data_915 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 915 _Entry.Title ; Assignment of the Backbone 1H and 15N NMR Resonances of Bacteriophage T4 Lysozyme ; _Entry.Type macromolecule _Entry.Version_type update _Entry.Submission_date 1995-07-31 _Entry.Accession_date 1996-03-25 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination BMRB _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Lawrence McIntosh . P. . 915 2 A. Wand . Joshua . 915 3 David Lowry . F. . 915 4 Alfred Redfield . G. . 915 5 Frederick Dahlquist . W. . 915 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 915 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '15N chemical shifts' 166 915 '1H chemical shifts' 719 915 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 4 . . 2010-06-11 . revision BMRB 'Complete natural source information' 915 3 . . 1999-06-14 . revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 915 2 . . 1996-03-25 . reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 915 1 . . 1995-07-31 . original BMRB 'Last release in original BMRB flat-file format' 915 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 915 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; McIntosh, Lawrence P., Wand, A. Joshua, Lowry, David F., Redfield, Alfred G., Dahlquist, Frederick W., "Assignment of the Backbone 1H and 15N NMR Resonances of Bacteriophage T4 Lysozyme," Biochemistry 29, 6341-6362 (1990). ; _Citation.Title ; Assignment of the Backbone 1H and 15N NMR Resonances of Bacteriophage T4 Lysozyme ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 29 _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 6341 _Citation.Page_last 6362 _Citation.Year 1990 _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 Lawrence McIntosh . P. . 915 1 2 A. Wand . Joshua . 915 1 3 David Lowry . F. . 915 1 4 Alfred Redfield . G. . 915 1 5 Frederick Dahlquist . W. . 915 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_T4_lysozyme _Assembly.Sf_category assembly _Assembly.Sf_framecode system_T4_lysozyme _Assembly.Entry_ID 915 _Assembly.ID 1 _Assembly.Name 'T4 lysozyme' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic . _Assembly.Thiol_state . _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 'T4 lysozyme' 1 $T4_lysozyme . . . . . . . . . 915 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'T4 lysozyme' system 915 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_T4_lysozyme _Entity.Sf_category entity _Entity.Sf_framecode T4_lysozyme _Entity.Entry_ID 915 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'T4 lysozyme' _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can ; MNIFEMLRIDEGLRLKIYKD TEGYYTIGIGHLLTKSPSLN AAKSELDKAIGRNCNGVITK DEAEKLFNQDVDAAVRGILR NAKLKPVYDSLDAVRRCALI NMVFQMGETGVAGFTNSLRM LQQKRWDEAAVNLAKSRWYN QTPNRAKRVITTFRTGTWDA YKNL ; _Entity.Polymer_seq_one_letter_code ; MNIFEMLRIDEGLRLKIYKD TEGYYTIGIGHLLTKSPSLN AAKSELDKAIGRNCNGVITK DEAEKLFNQDVDAAVRGILR NAKLKPVYDSLDAVRRCALI NMVFQMGETGVAGFTNSLRM LQQKRWDEAAVNLAKSRWYN QTPNRAKRVITTFRTGTWDA YKNL ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 164 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number 3.2.1.17 _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 96.95 96.95 5.42e-112 . . . . 915 1 2 no BMRB 17604 . T4_L99A . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 3 no PDB 102L . "How Amino-Acid Insertions Are Allowed In An Alpha-Helix Of T4 Lysozyme" . . . . . 100.61 165 98.18 98.18 9.98e-113 . . . . 915 1 4 no PDB 103L . "How Amino-Acid Insertions Are Allowed In An Alpha-Helix Of T4 Lysozyme" . . . . . 101.83 167 97.01 97.01 2.43e-112 . . . . 915 1 5 no PDB 104L . "How Amino-Acid Insertions Are Allowed In An Alpha-Helix Of T4 Lysozyme" . . . . . 101.22 166 97.59 97.59 1.16e-112 . . . . 915 1 6 no PDB 107L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 98.17 98.17 1.12e-113 . . . . 915 1 7 no PDB 108L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 98.17 98.17 1.73e-113 . . . . 915 1 8 no PDB 109L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 98.17 98.17 1.05e-113 . . . . 915 1 9 no PDB 110L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 98.17 98.17 1.70e-113 . . . . 915 1 10 no PDB 111L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 98.17 98.78 7.81e-114 . . . . 915 1 11 no PDB 112L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 98.17 98.17 1.04e-113 . . . . 915 1 12 no PDB 113L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 98.17 98.17 1.33e-113 . . . . 915 1 13 no PDB 114L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 98.17 98.78 4.23e-114 . . . . 915 1 14 no PDB 115L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 98.17 98.17 1.13e-113 . . . . 915 1 15 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 98.17 98.78 3.36e-114 . . . . 915 1 16 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 98.17 98.78 3.36e-114 . . . . 915 1 17 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 98.17 98.78 3.36e-114 . . . . 915 1 18 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 98.17 98.78 3.36e-114 . . . . 915 1 19 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 98.17 98.78 3.36e-114 . . . . 915 1 20 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 98.17 98.78 3.36e-114 . . . . 915 1 21 no PDB 126L . "The Energetic Cost And The Structural Consequences Of Burying A Hydroxyl Group Within The Core Of A Protein Determined From Ala" . . . . . 100.00 164 98.17 98.17 6.27e-114 . . . . 915 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 98.17 98.17 6.27e-114 . . . . 915 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 98.17 98.17 6.27e-114 . . . . 915 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 98.17 98.17 6.41e-114 . . . . 915 1 25 no PDB 130L . "Structures Of Randomly Generated Mutants Of T4 Lysozyme Show That Protein Stability Can Be Enhanced By Relaxation Of Strain And" . . . . . 100.00 164 98.17 98.78 3.96e-114 . . . . 915 1 26 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 98.17 98.78 3.96e-114 . . . . 915 1 27 no PDB 137L . "Structural Basis Of Amino Acid Alpha Helix Propensity" . . . . . 100.00 164 98.17 98.17 2.11e-113 . . . . 915 1 28 no PDB 138L . "Rapid Crystallization Of T4 Lysozyme By Intermolecular Disulfide Crosslinking" . . . . . 100.00 164 98.17 98.17 1.96e-113 . . . . 915 1 29 no PDB 139L . "Rapid Crystallization Of T4 Lysozyme By Intermolecular Disulfide Crosslinking" . . . . . 100.00 164 97.56 97.56 6.18e-112 . . . . 915 1 30 no PDB 140L . "Role Of Backbone Flexibility In The Accommodation Of Variants That Repack The Core Of T4 Lysozyme" . . . . . 100.00 164 96.95 96.95 4.76e-112 . . . . 915 1 31 no PDB 141L . "Role Of Backbone Flexibility In The Accommodation Of Variants That Repack The Core Of T4 Lysozyme" . . . . . 100.00 164 96.95 97.56 8.74e-113 . . . . 915 1 32 no PDB 145L . "Role Of Backbone Flexibility In The Accommodation Of Variants That Repack The Core Of T4 Lysozyme" . . . . . 100.00 164 96.95 98.17 1.65e-112 . . . . 915 1 33 no PDB 147L . "Role Of Backbone Flexibility In The Accommodation Of Variants That Repack The Core Of T4 Lysozyme" . . . . . 100.00 164 96.95 98.17 5.77e-113 . . . . 915 1 34 no PDB 148L . "A Covalent Enzyme-Substrate Intermediate With Saccharide Distortion In A Mutant T4 Lysozyme" . . . . . 100.00 164 98.17 98.17 1.33e-113 . . . . 915 1 35 no PDB 149L . "Conservation Of Solvent-Binding Sites In 10 Crystal Forms Of T4 Lysozyme" . . . . . 100.00 164 99.39 100.00 2.23e-116 . . . . 915 1 36 no PDB 150L . "Conservation Of Solvent-Binding Sites In 10 Crystal Forms Of T4 Lysozyme" . . . . . 100.00 164 99.39 100.00 3.93e-116 . . . . 915 1 37 no PDB 151L . "Conservation Of Solvent-Binding Sites In 10 Crystal Forms Of T4 Lysozyme" . . . . . 100.00 164 97.56 98.17 8.80e-114 . . . . 915 1 38 no PDB 152L . "Conservation Of Solvent-Binding Sites In 10 Crystal Forms Of T4 Lysozyme" . . . . . 99.39 164 96.93 96.93 2.08e-111 . . . . 915 1 39 no PDB 155L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 97.56 98.17 2.46e-113 . . . . 915 1 40 no PDB 156L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 97.56 97.56 7.50e-113 . . . . 915 1 41 no PDB 158L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 97.56 98.17 4.25e-113 . . . . 915 1 42 no PDB 159L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 97.56 97.56 1.32e-112 . . . . 915 1 43 no PDB 160L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 98.17 98.17 1.29e-113 . . . . 915 1 44 no PDB 161L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 98.17 98.17 1.35e-113 . . . . 915 1 45 no PDB 162L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 98.17 98.17 1.29e-113 . . . . 915 1 46 no PDB 163L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 98.17 98.17 1.29e-113 . . . . 915 1 47 no PDB 164L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 98.17 98.17 1.30e-113 . . . . 915 1 48 no PDB 165L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 98.17 98.78 4.33e-114 . . . . 915 1 49 no PDB 166L . "Control Of Enzyme Activity By An Engineered Disulfide Bond" . . . . . 100.00 164 98.17 98.17 7.81e-114 . . . . 915 1 50 no PDB 167L . "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" . . . . . 99.39 164 98.16 98.16 7.18e-113 . . . . 915 1 51 no PDB 170L . "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" . . . . . 100.00 164 98.17 98.17 1.98e-113 . . . . 915 1 52 no PDB 171L . "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" . . . . . 100.00 164 98.17 98.17 9.93e-114 . . . . 915 1 53 no PDB 172L . "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" . . . . . 100.00 164 99.39 99.39 4.58e-116 . . . . 915 1 54 no PDB 173L . "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" . . . . . 100.00 164 97.56 99.39 1.89e-114 . . . . 915 1 55 no PDB 175L . "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" . . . . . 100.00 164 98.17 98.17 1.30e-113 . . . . 915 1 56 no PDB 177L . "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" . . . . . 100.00 164 97.56 97.56 3.44e-111 . . . . 915 1 57 no PDB 178L . "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" . . . . . 100.00 164 97.56 97.56 3.44e-111 . . . . 915 1 58 no PDB 180L . "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" . . . . . 100.00 164 98.17 98.17 1.33e-113 . . . . 915 1 59 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 98.17 98.17 7.64e-114 . . . . 915 1 60 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 98.17 98.17 7.64e-114 . . . . 915 1 61 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 98.17 98.17 7.64e-114 . . . . 915 1 62 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 98.17 98.17 7.64e-114 . . . . 915 1 63 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 98.17 98.17 7.64e-114 . . . . 915 1 64 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 98.17 98.17 7.64e-114 . . . . 915 1 65 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 98.17 98.17 7.64e-114 . . . . 915 1 66 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 98.17 98.17 7.64e-114 . . . . 915 1 67 no PDB 190L . "A Helix Initiation Signal In T4 Lysozyme Identified By Polyalanine Mutagenesis" . . . . . 100.00 164 98.17 98.17 2.86e-114 . . . . 915 1 68 no PDB 195L . 'Thermodynamic And Structural Compensation In "size-Switch" Core-Repacking Variants Of T4 Lysozyme' . . . . . 100.00 164 98.17 98.17 1.04e-113 . . . . 915 1 69 no PDB 196L . 'Thermodynamic And Structural Compensation In "size-Switch" Core-Repacking Variants Of T4 Lysozyme' . . . . . 100.00 164 98.17 98.17 8.07e-114 . . . . 915 1 70 no PDB 197L . 'Thermodynamic And Structural Compensation In "size-Switch" Core-Repacking Variants Of T4 Lysozyme' . . . . . 100.00 164 97.56 97.56 1.72e-112 . . . . 915 1 71 no PDB 198L . 'Thermodynamic And Structural Compensation In "size-Switch" Core-Repacking Variants Of T4 Lysozyme' . . . . . 100.00 164 97.56 97.56 8.10e-113 . . . . 915 1 72 no PDB 199L . 'Thermodynamic And Structural Compensation In "size-Switch" Core-Repacking Variants Of T4 Lysozyme' . . . . . 100.00 164 97.56 97.56 5.52e-113 . . . . 915 1 73 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 97.56 97.56 1.02e-111 . . . . 915 1 74 no PDB 1C60 . "T4 Lysozyme Mutant C54tC97AF153A IN THE PRESENCE OF 8 ATM Argon" . . . . . 100.00 164 98.17 98.17 2.28e-113 . . . . 915 1 75 no PDB 1C61 . "T4 Lysozyme Mutant C54tC97AF153A IN THE PRESENCE OF 8 ATM Krypton" . . . . . 100.00 164 98.17 98.17 2.28e-113 . . . . 915 1 76 no PDB 1C62 . "T4 Lysozyme Mutant C54tC97AF153A IN THE PRESENCE OF 8 ATM Xenon" . . . . . 100.00 164 98.17 98.17 2.28e-113 . . . . 915 1 77 no PDB 1C63 . "T4 Lysozyme Mutant C54tC97AL121A IN THE PRESENCE OF 8 ATM Argon" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 78 no PDB 1C64 . "T4 Lysozyme Mutant C54tC97AL121A IN THE PRESENCE OF 8 ATM Krypton" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 79 no PDB 1C65 . "T4 Lysozyme Mutant C54tC97AL121A IN THE PRESENCE OF 8 ATM Xenon" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 80 no PDB 1C66 . "T4 Lysozyme Mutant C54tC97AL121AL133A IN THE PRESENCE OF 8 Atm Argon" . . . . . 100.00 164 97.56 97.56 4.54e-113 . . . . 915 1 81 no PDB 1C67 . "T4 Lysozyme Mutant C54tC97AL121AL133A IN THE PRESENCE OF 8 Atm Krypton" . . . . . 100.00 164 97.56 97.56 4.54e-113 . . . . 915 1 82 no PDB 1C68 . "T4 Lysozyme Mutant C54tC97AL121AL133A IN THE PRESENCE OF 8 Atm Xenon" . . . . . 100.00 164 97.56 97.56 4.54e-113 . . . . 915 1 83 no PDB 1C69 . "T4 Lysozyme Mutant C54tC97AL133A IN THE PRESENCE OF 8 ATM Argon" . . . . . 100.00 164 99.39 99.39 4.20e-116 . . . . 915 1 84 no PDB 1C6A . "T4 Lysozyme Mutant C54tC97AL133A IN THE PRESENCE OF 8 ATM Krypton" . . . . . 100.00 164 99.39 99.39 4.20e-116 . . . . 915 1 85 no PDB 1C6B . "T4 Lysozyme Mutant C54tC97AL133A IN THE PRESENCE OF 8 ATM Xenon" . . . . . 100.00 164 99.39 99.39 4.20e-116 . . . . 915 1 86 no PDB 1C6C . "T4 Lysozyme Mutant C54tC97AL99A IN THE PRESENCE OF 16 ATM Argon" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 87 no PDB 1C6D . "T4 Lysozyme Mutant C54tC97AL99A IN THE PRESENCE OF 16 ATM Krypton" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 88 no PDB 1C6E . "T4 Lysozyme Mutant C54tC97AL99A IN THE PRESENCE OF 2 ATM Xenon" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 89 no PDB 1C6F . "T4 Lysozyme Mutant C54tC97AL99A IN THE PRESENCE OF 32 ATM Argon" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 90 no PDB 1C6G . "T4 Lysozyme Mutant C54tC97AL99A IN THE PRESENCE OF 4 ATM Krypton" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 91 no PDB 1C6H . "T4 Lysozyme Mutant C54tC97AL99A IN THE PRESENCE OF 4 ATM Xenon" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 92 no PDB 1C6I . "T4 Lysozyme Mutant C54tC97AL99A IN THE PRESENCE OF 8 ATM Argon" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 93 no PDB 1C6J . "T4 Lysozyme Mutant C54tC97AL99A IN THE PRESENCE OF 8 ATM Krypton" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 94 no PDB 1C6K . "T4 Lysozyme Mutant C54tC97AL99A IN THE PRESENCE OF 8 ATM Xenon" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 95 no PDB 1C6L . "T4 Lysozyme Mutant C54tC97AL99AF153A IN THE PRESENCE OF 8 Atm Argon" . . . . . 100.00 164 97.56 97.56 1.40e-112 . . . . 915 1 96 no PDB 1C6M . "T4 Lysozyme Mutant C54tC97AL99AF153A IN THE PRESENCE OF 8 Atm Krypton" . . . . . 100.00 164 97.56 97.56 1.40e-112 . . . . 915 1 97 no PDB 1C6N . "T4 Lysozyme Mutant C54tC97AL99AF153A IN THE PRESENCE OF 8 Atm Xenon" . . . . . 100.00 164 97.56 97.56 1.40e-112 . . . . 915 1 98 no PDB 1C6P . "T4 Lysozyme Mutant C54tC97A IN THE PRESENCE OF 8 ATM ARGON" . . . . . 100.00 164 98.78 98.78 1.45e-114 . . . . 915 1 99 no PDB 1C6Q . "T4 Lysozyme Mutant C54tC97A IN THE PRESENCE OF 8 ATM Krypton" . . . . . 100.00 164 98.78 98.78 1.45e-114 . . . . 915 1 100 no PDB 1C6T . "T4 Lysozyme Mutant C54tC97A IN THE PRESENCE OF 8 ATM XENON" . . . . . 100.00 164 98.78 98.78 1.45e-114 . . . . 915 1 101 no PDB 1CTW . "T4 Lysozyme Mutant I78a" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 102 no PDB 1CU0 . "T4 Lysozyme Mutant I78m" . . . . . 100.00 164 98.17 98.78 3.48e-114 . . . . 915 1 103 no PDB 1CU2 . "T4 Lysozyme Mutant L84m" . . . . . 100.00 164 98.17 98.78 2.40e-114 . . . . 915 1 104 no PDB 1CU3 . "T4 Lysozyme Mutant V87m" . . . . . 100.00 164 98.17 98.78 4.10e-114 . . . . 915 1 105 no PDB 1CU5 . "T4 Lysozyme Mutant L91m" . . . . . 100.00 164 98.17 98.78 2.40e-114 . . . . 915 1 106 no PDB 1CU6 . "T4 Lysozyme Mutant L91a" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 107 no PDB 1CUP . "Methionine Core Mutant Of T4 Lysozyme" . . . . . 100.00 164 98.17 98.78 3.48e-114 . . . . 915 1 108 no PDB 1CUQ . "T4 Lysozyme Mutant V103m" . . . . . 100.00 164 98.17 98.78 4.10e-114 . . . . 915 1 109 no PDB 1CV0 . "T4 Lysozyme Mutant F104m" . . . . . 100.00 164 98.17 98.17 1.18e-113 . . . . 915 1 110 no PDB 1CV1 . "T4 Lysozyme Mutant V111m" . . . . . 100.00 164 98.17 98.78 4.10e-114 . . . . 915 1 111 no PDB 1CV3 . "T4 Lysozyme Mutant L121m" . . . . . 100.00 164 98.17 98.78 2.40e-114 . . . . 915 1 112 no PDB 1CV4 . "T4 Lysozyme Mutant L118m" . . . . . 100.00 164 98.17 98.78 2.40e-114 . . . . 915 1 113 no PDB 1CV5 . "T4 Lysozyme Mutant L133m" . . . . . 100.00 164 98.17 98.78 2.40e-114 . . . . 915 1 114 no PDB 1CV6 . "T4 Lysozyme Mutant V149m" . . . . . 100.00 164 98.17 98.78 4.10e-114 . . . . 915 1 115 no PDB 1CVK . "T4 Lysozyme Mutant L118a" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 116 no PDB 1D2W . "N-Terminal Domain Core Methionine Mutation" . . . . . 