data_7156 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 7156 _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. . 7156 2 D. Craik . J. . 7156 3 J. Wade . D. . 7156 4 M. McLeish . J. . 7156 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 2 7156 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 312 7156 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 . 7156 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID . 7154 'helix E (lys 92-107)' 7156 . 7155 'helix G (lys 124-137)' 7156 . 7157 'helix F (lys 113-125)' 7156 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 7156 _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. . 7156 1 2 D. Craik . J. . 7156 1 3 J. Wade . D. . 7156 1 4 M. McLeish . J. . 7156 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 7156 _Assembly.ID 1 _Assembly.Name 'HELIX H' _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 H (residues 136-157)' 1 $HELIX_H . . yes unfolded no no . . . 7156 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_HELIX_H _Entity.Sf_category entity _Entity.Sf_framecode HELIX_H _Entity.Entry_ID 7156 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'helix H (lys 136-157)' _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 ; SRWYNQTPNRAKRVITTFRT GT ; _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 22 _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 BMRB 17603 . T4_L99A/G113A/R119P . . . . . 100.00 164 100.00 100.00 3.72e-06 . . . . 7156 1 2 no BMRB 17604 . T4_L99A . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 3 no BMRB 915 . "T4 lysozyme" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 4 no PDB 102L . "How Amino-Acid Insertions Are Allowed In An Alpha-Helix Of T4 Lysozyme" . . . . . 100.00 165 100.00 100.00 3.39e-06 . . . . 7156 1 5 no PDB 103L . "How Amino-Acid Insertions Are Allowed In An Alpha-Helix Of T4 Lysozyme" . . . . . 100.00 167 100.00 100.00 3.34e-06 . . . . 7156 1 6 no PDB 104L . "How Amino-Acid Insertions Are Allowed In An Alpha-Helix Of T4 Lysozyme" . . . . . 100.00 166 100.00 100.00 3.45e-06 . . . . 7156 1 7 no PDB 107L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.72e-06 . . . . 7156 1 8 no PDB 108L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.50e-06 . . . . 7156 1 9 no PDB 109L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.61e-06 . . . . 7156 1 10 no PDB 110L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.47e-06 . . . . 7156 1 11 no PDB 111L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.72e-06 . . . . 7156 1 12 no PDB 112L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 4.11e-06 . . . . 7156 1 13 no PDB 113L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.76e-06 . . . . 7156 1 14 no PDB 114L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.79e-06 . . . . 7156 1 15 no PDB 115L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.50e-06 . . . . 7156 1 16 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 3.68e-06 . . . . 7156 1 17 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 3.68e-06 . . . . 7156 1 18 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 3.68e-06 . . . . 7156 1 19 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 3.68e-06 . . . . 7156 1 20 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 3.68e-06 . . . . 7156 1 21 no PDB 125L . "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 3.68e-06 . . . . 7156 1 22 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 3.72e-06 . . . . 7156 1 23 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 3.72e-06 . . . . 7156 1 24 no PDB 129L . "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 3.99e-06 . . . . 7156 1 25 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 3.43e-06 . . . . 7156 1 26 no PDB 137L . "Structural Basis Of Amino Acid Alpha Helix Propensity" . . . . . 100.00 164 100.00 100.00 3.76e-06 . . . . 7156 1 27 no PDB 138L . "Rapid Crystallization Of T4 Lysozyme By Intermolecular Disulfide Crosslinking" . . . . . 100.00 164 100.00 100.00 3.95e-06 . . . . 7156 1 28 no PDB 139L . "Rapid Crystallization Of T4 Lysozyme By Intermolecular Disulfide Crosslinking" . . . . . 100.00 164 100.00 100.00 4.03e-06 . . . . 7156 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 4.50e-06 . . . . 7156 1 30 no PDB 148L . "A Covalent Enzyme-Substrate Intermediate With Saccharide Distortion In A Mutant T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.23e-06 . . . . 7156 1 31 no PDB 149L . "Conservation Of Solvent-Binding Sites In 10 Crystal Forms Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.95e-06 . . . . 7156 1 32 no PDB 150L . "Conservation Of Solvent-Binding Sites In 10 Crystal Forms Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 4.11e-06 . . . . 7156 1 33 no PDB 151L . "Conservation Of Solvent-Binding Sites In 10 Crystal Forms Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 7.46e-06 . . . . 7156 1 34 no PDB 155L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 100.00 100.00 3.33e-06 . . . . 7156 1 35 no PDB 156L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 100.00 100.00 3.13e-06 . . . . 7156 1 36 no PDB 157L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 100.00 100.00 2.83e-06 . . . . 7156 1 37 no PDB 158L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 100.00 100.00 3.30e-06 . . . . 7156 1 38 no PDB 159L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 100.00 100.00 3.23e-06 . . . . 7156 1 39 no PDB 160L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 100.00 100.00 3.68e-06 . . . . 7156 1 40 no PDB 161L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 100.00 100.00 3.33e-06 . . . . 7156 1 41 no PDB 162L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 100.00 100.00 3.57e-06 . . . . 7156 1 42 no PDB 163L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 100.00 100.00 3.57e-06 . . . . 7156 1 43 no PDB 164L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 100.00 100.00 3.26e-06 . . . . 7156 1 44 no PDB 165L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 100.00 100.00 3.47e-06 . . . . 7156 1 45 no PDB 166L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 100.00 100.00 3.30e-06 . . . . 7156 1 46 no PDB 167L . "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 4.50e-06 . . . . 7156 1 47 no PDB 168L . "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" . . . . . 90.91 164 100.00 100.00 8.72e-05 . . . . 7156 1 48 no PDB 169L . "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" . . . . . 72.73 164 100.00 100.00 9.64e-01 . . . . 7156 1 49 no PDB 171L . "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.68e-06 . . . . 7156 1 50 no PDB 172L . "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 51 no PDB 174L . "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 1.10e-05 . . . . 7156 1 52 no PDB 175L . "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.26e-06 . . . . 7156 1 53 no PDB 176L . "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.47e-06 . . . . 7156 1 54 no PDB 180L . "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.23e-06 . . . . 7156 1 55 no PDB 181L . "Specificity Of Ligand Binding In A Buried Non-Polar Cavity Of T4 Lysozyme: Linkage Of Dynamics And Structural Plasticity" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 56 no PDB 182L . "Specificity Of Ligand Binding In A Buried Non-Polar Cavity Of T4 Lysozyme: Linkage Of Dynamics And Structural Plasticity" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 57 no PDB 183L . "Specificity Of Ligand Binding In A Buried Non-Polar Cavity Of T4 Lysozyme: Linkage Of Dynamics And Structural Plasticity" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 58 no PDB 184L . "Specificity Of Ligand Binding In A Buried Non-Polar Cavity Of T4 Lysozyme: Linkage Of Dynamics And Structural Plasticity" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 59 no PDB 185L . "Specificity Of Ligand Binding In A Buried Non-Polar Cavity Of T4 Lysozyme: Linkage Of Dynamics And Structural Plasticity" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 60 no PDB 186L . "Specificity Of Ligand Binding In A Buried Non-Polar Cavity Of T4 Lysozyme: Linkage Of Dynamics And Structural Plasticity" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 61 no PDB 187L . "Specificity Of Ligand Binding In A Buried Non-Polar Cavity Of T4 Lysozyme: Linkage Of Dynamics And Structural Plasticity" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 62 no PDB 188L . "Specificity Of Ligand Binding In A Buried Non-Polar Cavity Of T4 Lysozyme: Linkage Of Dynamics And Structural Plasticity" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 63 no PDB 190L . "A Helix Initiation Signal In T4 Lysozyme Identified By Polyalanine Mutagenesis" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 64 no PDB 191L . "A Helix Initiation Signal In T4 Lysozyme Identified By Polyalanine Mutagenesis" . . . . . 100.00 164 100.00 100.00 3.33e-06 . . . . 7156 1 65 no PDB 192L . "A Helix Initiation Signal In T4 Lysozyme Identified By Polyalanine Mutagenesis" . . . . . 100.00 164 100.00 100.00 3.01e-06 . . . . 7156 1 66 no PDB 195L . 'Thermodynamic And Structural Compensation In "size-Switch" Core-Repacking Variants Of T4 Lysozyme' . . . . . 100.00 164 100.00 100.00 3.47e-06 . . . . 7156 1 67 no PDB 196L . 'Thermodynamic And Structural Compensation In "size-Switch" Core-Repacking Variants Of T4 Lysozyme' . . . . . 100.00 164 100.00 100.00 3.47e-06 . . . . 7156 1 68 no PDB 198L . 'Thermodynamic And Structural Compensation In "size-Switch" Core-Repacking Variants Of T4 Lysozyme' . . . . . 100.00 164 100.00 100.00 3.61e-06 . . . . 7156 1 69 no PDB 199L . 'Thermodynamic And Structural Compensation In "size-Switch" Core-Repacking Variants Of T4 Lysozyme' . . . . . 100.00 164 100.00 100.00 3.40e-06 . . . . 7156 1 70 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 3.91e-06 . . . . 7156 1 71 no PDB 1C63 . "T4 Lysozyme Mutant C54tC97AL121A IN THE PRESENCE OF 8 ATM Argon" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 72 no PDB 1C64 . "T4 Lysozyme Mutant C54tC97AL121A IN THE PRESENCE OF 8 ATM Krypton" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 73 no PDB 1C65 . "T4 Lysozyme Mutant C54tC97AL121A IN THE PRESENCE OF 8 ATM Xenon" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 74 no PDB 1C66 . "T4 Lysozyme Mutant C54tC97AL121AL133A IN THE PRESENCE OF 8 Atm Argon" . . . . . 100.00 164 100.00 100.00 3.68e-06 . . . . 7156 1 75 no PDB 1C67 . "T4 Lysozyme Mutant C54tC97AL121AL133A IN THE PRESENCE OF 8 Atm Krypton" . . . . . 100.00 164 100.00 100.00 3.68e-06 . . . . 7156 1 76 no PDB 1C68 . "T4 Lysozyme Mutant C54tC97AL121AL133A IN THE PRESENCE OF 8 Atm Xenon" . . . . . 100.00 164 100.00 100.00 3.68e-06 . . . . 