data_5130 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignment of 1H, 13C and 15N resonances of Human Lysozyme at 35 C ; _BMRB_accession_number 5130 _BMRB_flat_file_name bmr5130.str _Entry_type original _Submission_date 2001-09-06 _Accession_date 2001-09-06 _Entry_origination author _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 Kumeta Hiroyuki . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 606 "13C chemical shifts" 248 "15N chemical shifts" 127 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-11-12 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 5142 'human lysozyme at 4 C' stop_ _Original_release_date 2001-09-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Assignment of 1H, 13C and 15N resonances of Human Lysozyme at 35 and 4 degree C ; _Citation_status 'in preparation' _Citation_type 'BMRB only' _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kumeta Hiroyuki . . stop_ _Journal_abbreviation . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . loop_ _Keyword 'human lysozyme' stop_ save_ ################################## # Molecular system description # ################################## save_system_human_lysozyme _Saveframe_category molecular_system _Mol_system_name 'human lysozyme at 35 degree C' _Abbreviation_common 'human lysozyme' _Enzyme_commission_number 3.2.1.17 loop_ _Mol_system_component_name _Mol_label 'human lysozyme' $human_lysozyme stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_human_lysozyme _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'human lysozyme' _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _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 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 2542 lysozyme 100.00 130 100.00 100.00 1.85e-70 BMRB 5123 lysozyme 100.00 130 100.00 100.00 1.85e-70 BMRB 5124 lysozyme 100.00 130 99.23 99.23 5.75e-70 BMRB 5125 lysozyme 100.00 130 99.23 99.23 8.58e-70 BMRB 5142 'human lysozyme' 100.00 130 100.00 100.00 1.85e-70 BMRB 76 lysozyme 100.00 130 99.23 100.00 3.75e-70 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 5.24e-70 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 5.42e-70 PDB 1B5U ; Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->ala Mutant ; 100.00 130 99.23 100.00 4.08e-70 PDB 1B5V ; Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->ala Mutants ; 100.00 130 99.23 100.00 4.08e-70 PDB 1B5W ; Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->ala Mutants ; 100.00 130 99.23 100.00 4.08e-70 PDB 1B5X ; Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->ala Mutants ; 100.00 130 99.23 100.00 4.08e-70 PDB 1B5Y ; Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->ala Mutants ; 100.00 130 99.23 100.00 4.08e-70 PDB 1B5Z ; Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->ala Mutants ; 100.00 130 99.23 100.00 4.08e-70 PDB 1B7L 'Verification Of Spmp Using Mutant Human Lysozymes' 100.00 130 99.23 99.23 6.85e-70 PDB 1B7M 'Verification Of Spmp Using Mutant Human Lysozymes' 100.00 130 99.23 99.23 6.04e-70 PDB 1B7N 'Verification Of Spmp Using Mutant Human Lysozymes' 100.00 130 99.23 99.23 1.43e-69 PDB 1B7O 'Verification Of Spmp Using Mutant Human Lysozymes' 100.00 130 99.23 99.23 1.02e-69 PDB 1B7P 'Verification Of Spmp Using Mutant Human Lysozymes' 100.00 130 99.23 99.23 2.78e-69 PDB 1B7Q 'Verification Of Spmp Using Mutant Human Lysozymes' 100.00 130 99.23 99.23 1.53e-69 PDB 1B7R 'Verification Of Spmp Using Mutant Human Lysozymes' 100.00 130 99.23 99.23 1.37e-69 PDB 1B7S 'Verification Of Spmp Using Mutant Human Lysozymes' 100.00 130 99.23 99.23 6.73e-70 PDB 1BB3 'Human Lysozyme Mutant A96l' 100.00 130 99.23 99.23 6.85e-70 PDB 1BB4 'Human Lysozyme Double Mutant A96l, W109h' 100.00 130 98.46 98.46 5.03e-69 PDB 1BB5 'Human Lysozyme Mutant A96l Complexed With Chitotriose' 100.00 130 99.23 99.23 6.85e-70 PDB 1C43 'Mutant Human Lysozyme With Foreign N-Terminal Residues' 99.23 130 100.00 100.00 6.19e-70 PDB 1C45 'Mutant Human Lysozyme With Foreign N-Terminal Residues' 99.23 130 100.00 100.00 6.41e-70 PDB 1C46 'Mutant Human Lysozyme With Foreign N-Terminal Residues' 100.00 131 100.00 100.00 1.76e-70 PDB 1C7P 'Crystal Structure Of Mutant Human Lysozyme With Four Extra Residues (Eaea) At The N-Terminal' 100.00 134 100.00 100.00 1.11e-70 PDB 1CJ6 'T11a Mutant Human Lysozyme' 100.00 130 99.23 99.23 6.57e-70 PDB 1CJ7 'T11v Mutant Human Lysozyme' 100.00 130 99.23 99.23 6.09e-70 PDB 1CJ8 'T40a Mutant Human Lysozyme' 100.00 130 99.23 99.23 6.57e-70 PDB 1CJ9 'T40v Mutant Human Lysozyme' 100.00 130 99.23 99.23 6.09e-70 PDB 1CKC 'T43a Mutant Human Lysozyme' 100.00 130 99.23 99.23 6.57e-70 PDB 1CKD 'T43v Mutant Human Lysozyme' 100.00 130 99.23 99.23 6.09e-70 PDB 1CKF 'T52a Mutant Human Lysozyme' 100.00 130 99.23 99.23 6.57e-70 PDB 1CKG 'T52v Mutant Human Lysozyme' 100.00 130 99.23 99.23 6.09e-70 PDB 1CKH 'T70v Mutant Human Lysozyme' 100.00 130 99.23 99.23 6.09e-70 PDB 1D6P "Human Lysozyme L63 Mutant Labelled With 2',3'-Epoxypropyl N, N'-Diacetylchitobiose" 100.00 130 99.23 99.23 1.14e-69 PDB 1D6Q "Human Lysozyme E102 Mutant Labelled With 2',3'-Epoxypropyl Glycoside Of N-Acetyllactosamine" 100.00 130 99.23 100.00 4.29e-70 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 1.22e-69 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 6.63e-68 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 1.38e-68 PDB 1EQ4 'Crystal Structures Of Salt Bridge Mutants Of Human Lysozyme' 100.00 130 99.23 100.00 4.47e-70 PDB 1EQ5 'Crystal Structures Of Salt Bridge Mutants Of Human Lysozyme' 100.00 130 99.23 100.00 5.84e-70 PDB 1EQE 'Crystal Structures Of Salt Bridge Mutants Of Human Lysozyme' 100.00 130 99.23 100.00 5.84e-70 PDB 1GAY 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 99.23 1.22e-69 PDB 1GAZ 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 100.00 2.35e-70 PDB 1GB0 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 100.00 3.75e-70 PDB 1GB2 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 100.00 3.51e-70 PDB 1GB3 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 99.23 5.47e-70 PDB 1GB5 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 99.23 1.22e-69 PDB 1GB6 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 