100.00 164 98.17 98.78 3.48e-114 . . . . 915 1 117 no PDB 1D2Y . "N-Terminal Domain Core Methionine Mutation" . . . . . 100.00 164 98.17 98.78 3.48e-114 . . . . 915 1 118 no PDB 1D3F . "N-Terminal Domain Core Methionine Mutation" . . . . . 100.00 164 98.17 98.78 3.48e-114 . . . . 915 1 119 no PDB 1D3J . "N-Terminal Domain Core Methionine Mutation" . . . . . 100.00 164 98.17 98.78 2.40e-114 . . . . 915 1 120 no PDB 1D9W . "Bacteriophage T4 Lysozyme Mutant" . . . . . 100.00 164 99.39 99.39 7.02e-116 . . . . 915 1 121 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 99.39 99.39 9.03e-116 . . . . 915 1 122 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 99.39 99.39 1.21e-115 . . . . 915 1 123 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 99.39 100.00 1.16e-116 . . . . 915 1 124 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 99.39 100.00 2.23e-116 . . . . 915 1 125 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 99.39 99.39 4.58e-116 . . . . 915 1 126 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 99.39 100.00 2.23e-116 . . . . 915 1 127 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 99.39 99.39 6.43e-116 . . . . 915 1 128 no PDB 1EPY . "T4 Lysozyme Mutant, T21hC54TC97AQ141HT142H" . . . . . 100.00 164 96.95 96.95 3.99e-112 . . . . 915 1 129 no PDB 1G06 . "Crystal Structure Of T4 Lysozyme Mutant V149s" . . . . . 100.00 164 98.17 98.17 7.98e-114 . . . . 915 1 130 no PDB 1G07 . "Crystal Structure Of T4 Lysozyme Mutant V149c" . . . . . 100.00 164 98.17 98.17 2.41e-113 . . . . 915 1 131 no PDB 1G0G . "Crystal Structure Of T4 Lysozyme Mutant T152a" . . . . . 100.00 164 98.17 98.17 7.81e-114 . . . . 915 1 132 no PDB 1G0J . "Crystal Structure Of T4 Lysozyme Mutant T152s" . . . . . 100.00 164 98.17 98.78 3.96e-114 . . . . 915 1 133 no PDB 1G0K . "Crystal Structure Of T4 Lysozyme Mutant T152c" . . . . . 100.00 164 98.17 98.17 2.66e-113 . . . . 915 1 134 no PDB 1G0L . "Crystal Structure Of T4 Lysozyme Mutant T152v" . . . . . 100.00 164 98.17 98.17 7.07e-114 . . . . 915 1 135 no PDB 1G0M . "Crystal Structure Of T4 Lysozyme Mutant T152i" . . . . . 100.00 164 98.17 98.17 9.10e-114 . . . . 915 1 136 no PDB 1G0P . "Crystal Structure Of T4 Lysozyme Mutant V149g" . . . . . 100.00 164 98.17 98.17 2.63e-113 . . . . 915 1 137 no PDB 1G0Q . "Crystal Structure Of T4 Lysozyme Mutant V149i" . . . . . 100.00 164 98.17 98.78 2.35e-114 . . . . 915 1 138 no PDB 1G1V . "T4 Lysozyme Mutant C54tC97AI58T" . . . . . 100.00 164 98.17 98.17 6.63e-114 . . . . 915 1 139 no PDB 1G1W . "T4 Lysozyme Mutant C54tC97AQ105M" . . . . . 100.00 164 98.17 98.17 1.21e-113 . . . . 915 1 140 no PDB 1I6S . "T4 Lysozyme Mutant C54tC97AN101A" . . . . . 100.00 164 98.17 98.17 1.35e-113 . . . . 915 1 141 no PDB 1JQU . "Are Carboxy Terminii Of Helices Coded By The Local Sequence Or By Tertiary Structure Contacts" . . . . . 100.00 164 98.17 98.17 4.69e-113 . . . . 915 1 142 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 98.78 98.78 1.93e-114 . . . . 915 1 143 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 98.78 98.78 1.93e-114 . . . . 915 1 144 no PDB 1KNI . "Stabilizing Disulfide Bridge Mutant Of T4 Lysozyme" . . . . . 100.00 164 97.56 97.56 4.08e-112 . . . . 915 1 145 no PDB 1KS3 . "Methionine Core Mutant Of T4 Lysozyme" . . . . . 98.78 162 97.53 98.77 1.46e-112 . . . . 915 1 146 no PDB 1KW5 . "Methionine Core Mutant Of T4 Lysozyme" . . . . . 98.78 162 96.91 98.77 2.07e-112 . . . . 915 1 147 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 99.39 99.39 8.93e-116 . . . . 915 1 148 no PDB 1L01 . "Structural Studies Of Mutants Of The Lysozyme Of Bacteriophage T4. The Temperature-Sensitive Mutant Protein Thr157 (Right Arrow" . . . . . 100.00 164 98.78 98.78 2.84e-115 . . . . 915 1 149 no PDB 1L02 . "Contributions Of Hydrogen Bonds Of Thr 157 To The Thermodynamic Stability Of Phage T4 Lysozyme" . . . . . 100.00 164 99.39 99.39 4.06e-116 . . . . 915 1 150 no PDB 1L03 . "Contributions Of Hydrogen Bonds Of Thr 157 To The Thermodynamic Stability Of Phage T4 Lysozyme" . . . . . 100.00 164 99.39 99.39 5.70e-116 . . . . 915 1 151 no PDB 1L04 . "Contributions Of Hydrogen Bonds Of Thr 157 To The Thermodynamic Stability Of Phage T4 Lysozyme" . . . . . 100.00 164 99.39 99.39 7.58e-116 . . . . 915 1 152 no PDB 1L05 . "Contributions Of Hydrogen Bonds Of Thr 157 To The Thermodynamic Stability Of Phage T4 Lysozyme" . . . . . 100.00 164 99.39 99.39 7.58e-116 . . . . 915 1 153 no PDB 1L06 . "Contributions Of Hydrogen Bonds Of Thr 157 To The Thermodynamic Stability Of Phage T4 Lysozyme" . . . . . 100.00 164 99.39 99.39 6.16e-116 . . . . 915 1 154 no PDB 1L07 . "Contributions Of Hydrogen Bonds Of Thr 157 To The Thermodynamic Stability Of Phage T4 Lysozyme" . . . . . 100.00 164 99.39 99.39 1.03e-115 . . . . 915 1 155 no PDB 1L08 . "Contributions Of Hydrogen Bonds Of Thr 157 To The Thermodynamic Stability Of Phage T4 Lysozyme" . . . . . 100.00 164 99.39 99.39 9.85e-116 . . . . 915 1 156 no PDB 1L09 . "Contributions Of Hydrogen Bonds Of Thr 157 To The Thermodynamic Stability Of Phage T4 Lysozyme" . . . . . 100.00 164 99.39 99.39 5.46e-116 . . . . 915 1 157 no PDB 1L10 . "Structural Studies Of Mutants Of The Lysozyme Of Bacteriophage T4. The Temperature-Sensitive Mutant Protein Thr157 (Right Arrow" . . . . . 100.00 164 99.39 99.39 4.34e-116 . . . . 915 1 158 no PDB 1L11 . "Contributions Of Hydrogen Bonds Of Thr 157 To The Thermodynamic Stability Of Phage T4 Lysozyme" . . . . . 100.00 164 99.39 99.39 5.64e-116 . . . . 915 1 159 no PDB 1L12 . "Contributions Of Hydrogen Bonds Of Thr 157 To The Thermodynamic Stability Of Phage T4 Lysozyme" . . . . . 100.00 164 99.39 99.39 5.00e-116 . . . . 915 1 160 no PDB 1L13 . "Contributions Of Hydrogen Bonds Of Thr 157 To The Thermodynamic Stability Of Phage T4 Lysozyme" . . . . . 100.00 164 99.39 99.39 1.04e-115 . . . . 915 1 161 no PDB 1L14 . "Contributions Of Hydrogen Bonds Of Thr 157 To The Thermodynamic Stability Of Phage T4 Lysozyme" . . . . . 100.00 164 99.39 100.00 1.52e-116 . . . . 915 1 162 no PDB 1L15 . "Contributions Of Hydrogen Bonds Of Thr 157 To The Thermodynamic Stability Of Phage T4 Lysozyme" . . . . . 100.00 164 99.39 99.39 3.93e-116 . . . . 915 1 163 no PDB 1L16 . "Structural Analysis Of The Temperature-Sensitive Mutant Of Bacteriophage T4 Lysozyme, Glycine 156 (Right Arrow) Aspartic Acid" . . . . . 100.00 164 99.39 99.39 9.43e-116 . . . . 915 1 164 no PDB 1L17 . "Hydrophobic Stabilization In T4 Lysozyme Determined Directly By Multiple Substitutions Of Ile 3" . . . . . 100.00 164 99.39 100.00 1.04e-116 . . . . 915 1 165 no PDB 1L18 . "Hydrophobic Stabilization In T4 Lysozyme Determined Directly By Multiple Substitutions Of Ile 3" . . . . . 100.00 164 99.39 99.39 6.16e-116 . . . . 915 1 166 no PDB 1L19 . "Enhanced Protein Thermostability From Designed Mutations That Interact With Alpha-helix Dipoles" . . . . . 100.00 164 99.39 99.39 5.00e-116 . . . . 915 1 167 no PDB 1L20 . "Enhanced Protein Thermostability From Designed Mutations That Interact With Alpha-helix Dipoles" . . . . . 100.00 164 99.39 100.00 4.15e-116 . . . . 915 1 168 no PDB 1L21 . "Contributions Of Left-Handed Helical Residues To The Structure And Stability Of Bacteriophage T4 Lysozyme" . . . . . 100.00 164 99.39 99.39 6.79e-116 . . . . 915 1 169 no PDB 1L22 . "Contributions Of Left-Handed Helical Residues To The Structure And Stability Of Bacteriophage T4 Lysozyme" . . . . . 100.00 164 99.39 99.39 9.53e-116 . . . . 915 1 170 no PDB 1L23 . "Enhanced Protein Thermostability From Site-Directed Mutations That Decrease The Entropy Of Unfolding" . . . . . 100.00 164 99.39 99.39 4.69e-116 . . . . 915 1 171 no PDB 1L24 . "Enhanced Protein Thermostability From Site-directed Mutations That Decrease The Entropy Of Unfolding" . . . . . 100.00 164 99.39 99.39 4.89e-116 . . . . 915 1 172 no PDB 1L25 . "Replacements Of Pro86 In Phage T4 Lysozyme Extend An Alpha-Helix But Do Not Alter Protein Stability" . . . . . 100.00 164 99.39 99.39 8.55e-116 . . . . 915 1 173 no PDB 1L26 . "Replacements Of Pro86 In Phage T4 Lysozyme Extend An Alpha-helix But Do Not Alter Protein Stability" . . . . . 100.00 164 99.39 99.39 3.24e-115 . . . . 915 1 174 no PDB 1L27 . "Replacements Of Pro86 In Phage T4 Lysozyme Extend An Alpha-Helix But Do Not Alter Protein Stability" . . . . . 100.00 164 99.39 99.39 1.78e-115 . . . . 915 1 175 no PDB 1L28 . "Replacements Of Pro86 In Phage T4 Lysozyme Extend An Alpha-Helix But Do Not Alter Protein Stability" . . . . . 100.00 164 99.39 99.39 1.98e-115 . . . . 915 1 176 no PDB 1L29 . "Replacements Of Pro86 In Phage T4 Lysozyme Extend An Alpha-Helix But Do Not Alter Protein Stability" . . . . . 100.00 164 99.39 99.39 1.10e-115 . . . . 915 1 177 no PDB 1L30 . "Replacements Of Pro86 In Phage T4 Lysozyme Extend An Alpha-Helix But Do Not Alter Protein Stability" . . . . . 100.00 164 99.39 99.39 2.64e-115 . . . . 915 1 178 no PDB 1L31 . "Replacements Of Pro86 In Phage T4 Lysozyme Extend An Alpha-Helix But Do Not Alter Protein Stability" . . . . . 100.00 164 99.39 99.39 1.86e-115 . . . . 915 1 179 no PDB 1L32 . "Replacements Of Pro86 In Phage T4 Lysozyme Extend An Alpha-Helix But Do Not Alter Protein Stability" . . . . . 100.00 164 99.39 99.39 7.58e-116 . . . . 915 1 180 no PDB 1L33 . "Contributions Of Left-Handed Helical Residues To The Structure And Stability Of Bacteriophage T4 Lysozyme" . . . . . 100.00 164 99.39 99.39 2.93e-116 . . . . 915 1 181 no PDB 1L34 . "High-Resolution Structure Of The Temperature-Sensitive Mutant Of Phage Lysozyme, Arg 96 (Right Arrow) His" . . . . . 100.00 164 99.39 99.39 4.48e-116 . . . . 915 1 182 no PDB 1L35 . "Structure Of A Thermostable Disulfide-Bridge Mutant Of Phage T4 Lysozyme Shows That An Engineered Crosslink In A Flexible Regio" . . . . . 99.39 164 98.16 98.16 2.21e-112 . . . . 915 1 183 no PDB 1L36 . "Toward A Simplification Of The Protein Folding Problem: A Stabilizing Polyalanine Alpha-Helix Engineered In T4 Lysozyme" . . . . . 100.00 164 98.17 98.17 2.62e-114 . . . . 915 1 184 no PDB 1L37 . "Contributions Of Engineered Surface Salt Bridges To The Stability Of T4 Lysozyme Determined By Directed Mutagenesis" . . . . . 100.00 164 99.39 99.39 6.16e-116 . . . . 915 1 185 no PDB 1L38 . "Contributions Of Engineered Surface Salt Bridges To The Stability Of T4 Lysozyme Determined By Directed Mutagenesis" . . . . . 100.00 164 99.39 100.00 3.23e-116 . . . . 915 1 186 no PDB 1L39 . "Contributions Of Engineered Surface Salt Bridges To The Stability Of T4 Lysozyme Determined By Directed Mutagenesis" . . . . . 100.00 164 98.17 98.17 1.12e-113 . . . . 915 1 187 no PDB 1L40 . "Contributions Of Engineered Surface Salt Bridges To The Stability Of T4 Lysozyme Determined By Directed Mutagenesis" . . . . . 100.00 164 98.17 98.17 1.12e-113 . . . . 915 1 188 no PDB 1L41 . "Contributions Of Engineered Surface Salt Bridges To The Stability Of T4 Lysozyme Determined By Directed Mutagenesis" . . . . . 100.00 164 97.56 97.56 8.74e-113 . . . . 915 1 189 no PDB 1L42 . "Cumulative Site-Directed Charge-Change Replacements In Bacteriophage T4 Lysozyme Suggest That Long-Range Electrostatic Interact" . . . . . 100.00 164 99.39 100.00 3.20e-116 . . . . 915 1 190 no PDB 1L43 . "Cumulative Site-Directed Charge-Change Replacements In Bacteriophage T4 Lysozyme Suggest That Long-Range Electrostatic Interact" . . . . . 100.00 164 99.39 100.00 3.20e-116 . . . . 915 1 191 no PDB 1L44 . "Cumulative Site-Directed Charge-Change Replacements In Bacteriophage T4 Lysozyme Suggest That Long-Range Electrostatic Interact" . . . . . 100.00 164 99.39 99.39 5.17e-116 . . . . 915 1 192 no PDB 1L45 . "Cumulative Site-Directed Charge-Change Replacements In Bacteriophage T4 Lysozyme Suggest That Long-Range Electrostatic Interact" . . . . . 100.00 164 99.39 100.00 3.20e-116 . . . . 915 1 193 no PDB 1L46 . "Cumulative Site-directed Charge-change Replacements In Bacteriophage T4 Lysozyme Suggest That Long-range Electrostatic Interact" . . . . . 100.00 164 99.39 100.00 3.20e-116 . . . . 915 1 194 no PDB 1L47 . "Cumulative Site-Directed Charge-Change Replacements In Bacteriophage T4 Lysozyme Suggest That Long-Range Electrostatic Interact" . . . . . 100.00 164 99.39 99.39 5.17e-116 . . . . 915 1 195 no PDB 1L48 . "Structural And Thermodynamic Analysis Of The Packing Of Two Alpha- Helices In Bacteriophage T4 Lysozyme" . . . . . 100.00 164 99.39 99.39 3.06e-116 . . . . 915 1 196 no PDB 1L49 . "Structural And Thermodynamic Analysis Of The Packing Of Two Alpha- Helices In Bacteriophage T4 Lysozyme" . . . . . 100.00 164 98.78 99.39 8.74e-116 . . . . 915 1 197 no PDB 1L50 . "Structural And Thermodynamic Analysis Of The Packing Of Two Alpha- Helices In Bacteriophage T4 Lysozyme" . . . . . 100.00 164 98.17 98.78 6.46e-115 . . . . 915 1 198 no PDB 1L51 . "Structural And Thermodynamic Analysis Of The Packing Of Two Alpha- Helices In Bacteriophage T4 Lysozyme" . . . . . 100.00 164 98.17 99.39 1.27e-115 . . . . 915 1 199 no PDB 1L52 . "Structural And Thermodynamic Analysis Of The Packing Of Two Alpha- Helices In Bacteriophage T4 Lysozyme" . . . . . 100.00 164 99.39 100.00 1.52e-116 . . . . 915 1 200 no PDB 1L53 . "Structural And Thermodynamic Analysis Of The Packing Of Two Alpha- Helices In Bacteriophage T4 Lysozyme" . . . . . 100.00 164 99.39 99.39 4.74e-116 . . . . 915 1 201 no PDB 1L54 . "The Structural And Thermodynamic Consequences Of Burying A Charged Residue Within The Hydrophobic Core Of T4 Lysozyme" . . . . . 100.00 164 98.17 98.17 1.77e-113 . . . . 915 1 202 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 98.17 98.78 7.47e-114 . . . . 915 1 203 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 99.39 99.39 6.94e-116 . . . . 915 1 204 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 99.39 100.00 4.15e-116 . . . . 915 1 205 no PDB 1L58 . "Analysis Of The Interaction Between Charged Side Chains And The Alpha-Helix Dipole Using Designed Thermostable Mutants Of Phage" . . . . . 100.00 164 99.39 99.39 8.55e-116 . . . . 915 1 206 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 98.17 98.17 1.14e-113 . . . . 915 1 207 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 99.39 99.39 4.69e-116 . . . . 915 1 208 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 98.17 98.78 7.81e-114 . . . . 915 1 209 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 98.17 98.17 1.61e-113 . . . . 915 1 210 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 98.78 98.78 1.45e-114 . . . . 915 1 211 no PDB 1L65 . "Tolerance Of T4 Lysozyme To Multiple Xaa (Right Arrow) Ala Substitutions: A Polyalanine Alpha-Helix Containing Ten Consecutive " . . . . . 100.00 164 98.17 98.17 1.71e-113 . . . . 915 1 212 no PDB 1L66 . "Tolerance Of T4 Lysozyme To Multiple Xaa (Right Arrow) Ala Substitutions: A Polyalanine Alpha-Helix Containing Ten Consecutive " . . . . . 100.00 164 98.17 98.17 8.61e-114 . . . . 915 1 213 no PDB 1L67 . "Tolerance Of T4 Lysozyme To Multiple Xaa (Right Arrow) Ala Substitutions: A Polyalanine Alpha-Helix Containing Ten Consecutive " . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 214 no PDB 1L68 . "Tolerance Of T4 Lysozyme To Multiple Xaa (Right Arrow) Ala Substitutions: A Polyalanine Alpha-Helix Containing Ten Consecutive " . . . . . 100.00 164 98.17 98.78 4.33e-114 . . . . 915 1 215 no PDB 1L69 . "Multiple Stabilizing Alanine Replacements Within Alpha- Helix 126-134 Of T4 Lysozyme Have Independent, Additive Effects On Both" . . . . . 100.00 164 99.39 99.39 4.20e-116 . . . . 915 1 216 no PDB 1L70 . "Multiple Stabilizing Alanine Replacements Within Alpha- Helix 126-134 Of T4 Lysozyme Have Independent, Additive Effects On Both" . . . . . 100.00 164 98.78 98.78 2.97e-115 . . . . 915 1 217 no PDB 1L71 . "Multiple Stabilizing Alanine Replacements Within Alpha- Helix 126-134 Of T4 Lysozyme Have Independent, Additive Effects On Both" . . . . . 100.00 164 98.78 98.78 2.21e-115 . . . . 915 1 218 no PDB 1L72 . "Multiple Stabilizing Alanine Replacements Within Alpha- Helix 126-134 Of T4 Lysozyme Have Independent, Additive Effects On Both" . . . . . 100.00 164 98.78 98.78 9.26e-115 . . . . 915 1 219 no PDB 1L73 . "Multiple Stabilizing Alanine Replacements Within Alpha- Helix 126-134 Of T4 Lysozyme Have Independent, Additive Effects On Both" . . . . . 100.00 164 97.56 97.56 2.63e-113 . . . . 915 1 220 no PDB 1L74 . "Multiple Stabilizing Alanine Replacements Within Alpha- Helix 126-134 Of T4 Lysozyme Have Independent, Additive Effects On Both" . . . . . 100.00 164 97.56 97.56 1.47e-113 . . . . 915 1 221 no PDB 1L75 . "Multiple Stabilizing Alanine Replacements Within Alpha- Helix 126-134 Of T4 Lysozyme Have Independent, Additive Effects On Both" . . . . . 100.00 164 96.95 96.95 1.19e-112 . . . . 915 1 222 no PDB 1L76 . "Tolerance Of T4 Lysozyme To Proline Substitutions Within The Long Interdomain Alpha-Helix Illustrates The Adaptability Of Prote" . . . . . 100.00 164 98.17 98.17 1.75e-113 . . . . 915 1 223 no PDB 1L77 . "Design And Structural Analysis Of Alternative Hydrophobic Core Packing Arrangements In Bacteriophage T4 Lysozyme" . . . . . 100.00 164 98.17 98.78 5.44e-114 . . . . 915 1 224 no PDB 1L79 . "Design And Structural Analysis Of Alternative Hydrophobic Core Packing Arrangements In Bacteriophage T4 Lysozyme" . . . . . 100.00 164 97.56 98.17 9.71e-114 . . . . 