 2 330 . 1 1 90 90 ALA HA H 1 4.08 0.01 . 1 . . . . . . . . 4943 2 331 . 1 1 90 90 ALA HB1 H 1 1.34 0.01 . 1 . . . . . . . . 4943 2 332 . 1 1 90 90 ALA HB2 H 1 1.34 0.01 . 1 . . . . . . . . 4943 2 333 . 1 1 90 90 ALA HB3 H 1 1.34 0.01 . 1 . . . . . . . . 4943 2 334 . 1 1 91 91 SER H H 1 7.78 0.01 . 1 . . . . . . . . 4943 2 335 . 1 1 91 91 SER HA H 1 4.09 0.01 . 1 . . . . . . . . 4943 2 336 . 1 1 91 91 SER HB2 H 1 3.99 0.01 . 2 . . . . . . . . 4943 2 337 . 1 1 91 91 SER HB3 H 1 3.49 0.01 . 2 . . . . . . . . 4943 2 338 . 1 1 92 92 VAL H H 1 8.37 0.01 . 1 . . . . . . . . 4943 2 339 . 1 1 92 92 VAL HA H 1 3.13 0.01 . 1 . . . . . . . . 4943 2 340 . 1 1 92 92 VAL HB H 1 1.89 0.01 . 1 . . . . . . . . 4943 2 341 . 1 1 93 93 ASN H H 1 8.63 0.01 . 1 . . . . . . . . 4943 2 342 . 1 1 93 93 ASN HA H 1 4.26 0.01 . 1 . . . . . . . . 4943 2 343 . 1 1 93 93 ASN HB2 H 1 2.88 0.01 . 2 . . . . . . . . 4943 2 344 . 1 1 93 93 ASN HB3 H 1 2.77 0.01 . 2 . . . . . . . . 4943 2 345 . 1 1 94 94 CYS H H 1 7.89 0.01 . 1 . . . . . . . . 4943 2 346 . 1 1 94 94 CYS HA H 1 5.00 0.01 . 1 . . . . . . . . 4943 2 347 . 1 1 94 94 CYS HB2 H 1 3.37 0.01 . 2 . . . . . . . . 4943 2 348 . 1 1 94 94 CYS HB3 H 1 2.71 0.01 . 2 . . . . . . . . 4943 2 349 . 1 1 95 95 ALA H H 1 8.70 0.01 . 1 . . . . . . . . 4943 2 350 . 1 1 95 95 ALA HA H 1 4.12 0.01 . 1 . . . . . . . . 4943 2 351 . 1 1 95 95 ALA HB1 H 1 1.53 0.01 . 1 . . . . . . . . 4943 2 352 . 1 1 95 95 ALA HB2 H 1 1.53 0.01 . 1 . . . . . . . . 4943 2 353 . 1 1 95 95 ALA HB3 H 1 1.53 0.01 . 1 . . . . . . . . 4943 2 354 . 1 1 96 96 LYS H H 1 8.03 0.01 . 1 . . . . . . . . 4943 2 355 . 1 1 96 96 LYS HA H 1 3.73 0.01 . 1 . . . . . . . . 4943 2 356 . 1 1 96 96 LYS HB2 H 1 1.68 0.01 . 1 . . . . . . . . 4943 2 357 . 1 1 96 96 LYS HB3 H 1 1.68 0.01 . 1 . . . . . . . . 4943 2 358 . 1 1 97 97 LYS H H 1 7.23 0.01 . 1 . . . . . . . . 4943 2 359 . 1 1 97 97 LYS HA H 1 4.16 0.01 . 1 . . . . . . . . 4943 2 360 . 1 1 97 97 LYS HB2 H 1 2.24 0.01 . 2 . . . . . . . . 4943 2 361 . 1 1 97 97 LYS HB3 H 1 2.13 0.01 . 2 . . . . . . . . 4943 2 362 . 1 1 98 98 ILE H H 1 7.98 0.01 . 1 . . . . . . . . 4943 2 363 . 1 1 98 98 ILE HA H 1 2.80 0.01 . 1 . . . . . . . . 4943 2 364 . 1 1 98 98 ILE HB H 1 1.49 0.01 . 1 . . . . . . . . 4943 2 365 . 1 1 99 99 VAL H H 1 8.23 0.01 . 1 . . . . . . . . 4943 2 366 . 1 1 99 99 VAL HA H 1 3.89 0.01 . 1 . . . . . . . . 4943 2 367 . 1 1 99 99 VAL HB H 1 2.41 0.01 . 1 . . . . . . . . 4943 2 368 . 1 1 100 100 SER H H 1 7.68 0.01 . 1 . . . . . . . . 4943 2 369 . 