7156 1 77 no PDB 1C69 . "T4 Lysozyme Mutant C54tC97AL133A IN THE PRESENCE OF 8 ATM Argon" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 78 no PDB 1C6A . "T4 Lysozyme Mutant C54tC97AL133A IN THE PRESENCE OF 8 ATM Krypton" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 79 no PDB 1C6B . "T4 Lysozyme Mutant C54tC97AL133A IN THE PRESENCE OF 8 ATM Xenon" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 80 no PDB 1C6C . "T4 Lysozyme Mutant C54tC97AL99A IN THE PRESENCE OF 16 ATM Argon" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 81 no PDB 1C6D . "T4 Lysozyme Mutant C54tC97AL99A IN THE PRESENCE OF 16 ATM Krypton" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 82 no PDB 1C6E . "T4 Lysozyme Mutant C54tC97AL99A IN THE PRESENCE OF 2 ATM Xenon" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 83 no PDB 1C6F . "T4 Lysozyme Mutant C54tC97AL99A IN THE PRESENCE OF 32 ATM Argon" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 84 no PDB 1C6G . "T4 Lysozyme Mutant C54tC97AL99A IN THE PRESENCE OF 4 ATM Krypton" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 85 no PDB 1C6H . "T4 Lysozyme Mutant C54tC97AL99A IN THE PRESENCE OF 4 ATM Xenon" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 86 no PDB 1C6I . "T4 Lysozyme Mutant C54tC97AL99A IN THE PRESENCE OF 8 ATM Argon" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 87 no PDB 1C6J . "T4 Lysozyme Mutant C54tC97AL99A IN THE PRESENCE OF 8 ATM Krypton" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 88 no PDB 1C6K . "T4 Lysozyme Mutant C54tC97AL99A IN THE PRESENCE OF 8 ATM Xenon" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 89 no PDB 1C6P . "T4 Lysozyme Mutant C54tC97A IN THE PRESENCE OF 8 ATM ARGON" . . . . . 100.00 164 100.00 100.00 3.61e-06 . . . . 7156 1 90 no PDB 1C6Q . "T4 Lysozyme Mutant C54tC97A IN THE PRESENCE OF 8 ATM Krypton" . . . . . 100.00 164 100.00 100.00 3.61e-06 . . . . 7156 1 91 no PDB 1C6T . "T4 Lysozyme Mutant C54tC97A IN THE PRESENCE OF 8 ATM XENON" . . . . . 100.00 164 100.00 100.00 3.61e-06 . . . . 7156 1 92 no PDB 1CTW . "T4 Lysozyme Mutant I78a" . . . . . 100.00 164 100.00 100.00 3.43e-06 . . . . 7156 1 93 no PDB 1CU0 . "T4 Lysozyme Mutant I78m" . . . . . 100.00 164 100.00 100.00 3.36e-06 . . . . 7156 1 94 no PDB 1CU2 . "T4 Lysozyme Mutant L84m" . . . . . 100.00 164 100.00 100.00 3.40e-06 . . . . 7156 1 95 no PDB 1CU3 . "T4 Lysozyme Mutant V87m" . . . . . 100.00 164 100.00 100.00 3.36e-06 . . . . 7156 1 96 no PDB 1CU5 . "T4 Lysozyme Mutant L91m" . . . . . 100.00 164 100.00 100.00 3.40e-06 . . . . 7156 1 97 no PDB 1CU6 . "T4 Lysozyme Mutant L91a" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 98 no PDB 1CUP . "Methionine Core Mutant Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.36e-06 . . . . 7156 1 99 no PDB 1CUQ . "T4 Lysozyme Mutant V103m" . . . . . 100.00 164 100.00 100.00 3.36e-06 . . . . 7156 1 100 no PDB 1CV0 . "T4 Lysozyme Mutant F104m" . . . . . 100.00 164 100.00 100.00 3.17e-06 . . . . 7156 1 101 no PDB 1CV1 . "T4 Lysozyme Mutant V111m" . . . . . 100.00 164 100.00 100.00 3.36e-06 . . . . 7156 1 102 no PDB 1CV3 . "T4 Lysozyme Mutant L121m" . . . . . 100.00 164 100.00 100.00 3.40e-06 . . . . 7156 1 103 no PDB 1CV4 . "T4 Lysozyme Mutant L118m" . . . . . 100.00 164 100.00 100.00 3.40e-06 . . . . 7156 1 104 no PDB 1CV5 . "T4 Lysozyme Mutant L133m" . . . . . 100.00 164 100.00 100.00 3.40e-06 . . . . 7156 1 105 no PDB 1CVK . "T4 Lysozyme Mutant L118a" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 106 no PDB 1D2W . "N-Terminal Domain Core Methionine Mutation" . . . . . 100.00 164 100.00 100.00 3.36e-06 . . . . 7156 1 107 no PDB 1D2Y . "N-Terminal Domain Core Methionine Mutation" . . . . . 100.00 164 100.00 100.00 3.36e-06 . . . . 7156 1 108 no PDB 1D3F . "N-Terminal Domain Core Methionine Mutation" . . . . . 100.00 164 100.00 100.00 3.36e-06 . . . . 7156 1 109 no PDB 1D3J . "N-Terminal Domain Core Methionine Mutation" . . . . . 100.00 164 100.00 100.00 3.40e-06 . . . . 7156 1 110 no PDB 1D3M . "Methionine Core Mutation" . . . . . 100.00 164 100.00 100.00 3.30e-06 . . . . 7156 1 111 no PDB 1D3N . "Methionine Core Mutation" . . . . . 100.00 164 100.00 100.00 5.57e-06 . . . . 7156 1 112 no PDB 1D9W . "Bacteriophage T4 Lysozyme Mutant" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 113 no PDB 1DYA . "Determination Of Alpha-Helix Propensity Within The Context Of A Folded Protein: Sites 44 And 131 In Bacteriophage T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 114 no PDB 1DYB . "Determination Of Alpha-Helix Propensity Within The Context Of A Folded Protein: Sites 44 And 131 In Bacteriophage T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 4.07e-06 . . . . 7156 1 115 no PDB 1DYC . "Determination Of Alpha-Helix Propensity Within The Context Of A Folded Protein: Sites 44 And 131 In Bacteriophage T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 4.03e-06 . . . . 7156 1 116 no PDB 1DYD . "Determination Of Alpha-Helix Propensity Within The Context Of A Folded Protein: Sites 44 And 131 In Bacteriophage T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.95e-06 . . . . 7156 1 117 no PDB 1DYE . "Determination Of Alpha-Helix Propensity Within The Context Of A Folded Protein: Sites 44 And 131 In Bacteriophage T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.95e-06 . . . . 7156 1 118 no PDB 1DYF . "Determination Of Alpha-Helix Propensity Within The Context Of A Folded Protein: Sites 44 And 131 In Bacteriophage T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.95e-06 . . . . 7156 1 119 no PDB 1DYG . "Determination Of Alpha-Helix Propensity Within The Context Of A Folded Protein: Sites 44 And 131 In Bacteriophage T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.91e-06 . . . . 7156 1 120 no PDB 1G1V . "T4 Lysozyme Mutant C54tC97AI58T" . . . . . 100.00 164 100.00 100.00 3.57e-06 . . . . 7156 1 121 no PDB 1G1W . "T4 Lysozyme Mutant C54tC97AQ105M" . . . . . 100.00 164 100.00 100.00 3.36e-06 . . . . 7156 1 122 no PDB 1I6S . "T4 Lysozyme Mutant C54tC97AN101A" . . . . . 100.00 164 100.00 100.00 3.33e-06 . . . . 7156 1 123 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 2.86e-06 . . . . 7156 1 124 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 4.12e-06 . . . . 7156 1 125 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 4.12e-06 . . . . 7156 1 126 no PDB 1KS3 . "Methionine Core Mutant Of T4 Lysozyme" . . . . . 100.00 162 100.00 100.00 3.70e-06 . . . . 7156 1 127 no PDB 1KW5 . "Methionine Core Mutant Of T4 Lysozyme" . . . . . 100.00 162 100.00 100.00 3.67e-06 . . . . 7156 1 128 no PDB 1KW7 . "Methionine Core Mutant Of T4 Lysozyme" . . . . . 100.00 162 100.00 100.00 3.67e-06 . . . . 7156 1 129 no PDB 1KY1 . "Methionine Core Mutant Of T4 Lysozyme" . . . . . 100.00 162 100.00 100.00 3.56e-06 . . . . 7156 1 130 no PDB 1L00 . "Perturbation Of Trp 138 In T4 Lysozyme By Mutations At Gln 105 Used To Correlate Changes In Structure, Stability, Solvation, An" . . . . . 100.00 164 100.00 100.00 3.87e-06 . . . . 7156 1 131 no PDB 1L04 . "Contributions Of Hydrogen Bonds Of Thr 157 To The Thermodynamic Stability Of Phage T4 Lysozyme" . . . . . 95.45 164 100.00 100.00 1.40e-05 . . . . 7156 1 132 no PDB 1L05 . "Contributions Of Hydrogen Bonds Of Thr 157 To The Thermodynamic Stability Of Phage T4 Lysozyme" . . . . . 95.45 164 100.00 100.00 1.40e-05 . . . . 7156 1 133 no PDB 1L06 . "Contributions Of Hydrogen Bonds Of Thr 157 To The Thermodynamic Stability Of Phage T4 Lysozyme" . . . . . 95.45 164 100.00 100.00 1.40e-05 . . . . 7156 1 134 no PDB 1L07 . "Contributions Of Hydrogen Bonds Of Thr 157 To The Thermodynamic Stability Of Phage T4 Lysozyme" . . . . . 95.45 164 100.00 100.00 1.47e-05 . . . . 7156 1 135 no PDB 1L08 . "Contributions Of Hydrogen Bonds Of Thr 157 To The Thermodynamic Stability Of Phage T4 Lysozyme" . . . . . 95.45 164 100.00 100.00 1.44e-05 . . . . 7156 1 136 no PDB 1L09 . "Contributions Of Hydrogen Bonds Of Thr 157 To The Thermodynamic Stability Of Phage T4 Lysozyme" . . . . . 95.45 164 100.00 100.00 1.42e-05 . . . . 7156 1 137 no PDB 1L0K . "Methionine Core Mutant Of T4 Lysozyme" . . . . . 100.00 162 100.00 100.00 3.35e-06 . . . . 7156 1 138 no PDB 1L10 . "Structural Studies Of Mutants Of The Lysozyme Of Bacteriophage T4. The Temperature-Sensitive Mutant Protein Thr157 (Right Arrow" . . . . . 95.45 164 100.00 100.00 1.43e-05 . . . . 7156 1 139 no PDB 1L11 . "Contributions Of Hydrogen Bonds Of Thr 157 To The Thermodynamic Stability Of Phage T4 Lysozyme" . . . . . 95.45 164 100.00 100.00 1.40e-05 . . . . 7156 1 140 no PDB 1L12 . "Contributions Of Hydrogen Bonds Of Thr 157 To The Thermodynamic Stability Of Phage T4 Lysozyme" . . . . . 95.45 164 100.00 100.00 1.46e-05 . . . . 7156 1 141 no PDB 1L13 . "Contributions Of Hydrogen Bonds Of Thr 157 To The Thermodynamic Stability Of Phage T4 Lysozyme" . . . . . 95.45 164 100.00 100.00 1.46e-05 . . . . 7156 1 142 no PDB 1L17 . "Hydrophobic Stabilization In T4 Lysozyme Determined Directly By Multiple Substitutions Of Ile 3" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 143 no PDB 1L18 . "Hydrophobic Stabilization In T4 Lysozyme Determined Directly By Multiple Substitutions Of Ile 3" . . . . . 100.00 164 100.00 100.00 4.15e-06 . . . . 7156 1 144 no PDB 1L19 . "Enhanced Protein Thermostability From Designed Mutations That Interact With Alpha-helix Dipoles" . . . . . 100.00 164 100.00 100.00 3.91e-06 . . . . 7156 1 145 no PDB 1L21 . "Contributions Of Left-Handed Helical Residues To The Structure And Stability Of Bacteriophage T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.95e-06 . . . . 7156 1 146 no PDB 1L22 . "Contributions Of Left-Handed Helical Residues To The Structure And Stability Of Bacteriophage T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 4.07e-06 . . . . 7156 1 147 no PDB 1L23 . "Enhanced Protein Thermostability From Site-Directed Mutations That Decrease The Entropy Of Unfolding" . . . . . 100.00 164 100.00 100.00 3.87e-06 . . . . 7156 1 148 no PDB 1L24 . "Enhanced Protein Thermostability From Site-directed Mutations That Decrease The Entropy Of Unfolding" . . . . . 100.00 164 100.00 100.00 4.78e-06 . . . . 7156 1 149 no PDB 1L25 . "Replacements Of Pro86 In Phage T4 Lysozyme Extend An Alpha-Helix But Do Not Alter Protein Stability" . . . . . 100.00 164 100.00 100.00 3.57e-06 . . . . 7156 1 150 no PDB 1L26 . "Replacements Of Pro86 In Phage T4 Lysozyme Extend An Alpha-helix But Do Not Alter Protein Stability" . . . . . 100.00 164 100.00 100.00 3.68e-06 . . . . 7156 1 151 no PDB 1L27 . "Replacements Of Pro86 In Phage T4 Lysozyme Extend An Alpha-Helix But Do Not Alter Protein Stability" . . . . . 100.00 164 100.00 100.00 3.57e-06 . . . . 7156 1 152 no PDB 1L28 . "Replacements Of Pro86 In Phage T4 Lysozyme Extend An Alpha-Helix But Do Not Alter Protein Stability" . . . . . 100.00 164 100.00 100.00 3.76e-06 . . . . 7156 1 153 no PDB 1L29 . "Replacements Of Pro86 In Phage T4 Lysozyme Extend An Alpha-Helix But Do Not Alter Protein Stability" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 154 no PDB 1L30 . "Replacements Of Pro86 In Phage T4 Lysozyme Extend An Alpha-Helix But Do Not Alter Protein Stability" . . . . . 100.00 164 100.00 100.00 3.47e-06 . . . . 7156 1 155 no PDB 1L31 . "Replacements Of Pro86 In Phage T4 Lysozyme Extend An Alpha-Helix But Do Not Alter Protein Stability" . . . . . 100.00 164 100.00 100.00 3.79e-06 . . . . 7156 1 156 no PDB 1L32 . "Replacements Of Pro86 In Phage T4 Lysozyme Extend An Alpha-Helix But Do Not Alter Protein Stability" . . . . . 100.00 164 100.00 100.00 3.57e-06 . . . . 7156 1 157 no PDB 1L33 . "Contributions Of Left-Handed Helical Residues To The Structure And Stability Of Bacteriophage T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.95e-06 . . . . 