data_915 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignment of the Backbone 1H and 15N NMR Resonances of Bacteriophage T4 Lysozyme ; _BMRB_accession_number 915 _BMRB_flat_file_name bmr915.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-03-25 _Entry_origination BMRB _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 McIntosh Lawrence P. . 2 Wand A. Joshua . 3 Lowry David F. . 4 Redfield Alfred G. . 5 Dahlquist Frederick W. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 635 "15N chemical shifts" 166 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-11 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; 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 _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 McIntosh Lawrence P. . 2 Wand A. Joshua . 3 Lowry David F. . 4 Redfield Alfred G. . 5 Dahlquist Frederick W. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 29 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 6341 _Page_last 6362 _Year 1990 _Details . save_ ################################## # Molecular system description # ################################## save_system_T4_lysozyme _Saveframe_category molecular_system _Mol_system_name 'T4 lysozyme' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'T4 lysozyme' $T4_lysozyme stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_T4_lysozyme _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'T4 lysozyme' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 164 _Mol_residue_sequence ; MNIFEMLRIDEGLRLKIYKD TEGYYTIGIGHLLTKSPSLN AAKSELDKAIGRNCNGVITK DEAEKLFNQDVDAAVRGILR NAKLKPVYDSLDAVRRCALI NMVFQMGETGVAGFTNSLRM LQQKRWDEAAVNLAKSRWYN QTPNRAKRVITTFRTGTWDA YKNL ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASN 3 ILE 4 PHE 5 GLU 6 MET 7 LEU 8 ARG 9 ILE 10 ASP 11 GLU 12 GLY 13 LEU 14 ARG 15 LEU 16 LYS 17 ILE 18 TYR 19 LYS 20 ASP 21 THR 22 GLU 23 GLY 24 TYR 25 TYR 26 THR 27 ILE 28 GLY 29 ILE 30 GLY 31 HIS 32 LEU 33 LEU 34 THR 35 LYS 36 SER 37 PRO 38 SER 39 LEU 40 ASN 41 ALA 42 ALA 43 LYS 44 SER 45 GLU 46 LEU 47 ASP 48 LYS 49 ALA 50 ILE 51 GLY 52 ARG 53 ASN 54 CYS 55 ASN 56 GLY 57 VAL 58 ILE 59 THR 60 LYS 61 ASP 62 GLU 63 ALA 64 GLU 65 LYS 66 LEU 67 PHE 68 ASN 69 GLN 70 ASP 71 VAL 72 ASP 73 ALA 74 ALA 75 VAL 76 ARG 77 GLY 78 ILE 79 LEU 80 ARG 81 ASN 82 ALA 83 LYS 84 LEU 85 LYS 86 PRO 87 VAL 88 TYR 89 ASP 90 SER 91 LEU 92 ASP 93 ALA 94 VAL 95 ARG 96 ARG 97 CYS 98 ALA 99 LEU 100 ILE 101 ASN 102 MET 103 VAL 104 PHE 105 GLN 106 MET 107 GLY 108 GLU 109 THR 110 GLY 111 VAL 112 ALA 113 GLY 114 PHE 115 THR 116 ASN 117 SER 118 LEU 119 ARG 120 MET 121 LEU 122 GLN 123 GLN 124 LYS 125 ARG 126 TRP 127 ASP 128 GLU 129 ALA 130 ALA 131 VAL 132 ASN 133 LEU 134 ALA 135 LYS 136 SER 137 ARG 138 TRP 139 TYR 140 ASN 141 GLN 142 THR 143 PRO 144 ASN 145 ARG 146 ALA 147 LYS 148 ARG 149 VAL 150 ILE 151 THR 152 THR 153 PHE 154 ARG 155 THR 156 GLY 157 THR 158 TRP 159 ASP 160 ALA 161 TYR 162 LYS 163 ASN 164 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 17603 T4_L99A/G113A/R119P 100.00 164 96.95 96.95 5.42e-112 BMRB 17604 T4_L99A 100.00 164 98.17 98.17 7.64e-114 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 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 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 PDB 107L "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" 100.00 164 98.17 98.17 1.12e-113 PDB 108L "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" 100.00 164 98.17 98.17 1.73e-113 PDB 109L "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" 100.00 164 98.17 98.17 1.05e-113 PDB 110L "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" 100.00 164 98.17 98.17 1.70e-113 PDB 111L "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" 100.00 164 98.17 98.78 7.81e-114 PDB 112L "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" 100.00 164 98.17 98.17 1.04e-113 PDB 113L "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" 100.00 164 98.17 98.17 1.33e-113 PDB 114L "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" 100.00 164 98.17 98.78 4.23e-114 PDB 115L "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" 100.00 164 98.17 98.17 1.13e-113 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 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 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 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 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 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 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 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 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 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 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 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 PDB 137L "Structural Basis Of Amino Acid Alpha Helix Propensity" 100.00 164 98.17 98.17 2.11e-113 PDB 138L "Rapid Crystallization Of T4 Lysozyme By Intermolecular Disulfide Crosslinking" 100.00 164 98.17 98.17 1.96e-113 PDB 139L "Rapid Crystallization Of T4 Lysozyme By Intermolecular Disulfide Crosslinking" 100.00 164 97.56 97.56 6.18e-112 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 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 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 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 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 PDB 149L "Conservation Of Solvent-Binding Sites In 10 Crystal Forms Of T4 Lysozyme" 100.00 164 99.39 100.00 2.23e-116 PDB 150L "Conservation Of Solvent-Binding Sites In 10 Crystal Forms Of T4 Lysozyme" 100.00 164 99.39 100.00 3.93e-116 PDB 151L "Conservation Of Solvent-Binding Sites In 10 Crystal Forms Of T4 Lysozyme" 100.00 164 97.56 98.17 8.80e-114 PDB 152L "Conservation Of Solvent-Binding Sites In 10 Crystal Forms Of T4 Lysozyme" 99.39 164 96.93 96.93 2.08e-111 PDB 155L "Control Of Enzyme Activity By An Engineered Disulfide Bond" 100.00 164 97.56 98.17 2.46e-113 PDB 156L "Control Of Enzyme Activity By An Engineered Disulfide Bond" 100.00 164 97.56 97.56 7.50e-113 PDB 158L "Control Of Enzyme Activity By An Engineered Disulfide Bond" 100.00 164 97.56 98.17 4.25e-113 PDB 159L "Control Of Enzyme Activity By An Engineered Disulfide Bond" 100.00 164 97.56 97.56 1.32e-112 PDB 160L "Control Of Enzyme Activity By An Engineered Disulfide Bond" 100.00 164 98.17 98.17 1.29e-113 PDB 161L "Control Of Enzyme Activity By An Engineered Disulfide Bond" 100.00 164 98.17 98.17 1.35e-113 PDB 162L "Control Of Enzyme Activity By An Engineered Disulfide Bond" 100.00 164 98.17 98.17 1.29e-113 PDB 163L "Control Of Enzyme Activity By An Engineered Disulfide Bond" 100.00 164 98.17 98.17 1.29e-113 PDB 164L "Control Of Enzyme Activity By An Engineered Disulfide Bond" 100.00 164 98.17 98.17 1.30e-113 PDB 165L "Control Of Enzyme Activity By An Engineered Disulfide Bond" 100.00 164 98.17 98.78 4.33e-114 PDB 166L "Control Of Enzyme Activity By An Engineered Disulfide Bond" 100.00 164 98.17 98.17 7.81e-114 PDB 167L "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" 99.39 164 98.16 98.16 7.18e-113 PDB 170L "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" 100.00 164 98.17 98.17 1.98e-113 PDB 171L "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" 100.00 164 98.17 98.17 9.93e-114 PDB 172L "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" 100.00 164 99.39 99.39 4.58e-116 PDB 173L "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" 100.00 164 97.56 99.39 1.89e-114 PDB 175L "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" 100.00 164 98.17 98.17 1.30e-113 PDB 177L "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" 100.00 164 97.56 97.56 3.44e-111 PDB 178L "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" 100.00 164 97.56 97.56 3.44e-111 PDB 180L "Protein Flexibility And Adaptability Seen In 25 Crystal