data_2542 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H and 15N NMR Study of Human Lysozyme ; _BMRB_accession_number 2542 _BMRB_flat_file_name bmr2542.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-04-13 _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 Ohkubo Tadayasu . . 2 Taniyama Yoshio . . 3 Kikuchi Masakazu . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "15N chemical shifts" 148 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-17 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-04-13 revision BMRB 'Link to the Protein Data Bank added' 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 ; Ohkubo, Tadayasu, Taniyama, Yoshio, Kikuchi, Masakazu, "1H and 15N NMR Study of Human Lysozyme," J. Biochem. 110 (6), 1022-1029 (1991). ; _Citation_title '1H and 15N NMR Study of Human 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 Ohkubo Tadayasu . . 2 Taniyama Yoshio . . 3 Kikuchi Masakazu . . stop_ _Journal_abbreviation 'J. Biochem.' _Journal_volume 110 _Journal_issue 6 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1022 _Page_last 1029 _Year 1991 _Details . save_ ################################## # Molecular system description # ################################## save_system_lysozyme _Saveframe_category molecular_system _Mol_system_name lysozyme _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label lysozyme $lysozyme stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_lysozyme _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common lysozyme _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 130 _Mol_residue_sequence ; KVFERCELARTLKRLGMDGY RGISLANWMCLAKWESGYNT RATNYNAGDRSTDYGIFQIN SRYWCNDGKTPGAVNACHLS CSALLQDNIADAVACAKRVV RDPQGIRAWVAWRNRCQNRD VRQYVQGCGV ; loop_ _Residue_seq_code _Residue_label 1 LYS 2 VAL 3 PHE 4 GLU 5 ARG 6 CYS 7 GLU 8 LEU 9 ALA 10 ARG 11 THR 12 LEU 13 LYS 14 ARG 15 LEU 16 GLY 17 MET 18 ASP 19 GLY 20 TYR 21 ARG 22 GLY 23 ILE 24 SER 25 LEU 26 ALA 27 ASN 28 TRP 29 MET 30 CYS 31 LEU 32 ALA 33 LYS 34 TRP 35 GLU 36 SER 37 GLY 38 TYR 39 ASN 40 THR 41 ARG 42 ALA 43 THR 44 ASN 45 TYR 46 ASN 47 ALA 48 GLY 49 ASP 50 ARG 51 SER 52 THR 53 ASP 54 TYR 55 GLY 56 ILE 57 PHE 58 GLN 59 ILE 60 ASN 61 SER 62 ARG 63 TYR 64 TRP 65 CYS 66 ASN 67 ASP 68 GLY 69 LYS 70 THR 71 PRO 72 GLY 73 ALA 74 VAL 75 ASN 76 ALA 77 CYS 78 HIS 79 LEU 80 SER 81 CYS 82 SER 83 ALA 84 LEU 85 LEU 86 GLN 87 ASP 88 ASN 89 ILE 90 ALA 91 ASP 92 ALA 93 VAL 94 ALA 95 CYS 96 ALA 97 LYS 98 ARG 99 VAL 100 VAL 101 ARG 102 ASP 103 PRO 104 GLN 105 GLY 106 ILE 107 ARG 108 ALA 109 TRP 110 VAL 111 ALA 112 TRP 113 ARG 114 ASN 115 ARG 116 CYS 117 GLN 118 ASN 119 ARG 120 ASP 121 VAL 122 ARG 123 GLN 124 TYR 125 VAL 126 GLN 127 GLY 128 CYS 129 GLY 130 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-14 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 PDB 133L "Role Of Arg 115 In The Catalytic Action Of Human Lysozyme. X-Ray Structure Of His 115 And Glu 115 Mutants" 100.00 130 99.23 99.23 1.09e-88 PDB 134L "Role Of Arg 115 In The Catalytic Action Of Human Lysozyme. X-Ray Structure Of His 115 And Glu 115 Mutants" 100.00 130 99.23 99.23 1.14e-88 PDB 1B5U "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->al" 100.00 130 99.23 100.00 7.89e-89 PDB 1B5V "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->al" 100.00 130 99.23 100.00 7.89e-89 PDB 1B5W "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->al" 100.00 130 99.23 100.00 7.89e-89 PDB 1B5X "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->al" 100.00 130 99.23 100.00 7.89e-89 PDB 1B5Y "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->al" 100.00 130 99.23 100.00 7.89e-89 PDB 1B5Z "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->al" 100.00 130 99.23 100.00 