7156 1 158 no PDB 1L34 . "High-Resolution Structure Of The Temperature-Sensitive Mutant Of Phage Lysozyme, Arg 96 (Right Arrow) His" . . . . . 100.00 164 100.00 100.00 3.87e-06 . . . . 7156 1 159 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 4.07e-06 . . . . 7156 1 160 no PDB 1L36 . "Toward A Simplification Of The Protein Folding Problem: A Stabilizing Polyalanine Alpha-Helix Engineered In T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.79e-06 . . . . 7156 1 161 no PDB 1L37 . "Contributions Of Engineered Surface Salt Bridges To The Stability Of T4 Lysozyme Determined By Directed Mutagenesis" . . . . . 100.00 164 100.00 100.00 3.79e-06 . . . . 7156 1 162 no PDB 1L38 . "Contributions Of Engineered Surface Salt Bridges To The Stability Of T4 Lysozyme Determined By Directed Mutagenesis" . . . . . 100.00 164 100.00 100.00 3.91e-06 . . . . 7156 1 163 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 3.64e-06 . . . . 7156 1 164 no PDB 1L42 . "Cumulative Site-Directed Charge-Change Replacements In Bacteriophage T4 Lysozyme Suggest That Long-Range Electrostatic Interact" . . . . . 100.00 164 100.00 100.00 3.91e-06 . . . . 7156 1 165 no PDB 1L43 . "Cumulative Site-Directed Charge-Change Replacements In Bacteriophage T4 Lysozyme Suggest That Long-Range Electrostatic Interact" . . . . . 100.00 164 100.00 100.00 3.91e-06 . . . . 7156 1 166 no PDB 1L44 . "Cumulative Site-Directed Charge-Change Replacements In Bacteriophage T4 Lysozyme Suggest That Long-Range Electrostatic Interact" . . . . . 100.00 164 100.00 100.00 3.83e-06 . . . . 7156 1 167 no PDB 1L45 . "Cumulative Site-Directed Charge-Change Replacements In Bacteriophage T4 Lysozyme Suggest That Long-Range Electrostatic Interact" . . . . . 100.00 164 100.00 100.00 3.91e-06 . . . . 7156 1 168 no PDB 1L48 . "Structural And Thermodynamic Analysis Of The Packing Of Two Alpha- Helices In Bacteriophage T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 169 no PDB 1L54 . "The Structural And Thermodynamic Consequences Of Burying A Charged Residue Within The Hydrophobic Core Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.83e-06 . . . . 7156 1 170 no PDB 1L55 . "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 3.91e-06 . . . . 7156 1 171 no PDB 1L56 . "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 4.64e-06 . . . . 7156 1 172 no PDB 1L57 . "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 3.83e-06 . . . . 7156 1 173 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 3.54e-06 . . . . 7156 1 174 no PDB 1L60 . "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 3.87e-06 . . . . 7156 1 175 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 3.72e-06 . . . . 7156 1 176 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 3.30e-06 . . . . 7156 1 177 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 3.61e-06 . . . . 7156 1 178 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 3.23e-06 . . . . 7156 1 179 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 3.50e-06 . . . . 7156 1 180 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 3.57e-06 . . . . 7156 1 181 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 3.64e-06 . . . . 7156 1 182 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 3.47e-06 . . . . 7156 1 183 no PDB 1L69 . "Multiple Stabilizing Alanine Replacements Within Alpha- Helix 126-134 Of T4 Lysozyme Have Independent, Additive Effects On Both" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 184 no PDB 1L70 . "Multiple Stabilizing Alanine Replacements Within Alpha- Helix 126-134 Of T4 Lysozyme Have Independent, Additive Effects On Both" . . . . . 100.00 164 100.00 100.00 3.76e-06 . . . . 7156 1 185 no PDB 1L71 . "Multiple Stabilizing Alanine Replacements Within Alpha- Helix 126-134 Of T4 Lysozyme Have Independent, Additive Effects On Both" . . . . . 100.00 164 100.00 100.00 3.91e-06 . . . . 7156 1 186 no PDB 1L72 . "Multiple Stabilizing Alanine Replacements Within Alpha- Helix 126-134 Of T4 Lysozyme Have Independent, Additive Effects On Both" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 187 no PDB 1L73 . "Multiple Stabilizing Alanine Replacements Within Alpha- Helix 126-134 Of T4 Lysozyme Have Independent, Additive Effects On Both" . . . . . 100.00 164 100.00 100.00 3.76e-06 . . . . 7156 1 188 no PDB 1L74 . "Multiple Stabilizing Alanine Replacements Within Alpha- Helix 126-134 Of T4 Lysozyme Have Independent, Additive Effects On Both" . . . . . 100.00 164 100.00 100.00 3.91e-06 . . . . 7156 1 189 no PDB 1L75 . "Multiple Stabilizing Alanine Replacements Within Alpha- Helix 126-134 Of T4 Lysozyme Have Independent, Additive Effects On Both" . . . . . 100.00 164 100.00 100.00 3.91e-06 . . . . 7156 1 190 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 4.11e-06 . . . . 7156 1 191 no PDB 1L77 . "Design And Structural Analysis Of Alternative Hydrophobic Core Packing Arrangements In Bacteriophage T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.68e-06 . . . . 7156 1 192 no PDB 1L79 . "Design And Structural Analysis Of Alternative Hydrophobic Core Packing Arrangements In Bacteriophage T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 4.07e-06 . . . . 7156 1 193 no PDB 1L80 . "Design And Structural Analysis Of Alternative Hydrophobic Core Packing Arrangements In Bacteriophage T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 4.07e-06 . . . . 7156 1 194 no PDB 1L83 . "A Cavity-Containing Mutant Of T4 Lysozyme Is Stabilized By Buried Benzene" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 195 no PDB 1L90 . "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 3.64e-06 . . . . 7156 1 196 no PDB 1L91 . "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 4.03e-06 . . . . 7156 1 197 no PDB 1L92 . "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 3.72e-06 . . . . 7156 1 198 no PDB 1L93 . "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 3.40e-06 . . . . 7156 1 199 no PDB 1L94 . "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 3.68e-06 . . . . 7156 1 200 no PDB 1L96 . "Structure Of A Hinge-bending Bacteriophage T4 Lysozyme Mutant, Ile3-> Pro" . . . . . 100.00 164 100.00 100.00 4.55e-06 . . . . 7156 1 201 no PDB 1L97 . "Structure Of A Hinge-Bending Bacteriophage T4 Lysozyme Mutant, Ile3-> Pro" . . . . . 100.00 164 100.00 100.00 4.55e-06 . . . . 7156 1 202 no PDB 1L98 . "Perturbation Of Trp 138 In T4 Lysozyme By Mutations At Gln 105 Used To Correlate Changes In Structure, Stability, Solvation, An" . . . . . 100.00 164 100.00 100.00 3.91e-06 . . . . 7156 1 203 no PDB 1L99 . "Perturbation Of Trp 138 In T4 Lysozyme By Mutations At Gln 105 Used To Correlate Changes In Structure, Stability, Solvation, An" . . . . . 100.00 164 100.00 100.00 4.03e-06 . . . . 7156 1 204 no PDB 1LGU . "T4 Lysozyme Mutant L99aM102Q" . . . . . 100.00 164 100.00 100.00 4.03e-06 . . . . 7156 1 205 no PDB 1LGW . "T4 Lysozyme Mutant L99aM102Q BOUND BY 2-Fluoroaniline" . . . . . 100.00 164 100.00 100.00 4.03e-06 . . . . 7156 1 206 no PDB 1LGX . "T4 Lysozyme Mutant L99aM102Q BOUND BY 3,5-Difluoroaniline" . . . . . 100.00 164 100.00 100.00 4.03e-06 . . . . 7156 1 207 no PDB 1LI2 . "T4 Lysozyme Mutant L99aM102Q BOUND BY PHENOL" . . . . . 100.00 164 100.00 100.00 4.03e-06 . . . . 7156 1 208 no PDB 1LI3 . "T4 Lysozyme Mutant L99aM102Q BOUND BY 3-Chlorophenol" . . . . . 100.00 164 100.00 100.00 4.03e-06 . . . . 7156 1 209 no PDB 1LI6 . "T4 Lysozyme Mutant L99aM102Q BOUND BY 5-Methylpyrrole" . . . . . 100.00 164 100.00 100.00 4.03e-06 . . . . 7156 1 210 no PDB 1LLH . "Are Carboxy Terminii Of Helices Coded By The Local Sequence Or By Tertiary Structure Contacts" . . . . . 95.45 164 100.00 100.00 1.28e-05 . . . . 7156 1 211 no PDB 1LPY . "Multiple Methionine Substitutions In T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 5.85e-06 . . . . 7156 1 212 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 3.61e-06 . . . . 7156 1 213 no PDB 1LWG . "Multiple Methionine Substitutions Are Tolerated In T4 Lysozyme And Have Coupled Effects On Folding And Stability" . . . . . 100.00 164 100.00 100.00 3.13e-06 . . . . 7156 1 214 no PDB 1LYD . "Crystal Structure Of T4-Lysozyme Generated From Synthetic Coding Dna Expressed In Escherichia Coli" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 215 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 3.50e-06 . . . . 7156 1 216 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 3.43e-06 . . . . 7156 1 217 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 3.54e-06 . . . . 7156 1 218 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 3.54e-06 . . . . 7156 1 219 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 3.30e-06 . . . . 7156 1 220 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 3.30e-06 . . . . 7156 1 221 no PDB 1NHB . "Specificity Of Ligand Binding In A Buried Non-polar Cavity Of T4 Lysozyme: Linkage Of Dynamics And Structural Plasticity" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 222 no PDB 1OV5 . "T4 Lysozyme Cavity Mutant L99aM102Q BOUND WITH 2- Allylphenol" . . . . . 100.00 164 100.00 100.00 4.03e-06 . . . . 7156 1 223 no PDB 1OV7 . "T4 Lysozyme Cavity Mutant L99aM102Q BOUND WITH 2-Allyl-6- Methyl-Phenol" . . . . . 100.00 164 100.00 100.00 4.03e-06 . . . . 7156 1 224 no PDB 1OVH . "T4 Lysozyme Cavity Mutant L99aM102Q BOUND WITH 2-Chloro-6- Methyl-Aniline" . . . . . 100.00 164 100.00 100.00 4.03e-06 . . . . 7156 1 225 no PDB 1OVJ . "T4 Lysozyme Cavity Mutant L99a/m102q Bound With 3-fluoro-2- Methyl_aniline" . . . . . 100.00 164 100.00 100.00 4.03e-06 . . . . 7156 1 226 no PDB 1OVK . "T4 Lysozyme Cavity Mutant L99aM102Q BOUND WITH N-Allyl- Aniline" . . . . . 100.00 164 100.00 100.00 4.03e-06 . . . . 7156 1 227 no PDB 1OWY . "T4 Lysozyme Cavity Mutant L99a/m102q Bound With 2-propyl- Aniline" . . . . . 100.00 164 100.00 100.00 4.03e-06 . . . . 7156 1 228 no PDB 1OWZ . "T4 Lysozyme Cavity Mutant L99aM102Q BOUND WITH 4- Fluorophenethyl Alcohol" . . . . . 100.00 164 100.00 100.00 4.03e-06 . . . . 7156 1 229 no PDB 1OYU . "Long-Distance Conformational Changes In A Protein Engineered By Modulated Sequence Duplication" . . . . . 100.00 175 100.00 100.00 5.89e-06 . . . . 7156 1 230 no PDB 1P2L . "T4 Lysozyme Core Repacking Mutant V87iTA" . . . . . 100.00 164 100.00 100.00 3.47e-06 . . . . 7156 1 231 no PDB 1P2R . "T4 Lysozyme Core Repacking Mutant I78vTA" . . . . . 100.00 164 100.00 100.00 3.57e-06 . . . . 7156 1 232 no PDB 1P36 . "T4 Lyoszyme Core Repacking Mutant I100vTA" . . . . . 100.00 164 100.00 100.00 3.57e-06 . . . . 7156 1 233 no PDB 1P46 . "T4 Lysozyme Core Repacking Mutant M106iTA" . . . . . 100.00 164 100.00 100.00 3.72e-06 . . . . 7156 1 234 no PDB 1P56 . "Duplication-Extension Of Helix A Of T4 Lysozyme" . . . . . 100.00 176 100.00 100.00 3.67e-06 . . . . 7156 1 235 no PDB 1P5C . "Circular Permutation Of Helix A In T4 Lysozyme" . . . . . 100.00 167 100.00 100.00 3.44e-06 . . . . 7156 1 236 no PDB 1P64 . "T4 Lysozyme Core Repacking Mutant L133fTA" . . . . . 100.00 164 100.00 100.00 4.03e-06 . . . . 7156 1 237 no PDB 1P6Y . "T4 Lysozyme Core Repacking Mutant M120y/ta" . . . . . 100.00 164 100.00 100.00 4.03e-06 . . . . 7156 1 238 no PDB 1P7S . "T4 Lysozyme Core Repacking Mutant V103iTA" . . . . . 