Forms Of T4 Lysozyme" 100.00 164 98.17 98.17 1.33e-113 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 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 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 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 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 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 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 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 PDB 190L "A Helix Initiation Signal In T4 Lysozyme Identified By Polyalanine Mutagenesis" 100.00 164 98.17 98.17 2.86e-114 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 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 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 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 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 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 PDB 1C60 "T4 Lysozyme Mutant C54tC97AF153A IN THE PRESENCE OF 8 ATM Argon" 100.00 164 98.17 98.17 2.28e-113 PDB 1C61 "T4 Lysozyme Mutant C54tC97AF153A IN THE PRESENCE OF 8 ATM Krypton" 100.00 164 98.17 98.17 2.28e-113 PDB 1C62 "T4 Lysozyme Mutant C54tC97AF153A IN THE PRESENCE OF 8 ATM Xenon" 100.00 164 98.17 98.17 2.28e-113 PDB 1C63 "T4 Lysozyme Mutant C54tC97AL121A IN THE PRESENCE OF 8 ATM Argon" 100.00 164 98.17 98.17 7.64e-114 PDB 1C64 "T4 Lysozyme Mutant C54tC97AL121A IN THE PRESENCE OF 8 ATM Krypton" 100.00 164 98.17 98.17 7.64e-114 PDB 1C65 "T4 Lysozyme Mutant C54tC97AL121A IN THE PRESENCE OF 8 ATM Xenon" 100.00 164 98.17 98.17 7.64e-114 PDB 1C66 "T4 Lysozyme Mutant C54tC97AL121AL133A IN THE PRESENCE OF 8 Atm Argon" 100.00 164 97.56 97.56 4.54e-113 PDB 1C67 "T4 Lysozyme Mutant C54tC97AL121AL133A IN THE PRESENCE OF 8 Atm Krypton" 100.00 164 97.56 97.56 4.54e-113 PDB 1C68 "T4 Lysozyme Mutant C54tC97AL121AL133A IN THE PRESENCE OF 8 Atm Xenon" 100.00 164 97.56 97.56 4.54e-113 PDB 1C69 "T4 Lysozyme Mutant C54tC97AL133A IN THE PRESENCE OF 8 ATM Argon" 100.00 164 99.39 99.39 4.20e-116 PDB 1C6A "T4 Lysozyme Mutant C54tC97AL133A IN THE PRESENCE OF 8 ATM Krypton" 100.00 164 99.39 99.39 4.20e-116 PDB 1C6B "T4 Lysozyme Mutant C54tC97AL133A IN THE PRESENCE OF 8 ATM Xenon" 100.00 164 99.39 99.39 4.20e-116 PDB 1C6C "T4 Lysozyme Mutant C54tC97AL99A IN THE PRESENCE OF 16 ATM Argon" 100.00 164 98.17 98.17 7.64e-114 PDB 1C6D "T4 Lysozyme Mutant C54tC97AL99A IN THE PRESENCE OF 16 ATM Krypton" 100.00 164 98.17 98.17 7.64e-114 PDB 1C6E "T4 Lysozyme Mutant C54tC97AL99A IN THE PRESENCE OF 2 ATM Xenon" 100.00 164 98.17 98.17 7.64e-114 PDB 1C6F "T4 Lysozyme Mutant C54tC97AL99A IN THE PRESENCE OF 32 ATM Argon" 100.00 164 98.17 98.17 7.64e-114 PDB 1C6G "T4 Lysozyme Mutant C54tC97AL99A IN THE PRESENCE OF 4 ATM Krypton" 100.00 164 98.17 98.17 7.64e-114 PDB 1C6H "T4 Lysozyme Mutant C54tC97AL99A IN THE PRESENCE OF 4 ATM Xenon" 100.00 164 98.17 98.17 7.64e-114 PDB 1C6I "T4 Lysozyme Mutant C54tC97AL99A IN THE PRESENCE OF 8 ATM Argon" 100.00 164 98.17 98.17 7.64e-114 PDB 1C6J "T4 Lysozyme Mutant C54tC97AL99A IN THE PRESENCE OF 8 ATM Krypton" 100.00 164 98.17 98.17 7.64e-114 PDB 1C6K "T4 Lysozyme Mutant C54tC97AL99A IN THE PRESENCE OF 8 ATM Xenon" 100.00 164 98.17 98.17 7.64e-114 PDB 1C6L "T4 Lysozyme Mutant C54tC97AL99AF153A IN THE PRESENCE OF 8 Atm Argon" 100.00 164 97.56 97.56 1.40e-112 PDB 1C6M "T4 Lysozyme Mutant C54tC97AL99AF153A IN THE PRESENCE OF 8 Atm Krypton" 100.00 164 97.56 97.56 1.40e-112 PDB 1C6N "T4 Lysozyme Mutant C54tC97AL99AF153A IN THE PRESENCE OF 8 Atm Xenon" 100.00 164 97.56 97.56 1.40e-112 PDB 1C6P "T4 Lysozyme Mutant C54tC97A IN THE PRESENCE OF 8 ATM ARGON" 100.00 164 98.78 98.78 1.45e-114 PDB 1C6Q "T4 Lysozyme Mutant C54tC97A IN THE PRESENCE OF 8 ATM Krypton" 100.00 164 98.78 98.78 1.45e-114 PDB 1C6T "T4 Lysozyme Mutant C54tC97A IN THE PRESENCE OF 8 ATM XENON" 100.00 164 98.78 98.78 1.45e-114 PDB 1CTW "T4 Lysozyme Mutant I78a" 100.00 164 98.17 98.17 7.64e-114 PDB 1CU0 "T4 Lysozyme Mutant I78m" 100.00 164 98.17 98.78 3.48e-114 PDB 1CU2 "T4 Lysozyme Mutant L84m" 100.00 164 98.17 98.78 2.40e-114 PDB 1CU3 "T4 Lysozyme Mutant V87m" 100.00 164 98.17 98.78 4.10e-114 PDB 1CU5 "T4 Lysozyme Mutant L91m" 100.00 164 98.17 98.78 2.40e-114 PDB 1CU6 "T4 Lysozyme Mutant L91a" 100.00 164 98.17 98.17 7.64e-114 PDB 1CUP "Methionine Core Mutant Of T4 Lysozyme" 100.00 164 98.17 98.78 3.48e-114 PDB 1CUQ "T4 Lysozyme Mutant V103m" 100.00 164 98.17 98.78 4.10e-114 PDB 1CV0 "T4 Lysozyme Mutant F104m" 100.00 164 98.17 98.17 1.18e-113 PDB 1CV1 "T4 Lysozyme Mutant V111m" 100.00 164 98.17 98.78 4.10e-114 PDB 1CV3 "T4 Lysozyme Mutant L121m" 100.00 164 98.17 98.78 2.40e-114 PDB 1CV4 "T4 Lysozyme Mutant L118m" 100.00 164 98.17 98.78 2.40e-114 PDB 1CV5 "T4 Lysozyme Mutant L133m" 100.00 164 98.17 98.78 2.40e-114 PDB 1CV6 "T4 Lysozyme Mutant V149m" 100.00 164 98.17 98.78 4.10e-114 PDB 1CVK "T4 Lysozyme Mutant L118a" 100.00 164 98.17 98.17 7.64e-114 PDB 1D2W "N-Terminal Domain Core Methionine Mutation" 100.00 164 98.17 98.78 3.48e-114 PDB 1D2Y "N-Terminal Domain Core Methionine Mutation" 100.00 164 98.17 98.78 3.48e-114 PDB 1D3F "N-Terminal Domain Core Methionine Mutation" 100.00 164 98.17 98.78 3.48e-114 PDB 1D3J "N-Terminal Domain Core Methionine Mutation" 100.00 164 98.17 98.78 2.40e-114 PDB 1D9W "Bacteriophage T4 Lysozyme Mutant" 100.00 164 99.39 99.39 7.02e-116 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 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 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 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 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 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 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 PDB 1EPY "T4 Lysozyme Mutant, T21hC54TC97AQ141HT142H" 100.00 164 96.95 96.95 3.99e-112 PDB 1G06 "Crystal Structure Of T4 Lysozyme Mutant V149s" 100.00 164 98.17 98.17 7.98e-114 PDB 1G07 "Crystal Structure Of T4 Lysozyme Mutant V149c" 100.00 164 98.17 98.17 2.41e-113 PDB 1G0G "Crystal Structure Of T4 Lysozyme Mutant T152a" 100.00 164 98.17 98.17 7.81e-114 PDB 1G0J "Crystal Structure Of T4 Lysozyme Mutant T152s" 100.00 164 98.17 98.78 3.96e-114 PDB 1G0K "Crystal Structure Of T4 Lysozyme Mutant T152c" 100.00 164 98.17 98.17 2.66e-113 PDB 1G0L "Crystal Structure Of T4 Lysozyme Mutant T152v" 100.00 164 98.17 98.17 7.07e-114 PDB 1G0M "Crystal Structure Of T4 Lysozyme Mutant T152i" 100.00 164 98.17 98.17 9.10e-114 PDB 1G0P "Crystal Structure Of T4 Lysozyme Mutant V149g" 100.00 164 98.17 98.17 2.63e-113 PDB 1G0Q "Crystal Structure Of T4 Lysozyme Mutant V149i" 100.00 164 98.17 98.78 2.35e-114 PDB 1G1V "T4 Lysozyme Mutant C54tC97AI58T" 100.00 164 98.17 98.17 6.63e-114 PDB 1G1W "T4 Lysozyme Mutant C54tC97AQ105M" 100.00 164 98.17 98.17 1.21e-113 PDB 1I6S "T4 Lysozyme Mutant C54tC97AN101A" 100.00 164 98.17 98.17 1.35e-113 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 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 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 PDB 1KNI "Stabilizing Disulfide Bridge Mutant Of T4 Lysozyme" 100.00 164 97.56 97.56 4.08e-112 PDB 1KS3 "Methionine Core Mutant Of T4 Lysozyme" 98.78 162 97.53 98.77 1.46e-112 PDB 1KW5 "Methionine Core Mutant Of T4 Lysozyme" 98.78 162 96.91 98.77 2.07e-112 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 PDB 1L19 "Enhanced Protein Thermostability From Designed Mutations That Interact With Alpha-helix Dipoles" 100.00 164 99.39 99.39 5.00e-116 PDB 1L20 "Enhanced Protein Thermostability From Designed Mutations That Interact With Alpha-helix Dipoles" 100.00 164 99.39 100.00 4.15e-116 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 PDB 1L83 "A Cavity-Containing Mutant Of T4 Lysozyme Is Stabilized By Buried Benzene" 100.00 164 98.17 98.17 7.64e-114 PDB 1L84 "A Cavity-Containing Mutant Of T4 Lysozyme Is Stabilized By Buried