7.89e-89 PDB 1B7L "Verification Of Spmp Using Mutant Human Lysozymes" 100.00 130 99.23 99.23 1.55e-88 PDB 1B7M "Verification Of Spmp Using Mutant Human Lysozymes" 100.00 130 99.23 99.23 1.32e-88 PDB 1B7N "Verification Of Spmp Using Mutant Human Lysozymes" 100.00 130 99.23 99.23 4.06e-88 PDB 1B7O "Verification Of Spmp Using Mutant Human Lysozymes" 100.00 130 99.23 99.23 2.62e-88 PDB 1B7P "Verification Of Spmp Using Mutant Human Lysozymes" 100.00 130 99.23 99.23 9.72e-88 PDB 1B7Q "Verification Of Spmp Using Mutant Human Lysozymes" 100.00 130 99.23 99.23 4.43e-88 PDB 1B7R "Verification Of Spmp Using Mutant Human Lysozymes" 100.00 130 99.23 99.23 3.84e-88 PDB 1B7S "Verification Of Spmp Using Mutant Human Lysozymes" 100.00 130 99.23 99.23 1.52e-88 PDB 1BB3 "Human Lysozyme Mutant A96l" 100.00 130 99.23 99.23 1.55e-88 PDB 1BB4 "Human Lysozyme Double Mutant A96l, W109h" 100.00 130 98.46 98.46 2.11e-87 PDB 1BB5 "Human Lysozyme Mutant A96l Complexed With Chitotriose" 100.00 130 99.23 99.23 1.55e-88 PDB 1C43 "Mutant Human Lysozyme With Foreign N-Terminal Residues" 99.23 130 100.00 100.00 1.36e-88 PDB 1C45 "Mutant Human Lysozyme With Foreign N-Terminal Residues" 99.23 130 100.00 100.00 1.42e-88 PDB 1C46 "Mutant Human Lysozyme With Foreign N-Terminal Residues" 100.00 131 100.00 100.00 2.70e-89 PDB 1C7P "Crystal Structure Of Mutant Human Lysozyme With Four Extra Residues (Eaea) At The N-Terminal" 100.00 134 100.00 100.00 1.64e-89 PDB 1CJ6 "T11a Mutant Human Lysozyme" 100.00 130 99.23 99.23 1.47e-88 PDB 1CJ7 "T11v Mutant Human Lysozyme" 100.00 130 99.23 99.23 1.33e-88 PDB 1CJ8 "T40a Mutant Human Lysozyme" 100.00 130 99.23 99.23 1.47e-88 PDB 1CJ9 "T40v Mutant Human Lysozyme" 100.00 130 99.23 99.23 1.33e-88 PDB 1CKC "T43a Mutant Human Lysozyme" 100.00 130 99.23 99.23 1.47e-88 PDB 1CKD "T43v Mutant Human Lysozyme" 100.00 130 99.23 99.23 1.33e-88 PDB 1CKF "T52a Mutant Human Lysozyme" 100.00 130 99.23 99.23 1.47e-88 PDB 1CKG "T52v Mutant Human Lysozyme" 100.00 130 99.23 99.23 1.33e-88 PDB 1CKH "T70v Mutant Human Lysozyme" 100.00 130 99.23 99.23 1.33e-88 PDB 1D6P "Human Lysozyme L63 Mutant Labelled With 2',3'-Epoxypropyl N,N'- Diacetylchitobiose" 100.00 130 99.23 99.23 3.02e-88 PDB 1D6Q "Human Lysozyme E102 Mutant Labelled With 2',3'-Epoxypropyl Glycoside Of N-Acetyllactosamine" 100.00 130 99.23 100.00 8.42e-89 PDB 1DI3 "Role Of Amino Acid Residues At Turns In The Conformational Stability And Folding Of Human Lysozyme" 100.00 130 99.23 99.23 3.30e-88 PDB 1DI4 "Role Of Amino Acid Residues At Turns In The Conformational Stability And Folding Of Human Lysozyme" 100.00 128 98.46 98.46 5.78e-86 PDB 1DI5 "Role Of Amino Acid Residues At Turns In The Conformational Stability And Folding Of Human Lysozyme" 100.00 129 99.23 99.23 7.66e-87 PDB 1EQ4 "Crystal Structures Of Salt Bridge Mutants Of Human Lysozyme" 100.00 130 99.23 100.00 8.89e-89 PDB 1EQ5 "Crystal Structures Of Salt Bridge Mutants Of Human Lysozyme" 100.00 130 99.23 100.00 1.26e-88 PDB 1EQE "Crystal Structures Of Salt Bridge Mutants Of Human Lysozyme" 100.00 130 99.23 100.00 1.26e-88 PDB 1GAY "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 99.23 3.30e-88 PDB 1GAZ "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 100.00 3.84e-89 PDB 1GB0 "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 100.00 7.07e-89 PDB 1GB2 "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 100.00 6.48e-89 PDB 1GB3 "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 99.23 1.16e-88 PDB 1GB5 "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 99.23 3.30e-88 PDB 1GB6 "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 100.00 3.84e-89 PDB 1GB7 "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 100.00 7.07e-89 PDB 1GB8 "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 100.00 6.48e-89 PDB 1GB9 "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 99.23 1.16e-88 PDB 1GBO "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 99.23 3.30e-88 PDB 1GBW "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 100.00 3.84e-89 PDB 1GBX "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 100.00 7.07e-89 PDB 1GBY "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 100.00 6.48e-89 PDB 1GBZ "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 99.23 1.16e-88 PDB 1GDW "Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions" 100.00 130 99.23 99.23 3.30e-88 PDB 1GDX "Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions" 100.00 130 99.23 99.23 2.08e-88 PDB 1GE0 "Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions" 100.00 130 99.23 99.23 6.28e-88 PDB 1GE1 "Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions" 100.00 130 99.23 99.23 1.97e-88 PDB 1GE2 "Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions" 100.00 130 99.23 99.23 6.42e-88 PDB 1GE3 "Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions" 100.00 130 99.23 99.23 2.15e-88 PDB 1GE4 "Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions" 100.00 130 99.23 99.23 2.71e-88 PDB 1GEV "Buried Polar Mutant Human Lysozyme" 100.00 130 99.23 99.23 1.38e-88 PDB 1GEZ "Buried Polar Mutant Human Lysozyme" 100.00 130 99.23 100.00 5.44e-89 PDB 1GF0 "Buried Polar Mutant Human Lysozyme" 100.00 130 99.23 100.00 5.44e-89 PDB 1GF3 "Buried Polar Mutant Human Lysozyme" 100.00 130 99.23 100.00 5.44e-89 PDB 1GF4 "Buried Polar Mutant Human Lysozyme" 100.00 130 99.23 99.23 9.29e-89 PDB 1GF5 "Buried Polar Mutant Human Lysozyme" 100.00 130 99.23 100.00 5.44e-89 PDB 1GF6 "Buried Polar Mutant Human Lysozyme" 100.00 130 99.23 99.23 9.29e-89 PDB 1GF7 "Buried Polar Mutant Human Lysozyme" 100.00 130 99.23 99.23 9.29e-89 PDB 1GF8 "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 99.23 1.52e-88 PDB 1GF9 "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 99.23 1.85e-88 PDB 1GFA "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 99.23 3.41e-88 PDB 1GFE "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 99.23 3.12e-88 PDB 1GFG "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 99.23 3.33e-88 PDB 1GFH "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 99.23 1.85e-88 PDB 1GFJ "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 99.23 3.41e-88 PDB 1GFK "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 99.23 3.12e-88 PDB 1GFR "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 99.23 3.33e-88 PDB 1GFT "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 99.23 1.85e-88 PDB 1GFU "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 99.23 3.41e-88 PDB 1GFV "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 99.23 3.12e-88 PDB 1HNL "Crystal Structure Of A Glutathionylated Human Lysozyme: A Folding Intermediate Mimic In The Formation Of A Disulfide Bond" 100.00 130 99.23 99.23 2.38e-88 PDB 1I1Z "Mutant Human Lysozyme (Q86d)" 100.00 130 99.23 99.23 2.38e-88 PDB 1I20 "Mutant Human Lysozyme (A92d)" 100.00 130 99.23 99.23 2.48e-88 PDB 1I22 "Mutant Human Lysozyme (A83kQ86DA92D)" 100.00 130 97.69 97.69 7.02e-87 PDB 1INU "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" 100.00 130 99.23 99.23 3.33e-88 PDB 1IOC "Crystal Structure Of Mutant Human Lysozyme, Eaea-I56t" 100.00 134 99.23 99.23 6.77e-89 PDB 1IP1 "G37a Human Lysozyme" 100.00 130 99.23 99.23 1.30e-88 PDB 1IP2 "G48a Human Lysozyme" 100.00 130 99.23 99.23 1.30e-88 PDB 1IP3 "G68a Human Lysozyme" 100.00 130 99.23 99.23 1.30e-88 PDB 1IP4 "G72a Human Lysozyme" 100.00 130 99.23 99.23 1.30e-88 PDB 1IP5 "G105a Human Lysozyme" 100.00 130 99.23 99.23 1.30e-88 PDB 1IP6 "G127a