100.00 2.35e-70 PDB 1GB7 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 100.00 3.75e-70 PDB 1GB8 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 100.00 3.51e-70 PDB 1GB9 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 99.23 5.47e-70 PDB 1GBO 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 99.23 1.22e-69 PDB 1GBW 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 100.00 2.35e-70 PDB 1GBX 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 100.00 3.75e-70 PDB 1GBY 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 100.00 3.51e-70 PDB 1GBZ 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 99.23 5.47e-70 PDB 1GDW 'Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions' 100.00 130 99.23 99.23 1.22e-69 PDB 1GDX 'Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions' 100.00 130 99.23 99.23 8.58e-70 PDB 1GE0 'Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions' 100.00 130 99.23 99.23 1.99e-69 PDB 1GE1 'Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions' 100.00 130 99.23 99.23 8.23e-70 PDB 1GE2 'Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions' 100.00 130 99.23 99.23 2.03e-69 PDB 1GE3 'Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions' 100.00 130 99.23 99.23 8.79e-70 PDB 1GE4 'Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions' 100.00 130 99.23 99.23 1.05e-69 PDB 1GEV 'Buried Polar Mutant Human Lysozyme' 100.00 130 99.23 99.23 6.25e-70 PDB 1GEZ 'Buried Polar Mutant Human Lysozyme' 100.00 130 99.23 100.00 3.07e-70 PDB 1GF0 'Buried Polar Mutant Human Lysozyme' 100.00 130 99.23 100.00 3.07e-70 PDB 1GF3 'Buried Polar Mutant Human Lysozyme' 100.00 130 99.23 100.00 3.07e-70 PDB 1GF4 'Buried Polar Mutant Human Lysozyme' 100.00 130 99.23 99.23 4.63e-70 PDB 1GF5 'Buried Polar Mutant Human Lysozyme' 100.00 130 99.23 100.00 3.07e-70 PDB 1GF6 'Buried Polar Mutant Human Lysozyme' 100.00 130 99.23 99.23 4.63e-70 PDB 1GF7 'Buried Polar Mutant Human Lysozyme' 100.00 130 99.23 99.23 4.63e-70 PDB 1GF8 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 99.23 6.73e-70 PDB 1GF9 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 99.23 7.83e-70 PDB 1GFA 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 99.23 1.25e-69 PDB 1GFE 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 99.23 1.17e-69 PDB 1GFG 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 99.23 1.23e-69 PDB 1GFH 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 99.23 7.83e-70 PDB 1GFJ 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 99.23 1.25e-69 PDB 1GFK 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 99.23 1.17e-69 PDB 1GFR 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 99.23 1.23e-69 PDB 1GFT 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 99.23 7.83e-70 PDB 1GFU 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 99.23 1.25e-69 PDB 1GFV 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 99.23 1.17e-69 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 9.48e-70 PDB 1I1Z 'Mutant Human Lysozyme (Q86d)' 100.00 130 99.23 99.23 9.48e-70 PDB 1I20 'Mutant Human Lysozyme (A92d)' 100.00 130 99.23 99.23 9.80e-70 PDB 1INU 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' 100.00 130 99.23 99.23 1.23e-69 PDB 1IOC 'Crystal Structure Of Mutant Human Lysozyme, Eaea-I56t' 100.00 134 99.23 99.23 3.29e-70 PDB 1IP1 'G37a Human Lysozyme' 100.00 130 99.23 99.23 5.99e-70 PDB 1IP2 'G48a Human Lysozyme' 100.00 130 99.23 99.23 5.99e-70 PDB 1IP3 'G68a Human Lysozyme' 100.00 130 99.23 99.23 5.99e-70 PDB 1IP4 'G72a Human Lysozyme' 100.00 130 99.23 99.23 5.99e-70 PDB 1IP5 'G105a Human Lysozyme' 100.00 130 99.23 99.23 5.99e-70 PDB 1IP6 'G127a Human Lysozyme' 100.00 130 99.23 99.23 5.99e-70 PDB 1IP7 'G129a Human Lysozyme' 100.00 130 99.23 99.23 5.99e-70 PDB 1IWT 'Crystal Structure Analysis Of Human Lysozyme At 113k.' 100.00 130 100.00 100.00 1.85e-70 PDB 1IWU 'Crystal Structure Analysis Of Human Lysozyme At 127k.' 100.00 130 100.00 100.00 1.85e-70 PDB 1IWV 'Crystal Structure Analysis Of Human Lysozyme At 147k.' 100.00 130 100.00 100.00 1.85e-70 PDB 1IWW 'Crystal Structure Analysis Of Human Lysozyme At 152k.' 100.00 130 100.00 100.00 1.85e-70 PDB 1IWX 'Crystal Structure Analysis Of Human Lysozyme At 161k.' 100.00 130 100.00 100.00 1.85e-70 PDB 1IWY 'Crystal Structure Analysis Of Human Lysozyme At 170k.' 100.00 130 100.00 100.00 1.85e-70 PDB 1IWZ 'Crystal Structure Analysis Of Human Lysozyme At 178k.' 100.00 130 100.00 100.00 1.85e-70 PDB 1IY3 'Solution Structure Of The Human Lysozyme At 4 Degree C' 100.00 130 100.00 100.00 1.85e-70 PDB 1IY4 'Solution Structure Of The Human Lysozyme At 35 Degree C' 100.00 130 100.00 100.00 1.85e-70 PDB 1JKA 'Human Lysozyme Mutant With Glu 35 Replaced By Asp' 100.00 130 99.23 100.00 5.79e-70 PDB 1JKB 'Human Lysozyme Mutant With Glu 35 Replaced By Ala' 100.00 130 99.23 99.23 8.44e-70 PDB 1JKC 'Human Lysozyme Mutant With Trp 109 Replaced By Phe' 100.00 130 99.23 100.00 5.79e-70 PDB 1JKD 'Human Lysozyme Mutant With Trp 109 Replaced By Ala' 100.00 130 99.23 99.23 1.69e-69 PDB 1JSF 'Full-Matrix Least-Squares Refinement Of Human Lysozyme' 100.00 130 100.00 100.00 1.85e-70 PDB 1JWR 'Crystal Structure Of Human Lysozyme At 100 K' 100.00 130 100.00 100.00 1.85e-70 PDB 1LAA 'X-Ray Structure Of Glu 53 Human Lysozyme' 100.00 130 99.23 100.00 4.29e-70 PDB 1LHH ; Role Of Proline Residues In Human Lysozyme Stability: A Scanning Calorimetric Study Combined With X-Ray Structure Analysis Of Proline Mutants ; 100.00 130 99.23 99.23 7.51e-70 PDB 1LHI ; Role Of Proline Residues In Human Lysozyme Stability: A Scanning Calorimetric Study Combined With X-Ray Structure Analysis Of Proline Mutants ; 100.00 130 99.23 99.23 2.41e-69 PDB 1LHJ ; Role Of Proline Residues In Human Lysozyme Stability: A Scanning Calorimetric Study Combined With X-Ray Structure Analysis Of Proline Mutants ; 100.00 130 99.23 99.23 2.41e-69 PDB 1LHK ; Role Of Proline Residues In Human Lysozyme Stability: A Scanning Calorimetric Study Combined With X-Ray Structure Analysis Of Proline Mutants ; 100.00 130 99.23 99.23 9.32e-70 PDB 1LHL ; Role Of Proline Residues In Human Lysozyme Stability: A Scanning Calorimetric Study Combined With X-Ray