915 1 225 no PDB 1L80 . "Design And Structural Analysis Of Alternative Hydrophobic Core Packing Arrangements In Bacteriophage T4 Lysozyme" . . . . . 100.00 164 96.95 98.17 3.65e-113 . . . . 915 1 226 no PDB 1L81 . "Design And Structural Analysis Of Alternative Hydrophobic Core Packing Arrangements In Bacteriophage T4 Lysozyme" . . . . . 100.00 164 96.95 97.56 1.65e-112 . . . . 915 1 227 no PDB 1L83 . "A Cavity-Containing Mutant Of T4 Lysozyme Is Stabilized By Buried Benzene" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 228 no PDB 1L84 . "A Cavity-Containing Mutant Of T4 Lysozyme Is Stabilized By Buried Benzene" . . . . . 100.00 164 97.56 97.56 1.40e-112 . . . . 915 1 229 no PDB 1L85 . "Similar Hydrophobic Replacements Of Leu 99 And Phe 153 Within The Core Of T4 Lysozyme Have Different Structural And Thermodynam" . . . . . 100.00 164 98.17 98.17 2.28e-113 . . . . 915 1 230 no PDB 1L86 . "Similar Hydrophobic Replacements Of Leu 99 And Phe 153 Within The Core Of T4 Lysozyme Have Different Structural And Thermodynam" . . . . . 100.00 164 98.17 98.17 1.21e-113 . . . . 915 1 231 no PDB 1L87 . "Similar Hydrophobic Replacements Of Leu 99 And Phe 153 Within The Core Of T4 Lysozyme Have Different Structural And Thermodynam" . . . . . 100.00 164 98.17 98.17 1.07e-113 . . . . 915 1 232 no PDB 1L88 . "Similar Hydrophobic Replacements Of Leu 99 And Phe 153 Within The Core Of T4 Lysozyme Have Different Structural And Thermodynam" . . . . . 100.00 164 98.17 98.17 1.18e-113 . . . . 915 1 233 no PDB 1L89 . "Similar Hydrophobic Replacements Of Leu 99 And Phe 153 Within The Core Of T4 Lysozyme Have Different Structural And Thermodynam" . . . . . 100.00 164 97.56 97.56 1.40e-112 . . . . 915 1 234 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 98.17 98.17 7.64e-114 . . . . 915 1 235 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 98.17 98.17 5.88e-114 . . . . 915 1 236 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 98.17 98.78 2.89e-114 . . . . 915 1 237 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 98.17 98.78 2.40e-114 . . . . 915 1 238 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 98.17 98.78 3.51e-114 . . . . 915 1 239 no PDB 1L95 . "Similar Hydrophobic Replacements Of Leu 99 And Phe 153 Within The Core Of T4 Lysozyme Have Different Structural And Thermodynam" . . . . . 100.00 164 98.17 98.17 1.54e-113 . . . . 915 1 240 no PDB 1L96 . "Structure Of A Hinge-bending Bacteriophage T4 Lysozyme Mutant, Ile3-> Pro" . . . . . 100.00 164 99.39 99.39 7.66e-116 . . . . 915 1 241 no PDB 1L97 . "Structure Of A Hinge-Bending Bacteriophage T4 Lysozyme Mutant, Ile3-> Pro" . . . . . 100.00 164 99.39 99.39 7.66e-116 . . . . 915 1 242 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 99.39 100.00 3.23e-116 . . . . 915 1 243 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 99.39 99.39 1.58e-115 . . . . 915 1 244 no PDB 1LGU . "T4 Lysozyme Mutant L99aM102Q" . . . . . 100.00 164 98.78 98.78 3.86e-115 . . . . 915 1 245 no PDB 1LGW . "T4 Lysozyme Mutant L99aM102Q BOUND BY 2-Fluoroaniline" . . . . . 100.00 164 98.78 98.78 3.86e-115 . . . . 915 1 246 no PDB 1LGX . "T4 Lysozyme Mutant L99aM102Q BOUND BY 3,5-Difluoroaniline" . . . . . 100.00 164 98.78 98.78 3.86e-115 . . . . 915 1 247 no PDB 1LI2 . "T4 Lysozyme Mutant L99aM102Q BOUND BY PHENOL" . . . . . 100.00 164 98.78 98.78 3.86e-115 . . . . 915 1 248 no PDB 1LI3 . "T4 Lysozyme Mutant L99aM102Q BOUND BY 3-Chlorophenol" . . . . . 100.00 164 98.78 98.78 3.86e-115 . . . . 915 1 249 no PDB 1LI6 . "T4 Lysozyme Mutant L99aM102Q BOUND BY 5-Methylpyrrole" . . . . . 100.00 164 98.78 98.78 3.86e-115 . . . . 915 1 250 no PDB 1LLH . "Are Carboxy Terminii Of Helices Coded By The Local Sequence Or By Tertiary Structure Contacts" . . . . . 100.00 164 98.17 98.17 9.10e-114 . . . . 915 1 251 no PDB 1LW9 . "Multiple Methionine Substitutions Are Tolerated In T4 Lysozyme And Have Coupled Effects On Folding And Stability" . . . . . 100.00 164 98.78 98.78 1.45e-114 . . . . 915 1 252 no PDB 1LYD . "Crystal Structure Of T4-Lysozyme Generated From Synthetic Coding Dna Expressed In Escherichia Coli" . . . . . 100.00 164 100.00 100.00 8.06e-117 . . . . 915 1 253 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 98.17 98.17 7.07e-114 . . . . 915 1 254 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 98.17 98.78 3.96e-114 . . . . 915 1 255 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 98.17 98.17 1.14e-113 . . . . 915 1 256 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 98.17 98.17 2.00e-113 . . . . 915 1 257 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 98.17 98.17 1.61e-113 . . . . 915 1 258 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 98.17 98.17 7.81e-114 . . . . 915 1 259 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 98.17 98.17 7.64e-114 . . . . 915 1 260 no PDB 1OV5 . "T4 Lysozyme Cavity Mutant L99aM102Q BOUND WITH 2- Allylphenol" . . . . . 100.00 164 98.78 98.78 3.86e-115 . . . . 915 1 261 no PDB 1OV7 . "T4 Lysozyme Cavity Mutant L99aM102Q BOUND WITH 2-Allyl-6- Methyl-Phenol" . . . . . 100.00 164 98.78 98.78 3.86e-115 . . . . 915 1 262 no PDB 1OVH . "T4 Lysozyme Cavity Mutant L99aM102Q BOUND WITH 2-Chloro-6- Methyl-Aniline" . . . . . 100.00 164 98.78 98.78 3.86e-115 . . . . 915 1 263 no PDB 1OVJ . "T4 Lysozyme Cavity Mutant L99a/m102q Bound With 3-fluoro-2- Methyl_aniline" . . . . . 100.00 164 98.78 98.78 3.86e-115 . . . . 915 1 264 no PDB 1OVK . "T4 Lysozyme Cavity Mutant L99aM102Q BOUND WITH N-Allyl- Aniline" . . . . . 100.00 164 98.78 98.78 3.86e-115 . . . . 915 1 265 no PDB 1OWY . "T4 Lysozyme Cavity Mutant L99a/m102q Bound With 2-propyl- Aniline" . . . . . 100.00 164 98.78 98.78 3.86e-115 . . . . 915 1 266 no PDB 1OWZ . "T4 Lysozyme Cavity Mutant L99aM102Q BOUND WITH 4- Fluorophenethyl Alcohol" . . . . . 100.00 164 98.78 98.78 3.86e-115 . . . . 915 1 267 no PDB 1P2L . "T4 Lysozyme Core Repacking Mutant V87iTA" . . . . . 100.00 164 98.17 98.78 2.35e-114 . . . . 915 1 268 no PDB 1P2R . "T4 Lysozyme Core Repacking Mutant I78vTA" . . . . . 100.00 164 98.17 98.78 2.10e-114 . . . . 915 1 269 no PDB 1P36 . "T4 Lyoszyme Core Repacking Mutant I100vTA" . . . . . 100.00 164 98.17 98.78 2.10e-114 . . . . 915 1 270 no PDB 1P46 . "T4 Lysozyme Core Repacking Mutant M106iTA" . . . . . 100.00 164 98.17 98.78 6.85e-114 . . . . 915 1 271 no PDB 1P56 . "Duplication-Extension Of Helix A Of T4 Lysozyme" . . . . . 99.39 176 98.16 98.77 5.87e-113 . . . . 915 1 272 no PDB 1P5C . "Circular Permutation Of Helix A In T4 Lysozyme" . . . . . 92.07 167 98.68 98.68 3.88e-104 . . . . 915 1 273 no PDB 1P64 . "T4 Lysozyme Core Repacking Mutant L133fTA" . . . . . 100.00 164 98.17 98.17 5.88e-114 . . . . 915 1 274 no PDB 1P6Y . "T4 Lysozyme Core Repacking Mutant M120y/ta" . . . . . 100.00 164 98.17 98.17 1.83e-113 . . . . 915 1 275 no PDB 1P7S . "T4 Lysozyme Core Repacking Mutant V103iTA" . . . . . 100.00 164 98.17 98.78 2.35e-114 . . . . 915 1 276 no PDB 1PQM . "T4 Lysozyme Core Repacking Mutant V149iT152VTA" . . . . . 100.00 164 97.56 98.17 1.12e-113 . . . . 915 1 277 no PDB 1PQO . "T4 Lysozyme Core Repacking Mutant L118iTA" . . . . . 100.00 164 98.17 98.78 2.89e-114 . . . . 915 1 278 no PDB 1QS5 . "The Introduction Of Strain And Its Effects On The Structure And Stability Of T4 Lysozyme" . . . . . 98.78 162 98.15 98.15 3.98e-112 . . . . 915 1 279 no PDB 1QS9 . "The Introduction Of Strain And Its Effects On The Structure And Stability Of T4 Lysozyme" . . . . . 98.78 162 98.15 98.15 1.94e-112 . . . . 915 1 280 no PDB 1QSB . "The Introduction Of Strain And Its Effects On The Structure And Stability Of T4 Lysozyme" . . . . . 98.78 162 98.15 98.15 4.44e-112 . . . . 915 1 281 no PDB 1QSQ . "Cavity Creating Mutation" . . . . . 100.00 164 98.17 98.17 1.29e-113 . . . . 915 1 282 no PDB 1QT3 . "T26d Mutant Of T4 Lysozyme" . . . . . 100.00 164 98.17 98.17 1.61e-113 . . . . 915 1 283 no PDB 1QT4 . "T26q Mutant Of T4 Lysozyme" . . . . . 100.00 164 98.17 98.17 1.18e-113 . . . . 915 1 284 no PDB 1QT5 . "D20e Mutant Structure Of T4 Lysozyme" . . . . . 100.00 164 98.17 98.78 6.77e-114 . . . . 915 1 285 no PDB 1QT6 . "E11h Mutant Of T4 Lysozyme" . . . . . 100.00 164 98.17 98.17 7.00e-114 . . . . 915 1 286 no PDB 1QT7 . "E11n Mutant Of T4 Lysozyme" . . . . . 100.00 164 98.17 98.17 1.24e-113 . . . . 915 1 287 no PDB 1QT8 . "T26h Mutant Of T4 Lysozyme" . . . . . 100.00 164 98.17 98.17 1.35e-113 . . . . 915 1 288 no PDB 1QTB . "The Introduction Of Strain And Its Effects On The Structure And Stability Of T4 Lysozyme" . . . . . 98.78 162 98.15 98.15 1.94e-112 . . . . 915 1 289 no PDB 1QTC . "The Introduction Of Strain And Its Effects On The Structure And Stability Of T4 Lysozyme" . . . . . 98.78 162 98.15 98.15 5.71e-112 . . . . 915 1 290 no PDB 1QTD . "The Introduction Of Strain And Its Effects On The Structure And Stability Of T4 Lysozyme" . . . . . 98.78 162 98.15 98.15 9.04e-112 . . . . 915 1 291 no PDB 1QTH . "The Introduction Of Strain And Its Effects On The Structure And Stability Of T4 Lysozyme" . . . . . 100.00 164 98.17 98.17 8.07e-114 . . . . 915 1 292 no PDB 1QTV . "T26e Apo Structure Of T4 Lysozyme" . . . . . 100.00 164 98.17 98.17 1.33e-113 . . . . 915 1 293 no PDB 1QTZ . "D20c Mutant Of T4 Lysozyme" . . . . . 100.00 164 98.17 98.17 9.86e-113 . . . . 915 1 294 no PDB 1QUD . "L99g Mutant Of T4 Lysozyme" . . . . . 98.78 162 98.15 98.15 8.56e-112 . . . . 915 1 295 no PDB 1QUG . "E108v Mutant Of T4 Lysozyme" . . . . . 98.78 162 98.15 98.15 6.51e-112 . . . . 915 1 296 no PDB 1QUH . "L99gE108V MUTANT OF T4 LYSOZYME" . . . . . 98.78 162 97.53 97.53 1.14e-110 . . . . 915 1 297 no PDB 1QUO . "L99aE108V MUTANT OF T4 LYSOZYME" . . . . . 98.78 162 97.53 97.53 4.27e-111 . . . . 915 1 298 no PDB 1SSY . "Crystal Structure Of Phage T4 Lysozyme Mutant G28aI29AG30AC54TC97A" . . . . . 100.00 164 96.95 96.95 2.58e-112 . . . . 915 1 299 no PDB 1SWY . "Use Of A Halide Binding Site To Bypass The 1000-Atom Limit To Ab Initio Structure Determination" . . . . . 100.00 164 98.78 98.78 5.66e-115 . . . . 915 1 300 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 98.78 98.78 5.66e-115 . . . . 915 1 301 no PDB 1SX2 . "Use Of A Halide Binding Site To Bypass The 1000-Atom Limit To Structure Determination By Direct Methods" . . . . . 100.00 164 98.78 98.78 5.66e-115 . . . . 915 1 302 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 98.78 98.78 5.66e-115 . . . . 915 1 303 no PDB 1T6H . "Crystal Structure T4 Lysozyme Incorporating An Unnatural Amino Acid P-Iodo-L-Phenylalanine At Position 153" . . . . . 100.00 164 99.39 99.39 1.16e-115 . . . . 915 1 304 no PDB 1T8G . "Crystal Structure Of Phage T4 Lysozyme Mutant L32aL33AT34AC54TC97AE108V" . . . . . 100.00 164 96.95 96.95 6.97e-112 . . . . 915 1 305 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 98.17 98.17 2.11e-113 . . . . 915 1 306 no PDB 1XEP . "Catechol In Complex With T4 Lysozyme L99aM102Q" . . . . . 100.00 164 98.78 98.78 3.86e-115 . . . . 915 1 307 no PDB 1ZUR . "Crystal Structure Of Spin Labeled T4 Lysozyme (V131r1f)" . . . . . 100.00 164 98.17 98.17 2.41e-113 . . . . 915 1 308 no PDB 1ZWN . "Crystal Structure Of Spin Labeled T4 Lysozyme (V131r1b)" . . . . . 100.00 164 98.17 98.17 2.41e-113 . . . . 915 1 309 no PDB 1ZYT . "Crystal Structure Of Spin Labeled T4 Lysozyme (A82r1)" . . . . . 100.00 164 98.17 98.17 1.96e-113 . . . . 915 1 310 no PDB 200L . 'Thermodynamic And Structural Compensation In "size-Switch" Core-Repacking Variants Of T4 Lysozyme' . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 311 no PDB 201L . "How Amino-Acid Insertions Are Allowed In An Alpha-Helix Of T4 Lysozyme" . . . . . 101.22 166 97.59 97.59 1.99e-112 . . . . 915 1 312 no PDB 205L . "How Amino-Acid Insertions Are Allowed In An Alpha-Helix Of T4 Lysozyme" . . . . . 101.83 167 97.01 97.01 1.33e-112 . . . . 915 1 313 no PDB 206L . "Phage T4 Lysozyme" . . . . . 100.00 164 98.17 98.78 3.36e-114 . . . . 915 1 314 no PDB 209L . "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" . . . . . 101.83 167 97.01 97.01 1.33e-112 . . . . 915 1 315 no PDB 210L . "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" . . . . . 100.00 163 98.17 98.17 4.30e-112 . . . . 915 1 316 no PDB 211L . "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" . . . . . 100.61 165 98.18 98.18 9.98e-113 . . . . 915 1 317 no PDB 212L . "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" . . . . . 100.00 168 98.78 98.78 9.42e-115 . . . . 915 1 318 no PDB 213L . "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" . . . . . 100.61 165 98.18 98.18 9.98e-113 . . . . 915 1 319 no PDB 214L . "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" . . . . . 100.61 165 98.18 98.18 9.98e-113 . . . . 915 1 320 no PDB 215L . "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" . . . . . 100.61 165 98.18 98.18 9.98e-113 . . . . 915 1 321 no PDB 216L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 98.17 98.17 4.79e-113 . . . . 915 1 322 no PDB 217L . "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" . . . . . 100.00 164 98.17 98.17 8.43e-114 . . . . 915 1 323 no PDB 218L . "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" . . . . . 100.61 165 98.18 98.18 9.98e-113 . . . . 915 1 324 no PDB 219L . "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" . . . . . 100.00 164 98.78 98.78 1.45e-114 . . . . 915 1 325 no PDB 220L . "Generating Ligand Binding Sites In T4 Lysozyme Using Deficiency-Creating Substitutions" . . . . . 100.00 164 98.17 98.17 1.29e-113 . . . . 915 1 326 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 98.17 98.78 3.36e-114 . . . . 915 1 327 no PDB 222L . "Generating Ligand Binding Sites In T4 Lysozyme Using Deficiency-Creating Substitutions" . . . . . 100.00 164 98.17 98.17 1.29e-113 . . . . 915 1 328 no PDB 223L . "Generating Ligand Binding Sites In T4 Lysozyme Using Deficiency-Creating Substitutions" . . . . . 100.00 164 99.39 99.39 1.27e-115 . . . . 915 1 329 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 98.17 98.78 3.36e-114 . . . . 915 1 330 no PDB 225L . "Generating Ligand Binding Sites In T4 Lysozyme Using Deficiency-Creating Substitutions" . . . . . 100.00 164 99.39 99.39 1.27e-115 . . . . 915 1 331 no PDB 226L . "Generating Ligand Binding Sites In T4 Lysozyme Using Deficiency-Creating Substitutions" . . . . . 100.00 164 99.39 99.39 1.27e-115 . . . . 915 1 332 no PDB 227L . "Generating Ligand Binding Sites In T4 Lysozyme Using Deficiency-Creating Substitutions" . . . . . 100.00 164 98.17 98.17 2.28e-113 . . . . 915 1 333 no PDB 228L . "Generating Ligand Binding Sites In T4 Lysozyme Using Deficiency-Creating Substitutions" . . . . . 100.00 164 98.17 98.17 2.28e-113 . . . . 915 1 334 no PDB 229L . "Generating Ligand Binding Sites In T4 Lysozyme Using Deficiency-Creating Substitutions" . . . . . 100.00 164 98.17 98.17 1.30e-113 . . . . 915 1 335 no PDB 230L . "T4 Lysozyme Mutant M6l" . . . . . 100.00 164 98.17 98.78 5.44e-114 . . . . 915 1 336 no PDB 231L . "T4 Lysozyme Mutant M106k" . . . . . 100.00 164 98.17 98.17 1.77e-113 . . . . 915 1 337 no PDB 232L . "T4 Lysozyme Mutant M120k" . . . . . 100.00 164 98.17 98.17 1.77e-113 . . . . 915 1 338 no PDB 233L . "T4 Lysozyme Mutant M120l" . . . . . 100.00 164 98.17 98.78 5.44e-114 . . . . 915 1 339 no PDB 234L . "T4 Lysozyme Mutant M106l" . . . . . 100.00 164 98.17 98.78 5.44e-114 . . . . 915 1 340 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 98.17 98.17 6.07e-114 . . . . 915 1 341 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 98.17 98.17 6.07e-114 . . . . 915 1 342 no PDB 237L . "The Response Of T4 Lysozyme To Large-To-Small Substitutions Within The Core And Its Relation To The Hydrophobic Effect" . . . . . 100.00 164 98.17 98.17 6.07e-114 . . . . 915 1 343 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 98.17 98.17 6.07e-114 . . . . 915 1 344 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 98.17 98.17 7.64e-114 . . . . 915 1 345 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 98.17 98.17 7.64e-114 . . . . 915 1 346 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 98.17 98.17 7.64e-114 . . . . 915 1 347 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 98.17 98.17 7.64e-114 . . . . 915 1 348 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 98.17 98.17 7.64e-114 . . . . 915 1 349 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 98.17 98.17 7.64e-114 . . . . 915 1 350 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 98.17 98.17 1.29e-113 . . . . 915 1 351 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 98.17 98.17 2.28e-113 . . . . 915 1 352 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 98.17 98.17 7.64e-114 . . . . 915 1 353 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 97.56 97.56 5.64e-113 . . . . 915 1 354 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 97.56 97.56 5.64e-113 . . . . 915 1 355 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 97.56 97.56 5.64e-113 . . . . 915 1 356 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 97.56 97.56 4.54e-113 . . . . 915 1 357 no PDB 252L . "Generating Ligand Binding Sites In T4 Lysozyme Using Deficiency-Creating Substitutions" . . . . . 100.00 164 97.56 97.56 1.35e-112 . . . . 915 1 358 no PDB 253L . Lysozyme . . . . . 100.00 164 98.17 98.17 1.71e-113 . . . . 915 1 359 no PDB 254L . Lysozyme . . . . . 100.00 164 98.17 98.17 8.61e-114 . . . . 915 1 360 no PDB 255L . Hydrolase . . . . . 100.00 164 98.17 98.78 7.47e-114 . . . . 