data_7154 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 7154 _Entry.Title ; NMR spectroscopy of T4 Lysozyme peptide fragments ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2006-06-07 _Entry.Accession_date 2006-06-07 _Entry.Last_release_date 2008-11-12 _Entry.Original_release_date 2008-11-12 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version . _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 L. Najbar . V. . 7154 2 D. Craik . J. . 7154 3 J. Wade . D. . 7154 4 M. McLeish . J. . 7154 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 7154 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 105 7154 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 . . 2008-11-12 2006-06-07 original author . 7154 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID . 7155 'helix G (lys 124-137)' 7154 . 7156 'helix H (lys 136-157)' 7154 . 7157 'helix F (lys 113-125)' 7154 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 7154 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10801343 _Citation.Full_citation . _Citation.Title 'Identification of initiation sites for T4 lysozyme folding using CD and NMR spectroscopy of peptide fragments' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 39 _Citation.Journal_issue 19 _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 5911 _Citation.Page_last 5920 _Citation.Year 2000 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 L. Najbar . V. . 7154 1 2 D. Craik . J. . 7154 1 3 J. Wade . D. . 7154 1 4 M. McLeish . J. . 7154 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 7154 _Assembly.ID 1 _Assembly.Name 'HELIX E' _Assembly.BMRB_code . _Assembly.Number_of_components 1 _Assembly.Organic_ligands 0 _Assembly.Metal_ions 0 _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states no _Assembly.Ambiguous_chem_comp_sites no _Assembly.Molecules_in_chemical_exchange no _Assembly.Paramagnetic no _Assembly.Thiol_state 'not present' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . 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 'fragment corresponding to Lys Helix E (residues 92-107)' 1 $HELIX_E . . yes unfolded no no . . . 7154 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_HELIX_E _Entity.Sf_category entity _Entity.Sf_framecode HELIX_E _Entity.Entry_ID 7154 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'helix E (lys 92-107)' _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 DAVRRAALINMVFQMG _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 16 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _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 PDB 102L . "How Amino-Acid Insertions Are Allowed In An Alpha-Helix Of T4 Lysozyme" . . . . . 100.00 165 100.00 100.00 5.65e-01 . . . . 7154 1 2 no PDB 103L . "How Amino-Acid Insertions Are Allowed In An Alpha-Helix Of T4 Lysozyme" . . . . . 100.00 167 100.00 100.00 1.31e+00 . . . . 7154 1 3 no PDB 104L . "How Amino-Acid Insertions Are Allowed In An Alpha-Helix Of T4 Lysozyme" . . . . . 100.00 166 100.00 100.00 5.65e-01 . . . . 7154 1 4 no PDB 107L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.88e-01 . . . . 7154 1 5 no PDB 108L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.76e-01 . . . . 7154 1 6 no PDB 109L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.70e-01 . . . . 7154 1 7 no PDB 110L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.64e-01 . . . . 7154 1 8 no PDB 111L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.82e-01 . . . . 7154 1 9 no PDB 112L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.70e-01 . . . . 7154 1 10 no PDB 113L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.82e-01 . . . . 7154 1 11 no PDB 114L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.53e-01 . . . . 7154 1 12 no PDB 115L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.70e-01 . . . . 7154 1 13 no PDB 118L . "The Energetic Cost And The Structural Consequences Of Burying A Hydroxyl Group Within The Core Of A Protein Determined From Ala" . . . . . 100.00 164 100.00 100.00 1.13e+00 . . . . 7154 1 14 no PDB 119L . "The Energetic Cost And The Structural Consequences Of Burying A Hydroxyl Group Within The Core Of A Protein Determined From Ala" . . . . . 100.00 164 100.00 100.00 1.13e+00 . . . . 7154 1 15 no PDB 120L . "The Energetic Cost And The Structural Consequences Of Burying A Hydroxyl Group Within The Core Of A Protein Determined From Ala" . . . . . 100.00 164 100.00 100.00 1.13e+00 . . . . 7154 1 16 no PDB 122L . "The Energetic Cost And The Structural Consequences Of Burying A Hydroxyl Group Within The Core Of A Protein Determined From Ala" . . . . . 100.00 164 100.00 100.00 1.13e+00 . . . . 7154 1 17 no PDB 123L . "The Energetic Cost And The Structural Consequences Of Burying A Hydroxyl Group Within The Core Of A Protein Determined From Ala" . . . . . 100.00 164 100.00 100.00 1.13e+00 . . . . 7154 1 18 no PDB 126L . "The Energetic Cost And The Structural Consequences Of Burying A Hydroxyl Group Within The Core Of A Protein Determined From Ala" . . . . . 100.00 164 100.00 100.00 1.15e+00 . . . . 7154 1 19 no PDB 127L . "The Energetic Cost And The Structural Consequences Of Burying A Hydroxyl Group Within The Core Of A Protein Determined From Ala" . . . . . 100.00 164 100.00 100.00 1.15e+00 . . . . 7154 1 20 no PDB 128L . "The Energetic Cost And The Structural Consequences Of Burying A Hydroxyl Group Within The Core Of A Protein Determined From Ala" . . . . . 100.00 164 100.00 100.00 1.15e+00 . . . . 7154 1 21 no PDB 130L . "Structures Of Randomly Generated Mutants Of T4 Lysozyme Show That Protein Stability Can Be Enhanced By Relaxation Of Strain And" . . . . . 100.00 164 100.00 100.00 5.58e-01 . . . . 7154 1 22 no PDB 131L . "Structures Of Randomly Generated Mutants Of T4 Lysozyme Show That Protein Stability Can Be Enhanced By Relaxation Of Strain And" . . . . . 100.00 164 100.00 100.00 5.58e-01 . . . . 7154 1 23 no PDB 137L . "Structural Basis Of Amino Acid Alpha Helix Propensity" . . . . . 100.00 164 100.00 100.00 5.88e-01 . . . . 7154 1 24 no PDB 140L . "Role Of Backbone Flexibility In The Accommodation Of Variants That Repack The Core Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.47e-01 . . . . 7154 1 25 no PDB 141L . "Role Of Backbone Flexibility In The Accommodation Of Variants That Repack The Core Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.53e-01 . . . . 7154 1 26 no PDB 142L . "Role Of Backbone Flexibility In The Accommodation Of Variants That Repack The Core Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.25e-01 . . . . 7154 1 27 no PDB 143L . "Role Of Backbone Flexibility In The Accommodation Of Variants That Repack The Core Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.53e-01 . . . . 7154 1 28 no PDB 144L . "Role Of Backbone Flexibility In The Accommodation Of Variants That Repack The Core Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 1.26e+00 . . . . 