1 1 100 100 SER HA H 1 4.43 0.01 . 1 . . . . . . . . 4943 2 370 . 1 1 100 100 SER HB2 H 1 4.20 0.01 . 2 . . . . . . . . 4943 2 371 . 1 1 100 100 SER HB3 H 1 4.10 0.01 . 2 . . . . . . . . 4943 2 372 . 1 1 101 101 ASP H H 1 7.99 0.01 . 1 . . . . . . . . 4943 2 373 . 1 1 101 101 ASP HA H 1 4.76 0.01 . 1 . . . . . . . . 4943 2 374 . 1 1 101 101 ASP HB2 H 1 2.99 0.01 . 1 . . . . . . . . 4943 2 375 . 1 1 101 101 ASP HB3 H 1 2.99 0.01 . 1 . . . . . . . . 4943 2 376 . 1 1 102 102 GLY H H 1 8.17 0.01 . 1 . . . . . . . . 4943 2 377 . 1 1 102 102 GLY HA2 H 1 4.11 0.01 . 2 . . . . . . . . 4943 2 378 . 1 1 102 102 GLY HA3 H 1 4.00 0.01 . 2 . . . . . . . . 4943 2 379 . 1 1 103 103 ASN H H 1 8.23 0.01 . 1 . . . . . . . . 4943 2 380 . 1 1 103 103 ASN HA H 1 4.93 0.01 . 1 . . . . . . . . 4943 2 381 . 1 1 103 103 ASN HB2 H 1 2.79 0.01 . 2 . . . . . . . . 4943 2 382 . 1 1 103 103 ASN HB3 H 1 2.72 0.01 . 2 . . . . . . . . 4943 2 383 . 1 1 104 104 GLY H H 1 8.21 0.01 . 1 . . . . . . . . 4943 2 384 . 1 1 104 104 GLY HA2 H 1 4.22 0.01 . 2 . . . . . . . . 4943 2 385 . 1 1 104 104 GLY HA3 H 1 4.08 0.01 . 2 . . . . . . . . 4943 2 386 . 1 1 105 105 MET H H 1 7.09 0.01 . 1 . . . . . . . . 4943 2 387 . 1 1 105 105 MET HA H 1 3.82 0.01 . 1 . . . . . . . . 4943 2 388 . 1 1 105 105 MET HB2 H 1 0.43 0.01 . 2 . . . . . . . . 4943 2 389 . 1 1 105 105 MET HB3 H 1 -0.98 0.01 . 2 . . . . . . . . 4943 2 390 . 1 1 106 106 ASN H H 1 7.64 0.01 . 1 . . . . . . . . 4943 2 391 . 1 1 106 106 ASN HA H 1 4.47 0.01 . 1 . . . . . . . . 4943 2 392 . 1 1 106 106 ASN HB2 H 1 3.03 0.01 . 2 . . . . . . . . 4943 2 393 . 1 1 106 106 ASN HB3 H 1 2.81 0.01 . 2 . . . . . . . . 4943 2 394 . 1 1 107 107 ALA H H 1 6.80 0.01 . 1 . . . . . . . . 4943 2 395 . 1 1 107 107 ALA HA H 1 3.85 0.01 . 1 . . . . . . . . 4943 2 396 . 1 1 107 107 ALA HB1 H 1 0.62 0.01 . 1 . . . . . . . . 4943 2 397 . 1 1 107 107 ALA HB2 H 1 0.62 0.01 . 1 . . . . . . . . 4943 2 398 . 1 1 107 107 ALA HB3 H 1 0.62 0.01 . 1 . . . . . . . . 4943 2 399 . 1 1 108 108 TRP H H 1 7.86 0.01 . 1 . . . . . . . . 4943 2 400 . 1 1 108 108 TRP HA H 1 4.70 0.01 . 1 . . . . . . . . 4943 2 401 . 1 1 108 108 TRP HB2 H 1 3.35 0.01 . 2 . . . . . . . . 4943 2 402 . 1 1 108 108 TRP HB3 H 1 3.27 0.01 . 2 . . . . . . . . 4943 2 403 . 1 1 109 109 VAL H H 1 8.95 0.01 . 1 . . . . . . . . 4943 2 404 . 1 1 109 109 VAL HA H 1 3.63 0.01 . 1 . . . . . . . . 4943 2 405 . 1 1 109 109 VAL HB H 1 2.17 0.01 . 1 . . . . . . . . 4943 2 406 . 1 1 110 110 ALA H H 1 8.04 0.01 . 1 . . . . . . . . 4943 2 407 . 