100.00 164 100.00 100.00 3.47e-06 . . . . 7156 1 239 no PDB 1PQO . "T4 Lysozyme Core Repacking Mutant L118iTA" . . . . . 100.00 164 100.00 100.00 3.72e-06 . . . . 7156 1 240 no PDB 1QS5 . "The Introduction Of Strain And Its Effects On The Structure And Stability Of T4 Lysozyme" . . . . . 100.00 162 100.00 100.00 3.74e-06 . . . . 7156 1 241 no PDB 1QS9 . "The Introduction Of Strain And Its Effects On The Structure And Stability Of T4 Lysozyme" . . . . . 100.00 162 100.00 100.00 3.78e-06 . . . . 7156 1 242 no PDB 1QSB . "The Introduction Of Strain And Its Effects On The Structure And Stability Of T4 Lysozyme" . . . . . 100.00 162 100.00 100.00 3.97e-06 . . . . 7156 1 243 no PDB 1QSQ . "Cavity Creating Mutation" . . . . . 100.00 164 100.00 100.00 3.68e-06 . . . . 7156 1 244 no PDB 1QT3 . "T26d Mutant Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.30e-06 . . . . 7156 1 245 no PDB 1QT4 . "T26q Mutant Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.43e-06 . . . . 7156 1 246 no PDB 1QT5 . "D20e Mutant Structure Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.57e-06 . . . . 7156 1 247 no PDB 1QT6 . "E11h Mutant Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 248 no PDB 1QT7 . "E11n Mutant Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.76e-06 . . . . 7156 1 249 no PDB 1QT8 . "T26h Mutant Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.68e-06 . . . . 7156 1 250 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 3.78e-06 . . . . 7156 1 251 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 3.89e-06 . . . . 7156 1 252 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 4.44e-06 . . . . 7156 1 253 no PDB 1QTH . "The Introduction Of Strain And Its Effects On The Structure And Stability Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.47e-06 . . . . 7156 1 254 no PDB 1QTV . "T26e Apo Structure Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.23e-06 . . . . 7156 1 255 no PDB 1QTZ . "D20c Mutant Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.95e-06 . . . . 7156 1 256 no PDB 1QUD . "L99g Mutant Of T4 Lysozyme" . . . . . 100.00 162 100.00 100.00 3.93e-06 . . . . 7156 1 257 no PDB 1QUG . "E108v Mutant Of T4 Lysozyme" . . . . . 100.00 162 100.00 100.00 3.82e-06 . . . . 7156 1 258 no PDB 1QUH . "L99gE108V MUTANT OF T4 LYSOZYME" . . . . . 100.00 162 100.00 100.00 4.01e-06 . . . . 7156 1 259 no PDB 1QUO . "L99aE108V MUTANT OF T4 LYSOZYME" . . . . . 100.00 162 100.00 100.00 3.85e-06 . . . . 7156 1 260 no PDB 1SSW . "Crystal Structure Of Phage T4 Lysozyme Mutant Y24aY25AT26AI27AC54TC97A" . . . . . 100.00 164 100.00 100.00 2.83e-06 . . . . 7156 1 261 no PDB 1SSY . "Crystal Structure Of Phage T4 Lysozyme Mutant G28aI29AG30AC54TC97A" . . . . . 100.00 164 100.00 100.00 3.20e-06 . . . . 7156 1 262 no PDB 1SWY . "Use Of A Halide Binding Site To Bypass The 1000-Atom Limit To Ab Initio Structure Determination" . . . . . 100.00 164 100.00 100.00 3.83e-06 . . . . 7156 1 263 no PDB 1SWZ . "Use Of An Ion-Binding Site To Bypass The 1000-Atom Limit To Ab Initio Structure Determination By Direct Methods" . . . . . 100.00 164 100.00 100.00 3.83e-06 . . . . 7156 1 264 no PDB 1SX2 . "Use Of A Halide Binding Site To Bypass The 1000-Atom Limit To Structure Determination By Direct Methods" . . . . . 100.00 164 100.00 100.00 3.83e-06 . . . . 7156 1 265 no PDB 1SX7 . "Use Of An Ion-Binding Site To Bypass The 1000-Atom Limit To Ab Initio Structure Determination By Direct Methods" . . . . . 100.00 164 100.00 100.00 3.83e-06 . . . . 7156 1 266 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 2.96e-06 . . . . 7156 1 267 no PDB 1T8F . "Crystal Structure Of Phage T4 Lysozyme Mutant R14aK16AI17AK19AT21AE22AC54TC97A" . . . . . 100.00 164 100.00 100.00 2.89e-06 . . . . 7156 1 268 no PDB 1T8G . "Crystal Structure Of Phage T4 Lysozyme Mutant L32aL33AT34AC54TC97AE108V" . . . . . 100.00 164 100.00 100.00 3.72e-06 . . . . 7156 1 269 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 2.96e-06 . . . . 7156 1 270 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 3.76e-06 . . . . 7156 1 271 no PDB 1XEP . "Catechol In Complex With T4 Lysozyme L99aM102Q" . . . . . 100.00 164 100.00 100.00 4.03e-06 . . . . 7156 1 272 no PDB 1ZUR . "Crystal Structure Of Spin Labeled T4 Lysozyme (V131r1f)" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 273 no PDB 1ZWN . "Crystal Structure Of Spin Labeled T4 Lysozyme (V131r1b)" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 274 no PDB 1ZYT . "Crystal Structure Of Spin Labeled T4 Lysozyme (A82r1)" . . . . . 100.00 164 100.00 100.00 3.95e-06 . . . . 7156 1 275 no PDB 200L . 'Thermodynamic And Structural Compensation In "size-Switch" Core-Repacking Variants Of T4 Lysozyme' . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 276 no PDB 201L . "How Amino-Acid Insertions Are Allowed In An Alpha-Helix Of T4 Lysozyme" . . . . . 100.00 166 100.00 100.00 4.09e-06 . . . . 7156 1 277 no PDB 205L . "How Amino-Acid Insertions Are Allowed In An Alpha-Helix Of T4 Lysozyme" . . . . . 100.00 167 100.00 100.00 3.37e-06 . . . . 7156 1 278 no PDB 206L . "Phage T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.68e-06 . . . . 7156 1 279 no PDB 209L . "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" . . . . . 100.00 167 100.00 100.00 3.37e-06 . . . . 7156 1 280 no PDB 210L . "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" . . . . . 100.00 163 100.00 100.00 3.84e-06 . . . . 7156 1 281 no PDB 211L . "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" . . . . . 100.00 165 100.00 100.00 3.39e-06 . . . . 7156 1 282 no PDB 212L . "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" . . . . . 100.00 168 100.00 100.00 3.27e-06 . . . . 7156 1 283 no PDB 214L . "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" . . . . . 100.00 165 100.00 100.00 3.39e-06 . . . . 7156 1 284 no PDB 215L . "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" . . . . . 100.00 165 100.00 100.00 3.39e-06 . . . . 7156 1 285 no PDB 216L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 4.46e-06 . . . . 7156 1 286 no PDB 217L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.54e-06 . . . . 7156 1 287 no PDB 218L . "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" . . . . . 100.00 165 100.00 100.00 3.39e-06 . . . . 7156 1 288 no PDB 219L . "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.61e-06 . . . . 7156 1 289 no PDB 220L . "Generating Ligand Binding Sites In T4 Lysozyme Using Deficiency-Creating Substitutions" . . . . . 100.00 164 100.00 100.00 3.68e-06 . . . . 7156 1 290 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 3.68e-06 . . . . 7156 1 291 no PDB 222L . "Generating Ligand Binding Sites In T4 Lysozyme Using Deficiency-Creating Substitutions" . . . . . 100.00 164 100.00 100.00 3.68e-06 . . . . 7156 1 292 no PDB 223L . "Generating Ligand Binding Sites In T4 Lysozyme Using Deficiency-Creating Substitutions" . . . . . 100.00 164 100.00 100.00 4.15e-06 . . . . 7156 1 293 no PDB 224L . "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 3.68e-06 . . . . 7156 1 294 no PDB 225L . "Generating Ligand Binding Sites In T4 Lysozyme Using Deficiency-Creating Substitutions" . . . . . 100.00 164 100.00 100.00 4.15e-06 . . . . 7156 1 295 no PDB 226L . "Generating Ligand Binding Sites In T4 Lysozyme Using Deficiency-Creating Substitutions" . . . . . 100.00 164 100.00 100.00 4.15e-06 . . . . 7156 1 296 no PDB 227L . "Generating Ligand Binding Sites In T4 Lysozyme Using Deficiency-Creating Substitutions" . . . . . 100.00 164 100.00 100.00 3.23e-06 . . . . 7156 1 297 no PDB 228L . "Generating Ligand Binding Sites In T4 Lysozyme Using Deficiency-Creating Substitutions" . . . . . 100.00 164 100.00 100.00 3.23e-06 . . . . 7156 1 298 no PDB 229L . "Generating Ligand Binding Sites In T4 Lysozyme Using Deficiency-Creating Substitutions" . . . . . 100.00 164 100.00 100.00 3.26e-06 . . . . 7156 1 299 no PDB 230L . "T4 Lysozyme Mutant M6l" . . . . . 100.00 164 100.00 100.00 3.68e-06 . . . . 7156 1 300 no PDB 231L . "T4 Lysozyme Mutant M106k" . . . . . 100.00 164 100.00 100.00 3.83e-06 . . . . 7156 1 301 no PDB 232L . "T4 Lysozyme Mutant M120k" . . . . . 100.00 164 100.00 100.00 3.83e-06 . . . . 7156 1 302 no PDB 233L . "T4 Lysozyme Mutant M120l" . . . . . 100.00 164 100.00 100.00 3.68e-06 . . . . 7156 1 303 no PDB 234L . "T4 Lysozyme Mutant M106l" . . . . . 100.00 164 100.00 100.00 3.68e-06 . . . . 7156 1 304 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 3.47e-06 . . . . 7156 1 305 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 3.47e-06 . . . . 7156 1 306 no PDB 238L . "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 3.47e-06 . . . . 7156 1 307 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 3.43e-06 . . . . 7156 1 308 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 3.43e-06 . . . . 7156 1 309 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 3.43e-06 . . . . 7156 1 310 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 3.43e-06 . . . . 7156 1 311 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 3.43e-06 . . . . 7156 1 312 no PDB 244L . "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 3.43e-06 . . . . 7156 1 313 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 3.68e-06 . . . . 7156 1 314 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 3.23e-06 . . . . 7156 1 315 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 3.64e-06 . . . . 7156 1 316 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 3.40e-06 . . . . 7156 1 317 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 3.40e-06 . . . . 7156 1 318 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 3.40e-06 . . . . 7156 1 319 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 3.68e-06 . . . . 7156 1 320 no PDB 252L . "Generating Ligand Binding Sites In T4 Lysozyme Using Deficiency-Creating Substitutions" . . . . . 100.00 164 100.00 100.00 3.72e-06 . . . . 7156 1 321 no PDB 253L . Lysozyme . . . . . 100.00 164 100.00 100.00 3.50e-06 . . . . 7156 1 322 no PDB 254L . Lysozyme . . . . . 100.00 164 100.00 100.00 3.61e-06 . . . . 7156 1 323 no PDB 255L . Hydrolase . . . . . 100.00 164 100.00 100.00 3.91e-06 . . . . 7156 1 324 no PDB 256L . "Bacteriophage T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 4.11e-06 . . . . 7156 1 325 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 3.32e-06 . . . . 7156 1 326 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 3.32e-06 . . . . 7156 1 327 no PDB 2A4T . "Crystal Structure Of Spin Labeled T4 Lysozyme (V131r7)" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 328 no PDB 2B6T . "T4 Lysozyme Mutant L99a At 200 Mpa" . . . . . 100.00 162 100.00 100.00 3.74e-06 . . . . 7156 1 329 no PDB 2B6W . "T4 Lysozyme Mutant L99a At 200 Mpa" . . . . . 100.00 162 100.00 100.00 3.74e-06 . . . . 7156 1 330 no PDB 2B6X . "T4 Lysozyme Mutant L99a At 200 Mpa" . . . . . 100.00 162 100.00 100.00 3.74e-06 . . . . 7156 1 331 no PDB 2B6Y . "T4 Lysozyme Mutant L99a At Ambient Pressure" . . . . . 100.00 162 100.00 100.00 3.74e-06 . . . . 7156 1 332 no PDB 2B6Z . "T4 Lysozyme Mutant L99a At Ambient Pressure" . . . . . 100.00 162 100.00 100.00 3.74e-06 . . . . 7156 1 333 no PDB 2B70 . "T4 Lysozyme Mutant L99a At Ambient Pressure" . . . . . 