7154 1 29 no PDB 145L . "Role Of Backbone Flexibility In The Accommodation Of Variants That Repack The Core Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.47e-01 . . . . 7154 1 30 no PDB 146L . "Role Of Backbone Flexibility In The Accommodation Of Variants That Repack The Core Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.41e-01 . . . . 7154 1 31 no PDB 147L . "Role Of Backbone Flexibility In The Accommodation Of Variants That Repack The Core Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.53e-01 . . . . 7154 1 32 no PDB 148L . "A Covalent Enzyme-Substrate Intermediate With Saccharide Distortion In A Mutant T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.70e-01 . . . . 7154 1 33 no PDB 155L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 100.00 100.00 5.94e-01 . . . . 7154 1 34 no PDB 156L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 100.00 100.00 5.53e-01 . . . . 7154 1 35 no PDB 157L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 100.00 100.00 5.64e-01 . . . . 7154 1 36 no PDB 158L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 100.00 100.00 5.53e-01 . . . . 7154 1 37 no PDB 159L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 100.00 100.00 5.30e-01 . . . . 7154 1 38 no PDB 160L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 100.00 100.00 1.23e+00 . . . . 7154 1 39 no PDB 161L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 100.00 100.00 5.53e-01 . . . . 7154 1 40 no PDB 162L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 100.00 100.00 5.53e-01 . . . . 7154 1 41 no PDB 163L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 100.00 100.00 5.53e-01 . . . . 7154 1 42 no PDB 164L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 100.00 100.00 5.41e-01 . . . . 7154 1 43 no PDB 165L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 100.00 100.00 5.76e-01 . . . . 7154 1 44 no PDB 166L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 100.00 100.00 5.76e-01 . . . . 7154 1 45 no PDB 171L . "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.64e-01 . . . . 7154 1 46 no PDB 174L . "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 6.66e-01 . . . . 7154 1 47 no PDB 176L . "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.76e-01 . . . . 7154 1 48 no PDB 177L . "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 8.98e-01 . . . . 7154 1 49 no PDB 178L . "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 8.98e-01 . . . . 7154 1 50 no PDB 180L . "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.70e-01 . . . . 7154 1 51 no PDB 192L . "A Helix Initiation Signal In T4 Lysozyme Identified By Polyalanine Mutagenesis" . . . . . 100.00 164 100.00 100.00 5.76e-01 . . . . 7154 1 52 no PDB 195L . 'Thermodynamic And Structural Compensation In "size-Switch" Core-Repacking Variants Of T4 Lysozyme' . . . . . 100.00 164 100.00 100.00 1.27e+00 . . . . 7154 1 53 no PDB 196L . 'Thermodynamic And Structural Compensation In "size-Switch" Core-Repacking Variants Of T4 Lysozyme' . . . . . 100.00 164 100.00 100.00 5.64e-01 . . . . 7154 1 54 no PDB 197L . 'Thermodynamic And Structural Compensation In "size-Switch" Core-Repacking Variants Of T4 Lysozyme' . . . . . 100.00 164 100.00 100.00 5.47e-01 . . . . 7154 1 55 no PDB 198L . 'Thermodynamic And Structural Compensation In "size-Switch" Core-Repacking Variants Of T4 Lysozyme' . . . . . 100.00 164 100.00 100.00 5.58e-01 . . . . 7154 1 56 no PDB 199L . 'Thermodynamic And Structural Compensation In "size-Switch" Core-Repacking Variants Of T4 Lysozyme' . . . . . 100.00 164 100.00 100.00 5.64e-01 . . . . 7154 1 57 no PDB 1B6I . "T4 Lysozyme Mutant With Cys 54 Replaced By Thr, Cys 97 Replaced By Ala, Thr 21 Replaced By Cys And Lys 124 Replaced By Cys (C54" . . . . . 100.00 164 100.00 100.00 6.59e-01 . . . . 7154 1 58 no PDB 1C60 . "T4 Lysozyme Mutant C54tC97AF153A IN THE PRESENCE OF 8 ATM Argon" . . . . . 100.00 164 100.00 100.00 5.25e-01 . . . . 7154 1 59 no PDB 1C61 . "T4 Lysozyme Mutant C54tC97AF153A IN THE PRESENCE OF 8 ATM Krypton" . . . . . 100.00 164 100.00 100.00 5.25e-01 . . . . 7154 1 60 no PDB 1C62 . "T4 Lysozyme Mutant C54tC97AF153A IN THE PRESENCE OF 8 ATM Xenon" . . . . . 100.00 164 100.00 100.00 5.25e-01 . . . . 7154 1 61 no PDB 1C63 . "T4 Lysozyme Mutant C54tC97AL121A IN THE PRESENCE OF 8 ATM Argon" . . . . . 100.00 164 100.00 100.00 5.47e-01 . . . . 7154 1 62 no PDB 1C64 . "T4 Lysozyme Mutant C54tC97AL121A IN THE PRESENCE OF 8 ATM Krypton" . . . . . 100.00 164 100.00 100.00 5.47e-01 . . . . 7154 1 63 no PDB 1C65 . "T4 Lysozyme Mutant C54tC97AL121A IN THE PRESENCE OF 8 ATM Xenon" . . . . . 100.00 164 100.00 100.00 5.47e-01 . . . . 7154 1 64 no PDB 1C66 . "T4 Lysozyme Mutant C54tC97AL121AL133A IN THE PRESENCE OF 8 Atm Argon" . . . . . 100.00 164 100.00 100.00 5.47e-01 . . . . 7154 1 65 no PDB 1C67 . "T4 Lysozyme Mutant C54tC97AL121AL133A IN THE PRESENCE OF 8 Atm Krypton" . . . . . 100.00 164 100.00 100.00 5.47e-01 . . . . 7154 1 66 no PDB 1C68 . "T4 Lysozyme Mutant C54tC97AL121AL133A IN THE PRESENCE OF 8 Atm Xenon" . . . . . 100.00 164 100.00 100.00 5.47e-01 . . . . 7154 1 67 no PDB 1C6P . "T4 Lysozyme Mutant C54tC97A IN THE PRESENCE OF 8 ATM ARGON" . . . . . 100.00 164 100.00 100.00 5.58e-01 . . . . 7154 1 68 no PDB 1C6Q . "T4 Lysozyme Mutant C54tC97A IN THE PRESENCE OF 8 ATM Krypton" . . . . . 100.00 164 100.00 100.00 5.58e-01 . . . . 7154 1 69 no PDB 1C6T . "T4 Lysozyme Mutant C54tC97A IN THE PRESENCE OF 8 ATM XENON" . . . . . 100.00 164 100.00 100.00 5.58e-01 . . . . 7154 1 70 no PDB 1CTW . "T4 Lysozyme Mutant I78a" . . . . . 100.00 164 100.00 100.00 5.36e-01 . . . . 7154 1 71 no PDB 1CU0 . "T4 Lysozyme Mutant I78m" . . . . . 100.00 164 100.00 100.00 5.53e-01 . . . . 7154 1 72 no PDB 1CU2 . "T4 Lysozyme Mutant L84m" . . . . . 100.00 164 100.00 100.00 5.64e-01 . . . . 7154 1 73 no PDB 1CU3 . "T4 Lysozyme Mutant V87m" . . . . . 100.00 164 100.00 100.00 5.53e-01 . . . . 7154 1 74 no PDB 1CU5 . "T4 Lysozyme Mutant L91m" . . . . . 100.00 164 100.00 100.00 5.64e-01 . . . . 7154 1 75 no PDB 1CU6 . "T4 Lysozyme Mutant L91a" . . . . . 100.00 164 100.00 100.00 5.47e-01 . . . . 7154 1 76 no PDB 1CV1 . "T4 Lysozyme Mutant V111m" . . . . . 100.00 164 100.00 100.00 5.53e-01 . . . . 7154 1 77 no PDB 1CV3 . "T4 Lysozyme Mutant L121m" . . . . . 100.00 164 100.00 100.00 5.64e-01 . . . . 7154 1 78 no PDB 1CV4 . "T4 Lysozyme Mutant L118m" . . . . . 100.00 164 100.00 100.00 5.64e-01 . . . . 7154 1 79 no PDB 1CV5 . "T4 Lysozyme Mutant L133m" . . . . . 100.00 164 100.00 100.00 5.64e-01 . . . . 7154 1 80 no PDB 1CV6 . "T4 Lysozyme Mutant V149m" . . . . . 100.00 164 100.00 100.00 5.53e-01 . . . . 7154 1 81 no PDB 1CVK . "T4 Lysozyme Mutant L118a" . . . . . 100.00 164 100.00 100.00 5.47e-01 . . . . 7154 1 82 no PDB 1D2W . "N-Terminal Domain Core Methionine Mutation" . . . . . 100.00 164 100.00 100.00 5.53e-01 . . . . 7154 1 83 no PDB 1D2Y . "N-Terminal Domain Core Methionine Mutation" . . . . . 100.00 164 100.00 100.00 5.53e-01 . . . . 7154 1 84 no PDB 1D3F . "N-Terminal Domain Core Methionine Mutation" . . . . . 