915 1 361 no PDB 256L . "Bacteriophage T4 Lysozyme" . . . . . 100.00 164 99.39 100.00 3.93e-116 . . . . 915 1 362 no PDB 257L . "An Adaptable Metal-Binding Site Engineered Into T4 Lysozyme" . . . . . 100.00 164 97.56 97.56 1.14e-112 . . . . 915 1 363 no PDB 258L . "An Adaptable Metal-Binding Site Engineered Into T4 Lysozyme" . . . . . 100.00 164 97.56 97.56 1.14e-112 . . . . 915 1 364 no PDB 259L . "An Adaptable Metal-Binding Site Engineered Into T4 Lysozyme" . . . . . 100.00 164 97.56 97.56 1.14e-112 . . . . 915 1 365 no PDB 260L . "An Adaptable Metal-Binding Site Engineered Into T4 Lysozyme" . . . . . 100.00 164 97.56 97.56 1.14e-112 . . . . 915 1 366 no PDB 2A4T . "Crystal Structure Of Spin Labeled T4 Lysozyme (V131r7)" . . . . . 100.00 164 98.17 98.17 2.41e-113 . . . . 915 1 367 no PDB 2B6T . "T4 Lysozyme Mutant L99a At 200 Mpa" . . . . . 98.78 162 98.15 98.15 2.28e-112 . . . . 915 1 368 no PDB 2B6W . "T4 Lysozyme Mutant L99a At 200 Mpa" . . . . . 98.78 162 98.15 98.15 2.28e-112 . . . . 915 1 369 no PDB 2B6X . "T4 Lysozyme Mutant L99a At 200 Mpa" . . . . . 98.78 162 98.15 98.15 2.28e-112 . . . . 915 1 370 no PDB 2B6Y . "T4 Lysozyme Mutant L99a At Ambient Pressure" . . . . . 98.78 162 98.15 98.15 2.28e-112 . . . . 915 1 371 no PDB 2B6Z . "T4 Lysozyme Mutant L99a At Ambient Pressure" . . . . . 98.78 162 98.15 98.15 2.28e-112 . . . . 915 1 372 no PDB 2B70 . "T4 Lysozyme Mutant L99a At Ambient Pressure" . . . . . 98.78 162 98.15 98.15 2.28e-112 . . . . 915 1 373 no PDB 2B72 . "T4 Lysozyme Mutant L99a At 100 Mpa" . . . . . 98.78 162 98.15 98.15 2.28e-112 . . . . 915 1 374 no PDB 2B73 . "T4 Lysozyme Mutant L99a At 100 Mpa" . . . . . 98.78 162 98.15 98.15 2.28e-112 . . . . 915 1 375 no PDB 2B74 . "T4 Lysozyme Mutant L99a At 100 Mpa" . . . . . 98.78 162 98.15 98.15 2.28e-112 . . . . 915 1 376 no PDB 2B75 . "T4 Lysozyme Mutant L99a At 150 Mpa" . . . . . 98.78 162 98.15 98.15 2.28e-112 . . . . 915 1 377 no PDB 2CUU . "Crystal Structure Of Spin Labeled T4 Lysozyme (v131r1)" . . . . . 100.00 164 98.17 98.17 2.41e-113 . . . . 915 1 378 no PDB 2HUK . "Crystal Structure Of T4 Lysozyme V131c Synthetic Dimer" . . . . . 100.00 164 98.17 98.17 2.41e-113 . . . . 915 1 379 no PDB 2HUL . "Crystal Structure Of T4 Lysozyme S44c Synthetic Dimer" . . . . . 100.00 164 98.17 98.17 2.93e-113 . . . . 915 1 380 no PDB 2HUM . "Crystal Structure Of T4 Lysozyme D72c Synthetic Dimer" . . . . . 100.00 164 98.17 98.17 9.86e-113 . . . . 915 1 381 no PDB 2IGC . "Structure Of Spin Labeled T4 Lysozyme Mutant T115r1a" . . . . . 100.00 164 98.17 98.17 2.66e-113 . . . . 915 1 382 no PDB 2L78 . "Design And Structural Analysis Of Alternative Hydrophobic Core Packing Arrangements In Bacteriophage T4 Lysozyme" . . . . . 100.00 164 98.17 98.78 2.35e-114 . . . . 915 1 383 no PDB 2LC9 . "Solution Structure Of A Minor And Transiently Formed State Of A T4 Lysozyme Mutant" . . . . . 100.00 164 96.95 96.95 5.42e-112 . . . . 915 1 384 no PDB 2LCB . "Solution Structure Of A Minor And Transiently Formed State Of A T4 Lysozyme Mutant" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 385 no PDB 2LZM . "Structure Of Bacteriophage T4 Lysozyme Refined At 1.7 Angstroms Resolution" . . . . . 100.00 164 100.00 100.00 8.06e-117 . . . . 915 1 386 no PDB 2NTG . "Structure Of Spin-Labeled T4 Lysozyme Mutant T115r7" . . . . . 100.00 164 98.17 98.17 2.66e-113 . . . . 915 1 387 no PDB 2NTH . "Structure Of Spin-Labeled T4 Lysozyme Mutant L118r1" . . . . . 100.00 164 98.17 98.17 2.51e-113 . . . . 915 1 388 no PDB 2O4W . "T4 Lysozyme Circular Permutant" . . . . . 92.68 171 98.68 98.68 2.09e-104 . . . . 915 1 389 no PDB 2O79 . "T4 Lysozyme With C-Terminal Extension" . . . . . 100.00 170 98.17 98.78 1.08e-113 . . . . 915 1 390 no PDB 2O7A . "T4 Lysozyme C-Terminal Fragment" . . . . . 64.02 124 99.05 99.05 1.56e-68 . . . . 915 1 391 no PDB 2OE4 . "High Pressure Psuedo Wild Type T4 Lysozyme" . . . . . 100.00 164 98.78 98.78 1.45e-114 . . . . 915 1 392 no PDB 2OE7 . "High-Pressure T4 Lysozyme" . . . . . 100.00 164 98.78 98.78 1.45e-114 . . . . 915 1 393 no PDB 2OE9 . "High-Pressure Structure Of Pseudo-Wt T4 Lysozyme" . . . . . 100.00 164 98.78 98.78 1.45e-114 . . . . 915 1 394 no PDB 2OEA . "High-Pressure Structure Of Pseudo-Wt T4 Lysozyme" . . . . . 100.00 164 98.78 98.78 1.45e-114 . . . . 915 1 395 no PDB 2OTY . "1,2-Dichlorobenzene In Complex With T4 Lysozyme L99a" . . . . . 98.78 162 98.15 98.15 2.28e-112 . . . . 915 1 396 no PDB 2OTZ . "N-Methylaniline In Complex With T4 Lysozyme L99a" . . . . . 98.78 162 98.15 98.15 2.28e-112 . . . . 915 1 397 no PDB 2OU0 . "1-Methylpyrrole In Complex With T4 Lysozyme L99a" . . . . . 98.78 162 98.15 98.15 2.28e-112 . . . . 915 1 398 no PDB 2OU8 . "Structure Of Spin-Labeled T4 Lysozyme Mutant T115r1 At Room Temperature" . . . . . 100.00 164 98.17 98.17 2.66e-113 . . . . 915 1 399 no PDB 2OU9 . "Structure Of Spin-Labeled T4 Lysozyme Mutant T115r1R119A" . . . . . 100.00 164 97.56 97.56 2.91e-112 . . . . 915 1 400 no PDB 2Q9D . "Structure Of Spin-Labeled T4 Lysozyme Mutant A41r1" . . . . . 100.00 164 98.17 98.17 1.96e-113 . . . . 915 1 401 no PDB 2Q9E . "Structure Of Spin-Labeled T4 Lysozyme Mutant S44r1" . . . . . 100.00 164 97.56 97.56 3.11e-112 . . . . 915 1 402 no PDB 2QAR . "Structure Of The 2tel Crystallization Module Fused To T4 Lysozyme With A Helical Linker" . . . . . 98.17 163 98.14 98.14 7.54e-111 . . . . 915 1 403 no PDB 2QB0 . "Structure Of The 2tel Crystallization Module Fused To T4 Lysozyme With An Ala-Gly-Pro Linker" . . . . . 98.17 241 97.52 97.52 2.59e-108 . . . . 915 1 404 no PDB 2RAY . "Beta-chlorophenetole In Complex With T4 Lysozyme L99a" . . . . . 98.78 162 98.15 98.15 2.28e-112 . . . . 915 1 405 no PDB 2RAZ . "4-(Methylthio)nitrobenzene In Complex With T4 Lysozyme L99a" . . . . . 98.78 162 98.15 98.15 2.28e-112 . . . . 915 1 406 no PDB 2RB0 . "2,6-Difluorobenzylbromide Complex With T4 Lysozyme L99a" . . . . . 98.78 162 98.15 98.15 2.28e-112 . . . . 915 1 407 no PDB 2RB1 . "2-Ethoxyphenol In Complex With T4 Lysozyme L99a" . . . . . 98.78 162 98.15 98.15 2.28e-112 . . . . 915 1 408 no PDB 2RB2 . "3-Methylbenzylazide In Complex With T4 Lysozyme L99a" . . . . . 98.78 162 98.15 98.15 2.28e-112 . . . . 915 1 409 no PDB 2RBN . "N-Phenylglycinonitrile In Complex With T4 Lysozyme L99aM102Q" . . . . . 98.78 162 98.77 98.77 8.49e-114 . . . . 915 1 410 no PDB 2RBO . "2-Nitrothiophene In Complex With T4 Lysozyme L99aM102Q" . . . . . 98.78 162 98.77 98.77 8.49e-114 . . . . 915 1 411 no PDB 2RBP . "2-(N-Propylthio)ethanol In Complex With T4 Lysozyme L99aM102Q" . . . . . 98.78 162 98.77 98.77 8.49e-114 . . . . 915 1 412 no PDB 2RBQ . "3-Methylbenzylazide In Complex With T4 L99aM102Q" . . . . . 98.78 162 98.77 98.77 8.49e-114 . . . . 915 1 413 no PDB 2RBR . "2-Phenoxyethanol In Complex With T4 Lysozyme L99aM102Q" . . . . . 98.78 162 98.77 98.77 8.49e-114 . . . . 915 1 414 no PDB 2RBS . "(r)(+)-3-chloro-1-phenyl-1-propanol In Complex With T4 Lysozyme L99a/m102q" . . . . . 98.78 162 98.77 98.77 8.49e-114 . . . . 915 1 415 no PDB 2RH1 . "High Resolution Crystal Structure Of Human B2-Adrenergic G Protein- Coupled Receptor" . . . . . 98.78 500 98.15 98.77 1.81e-107 . . . . 915 1 416 no PDB 3C7W . "Contributions Of All 20 Amino Acids At Site 96 To The Stability And Structure Of T4 Lysozyme" . . . . . 100.00 164 99.39 100.00 1.93e-116 . . . . 915 1 417 no PDB 3C7Y . "Mutant R96a Of T4 Lysozyme In Wildtype Background At 298k" . . . . . 100.00 164 99.39 99.39 8.55e-116 . . . . 915 1 418 no PDB 3C7Z . "T4 Lysozyme Mutant D89aR96H AT ROOM TEMPERATURE" . . . . . 100.00 164 98.78 98.78 4.36e-115 . . . . 915 1 419 no PDB 3C80 . "T4 Lysozyme Mutant R96y At Room Temperature" . . . . . 100.00 164 99.39 99.39 9.64e-116 . . . . 915 1 420 no PDB 3C81 . "Mutant K85a Of T4 Lysozyme In Wildtype Background At Room Temperature" . . . . . 100.00 164 99.39 99.39 5.77e-116 . . . . 915 1 421 no PDB 3C82 . "Bacteriophage Lysozyme T4 Lysozyme Mutant K85aR96H" . . . . . 100.00 164 98.78 98.78 2.47e-115 . . . . 915 1 422 no PDB 3C83 . "Bacteriophage T4 Lysozyme Mutant D89a In Wildtype Background At Room Temperature" . . . . . 100.00 164 99.39 99.39 1.05e-115 . . . . 915 1 423 no PDB 3C8Q . "Contribution Of All 20 Amino Acids At Site 96 To The Stability And Structure Of T4 Lysozyme" . . . . . 100.00 164 99.39 99.39 1.04e-115 . . . . 915 1 424 no PDB 3C8R . "Contributions Of All 20 Amino Acids At Site 96 To Stability And Structure Of T4 Lysozyme" . . . . . 100.00 164 99.39 99.39 1.49e-115 . . . . 915 1 425 no PDB 3C8S . "Contributions Of All 20 Amino Acids At Site 96 To The Stability And Structure Of T4 Lysozyme" . . . . . 100.00 164 99.39 99.39 5.17e-116 . . . . 915 1 426 no PDB 3CDO . "Bacteriophage T4 Lysozyme Mutant R96v In Wildtype Background At Low Temperature" . . . . . 100.00 164 99.39 99.39 1.04e-115 . . . . 915 1 427 no PDB 3CDQ . "Contributions Of All 20 Amino Acids At Site 96 To The Stability And Structure Of T4 Lysozyme" . . . . . 100.00 164 99.39 99.39 4.89e-116 . . . . 915 1 428 no PDB 3CDR . "R96q Mutant Of Wildtype Phage T4 Lysozyme At 298 K" . . . . . 100.00 164 99.39 100.00 3.03e-116 . . . . 915 1 429 no PDB 3CDT . "Contributions Of All 20 Amino Acids At Site 96 To The Stability And Structure Of T4 Lysozyme" . . . . . 100.00 164 99.39 99.39 6.36e-116 . . . . 915 1 430 no PDB 3CDV . "Contributions Of All 20 Amino Acids At Site 96 To The Stability And Structure Of T4 Lysozyme" . . . . . 100.00 164 99.39 99.39 7.25e-116 . . . . 915 1 431 no PDB 3D4S . "Cholesterol Bound Form Of Human Beta2 Adrenergic Receptor." . . . . . 98.78 490 98.15 98.77 9.72e-108 . . . . 915 1 432 no PDB 3DMV . "Free Of Ligand Binding In The Hydrophobic Cavity Of T4 Lysozyme L99a Mutant" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 433 no PDB 3DMX . "Benzene Binding In The Hydrophobic Cavity Of T4 Lysozyme L99a Mutant" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 434 no PDB 3DMZ . "Hexafluorobenzene Binding In The Hydrophobic Cavity Of T4 Lysozyme L99a Mutant" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 435 no PDB 3DN0 . "Pentafluorobenzene Binding In The Hydrophobic Cavity Of T4 Lysozyme L99a Mutant" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 436 no PDB 3DN1 . "Chloropentafluorobenzene Binding In The Hydrophobic Cavity Of T4 Lysozyme L99a Mutant" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 437 no PDB 3DN2 . "Bromopentafluorobenzene Binding In The Hydrophobic Cavity Of T4 Lysozyme L99a Mutant" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 438 no PDB 3DN3 . "Iodopentafluorobenzene Binding In The Hydrophobic Cavity Of T4 Lysozyme L99a Mutant" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 439 no PDB 3DN4 . "Iodobenzene Binding In The Hydrophobic Cavity Of T4 Lysozyme L99a Mutant" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 440 no PDB 3DN6 . "1,3,5-Trifluoro-2,4,6-Trichlorobenzene Binding In The Hydrophobic Cavity Of T4 Lysozyme L99a Mutant" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 441 no PDB 3EML . "The 2.6 A Crystal Structure Of A Human A2a Adenosine Receptor Bound To Zm241385." . . . . . 99.39 488 96.93 98.77 1.23e-107 . . . . 915 1 442 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 99.39 99.39 4.48e-116 . . . . 915 1 443 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 99.39 99.39 1.05e-115 . . . . 915 1 444 no PDB 3FA0 . "Evaulaution At Atomic Resolution Of The Role Of Strain In Destabilizing The Temperature Sensitive T4 Lysozyme Mutant Arg96-->hi" . . . . . 98.78 162 100.00 100.00 2.18e-115 . . . . 915 1 445 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 98.78 98.78 4.36e-115 . . . . 915 1 446 no PDB 3FI5 . "Crystal Structure Of T4 Lysozyme Mutant R96w" . . . . . 100.00 164 99.39 99.39 2.31e-115 . . . . 915 1 447 no PDB 3G3V . "Crystal Structure Of Spin Labeled T4 Lysozyme (V131r1) At 291 K" . . . . . 100.00 164 98.17 98.17 2.41e-113 . . . . 915 1 448 no PDB 3G3W . "Crystal Structure Of Spin Labeled T4 Lysozyme (T151r1) At 291 K" . . . . . 100.00 164 98.17 98.17 2.66e-113 . . . . 915 1 449 no PDB 3G3X . "Crystal Structure Of Spin Labeled T4 Lysozyme (T151r1) At 100 K" . . . . . 100.00 164 98.17 98.17 2.66e-113 . . . . 915 1 450 no PDB 3HH3 . "New Azaborine Compounds Bind To The T4 Lysozyme L99a Cavity - 1,2-Dihydro-1,2-Azaborine" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 451 no PDB 3HH4 . "New Azaborine Compounds Bind To The T4 Lysozyme L99a Cavity - Benzene As Control" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 452 no PDB 3HH5 . "New Azaborine Compounds Bind To The T4 Lysozyme L99a Cavity - 1-Ethyl-2-Hydro-1,2-Azaborine" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 453 no PDB 3HH6 . "New Azaborine Compounds Bind To The T4 Lysozyme L99a Cavity - Ethylbenzene As Control" . . . . . 100.00 164 98.17 98.17 7.64e-114 . . . . 915 1 454 no PDB 3HT6 . "2-Methylphenol In Complex With T4 Lysozyme L99aM102Q" . . . . . 100.00 164 97.56 98.17 1.55e-113 . . . . 915 1 455 no PDB 3HT7 . "2-Ethylphenol In Complex With T4 Lysozyme L99aM102Q" . . . . . 100.00 164 97.56 98.17 1.55e-113 . . . . 915 1 456 no PDB 3HT8 . "5-chloro-2-methylphenol In Complex With T4 Lysozyme L99a/m102q" . . . . . 100.00 164 97.56 98.17 1.55e-113 . . . . 915 1 457 no PDB 3HT9 . "2-Methoxyphenol In Complex With T4 Lysozyme L99aM102Q" . . . . . 100.00 164 97.56 98.17 1.55e-113 . . . . 915 1 458 no PDB 3HTB . "2-Propylphenol In Complex With T4 Lysozyme L99aM102Q" . . . . . 100.00 164 97.56 98.17 1.55e-113 . . . . 915 1 459 no PDB 3HTD . "(Z)-Thiophene-2-Carboxaldoxime In Complex With T4 Lysozyme L99aM102Q" . . . . . 100.00 164 97.56 98.17 1.55e-113 . . . . 915 1 460 no PDB 3HTF . "4-Chloro-1h-Pyrazole In Complex With T4 Lysozyme L99aM102Q" . . . . . 100.00 164 97.56 98.17 1.55e-113 . . . . 915 1 461 no PDB 3HTG . "2-Ethoxy-3,4-Dihydro-2h-Pyran In Complex With T4 Lysozyme L99aM102Q" . . . . . 100.00 164 97.56 98.17 1.55e-113 . . . . 915 1 462 no PDB 3HU8 . "2-Ethoxyphenol In Complex With T4 Lysozyme L99aM102Q" . . . . . 100.00 164 97.56 98.17 1.55e-113 . . . . 915 1 463 no PDB 3HU9 . "Nitrosobenzene In Complex With T4 Lysozyme L99aM102Q" . . . . . 100.00 164 97.56 98.17 1.55e-113 . . . . 915 1 464 no PDB 3HUA . "4,5,6,7-Tetrahydroindole In Complex With T4 Lysozyme L99aM102Q" . . . . . 100.00 164 97.56 98.17 1.55e-113 . . . . 915 1 465 no PDB 3HUK . "Benzylacetate In Complex With T4 Lysozyme L99aM102Q" . . . . . 100.00 164 97.56 98.17 1.55e-113 . . . . 915 1 466 no PDB 3HUQ . "Thieno[3,2-B]thiophene In Complex With T4 Lysozyme L99aM102Q" . . . . . 98.78 162 97.53 98.15 3.23e-112 . . . . 915 1 467 no PDB 3HWL . "Crystal Structure Of T4 Lysozyme With The Unnatural Amino Acid P- Acetyl-L-Phenylalanine Incorporated At Position 131" . . . . . 100.00 164 96.95 96.95 4.72e-111 . . . . 915 1 468 no PDB 3K2R . "Crystal Structure Of Spin Labeled T4 Lysozyme Mutant K65v1R76V1" . . . . . 100.00 164 97.56 97.56 2.37e-111 . . . . 915 1 469 no PDB 3L2X . "Crystal Structure Of Spin Labeled T4 Lysozyme Mutant 115-119rx" . . . . . 100.00 164 97.56 97.56 1.34e-111 . . . . 915 1 470 no PDB 3L64 . "T4 Lysozyme S44e/wt*" . . . . . 100.00 164 98.17 98.17 8.43e-114 . . . . 915 1 471 no PDB 3LZM . "Structural Studies Of Mutants Of T4 Lysozyme That Alter Hydrophobic Stabilization" . . . . . 100.00 164 100.00 100.00 8.06e-117 . . . . 915 1 472 no PDB 3NY8 . "Crystal Structure Of The Human Beta2 Adrenergic Receptor In Complex With The Inverse Agonist Ici 118,551" . . . . . 98.78 490 98.15 98.77 9.72e-108 . . . . 915 1 473 no PDB 3NY9 . "Crystal Structure Of The Human Beta2 Adrenergic Receptor In Complex With A Novel Inverse Agonist" . . . . . 98.78 490 98.15 98.77 9.72e-108 . . . . 915 1 474 no PDB 3NYA . "Crystal Structure Of The Human Beta2 Adrenergic Receptor In Complex With The Neutral Antagonist Alprenolol" . . . . . 98.78 490 98.15 98.77 9.72e-108 . . . . 915 1 475 no PDB 3ODU . "The 2.5 A Structure Of The Cxcr4 Chemokine Receptor In Complex With Small Molecule Antagonist It1t" . . . . . 97.56 502 98.75 98.75 2.26e-106 . . . . 915 1 476 no PDB 3OE0 . "Crystal Structure Of The Cxcr4 Chemokine Receptor In Complex With A Cyclic Peptide Antagonist Cvx15" . . . . . 98.17 499 98.14 98.14 3.16e-106 . . . . 915 1 477 no PDB 3OE6 . "Crystal Structure Of The Cxcr4 Chemokine Receptor In Complex With A Small Molecule Antagonist It1t In I222 Spacegroup" . . . . . 97.56 508 98.75 98.75 2.86e-106 . . . . 915 1 478 no PDB 3OE8 . "Crystal Structure Of The Cxcr4 Chemokine Receptor In Complex With A Small Molecule Antagonist It1t In P1 Spacegroup" . . . . . 97.56 502 98.75 98.75 2.26e-106 . . . . 915 1 479 no PDB 3OE9 . "Crystal Structure Of The Chemokine Cxcr4 Receptor In Complex With A Small Molecule Antagonist It1t In P1 Spacegroup" . . . . . 98.17 499 98.14 98.14 3.16e-106 . . . . 915 1 480 no PDB 3P0G . "Structure Of A Nanobody-Stabilized Active State Of The Beta2 Adrenoceptor" . . . . . 98.78 501 98.15 98.77 2.37e-107 . . . . 915 1 481 no PDB 3PBL . "Structure Of The Human Dopamine D3 Receptor In Complex With Eticlopride" . . . . . 97.56 481 98.75 98.75 3.26e-107 . . . . 915 1 482 no PDB 3PDS . "Irreversible Agonist-Beta2 Adrenoceptor Complex" . . . . . 98.78 458 98.15 98.77 1.63e-108 . . . . 915 1 483 no PDB 3QAK . "Agonist Bound Structure Of The Human Adenosine A2a Receptor" . . . . . 99.39 488 96.93 98.77 1.23e-107 . . . . 915 1 484 no PDB 3RUN . "New Strategy To Analyze Structures Of Glycopeptide Antibiotic-Target Complexes" . . . . . 