Structure Analysis Of Proline Mutants ; 100.00 130 99.23 99.23 5.60e-70 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 4.15e-69 PDB 1LOZ 'Amyloidogenic Variant (I56t) Variant Of Human Lysozyme' 100.00 130 99.23 99.23 5.75e-70 PDB 1LYY 'Amyloidogenic Variant (Asp67his) Of Human Lysozyme' 100.00 130 99.23 99.23 8.58e-70 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 1.85e-70 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 9.48e-70 PDB 1LZR ; Structural Changes Of The Active Site Cleft And Different saccharide Binding Modes In Human Lysozyme Co-Crystallized With Hexa-N-Acetyl-Chitohexaose At Ph 4.0 ; 100.00 130 100.00 100.00 1.85e-70 PDB 1LZS ; Structural Changes Of The Active Site Cleft And Different saccharide Binding Modes In Human Lysozyme Co-Crystallized With Hexa-N-Acetyl-Chitohexaose At Ph 4.0 ; 100.00 130 100.00 100.00 1.85e-70 PDB 1OP9 'Complex Of Human Lysozyme With Camelid Vhh Hl6 Antibody Fragment' 100.00 130 100.00 100.00 1.85e-70 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 5.75e-70 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 5.33e-70 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 5.33e-70 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 5.33e-70 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 5.33e-70 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 5.33e-70 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 5.33e-70 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 5.33e-70 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 5.33e-70 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 5.33e-70 PDB 1QSW 'Crystal Structure Analysis Of A Human Lysozyme Mutant W64c C65a' 100.00 130 98.46 98.46 1.74e-68 PDB 1RE2 "Human Lysozyme Labelled With Two 2',3'-Epoxypropyl Beta- Glycoside Of N-Acetyllactosamine" 100.00 130 100.00 100.00 1.85e-70 PDB 1REM 'Human Lysozyme With Man-B1,4-Glcnac Covalently Attached To Asp53' 100.00 130 100.00 100.00 1.85e-70 PDB 1REX 'Native Human Lysozyme' 100.00 130 100.00 100.00 1.85e-70 PDB 1REY "Human Lysozyme-N,N'-Diacetylchitobiose Complex" 100.00 130 100.00 100.00 1.85e-70 PDB 1REZ 'Human Lysozyme-N-Acetyllactosamine Complex' 100.00 130 100.00 100.00 1.85e-70 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 1.31e-69 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 1.14e-69 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 3.72e-70 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 8.51e-70 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 4.29e-70 PDB 1W08 'Structure Of T70n Human Lysozyme' 100.00 130 99.23 99.23 6.73e-70 PDB 1WQM 'Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme' 100.00 130 99.23 100.00 3.72e-70 PDB 1WQN 'Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme' 100.00 130 99.23 100.00 3.72e-70 PDB 1WQO 'Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme' 100.00 130 99.23 100.00 3.72e-70 PDB 1WQP 'Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme' 100.00 130 99.23 100.00 3.72e-70 PDB 1WQQ 'Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme' 100.00 130 99.23 100.00 3.72e-70 PDB 1WQR 'Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme' 100.00 130 99.23 100.00 3.72e-70 PDB 1YAM ; Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of The Five Isoleucine To Valine Mutants ; 100.00 130 99.23 100.00 2.62e-70 PDB 1YAN ; Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of The Five Isoleucine To Valine Mutants ; 100.00 130 99.23 100.00 2.62e-70 PDB 1YAO ; Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of The Five Isoleucine To Valine Mutants ; 100.00 130 99.23 100.00 2.62e-70 PDB 1YAP ; Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of The Five Isoleucine To Valine Mutants ; 100.00 130 99.23 100.00 2.62e-70 PDB 1YAQ ; Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of The Five Isoleucine To Valine Mutants ; 100.00 130 99.23 100.00 2.62e-70 PDB 207L 'Mutant Human Lysozyme C77a' 100.00 130 99.23 99.23 9.48e-70 PDB 208L 'Mutant Human Lysozyme C77a' 100.00 130 99.23 99.23 9.48e-70 PDB 2BQA 'Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme' 100.00 130 98.46 98.46 4.15e-69 PDB 2BQK 'Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme' 99.23 130 98.45 98.45 1.28e-68 PDB 2HEA 'Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability' 100.00 130 99.23 99.23 7.32e-70 PDB 2HEB 'Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability' 100.00 130 99.23 99.23 7.32e-70 PDB 2HEC 'Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability' 100.00 130 99.23 99.23 7.32e-70 PDB 2HED 'Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability' 100.00 130 99.23 99.23 7.32e-70 PDB 2HEE 'Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability' 100.00 130 99.23 99.23 1.48e-69 PDB 2HEF 'Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability' 100.00 130 99.23 99.23 7.32e-70 PDB 2LHM 'Crystal Structures Of The Apo-And Holomutant Human Lysozymes With An Introduced Ca2+ Binding Site' 100.00 130 98.46 98.46 4.74e-69 PDB 2MEA 'Changes In Conformational Stability Of A Series Of Mutant Human Lysozymes At Constant Positions' 100.00 130 99.23 99.23 5.24e-70 PDB 2MEB 'Changes In Conformational Stability Of A Series Of Mutant Human Lysozymes At Constant Positions' 100.00 130 99.23 100.00 3.20e-70 PDB 2MEC 'Changes In Conformational Stability Of A Series Of Mutant Human Lysozymes At Constant Positions' 100.00 130 99.23 100.00 3.60e-70 PDB 2MED 'Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme' 100.00 130 99.23 99.23 5.24e-70 PDB 2MEE 'Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme' 100.00 130 99.23 100.00 3.20e-70 PDB 2MEF 'Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme' 100.00 130 99.23 100.00 3.60e-70 PDB 2MEG 'Changes In Conformational Stability Of A Series Of Mutant Human Lysozymes At Constant Positions' 100.00 130 99.23 99.23 8.58e-70 PDB 2MEH 'Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme' 100.00 130 99.23 99.23 5.75e-70 PDB 2MEI 'Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme' 100.00 130 99.23 99.23 9.09e-70 PDB 2NWD 'Structure Of Chemically Synthesized Human Lysozyme At 1 Angstrom Resolution' 99.23 130 100.00 100.00 6.19e-70 PDB 3LHM 'Crystal