100.00 164 100.00 100.00 5.53e-01 . . . . 7154 1 85 no PDB 1D3J . "N-Terminal Domain Core Methionine Mutation" . . . . . 100.00 164 100.00 100.00 5.64e-01 . . . . 7154 1 86 no PDB 1EPY . "T4 Lysozyme Mutant, T21hC54TC97AQ141HT142H" . . . . . 100.00 164 100.00 100.00 1.03e+00 . . . . 7154 1 87 no PDB 1G06 . "Crystal Structure Of T4 Lysozyme Mutant V149s" . . . . . 100.00 164 100.00 100.00 1.20e+00 . . . . 7154 1 88 no PDB 1G07 . "Crystal Structure Of T4 Lysozyme Mutant V149c" . . . . . 100.00 164 100.00 100.00 1.06e+00 . . . . 7154 1 89 no PDB 1G0G . "Crystal Structure Of T4 Lysozyme Mutant T152a" . . . . . 100.00 164 100.00 100.00 5.76e-01 . . . . 7154 1 90 no PDB 1G0J . "Crystal Structure Of T4 Lysozyme Mutant T152s" . . . . . 100.00 164 100.00 100.00 5.58e-01 . . . . 7154 1 91 no PDB 1G0K . "Crystal Structure Of T4 Lysozyme Mutant T152c" . . . . . 100.00 164 100.00 100.00 5.82e-01 . . . . 7154 1 92 no PDB 1G0L . "Crystal Structure Of T4 Lysozyme Mutant T152v" . . . . . 100.00 164 100.00 100.00 5.70e-01 . . . . 7154 1 93 no PDB 1G0M . "Crystal Structure Of T4 Lysozyme Mutant T152i" . . . . . 100.00 164 100.00 100.00 5.64e-01 . . . . 7154 1 94 no PDB 1G0P . "Crystal Structure Of T4 Lysozyme Mutant V149g" . . . . . 100.00 164 100.00 100.00 1.23e+00 . . . . 7154 1 95 no PDB 1G0Q . "Crystal Structure Of T4 Lysozyme Mutant V149i" . . . . . 100.00 164 100.00 100.00 1.31e+00 . . . . 7154 1 96 no PDB 1G1V . "T4 Lysozyme Mutant C54tC97AI58T" . . . . . 100.00 164 100.00 100.00 1.20e+00 . . . . 7154 1 97 no PDB 1JQU . "Are Carboxy Terminii Of Helices Coded By The Local Sequence Or By Tertiary Structure Contacts" . . . . . 100.00 164 100.00 100.00 5.47e-01 . . . . 7154 1 98 no PDB 1JTM . "Alternative Structures Of A Sequence Extended T4 Lysozyme Show That The Highly Conserved Beta-Sheet Has Weak Intrinsic Folding " . . . . . 100.00 178 100.00 100.00 7.89e-01 . . . . 7154 1 99 no PDB 1JTN . "Alternative Structures Of A Sequence Extended T4 Lysozyme Show That The Highly Conserved Beta-Sheet Region Has Weak Intrinsic F" . . . . . 100.00 178 100.00 100.00 7.89e-01 . . . . 7154 1 100 no PDB 1KNI . "Stabilizing Disulfide Bridge Mutant Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 6.59e-01 . . . . 7154 1 101 no PDB 1KS3 . "Methionine Core Mutant Of T4 Lysozyme" . . . . . 100.00 162 100.00 100.00 5.56e-01 . . . . 7154 1 102 no PDB 1L35 . "Structure Of A Thermostable Disulfide-Bridge Mutant Of Phage T4 Lysozyme Shows That An Engineered Crosslink In A Flexible Regio" . . . . . 100.00 164 100.00 100.00 9.07e-01 . . . . 7154 1 103 no PDB 1L39 . "Contributions Of Engineered Surface Salt Bridges To The Stability Of T4 Lysozyme Determined By Directed Mutagenesis" . . . . . 100.00 164 100.00 100.00 1.23e+00 . . . . 7154 1 104 no PDB 1L40 . "Contributions Of Engineered Surface Salt Bridges To The Stability Of T4 Lysozyme Determined By Directed Mutagenesis" . . . . . 100.00 164 100.00 100.00 1.23e+00 . . . . 7154 1 105 no PDB 1L41 . "Contributions Of Engineered Surface Salt Bridges To The Stability Of T4 Lysozyme Determined By Directed Mutagenesis" . . . . . 100.00 164 100.00 100.00 5.58e-01 . . . . 7154 1 106 no PDB 1L59 . "Analysis Of The Interaction Between Charged Side Chains And The Alpha-Helix Dipole Using Designed Thermostable Mutants Of Phage" . . . . . 100.00 164 100.00 100.00 5.82e-01 . . . . 7154 1 107 no PDB 1L61 . "Analysis Of The Interaction Between Charged Side Chains And The Alpha-Helix Dipole Using Designed Thermostable Mutants Of Phage" . . . . . 100.00 164 100.00 100.00 5.82e-01 . . . . 7154 1 108 no PDB 1L62 . "Analysis Of The Interaction Between Charged Side Chains And The Alpha-Helix Dipole Using Designed Thermostable Mutants Of Phage" . . . . . 100.00 164 100.00 100.00 5.82e-01 . . . . 7154 1 109 no PDB 1L63 . "Analysis Of The Interaction Between Charged Side Chains And The Alpha-Helix Dipole Using Designed Thermostable Mutants Of Phage" . . . . . 100.00 164 100.00 100.00 5.58e-01 . . . . 7154 1 110 no PDB 1L64 . "Tolerance Of T4 Lysozyme To Multiple Xaa (Right Arrow) Ala Substitutions: A Polyalanine Alpha-Helix Containing Ten Consecutive " . . . . . 100.00 164 100.00 100.00 6.06e-01 . . . . 7154 1 111 no PDB 1L65 . "Tolerance Of T4 Lysozyme To Multiple Xaa (Right Arrow) Ala Substitutions: A Polyalanine Alpha-Helix Containing Ten Consecutive " . . . . . 100.00 164 100.00 100.00 5.47e-01 . . . . 7154 1 112 no PDB 1L66 . "Tolerance Of T4 Lysozyme To Multiple Xaa (Right Arrow) Ala Substitutions: A Polyalanine Alpha-Helix Containing Ten Consecutive " . . . . . 100.00 164 100.00 100.00 5.70e-01 . . . . 7154 1 113 no PDB 1L67 . "Tolerance Of T4 Lysozyme To Multiple Xaa (Right Arrow) Ala Substitutions: A Polyalanine Alpha-Helix Containing Ten Consecutive " . . . . . 100.00 164 100.00 100.00 5.47e-01 . . . . 7154 1 114 no PDB 1L68 . "Tolerance Of T4 Lysozyme To Multiple Xaa (Right Arrow) Ala Substitutions: A Polyalanine Alpha-Helix Containing Ten Consecutive " . . . . . 100.00 164 100.00 100.00 5.76e-01 . . . . 7154 1 115 no PDB 1L76 . "Tolerance Of T4 Lysozyme To Proline Substitutions Within The Long Interdomain Alpha-Helix Illustrates The Adaptability Of Prote" . . . . . 100.00 164 100.00 100.00 1.13e+00 . . . . 7154 1 116 no PDB 1L85 . "Similar Hydrophobic Replacements Of Leu 99 And Phe 153 Within The Core Of T4 Lysozyme Have Different Structural And Thermodynam" . . . . . 100.00 164 100.00 100.00 5.25e-01 . . . . 7154 1 117 no PDB 1L86 . "Similar Hydrophobic Replacements Of Leu 99 And Phe 153 Within The Core Of T4 Lysozyme Have Different Structural And Thermodynam" . . . . . 100.00 164 100.00 100.00 1.40e+00 . . . . 7154 1 118 no PDB 1L87 . "Similar Hydrophobic Replacements Of Leu 99 And Phe 153 Within The Core Of T4 Lysozyme Have Different Structural And Thermodynam" . . . . . 100.00 164 100.00 100.00 1.38e+00 . . . . 7154 1 119 no PDB 1L88 . "Similar Hydrophobic Replacements Of Leu 99 And Phe 153 Within The Core Of T4 Lysozyme Have Different Structural And Thermodynam" . . . . . 100.00 164 100.00 100.00 5.47e-01 . . . . 7154 1 120 no PDB 1L95 . "Similar Hydrophobic Replacements Of Leu 99 And Phe 153 Within The Core Of T4 Lysozyme Have Different Structural And Thermodynam" . . . . . 100.00 164 100.00 100.00 5.25e-01 . . . . 7154 1 121 no PDB 1LLH . "Are Carboxy Terminii Of Helices Coded By The Local Sequence Or By Tertiary Structure Contacts" . . . . . 100.00 164 100.00 100.00 5.64e-01 . . . . 7154 1 122 no PDB 1LW9 . "Multiple Methionine Substitutions Are Tolerated In T4 Lysozyme And Have Coupled Effects On Folding And Stability" . . . . . 100.00 164 100.00 100.00 5.58e-01 . . . . 7154 1 123 no PDB 1LYE . "Dissection Of Helix Capping In T4 Lysozyme By Structural And Thermodynamic Analysis Of Six Amino Acid Substitutions At Thr 59" . . . . . 100.00 164 100.00 100.00 5.70e-01 . . . . 7154 1 124 no PDB 1LYF . "Dissection Of Helix Capping In T4 Lysozyme By Structural And Thermodynamic Analysis Of Six Amino Acid Substitutions At Thr 59" . . . . . 