99.39 168 98.77 98.77 5.07e-114 . . . . 915 1 485 no PDB 3RZE . "Structure Of The Human Histamine H1 Receptor In Complex With Doxepin" . . . . . 99.39 452 96.93 98.16 1.60e-107 . . . . 915 1 486 no PDB 3SB5 . "Zn-Mediated Trimer Of T4 Lysozyme R125cE128C BY SYNTHETIC Symmetrization" . . . . . 98.78 165 97.53 97.53 1.32e-109 . . . . 915 1 487 no PDB 3SB8 . "Cu-Mediated Dimer Of T4 Lysozyme D61hK65H BY SYNTHETIC SYMMETRIZATION" . . . . . 98.78 165 97.53 97.53 2.27e-111 . . . . 915 1 488 no PDB 3SB9 . "Cu-Mediated Dimer Of T4 Lysozyme R76hR80H BY SYNTHETIC SYMMETRIZATION" . . . . . 98.78 165 97.53 97.53 1.75e-111 . . . . 915 1 489 no PDB 3SBA . "Zn-Mediated Hexamer Of T4 Lysozyme R76hR80H BY SYNTHETIC Symmetrization" . . . . . 98.78 165 97.53 97.53 1.75e-111 . . . . 915 1 490 no PDB 3SBB . "Disulphide-Mediated Tetramer Of T4 Lysozyme R76cR80C BY SYNTHETIC Symmetrization" . . . . . 98.78 165 97.53 97.53 1.25e-109 . . . . 915 1 491 no PDB 3SN6 . "Crystal Structure Of The Beta2 Adrenergic Receptor-Gs Protein Complex" . . . . . 97.56 514 98.75 98.75 2.59e-106 . . . . 915 1 492 no PDB 3UON . "Structure Of The Human M2 Muscarinic Acetylcholine Receptor Bound To An Antagonist" . . . . . 98.78 467 97.53 98.15 1.25e-107 . . . . 915 1 493 no PDB 3V2W . "Crystal Structure Of A Lipid G Protein-Coupled Receptor At 3.35a" . . . . . 98.78 520 97.53 98.15 2.22e-107 . . . . 915 1 494 no PDB 3V2Y . "Crystal Structure Of A Lipid G Protein-Coupled Receptor At 2.80a" . . . . . 98.78 520 97.53 98.15 2.22e-107 . . . . 915 1 495 no PDB 3VW7 . "Crystal Structure Of Human Protease-activated Receptor 1 (par1) Bound With Antagonist Vorapaxar At 2.2 Angstrom" . . . . . 98.78 484 97.53 98.15 5.95e-109 . . . . 915 1 496 no PDB 4ARJ . "Crystal Structure Of A Pesticin (translocation And Receptor Binding Domain) From Y. Pestis And T4-lysozyme Chimera" . . . . . 100.00 339 98.17 98.78 8.05e-113 . . . . 915 1 497 no PDB 4DAJ . "Structure Of The M3 Muscarinic Acetylcholine Receptor" . . . . . 98.17 479 98.76 98.76 1.34e-107 . . . . 915 1 498 no PDB 4DJH . "Structure Of The Human Kappa Opioid Receptor In Complex With Jdtic" . . . . . 98.17 480 98.14 98.76 8.37e-108 . . . . 915 1 499 no PDB 4DKL . "Crystal Structure Of The Mu-Opioid Receptor Bound To A Morphinan Antagonist" . . . . . 98.17 464 97.52 98.76 6.05e-107 . . . . 915 1 500 no PDB 4EJ4 . "Structure Of The Delta Opioid Receptor Bound To Naltrindole" . . . . . 98.17 461 97.52 98.76 9.31e-107 . . . . 915 1 501 no PDB 4EPI . "The Crystal Structure Of Pesticin-T4 Lysozyme Hybrid Stabilized By Engineered Disulfide Bonds" . . . . . 97.56 330 98.75 98.75 2.29e-110 . . . . 915 1 502 no PDB 4EXM . "The Crystal Structure Of An Engineered Phage Lysin Containing The Binding Domain Of Pesticin And The Killing Domain Of T4-Lysoz" . . . . . 98.78 347 97.53 97.53 1.67e-109 . . . . 915 1 503 no PDB 4GBR . "N-terminal T4 Lysozyme Fusion Facilitates Crystallization Of A G Protein Coupled Receptor" . . . . . 97.56 163 98.75 98.75 1.37e-111 . . . . 915 1 504 no PDB 4HTT . "Crystal Structure Of Twin Arginine Translocase Receptor- Tatc In Ddm" . . . . . 100.00 418 98.78 98.78 1.20e-113 . . . . 915 1 505 no PDB 4IAP . "Crystal Structure Of Ph Domain Of Osh3 From Saccharomyces Cerevisiae" . . . . . 97.56 260 98.13 98.75 8.20e-109 . . . . 915 1 506 no PDB 4LDE . "Structure Of Beta2 Adrenoceptor Bound To Bi167107 And An Engineered Nanobody" . . . . . 97.56 469 98.75 98.75 3.99e-107 . . . . 915 1 507 no PDB 4LDL . "Structure Of Beta2 Adrenoceptor Bound To Hydroxybenzylisoproterenol And An Engineered Nanobody" . . . . . 97.56 469 98.75 98.75 3.99e-107 . . . . 915 1 508 no PDB 4LDO . "Structure Of Beta2 Adrenoceptor Bound To Adrenaline And An Engineered Nanobody" . . . . . 97.56 469 98.75 98.75 3.99e-107 . . . . 915 1 509 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 8.06e-117 . . . . 915 1 510 no PDB 4OO9 . "Structure Of The Human Class C Gpcr Metabotropic Glutamate Receptor 5 Transmembrane Domain In Complex With The Negative Alloste" . . . . . 98.17 444 98.76 98.76 3.48e-109 . . . . 915 1 511 no PDB 4PHU . "Crystal Structure Of Human Gpr40 Bound To Allosteric Agonist Tak-875" . . . . . 99.39 491 97.55 98.16 2.51e-107 . . . . 915 1 512 no PDB 4PJZ . "Crystal Structure Of T4 Lysozyme-gss-peptide In Complex With Teicoplanin-a2-2" . . . . . 100.00 174 98.78 98.78 1.66e-114 . . . . 915 1 513 no PDB 4PK0 . "Crystal Structure Of T4 Lysozyme-peptide In Complex With Teicoplanin- A2-2" . . . . . 100.00 171 98.78 98.78 1.84e-114 . . . . 915 1 514 no PDB 4PLA . "Crystal Structure Of Phosphatidyl Inositol 4-kinase Ii Alpha In Complex With Atp" . . . . . 99.39 556 98.77 98.77 2.35e-108 . . . . 915 1 515 no PDB 4QKX . "Structure Of Beta2 Adrenoceptor Bound To A Covalent Agonist And An Engineered Nanobody" . . . . . 97.56 469 98.75 98.75 4.59e-107 . . . . 915 1 516 no PDB 4TN3 . "Structure Of The Bbox-coiled-coil Region Of Rhesus Trim5alpha" . . . . . 100.00 400 98.17 98.78 5.78e-112 . . . . 915 1 517 no PDB 4U14 . "Structure Of The M3 Muscarinic Acetylcholine Receptor Bound To The Antagonist Tiotropium Crystallized With Disulfide-stabilized" . . . . . 98.17 460 97.52 97.52 4.52e-107 . . . . 915 1 518 no PDB 4W8F . "Crystal Structure Of The Dynein Motor Domain In The Amppnp-bound State" . . . . . 97.56 2661 98.75 98.75 7.03e-100 . . . . 915 1 519 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 8.06e-117 . . . . 915 1 520 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 8.06e-117 . . . . 915 1 521 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 8.06e-117 . . . . 915 1 522 no DBJ BAI83135 . "lysozyme [Enterobacteria phage AR1]" . . . . . 100.00 164 98.17 98.78 6.53e-115 . . . . 915 1 523 no EMBL CAA28212 . "unnamed protein product [Enterobacteria phage T4]" . . . . . 100.00 164 98.78 98.78 2.17e-114 . . . . 915 1 524 no GB AAA72629 . "lysozyme [synthetic construct]" . . . . . 100.00 164 100.00 100.00 8.06e-117 . . . . 915 1 525 no GB AAA72664 . "synthetic T4-lysozyme [synthetic construct]" . . . . . 100.00 164 100.00 100.00 8.06e-117 . . . . 915 1 526 no GB AAD42568 . "e Lysozyme murein hydrolase [Enterobacteria phage T4]" . . . . . 100.00 164 98.78 98.78 2.17e-114 . . . . 915 1 527 no GB ABI94948 . "soluble lysozyme [Enterobacteria phage RB32]" . . . . . 100.00 164 98.17 98.78 6.53e-115 . . . . 915 1 528 no GB ACP30771 . "soluble lysozyme [Enterobacteria phage RB14]" . . . . . 100.00 164 98.78 98.78 1.82e-115 . . . . 915 1 529 no REF NP_049736 . "e Lysozyme murein hydrolase [Enterobacteria phage T4]" . . . . . 100.00 164 98.78 98.78 2.17e-114 . . . . 915 1 530 no REF YP_002854084 . "soluble lysozyme [Enterobacteria phage RB51]" . . . . . 100.00 164 98.17 98.78 6.53e-115 . . . . 915 1 531 no REF YP_002854463 . "soluble lysozyme [Enterobacteria phage RB14]" . . . . . 100.00 164 98.78 98.78 1.82e-115 . . . . 915 1 532 no REF YP_004415022 . "putative soluble lysozyme [Shigella phage Shfl2]" . . . . . 100.00 164 96.95 97.56 7.83e-113 . . . . 915 1 533 no REF YP_006986678 . "lysozyme murein hydrolase e [Enterobacteria phage vB_EcoM_ACG-C40]" . . . . . 100.00 164 98.17 98.78 6.53e-115 . . . . 915 1 534 no SP P00720 . "RecName: Full=Endolysin; AltName: Full=Lysis protein; AltName: Full=Lysozyme; AltName: Full=Muramidase [Enterobacteria phage T4" . . . . . 100.00 164 98.78 98.78 2.17e-114 . . . . 915 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'T4 lysozyme' common 915 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 . MET . 915 1 2 . ASN . 915 1 3 . ILE . 915 1 4 . PHE . 915 1 5 . GLU . 915 1 6 . MET . 915 1 7 . LEU . 915 1 8 . ARG . 915 1 9 . ILE . 915 1 10 . ASP . 915 1 11 . GLU . 915 1 12 . GLY . 915 1 13 . LEU . 915 1 14 . ARG . 915 1 15 . LEU . 915 1 16 . LYS . 915 1 17 . ILE . 915 1 18 . TYR . 915 1 19 . LYS . 915 1 20 . ASP . 915 1 21 . THR . 915 1 22 . GLU . 915 1 23 . GLY . 915 1 24 . TYR . 915 1 25 . TYR . 915 1 26 . THR . 915 1 27 . ILE . 915 1 28 . GLY . 915 1 29 . ILE . 915 1 30 . GLY . 915 1 31 . HIS . 915 1 32 . LEU . 915 1 33 . LEU . 915 1 34 . THR . 915 1 35 . LYS . 915 1 36 . SER . 915 1 37 . PRO . 915 1 38 . SER . 915 1 39 . LEU . 915 1 40 . ASN . 915 1 41 . ALA . 915 1 42 . ALA . 915 1 43 . LYS . 915 1 44 . SER . 915 1 45 . GLU . 915 1 46 . LEU . 915 1 47 . ASP . 915 1 48 . LYS . 915 1 49 . ALA . 915 1 50 . ILE . 915 1 51 . GLY . 915 1 52 . ARG . 915 1 53 . ASN . 915 1 54 . CYS . 915 1 55 . ASN . 915 1 56 . GLY . 915 1 57 . VAL . 915 1 58 . ILE . 915 1 59 . THR . 915 1 60 . LYS . 915 1 61 . ASP . 915 1 62 . GLU . 915 1 63 . ALA . 915 1 64 . GLU . 915 1 65 . LYS . 915 1 66 . LEU . 915 1 67 . PHE . 915 1 68 . ASN . 915 1 69 . GLN . 915 1 70 . ASP . 915 1 71 . VAL . 915 1 72 . ASP . 915 1 73 . ALA . 915 1 74 . ALA . 915 1 75 . VAL . 915 1 76 . ARG . 915 1 77 . GLY . 915 1 78 . ILE . 915 1 79 . LEU . 915 1 80 . ARG . 915 1 81 . ASN . 915 1 82 . ALA . 915 1 83 . LYS . 915 1 84 . LEU . 915 1 85 . LYS . 915 1 86 . PRO . 915 1 87 . VAL . 915 1 88 . TYR . 915 1 89 . ASP . 915 1 90 . SER . 915 1 91 . LEU . 915 1 92 . ASP . 915 1 93 . ALA . 915 1 94 . VAL . 915 1 95 . ARG . 915 1 96 . ARG . 915 1 97 . CYS . 915 1 98 . ALA . 915 1 99 . LEU . 915 1 100 . ILE . 915 1 101 . ASN . 915 1 102 . MET . 915 1 103 . VAL . 915 1 104 . PHE . 915 1 105 . GLN . 915 1 106 . MET . 915 1 107 . GLY . 915 1 108 . GLU . 915 1 109 . THR . 915 1 110 . GLY . 915 1 111 . VAL . 915 1 112 . ALA . 915 1 113 . GLY . 915 1 114 . PHE . 915 1 115 . THR . 915 1 116 . ASN . 915 1 117 . SER . 915 1 118 . LEU . 915 1 119 . ARG . 915 1 120 . MET . 915 1 121 . LEU . 915 1 122 . GLN . 915 1 123 . GLN . 915 1 124 . LYS . 915 1 125 . ARG . 915 1 126 . TRP . 915 1 127 . ASP . 915 1 128 . GLU . 915 1 129 . ALA . 915 1 130 . ALA . 915 1 131 . VAL . 915 1 132 . ASN . 915 1 133 . LEU . 915 1 134 . ALA . 915 1 135 . LYS . 915 1 136 . SER . 915 1 137 . ARG . 915 1 138 . TRP . 915 1 139 . TYR . 915 1 140 . ASN . 915 1 141 . GLN . 915 1 142 . THR . 915 1 143 . PRO . 915 1 144 . ASN . 915 1 145 . ARG . 915 1 146 . ALA . 915 1 147 . LYS . 915 1 148 . ARG . 915 1 149 . VAL . 915 1 150 . ILE . 915 1 151 . THR . 915 1 152 . THR . 915 1 153 . PHE . 915 1 154 . ARG . 915 1 155 . THR . 915 1 156 . GLY . 915 1 157 . THR . 915 1 158 . TRP . 915 1 159 . ASP . 915 1 160 . ALA . 915 1 161 . TYR . 915 1 162 . LYS . 915 1 163 . ASN . 915 1 164 . LEU . 915 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . MET 1 1 915 1 . ASN 2 2 915 1 . ILE 3 3 915 1 . PHE 4 4 915 1 . GLU 5 5 915 1 . MET 6 6 915 1 . LEU 7 7 915 1 . ARG 8 8 915 1 . ILE 9 9 915 1 . ASP 10 10 915 1 . GLU 11 11 915 1 . GLY 12 12 915 1 . LEU 13 13 915 1 . ARG 14 14 915 1 . LEU 15 15 915 1 . LYS 16 16 915 1 . ILE 17 17 915 1 . TYR 18 18 915 1 . LYS 19 19 915 1 . ASP 20 20 915 1 . THR 21 21 915 1 . GLU 22 22 915 1 . GLY 23 23 915 1 . TYR 24 24 915 1 . TYR 25 25 915 1 . THR 26 26 915 1 . ILE 27 27 915 1 . GLY 28 28 915 1 . ILE 29 29 915 1 . GLY 30 30 915 1 . HIS 31 31 915 1 . LEU 32 32 915 1 . LEU 33 33 915 1 . THR 34 34 915 1 . LYS 35 35 915 1 . SER 36 36 915 1 . PRO 37 37 915 1 . SER 38 38 915 1 . LEU 39 39 915 1 . ASN 40 40 915 1 . ALA 41 41 915 1 . ALA 42 42 915 1 . LYS 43 43 915 1 . SER 44 44 915 1 . GLU 45 45 915 1 . LEU 46 46 915 1 . ASP 47 47 915 1 . LYS 48 48 915 1 . ALA 49 49 915 1 . ILE 50 50 915 1 . GLY 51 51 915 1 . ARG 52 52 915 1 . ASN 53 53 915 1 . CYS 54 54 915 1 . ASN 55 55 915 1 . GLY 56 56 915 1 . VAL 57 57 915 1 . ILE 58 58 915 1 . THR 59 59 915 1 . LYS 60 60 915 1 . ASP 61 61 915 1 . GLU 62 62 915 1 . ALA 63 63 915 1 . GLU 64 64 915 1 . LYS 65 65 915 1 . LEU 66 66 915 1 . PHE 67 67 915 1 . ASN 68 68 915 1 . GLN 69 69 915 1 . ASP 70 70 915 1 . VAL 71 71 915 1 . ASP 72 72 915 1 . ALA 73 73 915 1 . ALA 74 74 915 1 . VAL 75 75 915 1 . ARG 76 76 915 1 . GLY 77 77 915 1 . ILE 78 78 915 1 . LEU 79 79 915 1 . ARG 80 80 915 1 . ASN 81 81 915 1 . ALA 82 82 915 1 . LYS 83 83 915 1 . LEU 84 84 915 1 . LYS 85 85 915 1 . PRO 86 86 915 1 . VAL 87 87 915 1 . TYR 88 88 915 1 . ASP 89 89 915 1 . SER 90 90 915 1 . LEU 91 91 915 1 . ASP 92 92 915 1 . ALA 93 93 915 1 . VAL 94 94 915 1 . ARG 95 95 915 1 . ARG 96 96 915 1 . CYS 97 97 915 1 . ALA 98 98 915 1 . LEU 99 99 915 1 . ILE 100 100 915 1 . ASN 101 101 915 1 . MET 102 102 915 1 . VAL 103 103 915 1 . PHE 104 104 915 1 . GLN 105 105 915 1 . MET 106 106 915 1 . GLY 107 107 915 1 . GLU 108 108 915 1 . THR 109 109 915 1 . GLY 110 110 915 1 . VAL 111 111 915 1 . ALA 112 112 915 1 . GLY 113 113 915 1 . PHE 114 114 915 1 . THR 115 115 915 1 . ASN 116 116 915 1 . SER 117 117 915 1 . LEU 118 118 915 1 . ARG 119 119 915 1 . MET 120 120 915 1 . LEU 121 121 915 1 . GLN 122 122 915 1 . GLN 123 123 915 1 . LYS 124 124 915 1 . ARG 125 125 915 1 . TRP 126 126 915 1 . ASP 127 127 915 1 . GLU 128 128 915 1 . ALA 129 129 915 1 . ALA 130 130 915 1 . VAL 131 131 915 1 . ASN 132 132 915 1 . LEU 133 133 915 1 . ALA 134 134 915 1 . LYS 135 135 915 1 . SER 136 136 915 1 . ARG 137 137 915 1 . TRP 138 138 915 1 . TYR 139 139 915 1 . ASN 140 140 915 1 . GLN 141 141 915 1 . THR 142 142 915 1 . PRO 143 143 915 1 . ASN 144 144 915 1 . ARG 145 145 915 1 . ALA 146 146 915 1 . LYS 147 147 915 1 . ARG 148 148 915 1 . VAL 149 149 915 1 . ILE 150 150 915 1 . THR 151 151 915 1 . THR 152 152 915 1 . PHE 153 153 915 1 . ARG 154 154 915 1 . THR 155 155 915 1 . GLY 156 156 915 1 . THR 157 157 915 1 . TRP 158 158 915 1 . ASP 159 159 915 1 . ALA 160 160 915 1 . TYR 161 161 915 1 . LYS 162 162 915 1 . ASN 163 163 915 1 . LEU 164 164 915 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 915 _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 $T4_lysozyme . 562 organism . 'Escherichia coli' 'Escherichia coli bacteriophage' . . Bacteria . Escherichia coli 'wild type T4' . . . . . . . . . . . . . . . . . . . . 915 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 915 _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 $T4_lysozyme . 'not available' 'Escherichia coli' . . . Escherichia coli generic . . . . . . . . . . . . . . . . . . . . . . 915 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 915 _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 . save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_condition_set_one _Sample_condition_list.Entry_ID 915 _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 5.6 . na 915 1 temperature 293 . K 915 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_list _NMR_spectrometer.Entry_ID 915 _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 915 _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 'spectrometer information not available' . . 915 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 915 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 . . . . . . . . . . . . 1 $sample_one . . . 1 $sample_condition_set_one . . . 1 $spectrometer_list . . . . . . . . . . . . . . . . 915 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chem_shift_reference_par_set_one _Chem_shift_reference.Entry_ID 915 _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 . DSS . . . . . . 0 . . . . . . 1 $entry_citation . . 1 $entry_citation 915 1 N . 'liquid ammonia' . . . . . . 0 . . . . . . 1 $entry_citation . . 1 $entry_citation 915 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_chemical_shift_assignment_data_set_one _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode 'chemical_shift_assignment_data_set_one' _Assigned_chem_shift_list.Entry_ID 915 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_condition_set_one _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chem_shift_reference_par_set_one _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 $sample_one . 915 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 MET N N 15 39.9 . . 1 . . . . . . . . 915 1 2 . 1 1 2 2 ASN H H 1 6.99 . . 1 . . . . . . . . 915 1 3 . 1 1 2 2 ASN HA H 1 4.49 . . 1 . . . . . . . . 915 1 4 . 1 1 2 2 ASN N N 15 116.9 . . 1 . . . . . . . . 915 1 5 . 1 1 3 3 ILE H H 1 8.89 . . 1 . . . . . . . . 915 1 6 . 1 1 3 3 ILE HA H 1 4.12 . . 1 . . . . . . . . 915 1 7 . 1 1 3 3 ILE N N 15 118.6 . . 1 . . . . . . . . 915 1 8 . 1 1 4 4 PHE H H 1 7.56 . . 1 . . . . . . . . 915 1 9 . 1 1 4 4 PHE HA H 1 3.83 . . 1 . . . . . . . . 915 1 10 . 1 1 4 4 PHE HB2 H 1 3.05 . . 2 . . . . . . . . 915 1 11 . 1 1 4 4 PHE HB3 H 1 3.17 . . 2 . . . . . . . . 915 1 12 . 1 1 4 4 PHE HD1 H 1 6.77 . . 1 . . . . . . . . 915 1 13 . 1 1 4 4 PHE HD2 H 1 6.77 . . 1 . . . . . . . . 915 1 14 . 1 1 4 4 PHE HE1 H 1 6.93 . . 1 . . . . . . . . 915 1 15 . 1 1 4 4 PHE HE2 H 1 6.93 . . 1 . . . . . . . . 915 1 16 . 1 1 4 4 PHE HZ H 1 6.99 . . 1 . . . . . . . . 915 1 17 . 1 1 4 4 PHE N N 15 124.3 . . 1 . . . . . . . . 915 1 18 . 1 1 5 5 GLU H H 1 8.06 . . 1 . . . . . . . . 915 1 19 . 1 1 5 5 GLU HA H 1 3.7 . . 1 . . . . . . . . 915 1 20 . 1 1 5 5 GLU HB2 H 1 1.8 . . 1 . . . . . . . . 915 1 21 . 1 1 5 5 GLU HB3 H 1 1.8 . . 1 . . . . . . . . 915 1 22 . 1 1 5 5 GLU N N 15 119.2 . . 1 . . . . . . . . 915 1 23 . 1 1 6 6 MET H H 1 7.84 . . 1 . . . . . . . . 915 1 24 . 1 1 6 6 MET HA H 1 3.3 . . 1 . . . . . . . . 915 1 25 . 1 1 6 6 MET N N 15 119.3 . . 1 . . . . . . . . 915 1 26 . 1 1 7 7 LEU H H 1 7.91 . . 1 . . . . . . . . 915 1 27 . 1 1 7 7 LEU HA H 1 3.97 . . 1 . . . . . . . . 915 1 28 . 1 1 7 7 LEU N N 15 119 . . 1 . . . . . . . . 915 1 29 . 1 1 8 8 ARG H H 1 8.48 . . 1 . . . . . . . . 915 1 30 . 1 1 8 8 ARG HA H 1 3.41 . . 1 . . . . . . . . 915 1 31 . 1 1 8 8 ARG HB2 H 1 1.73 . . 1 . . . . . . . . 915 1 32 . 