Benzene" 100.00 164 97.56 97.56 1.40e-112 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 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 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 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 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 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 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 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 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 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 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 PDB 1L96 "Structure Of A Hinge-bending Bacteriophage T4 Lysozyme Mutant, Ile3-> Pro" 100.00 164 99.39 99.39 7.66e-116 PDB 1L97 "Structure Of A Hinge-Bending Bacteriophage T4 Lysozyme Mutant, Ile3-> Pro" 100.00 164 99.39 99.39 7.66e-116 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 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 PDB 1LGU "T4 Lysozyme Mutant L99aM102Q" 100.00 164 98.78 98.78 3.86e-115 PDB 1LGW "T4 Lysozyme Mutant L99aM102Q BOUND BY 2-Fluoroaniline" 100.00 164 98.78 98.78 3.86e-115 PDB 1LGX "T4 Lysozyme Mutant L99aM102Q BOUND BY 3,5-Difluoroaniline" 100.00 164 98.78 98.78 3.86e-115 PDB 1LI2 "T4 Lysozyme Mutant L99aM102Q BOUND BY PHENOL" 100.00 164 98.78 98.78 3.86e-115 PDB 1LI3 "T4 Lysozyme Mutant L99aM102Q BOUND BY 3-Chlorophenol" 100.00 164 98.78 98.78 3.86e-115 PDB 1LI6 "T4 Lysozyme Mutant L99aM102Q BOUND BY 5-Methylpyrrole" 100.00 164 98.78 98.78 3.86e-115 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 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 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 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 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 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 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 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 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 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 PDB 1OV5 "T4 Lysozyme Cavity Mutant L99aM102Q BOUND WITH 2- Allylphenol" 100.00 164 98.78 98.78 3.86e-115 PDB 1OV7 "T4 Lysozyme Cavity Mutant L99aM102Q BOUND WITH 2-Allyl-6- Methyl-Phenol" 100.00 164 98.78 98.78 3.86e-115 PDB 1OVH "T4 Lysozyme Cavity Mutant L99aM102Q BOUND WITH 2-Chloro-6- Methyl-Aniline" 100.00 164 98.78 98.78 3.86e-115 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 PDB 1OVK "T4 Lysozyme Cavity Mutant L99aM102Q BOUND WITH N-Allyl- Aniline" 100.00 164 98.78 98.78 3.86e-115 PDB 1OWY "T4 Lysozyme Cavity Mutant L99a/m102q Bound With 2-propyl- Aniline" 100.00 164 98.78 98.78 3.86e-115 PDB 1OWZ "T4 Lysozyme Cavity Mutant L99aM102Q BOUND WITH 4- Fluorophenethyl Alcohol" 100.00 164 98.78 98.78 3.86e-115 PDB 1P2L "T4 Lysozyme Core Repacking Mutant V87iTA" 100.00 164 98.17 98.78 2.35e-114 PDB 1P2R "T4 Lysozyme Core Repacking Mutant I78vTA" 100.00 164 98.17 98.78 2.10e-114 PDB 1P36 "T4 Lyoszyme Core Repacking Mutant I100vTA" 100.00 164 98.17 98.78 2.10e-114 PDB 1P46 "T4 Lysozyme Core Repacking Mutant M106iTA" 100.00 164 98.17 98.78 6.85e-114 PDB 1P56 "Duplication-Extension Of Helix A Of T4 Lysozyme" 99.39 176 98.16 98.77 5.87e-113 PDB 1P5C "Circular Permutation Of Helix A In T4 Lysozyme" 92.07 167 98.68 98.68 3.88e-104 PDB 1P64 "T4 Lysozyme Core Repacking Mutant L133fTA" 100.00 164 98.17 98.17 5.88e-114 PDB 1P6Y "T4 Lysozyme Core Repacking Mutant M120y/ta" 100.00 164 98.17 98.17 1.83e-113 PDB 1P7S "T4 Lysozyme Core Repacking Mutant V103iTA" 100.00 164 98.17 98.78 2.35e-114 PDB 1PQM "T4 Lysozyme Core Repacking Mutant V149iT152VTA" 100.00 164 97.56 98.17 1.12e-113 PDB 1PQO "T4 Lysozyme Core Repacking Mutant L118iTA" 100.00 164 98.17 98.78 2.89e-114 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 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 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 PDB 1QSQ "Cavity Creating Mutation" 100.00 164 98.17 98.17 1.29e-113 PDB 1QT3 "T26d Mutant Of T4 Lysozyme" 100.00 164 98.17 98.17 1.61e-113 PDB 1QT4 "T26q Mutant Of T4 Lysozyme" 100.00 164 98.17 98.17 1.18e-113 PDB 1QT5 "D20e Mutant Structure Of T4 Lysozyme" 100.00 164 98.17 98.78 6.77e-114 PDB 1QT6 "E11h Mutant Of T4 Lysozyme" 100.00 164 98.17 98.17 7.00e-114 PDB 1QT7 "E11n Mutant Of T4 Lysozyme" 100.00 164 98.17 98.17 1.24e-113 PDB 1QT8 "T26h Mutant Of T4 Lysozyme" 100.00 164 98.17 98.17 1.35e-113 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 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 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 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 PDB 1QTV "T26e Apo Structure Of T4 Lysozyme" 100.00 164 98.17 98.17 1.33e-113 PDB 1QTZ "D20c Mutant Of T4 Lysozyme" 100.00 164 98.17 98.17 9.86e-113 PDB 1QUD "L99g Mutant Of T4 Lysozyme" 98.78 162 98.15 98.15 8.56e-112 PDB 1QUG "E108v Mutant Of T4 Lysozyme" 98.78 162 98.15 98.15 6.51e-112 PDB 1QUH "L99gE108V MUTANT OF T4 LYSOZYME" 98.78 162 97.53 97.53 1.14e-110 PDB 1QUO "L99aE108V MUTANT OF T4 LYSOZYME" 98.78 162 97.53 97.53 4.27e-111 PDB 1SSY "Crystal Structure Of Phage T4 Lysozyme Mutant G28aI29AG30AC54TC97A" 100.00 164 96.95 96.95 2.58e-112 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 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 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 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 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 PDB 1T8G "Crystal Structure Of Phage T4 Lysozyme Mutant L32aL33AT34AC54TC97AE108V" 100.00 164 96.95 96.95 6.97e-112 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 PDB 1XEP "Catechol In Complex With T4 Lysozyme L99aM102Q" 100.00 164 98.78 98.78 3.86e-115 PDB 1ZUR "Crystal Structure Of Spin Labeled T4 Lysozyme (V131r1f)" 100.00 164 98.17 98.17 2.41e-113 PDB 1ZWN "Crystal Structure Of Spin Labeled T4 Lysozyme (V131r1b)" 100.00 164 98.17 98.17 2.41e-113 PDB 1ZYT "Crystal Structure Of Spin Labeled T4 Lysozyme (A82r1)" 100.00 164 98.17 98.17 1.96e-113 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 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 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 PDB 206L "Phage T4 Lysozyme" 100.00 164 98.17 98.78 3.36e-114 PDB 209L "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" 101.83 167 97.01 97.01 1.33e-112 PDB 210L "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" 100.00 163 98.17 98.17 4.30e-112 PDB 211L "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" 100.61 165 98.18 98.18 9.98e-113 PDB 212L "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" 100.00 168 98.78 98.78 9.42e-115 PDB 213L "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" 100.61 165 98.18 98.18 9.98e-113 PDB 214L "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" 100.61 165 98.18 98.18 9.98e-113 PDB 215L "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" 100.61 165 98.18 98.18 9.98e-113 PDB 216L "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" 100.00 164 98.17 98.17 4.79e-113 PDB 217L "Structural Basis Of Alpha-Helix Propensity At Two Sites In T4 Lysozyme" 100.00 164 98.17 98.17 8.43e-114 PDB 218L "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" 100.61 165 98.18 98.18 9.98e-113 PDB 219L "Protein Structure Plasticity Exemplified By Insertion And Deletion Mutants In T4 Lysozyme" 100.00 164 98.78 98.78 1.45e-114 PDB 220L "Generating Ligand Binding Sites In T4 Lysozyme Using Deficiency-Creating Substitutions" 100.00 164 98.17 98.17 1.29e-113 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 PDB 222L "Generating Ligand Binding Sites In T4 Lysozyme Using Deficiency-Creating Substitutions" 100.00 164 98.17 98.17 1.29e-113 PDB 223L "Generating Ligand Binding Sites In T4 Lysozyme Using Deficiency-Creating Substitutions" 100.00 164 99.39 99.39 1.27e-115 