100.00 164 100.00 100.00 5.58e-01 . . . . 7154 1 125 no PDB 1LYG . "Dissection Of Helix Capping In T4 Lysozyme By Structural And Thermodynamic Analysis Of Six Amino Acid Substitutions At Thr 59" . . . . . 100.00 164 100.00 100.00 5.82e-01 . . . . 7154 1 126 no PDB 1LYH . "Dissection Of Helix Capping In T4 Lysozyme By Structural And Thermodynamic Analysis Of Six Amino Acid Substitutions At Thr 59" . . . . . 100.00 164 100.00 100.00 5.88e-01 . . . . 7154 1 127 no PDB 1LYI . "Dissection Of Helix Capping In T4 Lysozyme By Structural And Thermodynamic Analysis Of Six Amino Acid Substitutions At Thr 59" . . . . . 100.00 164 100.00 100.00 5.82e-01 . . . . 7154 1 128 no PDB 1LYJ . "Dissection Of Helix Capping In T4 Lysozyme By Structural And Thermodynamic Analysis Of Six Amino Acid Substitutions At Thr 59" . . . . . 100.00 164 100.00 100.00 5.76e-01 . . . . 7154 1 129 no PDB 1OYU . "Long-Distance Conformational Changes In A Protein Engineered By Modulated Sequence Duplication" . . . . . 100.00 175 100.00 100.00 1.37e+00 . . . . 7154 1 130 no PDB 1P2L . "T4 Lysozyme Core Repacking Mutant V87iTA" . . . . . 100.00 164 100.00 100.00 1.31e+00 . . . . 7154 1 131 no PDB 1P2R . "T4 Lysozyme Core Repacking Mutant I78vTA" . . . . . 100.00 164 100.00 100.00 5.53e-01 . . . . 7154 1 132 no PDB 1P56 . "Duplication-Extension Of Helix A Of T4 Lysozyme" . . . . . 100.00 176 100.00 100.00 6.73e-01 . . . . 7154 1 133 no PDB 1P5C . "Circular Permutation Of Helix A In T4 Lysozyme" . . . . . 100.00 167 100.00 100.00 5.66e-01 . . . . 7154 1 134 no PDB 1P64 . "T4 Lysozyme Core Repacking Mutant L133fTA" . . . . . 100.00 164 100.00 100.00 5.82e-01 . . . . 7154 1 135 no PDB 1P6Y . "T4 Lysozyme Core Repacking Mutant M120y/ta" . . . . . 100.00 164 100.00 100.00 9.55e-01 . . . . 7154 1 136 no PDB 1PQI . "T4 Lysozyme Core Repacking Mutant I118lCORE7TA" . . . . . 100.00 164 100.00 100.00 5.88e-01 . . . . 7154 1 137 no PDB 1PQK . "Repacking Of The Core Of T4 Lysozyme By Automated Design" . . . . . 100.00 164 100.00 100.00 5.64e-01 . . . . 7154 1 138 no PDB 1PQM . "T4 Lysozyme Core Repacking Mutant V149iT152VTA" . . . . . 100.00 164 100.00 100.00 5.64e-01 . . . . 7154 1 139 no PDB 1PQO . "T4 Lysozyme Core Repacking Mutant L118iTA" . . . . . 100.00 164 100.00 100.00 5.58e-01 . . . . 7154 1 140 no PDB 1QT3 . "T26d Mutant Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.82e-01 . . . . 7154 1 141 no PDB 1QT4 . "T26q Mutant Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.82e-01 . . . . 7154 1 142 no PDB 1QT5 . "D20e Mutant Structure Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 1.27e+00 . . . . 7154 1 143 no PDB 1QT6 . "E11h Mutant Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.64e-01 . . . . 7154 1 144 no PDB 1QT7 . "E11n Mutant Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.58e-01 . . . . 7154 1 145 no PDB 1QT8 . "T26h Mutant Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.70e-01 . . . . 7154 1 146 no PDB 1QTB . "The Introduction Of Strain And Its Effects On The Structure And Stability Of T4 Lysozyme" . . . . . 100.00 162 100.00 100.00 5.34e-01 . . . . 7154 1 147 no PDB 1QTC . "The Introduction Of Strain And Its Effects On The Structure And Stability Of T4 Lysozyme" . . . . . 100.00 162 100.00 100.00 5.39e-01 . . . . 7154 1 148 no PDB 1QTD . "The Introduction Of Strain And Its Effects On The Structure And Stability Of T4 Lysozyme" . . . . . 100.00 162 100.00 100.00 9.33e-01 . . . . 7154 1 149 no PDB 1QTV . "T26e Apo Structure Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.70e-01 . . . . 7154 1 150 no PDB 1QTZ . "D20c Mutant Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 1.20e+00 . . . . 7154 1 151 no PDB 1QUG . "E108v Mutant Of T4 Lysozyme" . . . . . 100.00 162 100.00 100.00 5.39e-01 . . . . 7154 1 152 no PDB 1SSW . "Crystal Structure Of Phage T4 Lysozyme Mutant Y24aY25AT26AI27AC54TC97A" . . . . . 100.00 164 100.00 100.00 5.53e-01 . . . . 7154 1 153 no PDB 1SSY . "Crystal Structure Of Phage T4 Lysozyme Mutant G28aI29AG30AC54TC97A" . . . . . 100.00 164 100.00 100.00 5.19e-01 . . . . 7154 1 154 no PDB 1T8A . "Use Of Sequence Duplication To Engineer A Ligand-Triggered Long-Distance Molecular Switch In T4 Lysosyme" . . . . . 100.00 175 100.00 100.00 1.61e+00 . . . . 7154 1 155 no PDB 1T8F . "Crystal Structure Of Phage T4 Lysozyme Mutant R14aK16AI17AK19AT21AE22AC54TC97A" . . . . . 100.00 164 100.00 100.00 5.88e-01 . . . . 7154 1 156 no PDB 1T8G . "Crystal Structure Of Phage T4 Lysozyme Mutant L32aL33AT34AC54TC97AE108V" . . . . . 100.00 164 100.00 100.00 5.58e-01 . . . . 7154 1 157 no PDB 1T97 . "Use Of Sequence Duplication To Engineer A Ligand-Triggered Long-Distance Molecular Switch In T4 Lysosyme" . . . . . 100.00 175 100.00 100.00 1.61e+00 . . . . 7154 1 158 no PDB 1TLA . "Hydrophobic Core Repacking And Aromatic-Aromatic Interaction In The Thermostable Mutant Of T4 Lysozyme Ser 117 (Right Arrow) Ph" . . . . . 100.00 164 100.00 100.00 5.88e-01 . . . . 7154 1 159 no PDB 1ZUR . "Crystal Structure Of Spin Labeled T4 Lysozyme (V131r1f)" . . . . . 100.00 164 100.00 100.00 1.06e+00 . . . . 7154 1 160 no PDB 1ZWN . "Crystal Structure Of Spin Labeled T4 Lysozyme (V131r1b)" . . . . . 100.00 164 100.00 100.00 1.06e+00 . . . . 7154 1 161 no PDB 1ZYT . "Crystal Structure Of Spin Labeled T4 Lysozyme (A82r1)" . . . . . 100.00 164 100.00 100.00 1.05e+00 . . . . 7154 1 162 no PDB 200L . 'Thermodynamic And Structural Compensation In "size-Switch" Core-Repacking Variants Of T4 Lysozyme' . . . . . 100.00 164 100.00 100.00 5.47e-01 . . . . 7154 1 163 no PDB 201L . "How Amino-Acid Insertions Are Allowed In An Alpha-Helix Of T4 Lysozyme" . . . . . 100.00 166 100.00 100.00 9.76e-01 . . . . 7154 1 164 no PDB 205L . "How Amino-Acid Insertions Are Allowed In An Alpha-Helix Of T4 Lysozyme" . . . . . 100.00 167 100.00 100.00 5.84e-01 . . . . 7154 1 165 no PDB 206L . "Phage T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 1.13e+00 . . . . 7154 1 166 no PDB 209L . "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" . . . . . 100.00 167 100.00 100.00 5.84e-01 . . . . 7154 1 167 no PDB 210L . "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" . . . . . 100.00 163 100.00 100.00 1.22e+00 . . . . 7154 1 168 no PDB 211L . "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" . . . . . 100.00 165 100.00 100.00 5.65e-01 . . . . 7154 1 169 no PDB 212L . "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" . . . . . 100.00 168 100.00 100.00 5.72e-01 . . . . 7154 1 170 no PDB 213L . "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" . . . . . 100.00 165 100.00 100.00 5.65e-01 . . . . 7154 1 171 no PDB 214L . "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" . . . . . 100.00 165 100.00 100.00 5.65e-01 . . . . 7154 1 172 no PDB 215L . "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" . . . . . 100.00 165 100.00 100.00 5.65e-01 . . . . 7154 1 173 no PDB 216L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.58e-01 . . . . 