Human Lysozyme" 100.00 130 99.23 99.23 1.30e-88 PDB 1IP7 "G129a Human Lysozyme" 100.00 130 99.23 99.23 1.30e-88 PDB 1IWT "Crystal Structure Analysis Of Human Lysozyme At 113k." 100.00 130 100.00 100.00 2.79e-89 PDB 1IWU "Crystal Structure Analysis Of Human Lysozyme At 127k." 100.00 130 100.00 100.00 2.79e-89 PDB 1IWV "Crystal Structure Analysis Of Human Lysozyme At 147k." 100.00 130 100.00 100.00 2.79e-89 PDB 1IWW "Crystal Structure Analysis Of Human Lysozyme At 152k." 100.00 130 100.00 100.00 2.79e-89 PDB 1IWX "Crystal Structure Analysis Of Human Lysozyme At 161k." 100.00 130 100.00 100.00 2.79e-89 PDB 1IWY "Crystal Structure Analysis Of Human Lysozyme At 170k." 100.00 130 100.00 100.00 2.79e-89 PDB 1IWZ "Crystal Structure Analysis Of Human Lysozyme At 178k." 100.00 130 100.00 100.00 2.79e-89 PDB 1IX0 "I59a-3ss Human Lysozyme" 100.00 130 97.69 97.69 1.11e-86 PDB 1IY3 "Solution Structure Of The Human Lysozyme At 4 Degree C" 100.00 130 100.00 100.00 2.79e-89 PDB 1IY4 "Solution Structure Of The Human Lysozyme At 35 Degree C" 100.00 130 100.00 100.00 2.79e-89 PDB 1JKA "Human Lysozyme Mutant With Glu 35 Replaced By Asp" 100.00 130 99.23 100.00 1.25e-88 PDB 1JKB "Human Lysozyme Mutant With Glu 35 Replaced By Ala" 100.00 130 99.23 99.23 2.04e-88 PDB 1JKC "Human Lysozyme Mutant With Trp 109 Replaced By Phe" 100.00 130 99.23 100.00 1.25e-88 PDB 1JKD "Human Lysozyme Mutant With Trp 109 Replaced By Ala" 100.00 130 99.23 99.23 5.05e-88 PDB 1JSF "Full-Matrix Least-Squares Refinement Of Human Lysozyme" 100.00 130 100.00 100.00 2.79e-89 PDB 1JWR "Crystal Structure Of Human Lysozyme At 100 K" 100.00 130 100.00 100.00 2.79e-89 PDB 1LAA "X-Ray Structure Of Glu 53 Human Lysozyme" 100.00 130 99.23 100.00 8.42e-89 PDB 1LHH "Role Of Proline Residues In Human Lysozyme Stability: A Scanning Calorimetric Study Combined With X-Ray Structure Analysis Of P" 100.00 130 99.23 99.23 1.75e-88 PDB 1LHI "Role Of Proline Residues In Human Lysozyme Stability: A Scanning Calorimetric Study Combined With X-Ray Structure Analysis Of P" 100.00 130 99.23 99.23 8.08e-88 PDB 1LHJ "Role Of Proline Residues In Human Lysozyme Stability: A Scanning Calorimetric Study Combined With X-Ray Structure Analysis Of P" 100.00 130 99.23 99.23 8.08e-88 PDB 1LHK "Role Of Proline Residues In Human Lysozyme Stability: A Scanning Calorimetric Study Combined With X-Ray Structure Analysis Of P" 100.00 130 99.23 99.23 2.33e-88 PDB 1LHL "Role Of Proline Residues In Human Lysozyme Stability: A Scanning Calorimetric Study Combined With X-Ray Structure Analysis Of P" 100.00 130 99.23 99.23 1.19e-88 PDB 1LHM "The Crystal Structure Of A Mutant Lysozyme C77(Slash)95a With Increased Secretion Efficiency In Yeast" 100.00 130 98.46 98.46 1.64e-87 PDB 1LOZ "Amyloidogenic Variant (i56t) Variant Of Human Lysozyme" 100.00 130 99.23 99.23 1.23e-88 PDB 1LYY "Amyloidogenic Variant (Asp67his) Of Human Lysozyme" 100.00 130 99.23 99.23 2.08e-88 PDB 1LZ1 "Refinement Of Human Lysozyme At 1.5 Angstroms Resolution. Analysis Of Non-Bonded And Hydrogen-Bond Interactions" 100.00 130 100.00 100.00 2.79e-89 PDB 1LZ4 "Enthalpic Destabilization Of A Mutant Human Lysozyme Lacking A Disulfide Bridge Between Cysteine-77 And Cysteine-95" 100.00 130 99.23 99.23 2.38e-88 PDB 1LZ5 "Structural And Functional Analyses Of The Arg-Gly-Asp Sequence Introduced Into Human Lysozyme" 103.08 134 97.01 97.01 6.94e-87 PDB 1LZR "Structural Changes Of The Active Site Cleft And Different Saccharide Binding Modes In Human Lysozyme Co-Crystallized With Hexa-" 100.00 130 100.00 100.00 2.79e-89 PDB 1LZS "Structural Changes Of The Active Site Cleft And Different Saccharide Binding Modes In Human Lysozyme Co-Crystallized With Hexa-" 100.00 130 100.00 100.00 2.79e-89 PDB 1OP9 "Complex