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 PDB 225L "Generating Ligand Binding Sites In T4 Lysozyme Using Deficiency-Creating Substitutions" 100.00 164 99.39 99.39 1.27e-115 PDB 226L "Generating Ligand Binding Sites In T4 Lysozyme Using Deficiency-Creating Substitutions" 100.00 164 99.39 99.39 1.27e-115 PDB 227L "Generating Ligand Binding Sites In T4 Lysozyme Using Deficiency-Creating Substitutions" 100.00 164 98.17 98.17 2.28e-113 PDB 228L "Generating Ligand Binding Sites In T4 Lysozyme Using Deficiency-Creating Substitutions" 100.00 164 98.17 98.17 2.28e-113 PDB 229L "Generating Ligand Binding Sites In T4 Lysozyme Using Deficiency-Creating Substitutions" 100.00 164 98.17 98.17 1.30e-113 PDB 230L "T4 Lysozyme Mutant M6l" 100.00 164 98.17 98.78 5.44e-114 PDB 231L "T4 Lysozyme Mutant M106k" 100.00 164 98.17 98.17 1.77e-113 PDB 232L "T4 Lysozyme Mutant M120k" 100.00 164 98.17 98.17 1.77e-113 PDB 233L "T4 Lysozyme Mutant M120l" 100.00 164 98.17 98.78 5.44e-114 PDB 234L "T4 Lysozyme Mutant M106l" 100.00 164 98.17 98.78 5.44e-114 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 PDB 252L "Generating Ligand Binding Sites In T4 Lysozyme Using Deficiency-Creating Substitutions" 100.00 164 97.56 97.56 1.35e-112 PDB 253L Lysozyme 100.00 164 98.17 98.17 1.71e-113 PDB 254L Lysozyme 100.00 164 98.17 98.17 8.61e-114 PDB 255L Hydrolase 100.00 164 98.17 98.78 7.47e-114 PDB 256L "Bacteriophage T4 Lysozyme" 100.00 164 99.39 100.00 3.93e-116 PDB 257L "An Adaptable Metal-Binding Site Engineered Into T4 Lysozyme" 100.00 164 97.56 97.56 1.14e-112 PDB 258L "An Adaptable Metal-Binding Site Engineered Into T4 Lysozyme" 100.00 164 97.56 97.56 1.14e-112 PDB 259L "An Adaptable Metal-Binding Site Engineered Into T4 Lysozyme" 100.00 164 97.56 97.56 1.14e-112 PDB 260L "An Adaptable Metal-Binding Site Engineered Into T4 Lysozyme" 100.00 164 97.56 97.56 1.14e-112 PDB 2A4T "Crystal Structure Of Spin Labeled T4 Lysozyme (V131r7)" 100.00 164 98.17 98.17 2.41e-113 PDB 2B6T "T4 Lysozyme Mutant L99a At 200 Mpa" 98.78 162 98.15 98.15 2.28e-112 PDB 2B6W "T4 Lysozyme Mutant L99a At 200 Mpa" 98.78 162 98.15 98.15 2.28e-112 PDB 2B6X "T4 Lysozyme Mutant L99a At 200 Mpa" 98.78 162 98.15 98.15 2.28e-112 PDB 2B6Y "T4 Lysozyme Mutant L99a At Ambient Pressure" 98.78 162 98.15 98.15 2.28e-112 PDB 2B6Z "T4 Lysozyme Mutant L99a At Ambient Pressure" 98.78 162 98.15 98.15 2.28e-112 PDB 2B70 "T4 Lysozyme Mutant L99a At Ambient Pressure" 98.78 162 98.15 98.15 2.28e-112 PDB 2B72 "T4 Lysozyme Mutant L99a At 100 Mpa" 98.78 162 98.15 98.15 2.28e-112 PDB 2B73 "T4 Lysozyme Mutant L99a At 100 Mpa" 98.78 162 98.15 98.15 2.28e-112 PDB 2B74 "T4 Lysozyme Mutant L99a At 100 Mpa" 98.78 162 98.15 98.15 2.28e-112 PDB 2B75 "T4 Lysozyme Mutant L99a At 150 Mpa" 98.78 162 98.15 98.15 2.28e-112 PDB 2CUU "Crystal Structure Of Spin Labeled T4 Lysozyme (v131r1)" 100.00 164 98.17 98.17 2.41e-113 PDB 2HUK "Crystal Structure Of T4 Lysozyme V131c Synthetic Dimer" 100.00 164 98.17 98.17 2.41e-113 PDB 2HUL "Crystal Structure Of T4 Lysozyme S44c Synthetic Dimer" 100.00 164 98.17 98.17 2.93e-113 PDB 2HUM "Crystal Structure Of T4 Lysozyme D72c Synthetic Dimer" 100.00 164 98.17 98.17 9.86e-113 PDB 2IGC "Structure Of Spin Labeled T4 Lysozyme Mutant T115r1a" 100.00 164 98.17 98.17 2.66e-113 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 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 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 PDB 2LZM "Structure Of Bacteriophage T4 Lysozyme Refined At 1.7 Angstroms Resolution" 100.00 164 100.00 100.00 8.06e-117 PDB 2NTG "Structure Of Spin-Labeled T4 Lysozyme Mutant T115r7" 100.00 164 98.17 98.17 2.66e-113 PDB 2NTH "Structure Of Spin-Labeled T4 Lysozyme Mutant L118r1" 100.00 164 98.17 98.17 2.51e-113 PDB 2O4W "T4 Lysozyme Circular Permutant" 92.68 171 98.68 98.68 2.09e-104 PDB 2O79 "T4 Lysozyme With C-Terminal Extension" 100.00 170 98.17 98.78 1.08e-113 PDB 2O7A "T4 Lysozyme C-Terminal Fragment" 64.02 124 99.05 99.05 1.56e-68 PDB 2OE4 "High Pressure Psuedo Wild Type T4 Lysozyme" 100.00 164 98.78 98.78 1.45e-114 PDB 2OE7 "High-Pressure T4 Lysozyme" 100.00 164 98.78 98.78 1.45e-114 PDB 2OE9 "High-Pressure Structure Of Pseudo-Wt T4 Lysozyme" 100.00 164 98.78 98.78 1.45e-114 PDB 2OEA "High-Pressure Structure Of Pseudo-Wt T4 Lysozyme" 100.00 164 98.78 98.78 1.45e-114 PDB 2OTY "1,2-Dichlorobenzene In Complex With T4 Lysozyme L99a" 98.78 162 98.15 98.15 2.28e-112 PDB 2OTZ "N-Methylaniline In Complex With T4 Lysozyme L99a" 98.78 162 98.15 98.15 2.28e-112 PDB 2OU0 "1-Methylpyrrole In Complex With T4 Lysozyme L99a" 98.78 162 98.15 98.15 2.28e-112 PDB 2OU8 "Structure Of Spin-Labeled T4 Lysozyme Mutant T115r1 At Room Temperature" 100.00 164 98.17 98.17 2.66e-113 PDB 2OU9 "Structure Of Spin-Labeled T4 Lysozyme Mutant T115r1R119A" 100.00 164 97.56 97.56 2.91e-112 PDB 2Q9D "Structure Of Spin-Labeled T4 Lysozyme Mutant A41r1" 100.00 164 98.17 98.17 1.96e-113 PDB 2Q9E "Structure Of Spin-Labeled T4 Lysozyme Mutant S44r1" 100.00 164 97.56 97.56 3.11e-112 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 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 PDB 2RAY "Beta-chlorophenetole In Complex With T4 Lysozyme L99a" 98.78 162 98.15 98.15 2.28e-112 PDB 2RAZ "4-(Methylthio)nitrobenzene In Complex With T4 Lysozyme L99a" 98.78 162 98.15 98.15 2.28e-112 PDB 2RB0 "2,6-Difluorobenzylbromide Complex With T4 Lysozyme L99a" 98.78 162 98.15 98.15 2.28e-112 PDB 2RB1 "2-Ethoxyphenol In Complex With T4 Lysozyme L99a" 98.78 162 98.15 98.15 2.28e-112 PDB 2RB2 "3-Methylbenzylazide In Complex With T4 Lysozyme L99a" 98.78 162 98.15 98.15 2.28e-112 PDB 2RBN "N-Phenylglycinonitrile In Complex With T4 Lysozyme L99aM102Q" 98.78 162 98.77 98.77 8.49e-114 PDB 2RBO "2-Nitrothiophene In Complex With T4 Lysozyme L99aM102Q" 98.78 162 98.77 98.77 8.49e-114 PDB 2RBP "2-(N-Propylthio)ethanol In Complex With T4 Lysozyme L99aM102Q" 98.78 162 98.77 98.77 8.49e-114 PDB 2RBQ "3-Methylbenzylazide In Complex With T4 L99aM102Q" 98.78 162 98.77 98.77 8.49e-114 PDB 2RBR "2-Phenoxyethanol In Complex With T4 Lysozyme L99aM102Q" 98.78 162 98.77 98.77 8.49e-114 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 PDB 2RH1 "High Resolution Crystal Structure Of Human B2-Adrenergic G Protein- Coupled Receptor" 98.78 500 98.15 98.77 1.81e-107 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 PDB 3C7Y "Mutant R96a Of T4 Lysozyme In Wildtype Background At 298k" 100.00 164 99.39 99.39 8.55e-116 PDB 3C7Z "T4 Lysozyme Mutant D89aR96H AT ROOM TEMPERATURE" 100.00 164 98.78 98.78 4.36e-115 PDB 3C80 "T4 Lysozyme Mutant R96y At Room Temperature" 100.00 164 99.39 99.39 9.64e-116 PDB 3C81 "Mutant K85a Of T4 Lysozyme In Wildtype Background At Room Temperature" 100.00 164 99.39 99.39 5.77e-116 PDB 3C82 "Bacteriophage Lysozyme T4 Lysozyme Mutant K85aR96H" 100.00 164 98.78 98.78 2.47e-115 PDB 3C83 "Bacteriophage T4 Lysozyme Mutant D89a In Wildtype Background At Room Temperature" 100.00 164 99.39 99.39 1.05e-115 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 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 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 PDB 3CDO "Bacteriophage T4 Lysozyme Mutant R96v In Wildtype Background At Low Temperature" 100.00 164 99.39 99.39 1.04e-115 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 PDB 3CDR "R96q Mutant Of Wildtype Phage T4 Lysozyme At 298 K" 100.00 164 99.39 100.00 3.03e-116 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 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 PDB 3D4S "Cholesterol Bound Form Of Human Beta2 Adrenergic Receptor." 