1 1 8 8 ARG HB3 H 1 1.73 . . 1 . . . . . . . . 915 1 33 . 1 1 8 8 ARG N N 15 123.9 . . 1 . . . . . . . . 915 1 34 . 1 1 9 9 ILE H H 1 7.52 . . 1 . . . . . . . . 915 1 35 . 1 1 9 9 ILE HA H 1 3.54 . . 1 . . . . . . . . 915 1 36 . 1 1 9 9 ILE HB H 1 2.08 . . 1 . . . . . . . . 915 1 37 . 1 1 9 9 ILE N N 15 120.8 . . 1 . . . . . . . . 915 1 38 . 1 1 10 10 ASP H H 1 7.97 . . 1 . . . . . . . . 915 1 39 . 1 1 10 10 ASP HA H 1 4.49 . . 1 . . . . . . . . 915 1 40 . 1 1 10 10 ASP HB2 H 1 2.6 . . 1 . . . . . . . . 915 1 41 . 1 1 10 10 ASP HB3 H 1 2.6 . . 1 . . . . . . . . 915 1 42 . 1 1 10 10 ASP N N 15 119.1 . . 1 . . . . . . . . 915 1 43 . 1 1 11 11 GLU H H 1 8.98 . . 1 . . . . . . . . 915 1 44 . 1 1 11 11 GLU HA H 1 4.59 . . 1 . . . . . . . . 915 1 45 . 1 1 11 11 GLU HB2 H 1 1.93 . . 2 . . . . . . . . 915 1 46 . 1 1 11 11 GLU HB3 H 1 2.11 . . 2 . . . . . . . . 915 1 47 . 1 1 11 11 GLU HG2 H 1 2.3 . . 1 . . . . . . . . 915 1 48 . 1 1 11 11 GLU HG3 H 1 2.3 . . 1 . . . . . . . . 915 1 49 . 1 1 11 11 GLU N N 15 119 . . 1 . . . . . . . . 915 1 50 . 1 1 12 12 GLY H H 1 7.4 . . 1 . . . . . . . . 915 1 51 . 1 1 12 12 GLY HA2 H 1 3.77 . . 2 . . . . . . . . 915 1 52 . 1 1 12 12 GLY HA3 H 1 4.13 . . 2 . . . . . . . . 915 1 53 . 1 1 12 12 GLY N N 15 110.3 . . 1 . . . . . . . . 915 1 54 . 1 1 13 13 LEU H H 1 7.98 . . 1 . . . . . . . . 915 1 55 . 1 1 13 13 LEU HA H 1 4.4 . . 1 . . . . . . . . 915 1 56 . 1 1 13 13 LEU HB2 H 1 1.69 . . 1 . . . . . . . . 915 1 57 . 1 1 13 13 LEU HB3 H 1 1.69 . . 1 . . . . . . . . 915 1 58 . 1 1 13 13 LEU N N 15 120.1 . . 1 . . . . . . . . 915 1 59 . 1 1 14 14 ARG H H 1 8.05 . . 1 . . . . . . . . 915 1 60 . 1 1 14 14 ARG HA H 1 4.69 . . 1 . . . . . . . . 915 1 61 . 1 1 14 14 ARG HB2 H 1 1.9 . . 1 . . . . . . . . 915 1 62 . 1 1 14 14 ARG HB3 H 1 1.9 . . 1 . . . . . . . . 915 1 63 . 1 1 14 14 ARG N N 15 128.5 . . 1 . . . . . . . . 915 1 64 . 1 1 15 15 LEU H H 1 8.83 . . 1 . . . . . . . . 915 1 65 . 1 1 15 15 LEU HA H 1 4.36 . . 1 . . . . . . . . 915 1 66 . 1 1 15 15 LEU HB2 H 1 1.6 . . 1 . . . . . . . . 915 1 67 . 1 1 15 15 LEU HB3 H 1 1.6 . . 1 . . . . . . . . 915 1 68 . 1 1 15 15 LEU N N 15 124.1 . . 1 . . . . . . . . 915 1 69 . 1 1 16 16 LYS H H 1 7.15 . . 1 . . . . . . . . 915 1 70 . 1 1 16 16 LYS HA H 1 5.43 . . 1 . . . . . . . . 915 1 71 . 1 1 16 16 LYS HB2 H 1 1.78 . . 2 . . . . . . . . 915 1 72 . 1 1 16 16 LYS HB3 H 1 1.93 . . 2 . . . . . . . . 915 1 73 . 1 1 16 16 LYS HG2 H 1 1.53 . . 1 . . . . . . . . 915 1 74 . 1 1 16 16 LYS HG3 H 1 1.53 . . 1 . . . . . . . . 915 1 75 . 1 1 16 16 LYS N N 15 115.7 . . 1 . . . . . . . . 915 1 76 . 1 1 17 17 ILE H H 1 7.53 . . 1 . . . . . . . . 915 1 77 . 1 1 17 17 ILE N N 15 121.4 . . 1 . . . . . . . . 915 1 78 . 1 1 18 18 TYR H H 1 9.48 . . 1 . . . . . . . . 915 1 79 . 1 1 18 18 TYR HA H 1 5.13 . . 1 . . . . . . . . 915 1 80 . 1 1 18 18 TYR HB2 H 1 3.01 . . 2 . . . . . . . . 915 1 81 . 1 1 18 18 TYR HB3 H 1 3.11 . . 2 . . . . . . . . 915 1 82 . 1 1 18 18 TYR HD1 H 1 7.19 . . 1 . . . . . . . . 915 1 83 . 1 1 18 18 TYR HD2 H 1 7.19 . . 1 . . . . . . . . 915 1 84 . 1 1 18 18 TYR HE1 H 1 6.57 . . 1 . . . . . . . . 915 1 85 . 1 1 18 18 TYR HE2 H 1 6.57 . . 1 . . . . . . . . 915 1 86 . 1 1 18 18 TYR N N 15 129 . . 1 . . . . . . . . 915 1 87 . 1 1 19 19 LYS H H 1 8.35 . . 1 . . . . . . . . 915 1 88 . 1 1 19 19 LYS HA H 1 4.58 . . 1 . . . . . . . . 915 1 89 . 1 1 19 19 LYS HB2 H 1 1.59 . . 1 . . . . . . . . 915 1 90 . 1 1 19 19 LYS HB3 H 1 1.59 . . 1 . . . . . . . . 915 1 91 . 1 1 19 19 LYS N N 15 121.9 . . 1 . . . . . . . . 915 1 92 . 1 1 20 20 ASP H H 1 8.54 . . 1 . . . . . . . . 915 1 93 . 1 1 20 20 ASP HA H 1 4.6 . . 1 . . . . . . . . 915 1 94 . 1 1 20 20 ASP N N 15 125.9 . . 1 . . . . . . . . 915 1 95 . 1 1 21 21 THR H H 1 8 . . 1 . . . . . . . . 915 1 96 . 1 1 21 21 THR HA H 1 4 . . 1 . . . . . . . . 915 1 97 . 1 1 21 21 THR HB H 1 4.32 . . 1 . . . . . . . . 915 1 98 . 1 1 21 21 THR HG21 H 1 1.38 . . 1 . . . . . . . . 915 1 99 . 1 1 21 21 THR HG22 H 1 1.38 . . 1 . . . . . . . . 915 1 100 . 1 1 21 21 THR HG23 H 1 1.38 . . 1 . . . . . . . . 915 1 101 . 1 1 21 21 THR N N 15 111.2 . . 1 . . . . . . . . 915 1 102 . 1 1 22 22 GLU H H 1 7.99 . . 1 . . . . . . . . 915 1 103 . 1 1 22 22 GLU HA H 1 4.17 . . 1 . . . . . . . . 915 1 104 . 1 1 22 22 GLU HB2 H 1 1.7 . . 1 . . . . . . . . 915 1 105 . 1 1 22 22 GLU HB3 H 1 1.7 . . 1 . . . . . . . . 915 1 106 . 1 1 22 22 GLU N N 15 121.3 . . 1 . . . . . . . . 915 1 107 . 1 1 23 23 GLY H H 1 7.88 . . 1 . . . . . . . . 915 1 108 . 1 1 23 23 GLY HA2 H 1 3.34 . . 2 . . . . . . . . 915 1 109 . 1 1 23 23 GLY HA3 H 1 3.98 . . 2 . . . . . . . . 915 1 110 . 1 1 23 23 GLY N N 15 108.1 . . 1 . . . . . . . . 915 1 111 . 1 1 24 24 TYR H H 1 8.16 . . 1 . . . . . . . . 915 1 112 . 1 1 24 24 TYR HA H 1 4.97 . . 1 . . . . . . . . 915 1 113 . 1 1 24 24 TYR HB2 H 1 2.91 . . 2 . . . . . . . . 915 1 114 . 1 1 24 24 TYR HB3 H 1 2.97 . . 2 . . . . . . . . 915 1 115 . 1 1 24 24 TYR HD1 H 1 7.12 . . 1 . . . . . . . . 915 1 116 . 1 1 24 24 TYR HD2 H 1 7.12 . . 1 . . . . . . . . 915 1 117 . 1 1 24 24 TYR HE1 H 1 6.81 . . 1 . . . . . . . . 915 1 118 . 1 1 24 24 TYR HE2 H 1 6.81 . . 1 . . . . . . . . 915 1 119 . 1 1 24 24 TYR N N 15 122.2 . . 1 . . . . . . . . 915 1 120 . 1 1 25 25 TYR H H 1 8.73 . . 1 . . . . . . . . 915 1 121 . 1 1 25 25 TYR HA H 1 4.9 . . 1 . . . . . . . . 915 1 122 . 1 1 25 25 TYR HB2 H 1 2.81 . . 1 . . . . . . . . 915 1 123 . 1 1 25 25 TYR HB3 H 1 2.81 . . 1 . . . . . . . . 915 1 124 . 1 1 25 25 TYR HD1 H 1 7.01 . . 1 . . . . . . . . 915 1 125 . 1 1 25 25 TYR HD2 H 1 7.01 . . 1 . . . . . . . . 915 1 126 . 1 1 25 25 TYR HE1 H 1 6.71 . . 1 . . . . . . . . 915 1 127 . 1 1 25 25 TYR HE2 H 1 6.71 . . 1 . . . . . . . . 915 1 128 . 1 1 25 25 TYR N N 15 124.1 . . 1 . . . . . . . . 915 1 129 . 1 1 26 26 THR H H 1 9.37 . . 1 . . . . . . . . 915 1 130 . 1 1 26 26 THR HA H 1 5.06 . . 1 . . . . . . . . 915 1 131 . 1 1 26 26 THR HB H 1 2.8 . . 1 . . . . . . . . 915 1 132 . 1 1 26 26 THR HG21 H 1 1.02 . . 1 . . . . . . . . 915 1 133 . 1 1 26 26 THR HG22 H 1 1.02 . . 1 . . . . . . . . 915 1 134 . 1 1 26 26 THR HG23 H 1 1.02 . . 1 . . . . . . . . 915 1 135 . 1 1 26 26 THR N N 15 122.6 . . 1 . . . . . . . . 915 1 136 . 1 1 27 27 ILE H H 1 8.85 . . 1 . . . . . . . . 915 1 137 . 1 1 27 27 ILE HA H 1 4.61 . . 1 . . . . . . . . 915 1 138 . 1 1 27 27 ILE N N 15 122.3 . . 1 . . . . . . . . 915 1 139 . 1 1 28 28 GLY H H 1 8.47 . . 1 . . . . . . . . 915 1 140 . 1 1 28 28 GLY HA2 H 1 3.58 . . 2 . . . . . . . . 915 1 141 . 1 1 28 28 GLY HA3 H 1 4.28 . . 2 . . . . . . . . 915 1 142 . 1 1 28 28 GLY N N 15 113.3 . . 1 . . . . . . . . 915 1 143 . 1 1 29 29 ILE H H 1 9.79 . . 1 . . . . . . . . 915 1 144 . 1 1 29 29 ILE HA H 1 4.75 . . 1 . . . . . . . . 915 1 145 . 1 1 29 29 ILE HB H 1 1.97 . . 1 . . . . . . . . 915 1 146 . 1 1 29 29 ILE N N 15 132 . . 1 . . . . . . . . 915 1 147 . 1 1 30 30 GLY H H 1 7.94 . . 1 . . . . . . . . 915 1 148 . 1 1 30 30 GLY N N 15 110 . . 1 . . . . . . . . 915 1 149 . 1 1 31 31 HIS H H 1 8.44 . . 1 . . . . . . . . 915 1 150 . 1 1 31 31 HIS HA H 1 4.61 . . 1 . . . . . . . . 915 1 151 . 1 1 31 31 HIS HB2 H 1 3.68 . . 1 . . . . . . . . 915 1 152 . 1 1 31 31 HIS HB3 H 1 3.68 . . 1 . . . . . . . . 915 1 153 . 1 1 31 31 HIS ND1 N 15 188 . . 1 . . . . . . . . 915 1 154 . 1 1 31 31 HIS NE2 N 15 174.4 . . 1 . . . . . . . . 915 1 155 . 1 1 31 31 HIS HD2 H 1 8.65 . . 1 . . . . . . . . 915 1 156 . 1 1 31 31 HIS HE1 H 1 6.38 . . 1 . . . . . . . . 915 1 157 . 1 1 31 31 HIS N N 15 117.6 . . 1 . . . . . . . . 915 1 158 . 1 1 32 32 LEU H H 1 8.17 . . 1 . . . . . . . . 915 1 159 . 1 1 32 32 LEU HA H 1 4.06 . . 1 . . . . . . . . 915 1 160 . 1 1 32 32 LEU HB2 H 1 1.41 . . 1 . . . . . . . . 915 1 161 . 1 1 32 32 LEU HB3 H 1 1.41 . . 1 . . . . . . . . 915 1 162 . 1 1 32 32 LEU N N 15 133.7 . . 1 . . . . . . . . 915 1 163 . 1 1 33 33 LEU H H 1 9.18 . . 1 . . . . . . . . 915 1 164 . 1 1 33 33 LEU HA H 1 4.48 . . 1 . . . . . . . . 915 1 165 . 1 1 33 33 LEU HB2 H 1 1.73 . . 1 . . . . . . . . 915 1 166 . 1 1 33 33 LEU HB3 H 1 1.73 . . 1 . . . . . . . . 915 1 167 . 1 1 33 33 LEU N N 15 127 . . 1 . . . . . . . . 915 1 168 . 1 1 34 34 THR H H 1 7.31 . . 1 . . . . . . . . 915 1 169 . 1 1 34 34 THR HA H 1 4.48 . . 1 . . . . . . . . 915 1 170 . 1 1 34 34 THR N N 15 110.9 . . 1 . . . . . . . . 915 1 171 . 1 1 35 35 LYS H H 1 8.61 . . 1 . . . . . . . . 915 1 172 . 1 1 35 35 LYS HA H 1 4.26 . . 1 . . . . . . . . 915 1 173 . 1 1 35 35 LYS HB2 H 1 1.42 . . 1 . . . . . . . . 915 1 174 . 1 1 35 35 LYS HB3 H 1 1.42 . . 1 . . . . . . . . 915 1 175 . 1 1 35 35 LYS N N 15 126.1 . . 1 . . . . . . . . 915 1 176 . 1 1 36 36 SER H H 1 8.81 . . 1 . . . . . . . . 915 1 177 . 1 1 36 36 SER HA H 1 4.66 . . 1 . . . . . . . . 915 1 178 . 1 1 36 36 SER HB2 H 1 3.88 . . 2 . . . . . . . . 915 1 179 . 1 1 36 36 SER HB3 H 1 4.03 . . 2 . . . . . . . . 915 1 180 . 1 1 36 36 SER N N 15 120.8 . . 1 . . . . . . . . 915 1 181 . 1 1 38 38 SER H H 1 8.26 . . 1 . . . . . . . . 915 1 182 . 1 1 38 38 SER HA H 1 4.74 . . 1 . . . . . . . . 915 1 183 . 1 1 38 38 SER HB2 H 1 3.88 . . 1 . . . . . . . . 915 1 184 . 1 1 38 38 SER HB3 H 1 3.88 . . 1 . . . . . . . . 915 1 185 . 1 1 38 38 SER N N 15 117.4 . . 1 . . . . . . . . 915 1 186 . 1 1 39 39 LEU H H 1 9 . . 1 . . . . . . . . 915 1 187 . 1 1 39 39 LEU HA H 1 3.37 . . 1 . . . . . . . . 915 1 188 . 1 1 39 39 LEU HB2 H 1 1.71 . . 1 . . . . . . . . 915 1 189 . 1 1 39 39 LEU HB3 H 1 1.71 . . 1 . . . . . . . . 915 1 190 . 1 1 39 39 LEU N N 15 134.4 . . 1 . . . . . . . . 915 1 191 . 1 1 40 40 ASN H H 1 8.31 . . 1 . . . . . . . . 915 1 192 . 1 1 40 40 ASN HA H 1 4.29 . . 1 . . . . . . . . 915 1 193 . 1 1 40 40 ASN HB2 H 1 2.62 . . 2 . . . . . . . . 915 1 194 . 1 1 40 40 ASN HB3 H 1 2.73 . . 2 . . . . . . . . 915 1 195 . 1 1 40 40 ASN N N 15 118.2 . . 1 . . . . . . . . 915 1 196 . 1 1 41 41 ALA H H 1 7.77 . . 1 . . . . . . . . 915 1 197 . 1 1 41 41 ALA HA H 1 4.24 . . 1 . . . . . . . . 915 1 198 . 1 1 41 41 ALA HB1 H 1 1.63 . . 1 . . . . . . . . 915 1 199 . 1 1 41 41 ALA HB2 H 1 1.63 . . 1 . . . . . . . . 915 1 200 . 1 1 41 41 ALA HB3 H 1 1.63 . . 1 . . . . . . . . 915 1 201 . 1 1 41 41 ALA N N 15 125.2 . . 1 . . . . . . . . 915 1 202 . 1 1 42 42 ALA H H 1 7.62 . . 1 . . . . . . . . 915 1 203 . 1 1 42 42 ALA HA H 1 3.74 . . 1 . . . . . . . . 915 1 204 . 1 1 42 42 ALA HB1 H 1 1.23 . . 1 . . . . . . . . 915 1 205 . 1 1 42 42 ALA HB2 H 1 1.23 . . 1 . . . . . . . . 915 1 206 . 1 1 42 42 ALA HB3 H 1 1.23 . . 1 . . . . . . . . 915 1 207 . 1 1 42 42 ALA N N 15 122.2 . . 1 . . . . . . . . 915 1 208 . 1 1 43 43 LYS H H 1 8.49 . . 1 . . . . . . . . 915 1 209 . 1 1 43 43 LYS HA H 1 3.73 . . 1 . . . . . . . . 915 1 210 . 1 1 43 43 LYS HB2 H 1 1.88 . . 1 . . . . . . . . 915 1 211 . 1 1 43 43 LYS HB3 H 1 1.88 . . 1 . . . . . . . . 915 1 212 . 1 1 43 43 LYS N N 15 117.9 . . 1 . . . . . . . . 915 1 213 . 1 1 44 44 SER H H 1 7.98 . . 1 . . . . . . . . 915 1 214 . 1 1 44 44 SER HA H 1 4.3 . . 1 . . . . . . . . 915 1 215 . 1 1 44 44 SER HB2 H 1 4.02 . . 1 . . . . . . . . 915 1 216 . 1 1 44 44 SER HB3 H 1 4.02 . . 1 . . . . . . . . 915 1 217 . 1 1 44 44 SER N N 15 115.7 . . 1 . . . . . . . . 915 1 218 . 1 1 45 45 GLU H H 1 8.16 . . 1 . . . . . . . . 915 1 219 . 1 1 45 45 GLU HA H 1 4.14 . . 1 . . . . . . . . 915 1 220 . 1 1 45 45 GLU HB2 H 1 2.02 . . 1 . . . . . . . . 915 1 221 . 1 1 45 45 GLU HB3 H 1 2.02 . . 1 . . . . . . . . 915 1 222 . 1 1 45 45 GLU N N 15 121.6 . . 1 . . . . . . . . 915 1 223 . 1 1 46 46 LEU H H 1 8.33 . . 1 . . . . . . . . 915 1 224 . 1 1 46 46 LEU HA H 1 3.97 . . 1 . . . . . . . . 915 1 225 . 1 1 46 46 LEU N N 15 123.4 . . 1 . . . . . . . . 915 1 226 . 1 1 47 47 ASP H H 1 8.12 . . 1 . . . . . . . . 915 1 227 . 1 1 47 47 ASP HA H 1 4.85 . . 1 . . . . . . . . 915 1 228 . 1 1 47 47 ASP HB2 H 1 2.72 . . 1 . . . . . . . . 915 1 229 . 1 1 47 47 ASP HB3 H 1 2.72 . . 1 . . . . . . . . 915 1 230 . 1 1 47 47 ASP N N 15 120.9 . . 1 . . . . . . . . 915 1 231 . 1 1 48 48 LYS H H 1 7.84 . . 1 . . . . . . . . 915 1 232 . 1 1 48 48 LYS HA H 1 4.02 . . 1 . . . . . . . . 915 1 233 . 1 1 48 48 LYS HB2 H 1 1.92 . . 1 . . . . . . . . 915 1 234 . 1 1 48 48 LYS HB3 H 1 1.92 . . 1 . . . . . . . . 915 1 235 . 1 1 48 48 LYS HG2 H 1 1.42 . . 2 . . . . . . . . 915 1 236 . 1 1 48 48 LYS HG3 H 1 1.61 . . 2 . . . . . . . . 915 1 237 . 1 1 48 48 LYS N N 15 122 . . 1 . . . . . . . . 915 1 238 . 1 1 49 49 ALA H H 1 8 . . 1 . . . . . . . . 915 1 239 . 1 1 49 49 ALA HA H 1 4.18 . . 1 . . . . . . . . 915 1 240 . 1 1 49 49 ALA HB1 H 1 1.5 . . 1 . . . . . . . . 915 1 241 . 1 1 49 49 ALA HB2 H 1 1.5 . . 1 . . . . . . . . 915 1 242 . 1 1 49 49 ALA HB3 H 1 1.5 . . 1 . . . . . . . . 915 1 243 . 1 1 49 49 ALA N N 15 122.4 . . 1 . . . . . . . . 915 1 244 . 1 1 50 50 ILE H H 1 8.32 . . 1 . . . . . . . . 915 1 245 . 1 1 50 50 ILE HA H 1 4.07 . . 1 . . . . . . . . 915 1 246 . 1 1 50 50 ILE HB H 1 1.96 . . 1 . . . . . . . . 915 1 247 . 1 1 50 50 ILE HG12 H 1 .93 . . 1 . . . . . . . . 915 1 248 . 1 1 50 50 ILE HG13 H 1 .93 . . 1 . . . . . . . . 915 1 249 . 1 1 50 50 ILE HG21 H 1 .93 . . 1 . . . . . . . . 915 1 250 . 1 1 50 50 ILE HG22 H 1 .93 . . 1 . . . . . . . . 915 1 251 . 1 1 50 50 ILE HG23 H 1 .93 . . 1 . . . . . . . . 915 1 252 . 1 1 50 50 ILE N N 15 115.8 . . 1 . . . . . . . . 915 1 253 . 1 1 51 51 GLY H H 1 8.36 . . 1 . . . . . . . . 915 1 254 . 1 1 51 51 GLY HA2 H 1 3.77 . . 2 . . . . . . . . 915 1 255 . 1 1 51 51 GLY HA3 H 1 4.17 . . 2 . . . . . . . . 915 1 256 . 1 1 51 51 GLY N N 15 110 . . 1 . . . . . . . . 915 1 257 . 1 1 52 52 ARG H H 1 7.65 . . 1 . . . . . . . . 915 1 258 . 1 1 52 52 ARG HA H 1 4.56 . . 1 . . . . . . . . 915 1 259 . 1 1 52 52 ARG HB2 H 1 1.74 . . 1 . . . . . . . . 915 1 260 . 1 1 52 52 ARG HB3 H 1 1.74 . . 1 . . . . . . . . 915 1 261 . 1 1 52 52 ARG N N 15 117.3 . . 1 . . . . . . . . 915 1 262 . 1 1 53 53 ASN H H 1 8.32 . . 1 . . . . . . . . 915 1 263 . 1 1 53 53 ASN HA H 1 4.72 . . 1 . . . . . . . . 915 1 264 . 1 1 53 53 ASN HB2 H 1 2.7 . . 2 . . . . . . . . 915 1 265 . 1 1 53 53 ASN HB3 H 1 2.85 . . 2 . . . . . . . . 915 1 266 . 1 1 53 53 ASN N N 15 117.3 . . 1 . . . . . . . . 915 1 267 . 1 1 54 54 CYS H H 1 9.28 . . 1 . . . . . . . . 915 1 268 . 1 1 54 54 CYS HA H 1 4.5 . . 1 . . . . . . . . 915 1 269 . 1 1 54 54 CYS HB2 H 1 3.05 . . 1 . . . . . . . . 915 1 270 . 1 1 54 54 CYS HB3 H 1 3.05 . . 1 . . . . . . . . 915 1 271 . 1 1 54 54 CYS N N 15 126.5 . . 1 . . . . . . . . 915 1 272 . 1 1 55 55 ASN H H 1 9.45 . . 1 . . . . . . . . 915 1 273 . 1 1 55 55 ASN HA H 1 4.32 . . 1 . . . . . . . . 915 1 274 . 1 1 55 55 ASN HB2 H 1 2.57 . . 2 . . . . . . . . 915 1 275 . 1 1 55 55 ASN HB3 H 1 3.14 . . 2 . . . . . . . . 915 1 276 . 1 1 55 55 ASN N N 15 121.4 . . 1 . . . . . . . . 915 1 277 . 1 1 56 56 GLY H H 1 9.1 . . 1 . . . . . . . . 915 1 278 . 1 1 56 56 GLY HA2 H 1 3.31 . . 2 . . . . . . . . 915 1 279 . 1 1 56 56 GLY HA3 H 1 4.09 . . 2 . . . . . . . . 915 1 280 . 1 1 56 56 GLY N N 15 103.1 . . 1 . . . . . . . . 915 1 281 . 1 1 57 57 VAL H H 1 7.54 . . 1 . . . . . . . . 915 1 282 . 1 1 57 57 VAL HA H 1 5.18 . . 1 . . . . . . . . 915 1 283 . 1 1 57 57 VAL HB H 1 1.96 . . 1 . . . . . . . . 915 1 284 . 1 1 57 57 VAL HG11 H 1 .99 . . 1 . . . . . . . . 915 1 285 . 1 1 57 57 VAL HG12 H 1 .99 . . 1 . . . . . . . . 915 1 286 . 1 1 57 57 VAL HG13 H 1 .99 . . 1 . . . . . . . . 915 1 287 . 1 1 57 57 VAL HG21 H 1 .99 . . 1 . . . . . . . . 915 1 288 . 1 1 57 57 VAL HG22 H 1 .99 . . 1 . . . . . . . . 915 1 289 . 1 1 57 57 VAL HG23 H 1 .99 . . 1 . . . . . . . . 915 1 290 . 1 1 57 57 VAL N N 15 121.7 . . 1 . . . . . . . . 915 1 291 . 1 1 58 58 ILE H H 1 8.6 . . 1 . . . . . . . . 915 1 292 . 1 1 58 58 ILE HA H 1 4.9 . . 1 . . . . . . . . 915 1 293 . 1 1 58 58 ILE N N 15 117.8 . . 1 . . . . . . . . 915 1 294 . 1 1 59 59 THR H H 1 8.76 . . 1 . . . . . . . . 915 1 295 . 1 1 59 59 THR HA H 1 4.64 . . 1 . . . . . . . . 915 1 296 . 1 1 59 59 THR N N 15 110.2 . . 1 . . . . . . . . 915 1 297 . 1 1 60 60 LYS H H 1 9.17 . . 1 . . . . . . . . 915 1 298 . 1 1 60 60 LYS HA H 1 3.88 . . 1 . . . . . . . . 915 1 299 . 1 1 60 60 LYS N N 15 122.6 . . 1 . . . . . . . . 915 1 300 . 1 1 61 61 ASP H H 1 8.29 . . 1 . . . . . . . . 915 1 301 . 1 1 61 61 ASP HA H 1 4.38 . . 1 . . . . . . . . 915 1 302 . 1 1 61 61 ASP HB2 H 1 2.6 . . 1 . . . . . . . . 915 1 303 . 1 1 61 61 ASP HB3 H 1 2.6 . . 1 . . . . . . . . 915 1 304 . 1 1 61 61 ASP N N 15 118.6 . . 1 . . . . . . . . 915 1 305 . 1 1 62 62 GLU H H 1 7.73 . . 1 . . . . . . . . 915 1 306 . 1 1 62 62 GLU HA H 1 3.9 . . 1 . . . . . . . . 915 1 307 . 1 1 62 62 GLU HB2 H 1 2.58 . . 1 . . . . . . . . 915 1 308 . 1 1 62 62 GLU HB3 H 1 2.58 . . 1 . . . . . . . . 915 1 309 . 1 1 62 62 GLU N N 15 122.9 . . 1 . . . . . . . . 915 1 310 . 1 1 63 63 ALA H H 1 8.57 . . 1 . . . . . . . . 915 1 311 . 1 1 63 63 ALA HA H 1 3.91 . . 1 . . . . . . . . 915 1 312 . 1 1 63 63 ALA HB1 H 1 1.51 . . 1 . . . . . . . . 915 1 313 . 1 1 63 63 ALA HB2 H 1 1.51 . . 1 . . . . . . . . 915 1 314 . 1 1 63 63 ALA HB3 H 1 1.51 . . 1 . . . . . . . . 915 1 315 . 1 1 63 63 ALA N N 15 122.5 . . 1 . . . . . . . . 915 1 316 . 1 1 64 64 GLU H H 1 8.43 . . 1 . . . . . . . . 915 1 317 . 1 1 64 64 GLU HA H 1 3.88 . . 1 . . . . . . . . 915 1 318 . 1 1 64 64 GLU N N 15 121.8 . . 1 . . . . . . . . 915 1 319 . 1 1 65 65 LYS H H 1 7.76 . . 1 . . . . . . . . 915 1 320 . 1 1 65 65 LYS HA H 1 4.12 . . 1 . . . . . . . . 915 1 321 . 1 1 65 65 LYS HB2 H 1 1.98 . . 1 . . . . . . . . 915 1 322 . 