Of Human Lysozyme With Camelid Vhh Hl6 Antibody Fragment" 100.00 130 100.00 100.00 2.79e-89 PDB 1OUA "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The I56t Mutant" 100.00 130 99.23 99.23 1.23e-88 PDB 1OUB "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-ray Structure Of The V100a Mutant" 100.00 130 99.23 99.23 1.12e-88 PDB 1OUC "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V110a Mutant" 100.00 130 99.23 99.23 1.12e-88 PDB 1OUD "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V121a Mutant" 100.00 130 99.23 99.23 1.12e-88 PDB 1OUE "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V125a Mutant" 100.00 130 99.23 99.23 1.12e-88 PDB 1OUF "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V130a Mutant" 99.23 130 100.00 100.00 1.12e-88 PDB 1OUG "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V2a Mutant" 100.00 130 99.23 99.23 1.12e-88 PDB 1OUH "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V74a Mutant" 100.00 130 99.23 99.23 1.12e-88 PDB 1OUI "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V93a Mutant" 100.00 130 99.23 99.23 1.12e-88 PDB 1OUJ "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V99a Mutant" 100.00 130 99.23 99.23 1.12e-88 PDB 1QSW "Crystal Structure Analysis Of A Human Lysozyme Mutant W64c C65a" 100.00 130 98.46 98.46 1.07e-86 PDB 1RE2 "Human Lysozyme Labelled With Two 2',3'-epoxypropyl Beta-glycoside Of N-acetyllactosamine" 100.00 130 100.00 100.00 2.79e-89 PDB 1REM "Human Lysozyme With Man-B1,4-Glcnac Covalently Attached To Asp53" 100.00 130 100.00 100.00 2.79e-89 PDB 1REX "Native Human Lysozyme" 100.00 130 100.00 100.00 2.79e-89 PDB 1REY "Human Lysozyme-N,N'-Diacetylchitobiose Complex" 100.00 130 100.00 100.00 2.79e-89 PDB 1REZ "Human Lysozyme-N-Acetyllactosamine Complex" 100.00 130 100.00 100.00 2.79e-89 PDB 1TAY "Dissection Of The Functional Role Of Structural Elements Of Tyrosine-63 In The Catalytic Action Of Human Lysozyme" 100.00 130 99.23 99.23 3.64e-88 PDB 1TBY "Dissection Of The Functional Role Of Structural Elements Of Tyrosine-63 In The Catalytic Action Of Human Lysozyme" 100.00 130 99.23 99.23 3.02e-88 PDB 1TCY "Dissection Of The Functional Role Of Structural Elements Of Tyrosine-63 In The Catalytic Action Of Human Lysozyme" 100.00 130 99.23 100.00 6.99e-89 PDB 1TDY "Dissection Of The Functional Role Of Structural Elements Of Tyrosine-63 In The Catalytic Action Of Human Lysozyme" 100.00 130 99.23 100.00 2.06e-88 PDB 1UBZ "Crystal Structure Of Glu102-Mutant Human Lysozyme Doubly Labeled With 2',3'-Epoxypropyl Beta-Glycoside Of N-Acetyllactosamine" 100.00 130 99.23 100.00 8.42e-89 PDB 1W08 "Structure Of T70n Human Lysozyme" 100.00 130 99.23 99.23 1.52e-88 PDB 1WQM "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme" 100.00 130 99.23 100.00 6.99e-89 PDB 1WQN "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme" 100.00 130 99.23 100.00 6.99e-89 PDB 1WQO "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme" 100.00 130 99.23 100.00 6.99e-89 PDB 1WQP "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme" 100.00 130 99.23 100.00 6.99e-89 PDB 1WQQ "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme" 100.00 130 99.23 100.00 6.99e-89 PDB 1WQR "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme" 100.00 130 99.23 100.00 6.99e-89 PDB 1YAM "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of " 100.00 130 99.23 100.00 4.42e-89 PDB 1YAN "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of " 100.00 130 99.23 100.00 4.42e-89 PDB 1YAO "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of " 100.00 130 99.23 100.00 4.42e-89 PDB 1YAP "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of " 100.00 130 99.23 100.00 4.42e-89 PDB 1YAQ "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of " 100.00 130 99.23 100.00 4.42e-89 PDB 207L "Mutant Human Lysozyme C77a" 100.00 130 99.23 99.23 2.38e-88 PDB 208L "Mutant Human Lysozyme C77a" 100.00 130 99.23 99.23 2.38e-88 PDB 2BQA "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" 100.00 130 98.46 98.46 1.64e-87 PDB 2BQB "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" 100.00 130 97.69 98.46 2.90e-87 PDB 2BQC "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" 100.00 130 97.69 98.46 2.90e-87 PDB 2BQD "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" 100.00 130 97.69 98.46 2.90e-87 PDB 2BQE "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" 100.00 130 97.69 98.46 2.90e-87 PDB 2BQF "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" 100.00 130 97.69 98.46 2.90e-87 PDB 2BQG "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" 100.00 130 97.69 97.69 7.17e-87 PDB 2BQH "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" 100.00 130 97.69 97.69 7.17e-87 PDB 2BQI "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" 100.00 130 97.69 97.69 7.17e-87 PDB 2BQJ "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" 100.00 130 97.69 97.69 7.17e-87 PDB 2BQK "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" 99.23 130 98.45 98.45 7.17e-87 PDB 2BQL "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" 100.00 130 97.69 97.69 7.17e-87 PDB 2BQM "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" 100.00 130 97.69 97.69 7.17e-87 PDB 2BQN "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" 100.00 130 97.69 97.69 7.17e-87 PDB 2BQO "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" 100.00 130 97.69 97.69 7.17e-87 PDB 2HEA "Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability" 100.00 130 99.23 99.23 1.69e-88 PDB 2HEB "Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability" 100.00 130 99.23 99.23 1.69e-88 PDB 2HEC "Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability" 100.00 130 99.23 99.23 1.69e-88 PDB 2HED "Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability" 100.00 130 99.23 99.23 1.69e-88 PDB 2HEE "Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability" 100.00 130 99.23 99.23 4.24e-88 PDB 2HEF "Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability" 100.00 130 99.23 99.23 1.69e-88 PDB 2LHM "Crystal Structures Of The Apo-And Holomutant Human Lysozymes With An Introduced Ca2+ Binding Site" 100.00 130 98.46 98.46 1.96e-87 PDB 2MEA "Changes In Conformational Stability Of A Series Of Mutant Human Lysozymes At Constant Positions" 100.00 130 99.23 99.23 1.09e-88 PDB 2MEB "Changes In Conformational Stability Of A Series Of Mutant Human Lysozymes At Constant Positions" 100.00 130 99.23 100.00 5.75e-89 PDB 2MEC "Changes In Conformational Stability Of A Series Of Mutant Human Lysozymes At Constant Positions" 100.00 130 99.23 100.00 6.70e-89 PDB 2MED "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" 100.00 130 99.23 99.23 1.09e-88 PDB 2MEE "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" 100.00 130 99.23 100.00 5.75e-89 PDB 2MEF "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" 100.00 130 99.23 100.00 6.70e-89 PDB 2MEG "Changes In Conformational Stability Of A Series Of Mutant Human Lysozymes At Constant Positions" 100.00 130 99.23 99.23 2.08e-88 PDB 2MEH "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" 100.00 130 99.23 99.23 1.23e-88 PDB 2MEI "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" 100.00 130 99.23 99.23 2.25e-88 PDB 2NWD "Structure Of Chemically Synthesized Human Lysozyme At 1 Angstrom Resolution" 100.00 130 100.00 100.00 2.79e-89 PDB 2ZIJ "Crystal Structure Of Human Lysozyme Expressed In E. Coli." 100.00 130 100.00 100.00 2.79e-89 PDB 2ZIK "Crystal Structure Of Human Lysozyme From