98.78 490 98.15 98.77 9.72e-108 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 PDB 3DMX "Benzene Binding In The Hydrophobic Cavity Of T4 Lysozyme L99a Mutant" 100.00 164 98.17 98.17 7.64e-114 PDB 3DMZ "Hexafluorobenzene Binding In The Hydrophobic Cavity Of T4 Lysozyme L99a Mutant" 100.00 164 98.17 98.17 7.64e-114 PDB 3DN0 "Pentafluorobenzene Binding In The Hydrophobic Cavity Of T4 Lysozyme L99a Mutant" 100.00 164 98.17 98.17 7.64e-114 PDB 3DN1 "Chloropentafluorobenzene Binding In The Hydrophobic Cavity Of T4 Lysozyme L99a Mutant" 100.00 164 98.17 98.17 7.64e-114 PDB 3DN2 "Bromopentafluorobenzene Binding In The Hydrophobic Cavity Of T4 Lysozyme L99a Mutant" 100.00 164 98.17 98.17 7.64e-114 PDB 3DN3 "Iodopentafluorobenzene Binding In The Hydrophobic Cavity Of T4 Lysozyme L99a Mutant" 100.00 164 98.17 98.17 7.64e-114 PDB 3DN4 "Iodobenzene Binding In The Hydrophobic Cavity Of T4 Lysozyme L99a Mutant" 100.00 164 98.17 98.17 7.64e-114 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 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 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 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 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 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 PDB 3FI5 "Crystal Structure Of T4 Lysozyme Mutant R96w" 100.00 164 99.39 99.39 2.31e-115 PDB 3G3V "Crystal Structure Of Spin Labeled T4 Lysozyme (V131r1) At 291 K" 100.00 164 98.17 98.17 2.41e-113 PDB 3G3W "Crystal Structure Of Spin Labeled T4 Lysozyme (T151r1) At 291 K" 100.00 164 98.17 98.17 2.66e-113 PDB 3G3X "Crystal Structure Of Spin Labeled T4 Lysozyme (T151r1) At 100 K" 100.00 164 98.17 98.17 2.66e-113 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 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 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 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 PDB 3HT6 "2-Methylphenol In Complex With T4 Lysozyme L99aM102Q" 100.00 164 97.56 98.17 1.55e-113 PDB 3HT7 "2-Ethylphenol In Complex With T4 Lysozyme L99aM102Q" 100.00 164 97.56 98.17 1.55e-113 PDB 3HT8 "5-chloro-2-methylphenol In Complex With T4 Lysozyme L99a/m102q" 100.00 164 97.56 98.17 1.55e-113 PDB 3HT9 "2-Methoxyphenol In Complex With T4 Lysozyme L99aM102Q" 100.00 164 97.56 98.17 1.55e-113 PDB 3HTB "2-Propylphenol In Complex With T4 Lysozyme L99aM102Q" 100.00 164 97.56 98.17 1.55e-113 PDB 3HTD "(Z)-Thiophene-2-Carboxaldoxime In Complex With T4 Lysozyme L99aM102Q" 100.00 164 97.56 98.17 1.55e-113 PDB 3HTF "4-Chloro-1h-Pyrazole In Complex With T4 Lysozyme L99aM102Q" 100.00 164 97.56 98.17 1.55e-113 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 PDB 3HU8 "2-Ethoxyphenol In Complex With T4 Lysozyme L99aM102Q" 100.00 164 97.56 98.17 1.55e-113 PDB 3HU9 "Nitrosobenzene In Complex With T4 Lysozyme L99aM102Q" 100.00 164 97.56 98.17 1.55e-113 PDB 3HUA "4,5,6,7-Tetrahydroindole In Complex With T4 Lysozyme L99aM102Q" 100.00 164 97.56 98.17 1.55e-113 PDB 3HUK "Benzylacetate In Complex With T4 Lysozyme L99aM102Q" 100.00 164 97.56 98.17 1.55e-113 PDB 3HUQ "Thieno[3,2-B]thiophene In Complex With T4 Lysozyme L99aM102Q" 98.78 162 97.53 98.15 3.23e-112 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 PDB 3K2R "Crystal Structure Of Spin Labeled T4 Lysozyme Mutant K65v1R76V1" 100.00 164 97.56 97.56 2.37e-111 PDB 3L2X "Crystal Structure Of Spin Labeled T4 Lysozyme Mutant 115-119rx" 100.00 164 97.56 97.56 1.34e-111 PDB 3L64 "T4 Lysozyme S44e/wt*" 100.00 164 98.17 98.17 8.43e-114 PDB 3LZM "Structural Studies Of Mutants Of T4 Lysozyme That Alter Hydrophobic Stabilization" 100.00 164 100.00 100.00 8.06e-117 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 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 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 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 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 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 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 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 PDB 3P0G "Structure Of A Nanobody-Stabilized Active State Of The Beta2 Adrenoceptor" 98.78 501 98.15 98.77 2.37e-107 PDB 3PBL "Structure Of The Human Dopamine D3 Receptor In Complex With Eticlopride" 97.56 481 98.75 98.75 3.26e-107 PDB 3PDS "Irreversible Agonist-Beta2 Adrenoceptor Complex" 98.78 458 98.15 98.77 1.63e-108 PDB 3QAK "Agonist Bound Structure Of The Human Adenosine A2a Receptor" 99.39 488 96.93 98.77 1.23e-107 PDB 3RUN "New Strategy To Analyze Structures Of Glycopeptide Antibiotic-Target Complexes" 99.39 168 98.77 98.77 5.07e-114 PDB 3RZE "Structure Of The Human Histamine H1 Receptor In Complex With Doxepin" 99.39 452 96.93 98.16 1.60e-107 PDB 3SB5 "Zn-Mediated Trimer Of T4 Lysozyme R125cE128C BY SYNTHETIC Symmetrization" 98.78 165 97.53 97.53 1.32e-109 PDB 3SB8 "Cu-Mediated Dimer Of T4 Lysozyme D61hK65H BY SYNTHETIC SYMMETRIZATION" 98.78 165 97.53 97.53 2.27e-111 PDB 3SB9 "Cu-Mediated Dimer Of T4 Lysozyme R76hR80H BY SYNTHETIC SYMMETRIZATION" 98.78 165 97.53 97.53 1.75e-111 PDB 3SBA "Zn-Mediated Hexamer Of T4 Lysozyme R76hR80H BY SYNTHETIC Symmetrization" 98.78 165 97.53 97.53 1.75e-111 PDB 3SBB "Disulphide-Mediated Tetramer Of T4 Lysozyme R76cR80C BY SYNTHETIC Symmetrization" 98.78 165 97.53 97.53 1.25e-109 PDB 3SN6 "Crystal Structure Of The Beta2 Adrenergic Receptor-Gs Protein Complex" 97.56 514 98.75 98.75 2.59e-106 PDB 3UON "Structure Of The Human M2 Muscarinic Acetylcholine Receptor Bound To An Antagonist" 98.78 467 97.53 98.15 1.25e-107 PDB 3V2W "Crystal Structure Of A Lipid G Protein-Coupled Receptor At 3.35a" 98.78 520 97.53 98.15 2.22e-107 PDB 3V2Y "Crystal Structure Of A Lipid G Protein-Coupled Receptor At 2.80a" 98.78 520 97.53 98.15 2.22e-107 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 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 PDB 4DAJ "Structure Of The M3 Muscarinic Acetylcholine Receptor" 98.17 479 98.76 98.76 1.34e-107 PDB 4DJH "Structure Of The Human Kappa Opioid Receptor In Complex With Jdtic" 98.17 480 98.14 98.76 8.37e-108 PDB 4DKL "Crystal Structure Of The Mu-Opioid Receptor Bound To A Morphinan Antagonist" 98.17 464 97.52 98.76 6.05e-107 PDB 4EJ4 "Structure Of The Delta Opioid Receptor Bound To Naltrindole" 98.17 461 97.52 98.76 9.31e-107 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 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 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 PDB 4HTT "Crystal Structure Of Twin Arginine Translocase Receptor- Tatc In Ddm" 100.00 418 98.78 98.78 1.20e-113 PDB 4IAP "Crystal Structure Of Ph Domain Of Osh3 From Saccharomyces Cerevisiae" 97.56 260 98.13 98.75 8.20e-109 PDB 4LDE "Structure Of Beta2 Adrenoceptor Bound To Bi167107 And An Engineered Nanobody" 97.56 469 98.75 98.75 3.99e-107 PDB 4LDL "Structure Of Beta2 Adrenoceptor Bound To Hydroxybenzylisoproterenol And An Engineered Nanobody" 97.56 469 98.75 98.75 3.99e-107 PDB 4LDO "Structure Of Beta2 Adrenoceptor Bound To Adrenaline And An Engineered Nanobody" 97.56 469 98.75 98.75 3.99e-107 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 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 PDB 4PHU "Crystal Structure Of Human Gpr40 Bound To Allosteric Agonist Tak-875" 99.39 491 97.55 98.16 2.51e-107 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 PDB 4PK0 "Crystal Structure Of T4 Lysozyme-peptide In Complex With Teicoplanin- A2-2" 100.00 171 98.78 98.78 1.84e-114 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 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 PDB 4TN3 "Structure Of The Bbox-coiled-coil Region Of Rhesus Trim5alpha" 100.00 400 98.17 98.78 5.78e-112 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 PDB 4W8F "Crystal Structure Of The Dynein Motor Domain In The Amppnp-bound State" 97.56 2661 98.75 98.75 7.03e-100 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 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 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 DBJ BAI83135 "lysozyme [Enterobacteria phage AR1]" 100.00 164 98.17 98.78 6.53e-115 EMBL CAA28212 "unnamed protein product [Enterobacteria phage T4]" 