100.00 162 100.00 100.00 3.74e-06 . . . . 7156 1 334 no PDB 2B72 . "T4 Lysozyme Mutant L99a At 100 Mpa" . . . . . 100.00 162 100.00 100.00 3.74e-06 . . . . 7156 1 335 no PDB 2B73 . "T4 Lysozyme Mutant L99a At 100 Mpa" . . . . . 100.00 162 100.00 100.00 3.74e-06 . . . . 7156 1 336 no PDB 2B74 . "T4 Lysozyme Mutant L99a At 100 Mpa" . . . . . 100.00 162 100.00 100.00 3.74e-06 . . . . 7156 1 337 no PDB 2B75 . "T4 Lysozyme Mutant L99a At 150 Mpa" . . . . . 100.00 162 100.00 100.00 3.74e-06 . . . . 7156 1 338 no PDB 2B7X . "Sequential Reorganization Of Beta-Sheet Topology By Insertion Of A Single Strand" . . . . . 100.00 170 100.00 100.00 4.11e-06 . . . . 7156 1 339 no PDB 2CUU . "Crystal Structure Of Spin Labeled T4 Lysozyme (v131r1)" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 340 no PDB 2F2Q . "High Resolution Crystal Strcuture Of T4 Lysosyme Mutant L20r63A LIGANDED TO GUANIDINIUM ION" . . . . . 100.00 175 100.00 100.00 2.96e-06 . . . . 7156 1 341 no PDB 2F32 . "Xray Crystal Structure Of Lysozyme Mutant L20R63A LIGANDED To Ethylguanidinium" . . . . . 100.00 175 100.00 100.00 2.96e-06 . . . . 7156 1 342 no PDB 2F47 . "Xray Crystal Structure Of T4 Lysozyme Mutant L20R63A Liganded To Methylguanidinium" . . . . . 100.00 175 100.00 100.00 2.96e-06 . . . . 7156 1 343 no PDB 2HUK . "Crystal Structure Of T4 Lysozyme V131c Synthetic Dimer" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 344 no PDB 2HUL . "Crystal Structure Of T4 Lysozyme S44c Synthetic Dimer" . . . . . 100.00 164 100.00 100.00 4.03e-06 . . . . 7156 1 345 no PDB 2HUM . "Crystal Structure Of T4 Lysozyme D72c Synthetic Dimer" . . . . . 100.00 164 100.00 100.00 3.95e-06 . . . . 7156 1 346 no PDB 2IGC . "Structure Of Spin Labeled T4 Lysozyme Mutant T115r1a" . . . . . 100.00 164 100.00 100.00 3.83e-06 . . . . 7156 1 347 no PDB 2L78 . "Design And Structural Analysis Of Alternative Hydrophobic Core Packing Arrangements In Bacteriophage T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.47e-06 . . . . 7156 1 348 no PDB 2LC9 . "Solution Structure Of A Minor And Transiently Formed State Of A T4 Lysozyme Mutant" . . . . . 100.00 164 100.00 100.00 3.72e-06 . . . . 7156 1 349 no PDB 2LCB . "Solution Structure Of A Minor And Transiently Formed State Of A T4 Lysozyme Mutant" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 350 no PDB 2LZM . "Structure Of Bacteriophage T4 Lysozyme Refined At 1.7 Angstroms Resolution" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 351 no PDB 2NTG . "Structure Of Spin-Labeled T4 Lysozyme Mutant T115r7" . . . . . 100.00 164 100.00 100.00 3.83e-06 . . . . 7156 1 352 no PDB 2NTH . "Structure Of Spin-Labeled T4 Lysozyme Mutant L118r1" . . . . . 100.00 164 100.00 100.00 4.07e-06 . . . . 7156 1 353 no PDB 2O4W . "T4 Lysozyme Circular Permutant" . . . . . 100.00 171 100.00 100.00 3.39e-06 . . . . 7156 1 354 no PDB 2O79 . "T4 Lysozyme With C-Terminal Extension" . . . . . 100.00 170 100.00 100.00 3.46e-06 . . . . 7156 1 355 no PDB 2O7A . "T4 Lysozyme C-Terminal Fragment" . . . . . 100.00 124 100.00 100.00 3.23e-06 . . . . 7156 1 356 no PDB 2OE4 . "High Pressure Psuedo Wild Type T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.61e-06 . . . . 7156 1 357 no PDB 2OE7 . "High-Pressure T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.61e-06 . . . . 7156 1 358 no PDB 2OE9 . "High-Pressure Structure Of Pseudo-Wt T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.61e-06 . . . . 7156 1 359 no PDB 2OEA . "High-Pressure Structure Of Pseudo-Wt T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.61e-06 . . . . 7156 1 360 no PDB 2OTY . "1,2-Dichlorobenzene In Complex With T4 Lysozyme L99a" . . . . . 100.00 162 100.00 100.00 3.74e-06 . . . . 7156 1 361 no PDB 2OTZ . "N-Methylaniline In Complex With T4 Lysozyme L99a" . . . . . 100.00 162 100.00 100.00 3.74e-06 . . . . 7156 1 362 no PDB 2OU0 . "1-Methylpyrrole In Complex With T4 Lysozyme L99a" . . . . . 100.00 162 100.00 100.00 3.74e-06 . . . . 7156 1 363 no PDB 2OU8 . "Structure Of Spin-Labeled T4 Lysozyme Mutant T115r1 At Room Temperature" . . . . . 100.00 164 100.00 100.00 3.83e-06 . . . . 7156 1 364 no PDB 2OU9 . "Structure Of Spin-Labeled T4 Lysozyme Mutant T115r1R119A" . . . . . 100.00 164 100.00 100.00 3.50e-06 . . . . 7156 1 365 no PDB 2Q9D . "Structure Of Spin-Labeled T4 Lysozyme Mutant A41r1" . . . . . 100.00 164 100.00 100.00 3.95e-06 . . . . 7156 1 366 no PDB 2Q9E . "Structure Of Spin-Labeled T4 Lysozyme Mutant S44r1" . . . . . 100.00 164 100.00 100.00 3.79e-06 . . . . 7156 1 367 no PDB 2QAR . "Structure Of The 2tel Crystallization Module Fused To T4 Lysozyme With A Helical Linker" . . . . . 100.00 163 100.00 100.00 5.09e-06 . . . . 7156 1 368 no PDB 2QB0 . "Structure Of The 2tel Crystallization Module Fused To T4 Lysozyme With An Ala-Gly-Pro Linker" . . . . . 100.00 241 100.00 100.00 1.36e-05 . . . . 7156 1 369 no PDB 2RAY . "Beta-chlorophenetole In Complex With T4 Lysozyme L99a" . . . . . 100.00 162 100.00 100.00 3.74e-06 . . . . 7156 1 370 no PDB 2RAZ . "4-(Methylthio)nitrobenzene In Complex With T4 Lysozyme L99a" . . . . . 100.00 162 100.00 100.00 3.74e-06 . . . . 7156 1 371 no PDB 2RB0 . "2,6-Difluorobenzylbromide Complex With T4 Lysozyme L99a" . . . . . 100.00 162 100.00 100.00 3.74e-06 . . . . 7156 1 372 no PDB 2RB1 . "2-Ethoxyphenol In Complex With T4 Lysozyme L99a" . . . . . 100.00 162 100.00 100.00 3.74e-06 . . . . 7156 1 373 no PDB 2RB2 . "3-Methylbenzylazide In Complex With T4 Lysozyme L99a" . . . . . 100.00 162 100.00 100.00 3.74e-06 . . . . 7156 1 374 no PDB 2RBN . "N-Phenylglycinonitrile In Complex With T4 Lysozyme L99aM102Q" . . . . . 100.00 162 100.00 100.00 4.22e-06 . . . . 7156 1 375 no PDB 2RBO . "2-Nitrothiophene In Complex With T4 Lysozyme L99aM102Q" . . . . . 100.00 162 100.00 100.00 4.22e-06 . . . . 7156 1 376 no PDB 2RBP . "2-(N-Propylthio)ethanol In Complex With T4 Lysozyme L99aM102Q" . . . . . 100.00 162 100.00 100.00 4.22e-06 . . . . 7156 1 377 no PDB 2RBQ . "3-Methylbenzylazide In Complex With T4 L99aM102Q" . . . . . 100.00 162 100.00 100.00 4.22e-06 . . . . 7156 1 378 no PDB 2RBR . "2-Phenoxyethanol In Complex With T4 Lysozyme L99aM102Q" . . . . . 100.00 162 100.00 100.00 4.22e-06 . . . . 7156 1 379 no PDB 2RBS . "(r)(+)-3-chloro-1-phenyl-1-propanol In Complex With T4 Lysozyme L99a/m102q" . . . . . 100.00 162 100.00 100.00 4.22e-06 . . . . 7156 1 380 no PDB 2RH1 . "High Resolution Crystal Structure Of Human B2-Adrenergic G Protein- Coupled Receptor" . . . . . 100.00 500 100.00 100.00 2.80e-05 . . . . 7156 1 381 no PDB 3C7W . "Contributions Of All 20 Amino Acids At Site 96 To The Stability And Structure Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.87e-06 . . . . 7156 1 382 no PDB 3C7Y . "Mutant R96a Of T4 Lysozyme In Wildtype Background At 298k" . . . . . 100.00 164 100.00 100.00 3.79e-06 . . . . 7156 1 383 no PDB 3C7Z . "T4 Lysozyme Mutant D89aR96H AT ROOM TEMPERATURE" . . . . . 100.00 164 100.00 100.00 3.87e-06 . . . . 7156 1 384 no PDB 3C80 . "T4 Lysozyme Mutant R96y At Room Temperature" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 385 no PDB 3C81 . "Mutant K85a Of T4 Lysozyme In Wildtype Background At Room Temperature" . . . . . 100.00 164 100.00 100.00 3.91e-06 . . . . 7156 1 386 no PDB 3C82 . "Bacteriophage Lysozyme T4 Lysozyme Mutant K85aR96H" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 387 no PDB 3C83 . "Bacteriophage T4 Lysozyme Mutant D89a In Wildtype Background At Room Temperature" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 388 no PDB 3C8Q . "Contribution Of All 20 Amino Acids At Site 96 To The Stability And Structure Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.79e-06 . . . . 7156 1 389 no PDB 3C8R . "Contributions Of All 20 Amino Acids At Site 96 To Stability And Structure Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.91e-06 . . . . 7156 1 390 no PDB 3C8S . "Contributions Of All 20 Amino Acids At Site 96 To The Stability And Structure Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.83e-06 . . . . 7156 1 391 no PDB 3CDO . "Bacteriophage T4 Lysozyme Mutant R96v In Wildtype Background At Low Temperature" . . . . . 100.00 164 100.00 100.00 3.83e-06 . . . . 7156 1 392 no PDB 3CDQ . "Contributions Of All 20 Amino Acids At Site 96 To The Stability And Structure Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.79e-06 . . . . 7156 1 393 no PDB 3CDR . "R96q Mutant Of Wildtype Phage T4 Lysozyme At 298 K" . . . . . 100.00 164 100.00 100.00 3.91e-06 . . . . 7156 1 394 no PDB 3CDT . "Contributions Of All 20 Amino Acids At Site 96 To The Stability And Structure Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.95e-06 . . . . 7156 1 395 no PDB 3CDV . "Contributions Of All 20 Amino Acids At Site 96 To The Stability And Structure Of T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 3.68e-06 . . . . 7156 1 396 no PDB 3D4S . "Cholesterol Bound Form Of Human Beta2 Adrenergic Receptor." . . . . . 100.00 490 100.00 100.00 2.63e-05 . . . . 7156 1 397 no PDB 3DKE . "Polar And Non-Polar Cavities In Phage T4 Lysozyme" . . . . . 100.00 164 100.00 100.00 4.28e-06 . . . . 7156 1 398 no PDB 3DMV . "Free Of Ligand Binding In The Hydrophobic Cavity Of T4 Lysozyme L99a Mutant" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 399 no PDB 3DMX . "Benzene Binding In The Hydrophobic Cavity Of T4 Lysozyme L99a Mutant" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 400 no PDB 3DMZ . "Hexafluorobenzene Binding In The Hydrophobic Cavity Of T4 Lysozyme L99a Mutant" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 401 no PDB 3DN0 . "Pentafluorobenzene Binding In The Hydrophobic Cavity Of T4 Lysozyme L99a Mutant" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 402 no PDB 3DN1 . "Chloropentafluorobenzene Binding In The Hydrophobic Cavity Of T4 Lysozyme L99a Mutant" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 403 no PDB 3DN2 . "Bromopentafluorobenzene Binding In The Hydrophobic Cavity Of T4 Lysozyme L99a Mutant" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 404 no PDB 3DN3 . "Iodopentafluorobenzene Binding In The Hydrophobic Cavity Of T4 Lysozyme L99a Mutant" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 405 no PDB 3DN4 . "Iodobenzene Binding In The Hydrophobic Cavity Of T4 Lysozyme L99a Mutant" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 406 no PDB 3DN6 . "1,3,5-Trifluoro-2,4,6-Trichlorobenzene Binding In The Hydrophobic Cavity Of T4 Lysozyme L99a Mutant" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 407 no PDB 3DN8 . "Iodopentafluorobenzene Binding In The Hydrophobic Cavity Of T4 Lysozyme L99a Mutant (Seleno Version)" . . . . . 100.00 164 100.00 100.00 4.50e-06 . . . . 7156 1 408 no PDB 3DNA . "Iodobenzene Binding In The Hydrophobic Cavity Of T4 Lysozyme L99a Mutant (Seleno Version)" . . . . . 100.00 164 100.00 100.00 4.50e-06 . . . . 7156 1 409 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 9.88e-07 . . . . 7156 1 410 no PDB 3F8V . "Evaulaution At Atomic Resolution Of The Role Of Strain In Destabilizing The Temperature Sensitive T4 Lysozyme Mutant Arg96-->hi" . . . . . 100.00 164 100.00 100.00 3.87e-06 . . . . 