Structures Of The Apo-And Holomutant Human Lysozymes With An Introduced Ca2+ Binding Site' 100.00 130 98.46 98.46 4.74e-69 DBJ BAA00314 'lysozyme [synthetic construct]' 100.00 131 99.23 99.23 9.97e-70 DBJ BAG34722 'unnamed protein product [Homo sapiens]' 100.00 148 100.00 100.00 3.48e-71 EMBL CAA32175 'lysozyme [Homo sapiens]' 100.00 130 100.00 100.00 1.85e-70 EMBL CAA53144 'lysozyme [synthetic construct]' 100.00 131 100.00 100.00 1.73e-70 GenBank AAA36188 'lysozyme precursor (EC 3.2.1.17)' 100.00 148 99.23 100.00 7.50e-71 GenBank AAA59535 'lysozyme precursor (EC 3.2.1.17)' 100.00 148 100.00 100.00 3.48e-71 GenBank AAA59536 'lysozyme precursor (EC 3.2.1.17)' 100.00 148 100.00 100.00 3.48e-71 GenBank AAA72819 lysozyme 100.00 130 100.00 100.00 1.85e-70 GenBank AAB26052 'lysozyme=amyloid fibril protein [human, Peptide Mutant, 130 aa]' 100.00 130 99.23 99.23 5.75e-70 REF NP_000230 'lysozyme precursor [Homo sapiens]' 100.00 148 100.00 100.00 3.48e-71 REF NP_001009073 'lysozyme [Pan troglodytes]' 100.00 148 100.00 100.00 3.48e-71 SWISS-PROT P61626 'Lysozyme C precursor (1,4-beta-N-acetylmuramidase C)' 100.00 148 100.00 100.00 3.48e-71 SWISS-PROT P61627 'Lysozyme C precursor (1,4-beta-N-acetylmuramidase C)' 100.00 148 100.00 100.00 3.48e-71 SWISS-PROT P61628 'Lysozyme C precursor (1,4-beta-N-acetylmuramidase C)' 100.00 148 100.00 100.00 3.48e-71 SWISS-PROT P79179 'Lysozyme C precursor (1,4-beta-N-acetylmuramidase C)' 100.00 148 100.00 100.00 4.05e-71 SWISS-PROT P79239 'Lysozyme C precursor (1,4-beta-N-acetylmuramidase C)' 100.00 148 99.23 99.23 9.88e-71 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $human_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 $human_lysozyme 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $human_lysozyme 2 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_15N-edited_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited NOESY' _Sample_label . save_ save_15N-edited_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited TOCSY' _Sample_label . save_ save_CBCA(CO)NNH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NNH _Sample_label . save_ save_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_13C-edited_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-edited NOESY' _Sample_label . save_ save_1H-13C-1H_HCCH-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C-1H HCCH-TOCSY' _Sample_label . save_ save_1H-15N_HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 3.8 0.1 n/a temperature 308 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 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_HL35_shift_set _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '15N-edited NOESY' '15N-edited TOCSY' CBCA(CO)NNH HNCACB '13C-edited NOESY' '1H-13C-1H HCCH-TOCSY' '1H-15N HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'human 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 LYS CA C 55.899 . . 2 . 1 LYS HA H 3.935 . . 3 . 1 LYS CB C 34.015 . . 4 . 1 LYS HB2 H 1.683 . . 5 . 1 LYS HG3 H 1.153 . . 6 . 1 LYS HD2 H 0.897 . . 7 . 1 LYS HD3 H 0.637 . . 8 . 1 LYS HE2 H 3.935 . . 9 . 2 VAL N N 127.203 . . 10 . 2 VAL H H 8.859 . . 11 . 2 VAL CA C 61.911 . . 12 . 2 VAL HA H 4.86 . . 13 . 2 VAL CB C 31.883 . . 14 . 2 VAL HB H 1.985 . . 15 . 2 VAL HG1 H 1.017 . . 16 . 2 VAL HG2 H 0.912 . . 17 . 3 PHE N N 127.487 . . 18 . 3 PHE H H 8.865 . . 19 . 3 PHE CA C 59.517 . . 20 . 3 PHE HA H 4.11 . . 21 . 3 PHE CB C 41.633 . . 22 . 3 PHE HB2 H 2.987 . . 23 . 3 PHE HB3 H 2.75 . . 24 . 4 GLU N N 120.766 . . 25 . 4 GLU H H 8.38 . . 26 . 4 GLU CA C 56.406 . . 27 . 4 GLU HA H 4.364 . . 28 . 4 GLU CB C 30.13 . . 29 . 4 GLU HB2 H 2.369 . . 30 . 4 GLU HB3 H 2.231 . . 31 . 4 GLU HG2 H 2.611 . . 32 . 4 GLU HG3 H 2.48 . . 33 . 5 ARG N N 125.877 . . 34 . 5 ARG H H 8.565 . . 35 . 5 ARG CA C 61.224 . . 36 . 5 ARG HA H 3.213 . . 37 . 5 ARG CB C 32.183 . . 38 . 5 ARG HB2 H 1.898 . . 39 . 5 ARG HG2 H 1.571 . . 40 . 5 ARG HG3 H 1.312 . . 41 . 5 ARG HD2 H 3.581 . . 42 . 5 ARG HD3 H 3.348 . . 43 . 6 CYS N N 114.737 . . 44 . 6 CYS H H 8.901 . . 45 . 6 CYS CA C 54.731 . . 46 . 6 CYS HA H 4.75 . . 47 . 6 CYS CB C 33.085 . . 48 . 6 CYS HB2 H 3.17 . . 49 . 6 CYS HB3 H 2.986 . . 50 . 7 GLU N N 125.732 . . 51 . 7 GLU H H 7.834 . . 52 . 7 GLU CA C 59.242 . . 53 . 7 GLU HA H 4.137 . . 54 . 7 GLU CB C 30.005 . . 55 . 7 GLU HB2 H 2.588 . . 56 . 7 GLU HG2 H 2.341 . . 57 . 8 LEU N N 122.074 . . 58 . 8 LEU H H 8.501 . . 59 . 8 LEU CA C 57.89 . . 60 . 8 LEU HA H 3.675 . . 61 . 8 LEU CB C 39.852 . . 62 . 8 LEU HB2 H 1.589 . . 63 . 8 LEU HB3 H 1.204 . . 64 . 8 LEU HG H 0.796 . . 65 . 8 LEU HD1 H 0.369 . . 66 . 8 LEU HD2 H -0.275 . . 67 . 9 ALA N N 123.004 . . 68 . 9 ALA H H 8.367 . . 69 . 9 ALA CA C 56.648 . . 70 . 9 ALA HA H 4.014 . . 71 . 9 ALA CB C 18.157 . . 72 . 9 ALA HB H 1.506 . . 73 . 10 ARG N N 115.113 . . 74 . 10 ARG H H 8.302 . . 75 . 10 ARG CA C 60.347 . . 76 . 10 ARG HA H 3.873 . . 77 . 10 ARG CB C 31.175 . . 78 . 10 ARG HB2 H 1.94 . . 79 . 10 ARG HB3 H 1.881 . . 80 . 10 ARG HG3 H 1.605 . . 81 . 10 ARG HD2 H 3.337 . . 82 . 10 ARG HD3 H 3.086 . . 83 . 11 THR N N 118.762 . . 84 . 11 THR H H 7.83 . . 85 . 11 THR CA C 67.392 . . 86 . 11 THR HA H 3.953 . . 87 . 11 THR CB C 68.566 . . 88 . 11 THR HB H 4.235 . . 89 . 11 THR HG2 H 1.187 . . 90 . 12 LEU N N 119.162 . . 91 . 12 LEU H H 8.804 . . 92 . 12 LEU CA C 58.163 . . 93 . 12 LEU HA H 3.639 . . 94 . 12 LEU CB C 41.45 . . 95 . 12 LEU HB2 H 1.904 . . 96 . 12 LEU HG H 1.654 . . 97 . 12 LEU HD1 H 0.742 . . 98 . 12 LEU HD2 H 0.504 . . 99 . 13 LYS N N 119.475 . . 100 . 13 LYS H H 8.172 . . 101 . 13 LYS CA C 59.09 . . 102 . 13 LYS HA H 4.049 . . 103 . 13 LYS CB C 33.028 . . 104 . 13 LYS HB2 H 2.184 . . 105 . 13 LYS HG3 H 1.921 . . 106 . 13 LYS HD2 H 1.718 . . 107 . 13 LYS HD3 H 1.554 . . 108 . 13 LYS HE2 H 3.166 . . 109 . 14 ARG N N 121.748 . . 110 . 14 ARG H H 7.967 . . 111 . 14 ARG CA C 59.394 . . 112 . 14 ARG HA H 4.178 . . 113 . 14 ARG CB C 30.152 . . 114 . 14 ARG HB2 H 2.055 . . 115 . 14 ARG HG3 H 1.808 . . 116 . 14 ARG HD2 H 3.283 . . 117 . 15 LEU N N 117.087 . . 118 . 15 LEU H H 7.508 . . 119 . 15 LEU CA C 54.784 . . 120 . 15 LEU HA H 4.405 . . 121 . 15 LEU CB C 42.084 . . 122 . 15 LEU HB2 H 1.917 . . 