100.00 164 98.78 98.78 2.17e-114 GB AAA72629 "lysozyme [synthetic construct]" 100.00 164 100.00 100.00 8.06e-117 GB AAA72664 "synthetic T4-lysozyme [synthetic construct]" 100.00 164 100.00 100.00 8.06e-117 GB AAD42568 "e Lysozyme murein hydrolase [Enterobacteria phage T4]" 100.00 164 98.78 98.78 2.17e-114 GB ABI94948 "soluble lysozyme [Enterobacteria phage RB32]" 100.00 164 98.17 98.78 6.53e-115 GB ACP30771 "soluble lysozyme [Enterobacteria phage RB14]" 100.00 164 98.78 98.78 1.82e-115 REF NP_049736 "e Lysozyme murein hydrolase [Enterobacteria phage T4]" 100.00 164 98.78 98.78 2.17e-114 REF YP_002854084 "soluble lysozyme [Enterobacteria phage RB51]" 100.00 164 98.17 98.78 6.53e-115 REF YP_002854463 "soluble lysozyme [Enterobacteria phage RB14]" 100.00 164 98.78 98.78 1.82e-115 REF YP_004415022 "putative soluble lysozyme [Shigella phage Shfl2]" 100.00 164 96.95 97.56 7.83e-113 REF YP_006986678 "lysozyme murein hydrolase e [Enterobacteria phage vB_EcoM_ACG-C40]" 100.00 164 98.17 98.78 6.53e-115 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 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $T4_lysozyme 'Escherichia coli bacteriophage' 562 Bacteria . Escherichia coli 'wild type T4' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $T4_lysozyme 'not available' . Escherichia coli generic . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.6 . na temperature 293 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H . . . 0 . . . . . $entry_citation $entry_citation 'liquid ammonia' N . . . 0 . . . . . $entry_citation $entry_citation 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 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name 'T4 lysozyme' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 MET N N 39.9 . 1 2 . 2 ASN H H 6.99 . 1 3 . 2 ASN HA H 4.49 . 1 4 . 2 ASN N N 116.9 . 1 5 . 3 ILE H H 8.89 . 1 6 . 3 ILE HA H 4.12 . 1 7 . 3 ILE N N 118.6 . 1 8 . 4 PHE H H 7.56 . 1 9 . 4 PHE HA H 3.83 . 1 10 . 4 PHE HB2 H 3.05 . 2 11 . 4 PHE HB3 H 3.17 . 2 12 . 4 PHE HD1 H 6.77 . 1 13 . 4 PHE HD2 H 6.77 . 1 14 . 4 PHE HE1 H 6.93 . 1 15 . 4 PHE HE2 H 6.93 . 1 16 . 4 PHE HZ H 6.99 . 1 17 . 4 PHE N N 124.3 . 1 18 . 5 GLU H H 8.06 . 1 19 . 5 GLU HA H 3.7 . 1 20 . 5 GLU HB2 H 1.8 . 1 21 . 5 GLU HB3 H 1.8 . 1 22 . 5 GLU N N 119.2 . 1 23 . 6 MET H H 7.84 . 1 24 . 6 MET HA H 3.3 . 1 25 . 6 MET N N 119.3 . 1 26 . 7 LEU H H 7.91 . 1 27 . 7 LEU HA H 3.97 . 1 28 . 7 LEU N N 119 . 1 29 . 8 ARG H H 8.48 . 1 30 . 8 ARG HA H 3.41 . 1 31 . 8 ARG HB2 H 1.73 . 1 32 . 8 ARG HB3 H 1.73 . 1 33 . 8 ARG N N 123.9 . 1 34 . 9 ILE H H 7.52 . 1 35 . 9 ILE HA H 3.54 . 1 36 . 9 ILE HB H 2.08 . 1 37 . 9 ILE N N 120.8 . 1 38 . 10 ASP H H 7.97 . 1 39 . 10 ASP HA H 4.49 . 1 40 . 10 ASP HB2 H 2.6 . 1 41 . 10 ASP HB3 H 2.6 . 1 42 . 10 ASP N N 119.1 . 1 43 . 11 GLU H H 8.98 . 1 44 . 11 GLU HA H 4.59 . 1 45 . 11 GLU HB2 H 1.93 . 2 46 . 11 GLU HB3 H 2.11 . 2 47 . 11 GLU HG2 H 2.3 . 1 48 . 11 GLU HG3 H 2.3 . 1 49 . 11 GLU N N 119 . 1 50 . 12 GLY H H 7.4 . 1 51 . 12 GLY HA2 H 3.77 . 2 52 . 12 GLY HA3 H 4.13 . 2 53 . 12 GLY N N 110.3 . 1 54 . 13 LEU H H 7.98 . 1 55 . 13 LEU HA H 4.4 . 1 56 . 13 LEU HB2 H 1.69 . 1 57 . 13 LEU HB3 H 1.69 . 1 58 . 13 LEU N N 120.1 . 1 59 . 14 ARG H H 8.05 . 1 60 . 14 ARG HA H 4.69 . 1 61 . 14 ARG HB2 H 1.9 . 1 62 . 14 ARG HB3 H 1.9 . 1 63 . 14 ARG N N 128.5 . 1 64 . 15 LEU H H 8.83 . 1 65 . 15 LEU HA H 4.36 . 1 66 . 15 LEU HB2 H 1.6 . 1 67 . 15 LEU HB3 H 1.6 . 1 68 . 15 LEU N N 124.1 . 1 69 . 16 LYS H H 7.15 . 1 70 . 16 LYS HA H 5.43 . 1 71 . 16 LYS HB2 H 1.78 . 2 72 . 16 LYS HB3 H 1.93 . 2 73 . 16 LYS HG2 H 1.53 . 1 74 . 16 LYS HG3 H 1.53 . 1 75 . 16 LYS N N 115.7 . 1 76 . 17 ILE H H 7.53 . 1 77 . 17 ILE N N 121.4 . 1 78 . 18 TYR H H 9.48 . 1 79 . 18 TYR HA H 5.13 . 1 80 . 18 TYR HB2 H 3.01 . 2 81 . 18 TYR HB3 H 3.11 . 2 82 . 18 TYR HD1 H 7.19 . 1 83 . 18 TYR HD2 H 7.19 . 1 84 . 18 TYR HE1 H 6.57 . 1 85 . 18 TYR HE2 H 6.57 . 1 86 . 18 TYR N N 129 . 1 87 . 19 LYS H H 8.35 . 1 88 . 19 LYS HA H 4.58 . 1 89 . 19 LYS HB2 H 1.59 . 1 90 . 19 LYS HB3 H 1.59 . 1 91 . 19 LYS N N 121.9 . 1 92 . 20 ASP H H 8.54 . 1 93 . 20 ASP HA H 4.6 . 1 94 . 20 ASP N N 125.9 . 1 95 . 21 THR H H 8 . 1 96 . 21 THR HA H 4 . 1 97 . 21 THR HB H 4.32 . 1 98 . 21 THR HG2 H 1.38 . 1 99 . 21 THR N N 111.2 . 1 100 . 22 GLU H H 7.99 . 1 101 . 22 GLU HA H 4.17 . 1 102 . 22 GLU HB2 H 1.7 . 1 103 . 22 GLU HB3 H 1.7 . 1 104 . 22 GLU N N 121.3 . 1 105 . 23 GLY H H 7.88 . 1 106 . 23 GLY HA2 H 3.34 . 2 107 . 23 GLY HA3 H 3.98 . 2 108 . 23 GLY N N 108.1 . 1 109 . 24 TYR H H 8.16 . 1 110 . 24 TYR HA H 4.97 . 1 111 . 24 TYR HB2 H 2.91 . 2 112 . 24 TYR HB3 H 2.97 . 2 113 . 24 TYR HD1 H 7.12 . 1 114 . 24 TYR HD2 H 7.12 . 1 115 . 24 TYR HE1 H 6.81 . 1 116 . 24 TYR HE2 H 6.81 . 1 117 . 24 TYR N N 122.2 . 1 118 . 25 TYR H H 8.73 . 1 119 . 25 TYR HA H 4.9 . 1 120 . 25 TYR HB2 H 2.81 . 1 121 . 25 TYR HB3 H 2.81 . 1 122 . 25 TYR HD1 H 7.01 . 1 123 . 25 TYR HD2 H 7.01 . 1 124 . 25 TYR HE1 H 6.71 . 1 125 . 25 TYR HE2 H 6.71 . 1 126 . 25 TYR N N 124.1 . 1 127 . 26 THR H H 9.37 . 1 128 . 26 THR HA H 5.06 . 1 129 . 26 THR HB H 2.8 . 1 130 . 26 THR HG2 H 1.02 . 1 131 . 26 THR N N 122.6 . 1 132 . 27 ILE H H 8.85 . 1 133 . 27 ILE HA H 4.61 . 1 134 . 27 ILE N N 122.3 . 1 135 . 28 GLY H H 8.47 . 1 136 . 28 GLY HA2 H 3.58 . 2 137 . 28 GLY HA3 H 4.28 . 2 138 . 28 GLY N N 113.3 . 1 139 . 29 ILE H H 9.79 . 1 140 . 29 ILE HA H 4.75 . 1 141 . 29 ILE HB H 1.97 . 1 142 . 29 ILE N N 132 . 1 143 . 30 GLY H H 7.94 . 1 144 . 30 GLY N N 110 . 1 145 . 31 HIS H H 8.44 . 1 146 . 31 HIS HA H 4.61 . 1 147 . 31 HIS HB2 H 3.68 . 1 148 . 31 HIS HB3 H 3.68 . 1 149 . 31 HIS ND1 N 188 . 1 150 . 31 HIS NE2 N 174.4 . 1 151 . 31 HIS HD2 H 8.65 . 1 152 . 31 HIS HE1 H 6.38 . 1 153 . 31 HIS N N 117.6 . 1 154 . 32 LEU H H 8.17 . 1 155 . 32 LEU HA H 4.06 . 1 156 . 32 LEU HB2 H 1.41 . 1 157 . 32 LEU HB3 H 1.41 . 1 158 . 32 LEU N N 133.7 . 1 159 . 33 LEU H H 9.18 . 1 160 . 33 LEU HA H 4.48 . 1 161 . 33 LEU HB2 H 1.73 . 1 162 . 33 LEU HB3 H 1.73 . 1 163 . 33 LEU N N 127 . 1 164 . 34 THR H H 7.31 . 1 165 . 34 THR HA H 4.48 . 1 166 . 34 THR N N 110.9 . 1 167 . 35 LYS H H 8.61 . 1 168 . 35 LYS HA H 4.26 . 1 169 . 35 LYS HB2 H 1.42 . 1 170 . 35 LYS HB3 H 1.42 . 1 171 . 35 LYS N N 126.1 . 1 172 . 36 SER H H 8.81 . 1 173 . 36 SER HA H 4.66 . 1 174 . 36 SER HB2 H 3.88 . 2 175 . 36 SER HB3 H 4.03 . 2 176 . 36 SER N N 120.8 . 1 177 . 38 SER H H 8.26 . 1 178 . 38 SER HA H 4.74 . 1 179 . 38 SER HB2 H 3.88 . 1 180 . 38 SER HB3 H 3.88 . 1 181 . 38 SER N N 117.4 . 1 182 . 39 LEU H H 9 . 1 183 . 39 LEU HA H 3.37 . 1 184 . 39 LEU HB2 H 1.71 . 1 185 . 39 LEU HB3 H 1.71 . 1 186 . 39 LEU N N 134.4 . 1 187 . 40 ASN H H 8.31 . 1 188 . 40 ASN HA H 4.29 . 1 189 . 40 ASN HB2 H 2.62 . 2 190 . 40 ASN HB3 H 2.73 . 2 191 . 40 ASN N N 118.2 . 1 192 . 41 ALA H H 7.77 . 1 193 . 41 ALA HA H 4.24 . 1 194 . 41 ALA HB H 1.63 . 1 195 . 41 ALA N N 125.2 . 1 196 . 42 ALA H H 7.62 . 1 197 . 42 ALA HA H 3.74 . 1 198 . 42 ALA HB H 1.23 . 1 199 . 42 ALA N N 122.2 . 1 200 . 43 LYS H H 8.49 . 1 201 . 43 LYS HA H 3.73 . 1 202 . 43 LYS HB2 H 1.88 . 1 203 . 43 LYS HB3 H 1.88 . 1 204 . 43 LYS N N 117.9 . 1 205 . 44 SER H H 7.98 . 1 206 . 44 SER HA H 4.3 . 1 207 . 44 SER HB2 H 4.02 . 1 208 . 44 SER HB3 H 4.02 . 1 209 . 44 SER N N 115.7 . 1 210 . 45 GLU H H 8.16 . 1 211 . 45 GLU HA H 4.14 . 1 212 . 45 GLU HB2 H 2.02 . 1 213 . 45 GLU HB3 H 2.02 . 1 214 . 45 GLU N N 121.6 . 1 215 . 46 LEU H H 8.33 . 1 216 . 46 LEU HA H 3.97 . 1 217 . 46 LEU N N 123.4 . 1 218 . 47 ASP H H 8.12 . 1 219 . 47 ASP HA H 4.85 . 1 220 . 47 ASP HB2 H 2.72 . 1 221 . 47 ASP HB3 H 2.72 . 1 222 . 47 ASP N N 120.9 . 1 223 . 48 LYS H H 7.84 . 1 224 . 48 LYS HA H 4.02 . 1 225 . 48 LYS HB2 H 1.92 . 1 226 . 48 LYS HB3 H 1.92 . 1 227 . 48 LYS HG2 H 1.42 . 2 228 . 48 LYS HG3 H 1.61 . 2 229 . 48 LYS N N 122 . 1 230 . 49 ALA H H 8 . 1 231 . 49 ALA HA H 4.18 . 1 232 . 49 ALA HB H 1.5 . 