1 1 65 65 LYS HB3 H 1 1.98 . . 1 . . . . . . . . 915 1 323 . 1 1 65 65 LYS N N 15 122.5 . . 1 . . . . . . . . 915 1 324 . 1 1 66 66 LEU H H 1 7.83 . . 1 . . . . . . . . 915 1 325 . 1 1 66 66 LEU HA H 1 3.91 . . 1 . . . . . . . . 915 1 326 . 1 1 66 66 LEU HB2 H 1 1.77 . . 1 . . . . . . . . 915 1 327 . 1 1 66 66 LEU HB3 H 1 1.77 . . 1 . . . . . . . . 915 1 328 . 1 1 66 66 LEU N N 15 119.6 . . 1 . . . . . . . . 915 1 329 . 1 1 67 67 PHE H H 1 8.22 . . 1 . . . . . . . . 915 1 330 . 1 1 67 67 PHE HA H 1 5.07 . . 1 . . . . . . . . 915 1 331 . 1 1 67 67 PHE HB2 H 1 3.39 . . 1 . . . . . . . . 915 1 332 . 1 1 67 67 PHE HB3 H 1 3.39 . . 1 . . . . . . . . 915 1 333 . 1 1 67 67 PHE HD1 H 1 7.57 . . 1 . . . . . . . . 915 1 334 . 1 1 67 67 PHE HD2 H 1 7.57 . . 1 . . . . . . . . 915 1 335 . 1 1 67 67 PHE HE1 H 1 7.04 . . 1 . . . . . . . . 915 1 336 . 1 1 67 67 PHE HE2 H 1 7.04 . . 1 . . . . . . . . 915 1 337 . 1 1 67 67 PHE N N 15 120.1 . . 1 . . . . . . . . 915 1 338 . 1 1 68 68 ASN H H 1 8.71 . . 1 . . . . . . . . 915 1 339 . 1 1 68 68 ASN HA H 1 4.29 . . 1 . . . . . . . . 915 1 340 . 1 1 68 68 ASN HB2 H 1 2.93 . . 1 . . . . . . . . 915 1 341 . 1 1 68 68 ASN HB3 H 1 2.93 . . 1 . . . . . . . . 915 1 342 . 1 1 68 68 ASN N N 15 119.3 . . 1 . . . . . . . . 915 1 343 . 1 1 69 69 GLN H H 1 7.65 . . 1 . . . . . . . . 915 1 344 . 1 1 69 69 GLN HA H 1 4.23 . . 1 . . . . . . . . 915 1 345 . 1 1 69 69 GLN HB2 H 1 2.44 . . 1 . . . . . . . . 915 1 346 . 1 1 69 69 GLN HB3 H 1 2.44 . . 1 . . . . . . . . 915 1 347 . 1 1 69 69 GLN N N 15 120 . . 1 . . . . . . . . 915 1 348 . 1 1 70 70 ASP H H 1 8.52 . . 1 . . . . . . . . 915 1 349 . 1 1 70 70 ASP HA H 1 4.64 . . 1 . . . . . . . . 915 1 350 . 1 1 70 70 ASP HB2 H 1 3.22 . . 1 . . . . . . . . 915 1 351 . 1 1 70 70 ASP HB3 H 1 3.22 . . 1 . . . . . . . . 915 1 352 . 1 1 70 70 ASP N N 15 124.6 . . 1 . . . . . . . . 915 1 353 . 1 1 71 71 VAL H H 1 9.2 . . 1 . . . . . . . . 915 1 354 . 1 1 71 71 VAL HA H 1 3.64 . . 1 . . . . . . . . 915 1 355 . 1 1 71 71 VAL HB H 1 1.94 . . 1 . . . . . . . . 915 1 356 . 1 1 71 71 VAL HG11 H 1 .47 . . 2 . . . . . . . . 915 1 357 . 1 1 71 71 VAL HG12 H 1 .47 . . 2 . . . . . . . . 915 1 358 . 1 1 71 71 VAL HG13 H 1 .47 . . 2 . . . . . . . . 915 1 359 . 1 1 71 71 VAL HG21 H 1 .84 . . 2 . . . . . . . . 915 1 360 . 1 1 71 71 VAL HG22 H 1 .84 . . 2 . . . . . . . . 915 1 361 . 1 1 71 71 VAL HG23 H 1 .84 . . 2 . . . . . . . . 915 1 362 . 1 1 71 71 VAL N N 15 126.2 . . 1 . . . . . . . . 915 1 363 . 1 1 72 72 ASP H H 1 7.75 . . 1 . . . . . . . . 915 1 364 . 1 1 72 72 ASP HA H 1 4.38 . . 1 . . . . . . . . 915 1 365 . 1 1 72 72 ASP HB2 H 1 2.87 . . 1 . . . . . . . . 915 1 366 . 1 1 72 72 ASP HB3 H 1 2.87 . . 1 . . . . . . . . 915 1 367 . 1 1 72 72 ASP N N 15 120.8 . . 1 . . . . . . . . 915 1 368 . 1 1 73 73 ALA H H 1 8.1 . . 1 . . . . . . . . 915 1 369 . 1 1 73 73 ALA HA H 1 4.04 . . 1 . . . . . . . . 915 1 370 . 1 1 73 73 ALA HB1 H 1 1.58 . . 1 . . . . . . . . 915 1 371 . 1 1 73 73 ALA HB2 H 1 1.58 . . 1 . . . . . . . . 915 1 372 . 1 1 73 73 ALA HB3 H 1 1.58 . . 1 . . . . . . . . 915 1 373 . 1 1 73 73 ALA N N 15 121.2 . . 1 . . . . . . . . 915 1 374 . 1 1 74 74 ALA H H 1 8.18 . . 1 . . . . . . . . 915 1 375 . 1 1 74 74 ALA HA H 1 4.19 . . 1 . . . . . . . . 915 1 376 . 1 1 74 74 ALA HB1 H 1 1.5 . . 1 . . . . . . . . 915 1 377 . 1 1 74 74 ALA HB2 H 1 1.5 . . 1 . . . . . . . . 915 1 378 . 1 1 74 74 ALA HB3 H 1 1.5 . . 1 . . . . . . . . 915 1 379 . 1 1 74 74 ALA N N 15 124.6 . . 1 . . . . . . . . 915 1 380 . 1 1 75 75 VAL H H 1 8.59 . . 1 . . . . . . . . 915 1 381 . 1 1 75 75 VAL HA H 1 3.26 . . 1 . . . . . . . . 915 1 382 . 1 1 75 75 VAL HB H 1 2.16 . . 1 . . . . . . . . 915 1 383 . 1 1 75 75 VAL HG11 H 1 .78 . . 2 . . . . . . . . 915 1 384 . 1 1 75 75 VAL HG12 H 1 .78 . . 2 . . . . . . . . 915 1 385 . 1 1 75 75 VAL HG13 H 1 .78 . . 2 . . . . . . . . 915 1 386 . 1 1 75 75 VAL HG21 H 1 1.05 . . 2 . . . . . . . . 915 1 387 . 1 1 75 75 VAL HG22 H 1 1.05 . . 2 . . . . . . . . 915 1 388 . 1 1 75 75 VAL HG23 H 1 1.05 . . 2 . . . . . . . . 915 1 389 . 1 1 75 75 VAL N N 15 120.7 . . 1 . . . . . . . . 915 1 390 . 1 1 76 76 ARG H H 1 8.22 . . 1 . . . . . . . . 915 1 391 . 1 1 76 76 ARG HA H 1 3.82 . . 1 . . . . . . . . 915 1 392 . 1 1 76 76 ARG HB2 H 1 1.9 . . 1 . . . . . . . . 915 1 393 . 1 1 76 76 ARG HB3 H 1 1.9 . . 1 . . . . . . . . 915 1 394 . 1 1 76 76 ARG N N 15 119 . . 1 . . . . . . . . 915 1 395 . 1 1 77 77 GLY H H 1 7.92 . . 1 . . . . . . . . 915 1 396 . 1 1 77 77 GLY HA2 H 1 3.7 . . 2 . . . . . . . . 915 1 397 . 1 1 77 77 GLY HA3 H 1 3.86 . . 2 . . . . . . . . 915 1 398 . 1 1 77 77 GLY N N 15 106.8 . . 1 . . . . . . . . 915 1 399 . 1 1 78 78 ILE H H 1 7.96 . . 1 . . . . . . . . 915 1 400 . 1 1 78 78 ILE HA H 1 3.35 . . 1 . . . . . . . . 915 1 401 . 1 1 78 78 ILE HB H 1 1.79 . . 1 . . . . . . . . 915 1 402 . 1 1 78 78 ILE N N 15 123.9 . . 1 . . . . . . . . 915 1 403 . 1 1 79 79 LEU H H 1 7.93 . . 1 . . . . . . . . 915 1 404 . 1 1 79 79 LEU HA H 1 3.8 . . 1 . . . . . . . . 915 1 405 . 1 1 79 79 LEU N N 15 115.3 . . 1 . . . . . . . . 915 1 406 . 1 1 80 80 ARG H H 1 7.46 . . 1 . . . . . . . . 915 1 407 . 1 1 80 80 ARG HA H 1 4.36 . . 1 . . . . . . . . 915 1 408 . 1 1 80 80 ARG HB2 H 1 1.86 . . 1 . . . . . . . . 915 1 409 . 1 1 80 80 ARG HB3 H 1 1.86 . . 1 . . . . . . . . 915 1 410 . 1 1 80 80 ARG N N 15 117.3 . . 1 . . . . . . . . 915 1 411 . 1 1 81 81 ASN H H 1 7.63 . . 1 . . . . . . . . 915 1 412 . 1 1 81 81 ASN HA H 1 4.76 . . 1 . . . . . . . . 915 1 413 . 1 1 81 81 ASN N N 15 123 . . 1 . . . . . . . . 915 1 414 . 1 1 82 82 ALA H H 1 9.01 . . 1 . . . . . . . . 915 1 415 . 1 1 82 82 ALA HA H 1 4.1 . . 1 . . . . . . . . 915 1 416 . 1 1 82 82 ALA HB1 H 1 1.48 . . 1 . . . . . . . . 915 1 417 . 1 1 82 82 ALA HB2 H 1 1.48 . . 1 . . . . . . . . 915 1 418 . 1 1 82 82 ALA HB3 H 1 1.48 . . 1 . . . . . . . . 915 1 419 . 1 1 82 82 ALA N N 15 130.3 . . 1 . . . . . . . . 915 1 420 . 1 1 83 83 LYS H H 1 8.22 . . 1 . . . . . . . . 915 1 421 . 1 1 83 83 LYS HA H 1 4.34 . . 1 . . . . . . . . 915 1 422 . 1 1 83 83 LYS HB2 H 1 1.91 . . 1 . . . . . . . . 915 1 423 . 1 1 83 83 LYS HB3 H 1 1.91 . . 1 . . . . . . . . 915 1 424 . 1 1 83 83 LYS N N 15 114.8 . . 1 . . . . . . . . 915 1 425 . 1 1 84 84 LEU H H 1 7.9 . . 1 . . . . . . . . 915 1 426 . 1 1 84 84 LEU HA H 1 4.41 . . 1 . . . . . . . . 915 1 427 . 1 1 84 84 LEU HB2 H 1 2.16 . . 1 . . . . . . . . 915 1 428 . 1 1 84 84 LEU HB3 H 1 2.16 . . 1 . . . . . . . . 915 1 429 . 1 1 84 84 LEU N N 15 117 . . 1 . . . . . . . . 915 1 430 . 1 1 85 85 LYS H H 1 8.87 . . 1 . . . . . . . . 915 1 431 . 1 1 85 85 LYS HA H 1 3.88 . . 1 . . . . . . . . 915 1 432 . 1 1 85 85 LYS N N 15 124.3 . . 1 . . . . . . . . 915 1 433 . 1 1 87 87 VAL H H 1 6.8 . . 1 . . . . . . . . 915 1 434 . 1 1 87 87 VAL HA H 1 3.51 . . 1 . . . . . . . . 915 1 435 . 1 1 87 87 VAL HB H 1 2.28 . . 1 . . . . . . . . 915 1 436 . 1 1 87 87 VAL HG11 H 1 .95 . . 2 . . . . . . . . 915 1 437 . 1 1 87 87 VAL HG12 H 1 .95 . . 2 . . . . . . . . 915 1 438 . 1 1 87 87 VAL HG13 H 1 .95 . . 2 . . . . . . . . 915 1 439 . 1 1 87 87 VAL HG21 H 1 1.11 . . 2 . . . . . . . . 915 1 440 . 1 1 87 87 VAL HG22 H 1 1.11 . . 2 . . . . . . . . 915 1 441 . 1 1 87 87 VAL HG23 H 1 1.11 . . 2 . . . . . . . . 915 1 442 . 1 1 87 87 VAL N N 15 117 . . 1 . . . . . . . . 915 1 443 . 1 1 88 88 TYR H H 1 8.43 . . 1 . . . . . . . . 915 1 444 . 1 1 88 88 TYR HA H 1 3.72 . . 1 . . . . . . . . 915 1 445 . 1 1 88 88 TYR HB2 H 1 3.13 . . 1 . . . . . . . . 915 1 446 . 1 1 88 88 TYR HB3 H 1 3.13 . . 1 . . . . . . . . 915 1 447 . 1 1 88 88 TYR HD1 H 1 7.03 . . 1 . . . . . . . . 915 1 448 . 1 1 88 88 TYR HD2 H 1 7.03 . . 1 . . . . . . . . 915 1 449 . 1 1 88 88 TYR HE1 H 1 6.73 . . 1 . . . . . . . . 915 1 450 . 1 1 88 88 TYR HE2 H 1 6.73 . . 1 . . . . . . . . 915 1 451 . 1 1 88 88 TYR N N 15 123 . . 1 . . . . . . . . 915 1 452 . 1 1 89 89 ASP H H 1 9.21 . . 1 . . . . . . . . 915 1 453 . 1 1 89 89 ASP HA H 1 4.31 . . 1 . . . . . . . . 915 1 454 . 1 1 89 89 ASP HB2 H 1 2.68 . . 1 . . . . . . . . 915 1 455 . 1 1 89 89 ASP HB3 H 1 2.68 . . 1 . . . . . . . . 915 1 456 . 1 1 89 89 ASP N N 15 118.8 . . 1 . . . . . . . . 915 1 457 . 1 1 90 90 SER H H 1 7.34 . . 1 . . . . . . . . 915 1 458 . 1 1 90 90 SER HA H 1 4.44 . . 1 . . . . . . . . 915 1 459 . 1 1 90 90 SER HB2 H 1 4.12 . . 1 . . . . . . . . 915 1 460 . 1 1 90 90 SER HB3 H 1 4.12 . . 1 . . . . . . . . 915 1 461 . 1 1 90 90 SER N N 15 114 . . 1 . . . . . . . . 915 1 462 . 1 1 91 91 LEU H H 1 7.3 . . 1 . . . . . . . . 915 1 463 . 1 1 91 91 LEU HA H 1 4.47 . . 1 . . . . . . . . 915 1 464 . 1 1 91 91 LEU HB2 H 1 2.34 . . 1 . . . . . . . . 915 1 465 . 1 1 91 91 LEU HB3 H 1 2.34 . . 1 . . . . . . . . 915 1 466 . 1 1 91 91 LEU N N 15 123.3 . . 1 . . . . . . . . 915 1 467 . 1 1 92 92 ASP H H 1 7.36 . . 1 . . . . . . . . 915 1 468 . 1 1 92 92 ASP HA H 1 4.64 . . 1 . . . . . . . . 915 1 469 . 1 1 92 92 ASP N N 15 115.7 . . 1 . . . . . . . . 915 1 470 . 1 1 93 93 ALA H H 1 8.72 . . 1 . . . . . . . . 915 1 471 . 1 1 93 93 ALA HA H 1 3.83 . . 1 . . . . . . . . 915 1 472 . 1 1 93 93 ALA HB1 H 1 1.55 . . 1 . . . . . . . . 915 1 473 . 1 1 93 93 ALA HB2 H 1 1.55 . . 1 . . . . . . . . 915 1 474 . 1 1 93 93 ALA HB3 H 1 1.55 . . 1 . . . . . . . . 915 1 475 . 1 1 93 93 ALA N N 15 120.8 . . 1 . . . . . . . . 915 1 476 . 1 1 94 94 VAL H H 1 7.77 . . 1 . . . . . . . . 915 1 477 . 1 1 94 94 VAL HA H 1 3.18 . . 1 . . . . . . . . 915 1 478 . 1 1 94 94 VAL HB H 1 1.32 . . 1 . . . . . . . . 915 1 479 . 1 1 94 94 VAL HG11 H 1 .78 . . 2 . . . . . . . . 915 1 480 . 1 1 94 94 VAL HG12 H 1 .78 . . 2 . . . . . . . . 915 1 481 . 1 1 94 94 VAL HG13 H 1 .78 . . 2 . . . . . . . . 915 1 482 . 1 1 94 94 VAL HG21 H 1 .56 . . 2 . . . . . . . . 915 1 483 . 1 1 94 94 VAL HG22 H 1 .56 . . 2 . . . . . . . . 915 1 484 . 1 1 94 94 VAL HG23 H 1 .56 . . 2 . . . . . . . . 915 1 485 . 1 1 94 94 VAL N N 15 118.8 . . 1 . . . . . . . . 915 1 486 . 1 1 95 95 ARG H H 1 7.94 . . 1 . . . . . . . . 915 1 487 . 1 1 95 95 ARG HA H 1 3.39 . . 1 . . . . . . . . 915 1 488 . 1 1 95 95 ARG HB2 H 1 1.64 . . 1 . . . . . . . . 915 1 489 . 1 1 95 95 ARG HB3 H 1 1.64 . . 1 . . . . . . . . 915 1 490 . 1 1 95 95 ARG N N 15 120.1 . . 1 . . . . . . . . 915 1 491 . 1 1 96 96 ARG H H 1 8.77 . . 1 . . . . . . . . 915 1 492 . 1 1 96 96 ARG HA H 1 3.7 . . 1 . . . . . . . . 915 1 493 . 1 1 96 96 ARG N N 15 119.4 . . 1 . . . . . . . . 915 1 494 . 1 1 97 97 CYS H H 1 7.3 . . 1 . . . . . . . . 915 1 495 . 1 1 97 97 CYS HA H 1 4.08 . . 1 . . . . . . . . 915 1 496 . 1 1 97 97 CYS N N 15 116.4 . . 1 . . . . . . . . 915 1 497 . 1 1 98 98 ALA H H 1 6.89 . . 1 . . . . . . . . 915 1 498 . 1 1 98 98 ALA HA H 1 3.68 . . 1 . . . . . . . . 915 1 499 . 1 1 98 98 ALA HB1 H 1 .41 . . 1 . . . . . . . . 915 1 500 . 1 1 98 98 ALA HB2 H 1 .41 . . 1 . . . . . . . . 915 1 501 . 1 1 98 98 ALA HB3 H 1 .41 . . 1 . . . . . . . . 915 1 502 . 1 1 98 98 ALA N N 15 122.2 . . 1 . . . . . . . . 915 1 503 . 1 1 99 99 LEU H H 1 7.41 . . 1 . . . . . . . . 915 1 504 . 1 1 99 99 LEU HA H 1 4.22 . . 1 . . . . . . . . 915 1 505 . 1 1 99 99 LEU HB2 H 1 2.29 . . 1 . . . . . . . . 915 1 506 . 1 1 99 99 LEU HB3 H 1 2.29 . . 1 . . . . . . . . 915 1 507 . 1 1 99 99 LEU N N 15 119.9 . . 1 . . . . . . . . 915 1 508 . 1 1 100 100 ILE H H 1 8.55 . . 1 . . . . . . . . 915 1 509 . 1 1 100 100 ILE HA H 1 3.42 . . 1 . . . . . . . . 915 1 510 . 1 1 100 100 ILE HB H 1 1.87 . . 1 . . . . . . . . 915 1 511 . 1 1 100 100 ILE N N 15 119.7 . . 1 . . . . . . . . 915 1 512 . 1 1 101 101 ASN H H 1 8.28 . . 1 . . . . . . . . 915 1 513 . 1 1 101 101 ASN HA H 1 4.06 . . 1 . . . . . . . . 915 1 514 . 1 1 101 101 ASN N N 15 119.9 . . 1 . . . . . . . . 915 1 515 . 1 1 102 102 MET H H 1 7.58 . . 1 . . . . . . . . 915 1 516 . 1 1 102 102 MET HA H 1 4.36 . . 1 . . . . . . . . 915 1 517 . 1 1 102 102 MET HB2 H 1 2.19 . . 1 . . . . . . . . 915 1 518 . 1 1 102 102 MET HB3 H 1 2.19 . . 1 . . . . . . . . 915 1 519 . 1 1 102 102 MET N N 15 116.4 . . 1 . . . . . . . . 915 1 520 . 1 1 103 103 VAL H H 1 8.1 . . 1 . . . . . . . . 915 1 521 . 1 1 103 103 VAL HA H 1 3.32 . . 1 . . . . . . . . 915 1 522 . 1 1 103 103 VAL HB H 1 2.22 . . 1 . . . . . . . . 915 1 523 . 1 1 103 103 VAL HG11 H 1 .9 . . 1 . . . . . . . . 915 1 524 . 1 1 103 103 VAL HG12 H 1 .9 . . 1 . . . . . . . . 915 1 525 . 1 1 103 103 VAL HG13 H 1 .9 . . 1 . . . . . . . . 915 1 526 . 1 1 103 103 VAL HG21 H 1 .9 . . 1 . . . . . . . . 915 1 527 . 1 1 103 103 VAL HG22 H 1 .9 . . 1 . . . . . . . . 915 1 528 . 1 1 103 103 VAL HG23 H 1 .9 . . 1 . . . . . . . . 915 1 529 . 1 1 103 103 VAL N N 15 121.3 . . 1 . . . . . . . . 915 1 530 . 1 1 104 104 PHE H H 1 9.26 . . 1 . . . . . . . . 915 1 531 . 1 1 104 104 PHE HA H 1 4.13 . . 1 . . . . . . . . 915 1 532 . 1 1 104 104 PHE HB2 H 1 3.24 . . 2 . . . . . . . . 915 1 533 . 1 1 104 104 PHE HB3 H 1 3.39 . . 2 . . . . . . . . 915 1 534 . 1 1 104 104 PHE HD1 H 1 7.31 . . 1 . . . . . . . . 915 1 535 . 1 1 104 104 PHE HD2 H 1 7.31 . . 1 . . . . . . . . 915 1 536 . 1 1 104 104 PHE N N 15 125 . . 1 . . . . . . . . 915 1 537 . 1 1 105 105 GLN H H 1 8.03 . . 1 . . . . . . . . 915 1 538 . 1 1 105 105 GLN HA H 1 4.42 . . 1 . . . . . . . . 915 1 539 . 1 1 105 105 GLN HB2 H 1 2.21 . . 1 . . . . . . . . 915 1 540 . 1 1 105 105 GLN HB3 H 1 2.21 . . 1 . . . . . . . . 915 1 541 . 1 1 105 105 GLN N N 15 118.2 . . 1 . . . . . . . . 915 1 542 . 1 1 106 106 MET H H 1 8.65 . . 1 . . . . . . . . 915 1 543 . 1 1 106 106 MET HA H 1 4.78 . . 1 . . . . . . . . 915 1 544 . 1 1 106 106 MET HB2 H 1 2.15 . . 1 . . . . . . . . 915 1 545 . 1 1 106 106 MET HB3 H 1 2.15 . . 1 . . . . . . . . 915 1 546 . 1 1 106 106 MET N N 15 114.2 . . 1 . . . . . . . . 915 1 547 . 1 1 107 107 GLY H H 1 8.47 . . 1 . . . . . . . . 915 1 548 . 1 1 107 107 GLY HA2 H 1 3.97 . . 2 . . . . . . . . 915 1 549 . 1 1 107 107 GLY HA3 H 1 4.49 . . 2 . . . . . . . . 915 1 550 . 1 1 107 107 GLY N N 15 112.6 . . 1 . . . . . . . . 915 1 551 . 1 1 108 108 GLU H H 1 9.05 . . 1 . . . . . . . . 915 1 552 . 1 1 108 108 GLU HA H 1 3.68 . . 1 . . . . . . . . 915 1 553 . 1 1 108 108 GLU HB2 H 1 1.89 . . 2 . . . . . . . . 915 1 554 . 1 1 108 108 GLU HB3 H 1 2 . . 2 . . . . . . . . 915 1 555 . 1 1 108 108 GLU HG2 H 1 2.24 . . 1 . . . . . . . . 915 1 556 . 1 1 108 108 GLU HG3 H 1 2.24 . . 1 . . . . . . . . 915 1 557 . 1 1 108 108 GLU N N 15 121.2 . . 1 . . . . . . . . 915 1 558 . 1 1 109 109 THR H H 1 8.38 . . 1 . . . . . . . . 915 1 559 . 1 1 109 109 THR HA H 1 3.84 . . 1 . . . . . . . . 915 1 560 . 1 1 109 109 THR HB H 1 4.13 . . 1 . . . . . . . . 915 1 561 . 1 1 109 109 THR HG21 H 1 1.23 . . 1 . . . . . . . . 915 1 562 . 1 1 109 109 THR HG22 H 1 1.23 . . 1 . . . . . . . . 915 1 563 . 1 1 109 109 THR HG23 H 1 1.23 . . 1 . . . . . . . . 915 1 564 . 1 1 109 109 THR N N 15 113.4 . . 1 . . . . . . . . 915 1 565 . 1 1 110 110 GLY H H 1 7.77 . . 1 . . . . . . . . 915 1 566 . 1 1 110 110 GLY HA2 H 1 3.59 . . 2 . . . . . . . . 915 1 567 . 1 1 110 110 GLY HA3 H 1 3.82 . . 2 . . . . . . . . 915 1 568 . 1 1 110 110 GLY N N 15 110.4 . . 1 . . . . . . . . 915 1 569 . 1 1 111 111 VAL H H 1 7.66 . . 1 . . . . . . . . 915 1 570 . 1 1 111 111 VAL HA H 1 3.65 . . 1 . . . . . . . . 915 1 571 . 1 1 111 111 VAL HB H 1 1.85 . . 1 . . . . . . . . 915 1 572 . 1 1 111 111 VAL HG11 H 1 .84 . . 2 . . . . . . . . 915 1 573 . 1 1 111 111 VAL HG12 H 1 .84 . . 2 . . . . . . . . 915 1 574 . 1 1 111 111 VAL HG13 H 1 .84 . . 2 . . . . . . . . 915 1 575 . 1 1 111 111 VAL HG21 H 1 .93 . . 2 . . . . . . . . 915 1 576 . 1 1 111 111 VAL HG22 H 1 .93 . . 2 . . . . . . . . 915 1 577 . 1 1 111 111 VAL HG23 H 1 .93 . . 2 . . . . . . . . 915 1 578 . 1 1 111 111 VAL N N 15 122.9 . . 1 . . . . . . . . 915 1 579 . 1 1 112 112 ALA H H 1 8.13 . . 1 . . . . . . . . 915 1 580 . 1 1 112 112 ALA HA H 1 3.88 . . 1 . . . . . . . . 915 1 581 . 1 1 112 112 ALA HB1 H 1 1.43 . . 1 . . . . . . . . 915 1 582 . 1 1 112 112 ALA HB2 H 1 1.43 . . 1 . . . . . . . . 915 1 583 . 1 1 112 112 ALA HB3 H 1 1.43 . . 1 . . . . . . . . 915 1 584 . 1 1 112 112 ALA N N 15 119.8 . . 1 . . . . . . . . 915 1 585 . 1 1 113 113 GLY H H 1 7.28 . . 1 . . . . . . . . 915 1 586 . 1 1 113 113 GLY HA2 H 1 4.15 . . 2 . . . . . . . . 915 1 587 . 1 1 113 113 GLY HA3 H 1 3.8 . . 2 . . . . . . . . 915 1 588 . 1 1 113 113 GLY N N 15 102.8 . . 1 . . . . . . . . 915 1 589 . 1 1 114 114 PHE H H 1 7.99 . . 1 . . . . . . . . 915 1 590 . 1 1 114 114 PHE HA H 1 5.03 . . 1 . . . . . . . . 915 1 591 . 1 1 114 114 PHE HB2 H 1 3.13 . . 2 . . . . . . . . 915 1 592 . 1 1 114 114 PHE HB3 H 1 3.35 . . 2 . . . . . . . . 915 1 593 . 1 1 114 114 PHE HD1 H 1 7.5 . . 1 . . . . . . . . 915 1 594 . 1 1 114 114 PHE HD2 H 1 7.5 . . 1 . . . . . . . . 915 1 595 . 1 1 114 114 PHE HE1 H 1 7.27 . . 1 . . . . . . . . 915 1 596 . 1 1 114 114 PHE HE2 H 1 7.27 . . 1 . . . . . . . . 915 1 597 . 1 1 114 114 PHE HZ H 1 7.21 . . 1 . . . . . . . . 915 1 598 . 1 1 114 114 PHE N N 15 125.1 . . 1 . . . . . . . . 915 1 599 . 1 1 115 115 THR H H 1 7.87 . . 1 . . . . . . . . 915 1 600 . 1 1 115 115 THR HA H 1 3.69 . . 1 . . . . . . . . 915 1 601 . 1 1 115 115 THR HB H 1 4.07 . . 1 . . . . . . . . 915 1 602 . 1 1 115 115 THR HG21 H 1 1.27 . . 1 . . . . . . . . 915 1 603 . 1 1 115 115 THR HG22 H 1 1.27 . . 1 . . . . . . . . 915 1 604 . 1 1 115 115 THR HG23 H 1 1.27 . . 1 . . . . . . . . 915 1 605 . 1 1 115 115 THR N N 15 115.6 . . 1 . . . . . . . . 915 1 606 . 1 1 116 116 ASN H H 1 8.76 . . 1 . . . . . . . . 915 1 607 . 