1 1 110 110 ALA HA H 1 4.27 0.01 . 1 . . . . . . . . 4943 2 408 . 1 1 110 110 ALA HB1 H 1 1.33 0.01 . 1 . . . . . . . . 4943 2 409 . 1 1 110 110 ALA HB2 H 1 1.33 0.01 . 1 . . . . . . . . 4943 2 410 . 1 1 110 110 ALA HB3 H 1 1.33 0.01 . 1 . . . . . . . . 4943 2 411 . 1 1 111 111 TRP H H 1 7.25 0.01 . 1 . . . . . . . . 4943 2 412 . 1 1 111 111 TRP HA H 1 3.72 0.01 . 1 . . . . . . . . 4943 2 413 . 1 1 111 111 TRP HB2 H 1 4.06 0.01 . 2 . . . . . . . . 4943 2 414 . 1 1 111 111 TRP HB3 H 1 2.79 0.01 . 2 . . . . . . . . 4943 2 415 . 1 1 112 112 ARG H H 1 8.26 0.01 . 1 . . . . . . . . 4943 2 416 . 1 1 112 112 ARG HA H 1 3.38 0.01 . 1 . . . . . . . . 4943 2 417 . 1 1 112 112 ARG HB2 H 1 2.12 0.01 . 2 . . . . . . . . 4943 2 418 . 1 1 112 112 ARG HB3 H 1 2.01 0.01 . 2 . . . . . . . . 4943 2 419 . 1 1 113 113 ASN H H 1 7.97 0.01 . 1 . . . . . . . . 4943 2 420 . 1 1 113 113 ASN HA H 1 4.53 0.01 . 1 . . . . . . . . 4943 2 421 . 1 1 113 113 ASN HB2 H 1 2.68 0.01 . 1 . . . . . . . . 4943 2 422 . 1 1 113 113 ASN HB3 H 1 2.68 0.01 . 1 . . . . . . . . 4943 2 423 . 1 1 114 114 ARG H H 1 7.66 0.01 . 1 . . . . . . . . 4943 2 424 . 1 1 114 114 ARG HA H 1 4.32 0.01 . 1 . . . . . . . . 4943 2 425 . 1 1 114 114 ARG HB2 H 1 1.19 0.01 . 2 . . . . . . . . 4943 2 426 . 1 1 114 114 ARG HB3 H 1 0.60 0.01 . 2 . . . . . . . . 4943 2 427 . 1 1 115 115 CYS H H 1 7.33 0.01 . 1 . . . . . . . . 4943 2 428 . 1 1 115 115 CYS HA H 1 4.54 0.01 . 1 . . . . . . . . 4943 2 429 . 1 1 115 115 CYS HB2 H 1 2.61 0.01 . 2 . . . . . . . . 4943 2 430 . 1 1 115 115 CYS HB3 H 1 2.48 0.01 . 2 . . . . . . . . 4943 2 431 . 1 1 116 116 LYS H H 1 7.06 0.01 . 1 . . . . . . . . 4943 2 432 . 1 1 116 116 LYS HA H 1 3.44 0.01 . 1 . . . . . . . . 4943 2 433 . 1 1 116 116 LYS HB2 H 1 -0.17 0.01 . 2 . . . . . . . . 4943 2 434 . 1 1 116 116 LYS HB3 H 1 1.22 0.01 . 2 . . . . . . . . 4943 2 435 . 1 1 117 117 GLY H H 1 8.70 0.01 . 1 . . . . . . . . 4943 2 436 . 1 1 117 117 GLY HA2 H 1 4.12 0.01 . 2 . . . . . . . . 4943 2 437 . 1 1 117 117 GLY HA3 H 1 3.81 0.01 . 2 . . . . . . . . 4943 2 438 . 1 1 118 118 THR H H 1 7.65 0.01 . 1 . . . . . . . . 4943 2 439 . 1 1 118 118 THR HA H 1 4.75 0.01 . 1 . . . . . . . . 4943 2 440 . 1 1 118 118 THR HB H 1 4.31 0.01 . 1 . . . . . . . . 4943 2 441 . 1 1 119 119 ASP H H 1 8.64 0.01 . 1 . . . . . . . . 4943 2 442 . 1 1 119 119 ASP HA H 1 5.00 0.01 . 1 . . . . . . . . 4943 2 443 . 1 1 119 119 ASP HB2 H 1 2.93 0.01 . 2 . . . . . . . . 4943 2 444 . 1 1 119 119 ASP HB3 H 1 2.71 0.01 . 2 . . . . . . . . 4943 2 445 . 