7154 1 174 no PDB 217L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.70e-01 . . . . 7154 1 175 no PDB 218L . "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" . . . . . 100.00 165 100.00 100.00 5.65e-01 . . . . 7154 1 176 no PDB 219L . "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.58e-01 . . . . 7154 1 177 no PDB 221L . "The Energetic Cost And The Structural Consequences Of Burying A Hydroxyl Group Within The Core Of A Protein Determined From Ala" . . . . . 100.00 164 100.00 100.00 1.13e+00 . . . . 7154 1 178 no PDB 230L . "T4 Lysozyme Mutant M6l" . . . . . 100.00 164 100.00 100.00 1.11e+00 . . . . 7154 1 179 no PDB 232L . "T4 Lysozyme Mutant M120k" . . . . . 100.00 164 100.00 100.00 1.05e+00 . . . . 7154 1 180 no PDB 233L . "T4 Lysozyme Mutant M120l" . . . . . 100.00 164 100.00 100.00 1.11e+00 . . . . 7154 1 181 no PDB 235L . "The Response Of T4 Lysozyme To Large-To-Small Substitutions Within The Core And Its Relation To The Hydrophobic Effect" . . . . . 100.00 164 100.00 100.00 5.58e-01 . . . . 7154 1 182 no PDB 236L . "The Response Of T4 Lysozyme To Large-To-Small Substitutions Within The Core And Its Relation To The Hydrophobic Effect" . . . . . 100.00 164 100.00 100.00 5.58e-01 . . . . 7154 1 183 no PDB 237L . "The Response Of T4 Lysozyme To Large-To-Small Substitutions Within The Core And Its Relation To The Hydrophobic Effect" . . . . . 100.00 164 100.00 100.00 5.58e-01 . . . . 7154 1 184 no PDB 239L . "The Response Of T4 Lysozyme To Large-To-Small Substitutions Within The Core And Its Relation To The Hydrophobic Effect" . . . . . 100.00 164 100.00 100.00 5.36e-01 . . . . 7154 1 185 no PDB 240L . "The Response Of T4 Lysozyme To Large-To-Small Substitutions Within The Core And Its Relation To The Hydrophobic Effect" . . . . . 100.00 164 100.00 100.00 5.36e-01 . . . . 7154 1 186 no PDB 241L . "The Response Of T4 Lysozyme To Large-To-Small Substitutions Within The Core And Its Relation To The Hydrophobic Effect" . . . . . 100.00 164 100.00 100.00 5.36e-01 . . . . 7154 1 187 no PDB 242L . "The Response Of T4 Lysozyme To Large-To-Small Substitutions Within The Core And Its Relation To The Hydrophobic Effect" . . . . . 100.00 164 100.00 100.00 5.36e-01 . . . . 7154 1 188 no PDB 243L . "The Response Of T4 Lysozyme To Large-To-Small Substitutions Within The Core And Its Relation To The Hydrophobic Effect" . . . . . 100.00 164 100.00 100.00 5.36e-01 . . . . 7154 1 189 no PDB 245L . "The Response Of T4 Lysozyme To Large-To-Small Substitutions Within The Core And Its Relation To The Hydrophobic Effect" . . . . . 100.00 164 100.00 100.00 1.23e+00 . . . . 7154 1 190 no PDB 246L . "The Response Of T4 Lysozyme To Large-To-Small Substitutions Within The Core And Its Relation To The Hydrophobic Effect" . . . . . 100.00 164 100.00 100.00 5.25e-01 . . . . 7154 1 191 no PDB 247L . "The Response Of T4 Lysozyme To Large-To-Small Substitutions Within The Core And Its Relation To The Hydrophobic Effect" . . . . . 100.00 164 100.00 100.00 5.47e-01 . . . . 7154 1 192 no PDB 248L . "The Response Of T4 Lysozyme To Large-To-Small Substitutions Within The Core And Its Relation To The Hydrophobic Effect" . . . . . 100.00 164 100.00 100.00 5.36e-01 . . . . 7154 1 193 no PDB 249L . "The Response Of T4 Lysozyme To Large-To-Small Substitutions Within The Core And Its Relation To The Hydrophobic Effect" . . . . . 100.00 164 100.00 100.00 5.36e-01 . . . . 7154 1 194 no PDB 250L . "The Response Of T4 Lysozyme To Large-To-Small Substitutions Within The Core And Its Relation To The Hydrophobic Effect" . . . . . 100.00 164 100.00 100.00 5.36e-01 . . . . 7154 1 195 no PDB 251L . "The Response Of T4 Lysozyme To Large-To-Small Substitutions Within The Core And Its Relation To The Hydrophobic Effect" . . . . . 100.00 164 100.00 100.00 5.47e-01 . . . . 7154 1 196 no PDB 253L . Lysozyme . . . . . 100.00 164 100.00 100.00 5.47e-01 . . . . 7154 1 197 no PDB 254L . Lysozyme . . . . . 100.00 164 100.00 100.00 1.31e+00 . . . . 7154 1 198 no PDB 255L . Hydrolase . . . . . 100.00 164 100.00 100.00 5.53e-01 . . . . 7154 1 199 no PDB 257L . "An Adaptable Metal-Binding Site Engineered Into T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.76e-01 . . . . 7154 1 200 no PDB 258L . "An Adaptable Metal-Binding Site Engineered Into T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.76e-01 . . . . 7154 1 201 no PDB 259L . "An Adaptable Metal-Binding Site Engineered Into T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.76e-01 . . . . 7154 1 202 no PDB 260L . "An Adaptable Metal-Binding Site Engineered Into T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.76e-01 . . . . 7154 1 203 no PDB 261L . "Structural Characterisation Of An Engineered Tandem Repeat Contrasts The Importance Of Context And Sequence In Protein Folding" . . . . . 100.00 173 100.00 100.00 1.55e+00 . . . . 7154 1 204 no PDB 262L . "Structural Characterisation Of An Engineered Tandem Repeat Contrasts The Importance Of Context And Sequence In Protein Folding" . . . . . 100.00 173 100.00 100.00 1.55e+00 . . . . 7154 1 205 no PDB 2A4T . "Crystal Structure Of Spin Labeled T4 Lysozyme (V131r7)" . . . . . 100.00 164 100.00 100.00 1.06e+00 . . . . 7154 1 206 no PDB 2B7X . "Sequential Reorganization Of Beta-Sheet Topology By Insertion Of A Single Strand" . . . . . 100.00 170 100.00 100.00 1.20e+00 . . . . 7154 1 207 no PDB 2CUU . "Crystal Structure Of Spin Labeled T4 Lysozyme (v131r1)" . . . . . 100.00 164 100.00 100.00 1.06e+00 . . . . 7154 1 208 no PDB 2F2Q . "High Resolution Crystal Strcuture Of T4 Lysosyme Mutant L20r63A LIGANDED TO GUANIDINIUM ION" . . . . . 100.00 175 100.00 100.00 1.61e+00 . . . . 7154 1 209 no PDB 2F32 . "Xray Crystal Structure Of Lysozyme Mutant L20R63A LIGANDED To Ethylguanidinium" . . . . . 100.00 175 100.00 100.00 1.61e+00 . . . . 7154 1 210 no PDB 2F47 . "Xray Crystal Structure Of T4 Lysozyme Mutant L20R63A Liganded To Methylguanidinium" . . . . . 100.00 175 100.00 100.00 1.61e+00 . . . . 7154 1 211 no PDB 2HUK . "Crystal Structure Of T4 Lysozyme V131c Synthetic Dimer" . . . . . 100.00 164 100.00 100.00 1.06e+00 . . . . 7154 1 212 no PDB 2HUL . "Crystal Structure Of T4 Lysozyme S44c Synthetic Dimer" . . . . . 100.00 164 100.00 100.00 5.88e-01 . . . . 7154 1 213 no PDB 2HUM . "Crystal Structure Of T4 Lysozyme D72c Synthetic Dimer" . . . . . 100.00 164 100.00 100.00 1.20e+00 . . . . 7154 1 214 no PDB 2IGC . "Structure Of Spin Labeled T4 Lysozyme Mutant T115r1a" . . . . . 100.00 164 100.00 100.00 5.82e-01 . . . . 7154 1 215 no PDB 2L78 . "Design And Structural Analysis Of Alternative Hydrophobic Core Packing Arrangements In Bacteriophage T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 1.31e+00 . . . . 7154 1 216 no PDB 2NTG . "Structure Of Spin-Labeled T4 Lysozyme Mutant T115r7" . . . . . 100.00 164 100.00 100.00 5.82e-01 . . . . 7154 1 217 no PDB 2NTH . "Structure Of Spin-Labeled T4 Lysozyme Mutant L118r1" . . . . . 100.00 164 100.00 100.00 1.10e+00 . . . . 