Pichia Pastoris" 100.00 130 100.00 100.00 2.79e-89 PDB 2ZIL "Crystal Structure Of Human Lysozyme From Urine" 100.00 130 100.00 100.00 2.79e-89 PDB 2ZWB "Neutron Crystal Structure Of Wild Type Human Lysozyme In D2o" 100.00 130 100.00 100.00 2.79e-89 PDB 3EBA "Cabhul6 Fglw Mutant (Humanized) In Complex With Human Lysozyme" 100.00 130 100.00 100.00 2.79e-89 PDB 3FE0 "X-Ray Crystal Structure Of Wild Type Human Lysozyme In D2o" 100.00 130 100.00 100.00 2.79e-89 PDB 3LHM "Crystal Structures Of The Apo-And Holomutant Human Lysozymes With An Introduced Ca2+ Binding Site" 100.00 130 98.46 98.46 1.96e-87 PDB 3LN2 "Crystal Structure Of A Charge Engineered Human Lysozyme Variant" 100.00 130 98.46 98.46 1.05e-87 PDB 4I0C "The Structure Of The Camelid Antibody Cabhul5 In Complex With Human Lysozyme" 100.00 130 100.00 100.00 2.79e-89 PDB 4ML7 "Crystal Structure Of Brucella Abortus Plic In Complex With Human Lysozyme" 100.00 130 100.00 100.00 2.79e-89 DBJ BAA00314 "lysozyme [synthetic construct]" 100.00 131 99.23 99.23 2.62e-88 DBJ BAG34722 "unnamed protein product [Homo sapiens]" 100.00 148 100.00 100.00 5.70e-90 DBJ BAG73364 "lysozyme [synthetic construct]" 100.00 148 99.23 99.23 5.00e-89 EMBL CAA32175 "lysozyme [Homo sapiens]" 100.00 130 100.00 100.00 2.79e-89 EMBL CAA53144 "lysozyme [synthetic construct]" 100.00 131 100.00 100.00 2.65e-89 GB AAA36188 "lysozyme precursor (EC 3.2.1.17) [Homo sapiens]" 100.00 148 99.23 100.00 1.56e-89 GB AAA59535 "lysozyme precursor (EC 3.2.1.17) [Homo sapiens]" 100.00 148 100.00 100.00 5.70e-90 GB AAA59536 "lysozyme precursor (EC 3.2.1.17) [Homo sapiens]" 100.00 148 100.00 100.00 5.70e-90 GB AAA72819 "lysozyme, partial [synthetic construct]" 100.00 130 100.00 100.00 2.79e-89 GB AAB26052 "lysozyme=amyloid fibril protein [human, Peptide Mutant, 130 aa]" 100.00 130 99.23 99.23 1.23e-88 REF NP_000230 "lysozyme C precursor [Homo sapiens]" 100.00 148 100.00 100.00 5.70e-90 REF NP_001009073 "lysozyme C precursor [Pan troglodytes]" 100.00 148 100.00 100.00 5.70e-90 REF NP_001266591 "lysozyme precursor [Gorilla gorilla]" 100.00 148 100.00 100.00 6.93e-90 REF XP_002823550 "PREDICTED: lysozyme C [Pongo abelii]" 100.00 148 99.23 99.23 2.23e-89 REF XP_003259554 "PREDICTED: lysozyme C isoform X2 [Nomascus leucogenys]" 100.00 148 96.92 99.23 4.90e-88 SP P61626 "RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor" 100.00 148 100.00 100.00 5.70e-90 SP P61627 "RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor" 100.00 148 100.00 100.00 5.70e-90 SP P61628 "RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor" 100.00 148 100.00 100.00 5.70e-90 SP P79179 "RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor" 100.00 148 100.00 100.00 6.93e-90 SP P79180 "RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor" 100.00 148 96.92 99.23 3.57e-88 TPE CDM98740 "TPA: lysozyme F1 [Homo sapiens]" 100.00 148 100.00 100.00 5.70e-90 TPE CDM98750 "TPA: lysozyme F1 [Pongo abelii]" 100.00 148 99.23 99.23 2.23e-89 TPE CDM98754 "TPA: lysozyme F1 [Nomascus leucogenys]" 100.00 148 96.92 99.23 4.90e-88 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $lysozyme Human 9606 Eukaryota Metazoa Homo sapiens 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 $lysozyme 'not available' . . . . . 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 4 . na temperature 313 . 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 'liquid NH3' N . . ppm 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 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 . 2 VAL N N 129.1 . 1 2 . 3 PHE N N 129.7 . 1 3 . 4 GLU N N 122.4 . 1 4 . 5 ARG N N 127.9 . 1 5 . 6 CYS N N 116.6 . 1 6 . 7 GLU N N 125.8 . 1 7 . 8 LEU N N 124.1 . 1 8 . 9 ALA N N 126 . 1 9 . 10 ARG N N 117.4 . 1 10 . 