123 . 15 LEU HB3 H 1.797 . . 124 . 15 LEU HG H 1.497 . . 125 . 15 LEU HD1 H 0.843 . . 126 . 15 LEU HD2 H 0.726 . . 127 . 16 GLY N N 106.523 . . 128 . 16 GLY H H 7.555 . . 129 . 16 GLY CA C 47.589 . . 130 . 16 GLY HA2 H 4.088 . . 131 . 16 GLY HA3 H 3.894 . . 132 . 17 MET N N 114.251 . . 133 . 17 MET H H 7.427 . . 134 . 17 MET CA C 57.005 . . 135 . 17 MET HA H 4.019 . . 136 . 17 MET CB C 34.4 . . 137 . 17 MET HB2 H 1.346 . . 138 . 17 MET HB3 H 1.285 . . 139 . 17 MET HG2 H 1.499 . . 140 . 18 ASP N N 118.685 . . 141 . 18 ASP H H 8.98 . . 142 . 18 ASP CA C 56.005 . . 143 . 18 ASP HA H 4.46 . . 144 . 18 ASP CB C 41.609 . . 145 . 18 ASP HB2 H 3.283 . . 146 . 18 ASP HB3 H 2.354 . . 147 . 19 GLY N N 119.43 . . 148 . 19 GLY H H 9.036 . . 149 . 19 GLY CA C 45.923 . . 150 . 19 GLY HA2 H 4.229 . . 151 . 19 GLY HA3 H 3.306 . . 152 . 20 TYR N N 126.315 . . 153 . 20 TYR H H 7.899 . . 154 . 20 TYR CA C 60.925 . . 155 . 20 TYR HA H 4.153 . . 156 . 20 TYR CB C 38.852 . . 157 . 20 TYR HB2 H 3.351 . . 158 . 20 TYR HB3 H 3.115 . . 159 . 21 ARG N N 126.013 . . 160 . 21 ARG H H 8.908 . . 161 . 21 ARG CA C 56.709 . . 162 . 21 ARG HA H 3.566 . . 163 . 21 ARG CB C 27.378 . . 164 . 21 ARG HB2 H 2.048 . . 165 . 21 ARG HG2 H 1.108 . . 166 . 21 ARG HG3 H 1.624 . . 167 . 21 ARG HD2 H 3.092 . . 168 . 21 ARG HD3 H 2.965 . . 169 . 22 GLY N N 103.392 . . 170 . 22 GLY H H 7.838 . . 171 . 22 GLY CA C 45.651 . . 172 . 22 GLY HA2 H 4.037 . . 173 . 22 GLY HA3 H 3.584 . . 174 . 23 ILE N N 124.579 . . 175 . 23 ILE H H 7.759 . . 176 . 23 ILE CA C 61.132 . . 177 . 23 ILE HA H 3.859 . . 178 . 23 ILE CB C 38.168 . . 179 . 23 ILE HB H 2.021 . . 180 . 23 ILE HG12 H 1.298 . . 181 . 23 ILE HG13 H 1.298 . . 182 . 23 ILE HG2 H 0.595 . . 183 . 23 ILE HD1 H -0.277 . . 184 . 24 SER N N 123.121 . . 185 . 24 SER H H 8.775 . . 186 . 24 SER CA C 57.864 . . 187 . 24 SER HA H 4.46 . . 188 . 24 SER CB C 65.594 . . 189 . 24 SER HB2 H 4.41 . . 190 . 24 SER HB3 H 4.172 . . 191 . 25 LEU N N 121.883 . . 192 . 25 LEU H H 8.838 . . 193 . 25 LEU CA C 58.773 . . 194 . 25 LEU HA H 4.211 . . 195 . 25 LEU CB C 42.782 . . 196 . 25 LEU HB2 H 1.974 . . 197 . 25 LEU HG H 1.399 . . 198 . 25 LEU HD1 H 0.976 . . 199 . 25 LEU HD2 H 0.976 . . 200 . 26 ALA N N 118.808 . . 201 . 26 ALA H H 8.836 . . 202 . 26 ALA CA C 56.319 . . 203 . 26 ALA HA H 3.925 . . 204 . 26 ALA CB C 18.564 . . 205 . 26 ALA HB H 1.558 . . 206 . 27 ASN N N 117.054 . . 207 . 27 ASN H H 7.752 . . 208 . 27 ASN CA C 58.488 . . 209 . 27 ASN HA H 4.581 . . 210 . 27 ASN CB C 40.845 . . 211 . 27 ASN HB2 H 3.038 . . 212 . 27 ASN HB3 H 2.105 . . 213 . 27 ASN HD21 H 7.575 . . 214 . 27 ASN HD22 H 6.884 . . 215 . 28 TRP N N 120.179 . . 216 . 28 TRP H H 7.819 . . 217 . 28 TRP CA C 60.734 . . 218 . 28 TRP HA H 4.378 . . 219 . 28 TRP CB C 30.816 . . 220 . 28 TRP HB2 H 3.323 . . 221 . 28 TRP HB3 H 3.054 . . 222 . 29 MET N N 116.706 . . 223 . 29 MET H H 8.384 . . 224 . 29 MET CA C 55.879 . . 225 . 29 MET HA H 4.435 . . 226 . 29 MET CB C 31.059 . . 227 . 29 MET HB2 H 2.281 . . 228 . 29 MET HB3 H 2.072 . . 229 . 29 MET HG2 H 2.397 . . 230 . 29 MET HG3 H 2.283 . . 231 . 30 CYS N N 119.92 . . 232 . 30 CYS H H 8.024 . . 233 . 30 CYS CA C 60.704 . . 234 . 30 CYS HA H 2.96 . . 235 . 30 CYS CB C 44.861 . . 236 . 30 CYS HB2 H 3.147 . . 237 . 31 LEU N N 118.658 . . 238 . 31 LEU H H 8.102 . . 239 . 31 LEU CA C 59.34 . . 240 . 31 LEU HA H 3.988 . . 241 . 31 LEU CB C 42.591 . . 242 . 31 LEU HB2 H 2.366 . . 243 . 31 LEU HB3 H 1.523 . . 244 . 31 LEU HG H 1.091 . . 245 . 31 LEU HD1 H 0.473 . . 246 . 31 LEU HD2 H -0.09 . . 247 . 32 ALA N N 119.313 . . 248 . 32 ALA H H 8.385 . . 249 . 32 ALA CA C 55.408 . . 250 . 32 ALA HA H 4.084 . . 251 . 32 ALA CB C 18.83 . . 252 . 32 ALA HB H 1.386 . . 253 . 33 LYS N N 119.869 . . 254 . 33 LYS H H 8.673 . . 255 . 33 LYS CA C 60.639 . . 256 . 33 LYS HA H 4.228 . . 257 . 33 LYS CB C 30.973 . . 258 . 33 LYS HB2 H 2.07 . . 259 . 33 LYS HG3 H 1.47 . . 260 . 33 LYS HD2 H 0.652 . . 261 . 33 LYS HD3 H 0.52 . . 262 . 33 LYS HE2 H 2.661 . . 263 . 34 TRP N N 118.114 . . 264 . 34 TRP H H 7.714 . . 265 . 34 TRP CA C 59.594 . . 266 . 34 TRP HA H 4.347 . . 267 . 34 TRP CB C 29.866 . . 268 . 34 TRP HB2 H 3.332 . . 269 . 34 TRP HB3 H 2.792 . . 270 . 35 GLU N N 116.361 . . 271 . 35 GLU H H 8.721 . . 272 . 35 GLU CA C 58.032 . . 273 . 35 GLU HA H 4.5 . . 274 . 35 GLU CB C 27.975 . . 275 . 35 GLU HB2 H 2.036 . . 276 . 35 GLU HB3 H 2.069 . . 277 . 35 GLU HG2 H 1.694 . . 278 . 35 GLU HG3 H 1.867 . . 279 . 36 SER N N 108.082 . . 280 . 36 SER H H 7.88 . . 281 . 36 SER CA C 58.355 . . 282 . 36 SER HA H 4.67 . . 283 . 36 SER CB C 68.273 . . 284 . 36 SER HB2 H 4.457 . . 285 . 36 SER HB3 H 3.577 . . 286 . 37 GLY N N 116.085 . . 287 . 37 GLY H H 8.112 . . 288 . 37 GLY CA C 47.79 . . 289 . 37 GLY HA2 H 3.758 . . 290 . 37 GLY HA3 H 3.466 . . 291 . 38 TYR N N 108.777 . . 292 . 38 TYR H H 7.391 . . 293 . 38 TYR CA C 56.881 . . 294 . 38 TYR HA H 3.701 . . 295 . 38 TYR CB C 36.949 . . 296 . 38 TYR HB2 H 3.213 . . 297 . 39 ASN N N 117.484 . . 298 . 39 ASN H H 7.135 . . 299 . 39 ASN CA C 51.849 . . 300 . 39 ASN HA H 5.518 . . 301 . 39 ASN CB C 40.674 . . 302 . 39 ASN HB2 H 3.484 . . 303 . 39 ASN HB3 H 2.723 . . 304 . 39 ASN HD21 H 7.745 . . 305 . 39 ASN HD22 H 7.03 . . 306 . 40 THR N N 115.424 . . 307 . 40 THR H H 9.185 . . 308 . 40 THR CA C 64.743 . . 309 . 40 THR HA H 4.048 . . 310 . 40 THR CB C 69.784 . . 311 . 40 THR HB H 4.457 . . 312 . 40 THR HG2 H 1.547 . . 313 . 41 ARG N N 114.739 . . 314 . 41 ARG H H 7.652 . . 315 . 41 ARG CA C 55.258 . . 316 . 41 ARG HA H 4.497 . . 317 . 41 ARG CB C 30.145 . . 318 . 41 ARG HB2 H 2.114 . . 319 . 41 ARG HG2 H 1.744 . . 320 . 41 ARG HG3 H 1.586 . . 321 . 41 ARG HD2 H 3.259 . . 322 . 42 ALA N N 122.801 . . 323 . 42 ALA H H 6.788 . . 324 . 42 ALA CA C 53.804 . . 325 . 42 ALA HA H 4.048 . . 326 . 42 ALA CB C 19.428 . . 327 . 42 ALA HB H 1.342 . . 328 . 43 THR N N 114.051 . . 329 . 43 THR H H 8.225 . . 330 . 43 THR CA C 60.553 . . 331 . 43 THR HA H 5.274 . . 332 . 43 THR CB C 73.115 . . 333 . 43 THR HB H 3.788 . . 334 . 43 THR HG2 H 1.125 . . 335 . 44 ASN N N 119.321 . . 336 . 44 ASN H H 8.115 . . 337 . 44 ASN CA C 53.688 . . 338 . 44 ASN HA H 5.06 . . 339 . 44 ASN CB C 43.54 . . 