7156 1 411 no PDB 3F9L . "Evaulaution At Atomic Resolution Of The Role Of Strain In Destabilizing The Temperature Sensitive T4 Lysozyme Mutant Arg96-->hi" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 412 no PDB 3FA0 . "Evaulaution At Atomic Resolution Of The Role Of Strain In Destabilizing The Temperature Sensitive T4 Lysozyme Mutant Arg96-->hi" . . . . . 100.00 162 100.00 100.00 3.93e-06 . . . . 7156 1 413 no PDB 3FAD . "Evaulaution At Atomic Resolution Of The Role Of Strain In Destabilizing The Temperature Sensitive T4 Lysozyme Mutant Arg96-->hi" . . . . . 100.00 164 100.00 100.00 3.87e-06 . . . . 7156 1 414 no PDB 3FI5 . "Crystal Structure Of T4 Lysozyme Mutant R96w" . . . . . 100.00 164 100.00 100.00 4.69e-06 . . . . 7156 1 415 no PDB 3G3V . "Crystal Structure Of Spin Labeled T4 Lysozyme (V131r1) At 291 K" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 416 no PDB 3HH3 . "New Azaborine Compounds Bind To The T4 Lysozyme L99a Cavity - 1,2-Dihydro-1,2-Azaborine" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 417 no PDB 3HH4 . "New Azaborine Compounds Bind To The T4 Lysozyme L99a Cavity - Benzene As Control" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 418 no PDB 3HH5 . "New Azaborine Compounds Bind To The T4 Lysozyme L99a Cavity - 1-Ethyl-2-Hydro-1,2-Azaborine" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 419 no PDB 3HH6 . "New Azaborine Compounds Bind To The T4 Lysozyme L99a Cavity - Ethylbenzene As Control" . . . . . 100.00 164 100.00 100.00 3.64e-06 . . . . 7156 1 420 no PDB 3HWL . "Crystal Structure Of T4 Lysozyme With The Unnatural Amino Acid P- Acetyl-L-Phenylalanine Incorporated At Position 131" . . . . . 100.00 164 100.00 100.00 4.03e-06 . . . . 7156 1 421 no PDB 3JR6 . "Sequential Reorganization Of Beta-Sheet Topology By Insertion Of A Single Strand" . . . . . 100.00 170 100.00 100.00 3.61e-06 . . . . 7156 1 422 no PDB 3K2R . "Crystal Structure Of Spin Labeled T4 Lysozyme Mutant K65v1R76V1" . . . . . 100.00 164 100.00 100.00 3.79e-06 . . . . 7156 1 423 no PDB 3L2X . "Crystal Structure Of Spin Labeled T4 Lysozyme Mutant 115-119rx" . . . . . 100.00 164 100.00 100.00 3.79e-06 . . . . 7156 1 424 no PDB 3L64 . "T4 Lysozyme S44e/wt*" . . . . . 100.00 164 100.00 100.00 3.54e-06 . . . . 7156 1 425 no PDB 3LZM . "Structural Studies Of Mutants Of T4 Lysozyme That Alter Hydrophobic Stabilization" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 426 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 2.63e-05 . . . . 7156 1 427 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 2.63e-05 . . . . 7156 1 428 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 2.63e-05 . . . . 7156 1 429 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 1.62e-06 . . . . 7156 1 430 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 1.38e-06 . . . . 7156 1 431 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 1.75e-06 . . . . 7156 1 432 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 1.62e-06 . . . . 7156 1 433 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 1.38e-06 . . . . 7156 1 434 no PDB 3P0G . "Structure Of A Nanobody-Stabilized Active State Of The Beta2 Adrenoceptor" . . . . . 100.00 501 100.00 100.00 2.77e-05 . . . . 7156 1 435 no PDB 3PBL . "Structure Of The Human Dopamine D3 Receptor In Complex With Eticlopride" . . . . . 100.00 481 100.00 100.00 2.55e-05 . . . . 7156 1 436 no PDB 3PDS . "Irreversible Agonist-Beta2 Adrenoceptor Complex" . . . . . 100.00 458 100.00 100.00 2.35e-05 . . . . 7156 1 437 no PDB 3QAK . "Agonist Bound Structure Of The Human Adenosine A2a Receptor" . . . . . 100.00 488 100.00 100.00 9.88e-07 . . . . 7156 1 438 no PDB 3RUN . "New Strategy To Analyze Structures Of Glycopeptide Antibiotic-Target Complexes" . . . . . 100.00 168 100.00 100.00 3.65e-06 . . . . 7156 1 439 no PDB 3RZE . "Structure Of The Human Histamine H1 Receptor In Complex With Doxepin" . . . . . 100.00 452 100.00 100.00 2.93e-05 . . . . 7156 1 440 no PDB 3SB5 . "Zn-Mediated Trimer Of T4 Lysozyme R125cE128C BY SYNTHETIC Symmetrization" . . . . . 100.00 165 100.00 100.00 4.58e-06 . . . . 7156 1 441 no PDB 3SB6 . "Cu-Mediated Dimer Of T4 Lysozyme D61hK65HR76HR80H BY SYNTHETIC Symmetrization" . . . . . 100.00 165 100.00 100.00 3.82e-06 . . . . 7156 1 442 no PDB 3SB7 . "Cu-Mediated Trimer Of T4 Lysozyme D61hK65HR76HR80H BY SYNTHETIC Symmetrization" . . . . . 100.00 165 100.00 100.00 3.82e-06 . . . . 7156 1 443 no PDB 3SB8 . "Cu-Mediated Dimer Of T4 Lysozyme D61hK65H BY SYNTHETIC SYMMETRIZATION" . . . . . 100.00 165 100.00 100.00 4.36e-06 . . . . 7156 1 444 no PDB 3SB9 . "Cu-Mediated Dimer Of T4 Lysozyme R76hR80H BY SYNTHETIC SYMMETRIZATION" . . . . . 100.00 165 100.00 100.00 3.75e-06 . . . . 7156 1 445 no PDB 3SBA . "Zn-Mediated Hexamer Of T4 Lysozyme R76hR80H BY SYNTHETIC Symmetrization" . . . . . 100.00 165 100.00 100.00 3.75e-06 . . . . 7156 1 446 no PDB 3SBB . "Disulphide-Mediated Tetramer Of T4 Lysozyme R76cR80C BY SYNTHETIC Symmetrization" . . . . . 100.00 165 100.00 100.00 4.06e-06 . . . . 7156 1 447 no PDB 3SN6 . "Crystal Structure Of The Beta2 Adrenergic Receptor-Gs Protein Complex" . . . . . 100.00 514 100.00 100.00 2.58e-05 . . . . 7156 1 448 no PDB 3UON . "Structure Of The Human M2 Muscarinic Acetylcholine Receptor Bound To An Antagonist" . . . . . 100.00 467 100.00 100.00 3.12e-05 . . . . 7156 1 449 no PDB 3V2W . "Crystal Structure Of A Lipid G Protein-Coupled Receptor At 3.35a" . . . . . 100.00 520 100.00 100.00 1.78e-06 . . . . 7156 1 450 no PDB 3V2Y . "Crystal Structure Of A Lipid G Protein-Coupled Receptor At 2.80a" . . . . . 100.00 520 100.00 100.00 1.78e-06 . . . . 7156 1 451 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 1.31e-06 . . . . 7156 1 452 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 1.64e-05 . . . . 7156 1 453 no PDB 4DAJ . "Structure Of The M3 Muscarinic Acetylcholine Receptor" . . . . . 100.00 479 100.00 100.00 3.93e-05 . . . . 7156 1 454 no PDB 4DJH . "Structure Of The Human Kappa Opioid Receptor In Complex With Jdtic" . . . . . 100.00 480 100.00 100.00 2.00e-05 . . . . 7156 1 455 no PDB 4DKL . "Crystal Structure Of The Mu-Opioid Receptor Bound To A Morphinan Antagonist" . . . . . 100.00 464 100.00 100.00 3.02e-05 . . . . 7156 1 456 no PDB 4EJ4 . "Structure Of The Delta Opioid Receptor Bound To Naltrindole" . . . . . 100.00 461 100.00 100.00 2.50e-05 . . . . 7156 1 457 no PDB 4EPI . "The Crystal Structure Of Pesticin-T4 Lysozyme Hybrid Stabilized By Engineered Disulfide Bonds" . . . . . 100.00 330 100.00 100.00 1.24e-05 . . . . 7156 1 458 no PDB 4GBR . "N-terminal T4 Lysozyme Fusion Facilitates Crystallization Of A G Protein Coupled Receptor" . . . . . 100.00 163 100.00 100.00 3.77e-06 . . . . 7156 1 459 no PDB 4GRV . "The Crystal Structure Of The Neurotensin Receptor Nts1 In Complex With Neurotensin (8-13)" . . . . . 100.00 510 100.00 100.00 6.76e-06 . . . . 7156 1 460 no PDB 4HTT . "Crystal Structure Of Twin Arginine Translocase Receptor- Tatc In Ddm" . . . . . 100.00 418 100.00 100.00 5.81e-07 . . . . 7156 1 461 no PDB 4IAP . "Crystal Structure Of Ph Domain Of Osh3 From Saccharomyces Cerevisiae" . . . . . 100.00 260 100.00 100.00 1.37e-05 . . . . 7156 1 462 no PDB 4LDE . "Structure Of Beta2 Adrenoceptor Bound To Bi167107 And An Engineered Nanobody" . . . . . 100.00 469 100.00 100.00 2.36e-05 . . . . 7156 1 463 no PDB 4LDL . "Structure Of Beta2 Adrenoceptor Bound To Hydroxybenzylisoproterenol And An Engineered Nanobody" . . . . . 100.00 469 100.00 100.00 2.36e-05 . . . . 7156 1 464 no PDB 4LDO . "Structure Of Beta2 Adrenoceptor Bound To Adrenaline And An Engineered Nanobody" . . . . . 100.00 469 100.00 100.00 2.36e-05 . . . . 7156 1 465 no PDB 4LZM . "Comparison Of The Crystal Structure Of Bacteriophage T4 Lysozyme At Low, Medium, And High Ionic Strengths" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 466 no PDB 4N9N . "Crystal Structure Of Saccharomyces Cerevisiae Upc2 Transcription Factor Fused With T4 Lysozyme" . . . . . 100.00 438 100.00 100.00 5.21e-06 . . . . 7156 1 467 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 2.22e-06 . . . . 7156 1 468 no PDB 4PHU . "Crystal Structure Of Human Gpr40 Bound To Allosteric Agonist Tak-875" . . . . . 100.00 491 100.00 100.00 2.08e-06 . . . . 7156 1 469 no PDB 4PJZ . "Crystal Structure Of T4 Lysozyme-gss-peptide In Complex With Teicoplanin-a2-2" . . . . . 100.00 174 100.00 100.00 3.71e-06 . . . . 7156 1 470 no PDB 4PK0 . "Crystal Structure Of T4 Lysozyme-peptide In Complex With Teicoplanin- A2-2" . . . . . 100.00 171 100.00 100.00 3.57e-06 . . . . 7156 1 471 no PDB 4PLA . "Crystal Structure Of Phosphatidyl Inositol 4-kinase Ii Alpha In Complex With Atp" . . . . . 100.00 556 100.00 100.00 1.85e-05 . . . . 7156 1 472 no PDB 4QKX . "Structure Of Beta2 Adrenoceptor Bound To A Covalent Agonist And An Engineered Nanobody" . . . . . 100.00 469 100.00 100.00 2.34e-05 . . . . 7156 1 473 no PDB 4TN3 . "Structure Of The Bbox-coiled-coil Region Of Rhesus Trim5alpha" . . . . . 100.00 400 100.00 100.00 1.51e-06 . . . . 7156 1 474 no PDB 4U15 . "M3-mt4l Receptor Bound To Tiotropium" . . . . . 100.00 418 100.00 100.00 3.69e-05 . . . . 7156 1 475 no PDB 4U16 . "M3-mt4l Receptor Bound To Nms" . . . . . 100.00 418 100.00 100.00 3.69e-05 . . . . 7156 1 476 no PDB 4W8F . "Crystal Structure Of The Dynein Motor Domain In The Amppnp-bound State" . . . . . 100.00 2661 100.00 100.00 2.37e-06 . . . . 7156 1 477 no PDB 5LZM . "Comparison Of The Crystal Structure Of Bacteriophage T4 Lysozyme At Low, Medium, And High Ionic Strengths" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 478 no PDB 6LZM . "Comparison Of The Crystal Structure Of Bacteriophage T4 Lysozyme At Low, Medium, And High Ionic Strengths" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 479 no PDB 7LZM . "Comparison Of The Crystal Structure Of Bacteriophage T4 Lysozyme At Low, Medium, And High Ionic Strengths" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 480 no GB AAA72629 . "lysozyme [synthetic construct]" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 481 no GB AAA72664 . "synthetic T4-lysozyme [synthetic construct]" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 482 no GB ADJ39843 . "lysozyme murein hydrolase [Enterobacteria phage T4T]" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 483 no GB AIT75037 . "lysozyme murein hydrolase [Enterobacteria phage RB55]" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 1 484 no GB AIT75310 . "lysozyme murein hydrolase [Enterobacteria phage RB59]" . . . . . 100.00 164 100.00 100.00 3.99e-06 . . . . 7156 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 1 136 SER . 7156 1 2 137 ARG . 7156 1 3 138 TRP . 7156 1 4 139 TYR . 7156 1 5 140 ASN . 7156 1 6 141 GLN . 7156 1 7 142 THR . 7156 1 8 143 PRO . 7156 1 9 144 ASN . 7156 1 10 145 ARG . 7156 1 11 146 ALA . 7156 1 12 147 LYS . 7156 1 13 148 ARG . 7156 1 14 149 VAL . 7156 1 15 150 ILE . 7156 1 16 151 THR . 7156 1 17 152 THR . 7156 1 18 153 PHE . 7156 1 19 154 ARG . 7156 1 20 155 THR . 7156 1 21 156 GLY . 7156 1 22 157 THR . 7156 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 . SER 1 1 7156 1 . ARG 2 2 7156 1 . TRP 3 3 7156 1 . TYR 4 4 7156 1 . ASN 5 5 7156 1 . GLN 6 6 7156 1 . THR 7 7 7156 1 . PRO 8 8 7156 1 . ASN 9 9 7156 1 . ARG 10 10 7156 1 . ALA 11 11 7156 1 . LYS 12 12 7156 1 . ARG 13 13 7156 1 . VAL 14 14 7156 1 . ILE 15 15 7156 1 . THR 16 16 7156 1 . THR 17 17 7156 1 . PHE 18 18 7156 1 . ARG 19 19 7156 1 . THR 20 20 7156 1 . GLY 21 21 7156 1 . THR 22 22 7156 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 7156 _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_H . . . no . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 7156 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 7156 _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_H . 'chemical synthesis' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 7156 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 7156 _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 H (lys 136-157)' . . . 1 $HELIX_H . . . 1 2 mM . . . . 7156 1 2 H2O . . . . . . . 90 . . % . . . . 7156 1 3 D2O . . . . . . . 10 . . % . . . . 7156 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 7156 _Sample.ID 2 _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 H (lys 136-157)' . . . 1 $HELIX_H . . . 1 2 Mm . . . . 7156 2 2 TFE . . . . . . . 50 . . % . . . . 7156 2 3 H2O . . . . . . . 40 . . % . . . . 7156 2 4 D2O . . . . . . . 10 . . % . . . . 7156 2 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 7156 _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 . . . 7156 1 temperature 283 0 K 7156 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 7156 _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 7156 _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 . . . 7156 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 7156 _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 . . . . . . . . . . isotropic . . 1 $conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7156 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 7156 _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 7156 _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 7156 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 7156 _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 . . isotropic 7156 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 SER HA H 1 4.12 . . . . . . . 1 SER HA . 7156 1 2 . 1 1 1 1 SER HB2 H 1 3.9 . . . . . . . 1 SER HB2 . 7156 1 3 . 1 1 2 2 ARG H H 1 8.74 . . . . . . . 2 ARG H . 7156 1 4 . 1 1 2 2 ARG HA H 1 4.28 . . . . . . . 2 ARG HA . 7156 1 5 . 1 1 2 2 ARG HB2 H 1 1.59 . . . . . . . 2 ARG HB2 . 7156 1 6 . 1 1 2 2 ARG HG2 H 1 1.34 . . . . . . . 2 ARG HG2 . 7156 1 7 . 1 1 2 2 ARG HG3 H 1 1.34 . . . . . . . 2 ARG HG3 . 7156 1 8 . 1 1 2 2 ARG HD2 H 1 3.06 . . . . . . . 2 ARG HD2 . 7156 1 9 . 1 1 2 2 ARG HD3 H 1 3.06 . . . . . . . 2 ARG HD3 . 7156 1 10 . 1 1 2 2 ARG HH11 H 1 7.2 . . . . . . . 2 ARG NH1 . 7156 1 11 . 1 1 3 3 TRP H H 1 8.36 . . . . . . . 3 TRP H . 7156 1 12 . 1 1 3 3 TRP HA H 1 4.66 . . . . . . . 3 TRP HA . 7156 1 13 . 1 1 3 3 TRP HB2 H 1 3.2 . . . . . . . 3 TRP HB2 . 7156 1 14 . 1 1 3 3 TRP HB3 H 1 3.17 . . . . . . . 3 TRP HB3 . 7156 1 15 . 1 1 3 3 TRP HD1 H 1 7.23 . . . . . . . 3 TRP HD1 . 7156 1 16 . 1 1 3 3 TRP HE1 H 1 9.47 . . . . . . . 3 TRP HE1 . 7156 1 17 . 1 1 3 3 TRP HE3 H 1 7.47 . . . . . . . 3 TRP HE3 . 7156 1 18 . 1 1 3 3 TRP HZ2 H 1 7.57 . . . . . . . 3 TRP HZ2 . 7156 1 19 . 1 1 3 3 TRP HZ3 H 1 7.23 . . . . . . . 3 TRP HZ3 . 7156 1 20 . 1 1 3 3 TRP HH2 H 1 7.14 . . . . . . . 3 TRP HH2 . 7156 1 21 . 1 1 4 4 TYR H H 1 7.92 . . . . . . . 4 TYR H . 7156 1 22 . 1 1 4 4 TYR HA H 1 4.43 . . . . . . . 4 TYR HA . 7156 1 23 . 1 1 4 4 TYR HB2 H 1 2.83 . . . . . . . 4 TYR HB2 . 7156 1 24 . 1 1 4 4 TYR HB3 H 1 2.78 . . . . . . . 4 TYR HB3 . 7156 1 25 . 1 1 4 4 TYR HD1 H 1 7.03 . . . . . . . 4 TYR HD1 . 7156 1 26 . 1 1 4 4 TYR HD2 H 1 7.03 . . . . . . . 4 TYR HD2 . 7156 1 27 . 1 1 4 4 TYR HE1 H 1 6.76 . . . . . . . 4 TYR HE1 . 7156 1 28 . 1 1 4 4 TYR HE2 H 1 6.76 . . . . . . . 4 TYR HE2 . 7156 1 29 . 1 1 5 5 ASN H H 1 8.29 . . . . . . . 5 ASN H . 7156 1 30 . 1 1 5 5 ASN HA H 1 4.47 . . . . . . . 5 ASN HA . 7156 1 31 . 1 1 5 5 ASN HB2 H 1 2.73 . . . . . . . 5 ASN HB2 . 7156 1 32 . 1 1 5 5 ASN HB3 H 1 2.58 . . . . . . . 5 ASN HB3 . 7156 1 33 . 1 1 5 5 ASN HD21 H 1 7.68 . . . . . . . 5 ASN HD21 . 7156 1 34 . 1 1 5 5 ASN HD22 H 1 6.99 . . . . . . . 5 ASN HD22 . 7156 1 35 . 1 1 6 6 GLN H H 1 8.36 . . . . . . . 6 GLN H . 7156 1 36 . 1 1 6 6 GLN HA H 1 4.31 . . . . . . . 6 GLN HA . 7156 1 37 . 1 1 6 6 GLN HB2 H 1 1.91 . . . . . . . 6 GLN HB2 . 7156 1 38 . 1 1 6 6 GLN HG2 H 1 2.27 . . . . . . . 6 GLN HG2 . 7156 1 39 . 1 1 6 6 GLN HG3 H 1 2.07 . . . . . . . 6 GLN HG3 . 7156 1 40 . 1 1 6 6 GLN HE21 H 1 7.57 . . . . . . . 6 GLN HE21 . 7156 1 41 . 1 1 6 6 GLN HE22 H 1 6.91 . . . . . . . 6 GLN HE22 . 7156 1 42 . 1 1 7 7 THR H H 1 8.37 . . . . . . . 7 THR H . 7156 1 43 . 1 1 7 7 THR HA H 1 4.44 . . . . . . . 7 THR HA . 7156 1 44 . 1 1 7 7 THR HB H 1 4.15 . . . . . . . 7 THR HB . 7156 1 45 . 1 1 7 7 THR HG21 H 1 1.12 . . . . . . . 7 THR HG2 . 7156 1 46 . 1 1 7 7 THR HG22 H 1 1.12 . . . . . . . 7 THR HG2 . 7156 1 47 . 1 1 7 7 THR HG23 H 1 1.12 . . . . . . . 7 THR HG2 . 7156 1 48 . 1 1 8 8 PRO HA H 1 4.38 . . . . . . . 8 PRO HA . 7156 1 49 . 1 1 8 8 PRO HB2 H 1 2.27 . . . . . . . 8 PRO HB2 . 7156 1 50 . 1 1 8 8 PRO HG2 H 1 1.98 . . . . . . . 8 PRO HG2 . 7156 1 51 . 1 1 8 8 PRO HG3 H 1 1.98 . . . . . . . 8 PRO HG3 . 7156 1 52 . 1 1 8 8 PRO HD2 H 1 3.82 . . . . . . . 8 PRO HD2 . 7156 1 53 . 1 1 8 8 PRO HD3 H 1 3.69 . . . . . . . 8 PRO HD3 . 7156 1 54 . 1 1 9 9 ASN H H 1 8.65 . . . . . . . 9 ASN H . 7156 1 55 . 1 1 9 9 ASN HA H 1 4.63 . . . . . . . 9 ASN HA . 7156 1 56 . 1 1 9 9 ASN HB2 H 1 2.79 . . . . . . . 9 ASN HB2 . 7156 1 57 . 1 1 9 9 ASN HB3 H 1 2.76 . . . . . . . 9 ASN HB3 . 7156 1 58 . 1 1 9 9 ASN HD21 H 1 7.73 . . . . . . . 9 ASN HD21 . 7156 1 59 . 1 1 9 9 ASN HD22 H 1 7.05 . . . . . . . 9 ASN HD22 . 7156 1 60 . 1 1 10 10 ARG H H 1 8.47 . . . . . . . 10 ARG H . 7156 1 61 . 1 1 10 10 ARG HA H 1 4.31 . . . . . . . 10 ARG HA . 7156 1 62 . 1 1 10 10 ARG HB2 H 1 1.77 . . . . . . . 10 ARG HB2 . 7156 1 63 . 1 1 10 10 ARG HB3 H 1 1.73 . . . . . . . 10 ARG HB3 . 7156 1 64 . 1 1 10 10 ARG HG2 H 1 1.62 . . . . . . . 10 ARG HG2 . 7156 1 65 . 1 1 10 10 ARG HG3 H 1 1.62 . . . . . . . 10 ARG HG3 . 7156 1 66 . 1 1 10 10 ARG HD2 H 1 3.19 . . . . . . . 10 ARG HD2 . 7156 1 67 . 1 1 10 10 ARG HD3 H 1 3.19 . . . . . . . 10 ARG HD3 . 7156 1 68 . 1 1 10 10 ARG HH11 H 1 7.2 . . . . . . . 10 ARG NH1 . 7156 1 69 . 1 1 11 11 ALA H H 1 8.36 . . . . . . . 11 ALA H . 7156 1 70 . 1 1 11 11 ALA HA H 1 4.27 . . . . . . . 11 ALA HA . 7156 1 71 . 1 1 11 11 ALA HB1 H 1 1.37 . . . . . . . 11 ALA HB . 7156 1 72 . 1 1 11 11 ALA HB2 H 1 1.37 . . . . . . . 11 ALA HB . 7156 1 73 . 1 1 11 11 ALA HB3 H 1 1.37 . . . . . . . 11 ALA HB . 7156 1 74 . 1 1 12 12 LYS H H 1 8.36 . . . . . . . 12 LYS H . 7156 1 75 . 1 1 12 12 LYS HA H 1 4.25 . . . . . . . 12 LYS HA . 7156 1 76 . 1 1 12 12 LYS HB2 H 1 1.8 . . . . . . . 12 LYS HB2 . 7156 1 77 . 1 1 12 12 LYS HB3 H 1 1.75 . . . . . . . 12 LYS HB3 . 7156 1 78 . 1 1 12 12 LYS HG2 H 1 1.46 . . . . . . . 12 LYS HG2 . 7156 1 79 . 1 1 12 12 LYS HG3 H 1 1.4 . . . . . . . 12 LYS HG3 . 7156 1 80 . 1 1 12 12 LYS HD2 H 1 1.67 . . . . . . . 12 LYS HD2 . 7156 1 81 . 1 1 12 12 LYS HD3 H 1 1.67 . . . . . . . 12 LYS HD3 . 7156 1 82 . 1 1 12 12 LYS HE2 H 1 3 . . . . . . . 12 LYS HE2 . 7156 1 83 . 1 1 12 12 LYS HE3 H 1 3 . . . . . . . 12 LYS HE3 . 7156 1 84 . 1 1 13 13 ARG H H 1 8.36 . . . . . . . 13 ARG H . 7156 1 85 . 1 1 13 13 ARG HA H 1 4.35 . . . . . . . 13 ARG HA . 7156 1 86 . 1 1 13 13 ARG HB2 H 1 1.8 . . . . . . . 13 ARG HB2 . 7156 1 87 . 1 1 13 13 ARG HB3 H 1 1.75 . . . . . . . 13 ARG HB3 . 7156 1 88 . 1 1 13 13 ARG HG2 H 1 1.6 . . . . . . . 13 ARG HG2 . 7156 1 89 . 1 1 13 13 ARG HG3 H 1 1.65 . . . . . . . 13 ARG HG3 . 7156 1 90 . 1 1 13 13 ARG HD2 H 1 3.2 . . . . . . . 13 ARG HD2 . 7156 1 91 . 1 1 13 13 ARG HD3 H 1 3.2 . . . . . . . 13 ARG HD3 . 7156 1 92 . 1 1 14 14 VAL H H 1 8.51 . . . . . . . 14 VAL H . 7156 1 93 . 1 1 14 14 VAL HA H 1 4.09 . . . . . . . 14 VAL HA . 7156 1 94 . 1 1 14 14 VAL HB H 1 2.02 . . . . . . . 14 VAL HB . 7156 1 95 . 1 1 14 14 VAL HG11 H 1 0.93 . . . . . . . 14 VAL HG1 . 7156 1 96 . 1 1 14 14 VAL HG12 H 1 0.93 . . . . . . . 14 VAL HG1 . 7156 1 97 . 1 1 14 14 VAL HG13 H 1 0.93 . . . . . . . 14 VAL HG1 . 7156 1 98 . 1 1 14 14 VAL HG21 H 1 0.89 . . . . . . . 14 VAL HG2 . 7156 1 99 . 1 1 14 14 VAL HG22 H 1 0.89 . . . . . . . 14 VAL HG2 . 7156 1 100 . 1 1 14 14 VAL HG23 H 1 0.89 . . . . . . . 14 VAL HG2 . 7156 1 101 . 1 1 15 15 ILE H H 1 8.57 . . . . . . . 15 ILE H . 7156 1 102 . 1 1 15 15 ILE HA H 1 4.26 . . . . . . . 15 ILE HA . 7156 1 103 . 1 1 15 15 ILE HB H 1 1.86 . . . . . . . 15 ILE HB . 7156 1 104 . 1 1 15 15 ILE HG12 H 1 1.47 . . . . . . . 15 ILE HG12 . 7156 1 105 . 1 1 15 15 ILE HG13 H 1 1.18 . . . . . . . 15 ILE HG13 . 7156 1 106 . 1 1 15 15 ILE HG21 H 1 0.87 . . . . . . . 15 ILE HG2 . 7156 1 107 . 1 1 15 15 ILE HG22 H 1 0.87 . . . . . . . 15 ILE HG2 . 7156 1 108 . 1 1 15 15 ILE HG23 H 1 0.87 . . . . . . . 15 ILE HG2 . 7156 1 109 . 1 1 15 15 ILE HD11 H 1 0.83 . . . . . . . 15 ILE HD1 . 7156 1 110 . 1 1 15 15 ILE HD12 H 1 0.83 . . . . . . . 15 ILE HD1 . 7156 1 111 . 1 1 15 15 ILE HD13 H 1 0.83 . . . . . . . 15 ILE HD1 . 7156 1 112 . 1 1 16 16 THR H H 1 8.39 . . . . . . . 16 THR H . 7156 1 113 . 1 1 16 16 THR HA H 1 4.31 . . . . . . . 16 THR HA . 7156 1 114 . 1 1 16 16 THR HB H 1 4.24 . . . . . . . 16 THR HB . 7156 1 115 . 1 1 16 16 THR HG21 H 1 1.24 . . . . . . . 16 THR HG2 . 7156 1 116 . 1 1 16 16 THR HG22 H 1 1.24 . . . . . . . 16 THR HG2 . 7156 1 117 . 1 1 16 16 THR HG23 H 1 1.24 . . . . . . . 16 THR HG2 . 7156 1 118 . 1 1 17 17 THR H H 1 8.45 . . . . . . . 17 THR H . 7156 1 119 . 1 1 17 17 THR HA H 1 4.41 . . . . . . . 17 THR HA . 7156 1 120 . 1 1 17 17 THR HB H 1 4.29 . . . . . . . 17 THR HB . 7156 1 121 . 1 1 17 17 THR HG21 H 1 1.15 . . . . . . . 17 THR HG2 . 7156 1 122 . 1 1 17 17 THR HG22 H 1 1.15 . . . . . . . 17 THR HG2 . 7156 1 123 . 1 1 17 17 THR HG23 H 1 1.15 . . . . . . . 17 THR HG2 . 7156 1 124 . 1 1 18 18 PHE H H 1 8.4 . . . . . . . 18 PHE H . 7156 1 125 . 1 1 18 18 PHE HA H 1 4.59 . . . . . . . 18 PHE HA . 7156 1 126 . 1 1 18 18 PHE HB2 H 1 3.08 . . . . . . . 18 PHE HB2 . 7156 1 127 . 1 1 18 18 PHE HB3 H 1 3.03 . . . . . . . 18 PHE HB3 . 7156 1 128 . 1 1 18 18 PHE HD1 H 1 7.22 . . . . . . . 18 PHE HD1 . 7156 1 129 . 1 1 18 18 PHE HD2 H 1 7.22 . . . . . . . 18 PHE HD2 . 7156 1 130 . 1 1 18 18 PHE HE1 H 1 7.28 . . . . . . . 18 PHE HE1 . 7156 1 131 . 1 1 18 18 PHE HE2 H 1 7.28 . . . . . . . 18 PHE HE2 . 7156 1 132 . 1 1 18 18 PHE HZ H 1 7.34 . . . . . . . 18 PHE HZ . 7156 1 133 . 1 1 19 19 ARG H H 1 8.39 . . . . . . . 19 ARG H . 7156 1 134 . 1 1 19 19 ARG HA H 1 4.39 . . . . . . . 19 ARG HA . 7156 1 135 . 1 1 19 19 ARG HB2 H 1 1.77 . . . . . . . 19 ARG HB2 . 7156 1 136 . 1 1 19 19 ARG HB3 H 1 1.73 . . . . . . . 19 ARG HB3 . 7156 1 137 . 1 1 19 19 ARG HG2 H 1 1.54 . . . . . . . 19 ARG HG2 . 7156 1 138 . 1 1 19 19 ARG HG3 H 1 1.54 . . . . . . . 19 ARG HG3 . 7156 1 139 . 1 1 19 19 ARG HD2 H 1 3.17 . . . . . . . 19 ARG HD2 . 7156 1 140 . 1 1 19 19 ARG HD3 H 1 3.17 . . . . . . . 19 ARG HD3 . 7156 1 141 . 1 1 19 19 ARG HH11 H 1 7.2 . . . . . . . 19 ARG NH1 . 7156 1 142 . 1 1 20 20 THR H H 1 8.21 . . . . . . . 20 THR H . 7156 1 143 . 1 1 20 20 THR HA H 1 4.31 . . . . . . . 20 THR HA . 