7154 1 218 no PDB 2O4W . "T4 Lysozyme Circular Permutant" . . . . . 100.00 171 100.00 100.00 6.28e-01 . . . . 7154 1 219 no PDB 2O79 . "T4 Lysozyme With C-Terminal Extension" . . . . . 100.00 170 100.00 100.00 5.97e-01 . . . . 7154 1 220 no PDB 2O7A . "T4 Lysozyme C-Terminal Fragment" . . . . . 100.00 124 100.00 100.00 4.06e-01 . . . . 7154 1 221 no PDB 2OE4 . "High Pressure Psuedo Wild Type T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.58e-01 . . . . 7154 1 222 no PDB 2OE7 . "High-Pressure T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.58e-01 . . . . 7154 1 223 no PDB 2OE9 . "High-Pressure Structure Of Pseudo-Wt T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.58e-01 . . . . 7154 1 224 no PDB 2OEA . "High-Pressure Structure Of Pseudo-Wt T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.58e-01 . . . . 7154 1 225 no PDB 2OU8 . "Structure Of Spin-Labeled T4 Lysozyme Mutant T115r1 At Room Temperature" . . . . . 100.00 164 100.00 100.00 5.82e-01 . . . . 7154 1 226 no PDB 2OU9 . "Structure Of Spin-Labeled T4 Lysozyme Mutant T115r1R119A" . . . . . 100.00 164 100.00 100.00 5.70e-01 . . . . 7154 1 227 no PDB 2Q9D . "Structure Of Spin-Labeled T4 Lysozyme Mutant A41r1" . . . . . 100.00 164 100.00 100.00 1.05e+00 . . . . 7154 1 228 no PDB 2Q9E . "Structure Of Spin-Labeled T4 Lysozyme Mutant S44r1" . . . . . 100.00 164 100.00 100.00 6.06e-01 . . . . 7154 1 229 no PDB 2RH1 . "High Resolution Crystal Structure Of Human B2-Adrenergic G Protein- Coupled Receptor" . . . . . 100.00 500 100.00 100.00 1.55e+00 . . . . 7154 1 230 no PDB 3D4S . "Cholesterol Bound Form Of Human Beta2 Adrenergic Receptor." . . . . . 100.00 490 100.00 100.00 9.22e-01 . . . . 7154 1 231 no PDB 3EML . "The 2.6 A Crystal Structure Of A Human A2a Adenosine Receptor Bound To Zm241385." . . . . . 100.00 488 100.00 100.00 1.64e+00 . . . . 7154 1 232 no PDB 3G3V . "Crystal Structure Of Spin Labeled T4 Lysozyme (V131r1) At 291 K" . . . . . 100.00 164 100.00 100.00 1.06e+00 . . . . 7154 1 233 no PDB 3G3W . "Crystal Structure Of Spin Labeled T4 Lysozyme (T151r1) At 291 K" . . . . . 100.00 164 100.00 100.00 5.82e-01 . . . . 7154 1 234 no PDB 3G3X . "Crystal Structure Of Spin Labeled T4 Lysozyme (T151r1) At 100 K" . . . . . 100.00 164 100.00 100.00 5.82e-01 . . . . 7154 1 235 no PDB 3JR6 . "Sequential Reorganization Of Beta-Sheet Topology By Insertion Of A Single Strand" . . . . . 100.00 170 100.00 100.00 1.27e+00 . . . . 7154 1 236 no PDB 3K2R . "Crystal Structure Of Spin Labeled T4 Lysozyme Mutant K65v1R76V1" . . . . . 100.00 164 100.00 100.00 9.07e-01 . . . . 7154 1 237 no PDB 3L2X . "Crystal Structure Of Spin Labeled T4 Lysozyme Mutant 115-119rx" . . . . . 100.00 164 100.00 100.00 9.26e-01 . . . . 7154 1 238 no PDB 3L64 . "T4 Lysozyme S44e/wt*" . . . . . 100.00 164 100.00 100.00 5.70e-01 . . . . 7154 1 239 no PDB 3NY8 . "Crystal Structure Of The Human Beta2 Adrenergic Receptor In Complex With The Inverse Agonist Ici 118,551" . . . . . 100.00 490 100.00 100.00 9.22e-01 . . . . 7154 1 240 no PDB 3NY9 . "Crystal Structure Of The Human Beta2 Adrenergic Receptor In Complex With A Novel Inverse Agonist" . . . . . 100.00 490 100.00 100.00 9.22e-01 . . . . 7154 1 241 no PDB 3NYA . "Crystal Structure Of The Human Beta2 Adrenergic Receptor In Complex With The Neutral Antagonist Alprenolol" . . . . . 100.00 490 100.00 100.00 9.22e-01 . . . . 7154 1 242 no PDB 3ODU . "The 2.5 A Structure Of The Cxcr4 Chemokine Receptor In Complex With Small Molecule Antagonist It1t" . . . . . 100.00 502 100.00 100.00 4.39e-01 . . . . 7154 1 243 no PDB 3OE0 . "Crystal Structure Of The Cxcr4 Chemokine Receptor In Complex With A Cyclic Peptide Antagonist Cvx15" . . . . . 100.00 499 100.00 100.00 4.38e-01 . . . . 7154 1 244 no PDB 3OE6 . "Crystal Structure Of The Cxcr4 Chemokine Receptor In Complex With A Small Molecule Antagonist It1t In I222 Spacegroup" . . . . . 100.00 508 100.00 100.00 4.53e-01 . . . . 7154 1 245 no PDB 3OE8 . "Crystal Structure Of The Cxcr4 Chemokine Receptor In Complex With A Small Molecule Antagonist It1t In P1 Spacegroup" . . . . . 100.00 502 100.00 100.00 4.39e-01 . . . . 7154 1 246 no PDB 3OE9 . "Crystal Structure Of The Chemokine Cxcr4 Receptor In Complex With A Small Molecule Antagonist It1t In P1 Spacegroup" . . . . . 100.00 499 100.00 100.00 4.38e-01 . . . . 7154 1 247 no PDB 3P0G . "Structure Of A Nanobody-Stabilized Active State Of The Beta2 Adrenoceptor" . . . . . 100.00 501 100.00 100.00 1.52e+00 . . . . 7154 1 248 no PDB 3PBL . "Structure Of The Human Dopamine D3 Receptor In Complex With Eticlopride" . . . . . 100.00 481 100.00 100.00 7.29e-01 . . . . 7154 1 249 no PDB 3PDS . "Irreversible Agonist-Beta2 Adrenoceptor Complex" . . . . . 100.00 458 100.00 100.00 1.07e+00 . . . . 7154 1 250 no PDB 3QAK . "Agonist Bound Structure Of The Human Adenosine A2a Receptor" . . . . . 100.00 488 100.00 100.00 1.64e+00 . . . . 7154 1 251 no PDB 3RUN . "New Strategy To Analyze Structures Of Glycopeptide Antibiotic-Target Complexes" . . . . . 100.00 168 100.00 100.00 5.66e-01 . . . . 7154 1 252 no PDB 3RZE . "Structure Of The Human Histamine H1 Receptor In Complex With Doxepin" . . . . . 100.00 452 100.00 100.00 1.01e+00 . . . . 7154 1 253 no PDB 3SB5 . "Zn-Mediated Trimer Of T4 Lysozyme R125cE128C BY SYNTHETIC Symmetrization" . . . . . 100.00 165 100.00 100.00 7.16e-01 . . . . 7154 1 254 no PDB 3SB6 . "Cu-Mediated Dimer Of T4 Lysozyme D61hK65HR76HR80H BY SYNTHETIC Symmetrization" . . . . . 100.00 165 100.00 100.00 4.79e-01 . . . . 7154 1 255 no PDB 3SB7 . "Cu-Mediated Trimer Of T4 Lysozyme D61hK65HR76HR80H BY SYNTHETIC Symmetrization" . . . . . 100.00 165 100.00 100.00 4.79e-01 . . . . 7154 1 256 no PDB 3SB8 . "Cu-Mediated Dimer Of T4 Lysozyme D61hK65H BY SYNTHETIC SYMMETRIZATION" . . . . . 100.00 165 100.00 100.00 8.36e-01 . . . . 7154 1 257 no PDB 3SB9 . "Cu-Mediated Dimer Of T4 Lysozyme R76hR80H BY SYNTHETIC SYMMETRIZATION" . . . . . 100.00 165 100.00 100.00 6.13e-01 . . . . 7154 1 258 no PDB 3SBA . "Zn-Mediated Hexamer Of T4 Lysozyme R76hR80H BY SYNTHETIC Symmetrization" . . . . . 100.00 165 100.00 100.00 6.13e-01 . . . . 7154 1 259 no PDB 3SBB . "Disulphide-Mediated Tetramer Of T4 Lysozyme R76cR80C BY SYNTHETIC Symmetrization" . . . . . 100.00 165 100.00 100.00 5.53e-01 . . . . 7154 1 260 no PDB 3SN6 . "Crystal Structure Of The Beta2 Adrenergic Receptor-Gs Protein Complex" . . . . . 100.00 514 100.00 100.00 9.11e-01 . . . . 7154 1 261 no PDB 3UON . "Structure Of The Human M2 Muscarinic Acetylcholine Receptor Bound To An Antagonist" . . . . . 100.00 467 100.00 100.00 7.71e-01 . . . . 7154 1 262 no PDB 3V2W . "Crystal Structure Of A Lipid G Protein-Coupled Receptor At 3.35a" . . . . . 100.00 520 100.00 100.00 6.14e-01 . . . . 7154 1 263 no PDB 3V2Y . "Crystal Structure Of A Lipid G Protein-Coupled Receptor At 2.80a" . . . . . 100.00 520 100.00 100.00 6.14e-01 . . . . 7154 1 264 no PDB 3VW7 . "Crystal Structure Of Human Protease-activated Receptor 1 (par1) Bound With Antagonist Vorapaxar At 2.2 Angstrom" . . . . . 