340 . 44 ASN HB2 H 2.797 . . 341 . 45 TYR N N 127.64 . . 342 . 45 TYR H H 8.944 . . 343 . 45 TYR CA C 57.909 . . 344 . 45 TYR HA H 4.857 . . 345 . 45 TYR CB C 40.029 . . 346 . 45 TYR HB2 H 3.048 . . 347 . 45 TYR HB3 H 2.845 . . 348 . 46 ASN N N 127.927 . . 349 . 46 ASN H H 8.875 . . 350 . 46 ASN CA C 51.903 . . 351 . 46 ASN HA H 4.697 . . 352 . 46 ASN CB C 39.287 . . 353 . 46 ASN HB2 H 2.756 . . 354 . 46 ASN HD21 H 7.998 . . 355 . 46 ASN HD22 H 6.926 . . 356 . 47 ALA N N 125.556 . . 357 . 47 ALA H H 8.421 . . 358 . 47 ALA CA C 54.773 . . 359 . 47 ALA HA H 3.696 . . 360 . 47 ALA CB C 18.771 . . 361 . 47 ALA HB H 1.465 . . 362 . 48 GLY N N 104.336 . . 363 . 48 GLY H H 8.521 . . 364 . 48 GLY CA C 47.422 . . 365 . 48 GLY HA2 H 3.872 . . 366 . 48 GLY HA3 H 3.828 . . 367 . 49 ASP N N 116.994 . . 368 . 49 ASP H H 7.156 . . 369 . 49 ASP CA C 52.774 . . 370 . 49 ASP HA H 4.736 . . 371 . 49 ASP CB C 40.958 . . 372 . 49 ASP HB2 H 2.91 . . 373 . 49 ASP HB3 H 2.449 . . 374 . 50 ARG N N 114.264 . . 375 . 50 ARG H H 7.88 . . 376 . 50 ARG CA C 57.79 . . 377 . 50 ARG HA H 3.832 . . 378 . 50 ARG CB C 27.468 . . 379 . 50 ARG HB2 H 2.247 . . 380 . 50 ARG HB3 H 2.1 . . 381 . 50 ARG HG2 H 1.726 . . 382 . 50 ARG HG3 H 1.639 . . 383 . 50 ARG HD2 H 3.262 . . 384 . 51 SER N N 114.057 . . 385 . 51 SER H H 7.999 . . 386 . 51 SER CA C 57.396 . . 387 . 51 SER HA H 4.742 . . 388 . 51 SER CB C 66.767 . . 389 . 51 SER HB2 H 4.16 . . 390 . 51 SER HB3 H 3.598 . . 391 . 52 THR N N 116.36 . . 392 . 52 THR H H 9.053 . . 393 . 52 THR CA C 62.072 . . 394 . 52 THR HA H 5.061 . . 395 . 52 THR CB C 71.735 . . 396 . 52 THR HB H 3.844 . . 397 . 52 THR HG2 H 0.414 . . 398 . 53 ASP N N 124.539 . . 399 . 53 ASP H H 8.888 . . 400 . 53 ASP CA C 52.399 . . 401 . 53 ASP HA H 5.259 . . 402 . 53 ASP CB C 42.306 . . 403 . 53 ASP HB2 H 2.773 . . 404 . 53 ASP HB3 H 2.061 . . 405 . 54 TYR N N 118.503 . . 406 . 54 TYR H H 9.134 . . 407 . 54 TYR CA C 59.969 . . 408 . 54 TYR HA H 4.837 . . 409 . 54 TYR CB C 43.436 . . 410 . 54 TYR HB2 H 3 . . 411 . 54 TYR HB3 H 2.726 . . 412 . 55 GLY N N 112.562 . . 413 . 55 GLY H H 9.069 . . 414 . 55 GLY CA C 46.895 . . 415 . 55 GLY HA2 H 4.527 . . 416 . 55 GLY HA3 H 4.479 . . 417 . 56 ILE N N 121.805 . . 418 . 56 ILE H H 9.215 . . 419 . 56 ILE CA C 62.615 . . 420 . 56 ILE HA H 4.132 . . 421 . 56 ILE CB C 39.594 . . 422 . 56 ILE HB H 1.746 . . 423 . 56 ILE HG12 H 0.571 . . 424 . 56 ILE HG13 H 0.391 . . 425 . 56 ILE HG2 H 0.055 . . 426 . 56 ILE HD1 H 1.206 . . 427 . 57 PHE N N 115.646 . . 428 . 57 PHE H H 8.296 . . 429 . 57 PHE CA C 55.96 . . 430 . 57 PHE HA H 4.672 . . 431 . 57 PHE CB C 39.992 . . 432 . 57 PHE HB2 H 3.478 . . 433 . 57 PHE HB3 H 2.71 . . 434 . 58 GLN N N 113.982 . . 435 . 58 GLN H H 7.916 . . 436 . 58 GLN CA C 55.59 . . 437 . 58 GLN HA H 3.488 . . 438 . 58 GLN CB C 27.331 . . 439 . 58 GLN HB2 H 2.579 . . 440 . 58 GLN HB3 H 2.599 . . 441 . 58 GLN HG2 H 1.966 . . 442 . 58 GLN HG3 H 1.991 . . 443 . 58 GLN HE21 H 7.821 . . 444 . 58 GLN HE22 H 7.245 . . 445 . 59 ILE N N 122.23 . . 446 . 59 ILE H H 7.881 . . 447 . 59 ILE CA C 61.882 . . 448 . 59 ILE HA H 4.358 . . 449 . 59 ILE CB C 39.655 . . 450 . 59 ILE HB H 1.938 . . 451 . 59 ILE HG12 H 1.316 . . 452 . 59 ILE HG2 H 1.316 . . 453 . 59 ILE HD1 H 1.096 . . 454 . 60 ASN N N 127.899 . . 455 . 60 ASN H H 8.515 . . 456 . 60 ASN CA C 56.545 . . 457 . 60 ASN HA H 5.73 . . 458 . 60 ASN CB C 44.162 . . 459 . 60 ASN HB2 H 3.442 . . 460 . 60 ASN HB3 H 3.021 . . 461 . 60 ASN HD21 H 7.658 . . 462 . 61 SER N N 119.565 . . 463 . 61 SER H H 9.221 . . 464 . 61 SER CA C 60.992 . . 465 . 61 SER HA H 5.149 . . 466 . 61 SER CB C 65.206 . . 467 . 61 SER HB2 H 4.473 . . 468 . 62 ARG N N 123.956 . . 469 . 62 ARG H H 8.747 . . 470 . 62 ARG CA C 58.941 . . 471 . 62 ARG HA H 4.193 . . 472 . 62 ARG CB C 29.982 . . 473 . 62 ARG HB2 H 1.766 . . 474 . 62 ARG HB3 H 1.459 . . 475 . 62 ARG HG2 H 1.198 . . 476 . 62 ARG HG3 H 0.825 . . 477 . 62 ARG HD2 H 3.096 . . 478 . 62 ARG HD3 H 3.009 . . 479 . 63 TYR N N 114.62 . . 480 . 63 TYR H H 7.315 . . 481 . 63 TYR CA C 59.023 . . 482 . 63 TYR HA H 4.34 . . 483 . 63 TYR CB C 39.996 . . 484 . 63 TYR HB2 H 1.611 . . 485 . 63 TYR HB3 H 1.631 . . 486 . 64 TRP N N 114.706 . . 487 . 64 TRP H H 7.235 . . 488 . 64 TRP CA C 59.325 . . 489 . 64 TRP HA H 5.044 . . 490 . 64 TRP CB C 33.939 . . 491 . 64 TRP HB2 H 3.397 . . 492 . 65 CYS N N 111.294 . . 493 . 65 CYS H H 7.462 . . 494 . 65 CYS CA C 53.221 . . 495 . 65 CYS HA H 5.737 . . 496 . 65 CYS CB C 45.849 . . 497 . 65 CYS HB2 H 2.891 . . 498 . 65 CYS HB3 H 2.517 . . 499 . 66 ASN N N 119.416 . . 500 . 66 ASN H H 8.709 . . 501 . 66 ASN CA C 51.617 . . 502 . 66 ASN HA H 5.634 . . 503 . 66 ASN CB C 40.889 . . 504 . 66 ASN HB2 H 2.899 . . 505 . 66 ASN HB3 H 2.439 . . 506 . 67 ASP N N 131.536 . . 507 . 67 ASP H H 10.354 . . 508 . 67 ASP CA C 51.948 . . 509 . 67 ASP HA H 4.966 . . 510 . 67 ASP CB C 41.528 . . 511 . 67 ASP HB2 H 3.264 . . 512 . 67 ASP HB3 H 2.294 . . 513 . 68 GLY N N 108.663 . . 514 . 68 GLY H H 8.252 . . 515 . 68 GLY CA C 46.749 . . 516 . 68 GLY HA2 H 4.143 . . 517 . 68 GLY HA3 H 3.868 . . 518 . 69 LYS N N 117.928 . . 519 . 69 LYS H H 8.188 . . 520 . 69 LYS CA C 55.638 . . 521 . 69 LYS HA H 4.797 . . 522 . 69 LYS CB C 34.175 . . 523 . 69 LYS HB2 H 1.855 . . 524 . 69 LYS HG3 H 1.652 . . 525 . 69 LYS HD2 H 1.287 . . 526 . 69 LYS HE2 H 2.993 . . 527 . 70 THR N N 121.014 . . 528 . 70 THR H H 8.342 . . 529 . 70 THR CA C 60.636 . . 530 . 70 THR HA H 4.807 . . 531 . 70 THR CB C 70.834 . . 532 . 70 THR HB H 4.158 . . 533 . 70 THR HG2 H 1.092 . . 534 . 71 PRO CA C 63.496 . . 535 . 71 PRO HA H 4.404 . . 536 . 71 PRO CB C 32.232 . . 537 . 71 PRO HB2 H 2.323 . . 538 . 71 PRO HG2 H 2.089 . . 539 . 71 PRO HG3 H 1.959 . . 540 . 71 PRO HD2 H 4.115 . . 541 . 71 PRO HD3 H 3.894 . . 542 . 72 GLY N N 110.275 . . 543 . 72 GLY H H 8.697 . . 544 . 72 GLY CA C 46.424 . . 545 . 72 GLY HA2 H 3.867 . . 546 . 72 GLY HA3 H 3.751 . . 547 . 73 ALA N N 120.953 . . 548 . 73 ALA H H 7.115 . . 549 . 73 ALA CA C 53.08 . . 550 . 73 ALA HA H 4.603 . . 551 . 73 ALA CB C 20.925 . . 552 . 73 ALA HB H 1.562 . . 553 . 74 VAL N N 120.346 . . 554 . 74 VAL H H 7.816 . . 555 . 74 VAL CA C 63.151 . . 556 . 