1 1 116 116 ASN HA H 1 4.54 . . 1 . . . . . . . . 915 1 608 . 1 1 116 116 ASN HB2 H 1 2.71 . . 2 . . . . . . . . 915 1 609 . 1 1 116 116 ASN HB3 H 1 2.98 . . 2 . . . . . . . . 915 1 610 . 1 1 116 116 ASN N N 15 120.2 . . 1 . . . . . . . . 915 1 611 . 1 1 117 117 SER H H 1 8.45 . . 1 . . . . . . . . 915 1 612 . 1 1 117 117 SER HA H 1 4.19 . . 1 . . . . . . . . 915 1 613 . 1 1 117 117 SER HB2 H 1 4 . . 1 . . . . . . . . 915 1 614 . 1 1 117 117 SER HB3 H 1 4 . . 1 . . . . . . . . 915 1 615 . 1 1 117 117 SER N N 15 119.7 . . 1 . . . . . . . . 915 1 616 . 1 1 118 118 LEU H H 1 8.59 . . 1 . . . . . . . . 915 1 617 . 1 1 118 118 LEU HA H 1 3.87 . . 1 . . . . . . . . 915 1 618 . 1 1 118 118 LEU HB2 H 1 1.91 . . 1 . . . . . . . . 915 1 619 . 1 1 118 118 LEU HB3 H 1 1.91 . . 1 . . . . . . . . 915 1 620 . 1 1 118 118 LEU N N 15 121.2 . . 1 . . . . . . . . 915 1 621 . 1 1 119 119 ARG H H 1 7.5 . . 1 . . . . . . . . 915 1 622 . 1 1 119 119 ARG HA H 1 4.08 . . 1 . . . . . . . . 915 1 623 . 1 1 119 119 ARG HB2 H 1 1.96 . . 1 . . . . . . . . 915 1 624 . 1 1 119 119 ARG HB3 H 1 1.96 . . 1 . . . . . . . . 915 1 625 . 1 1 119 119 ARG N N 15 119.9 . . 1 . . . . . . . . 915 1 626 . 1 1 120 120 MET H H 1 7.72 . . 1 . . . . . . . . 915 1 627 . 1 1 120 120 MET HA H 1 3.97 . . 1 . . . . . . . . 915 1 628 . 1 1 120 120 MET N N 15 117.7 . . 1 . . . . . . . . 915 1 629 . 1 1 121 121 LEU H H 1 8.2 . . 1 . . . . . . . . 915 1 630 . 1 1 121 121 LEU HA H 1 3.87 . . 1 . . . . . . . . 915 1 631 . 1 1 121 121 LEU N N 15 119.8 . . 1 . . . . . . . . 915 1 632 . 1 1 122 122 GLN H H 1 8.23 . . 1 . . . . . . . . 915 1 633 . 1 1 122 122 GLN HA H 1 3.98 . . 1 . . . . . . . . 915 1 634 . 1 1 122 122 GLN HB2 H 1 2.28 . . 1 . . . . . . . . 915 1 635 . 1 1 122 122 GLN HB3 H 1 2.28 . . 1 . . . . . . . . 915 1 636 . 1 1 122 122 GLN N N 15 121.9 . . 1 . . . . . . . . 915 1 637 . 1 1 123 123 GLN H H 1 7.33 . . 1 . . . . . . . . 915 1 638 . 1 1 123 123 GLN HA H 1 4.1 . . 1 . . . . . . . . 915 1 639 . 1 1 123 123 GLN HB2 H 1 1.74 . . 1 . . . . . . . . 915 1 640 . 1 1 123 123 GLN HB3 H 1 1.74 . . 1 . . . . . . . . 915 1 641 . 1 1 123 123 GLN N N 15 114.8 . . 1 . . . . . . . . 915 1 642 . 1 1 124 124 LYS H H 1 7.42 . . 1 . . . . . . . . 915 1 643 . 1 1 124 124 LYS HA H 1 1.4 . . 1 . . . . . . . . 915 1 644 . 1 1 124 124 LYS N N 15 115.6 . . 1 . . . . . . . . 915 1 645 . 1 1 125 125 ARG H H 1 7.77 . . 1 . . . . . . . . 915 1 646 . 1 1 125 125 ARG HA H 1 4.24 . . 1 . . . . . . . . 915 1 647 . 1 1 125 125 ARG HB2 H 1 1.42 . . 1 . . . . . . . . 915 1 648 . 1 1 125 125 ARG HB3 H 1 1.42 . . 1 . . . . . . . . 915 1 649 . 1 1 125 125 ARG N N 15 121.2 . . 1 . . . . . . . . 915 1 650 . 1 1 126 126 TRP H H 1 6.76 . . 1 . . . . . . . . 915 1 651 . 1 1 126 126 TRP HA H 1 4.35 . . 1 . . . . . . . . 915 1 652 . 1 1 126 126 TRP HB2 H 1 3.27 . . 2 . . . . . . . . 915 1 653 . 1 1 126 126 TRP HB3 H 1 3.87 . . 2 . . . . . . . . 915 1 654 . 1 1 126 126 TRP NE1 N 15 132 . . 1 . . . . . . . . 915 1 655 . 1 1 126 126 TRP HD1 H 1 7.42 . . 1 . . . . . . . . 915 1 656 . 1 1 126 126 TRP HE1 H 1 10.38 . . 1 . . . . . . . . 915 1 657 . 1 1 126 126 TRP HE3 H 1 7.26 . . 1 . . . . . . . . 915 1 658 . 1 1 126 126 TRP HZ2 H 1 7.58 . . 1 . . . . . . . . 915 1 659 . 1 1 126 126 TRP HZ3 H 1 6.92 . . 1 . . . . . . . . 915 1 660 . 1 1 126 126 TRP HH2 H 1 7.35 . . 1 . . . . . . . . 915 1 661 . 1 1 126 126 TRP N N 15 119.8 . . 1 . . . . . . . . 915 1 662 . 1 1 127 127 ASP H H 1 8.59 . . 1 . . . . . . . . 915 1 663 . 1 1 127 127 ASP HA H 1 4.43 . . 1 . . . . . . . . 915 1 664 . 1 1 127 127 ASP HB2 H 1 2.72 . . 1 . . . . . . . . 915 1 665 . 1 1 127 127 ASP HB3 H 1 2.72 . . 1 . . . . . . . . 915 1 666 . 1 1 127 127 ASP N N 15 117.8 . . 1 . . . . . . . . 915 1 667 . 1 1 128 128 GLU H H 1 8.33 . . 1 . . . . . . . . 915 1 668 . 1 1 128 128 GLU HA H 1 3.97 . . 1 . . . . . . . . 915 1 669 . 1 1 128 128 GLU HB2 H 1 2.11 . . 1 . . . . . . . . 915 1 670 . 1 1 128 128 GLU HB3 H 1 2.11 . . 1 . . . . . . . . 915 1 671 . 1 1 128 128 GLU N N 15 121.8 . . 1 . . . . . . . . 915 1 672 . 1 1 129 129 ALA H H 1 8.66 . . 1 . . . . . . . . 915 1 673 . 1 1 129 129 ALA HA H 1 4 . . 1 . . . . . . . . 915 1 674 . 1 1 129 129 ALA HB1 H 1 1.32 . . 1 . . . . . . . . 915 1 675 . 1 1 129 129 ALA HB2 H 1 1.32 . . 1 . . . . . . . . 915 1 676 . 1 1 129 129 ALA HB3 H 1 1.32 . . 1 . . . . . . . . 915 1 677 . 1 1 129 129 ALA N N 15 123.6 . . 1 . . . . . . . . 915 1 678 . 1 1 130 130 ALA H H 1 8.2 . . 1 . . . . . . . . 915 1 679 . 1 1 130 130 ALA HA H 1 4.07 . . 1 . . . . . . . . 915 1 680 . 1 1 130 130 ALA HB1 H 1 1.59 . . 1 . . . . . . . . 915 1 681 . 1 1 130 130 ALA HB2 H 1 1.59 . . 1 . . . . . . . . 915 1 682 . 1 1 130 130 ALA HB3 H 1 1.59 . . 1 . . . . . . . . 915 1 683 . 1 1 130 130 ALA N N 15 120 . . 1 . . . . . . . . 915 1 684 . 1 1 131 131 VAL H H 1 7.82 . . 1 . . . . . . . . 915 1 685 . 1 1 131 131 VAL HA H 1 3.6 . . 1 . . . . . . . . 915 1 686 . 1 1 131 131 VAL HB H 1 2.13 . . 1 . . . . . . . . 915 1 687 . 1 1 131 131 VAL HG11 H 1 .92 . . 2 . . . . . . . . 915 1 688 . 1 1 131 131 VAL HG12 H 1 .92 . . 2 . . . . . . . . 915 1 689 . 1 1 131 131 VAL HG13 H 1 .92 . . 2 . . . . . . . . 915 1 690 . 1 1 131 131 VAL HG21 H 1 1.09 . . 2 . . . . . . . . 915 1 691 . 1 1 131 131 VAL HG22 H 1 1.09 . . 2 . . . . . . . . 915 1 692 . 1 1 131 131 VAL HG23 H 1 1.09 . . 2 . . . . . . . . 915 1 693 . 1 1 131 131 VAL N N 15 119.3 . . 1 . . . . . . . . 915 1 694 . 1 1 132 132 ASN H H 1 7.74 . . 1 . . . . . . . . 915 1 695 . 1 1 132 132 ASN HA H 1 4.33 . . 1 . . . . . . . . 915 1 696 . 1 1 132 132 ASN HB2 H 1 2.77 . . 1 . . . . . . . . 915 1 697 . 1 1 132 132 ASN HB3 H 1 2.77 . . 1 . . . . . . . . 915 1 698 . 1 1 132 132 ASN N N 15 119.4 . . 1 . . . . . . . . 915 1 699 . 1 1 133 133 LEU H H 1 9.01 . . 1 . . . . . . . . 915 1 700 . 1 1 133 133 LEU HA H 1 4.2 . . 1 . . . . . . . . 915 1 701 . 1 1 133 133 LEU HB2 H 1 2.09 . . 1 . . . . . . . . 915 1 702 . 1 1 133 133 LEU HB3 H 1 2.09 . . 1 . . . . . . . . 915 1 703 . 1 1 133 133 LEU N N 15 123.2 . . 1 . . . . . . . . 915 1 704 . 1 1 134 134 ALA H H 1 7.39 . . 1 . . . . . . . . 915 1 705 . 1 1 134 134 ALA HA H 1 3.67 . . 1 . . . . . . . . 915 1 706 . 1 1 134 134 ALA HB1 H 1 .9 . . 1 . . . . . . . . 915 1 707 . 1 1 134 134 ALA HB2 H 1 .9 . . 1 . . . . . . . . 915 1 708 . 1 1 134 134 ALA HB3 H 1 .9 . . 1 . . . . . . . . 915 1 709 . 1 1 134 134 ALA N N 15 120.6 . . 1 . . . . . . . . 915 1 710 . 1 1 135 135 LYS H H 1 7.18 . . 1 . . . . . . . . 915 1 711 . 1 1 135 135 LYS HA H 1 4.42 . . 1 . . . . . . . . 915 1 712 . 1 1 135 135 LYS HB2 H 1 1.84 . . 1 . . . . . . . . 915 1 713 . 1 1 135 135 LYS HB3 H 1 1.84 . . 1 . . . . . . . . 915 1 714 . 1 1 135 135 LYS N N 15 119.3 . . 1 . . . . . . . . 915 1 715 . 1 1 136 136 SER H H 1 7.56 . . 1 . . . . . . . . 915 1 716 . 1 1 136 136 SER HA H 1 4.66 . . 1 . . . . . . . . 915 1 717 . 1 1 136 136 SER HB2 H 1 4.79 . . 1 . . . . . . . . 915 1 718 . 1 1 136 136 SER HB3 H 1 4.79 . . 1 . . . . . . . . 915 1 719 . 1 1 136 136 SER N N 15 114.4 . . 1 . . . . . . . . 915 1 720 . 1 1 137 137 ARG H H 1 8.96 . . 1 . . . . . . . . 915 1 721 . 1 1 137 137 ARG HA H 1 4.26 . . 1 . . . . . . . . 915 1 722 . 1 1 137 137 ARG HB2 H 1 2.02 . . 1 . . . . . . . . 915 1 723 . 1 1 137 137 ARG HB3 H 1 2.02 . . 1 . . . . . . . . 915 1 724 . 1 1 137 137 ARG N N 15 124.2 . . 1 . . . . . . . . 915 1 725 . 1 1 138 138 TRP H H 1 8.17 . . 1 . . . . . . . . 915 1 726 . 1 1 138 138 TRP HA H 1 4.55 . . 1 . . . . . . . . 915 1 727 . 1 1 138 138 TRP HB2 H 1 3.59 . . 2 . . . . . . . . 915 1 728 . 1 1 138 138 TRP HB3 H 1 3.68 . . 2 . . . . . . . . 915 1 729 . 1 1 138 138 TRP NE1 N 15 131.4 . . 1 . . . . . . . . 915 1 730 . 1 1 138 138 TRP HD1 H 1 7.3 . . 1 . . . . . . . . 915 1 731 . 1 1 138 138 TRP HE1 H 1 10.21 . . 1 . . . . . . . . 915 1 732 . 1 1 138 138 TRP HE3 H 1 7.78 . . 1 . . . . . . . . 915 1 733 . 1 1 138 138 TRP HZ2 H 1 7.66 . . 1 . . . . . . . . 915 1 734 . 1 1 138 138 TRP HZ3 H 1 6.95 . . 1 . . . . . . . . 915 1 735 . 1 1 138 138 TRP HH2 H 1 7.16 . . 1 . . . . . . . . 915 1 736 . 1 1 138 138 TRP N N 15 121.7 . . 1 . . . . . . . . 915 1 737 . 1 1 139 139 TYR H H 1 7.6 . . 1 . . . . . . . . 915 1 738 . 1 1 139 139 TYR HD1 H 1 6.71 . . 1 . . . . . . . . 915 1 739 . 1 1 139 139 TYR HD2 H 1 6.71 . . 1 . . . . . . . . 915 1 740 . 1 1 139 139 TYR HE1 H 1 6.63 . . 1 . . . . . . . . 915 1 741 . 1 1 139 139 TYR HE2 H 1 6.63 . . 1 . . . . . . . . 915 1 742 . 1 1 139 139 TYR N N 15 119 . . 1 . . . . . . . . 915 1 743 . 1 1 140 140 ASN H H 1 7.27 . . 1 . . . . . . . . 915 1 744 . 1 1 140 140 ASN HA H 1 4.37 . . 1 . . . . . . . . 915 1 745 . 1 1 140 140 ASN HB2 H 1 2.84 . . 2 . . . . . . . . 915 1 746 . 1 1 140 140 ASN HB3 H 1 2.89 . . 2 . . . . . . . . 915 1 747 . 1 1 140 140 ASN N N 15 112 . . 1 . . . . . . . . 915 1 748 . 1 1 141 141 GLN H H 1 8.32 . . 1 . . . . . . . . 915 1 749 . 1 1 141 141 GLN HA H 1 4.22 . . 1 . . . . . . . . 915 1 750 . 1 1 141 141 GLN HB2 H 1 2.22 . . 2 . . . . . . . . 915 1 751 . 1 1 141 141 GLN HB3 H 1 2.37 . . 2 . . . . . . . . 915 1 752 . 1 1 141 141 GLN N N 15 119.6 . . 1 . . . . . . . . 915 1 753 . 1 1 142 142 THR H H 1 7.62 . . 1 . . . . . . . . 915 1 754 . 1 1 142 142 THR HA H 1 4.74 . . 1 . . . . . . . . 915 1 755 . 1 1 142 142 THR HB H 1 4.51 . . 1 . . . . . . . . 915 1 756 . 1 1 142 142 THR HG21 H 1 1.17 . . 1 . . . . . . . . 915 1 757 . 1 1 142 142 THR HG22 H 1 1.17 . . 1 . . . . . . . . 915 1 758 . 1 1 142 142 THR HG23 H 1 1.17 . . 1 . . . . . . . . 915 1 759 . 1 1 142 142 THR N N 15 107.7 . . 1 . . . . . . . . 915 1 760 . 1 1 144 144 ASN H H 1 8 . . 1 . . . . . . . . 915 1 761 . 1 1 144 144 ASN HA H 1 4.31 . . 1 . . . . . . . . 915 1 762 . 1 1 144 144 ASN HB2 H 1 2.62 . . 1 . . . . . . . . 915 1 763 . 1 1 144 144 ASN HB3 H 1 2.62 . . 1 . . . . . . . . 915 1 764 . 1 1 144 144 ASN N N 15 117.9 . . 1 . . . . . . . . 915 1 765 . 1 1 145 145 ARG H H 1 7.84 . . 1 . . . . . . . . 915 1 766 . 1 1 145 145 ARG HA H 1 3.91 . . 1 . . . . . . . . 915 1 767 . 1 1 145 145 ARG N N 15 122 . . 1 . . . . . . . . 915 1 768 . 1 1 146 146 ALA H H 1 8.07 . . 1 . . . . . . . . 915 1 769 . 1 1 146 146 ALA HA H 1 3.71 . . 1 . . . . . . . . 915 1 770 . 1 1 146 146 ALA HB1 H 1 .02 . . 1 . . . . . . . . 915 1 771 . 1 1 146 146 ALA HB2 H 1 .02 . . 1 . . . . . . . . 915 1 772 . 1 1 146 146 ALA HB3 H 1 .02 . . 1 . . . . . . . . 915 1 773 . 1 1 146 146 ALA N N 15 120.2 . . 1 . . . . . . . . 915 1 774 . 1 1 147 147 LYS H H 1 8.31 . . 1 . . . . . . . . 915 1 775 . 1 1 147 147 LYS HA H 1 3.96 . . 1 . . . . . . . . 915 1 776 . 1 1 147 147 LYS HB2 H 1 1.93 . . 1 . . . . . . . . 915 1 777 . 1 1 147 147 LYS HB3 H 1 1.93 . . 1 . . . . . . . . 915 1 778 . 1 1 147 147 LYS N N 15 116.9 . . 1 . . . . . . . . 915 1 779 . 1 1 148 148 ARG H H 1 7.35 . . 1 . . . . . . . . 915 1 780 . 1 1 148 148 ARG HA H 1 3.8 . . 1 . . . . . . . . 915 1 781 . 1 1 148 148 ARG N N 15 120.6 . . 1 . . . . . . . . 915 1 782 . 1 1 149 149 VAL H H 1 8.59 . . 1 . . . . . . . . 915 1 783 . 1 1 149 149 VAL HA H 1 3.36 . . 1 . . . . . . . . 915 1 784 . 1 1 149 149 VAL HB H 1 2.58 . . 1 . . . . . . . . 915 1 785 . 1 1 149 149 VAL HG11 H 1 1.1 . . 2 . . . . . . . . 915 1 786 . 1 1 149 149 VAL HG12 H 1 1.1 . . 2 . . . . . . . . 915 1 787 . 1 1 149 149 VAL HG13 H 1 1.1 . . 2 . . . . . . . . 915 1 788 . 1 1 149 149 VAL HG21 H 1 1.3 . . 2 . . . . . . . . 915 1 789 . 1 1 149 149 VAL HG22 H 1 1.3 . . 2 . . . . . . . . 915 1 790 . 1 1 149 149 VAL HG23 H 1 1.3 . . 2 . . . . . . . . 915 1 791 . 1 1 149 149 VAL N N 15 126.1 . . 1 . . . . . . . . 915 1 792 . 1 1 150 150 ILE H H 1 9.63 . . 1 . . . . . . . . 915 1 793 . 1 1 150 150 ILE HA H 1 3.9 . . 1 . . . . . . . . 915 1 794 . 1 1 150 150 ILE HB H 1 2.11 . . 1 . . . . . . . . 915 1 795 . 1 1 150 150 ILE N N 15 121.4 . . 1 . . . . . . . . 915 1 796 . 1 1 151 151 THR H H 1 8.67 . . 1 . . . . . . . . 915 1 797 . 1 1 151 151 THR HA H 1 3.95 . . 1 . . . . . . . . 915 1 798 . 1 1 151 151 THR HB H 1 4.24 . . 1 . . . . . . . . 915 1 799 . 1 1 151 151 THR HG21 H 1 1.31 . . 1 . . . . . . . . 915 1 800 . 1 1 151 151 THR HG22 H 1 1.31 . . 1 . . . . . . . . 915 1 801 . 1 1 151 151 THR HG23 H 1 1.31 . . 1 . . . . . . . . 915 1 802 . 1 1 151 151 THR N N 15 118.8 . . 1 . . . . . . . . 915 1 803 . 1 1 152 152 THR H H 1 7.9 . . 1 . . . . . . . . 915 1 804 . 1 1 152 152 THR HA H 1 3.95 . . 1 . . . . . . . . 915 1 805 . 1 1 152 152 THR HB H 1 4.31 . . 1 . . . . . . . . 915 1 806 . 1 1 152 152 THR HG1 H 1 5.54 . . 1 . . . . . . . . 915 1 807 . 1 1 152 152 THR HG21 H 1 .56 . . 1 . . . . . . . . 915 1 808 . 1 1 152 152 THR HG22 H 1 .56 . . 1 . . . . . . . . 915 1 809 . 1 1 152 152 THR HG23 H 1 .56 . . 1 . . . . . . . . 915 1 810 . 1 1 152 152 THR N N 15 123.3 . . 1 . . . . . . . . 915 1 811 . 1 1 153 153 PHE H H 1 8.27 . . 1 . . . . . . . . 915 1 812 . 1 1 153 153 PHE HA H 1 4.14 . . 1 . . . . . . . . 915 1 813 . 1 1 153 153 PHE HB2 H 1 3.33 . . 1 . . . . . . . . 915 1 814 . 1 1 153 153 PHE HB3 H 1 3.33 . . 1 . . . . . . . . 915 1 815 . 1 1 153 153 PHE HD1 H 1 6.95 . . 1 . . . . . . . . 915 1 816 . 1 1 153 153 PHE HD2 H 1 6.95 . . 1 . . . . . . . . 915 1 817 . 1 1 153 153 PHE HE1 H 1 7.4 . . 1 . . . . . . . . 915 1 818 . 1 1 153 153 PHE HE2 H 1 7.4 . . 1 . . . . . . . . 915 1 819 . 1 1 153 153 PHE HZ H 1 6.72 . . 1 . . . . . . . . 915 1 820 . 1 1 153 153 PHE N N 15 121.2 . . 1 . . . . . . . . 915 1 821 . 1 1 154 154 ARG H H 1 9.06 . . 1 . . . . . . . . 915 1 822 . 1 1 154 154 ARG HA H 1 4.1 . . 1 . . . . . . . . 915 1 823 . 1 1 154 154 ARG HB2 H 1 2.09 . . 1 . . . . . . . . 915 1 824 . 1 1 154 154 ARG HB3 H 1 2.09 . . 1 . . . . . . . . 915 1 825 . 1 1 154 154 ARG N N 15 120.1 . . 1 . . . . . . . . 915 1 826 . 1 1 155 155 THR H H 1 8.19 . . 1 . . . . . . . . 915 1 827 . 1 1 155 155 THR HA H 1 4.26 . . 1 . . . . . . . . 915 1 828 . 1 1 155 155 THR N N 15 105.2 . . 1 . . . . . . . . 915 1 829 . 1 1 156 156 GLY H H 1 8.49 . . 1 . . . . . . . . 915 1 830 . 1 1 156 156 GLY HA2 H 1 3.15 . . 2 . . . . . . . . 915 1 831 . 1 1 156 156 GLY HA3 H 1 3.68 . . 2 . . . . . . . . 915 1 832 . 1 1 156 156 GLY N N 15 112.7 . . 1 . . . . . . . . 915 1 833 . 1 1 157 157 THR H H 1 7.61 . . 1 . . . . . . . . 915 1 834 . 1 1 157 157 THR HA H 1 4.67 . . 1 . . . . . . . . 915 1 835 . 1 1 157 157 THR HB H 1 4.4 . . 1 . . . . . . . . 915 1 836 . 1 1 157 157 THR HG21 H 1 1.09 . . 1 . . . . . . . . 915 1 837 . 1 1 157 157 THR HG22 H 1 1.09 . . 1 . . . . . . . . 915 1 838 . 1 1 157 157 THR HG23 H 1 1.09 . . 1 . . . . . . . . 915 1 839 . 1 1 157 157 THR N N 15 109.2 . . 1 . . . . . . . . 915 1 840 . 1 1 158 158 TRP H H 1 8.66 . . 1 . . . . . . . . 915 1 841 . 1 1 158 158 TRP HA H 1 5.11 . . 1 . . . . . . . . 915 1 842 . 1 1 158 158 TRP HB2 H 1 2.99 . . 2 . . . . . . . . 915 1 843 . 1 1 158 158 TRP HB3 H 1 3.79 . . 2 . . . . . . . . 915 1 844 . 1 1 158 158 TRP NE1 N 15 129.7 . . 1 . . . . . . . . 915 1 845 . 1 1 158 158 TRP HD1 H 1 7.23 . . 1 . . . . . . . . 915 1 846 . 1 1 158 158 TRP HE1 H 1 9.97 . . 1 . . . . . . . . 915 1 847 . 1 1 158 158 TRP HE3 H 1 7.27 . . 1 . . . . . . . . 915 1 848 . 1 1 158 158 TRP HZ2 H 1 7.42 . . 1 . . . . . . . . 915 1 849 . 1 1 158 158 TRP HZ3 H 1 6.38 . . 1 . . . . . . . . 915 1 850 . 1 1 158 158 TRP HH2 H 1 6.93 . . 1 . . . . . . . . 915 1 851 . 1 1 158 158 TRP N N 15 118.8 . . 1 . . . . . . . . 915 1 852 . 1 1 159 159 ASP H H 1 7.99 . . 1 . . . . . . . . 915 1 853 . 1 1 159 159 ASP HA H 1 4.31 . . 1 . . . . . . . . 915 1 854 . 1 1 159 159 ASP N N 15 120.8 . . 1 . . . . . . . . 915 1 855 . 1 1 160 160 ALA H H 1 9.12 . . 1 . . . . . . . . 915 1 856 . 1 1 160 160 ALA HA H 1 4.21 . . 1 . . . . . . . . 915 1 857 . 1 1 160 160 ALA HB1 H 1 1.24 . . 1 . . . . . . . . 915 1 858 . 1 1 160 160 ALA HB2 H 1 1.24 . . 1 . . . . . . . . 915 1 859 . 1 1 160 160 ALA HB3 H 1 1.24 . . 1 . . . . . . . . 915 1 860 . 1 1 160 160 ALA N N 15 120.6 . . 1 . . . . . . . . 915 1 861 . 1 1 161 161 TYR H H 1 8.06 . . 1 . . . . . . . . 915 1 862 . 1 1 161 161 TYR HA H 1 4.28 . . 1 . . . . . . . . 915 1 863 . 1 1 161 161 TYR HB2 H 1 2.79 . . 1 . . . . . . . . 915 1 864 . 1 1 161 161 TYR HB3 H 1 2.79 . . 1 . . . . . . . . 915 1 865 . 1 1 161 161 TYR HD1 H 1 7.14 . . 1 . . . . . . . . 915 1 866 . 1 1 161 161 TYR HD2 H 1 7.14 . . 1 . . . . . . . . 915 1 867 . 1 1 161 161 TYR HE1 H 1 6.61 . . 1 . . . . . . . . 915 1 868 . 1 1 161 161 TYR HE2 H 1 6.61 . . 1 . . . . . . . . 915 1 869 . 1 1 161 161 TYR HH H 1 11.29 . . 1 . . . . . . . . 915 1 870 . 1 1 161 161 TYR N N 15 114.7 . . 1 . . . . . . . . 915 1 871 . 1 1 162 162 LYS H H 1 7.26 . . 1 . . . . . . . . 915 1 872 . 1 1 162 162 LYS HA H 1 4.13 . . 1 . . . . . . . . 915 1 873 . 1 1 162 162 LYS HB2 H 1 1.81 . . 1 . . . . . . . . 915 1 874 . 1 1 162 162 LYS HB3 H 1 1.81 . . 1 . . . . . . . . 915 1 875 . 1 1 162 162 LYS N N 15 120.5 . . 1 . . . . . . . . 915 1 876 . 1 1 163 163 ASN H H 1 8.6 . . 1 . . . . . . . . 915 1 877 . 1 1 163 163 ASN HA H 1 4.59 . . 1 . . . . . . . . 915 1 878 . 1 1 163 163 ASN HB2 H 1 2.82 . . 2 . . . . . . . . 915 1 879 . 1 1 163 163 ASN HB3 H 1 2.92 . . 2 . . . . . . . . 915 1 880 . 1 1 163 163 ASN N N 15 117.8 . . 1 . . . . . . . . 915 1 881 . 1 1 164 164 LEU H H 1 7.4 . . 1 . . . . . . . . 915 1 882 . 1 1 164 164 LEU HA H 1 4.21 . . 1 . . . . . . . . 915 1 883 . 1 1 164 164 LEU HB2 H 1 1.56 . . 2 . . . . . . . . 915 1 884 . 1 1 164 164 LEU HB3 H 1 1.65 . . 2 . . . . . . . . 915 1 885 . 1 1 164 164 LEU N N 15 126.8 . . 1 . . . . . . . . 915 1 stop_ save_