1 233 . 49 ALA N N 122.4 . 1 234 . 50 ILE H H 8.32 . 1 235 . 50 ILE HA H 4.07 . 1 236 . 50 ILE HB H 1.96 . 1 237 . 50 ILE HG12 H .93 . 1 238 . 50 ILE HG13 H .93 . 1 239 . 50 ILE HG2 H .93 . 1 240 . 50 ILE N N 115.8 . 1 241 . 51 GLY H H 8.36 . 1 242 . 51 GLY HA2 H 3.77 . 2 243 . 51 GLY HA3 H 4.17 . 2 244 . 51 GLY N N 110 . 1 245 . 52 ARG H H 7.65 . 1 246 . 52 ARG HA H 4.56 . 1 247 . 52 ARG HB2 H 1.74 . 1 248 . 52 ARG HB3 H 1.74 . 1 249 . 52 ARG N N 117.3 . 1 250 . 53 ASN H H 8.32 . 1 251 . 53 ASN HA H 4.72 . 1 252 . 53 ASN HB2 H 2.7 . 2 253 . 53 ASN HB3 H 2.85 . 2 254 . 53 ASN N N 117.3 . 1 255 . 54 CYS H H 9.28 . 1 256 . 54 CYS HA H 4.5 . 1 257 . 54 CYS HB2 H 3.05 . 1 258 . 54 CYS HB3 H 3.05 . 1 259 . 54 CYS N N 126.5 . 1 260 . 55 ASN H H 9.45 . 1 261 . 55 ASN HA H 4.32 . 1 262 . 55 ASN HB2 H 2.57 . 2 263 . 55 ASN HB3 H 3.14 . 2 264 . 55 ASN N N 121.4 . 1 265 . 56 GLY H H 9.1 . 1 266 . 56 GLY HA2 H 3.31 . 2 267 . 56 GLY HA3 H 4.09 . 2 268 . 56 GLY N N 103.1 . 1 269 . 57 VAL H H 7.54 . 1 270 . 57 VAL HA H 5.18 . 1 271 . 57 VAL HB H 1.96 . 1 272 . 57 VAL HG1 H .99 . 1 273 . 57 VAL HG2 H .99 . 1 274 . 57 VAL N N 121.7 . 1 275 . 58 ILE H H 8.6 . 1 276 . 58 ILE HA H 4.9 . 1 277 . 58 ILE N N 117.8 . 1 278 . 59 THR H H 8.76 . 1 279 . 59 THR HA H 4.64 . 1 280 . 59 THR N N 110.2 . 1 281 . 60 LYS H H 9.17 . 1 282 . 60 LYS HA H 3.88 . 1 283 . 60 LYS N N 122.6 . 1 284 . 61 ASP H H 8.29 . 1 285 . 61 ASP HA H 4.38 . 1 286 . 61 ASP HB2 H 2.6 . 1 287 . 61 ASP HB3 H 2.6 . 1 288 . 61 ASP N N 118.6 . 1 289 . 62 GLU H H 7.73 . 1 290 . 62 GLU HA H 3.9 . 1 291 . 62 GLU HB2 H 2.58 . 1 292 . 62 GLU HB3 H 2.58 . 1 293 . 62 GLU N N 122.9 . 1 294 . 63 ALA H H 8.57 . 1 295 . 63 ALA HA H 3.91 . 1 296 . 63 ALA HB H 1.51 . 1 297 . 63 ALA N N 122.5 . 1 298 . 64 GLU H H 8.43 . 1 299 . 64 GLU HA H 3.88 . 1 300 . 64 GLU N N 121.8 . 1 301 . 65 LYS H H 7.76 . 1 302 . 65 LYS HA H 4.12 . 1 303 . 65 LYS HB2 H 1.98 . 1 304 . 65 LYS HB3 H 1.98 . 1 305 . 65 LYS N N 122.5 . 1 306 . 66 LEU H H 7.83 . 1 307 . 66 LEU HA H 3.91 . 1 308 . 66 LEU HB2 H 1.77 . 1 309 . 66 LEU HB3 H 1.77 . 1 310 . 66 LEU N N 119.6 . 1 311 . 67 PHE H H 8.22 . 1 312 . 67 PHE HA H 5.07 . 1 313 . 67 PHE HB2 H 3.39 . 1 314 . 67 PHE HB3 H 3.39 . 1 315 . 67 PHE HD1 H 7.57 . 1 316 . 67 PHE HD2 H 7.57 . 1 317 . 67 PHE HE1 H 7.04 . 1 318 . 67 PHE HE2 H 7.04 . 1 319 . 67 PHE N N 120.1 . 1 320 . 68 ASN H H 8.71 . 1 321 . 68 ASN HA H 4.29 . 1 322 . 68 ASN HB2 H 2.93 . 1 323 . 68 ASN HB3 H 2.93 . 1 324 . 68 ASN N N 119.3 . 1 325 . 69 GLN H H 7.65 . 1 326 . 69 GLN HA H 4.23 . 1 327 . 69 GLN HB2 H 2.44 . 1 328 . 69 GLN HB3 H 2.44 . 1 329 . 69 GLN N N 120 . 1 330 . 70 ASP H H 8.52 . 1 331 . 70 ASP HA H 4.64 . 1 332 . 70 ASP HB2 H 3.22 . 1 333 . 70 ASP HB3 H 3.22 . 1 334 . 70 ASP N N 124.6 . 1 335 . 71 VAL H H 9.2 . 1 336 . 71 VAL HA H 3.64 . 1 337 . 71 VAL HB H 1.94 . 1 338 . 71 VAL HG1 H .47 . 2 339 . 71 VAL HG2 H .84 . 2 340 . 71 VAL N N 126.2 . 1 341 . 72 ASP H H 7.75 . 1 342 . 72 ASP HA H 4.38 . 1 343 . 72 ASP HB2 H 2.87 . 1 344 . 72 ASP HB3 H 2.87 . 1 345 . 72 ASP N N 120.8 . 1 346 . 73 ALA H H 8.1 . 1 347 . 73 ALA HA H 4.04 . 1 348 . 73 ALA HB H 1.58 . 1 349 . 73 ALA N N 121.2 . 1 350 . 74 ALA H H 8.18 . 1 351 . 74 ALA HA H 4.19 . 1 352 . 74 ALA HB H 1.5 . 1 353 . 74 ALA N N 124.6 . 1 354 . 75 VAL H H 8.59 . 1 355 . 75 VAL HA H 3.26 . 1 356 . 75 VAL HB H 2.16 . 1 357 . 75 VAL HG1 H .78 . 2 358 . 75 VAL HG2 H 1.05 . 2 359 . 75 VAL N N 120.7 . 1 360 . 76 ARG H H 8.22 . 1 361 . 76 ARG HA H 3.82 . 1 362 . 76 ARG HB2 H 1.9 . 1 363 . 76 ARG HB3 H 1.9 . 1 364 . 76 ARG N N 119 . 1 365 . 77 GLY H H 7.92 . 1 366 . 77 GLY HA2 H 3.7 . 2 367 . 77 GLY HA3 H 3.86 . 2 368 . 77 GLY N N 106.8 . 1 369 . 78 ILE H H 7.96 . 1 370 . 78 ILE HA H 3.35 . 1 371 . 78 ILE HB H 1.79 . 1 372 . 78 ILE N N 123.9 . 1 373 . 79 LEU H H 7.93 . 1 374 . 79 LEU HA H 3.8 . 1 375 . 79 LEU N N 115.3 . 1 376 . 80 ARG H H 7.46 . 1 377 . 80 ARG HA H 4.36 . 1 378 . 80 ARG HB2 H 1.86 . 1 379 . 80 ARG HB3 H 1.86 . 1 380 . 80 ARG N N 117.3 . 1 381 . 81 ASN H H 7.63 . 1 382 . 81 ASN HA H 4.76 . 1 383 . 81 ASN N N 123 . 1 384 . 82 ALA H H 9.01 . 1 385 . 82 ALA HA H 4.1 . 1 386 . 82 ALA HB H 1.48 . 1 387 . 82 ALA N N 130.3 . 1 388 . 83 LYS H H 8.22 . 1 389 . 83 LYS HA H 4.34 . 1 390 . 83 LYS HB2 H 1.91 . 1 391 . 83 LYS HB3 H 1.91 . 1 392 . 83 LYS N N 114.8 . 1 393 . 84 LEU H H 7.9 . 1 394 . 84 LEU HA H 4.41 . 1 395 . 84 LEU HB2 H 2.16 . 1 396 . 84 LEU HB3 H 2.16 . 1 397 . 84 LEU N N 117 . 1 398 . 85 LYS H H 8.87 . 1 399 . 85 LYS HA H 3.88 . 1 400 . 85 LYS N N 124.3 . 1 401 . 87 VAL H H 6.8 . 1 402 . 87 VAL HA H 3.51 . 1 403 . 87 VAL HB H 2.28 . 1 404 . 87 VAL HG1 H .95 . 2 405 . 87 VAL HG2 H 1.11 . 2 406 . 87 VAL N N 117 . 1 407 . 88 TYR H H 8.43 . 1 408 . 88 TYR HA H 3.72 . 1 409 . 88 TYR HB2 H 3.13 . 1 410 . 88 TYR HB3 H 3.13 . 1 411 . 88 TYR HD1 H 7.03 . 1 412 . 88 TYR HD2 H 7.03 . 1 413 . 88 TYR HE1 H 6.73 . 1 414 . 88 TYR HE2 H 6.73 . 1 415 . 88 TYR N N 123 . 1 416 . 89 ASP H H 9.21 . 1 417 . 89 ASP HA H 4.31 . 1 418 . 89 ASP HB2 H 2.68 . 1 419 . 89 ASP HB3 H 2.68 . 1 420 . 89 ASP N N 118.8 . 1 421 . 90 SER H H 7.34 . 1 422 . 90 SER HA H 4.44 . 1 423 . 90 SER HB2 H 4.12 . 1 424 . 90 SER HB3 H 4.12 . 1 425 . 90 SER N N 114 . 1 426 . 91 LEU H H 7.3 . 1 427 . 91 LEU HA H 4.47 . 1 428 . 91 LEU HB2 H 2.34 . 1 429 . 91 LEU HB3 H 2.34 . 1 430 . 91 LEU N N 123.3 . 1 431 . 92 ASP H H 7.36 . 1 432 . 92 ASP HA H 4.64 . 1 433 . 92 ASP N N 115.7 . 1 434 . 93 ALA H H 8.72 . 1 435 . 93 ALA HA H 3.83 . 1 436 . 93 ALA HB H 1.55 . 1 437 . 93 ALA N N 120.8 . 1 438 . 94 VAL H H 7.77 . 1 439 . 94 VAL HA H 3.18 . 1 440 . 94 VAL HB H 1.32 . 1 441 . 94 VAL HG1 H .78 . 2 442 . 94 VAL HG2 H .56 . 2 443 . 94 VAL N N 118.8 . 1 444 . 95 ARG H H 7.94 . 1 445 . 95 ARG HA H 3.39 . 1 446 . 95 ARG HB2 H 1.64 . 1 447 . 95 ARG HB3 H 1.64 . 1 448 . 95 ARG N N 120.1 . 1 449 . 96 ARG H H 8.77 . 1 450 . 96 ARG HA H 3.7 . 1 451 . 96 ARG N N 119.4 . 1 452 . 97 CYS H H 7.3 . 1 453 . 97 CYS HA H 4.08 . 1 454 . 97 CYS N N 116.4 . 1 455 . 98 ALA H H 6.89 . 1 456 . 98 ALA HA H 3.68 . 1 457 . 98 ALA HB H .41 . 1 458 . 98 ALA N N 122.2 . 1 459 . 99 LEU H H 7.41 . 1 460 . 99 LEU HA H 4.22 . 1 461 . 99 LEU HB2 H 2.29 . 1 462 . 99 LEU HB3 H 2.29 . 1 463 . 99 LEU N N 119.9 . 1 464 . 100 ILE H H 8.55 . 1 465 . 100 ILE HA H 3.42 . 1 466 . 100 ILE HB H 1.87 . 1 467 . 100 ILE N N 119.7 . 1 468 . 101 ASN H H 8.28 . 1 469 . 101 ASN HA H 4.06 . 1 470 . 101 ASN N N 119.9 . 1 471 . 102 MET H H 7.58 . 1 472 . 102 MET HA H 4.36 . 1 473 . 102 MET HB2 H 2.19 . 1 474 . 102 MET HB3 H 2.19 . 1 475 . 102 MET N N 116.4 . 1 476 . 103 VAL H H 8.1 . 1 477 . 103 VAL HA H 3.32 . 1 478 . 103 VAL HB H 2.22 . 1 479 . 103 VAL HG1 H .9 . 1 480 . 103 VAL HG2 H .9 . 1 481 . 103 VAL N N 121.3 . 1 482 . 104 PHE H H 9.26 . 1 483 . 104 PHE HA H 4.13 . 1 484 . 104 PHE HB2 H 3.24 . 2 485 . 104 PHE HB3 H 3.39 . 2 486 . 104 PHE HD1 H 7.31 . 1 487 . 104 PHE HD2 H 7.31 . 1 488 . 104 PHE N N 125 . 1 489 . 105 GLN H H 8.03 . 1 490 . 105 GLN HA H 4.42 . 1 491 . 105 GLN HB2 H 2.21 . 1 492 . 105 GLN HB3 H 2.21 . 1 493 . 105 GLN N N 118.2 . 1 494 . 106 MET H H 8.65 . 1 495 . 106 MET HA H 4.78 . 1 496 . 106 MET HB2 H 2.15 . 1 497 . 106 MET HB3 H 2.15 . 1 498 . 106 MET N N 114.2 . 1 499 . 107 GLY H H 8.47 . 1 500 . 107 GLY HA2 H 3.97 . 2 501 . 107 GLY HA3 H 4.49 . 2 502 . 107 GLY N N 112.6 . 1 503 . 108 GLU H H 9.05 . 1 504 . 108 GLU HA H 3.68 . 1 505 . 108 GLU HB2 H 1.89 . 2 506 . 108 GLU HB3 H 2 . 2 507 . 108 GLU HG2 H 2.24 . 1 508 . 108 GLU HG3 H 2.24 . 1 509 . 108 GLU N N 121.2 . 1 510 . 109 THR H H 8.38 . 1 511 . 109 THR HA H 3.84 . 1 512 . 109 THR HB H 4.13 . 1 513 . 109 THR HG2 H 1.23 . 1 514 . 109 THR N N 113.4 . 1 515 . 110 GLY H H 7.77 . 1 516 . 110 GLY HA2 H 3.59 . 2 517 . 110 GLY HA3 H 3.82 . 2 518 . 110 GLY N N 110.4 . 1 519 . 111 VAL H H 7.66 . 1 520 . 111 VAL HA H 3.65 . 1 521 . 111 VAL HB H 1.85 . 1 522 . 