74 VAL HA H 3.907 . . 557 . 74 VAL CB C 34.081 . . 558 . 74 VAL HB H 1.975 . . 559 . 74 VAL HG1 H 0.959 . . 560 . 74 VAL HG2 H 0.751 . . 561 . 75 ASN N N 119.028 . . 562 . 75 ASN H H 8.727 . . 563 . 75 ASN CA C 51.962 . . 564 . 75 ASN HA H 3.808 . . 565 . 75 ASN CB C 37.535 . . 566 . 75 ASN HB2 H 3.116 . . 567 . 75 ASN HB3 H 1.978 . . 568 . 75 ASN HD21 H 7.748 . . 569 . 75 ASN HD22 H 7.146 . . 570 . 76 ALA N N 120.577 . . 571 . 76 ALA H H 8.359 . . 572 . 76 ALA CA C 55.371 . . 573 . 76 ALA HA H 4.062 . . 574 . 76 ALA CB C 19.461 . . 575 . 76 ALA HB H 1.477 . . 576 . 77 CYS N N 111.151 . . 577 . 77 CYS H H 9.38 . . 578 . 77 CYS CA C 56.449 . . 579 . 77 CYS HA H 4.383 . . 580 . 77 CYS CB C 39.917 . . 581 . 77 CYS HB2 H 3.51 . . 582 . 77 CYS HB3 H 3.807 . . 583 . 78 HIS N N 118.023 . . 584 . 78 HIS H H 7.817 . . 585 . 78 HIS CA C 56.204 . . 586 . 78 HIS HA H 3.982 . . 587 . 78 HIS CB C 26.112 . . 588 . 78 HIS HB2 H 3.388 . . 589 . 79 LEU N N 118.528 . . 590 . 79 LEU H H 8.72 . . 591 . 79 LEU CA C 54.196 . . 592 . 79 LEU HA H 4.703 . . 593 . 79 LEU CB C 47.372 . . 594 . 79 LEU HB2 H 1.664 . . 595 . 79 LEU HD1 H 1.25 . . 596 . 79 LEU HD2 H 0.812 . . 597 . 80 SER N N 117.653 . . 598 . 80 SER H H 8.639 . . 599 . 80 SER CA C 57.722 . . 600 . 80 SER HA H 5.005 . . 601 . 80 SER CB C 63.871 . . 602 . 80 SER HB2 H 3.963 . . 603 . 81 CYS N N 125.91 . . 604 . 81 CYS H H 8.5 . . 605 . 81 CYS CA C 57.323 . . 606 . 81 CYS HA H 3.947 . . 607 . 81 CYS CB C 37.891 . . 608 . 81 CYS HB2 H 1.861 . . 609 . 81 CYS HB3 H 1.181 . . 610 . 82 SER N N 114.672 . . 611 . 82 SER H H 8.378 . . 612 . 82 SER CA C 61.683 . . 613 . 82 SER HA H 3.903 . . 614 . 82 SER HB2 H 1.683 . . 615 . 83 ALA N N 125.947 . . 616 . 83 ALA H H 7.81 . . 617 . 83 ALA CA C 54.553 . . 618 . 83 ALA HA H 4.35 . . 619 . 83 ALA CB C 18.496 . . 620 . 83 ALA HB H 1.679 . . 621 . 84 LEU N N 116.688 . . 622 . 84 LEU H H 7.876 . . 623 . 84 LEU CA C 54.5 . . 624 . 84 LEU HA H 4.338 . . 625 . 84 LEU CB C 40.948 . . 626 . 84 LEU HB2 H 2.228 . . 627 . 84 LEU HB3 H 1.753 . . 628 . 84 LEU HG H 1.735 . . 629 . 84 LEU HD1 H 1.041 . . 630 . 84 LEU HD2 H 0.802 . . 631 . 85 LEU N N 117.659 . . 632 . 85 LEU H H 7.164 . . 633 . 85 LEU CA C 53.654 . . 634 . 85 LEU HA H 5.633 . . 635 . 85 LEU CB C 43.228 . . 636 . 85 LEU HB2 H 1.777 . . 637 . 85 LEU HG H 1.119 . . 638 . 85 LEU HD1 H 1.04 . . 639 . 85 LEU HD2 H 1.04 . . 640 . 86 GLN N N 116.628 . . 641 . 86 GLN H H 6.754 . . 642 . 86 GLN CA C 55.093 . . 643 . 86 GLN HA H 4.424 . . 644 . 86 GLN CB C 31.27 . . 645 . 86 GLN HB2 H 2.67 . . 646 . 86 GLN HB3 H 2.495 . . 647 . 86 GLN HG2 H 2.063 . . 648 . 86 GLN HG3 H 2.073 . . 649 . 87 ASP N N 120.244 . . 650 . 87 ASP H H 8.698 . . 651 . 87 ASP CA C 57.394 . . 652 . 87 ASP HA H 4.222 . . 653 . 87 ASP CB C 40.499 . . 654 . 87 ASP HB2 H 2.641 . . 655 . 87 ASP HB3 H 2.506 . . 656 . 88 ASN N N 114.457 . . 657 . 88 ASN H H 7.396 . . 658 . 88 ASN CA C 52.516 . . 659 . 88 ASN HA H 4.895 . . 660 . 88 ASN CB C 38.579 . . 661 . 88 ASN HB2 H 3.018 . . 662 . 88 ASN HB3 H 2.834 . . 663 . 89 ILE N N 118.83 . . 664 . 89 ILE H H 8.248 . . 665 . 89 ILE CA C 61.865 . . 666 . 89 ILE HA H 4.623 . . 667 . 89 ILE CB C 39.009 . . 668 . 89 ILE HB H 2.106 . . 669 . 89 ILE HG12 H 1.303 . . 670 . 89 ILE HG2 H 1.003 . . 671 . 89 ILE HD1 H 0.284 . . 672 . 90 ALA N N 126.104 . . 673 . 90 ALA H H 8.192 . . 674 . 90 ALA CA C 57.269 . . 675 . 90 ALA HA H 3.869 . . 676 . 90 ALA CB C 18.091 . . 677 . 90 ALA HB H 1.463 . . 678 . 91 ASP N N 118.493 . . 679 . 91 ASP H H 9.038 . . 680 . 91 ASP CA C 57.019 . . 681 . 91 ASP HA H 4.515 . . 682 . 91 ASP CB C 38.611 . . 683 . 91 ASP HB2 H 2.692 . . 684 . 91 ASP HB3 H 2.482 . . 685 . 92 ALA N N 123.204 . . 686 . 92 ALA H H 7.679 . . 687 . 92 ALA CA C 55.91 . . 688 . 92 ALA HA H 3.986 . . 689 . 92 ALA CB C 17.996 . . 690 . 92 ALA HB H 1.582 . . 691 . 93 VAL N N 118.291 . . 692 . 93 VAL H H 8.623 . . 693 . 93 VAL CA C 67.225 . . 694 . 93 VAL HA H 3.269 . . 695 . 93 VAL CB C 31.357 . . 696 . 93 VAL HB H 2.179 . . 697 . 93 VAL HG1 H 0.853 . . 698 . 93 VAL HG2 H 0.853 . . 699 . 94 ALA N N 121.62 . . 700 . 94 ALA H H 8.03 . . 701 . 94 ALA CA C 55.839 . . 702 . 94 ALA HA H 3.883 . . 703 . 94 ALA CB C 18.139 . . 704 . 94 ALA HB H 1.552 . . 705 . 95 CYS N N 115.939 . . 706 . 95 CYS H H 8.307 . . 707 . 95 CYS CA C 55.344 . . 708 . 95 CYS HA H 4.962 . . 709 . 95 CYS CB C 35.337 . . 710 . 95 CYS HB2 H 3.345 . . 711 . 95 CYS HB3 H 2.684 . . 712 . 96 ALA N N 124.455 . . 713 . 96 ALA H H 8.826 . . 714 . 96 ALA CA C 56.369 . . 715 . 96 ALA HA H 3.794 . . 716 . 96 ALA CB C 17.731 . . 717 . 96 ALA HB H 0.872 . . 718 . 97 LYS N N 114.307 . . 719 . 97 LYS H H 7.968 . . 720 . 97 LYS CA C 60.219 . . 721 . 97 LYS HA H 3.646 . . 722 . 97 LYS CB C 33.231 . . 723 . 97 LYS HB2 H 1.647 . . 724 . 97 LYS HG2 H 1.309 . . 725 . 97 LYS HG3 H 1.123 . . 726 . 97 LYS HD2 H 2.221 . . 727 . 97 LYS HD3 H 1.964 . . 728 . 97 LYS HE2 H -0.42 . . 729 . 97 LYS HE3 H 0.008 . . 730 . 98 ARG N N 118.441 . . 731 . 98 ARG H H 7.142 . . 732 . 98 ARG CA C 58.468 . . 733 . 98 ARG HA H 4.089 . . 734 . 98 ARG CB C 28.768 . . 735 . 98 ARG HB2 H 1.812 . . 736 . 98 ARG HB3 H 1.683 . . 737 . 98 ARG HG3 H 2.014 . . 738 . 98 ARG HD2 H 2.62 . . 739 . 98 ARG HD3 H 2.477 . . 740 . 99 VAL N N 123.427 . . 741 . 99 VAL H H 8.303 . . 742 . 99 VAL CA C 66.072 . . 743 . 99 VAL HA H 2.483 . . 744 . 99 VAL CB C 30.96 . . 745 . 99 VAL HB H 1.886 . . 746 . 99 VAL HG1 H -0.343 . . 747 . 99 VAL HG2 H -0.576 . . 748 . 100 VAL N N 108.312 . . 749 . 100 VAL H H 7.462 . . 750 . 100 VAL CA C 63.527 . . 751 . 100 VAL HA H 3.915 . . 752 . 100 VAL CB C 31.444 . . 753 . 100 VAL HB H 2.45 . . 754 . 100 VAL HG1 H 1.39 . . 755 . 100 VAL HG2 H 1.111 . . 756 . 101 ARG N N 119.387 . . 757 . 101 ARG H H 7.55 . . 758 . 101 ARG CA C 58.566 . . 759 . 101 ARG HA H 4.176 . . 760 . 101 ARG CB C 31.165 . . 761 . 101 ARG HB2 H 2.474 . . 762 . 101 ARG HB3 H 2.087 . . 763 . 101 ARG HG2 H 2.138 . . 764 . 101 ARG HG3 H 1.481 . . 765 . 101 ARG HD2 H 3.46 . . 766 . 101 ARG HD3 H 3.332 . . 767 . 102 ASP N N 121.469 . . 768 . 102 ASP H H 7.4 . . 769 . 102 ASP CA C 54.023 . . 770 . 102 ASP HA H 4.926 . . 771 . 102 ASP CB C 39.787 . . 772 . 102 ASP HB2 H 3.026 . . 