100.00 484 100.00 100.00 3.86e-01 . . . . 7154 1 265 no PDB 4ARJ . "Crystal Structure Of A Pesticin (translocation And Receptor Binding Domain) From Y. Pestis And T4-lysozyme Chimera" . . . . . 100.00 339 100.00 100.00 6.12e-01 . . . . 7154 1 266 no PDB 4DAJ . "Structure Of The M3 Muscarinic Acetylcholine Receptor" . . . . . 100.00 479 100.00 100.00 6.62e-01 . . . . 7154 1 267 no PDB 4DJH . "Structure Of The Human Kappa Opioid Receptor In Complex With Jdtic" . . . . . 100.00 480 100.00 100.00 1.49e+00 . . . . 7154 1 268 no PDB 4DKL . "Crystal Structure Of The Mu-Opioid Receptor Bound To A Morphinan Antagonist" . . . . . 100.00 464 100.00 100.00 7.06e-01 . . . . 7154 1 269 no PDB 4EJ4 . "Structure Of The Delta Opioid Receptor Bound To Naltrindole" . . . . . 100.00 461 100.00 100.00 1.51e+00 . . . . 7154 1 270 no PDB 4EXM . "The Crystal Structure Of An Engineered Phage Lysin Containing The Binding Domain Of Pesticin And The Killing Domain Of T4-Lysoz" . . . . . 100.00 347 100.00 100.00 5.07e-01 . . . . 7154 1 271 no PDB 4GBR . "N-terminal T4 Lysozyme Fusion Facilitates Crystallization Of A G Protein Coupled Receptor" . . . . . 100.00 163 100.00 100.00 5.52e-01 . . . . 7154 1 272 no PDB 4GRV . "The Crystal Structure Of The Neurotensin Receptor Nts1 In Complex With Neurotensin (8-13)" . . . . . 100.00 510 100.00 100.00 8.50e-01 . . . . 7154 1 273 no PDB 4HTT . "Crystal Structure Of Twin Arginine Translocase Receptor- Tatc In Ddm" . . . . . 100.00 418 100.00 100.00 1.36e+00 . . . . 7154 1 274 no PDB 4IAP . "Crystal Structure Of Ph Domain Of Osh3 From Saccharomyces Cerevisiae" . . . . . 100.00 260 100.00 100.00 8.34e-01 . . . . 7154 1 275 no PDB 4LDE . "Structure Of Beta2 Adrenoceptor Bound To Bi167107 And An Engineered Nanobody" . . . . . 100.00 469 100.00 100.00 1.23e+00 . . . . 7154 1 276 no PDB 4LDL . "Structure Of Beta2 Adrenoceptor Bound To Hydroxybenzylisoproterenol And An Engineered Nanobody" . . . . . 100.00 469 100.00 100.00 1.23e+00 . . . . 7154 1 277 no PDB 4LDO . "Structure Of Beta2 Adrenoceptor Bound To Adrenaline And An Engineered Nanobody" . . . . . 100.00 469 100.00 100.00 1.23e+00 . . . . 7154 1 278 no PDB 4OO9 . "Structure Of The Human Class C Gpcr Metabotropic Glutamate Receptor 5 Transmembrane Domain In Complex With The Negative Alloste" . . . . . 100.00 444 100.00 100.00 8.56e-01 . . . . 7154 1 279 no PDB 4PHU . "Crystal Structure Of Human Gpr40 Bound To Allosteric Agonist Tak-875" . . . . . 100.00 491 100.00 100.00 5.17e-01 . . . . 7154 1 280 no PDB 4PJZ . "Crystal Structure Of T4 Lysozyme-gss-peptide In Complex With Teicoplanin-a2-2" . . . . . 100.00 174 100.00 100.00 1.22e+00 . . . . 7154 1 281 no PDB 4PK0 . "Crystal Structure Of T4 Lysozyme-peptide In Complex With Teicoplanin- A2-2" . . . . . 100.00 171 100.00 100.00 6.03e-01 . . . . 7154 1 282 no PDB 4PLA . "Crystal Structure Of Phosphatidyl Inositol 4-kinase Ii Alpha In Complex With Atp" . . . . . 100.00 556 100.00 100.00 4.81e-01 . . . . 7154 1 283 no PDB 4QKX . "Structure Of Beta2 Adrenoceptor Bound To A Covalent Agonist And An Engineered Nanobody" . . . . . 100.00 469 100.00 100.00 1.17e+00 . . . . 7154 1 284 no PDB 4TN3 . "Structure Of The Bbox-coiled-coil Region Of Rhesus Trim5alpha" . . . . . 100.00 400 100.00 100.00 5.58e-01 . . . . 7154 1 285 no PDB 4U15 . "M3-mt4l Receptor Bound To Tiotropium" . . . . . 100.00 418 100.00 100.00 6.45e-01 . . . . 7154 1 286 no PDB 4U16 . "M3-mt4l Receptor Bound To Nms" . . . . . 100.00 418 100.00 100.00 6.45e-01 . . . . 7154 1 287 no PDB 4W8F . "Crystal Structure Of The Dynein Motor Domain In The Amppnp-bound State" . . . . . 100.00 2661 100.00 100.00 5.05e-01 . . . . 7154 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 92 ASP . 7154 1 2 93 ALA . 7154 1 3 94 VAL . 7154 1 4 95 ARG . 7154 1 5 96 ARG . 7154 1 6 97 ALA . 7154 1 7 98 ALA . 7154 1 8 99 LEU . 7154 1 9 100 ILE . 7154 1 10 101 ASN . 7154 1 11 102 MET . 7154 1 12 103 VAL . 7154 1 13 104 PHE . 7154 1 14 105 GLN . 7154 1 15 106 MET . 7154 1 16 107 GLY . 7154 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 . ASP 1 1 7154 1 . ALA 2 2 7154 1 . VAL 3 3 7154 1 . ARG 4 4 7154 1 . ARG 5 5 7154 1 . ALA 6 6 7154 1 . ALA 7 7 7154 1 . LEU 8 8 7154 1 . ILE 9 9 7154 1 . ASN 10 10 7154 1 . MET 11 11 7154 1 . VAL 12 12 7154 1 . PHE 13 13 7154 1 . GLN 14 14 7154 1 . MET 15 15 7154 1 . GLY 16 16 7154 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 7154 _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 $HELIX_E . . . no . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 7154 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 7154 _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 $HELIX_E . 'chemical synthesis' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 7154 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 7154 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'helix E (lys 92-107)' . . . 1 $HELIX_E . . . 1 2 mM . . . . 7154 1 2 TFE . . . . . . . 50 . . % . . . . 7154 1 3 H2O . . . . . . . 45 . . % . . . . 7154 1 4 D2O . . . . . . . 5 . . % . . . . 7154 1 stop_ save_ ####################### # Sample conditions # ####################### save_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode conditions_1 _Sample_condition_list.Entry_ID 7154 _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 . . . 7154 1 temperature 288 0 K 7154 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 7154 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'spectrometer information not available' _NMR_spectrometer.Manufacturer unknown _NMR_spectrometer.Model unknown _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 0 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 7154 _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 spectrometer_1 unknown unknown . 0 . . . 7154 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 7154 _Experiment_list.ID 1 _Experiment_list.Details 'experiment information not available' 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 unknown no 1 $NMR_spec_expt . . . . . . . . 1 $sample_1 isotropic . . 1 $conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7154 1 stop_ save_ save_NMR_spec_expt _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt _NMR_spec_expt.Entry_ID 7154 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name unknown _NMR_spec_expt.Type unknown _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 $spectrometer_1 _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 'experiment information not available' save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_referencing _Chem_shift_reference.Entry_ID 7154 _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 TSP 'methyl protons' . . . . ppm 0.00 external direct 1.0 . . . 1 $entry_citation . . 