1 1 120 120 VAL H H 1 8.12 0.01 . 1 . . . . . . . . 4943 2 446 . 1 1 120 120 VAL HA H 1 4.35 0.01 . 1 . . . . . . . . 4943 2 447 . 1 1 120 120 VAL HB H 1 2.17 0.01 . 1 . . . . . . . . 4943 2 448 . 1 1 121 121 GLN H H 1 8.44 0.01 . 1 . . . . . . . . 4943 2 449 . 1 1 121 121 GLN HA H 1 4.33 0.01 . 1 . . . . . . . . 4943 2 450 . 1 1 121 121 GLN HB2 H 1 2.27 0.01 . 2 . . . . . . . . 4943 2 451 . 1 1 121 121 GLN HB3 H 1 2.19 0.01 . 2 . . . . . . . . 4943 2 452 . 1 1 122 122 ALA H H 1 7.71 0.01 . 1 . . . . . . . . 4943 2 453 . 1 1 122 122 ALA HA H 1 3.82 0.01 . 1 . . . . . . . . 4943 2 454 . 1 1 122 122 ALA HB1 H 1 1.17 0.01 . 1 . . . . . . . . 4943 2 455 . 1 1 122 122 ALA HB2 H 1 1.17 0.01 . 1 . . . . . . . . 4943 2 456 . 1 1 122 122 ALA HB3 H 1 1.17 0.01 . 1 . . . . . . . . 4943 2 457 . 1 1 123 123 TRP H H 1 7.58 0.01 . 1 . . . . . . . . 4943 2 458 . 1 1 123 123 TRP HA H 1 4.12 0.01 . 1 . . . . . . . . 4943 2 459 . 1 1 123 123 TRP HB2 H 1 3.51 0.01 . 2 . . . . . . . . 4943 2 460 . 1 1 123 123 TRP HB3 H 1 3.41 0.01 . 2 . . . . . . . . 4943 2 461 . 1 1 124 124 ILE H H 1 7.56 0.01 . 1 . . . . . . . . 4943 2 462 . 1 1 124 124 ILE HA H 1 4.73 0.01 . 1 . . . . . . . . 4943 2 463 . 1 1 124 124 ILE HB H 1 2.22 0.01 . 1 . . . . . . . . 4943 2 464 . 1 1 125 125 ARG H H 1 7.33 0.01 . 1 . . . . . . . . 4943 2 465 . 1 1 125 125 ARG HA H 1 4.16 0.01 . 1 . . . . . . . . 4943 2 466 . 1 1 125 125 ARG HB2 H 1 1.83 0.01 . 2 . . . . . . . . 4943 2 467 . 1 1 125 125 ARG HB3 H 1 1.76 0.01 . 2 . . . . . . . . 4943 2 468 . 1 1 126 126 GLY H H 1 9.13 0.01 . 1 . . . . . . . . 4943 2 469 . 1 1 126 126 GLY HA2 H 1 4.30 0.01 . 2 . . . . . . . . 4943 2 470 . 1 1 126 126 GLY HA3 H 1 3.75 0.01 . 2 . . . . . . . . 4943 2 471 . 1 1 127 127 CYS H H 1 7.47 0.01 . 1 . . . . . . . . 4943 2 472 . 1 1 127 127 CYS HA H 1 4.92 0.01 . 1 . . . . . . . . 4943 2 473 . 1 1 127 127 CYS HB2 H 1 3.08 0.01 . 2 . . . . . . . . 4943 2 474 . 1 1 127 127 CYS HB3 H 1 2.65 0.01 . 2 . . . . . . . . 4943 2 475 . 1 1 128 128 ARG H H 1 8.89 0.01 . 1 . . . . . . . . 4943 2 476 . 1 1 128 128 ARG HA H 1 4.36 0.01 . 1 . . . . . . . . 4943 2 477 . 1 1 128 128 ARG HB2 H 1 1.87 0.01 . 2 . . . . . . . . 4943 2 478 . 1 1 128 128 ARG HB3 H 1 1.79 0.01 . 2 . . . . . . . . 4943 2 479 . 1 1 129 129 LEU H H 1 7.93 0.01 . 1 . . . . . . . . 4943 2 480 . 1 1 129 129 LEU HA H 1 4.28 0.01 . 1 . . . . . . . . 4943 2 481 . 1 1 129 129 LEU HB2 H 1 1.65 0.01 . 2 . . . . . . . . 4943 2 482 . 1 1 129 129 LEU HB3 H 1 1.47 0.01 . 2 . . . . . . . . 4943 2 stop_ save_