773 . 103 PRO CA C 66.494 . . 774 . 103 PRO HA H 4.228 . . 775 . 103 PRO CB C 32.443 . . 776 . 103 PRO HB2 H 2.408 . . 777 . 103 PRO HG2 H 2.123 . . 778 . 103 PRO HG3 H 1.894 . . 779 . 103 PRO HD2 H 3.837 . . 780 . 104 GLN N N 113.753 . . 781 . 104 GLN H H 8.468 . . 782 . 104 GLN CA C 57.718 . . 783 . 104 GLN HA H 4.13 . . 784 . 104 GLN CB C 29.178 . . 785 . 104 GLN HB2 H 2.319 . . 786 . 104 GLN HG3 H 2.564 . . 787 . 105 GLY N N 108.837 . . 788 . 105 GLY H H 8.086 . . 789 . 105 GLY CA C 46.378 . . 790 . 105 GLY HA2 H 4.011 . . 791 . 105 GLY HA3 H 4.001 . . 792 . 106 ILE N N 126.629 . . 793 . 106 ILE H H 8.483 . . 794 . 106 ILE CA C 62.856 . . 795 . 106 ILE HA H 3.994 . . 796 . 106 ILE CB C 39.17 . . 797 . 106 ILE HB H 0.916 . . 798 . 106 ILE HG12 H 0.195 . . 799 . 106 ILE HG2 H -0.451 . . 800 . 106 ILE HD1 H -0.629 . . 801 . 107 ARG N N 116.868 . . 802 . 107 ARG H H 7.315 . . 803 . 107 ARG CA C 58.042 . . 804 . 107 ARG HA H 4.113 . . 805 . 107 ARG CB C 29.497 . . 806 . 107 ARG HB2 H 2.112 . . 807 . 107 ARG HB3 H 2.067 . . 808 . 107 ARG HG3 H 1.818 . . 809 . 107 ARG HD2 H 3.383 . . 810 . 108 ALA N N 120.306 . . 811 . 108 ALA H H 7.231 . . 812 . 108 ALA CA C 54.444 . . 813 . 108 ALA HA H 3.846 . . 814 . 108 ALA CB C 19.106 . . 815 . 108 ALA HB H 0.914 . . 816 . 109 TRP N N 116.299 . . 817 . 109 TRP H H 7.492 . . 818 . 109 TRP CA C 59.694 . . 819 . 109 TRP HA H 4.842 . . 820 . 109 TRP CB C 30.121 . . 821 . 109 TRP HB2 H 3.254 . . 822 . 110 VAL N N 128.39 . . 823 . 110 VAL H H 8.823 . . 824 . 110 VAL CA C 66.665 . . 825 . 110 VAL HA H 3.657 . . 826 . 110 VAL CB C 31.966 . . 827 . 110 VAL HB H 2.193 . . 828 . 110 VAL HG1 H 1.161 . . 829 . 110 VAL HG2 H 1.059 . . 830 . 111 ALA N N 119.562 . . 831 . 111 ALA H H 8.648 . . 832 . 111 ALA CA C 55.54 . . 833 . 111 ALA HA H 4.229 . . 834 . 111 ALA CB C 18.463 . . 835 . 111 ALA HB H 1.436 . . 836 . 112 TRP N N 114.721 . . 837 . 112 TRP H H 7.379 . . 838 . 112 TRP CA C 62.98 . . 839 . 112 TRP HA H 3.792 . . 840 . 112 TRP CB C 29.029 . . 841 . 112 TRP HB2 H 3.109 . . 842 . 112 TRP HB3 H 2.836 . . 843 . 113 ARG N N 119.275 . . 844 . 113 ARG H H 7.747 . . 845 . 113 ARG CA C 59.952 . . 846 . 113 ARG HA H 3.776 . . 847 . 113 ARG CB C 30.63 . . 848 . 113 ARG HB2 H 2.206 . . 849 . 113 ARG HG2 H 1.945 . . 850 . 113 ARG HG3 H 1.743 . . 851 . 113 ARG HD2 H 3.578 . . 852 . 113 ARG HD3 H 3.334 . . 853 . 114 ASN N N 113.165 . . 854 . 114 ASN H H 7.859 . . 855 . 114 ASN CA C 54.858 . . 856 . 114 ASN HA H 4.482 . . 857 . 114 ASN CB C 39.477 . . 858 . 114 ASN HB2 H 2.627 . . 859 . 114 ASN HB3 H 2.798 . . 860 . 115 ARG N N 114.016 . . 861 . 115 ARG H H 7.787 . . 862 . 115 ARG CA C 54.919 . . 863 . 115 ARG HA H 4.009 . . 864 . 115 ARG CB C 31.767 . . 865 . 115 ARG HB2 H 1.325 . . 866 . 115 ARG HB3 H 1.043 . . 867 . 115 ARG HG2 H 0.619 . . 868 . 115 ARG HG3 H 0.258 . . 869 . 115 ARG HD2 H 2.205 . . 870 . 116 CYS N N 114.709 . . 871 . 116 CYS H H 7.313 . . 872 . 116 CYS CA C 55.082 . . 873 . 116 CYS HA H 4.368 . . 874 . 116 CYS CB C 44.394 . . 875 . 116 CYS HB2 H 2.518 . . 876 . 116 CYS HB3 H 1.692 . . 877 . 117 GLN N N 121.003 . . 878 . 117 GLN H H 6.652 . . 879 . 117 GLN CA C 57.576 . . 880 . 117 GLN HA H 3.159 . . 881 . 117 GLN CB C 28.754 . . 882 . 117 GLN HB2 H 1.655 . . 883 . 117 GLN HG3 H 0.698 . . 884 . 118 ASN N N 119.82 . . 885 . 118 ASN H H 9.082 . . 886 . 118 ASN CA C 54.885 . . 887 . 118 ASN HA H 4.423 . . 888 . 118 ASN CB C 37.657 . . 889 . 118 ASN HB2 H 3.052 . . 890 . 118 ASN HB3 H 2.9 . . 891 . 119 ARG N N 116.716 . . 892 . 119 ARG H H 7.444 . . 893 . 119 ARG CA C 54.01 . . 894 . 119 ARG HA H 4.585 . . 895 . 119 ARG CB C 32.581 . . 896 . 119 ARG HB2 H 2.936 . . 897 . 119 ARG HB3 H 2.766 . . 898 . 119 ARG HG2 H 1.769 . . 899 . 119 ARG HG3 H 1.78 . . 900 . 119 ARG HD2 H 4.288 . . 901 . 120 ASP N N 119.358 . . 902 . 120 ASP H H 8.445 . . 903 . 120 ASP CA C 54.423 . . 904 . 120 ASP HA H 4.736 . . 905 . 120 ASP CB C 40.171 . . 906 . 120 ASP HB2 H 2.918 . . 907 . 120 ASP HB3 H 2.725 . . 908 . 121 VAL N N 119.071 . . 909 . 121 VAL H H 8.514 . . 910 . 121 VAL CA C 61.644 . . 911 . 121 VAL HA H 4.819 . . 912 . 121 VAL CB C 32.396 . . 913 . 121 VAL HB H 2.702 . . 914 . 121 VAL HG1 H 1.173 . . 915 . 121 VAL HG2 H 0.889 . . 916 . 122 ARG N N 123.27 . . 917 . 122 ARG H H 8.28 . . 918 . 122 ARG CA C 60 . . 919 . 122 ARG HA H 3.96 . . 920 . 122 ARG CB C 29.879 . . 921 . 122 ARG HB2 H 2.011 . . 922 . 122 ARG HB3 H 1.956 . . 923 . 122 ARG HG3 H 1.825 . . 924 . 122 ARG HD2 H 3.257 . . 925 . 122 ARG HD3 H 3.298 . . 926 . 123 GLN N N 116.049 . . 927 . 123 GLN H H 8.715 . . 928 . 123 GLN CA C 58.076 . . 929 . 123 GLN HA H 4.085 . . 930 . 123 GLN CB C 27.985 . . 931 . 123 GLN HB2 H 1.828 . . 932 . 123 GLN HG3 H 1.363 . . 933 . 124 TYR N N 116.751 . . 934 . 124 TYR H H 7.585 . . 935 . 124 TYR CA C 62.537 . . 936 . 124 TYR HA H 4.167 . . 937 . 124 TYR CB C 39.13 . . 938 . 124 TYR HB2 H 3.233 . . 939 . 124 TYR HB3 H 2.982 . . 940 . 125 VAL N N 104.745 . . 941 . 125 VAL H H 7.272 . . 942 . 125 VAL CA C 60.341 . . 943 . 125 VAL HA H 4.531 . . 944 . 125 VAL CB C 33.316 . . 945 . 125 VAL HB H 2.344 . . 946 . 125 VAL HG1 H 0.964 . . 947 . 125 VAL HG2 H 0.826 . . 948 . 126 GLN N N 124.589 . . 949 . 126 GLN H H 7.38 . . 950 . 126 GLN CA C 57.851 . . 951 . 126 GLN HA H 4.205 . . 952 . 126 GLN CB C 28.821 . . 953 . 126 GLN HB2 H 2.103 . . 954 . 126 GLN HB3 H 2.002 . . 955 . 126 GLN HG2 H 2.415 . . 956 . 126 GLN HG3 H 2.401 . . 957 . 127 GLY N N 113.537 . . 958 . 127 GLY H H 9.138 . . 959 . 127 GLY CA C 46.078 . . 960 . 127 GLY HA2 H 4.303 . . 961 . 127 GLY HA3 H 3.875 . . 962 . 128 CYS N N 114.401 . . 963 . 128 CYS H H 7.645 . . 964 . 128 CYS CA C 52.34 . . 965 . 128 CYS HA H 4.946 . . 966 . 128 CYS CB C 35.395 . . 967 . 128 CYS HB2 H 3.215 . . 968 . 128 CYS HB3 H 2.707 . . 969 . 129 GLY N N 111.709 . . 970 . 129 GLY H H 8.874 . . 971 . 129 GLY CA C 47.212 . . 972 . 129 GLY HA2 H 3.975 . . 973 . 129 GLY HA3 H 3.924 . . 974 . 130 VAL N N 116.635 . . 975 . 130 VAL H H 7.454 . . 976 . 130 VAL CA C 61.647 . . 977 . 130 VAL HA H 4.304 . . 978 . 130 VAL CB C 33.79 . . 979 . 130 VAL HB H 2.192 . . 980 . 130 VAL HG1 H 1.474 . . 981 . 130 VAL HG2 H 1.347 . . stop_ save_