7156 1 144 . 1 1 20 20 THR HB H 1 4.19 . . . . . . . 20 THR HB . 7156 1 145 . 1 1 20 20 THR HG21 H 1 1.24 . . . . . . . 20 THR HG2 . 7156 1 146 . 1 1 20 20 THR HG22 H 1 1.24 . . . . . . . 20 THR HG2 . 7156 1 147 . 1 1 20 20 THR HG23 H 1 1.24 . . . . . . . 20 THR HG2 . 7156 1 148 . 1 1 21 21 GLY H H 1 8.61 . . . . . . . 21 GLY H . 7156 1 149 . 1 1 21 21 GLY HA2 H 1 4.04 . . . . . . . 21 GLY HA2 . 7156 1 150 . 1 1 22 22 THR H H 1 7.91 . . . . . . . 22 THR H . 7156 1 151 . 1 1 22 22 THR HA H 1 4.21 . . . . . . . 22 THR HA . 7156 1 152 . 1 1 22 22 THR HB H 1 4.16 . . . . . . . 22 THR HB . 7156 1 153 . 1 1 22 22 THR HG21 H 1 1.24 . . . . . . . 22 THR HG2 . 7156 1 154 . 1 1 22 22 THR HG22 H 1 1.24 . . . . . . . 22 THR HG2 . 7156 1 155 . 1 1 22 22 THR HG23 H 1 1.24 . . . . . . . 22 THR HG2 . 7156 1 stop_ save_ save_chem_shift_list_2 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chem_shift_list_2 _Assigned_chem_shift_list.Entry_ID 7156 _Assigned_chem_shift_list.ID 2 _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 . . 2 $sample_2 isotropic 7156 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 1 1 SER HA H 1 4.19 . . . . . . . 1 SER HA . 7156 2 2 . 1 1 1 1 SER HB2 H 1 3.97 . . . . . . . 1 SER HB2 . 7156 2 3 . 1 1 2 2 ARG H H 1 8.77 . . . . . . . 2 ARG H . 7156 2 4 . 1 1 2 2 ARG HA H 1 4.32 . . . . . . . 2 ARG HA . 7156 2 5 . 1 1 2 2 ARG HB2 H 1 1.56 . . . . . . . 2 ARG HB2 . 7156 2 6 . 1 1 2 2 ARG HG2 H 1 1.57 . . . . . . . 2 ARG HG2 . 7156 2 7 . 1 1 2 2 ARG HG3 H 1 1.57 . . . . . . . 2 ARG HG3 . 7156 2 8 . 1 1 2 2 ARG HD2 H 1 3.21 . . . . . . . 2 ARG HD2 . 7156 2 9 . 1 1 2 2 ARG HD3 H 1 3.21 . . . . . . . 2 ARG HD3 . 7156 2 10 . 1 1 2 2 ARG HH11 H 1 7.26 . . . . . . . 2 ARG NH1 . 7156 2 11 . 1 1 3 3 TRP H H 1 8.16 . . . . . . . 3 TRP H . 7156 2 12 . 1 1 3 3 TRP HA H 1 4.61 . . . . . . . 3 TRP HA . 7156 2 13 . 1 1 3 3 TRP HB2 H 1 2.85 . . . . . . . 3 TRP HB2 . 7156 2 14 . 1 1 3 3 TRP HB3 H 1 2.7 . . . . . . . 3 TRP HB3 . 7156 2 15 . 1 1 3 3 TRP HD1 H 1 7.25 . . . . . . . 3 TRP HD1 . 7156 2 16 . 1 1 3 3 TRP HE1 H 1 9.46 . . . . . . . 3 TRP HE1 . 7156 2 17 . 1 1 3 3 TRP HE3 H 1 7.5 . . . . . . . 3 TRP HE3 . 7156 2 18 . 1 1 3 3 TRP HZ2 H 1 7.6 . . . . . . . 3 TRP HZ2 . 7156 2 19 . 1 1 3 3 TRP HZ3 H 1 7.25 . . . . . . . 3 TRP HZ3 . 7156 2 20 . 1 1 3 3 TRP HH2 H 1 7.17 . . . . . . . 3 TRP HH2 . 7156 2 21 . 1 1 4 4 TYR H H 1 7.4 . . . . . . . 4 TYR H . 7156 2 22 . 1 1 4 4 TYR HA H 1 4.35 . . . . . . . 4 TYR HA . 7156 2 23 . 1 1 4 4 TYR HB2 H 1 2.85 . . . . . . . 4 TYR HB2 . 7156 2 24 . 1 1 4 4 TYR HB3 H 1 2.66 . . . . . . . 4 TYR HB3 . 7156 2 25 . 1 1 4 4 TYR HD1 H 1 7.01 . . . . . . . 4 TYR HD1 . 7156 2 26 . 1 1 4 4 TYR HD2 H 1 7.01 . . . . . . . 4 TYR HD2 . 7156 2 27 . 1 1 4 4 TYR HE1 H 1 6.8 . . . . . . . 4 TYR HE1 . 7156 2 28 . 1 1 4 4 TYR HE2 H 1 6.8 . . . . . . . 4 TYR HE2 . 7156 2 29 . 1 1 5 5 ASN H H 1 8.04 . . . . . . . 5 ASN H . 7156 2 30 . 1 1 5 5 ASN HA H 1 4.6 . . . . . . . 5 ASN HA . 7156 2 31 . 1 1 5 5 ASN HB2 H 1 3.25 . . . . . . . 5 ASN HB2 . 7156 2 32 . 1 1 5 5 ASN HB3 H 1 3.3 . . . . . . . 5 ASN HB3 . 7156 2 33 . 1 1 5 5 ASN HD21 H 1 7.6 . . . . . . . 5 ASN HD21 . 7156 2 34 . 1 1 5 5 ASN HD22 H 1 6.9 . . . . . . . 5 ASN HD22 . 7156 2 35 . 1 1 6 6 GLN H H 1 8.16 . . . . . . . 6 GLN H . 7156 2 36 . 1 1 6 6 GLN HA H 1 4.4 . . . . . . . 6 GLN HA . 7156 2 37 . 1 1 6 6 GLN HB2 H 1 2.36 . . . . . . . 6 GLN HB2 . 7156 2 38 . 1 1 6 6 GLN HB3 H 1 2 . . . . . . . 6 GLN HB3 . 7156 2 39 . 1 1 6 6 GLN HG2 H 1 7.5 . . . . . . . 6 GLN HG2 . 7156 2 40 . 1 1 6 6 GLN HG3 H 1 6.75 . . . . . . . 6 GLN HG3 . 7156 2 41 . 1 1 6 6 GLN HE21 H 1 2.35 . . . . . . . 6 GLN HE21 . 7156 2 42 . 1 1 6 6 GLN HE22 H 1 2.23 . . . . . . . 6 GLN HE22 . 7156 2 43 . 1 1 7 7 THR H H 1 8.19 . . . . . . . 7 THR H . 7156 2 44 . 1 1 7 7 THR HA H 1 4.49 . . . . . . . 7 THR HA . 7156 2 45 . 1 1 7 7 THR HB H 1 4.26 . . . . . . . 7 THR HB . 7156 2 46 . 1 1 7 7 THR HG21 H 1 1.28 . . . . . . . 7 THR HG2 . 7156 2 47 . 1 1 7 7 THR HG22 H 1 1.28 . . . . . . . 7 THR HG2 . 7156 2 48 . 1 1 7 7 THR HG23 H 1 1.28 . . . . . . . 7 THR HG2 . 7156 2 49 . 1 1 8 8 PRO HA H 1 4.39 . . . . . . . 8 PRO HA . 7156 2 50 . 1 1 8 8 PRO HB2 H 1 2.33 . . . . . . . 8 PRO HB2 . 7156 2 51 . 1 1 8 8 PRO HG2 H 1 2.1 . . . . . . . 8 PRO HG2 . 7156 2 52 . 1 1 8 8 PRO HG3 H 1 2.03 . . . . . . . 8 PRO HG3 . 7156 2 53 . 1 1 8 8 PRO HD2 H 1 3.82 . . . . . . . 8 PRO HD2 . 7156 2 54 . 1 1 8 8 PRO HD3 H 1 3.73 . . . . . . . 8 PRO HD3 . 7156 2 55 . 1 1 9 9 ASN H H 1 8.16 . . . . . . . 9 ASN H . 7156 2 56 . 1 1 9 9 ASN HA H 1 4.6 . . . . . . . 9 ASN HA . 7156 2 57 . 1 1 9 9 ASN HB2 H 1 2.94 . . . . . . . 9 ASN HB2 . 7156 2 58 . 1 1 9 9 ASN HB3 H 1 2.87 . . . . . . . 9 ASN HB3 . 7156 2 59 . 1 1 9 9 ASN HD21 H 1 7.73 . . . . . . . 9 ASN HD21 . 7156 2 60 . 1 1 9 9 ASN HD22 H 1 6.88 . . . . . . . 9 ASN HD22 . 7156 2 61 . 1 1 10 10 ARG H H 1 8.31 . . . . . . . 10 ARG H . 7156 2 62 . 1 1 10 10 ARG HA H 1 4.07 . . . . . . . 10 ARG HA . 7156 2 63 . 1 1 10 10 ARG HB2 H 1 1.92 . . . . . . . 10 ARG HB2 . 7156 2 64 . 1 1 10 10 ARG HB3 H 1 1.73 . . . . . . . 10 ARG HB3 . 7156 2 65 . 1 1 10 10 ARG HG2 H 1 1.65 . . . . . . . 10 ARG HG2 . 7156 2 66 . 1 1 10 10 ARG HG3 H 1 1.65 . . . . . . . 10 ARG HG3 . 7156 2 67 . 1 1 10 10 ARG HD2 H 1 3.2 . . . . . . . 10 ARG HD2 . 7156 2 68 . 1 1 10 10 ARG HD3 H 1 3.2 . . . . . . . 10 ARG HD3 . 7156 2 69 . 1 1 10 10 ARG HH11 H 1 7.26 . . . . . . . 10 ARG NH1 . 7156 2 70 . 1 1 11 11 ALA H H 1 8.08 . . . . . . . 11 ALA H . 7156 2 71 . 1 1 11 11 ALA HA H 1 4.09 . . . . . . . 11 ALA HA . 7156 2 72 . 1 1 11 11 ALA HB1 H 1 1.47 . . . . . . . 11 ALA HB . 7156 2 73 . 1 1 11 11 ALA HB2 H 1 1.47 . . . . . . . 11 ALA HB . 7156 2 74 . 1 1 11 11 ALA HB3 H 1 1.47 . . . . . . . 11 ALA HB . 7156 2 75 . 1 1 12 12 LYS H H 1 7.97 . . . . . . . 12 LYS H . 7156 2 76 . 1 1 12 12 LYS HA H 1 4 . . . . . . . 12 LYS HA . 7156 2 77 . 1 1 12 12 LYS HB2 H 1 1.94 . . . . . . . 12 LYS HB2 . 7156 2 78 . 1 1 12 12 LYS HB3 H 1 1.78 . . . . . . . 12 LYS HB3 . 7156 2 79 . 1 1 12 12 LYS HG2 H 1 1.57 . . . . . . . 12 LYS HG2 . 7156 2 80 . 1 1 12 12 LYS HG3 H 1 1.57 . . . . . . . 12 LYS HG3 . 7156 2 81 . 1 1 12 12 LYS HD2 H 1 1.72 . . . . . . . 12 LYS HD2 . 7156 2 82 . 1 1 12 12 LYS HD3 H 1 1.72 . . . . . . . 12 LYS HD3 . 7156 2 83 . 1 1 12 12 LYS HE2 H 1 2.96 . . . . . . . 12 LYS HE2 . 7156 2 84 . 1 1 12 12 LYS HE3 H 1 2.96 . . . . . . . 12 LYS HE3 . 7156 2 85 . 1 1 13 13 ARG H H 1 7.97 . . . . . . . 13 ARG H . 7156 2 86 . 1 1 13 13 ARG HA H 1 4.1 . . . . . . . 13 ARG HA . 7156 2 87 . 1 1 13 13 ARG HB2 H 1 2.1 . . . . . . . 13 ARG HB2 . 7156 2 88 . 1 1 13 13 ARG HB3 H 1 2 . . . . . . . 13 ARG HB3 . 7156 2 89 . 1 1 13 13 ARG HG2 H 1 1.75 . . . . . . . 13 ARG HG2 . 7156 2 90 . 1 1 13 13 ARG HG3 H 1 1.65 . . . . . . . 13 ARG HG3 . 7156 2 91 . 1 1 13 13 ARG HD2 H 1 3.2 . . . . . . . 13 ARG HD2 . 7156 2 92 . 1 1 13 13 ARG HD3 H 1 3.2 . . . . . . . 13 ARG HD3 . 7156 2 93 . 1 1 13 13 ARG HH11 H 1 7.3 . . . . . . . 13 ARG NH1 . 7156 2 94 . 1 1 14 14 VAL H H 1 8.21 . . . . . . . 14 VAL H . 7156 2 95 . 1 1 14 14 VAL HA H 1 3.66 . . . . . . . 14 VAL HA . 7156 2 96 . 1 1 14 14 VAL HB H 1 2.24 . . . . . . . 14 VAL HB . 7156 2 97 . 1 1 14 14 VAL HG11 H 1 1.07 . . . . . . . 14 VAL HG1 . 7156 2 98 . 1 1 14 14 VAL HG12 H 1 1.07 . . . . . . . 14 VAL HG1 . 7156 2 99 . 1 1 14 14 VAL HG13 H 1 1.07 . . . . . . . 14 VAL HG1 . 7156 2 100 . 1 1 14 14 VAL HG21 H 1 0.93 . . . . . . . 14 VAL HG2 . 7156 2 101 . 1 1 14 14 VAL HG22 H 1 0.93 . . . . . . . 14 VAL HG2 . 7156 2 102 . 1 1 14 14 VAL HG23 H 1 0.93 . . . . . . . 14 VAL HG2 . 7156 2 103 . 1 1 15 15 ILE H H 1 8.56 . . . . . . . 15 ILE H . 7156 2 104 . 1 1 15 15 ILE HA H 1 3.8 . . . . . . . 15 ILE HA . 7156 2 105 . 1 1 15 15 ILE HB H 1 1.9 . . . . . . . 15 ILE HB . 7156 2 106 . 1 1 15 15 ILE HG12 H 1 1.39 . . . . . . . 15 ILE HG12 . 7156 2 107 . 1 1 15 15 ILE HG13 H 1 1.2 . . . . . . . 15 ILE HG13 . 7156 2 108 . 1 1 15 15 ILE HG21 H 1 0.96 . . . . . . . 15 ILE HG2 . 7156 2 109 . 1 1 15 15 ILE HG22 H 1 0.96 . . . . . . . 15 ILE HG2 . 7156 2 110 . 1 1 15 15 ILE HG23 H 1 0.96 . . . . . . . 15 ILE HG2 . 7156 2 111 . 1 1 15 15 ILE HD11 H 1 0.85 . . . . . . . 15 ILE HD1 . 7156 2 112 . 1 1 15 15 ILE HD12 H 1 0.85 . . . . . . . 15 ILE HD1 . 7156 2 113 . 1 1 15 15 ILE HD13 H 1 0.85 . . . . . . . 15 ILE HD1 . 7156 2 114 . 1 1 16 16 THR H H 1 8.14 . . . . . . . 16 THR H . 7156 2 115 . 1 1 16 16 THR HA H 1 4.03 . . . . . . . 16 THR HA . 7156 2 116 . 1 1 16 16 THR HB H 1 4.31 . . . . . . . 16 THR HB . 7156 2 117 . 1 1 16 16 THR HG21 H 1 1.29 . . . . . . . 16 THR HG2 . 7156 2 118 . 1 1 16 16 THR HG22 H 1 1.29 . . . . . . . 16 THR HG2 . 7156 2 119 . 1 1 16 16 THR HG23 H 1 1.29 . . . . . . . 16 THR HG2 . 7156 2 120 . 1 1 17 17 THR H H 1 8.06 . . . . . . . 17 THR H . 7156 2 121 . 1 1 17 17 THR HA H 1 4.04 . . . . . . . 17 THR HA . 7156 2 122 . 1 1 17 17 THR HB H 1 4.32 . . . . . . . 17 THR HB . 7156 2 123 . 1 1 17 17 THR HG21 H 1 1.14 . . . . . . . 17 THR HG2 . 7156 2 124 . 1 1 17 17 THR HG22 H 1 1.14 . . . . . . . 17 THR HG2 . 7156 2 125 . 1 1 17 17 THR HG23 H 1 1.14 . . . . . . . 17 THR HG2 . 7156 2 126 . 1 1 18 18 PHE H H 1 8.34 . . . . . . . 18 PHE H . 7156 2 127 . 1 1 18 18 PHE HA H 1 4.46 . . . . . . . 18 PHE HA . 7156 2 128 . 1 1 18 18 PHE HB2 H 1 3.27 . . . . . . . 18 PHE HB2 . 7156 2 129 . 1 1 18 18 PHE HB3 H 1 3.22 . . . . . . . 18 PHE HB3 . 7156 2 130 . 1 1 18 18 PHE HD1 H 1 7.27 . . . . . . . 18 PHE HD1 . 7156 2 131 . 1 1 18 18 PHE HD2 H 1 7.27 . . . . . . . 18 PHE HD2 . 7156 2 132 . 1 1 18 18 PHE HE1 H 1 7.32 . . . . . . . 18 PHE HE1 . 7156 2 133 . 1 1 18 18 PHE HE2 H 1 7.32 . . . . . . . 18 PHE HE2 . 7156 2 134 . 1 1 18 18 PHE HZ H 1 7.3 . . . . . . . 18 PHE HZ . 7156 2 135 . 1 1 19 19 ARG H H 1 8.46 . . . . . . . 19 ARG H . 7156 2 136 . 1 1 19 19 ARG HA H 1 4.24 . . . . . . . 19 ARG HA . 7156 2 137 . 1 1 19 19 ARG HB2 H 1 2.03 . . . . . . . 19 ARG HB2 . 7156 2 138 . 1 1 19 19 ARG HB3 H 1 1.96 . . . . . . . 19 ARG HB3 . 7156 2 139 . 1 1 19 19 ARG HG2 H 1 1.74 . . . . . . . 19 ARG HG2 . 7156 2 140 . 1 1 19 19 ARG HG3 H 1 1.74 . . . . . . . 19 ARG HG3 . 7156 2 141 . 1 1 19 19 ARG HD2 H 1 3.2 . . . . . . . 19 ARG HD2 . 7156 2 142 . 1 1 19 19 ARG HD3 H 1 3.2 . . . . . . . 19 ARG HD3 . 7156 2 143 . 1 1 19 19 ARG HH11 H 1 7.26 . . . . . . . 19 ARG NH1 . 7156 2 144 . 1 1 20 20 THR H H 1 8.03 . . . . . . . 20 THR H . 7156 2 145 . 1 1 20 20 THR HA H 1 4.38 . . . . . . . 20 THR HA . 7156 2 146 . 1 1 20 20 THR HB H 1 4.36 . . . . . . . 20 THR HB . 7156 2 147 . 1 1 20 20 THR HG21 H 1 1.32 . . . . . . . 20 THR HG2 . 7156 2 148 . 1 1 20 20 THR HG22 H 1 1.32 . . . . . . . 20 THR HG2 . 7156 2 149 . 1 1 20 20 THR HG23 H 1 1.32 . . . . . . . 20 THR HG2 . 7156 2 150 . 1 1 21 21 GLY H H 1 8.26 . . . . . . . 21 GLY H . 7156 2 151 . 1 1 21 21 GLY HA2 H 1 4.05 . . . . . . . 21 GLY HA2 . 7156 2 152 . 1 1 22 22 THR H H 1 7.79 . . . . . . . 22 THR H . 7156 2 153 . 1 1 22 22 THR HA H 1 4.43 . . . . . . . 22 THR HA . 7156 2 154 . 1 1 22 22 THR HB H 1 4.34 . . . . . . . 22 THR HB . 7156 2 155 . 1 1 22 22 THR HG21 H 1 1.18 . . . . . . . 22 THR HG2 . 7156 2 156 . 1 1 22 22 THR HG22 H 1 1.18 . . . . . . . 22 THR HG2 . 7156 2 157 . 1 1 22 22 THR HG23 H 1 1.18 . . . . . . . 22 THR HG2 . 7156 2 stop_ save_