11 THR N N 120.8 . 1 11 . 12 LEU N N 121.4 . 1 12 . 13 LYS N N 121.6 . 1 13 . 14 ARG N N 123.8 . 1 14 . 15 LEU N N 119.3 . 1 15 . 16 GLY N N 108.6 . 1 16 . 17 MET N N 116.4 . 1 17 . 18 ASP N N 120.6 . 1 18 . 19 GLY N N 121.4 . 1 19 . 20 TYR N N 128.4 . 1 20 . 21 ARG N N 128.1 . 1 21 . 22 GLY N N 105.5 . 1 22 . 23 ILE N N 126.6 . 1 23 . 24 SER N N 125.2 . 1 24 . 25 LEU N N 124.1 . 1 25 . 26 ALA N N 120.8 . 1 26 . 27 ASN ND2 N 116.7 . 1 27 . 27 ASN N N 119.1 . 1 28 . 28 TRP NE1 N 130.8 . 1 29 . 28 TRP N N 122.3 . 1 30 . 29 MET N N 118.7 . 1 31 . 30 CYS N N 122 . 1 32 . 31 LEU N N 120.9 . 1 33 . 32 ALA N N 121.4 . 1 34 . 33 LYS N N 122.1 . 1 35 . 34 TRP NE1 N 129.2 . 1 36 . 34 TRP N N 120.1 . 1 37 . 35 GLU N N 118.5 . 1 38 . 36 SER N N 110.2 . 1 39 . 37 GLY N N 118.3 . 1 40 . 38 TYR N N 110.8 . 1 41 . 39 ASN ND2 N 113.5 . 1 42 . 39 ASN N N 119.6 . 1 43 . 40 THR N N 117.6 . 1 44 . 41 ARG N N 114.1 . 1 45 . 42 ALA N N 124.9 . 1 46 . 43 THR N N 116.2 . 1 47 . 44 ASN ND2 N 116.8 . 1 48 . 44 ASN N N 121.5 . 1 49 . 45 TYR N N 129.6 . 1 50 . 46 ASN ND2 N 116.1 . 1 51 . 46 ASN N N 130.3 . 1 52 . 47 ALA N N 127.8 . 1 53 . 48 GLY N N 106.4 . 1 54 . 49 ASP N N 119.1 . 1 55 . 50 ARG N N 116.6 . 1 56 . 51 SER N N 115.9 . 1 57 . 52 THR N N 118.5 . 1 58 . 53 ASP N N 126.7 . 1 59 . 54 TYR N N 120.7 . 1 60 . 55 GLY N N 114.6 . 1 61 . 56 ILE N N 123.9 . 1 62 . 57 PHE N N 117.6 . 1 63 . 58 GLN NE2 N 117.8 . 1 64 . 58 GLN N N 116.2 . 1 65 . 59 ILE N N 124.3 . 1 66 . 60 ASN ND2 N 117.8 . 1 67 . 60 ASN N N 129.9 . 1 68 . 61 SER N N 121.6 . 1 69 . 62 ARG N N 126 . 1 70 . 63 TYR N N 116.5 . 1 71 . 64 TRP NE1 N 130.3 . 1 72 . 64 TRP N N 116.9 . 1 73 . 65 CYS N N 113.4 . 1 74 . 66 ASN ND2 N 115.3 . 1 75 . 66 ASN N N 121.6 . 1 76 . 67 ASP N N 133.4 . 1 77 . 68 GLY N N 110.9 . 1 78 . 69 LYS N N 120 . 1 79 . 70 THR N N 122.9 . 1 80 . 72 GLY N N 112.5 . 1 81 . 73 ALA N N 113.1 . 1 82 . 74 VAL N N 122.7 . 1 83 . 75 ASN ND2 N 107.5 . 1 84 . 75 ASN N N 120.9 . 1 85 . 76 ALA N N 122.8 . 1 86 . 77 CYS N N 113 . 1 87 . 78 HIS N N 119.8 . 1 88 . 79 LEU N N 120.4 . 1 89 . 80 SER N N 119.6 . 1 90 . 81 CYS N N 128 . 1 91 . 82 SER N N 116.7 . 1 92 . 83 ALA N N 128 . 1 93 . 84 LEU N N 118.7 . 1 94 . 85 LEU N N 119.8 . 1 95 . 86 GLN NE2 N 115.1 . 1 96 . 86 GLN N N 118.6 . 1 97 . 87 ASP N N 122.3 . 1 98 . 88 ASN ND2 N 114.3 . 1 99 . 88 ASN N N 116.7 . 1 100 . 89 ILE N N 120.4 . 1 101 . 90 ALA N N 128.2 . 1 102 . 91 ASP N N 120.4 . 1 103 . 92 ALA N N 125.3 . 1 104 . 93 VAL N N 120.4 . 1 105 . 94 ALA N N 123.7 . 1 106 . 95 CYS N N 117.8 . 1 107 . 96 ALA N N 126.5 . 1 108 . 97 LYS N N 116.5 . 1 109 . 98 ARG N N 120.6 . 1 110 . 99 VAL N N 125.4 . 1 111 . 100 VAL N N 110.8 . 1 112 . 101 ARG N N 119.5 . 1 113 . 102 ASP N N 123.5 . 1 114 . 104 GLN NE2 N 113.4 . 1 115 . 104 GLN N N 116.2 . 1 116 . 105 GLY N N 111 . 1 117 . 106 ILE N N 128.4 . 1 118 . 107 ARG N N 119.1 . 1 119 . 108 ALA N N 122.4 . 1 120 . 109 TRP NE1 N 132.4 . 1 121 . 109 TRP N N 118.8 . 1 122 . 110 VAL N N 126.3 . 1 123 . 111 ALA N N 122.3 . 1 124 . 112 TRP NE1 N 130.6 . 1 125 . 112 TRP N N 117.1 . 1 126 . 113 ARG N N 121 . 1 127 . 114 ASN ND2 N 113.3 . 1 128 . 114 ASN N N 114 . 1 129 . 115 ARG N N 116.2 . 1 130 . 116 CYS N N 116.7 . 1 131 . 117 GLN NE2 N 111.5 . 1 132 . 117 GLN N N 123 . 1 133 . 118 ASN ND2 N 114.9 . 1 134 . 118 ASN N N 121.6 . 1 135 . 119 ARG N N 118.9 . 1 136 . 120 ASP N N 121.5 . 1 137 . 121 VAL N N 120.8 . 1 138 . 122 ARG N N 125.8 . 1 139 . 123 GLN NE2 N 113.5 . 1 140 . 123 GLN N N 118.2 . 1 141 . 124 TYR N N 118.8 . 1 142 . 125 VAL N N 107.1 . 1 143 . 126 GLN NE2 N 113.3 . 1 144 . 126 GLN N N 126.7 . 1 145 . 127 GLY N N 115.7 . 1 146 . 128 CYS N N 116.5 . 1 147 . 129 GLY N N 113.8 . 1 148 . 130 VAL N N 119.1 . 1 stop_ save_