1 $entry_citation 7154 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_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 7154 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_referencing _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 unknown 1 $sample_1 isotropic 7154 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 1 1 ASP HA H 1 4.30 . . . . . . . 92 ASP HA . 7154 1 2 . 1 1 1 1 ASP HB2 H 1 3.09 . . . . . . . 92 ASP HB2 . 7154 1 3 . 1 1 1 1 ASP HB3 H 1 2.99 . . . . . . . 92 ASP HB3 . 7154 1 4 . 1 1 2 2 ALA H H 1 8.86 . . . . . . . 93 ALA H . 7154 1 5 . 1 1 2 2 ALA HA H 1 4.26 . . . . . . . 93 ALA HA . 7154 1 6 . 1 1 2 2 ALA HB1 H 1 1.50 . . . . . . . 93 ALA HB . 7154 1 7 . 1 1 2 2 ALA HB2 H 1 1.50 . . . . . . . 93 ALA HB . 7154 1 8 . 1 1 2 2 ALA HB3 H 1 1.50 . . . . . . . 93 ALA HB . 7154 1 9 . 1 1 3 3 VAL H H 1 7.77 . . . . . . . 94 VAL H . 7154 1 10 . 1 1 3 3 VAL HA H 1 3.84 . . . . . . . 94 VAL HA . 7154 1 11 . 1 1 3 3 VAL HB H 1 2.16 . . . . . . . 94 VAL HB . 7154 1 12 . 1 1 3 3 VAL HG11 H 1 1.06 . . . . . . . 94 VAL HG1 . 7154 1 13 . 1 1 3 3 VAL HG12 H 1 1.06 . . . . . . . 94 VAL HG1 . 7154 1 14 . 1 1 3 3 VAL HG13 H 1 1.06 . . . . . . . 94 VAL HG1 . 7154 1 15 . 1 1 3 3 VAL HG21 H 1 0.99 . . . . . . . 94 VAL HG2 . 7154 1 16 . 1 1 3 3 VAL HG22 H 1 0.99 . . . . . . . 94 VAL HG2 . 7154 1 17 . 1 1 3 3 VAL HG23 H 1 0.99 . . . . . . . 94 VAL HG2 . 7154 1 18 . 1 1 4 4 ARG H H 1 7.99 . . . . . . . 95 ARG H . 7154 1 19 . 1 1 4 4 ARG HA H 1 4.16 . . . . . . . 95 ARG HA . 7154 1 20 . 1 1 4 4 ARG HB2 H 1 1.88 . . . . . . . 95 ARG HB2 . 7154 1 21 . 1 1 4 4 ARG HG2 H 1 1.83 . . . . . . . 95 ARG HG2 . 7154 1 22 . 1 1 4 4 ARG HG3 H 1 1.83 . . . . . . . 95 ARG HG3 . 7154 1 23 . 1 1 4 4 ARG HD2 H 1 3.24 . . . . . . . 95 ARG HD2 . 7154 1 24 . 1 1 4 4 ARG HD3 H 1 3.24 . . . . . . . 95 ARG HD3 . 7154 1 25 . 1 1 4 4 ARG HH11 H 1 7.16 . . . . . . . 95 ARG HH1 . 7154 1 26 . 1 1 4 4 ARG HH12 H 1 6.57 . . . . . . . 95 ARG HH2 . 7154 1 27 . 1 1 5 5 ARG H H 1 7.94 . . . . . . . 96 ARG H . 7154 1 28 . 1 1 5 5 ARG HA H 1 4.07 . . . . . . . 96 ARG HA . 7154 1 29 . 1 1 5 5 ARG HB2 H 1 1.91 . . . . . . . 96 ARG HB2 . 7154 1 30 . 1 1 5 5 ARG HG2 H 1 1.78 . . . . . . . 96 ARG HG2 . 7154 1 31 . 1 1 5 5 ARG HG3 H 1 1.68 . . . . . . . 96 ARG HG3 . 7154 1 32 . 1 1 5 5 ARG HD2 H 1 3.24 . . . . . . . 96 ARG HD2 . 7154 1 33 . 1 1 5 5 ARG HD3 H 1 3.24 . . . . . . . 96 ARG HD3 . 7154 1 34 . 1 1 5 5 ARG HH11 N 1 7.16 . . . . . . . 96 ARG HH1 . 7154 1 35 . 1 1 5 5 ARG HH12 N 1 6.57 . . . . . . . 96 ARG HH2 . 7154 1 36 . 1 1 6 6 ALA H H 1 8.02 . . . . . . . 97 ALA H . 7154 1 37 . 1 1 6 6 ALA HA H 1 4.09 . . . . . . . 97 ALA HA . 7154 1 38 . 1 1 6 6 ALA HB1 H 1 1.51 . . . . . . . 97 ALA HB . 7154 1 39 . 1 1 6 6 ALA HB2 H 1 1.51 . . . . . . . 97 ALA HB . 7154 1 40 . 1 1 6 6 ALA HB3 H 1 1.51 . . . . . . . 97 ALA HB . 7154 1 41 . 1 1 7 7 ALA H H 1 8.08 . . . . . . . 98 ALA H . 7154 1 42 . 1 1 7 7 ALA HA H 1 4.16 . . . . . . . 98 ALA HA . 7154 1 43 . 1 1 7 7 ALA HB1 H 1 1.55 . . . . . . . 98 ALA HB . 7154 1 44 . 1 1 7 7 ALA HB2 H 1 1.55 . . . . . . . 98 ALA HB . 7154 1 45 . 1 1 7 7 ALA HB3 H 1 1.55 . . . . . . . 98 ALA HB . 7154 1 46 . 1 1 8 8 LEU H H 1 7.97 . . . . . . . 99 LEU H . 7154 1 47 . 1 1 8 8 LEU HA H 1 4.20 . . . . . . . 99 LEU HA . 7154 1 48 . 1 1 8 8 LEU HB2 H 1 1.81 . . . . . . . 99 LEU HB2 . 7154 1 49 . 1 1 8 8 LEU HG H 1 1.76 . . . . . . . 99 LEU HG . 7154 1 50 . 1 1 8 8 LEU HD11 H 1 0.94 . . . . . . . 99 LEU HD1 . 7154 1 51 . 1 1 8 8 LEU HD12 H 1 0.94 . . . . . . . 99 LEU HD1 . 7154 1 52 . 1 1 8 8 LEU HD13 H 1 0.94 . . . . . . . 99 LEU HD1 . 7154 1 53 . 1 1 9 9 ILE H H 1 8.19 . . . . . . . 100 ILE H . 7154 1 54 . 1 1 9 9 ILE HA H 1 3.72 . . . . . . . 100 ILE HA . 7154 1 55 . 1 1 9 9 ILE HB H 1 1.92 . . . . . . . 100 ILE HB . 7154 1 56 . 1 1 9 9 ILE HG13 H 1 1.19 . . . . . . . 100 ILE HG13 . 7154 1 57 . 1 1 9 9 ILE HG21 H 1 0.91 . . . . . . . 100 ILE HG2 . 7154 1 58 . 1 1 9 9 ILE HG22 H 1 0.91 . . . . . . . 100 ILE HG2 . 7154 1 59 . 1 1 9 9 ILE HG23 H 1 0.91 . . . . . . . 100 ILE HG2 . 7154 1 60 . 1 1 9 9 ILE HD11 H 1 0.87 . . . . . . . 100 ILE HD1 . 7154 1 61 . 1 1 9 9 ILE HD12 H 1 0.87 . . . . . . . 100 ILE HD1 . 7154 1 62 . 1 1 9 9 ILE HD13 H 1 0.87 . . . . . . . 100 ILE HD1 . 7154 1 63 . 1 1 10 10 ASN H H 1 8.05 . . . . . . . 101 ASN H . 7154 1 64 . 1 1 10 10 ASN HA H 1 4.51 . . . . . . . 101 ASN HA . 7154 1 65 . 1 1 10 10 ASN HB2 H 1 2.93 . . . . . . . 101 ASN HB2 . 7154 1 66 . 1 1 10 10 ASN HB3 H 1 2.81 . . . . . . . 101 ASN HB3 . 7154 1 67 . 1 1 10 10 ASN HD21 H 1 7.40 . . . . . . . 101 ASN HD21 . 7154 1 68 . 1 1 10 10 ASN HD22 H 1 6.40 . . . . . . . 101 ASN HD22 . 7154 1 69 . 1 1 11 11 MET H H 1 8.05 . . . . . . . 102 MET H . 7154 1 70 . 1 1 11 11 MET HA H 1 4.24 . . . . . . . 102 MET HA . 7154 1 71 . 1 1 11 11 MET HB2 H 1 2.33 . . . . . . . 102 MET HB2 . 7154 1 72 . 1 1 11 11 MET HG2 H 1 2.72 . . . . . . . 102 MET HG2 . 7154 1 73 . 1 1 11 11 MET HG3 H 1 2.60 . . . . . . . 102 MET HG3 . 7154 1 74 . 1 1 12 12 VAL H H 1 8.34 . . . . . . . 103 VAL H . 7154 1 75 . 1 1 12 12 VAL HA H 1 3.70 . . . . . . . 103 VAL HA . 7154 1 76 . 1 1 12 12 VAL HB H 1 2.16 . . . . . . . 103 VAL HB . 7154 1 77 . 1 1 12 12 VAL HG11 H 1 1.04 . . . . . . . 103 VAL HG1 . 7154 1 78 . 1 1 12 12 VAL HG12 H 1 1.04 . . . . . . . 103 VAL HG1 . 7154 1 79 . 1 1 12 12 VAL HG13 H 1 1.04 . . . . . . . 103 VAL HG1 . 7154 1 80 . 1 1 12 12 VAL HG21 H 1 0.78 . . . . . . . 103 VAL HG2 . 7154 1 81 . 1 1 12 12 VAL HG22 H 1 0.78 . . . . . . . 103 VAL HG2 . 7154 1 82 . 1 1 12 12 VAL HG23 H 1 0.78 . . . . . . . 103 VAL HG2 . 7154 1 83 . 1 1 13 13 PHE H H 1 8.83 . . . . . . . 104 PHE H . 7154 1 84 . 1 1 13 13 PHE HA H 1 4.45 . . . . . . . 104 PHE HA . 7154 1 85 . 1 1 13 13 PHE HB2 H 1 3.28 . . . . . . . 104 PHE HB2 . 7154 1 86 . 1 1 13 13 PHE HB3 H 1 3.21 . . . . . . . 104 PHE HB3 . 7154 1 87 . 1 1 13 13 PHE HD1 H 1 7.30 . . . . . . . 104 PHE HD1 . 7154 1 88 . 1 1 13 13 PHE HD2 H 1 7.30 . . . . . . . 104 PHE HD2 . 7154 1 89 . 1 1 13 13 PHE HE1 H 1 7.38 . . . . . . . 104 PHE HE1 . 7154 1 90 . 1 1 13 13 PHE HE2 H 1 7.38 . . . . . . . 104 PHE HE2 . 7154 1 91 . 1 1 13 13 PHE HZ H 1 7.34 . . . . . . . 104 PHE HZ . 7154 1 92 . 1 1 14 14 GLN H H 1 8.05 . . . . . . . 105 GLN H . 7154 1 93 . 1 1 14 14 GLN HA H 1 4.24 . . . . . . . 105 GLN HA . 7154 1 94 . 1 1 14 14 GLN HB2 H 1 2.25 . . . . . . . 105 GLN HB2 . 7154 1 95 . 1 1 14 14 GLN HG2 H 1 2.50 . . . . . . . 105 GLN HG2 . 7154 1 96 . 1 1 14 14 GLN HG3 H 1 2.50 . . . . . . . 105 GLN HG3 . 7154 1 97 . 1 1 14 14 GLN HE21 H 1 7.60 . . . . . . . 105 GLN HE21 . 7154 1 98 . 1 1 14 14 GLN HE22 H 1 6.80 . . . . . . . 105 GLN HE22 . 7154 1 99 . 1 1 15 15 MET H H 1 8.16 . . . . . . . 106 MET H . 7154 1 100 . 1 1 15 15 MET HA H 1 4.50 . . . . . . . 106 MET HA . 7154 1 101 . 1 1 15 15 MET HB2 H 1 2.20 . . . . . . . 106 MET HB2 . 7154 1 102 . 1 1 15 15 MET HG2 H 1 2.77 . . . . . . . 106 MET HG2 . 7154 1 103 . 1 1 15 15 MET HG3 H 1 2.66 . . . . . . . 106 MET HG3 . 7154 1 104 . 1 1 16 16 GLY H H 1 7.80 . . . . . . . 107 GLY H . 7154 1 105 . 1 1 16 16 GLY HA2 H 1 4.00 . . . . . . . 107 GLY HA2 . 7154 1 stop_ save_