111 VAL HG1 H .84 . 2 523 . 111 VAL HG2 H .93 . 2 524 . 111 VAL N N 122.9 . 1 525 . 112 ALA H H 8.13 . 1 526 . 112 ALA HA H 3.88 . 1 527 . 112 ALA HB H 1.43 . 1 528 . 112 ALA N N 119.8 . 1 529 . 113 GLY H H 7.28 . 1 530 . 113 GLY HA2 H 4.15 . 2 531 . 113 GLY HA3 H 3.8 . 2 532 . 113 GLY N N 102.8 . 1 533 . 114 PHE H H 7.99 . 1 534 . 114 PHE HA H 5.03 . 1 535 . 114 PHE HB2 H 3.13 . 2 536 . 114 PHE HB3 H 3.35 . 2 537 . 114 PHE HD1 H 7.5 . 1 538 . 114 PHE HD2 H 7.5 . 1 539 . 114 PHE HE1 H 7.27 . 1 540 . 114 PHE HE2 H 7.27 . 1 541 . 114 PHE HZ H 7.21 . 1 542 . 114 PHE N N 125.1 . 1 543 . 115 THR H H 7.87 . 1 544 . 115 THR HA H 3.69 . 1 545 . 115 THR HB H 4.07 . 1 546 . 115 THR HG2 H 1.27 . 1 547 . 115 THR N N 115.6 . 1 548 . 116 ASN H H 8.76 . 1 549 . 116 ASN HA H 4.54 . 1 550 . 116 ASN HB2 H 2.71 . 2 551 . 116 ASN HB3 H 2.98 . 2 552 . 116 ASN N N 120.2 . 1 553 . 117 SER H H 8.45 . 1 554 . 117 SER HA H 4.19 . 1 555 . 117 SER HB2 H 4 . 1 556 . 117 SER HB3 H 4 . 1 557 . 117 SER N N 119.7 . 1 558 . 118 LEU H H 8.59 . 1 559 . 118 LEU HA H 3.87 . 1 560 . 118 LEU HB2 H 1.91 . 1 561 . 118 LEU HB3 H 1.91 . 1 562 . 118 LEU N N 121.2 . 1 563 . 119 ARG H H 7.5 . 1 564 . 119 ARG HA H 4.08 . 1 565 . 119 ARG HB2 H 1.96 . 1 566 . 119 ARG HB3 H 1.96 . 1 567 . 119 ARG N N 119.9 . 1 568 . 120 MET H H 7.72 . 1 569 . 120 MET HA H 3.97 . 1 570 . 120 MET N N 117.7 . 1 571 . 121 LEU H H 8.2 . 1 572 . 121 LEU HA H 3.87 . 1 573 . 121 LEU N N 119.8 . 1 574 . 122 GLN H H 8.23 . 1 575 . 122 GLN HA H 3.98 . 1 576 . 122 GLN HB2 H 2.28 . 1 577 . 122 GLN HB3 H 2.28 . 1 578 . 122 GLN N N 121.9 . 1 579 . 123 GLN H H 7.33 . 1 580 . 123 GLN HA H 4.1 . 1 581 . 123 GLN HB2 H 1.74 . 1 582 . 123 GLN HB3 H 1.74 . 1 583 . 123 GLN N N 114.8 . 1 584 . 124 LYS H H 7.42 . 1 585 . 124 LYS HA H 1.4 . 1 586 . 124 LYS N N 115.6 . 1 587 . 125 ARG H H 7.77 . 1 588 . 125 ARG HA H 4.24 . 1 589 . 125 ARG HB2 H 1.42 . 1 590 . 125 ARG HB3 H 1.42 . 1 591 . 125 ARG N N 121.2 . 1 592 . 126 TRP H H 6.76 . 1 593 . 126 TRP HA H 4.35 . 1 594 . 126 TRP HB2 H 3.27 . 2 595 . 126 TRP HB3 H 3.87 . 2 596 . 126 TRP NE1 N 132 . 1 597 . 126 TRP HD1 H 7.42 . 1 598 . 126 TRP HE1 H 10.38 . 1 599 . 126 TRP HE3 H 7.26 . 1 600 . 126 TRP HZ2 H 7.58 . 1 601 . 126 TRP HZ3 H 6.92 . 1 602 . 126 TRP HH2 H 7.35 . 1 603 . 126 TRP N N 119.8 . 1 604 . 127 ASP H H 8.59 . 1 605 . 127 ASP HA H 4.43 . 1 606 . 127 ASP HB2 H 2.72 . 1 607 . 127 ASP HB3 H 2.72 . 1 608 . 127 ASP N N 117.8 . 1 609 . 128 GLU H H 8.33 . 1 610 . 128 GLU HA H 3.97 . 1 611 . 128 GLU HB2 H 2.11 . 1 612 . 128 GLU HB3 H 2.11 . 1 613 . 128 GLU N N 121.8 . 1 614 . 129 ALA H H 8.66 . 1 615 . 129 ALA HA H 4 . 1 616 . 129 ALA HB H 1.32 . 1 617 . 129 ALA N N 123.6 . 1 618 . 130 ALA H H 8.2 . 1 619 . 130 ALA HA H 4.07 . 1 620 . 130 ALA HB H 1.59 . 1 621 . 130 ALA N N 120 . 1 622 . 131 VAL H H 7.82 . 1 623 . 131 VAL HA H 3.6 . 1 624 . 131 VAL HB H 2.13 . 1 625 . 131 VAL HG1 H .92 . 2 626 . 131 VAL HG2 H 1.09 . 2 627 . 131 VAL N N 119.3 . 1 628 . 132 ASN H H 7.74 . 1 629 . 132 ASN HA H 4.33 . 1 630 . 132 ASN HB2 H 2.77 . 1 631 . 132 ASN HB3 H 2.77 . 1 632 . 132 ASN N N 119.4 . 1 633 . 133 LEU H H 9.01 . 1 634 . 133 LEU HA H 4.2 . 1 635 . 133 LEU HB2 H 2.09 . 1 636 . 133 LEU HB3 H 2.09 . 1 637 . 133 LEU N N 123.2 . 1 638 . 134 ALA H H 7.39 . 1 639 . 134 ALA HA H 3.67 . 1 640 . 134 ALA HB H .9 . 1 641 . 134 ALA N N 120.6 . 1 642 . 135 LYS H H 7.18 . 1 643 . 135 LYS HA H 4.42 . 1 644 . 135 LYS HB2 H 1.84 . 1 645 . 135 LYS HB3 H 1.84 . 1 646 . 135 LYS N N 119.3 . 1 647 . 136 SER H H 7.56 . 1 648 . 136 SER HA H 4.66 . 1 649 . 136 SER HB2 H 4.79 . 1 650 . 136 SER HB3 H 4.79 . 1 651 . 136 SER N N 114.4 . 1 652 . 137 ARG H H 8.96 . 1 653 . 137 ARG HA H 4.26 . 1 654 . 137 ARG HB2 H 2.02 . 1 655 . 137 ARG HB3 H 2.02 . 1 656 . 137 ARG N N 124.2 . 1 657 . 138 TRP H H 8.17 . 1 658 . 138 TRP HA H 4.55 . 1 659 . 138 TRP HB2 H 3.59 . 2 660 . 138 TRP HB3 H 3.68 . 2 661 . 138 TRP NE1 N 131.4 . 1 662 . 138 TRP HD1 H 7.3 . 1 663 . 138 TRP HE1 H 10.21 . 1 664 . 138 TRP HE3 H 7.78 . 1 665 . 138 TRP HZ2 H 7.66 . 1 666 . 138 TRP HZ3 H 6.95 . 1 667 . 138 TRP HH2 H 7.16 . 1 668 . 138 TRP N N 121.7 . 1 669 . 139 TYR H H 7.6 . 1 670 . 139 TYR HD1 H 6.71 . 1 671 . 139 TYR HD2 H 6.71 . 1 672 . 139 TYR HE1 H 6.63 . 1 673 . 139 TYR HE2 H 6.63 . 1 674 . 139 TYR N N 119 . 1 675 . 140 ASN H H 7.27 . 1 676 . 140 ASN HA H 4.37 . 1 677 . 140 ASN HB2 H 2.84 . 2 678 . 140 ASN HB3 H 2.89 . 2 679 . 140 ASN N N 112 . 1 680 . 141 GLN H H 8.32 . 1 681 . 141 GLN HA H 4.22 . 1 682 . 141 GLN HB2 H 2.22 . 2 683 . 141 GLN HB3 H 2.37 . 2 684 . 141 GLN N N 119.6 . 1 685 . 142 THR H H 7.62 . 1 686 . 142 THR HA H 4.74 . 1 687 . 142 THR HB H 4.51 . 1 688 . 142 THR HG2 H 1.17 . 1 689 . 142 THR N N 107.7 . 1 690 . 144 ASN H H 8 . 1 691 . 144 ASN HA H 4.31 . 1 692 . 144 ASN HB2 H 2.62 . 1 693 . 144 ASN HB3 H 2.62 . 1 694 . 144 ASN N N 117.9 . 1 695 . 145 ARG H H 7.84 . 1 696 . 145 ARG HA H 3.91 . 1 697 . 145 ARG N N 122 . 1 698 . 146 ALA H H 8.07 . 1 699 . 146 ALA HA H 3.71 . 1 700 . 146 ALA HB H .02 . 1 701 . 146 ALA N N 120.2 . 1 702 . 147 LYS H H 8.31 . 1 703 . 147 LYS HA H 3.96 . 1 704 . 147 LYS HB2 H 1.93 . 1 705 . 147 LYS HB3 H 1.93 . 1 706 . 147 LYS N N 116.9 . 1 707 . 148 ARG H H 7.35 . 1 708 . 148 ARG HA H 3.8 . 1 709 . 148 ARG N N 120.6 . 1 710 . 149 VAL H H 8.59 . 1 711 . 149 VAL HA H 3.36 . 1 712 . 149 VAL HB H 2.58 . 1 713 . 149 VAL HG1 H 1.1 . 2 714 . 149 VAL HG2 H 1.3 . 2 715 . 149 VAL N N 126.1 . 1 716 . 150 ILE H H 9.63 . 1 717 . 150 ILE HA H 3.9 . 1 718 . 150 ILE HB H 2.11 . 1 719 . 150 ILE N N 121.4 . 1 720 . 151 THR H H 8.67 . 1 721 . 151 THR HA H 3.95 . 1 722 . 151 THR HB H 4.24 . 1 723 . 151 THR HG2 H 1.31 . 1 724 . 151 THR N N 118.8 . 1 725 . 152 THR H H 7.9 . 1 726 . 152 THR HA H 3.95 . 1 727 . 152 THR HB H 4.31 . 1 728 . 152 THR HG1 H 5.54 . 1 729 . 152 THR HG2 H .56 . 1 730 . 152 THR N N 123.3 . 1 731 . 153 PHE H H 8.27 . 1 732 . 153 PHE HA H 4.14 . 1 733 . 153 PHE HB2 H 3.33 . 1 734 . 153 PHE HB3 H 3.33 . 1 735 . 153 PHE HD1 H 6.95 . 1 736 . 153 PHE HD2 H 6.95 . 1 737 . 153 PHE HE1 H 7.4 . 1 738 . 153 PHE HE2 H 7.4 . 1 739 . 153 PHE HZ H 6.72 . 1 740 . 153 PHE N N 121.2 . 1 741 . 154 ARG H H 9.06 . 1 742 . 154 ARG HA H 4.1 . 1 743 . 154 ARG HB2 H 2.09 . 1 744 . 154 ARG HB3 H 2.09 . 1 745 . 154 ARG N N 120.1 . 1 746 . 155 THR H H 8.19 . 1 747 . 155 THR HA H 4.26 . 1 748 . 155 THR N N 105.2 . 1 749 . 156 GLY H H 8.49 . 1 750 . 156 GLY HA2 H 3.15 . 2 751 . 156 GLY HA3 H 3.68 . 2 752 . 156 GLY N N 112.7 . 1 753 . 157 THR H H 7.61 . 1 754 . 157 THR HA H 4.67 . 1 755 . 157 THR HB H 4.4 . 1 756 . 157 THR HG2 H 1.09 . 1 757 . 157 THR N N 109.2 . 1 758 . 158 TRP H H 8.66 . 1 759 . 158 TRP HA H 5.11 . 1 760 . 158 TRP HB2 H 2.99 . 2 761 . 158 TRP HB3 H 3.79 . 2 762 . 158 TRP NE1 N 129.7 . 1 763 . 158 TRP HD1 H 7.23 . 1 764 . 158 TRP HE1 H 9.97 . 1 765 . 158 TRP HE3 H 7.27 . 1 766 . 158 TRP HZ2 H 7.42 . 1 767 . 158 TRP HZ3 H 6.38 . 1 768 . 158 TRP HH2 H 6.93 . 1 769 . 158 TRP N N 118.8 . 1 770 . 159 ASP H H 7.99 . 1 771 . 159 ASP HA H 4.31 . 1 772 . 159 ASP N N 120.8 . 1 773 . 160 ALA H H 9.12 . 1 774 . 160 ALA HA H 4.21 . 1 775 . 160 ALA HB H 1.24 . 1 776 . 160 ALA N N 120.6 . 1 777 . 161 TYR H H 8.06 . 1 778 . 161 TYR HA H 4.28 . 1 779 . 161 TYR HB2 H 2.79 . 1 780 . 161 TYR HB3 H 2.79 . 1 781 . 161 TYR HD1 H 7.14 . 1 782 . 161 TYR HD2 H 7.14 . 1 783 . 161 TYR HE1 H 6.61 . 1 784 . 161 TYR HE2 H 6.61 . 1 785 . 161 TYR HH H 11.29 . 1 786 . 161 TYR N N 114.7 . 1 787 . 162 LYS H H 7.26 . 1 788 . 162 LYS HA H 4.13 . 1 789 . 162 LYS HB2 H 1.81 . 1 790 . 162 LYS HB3 H 1.81 . 1 791 . 162 LYS N N 120.5 . 1 792 . 163 ASN H H 8.6 . 1 793 . 163 ASN HA H 4.59 . 1 794 . 163 ASN HB2 H 2.82 . 2 795 . 163 ASN HB3 H 2.92 . 2 796 . 163 ASN N N 117.8 . 1 797 . 164 LEU H H 7.4 . 1 798 . 164 LEU HA H 4.21 . 1 799 . 164 LEU HB2 H 1.56 . 2 800 . 164 LEU HB3 H 1.65 . 2 801 . 164 LEU N N 126.8 . 1 stop_ save_