data_435 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Complete Resonance Assignment for the Polypeptide Backbone of Interleukin 1beta Using Three-Dimensional Heteronuclear NMR Spectroscopy ; _BMRB_accession_number 435 _BMRB_flat_file_name bmr435.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 Driscoll Paul C. . 2 Clore G. Marius . 3 Marion Dominique . . 4 Wingfield Paul . . 5 Gronenborn Angela M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 665 "15N chemical shifts" 144 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-11 revision BMRB 'Compelte 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 ; Driscoll, Paul C., Clore, G. Marius, Marion, Dominique, Wingfield, Paul, Gronenborn, Angela M., "Complete Resonance Assignment for the Polypeptide Backbone of Interleukin 1beta Using Three-Dimensional Heteronuclear NMR Spectroscopy," Biochemistry 29, 3542-3556 (1990). ; _Citation_title ; Complete Resonance Assignment for the Polypeptide Backbone of Interleukin 1beta Using Three-Dimensional Heteronuclear NMR Spectroscopy ; _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 Driscoll Paul C. . 2 Clore G. Marius . 3 Marion Dominique . . 4 Wingfield Paul . . 5 Gronenborn Angela M. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 29 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3542 _Page_last 3556 _Year 1990 _Details . save_ ################################## # Molecular system description # ################################## save_system_interleukin_1-beta _Saveframe_category molecular_system _Mol_system_name 'interleukin 1-beta' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'interleukin 1-beta' $interleukin_1-beta stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_interleukin_1-beta _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'interleukin 1-beta' _Name_variant des-ala-1-IL-1beta _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 152 _Mol_residue_sequence ; PVRSLNCTLRDSQQKSLVMS GPYELKALHLQGQDMEQQVV FSMSFVQGEESNDKIPVALG LKEKNLYLSCVLKDDKPTLQ LESVDPKNYPKKKMEKRFVF NKIEINNKLEFESAQFPNWY ISTSQAENMPVFLGGTKGGQ DITDFTMQFVSS ; loop_ _Residue_seq_code _Residue_label 1 PRO 2 VAL 3 ARG 4 SER 5 LEU 6 ASN 7 CYS 8 THR 9 LEU 10 ARG 11 ASP 12 SER 13 GLN 14 GLN 15 LYS 16 SER 17 LEU 18 VAL 19 MET 20 SER 21 GLY 22 PRO 23 TYR 24 GLU 25 LEU 26 LYS 27 ALA 28 LEU 29 HIS 30 LEU 31 GLN 32 GLY 33 GLN 34 ASP 35 MET 36 GLU 37 GLN 38 GLN 39 VAL 40 VAL 41 PHE 42 SER 43 MET 44 SER 45 PHE 46 VAL 47 GLN 48 GLY 49 GLU 50 GLU 51 SER 52 ASN 53 ASP 54 LYS 55 ILE 56 PRO 57 VAL 58 ALA 59 LEU 60 GLY 61 LEU 62 LYS 63 GLU 64 LYS 65 ASN 66 LEU 67 TYR 68 LEU 69 SER 70 CYS 71 VAL 72 LEU 73 LYS 74 ASP 75 ASP 76 LYS 77 PRO 78 THR 79 LEU 80 GLN 81 LEU 82 GLU 83 SER 84 VAL 85 ASP 86 PRO 87 LYS 88 ASN 89 TYR 90 PRO 91 LYS 92 LYS 93 LYS 94 MET 95 GLU 96 LYS 97 ARG 98 PHE 99 VAL 100 PHE 101 ASN 102 LYS 103 ILE 104 GLU 105 ILE 106 ASN 107 ASN 108 LYS 109 LEU 110 GLU 111 PHE 112 GLU 113 SER 114 ALA 115 GLN 116 PHE 117 PRO 118 ASN 119 TRP 120 TYR 121 ILE 122 SER 123 THR 124 SER 125 GLN 126 ALA 127 GLU 128 ASN 129 MET 130 PRO 131 VAL 132 PHE 133 LEU 134 GLY 135 GLY 136 THR 137 LYS 138 GLY 139 GLY 140 GLN 141 ASP 142 ILE 143 THR 144 ASP 145 PHE 146 THR 147 MET 148 GLN 149 PHE 150 VAL 151 SER 152 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-22 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 1061 "interleukin 1-beta" 100.00 153 100.00 100.00 1.29e-106 BMRB 1062 "interleukin 1-beta" 100.00 152 100.00 100.00 1.32e-106 BMRB 2718 "interleukin 1-beta" 100.00 153 100.00 100.00 1.29e-106 BMRB 2719 "interleukin 1-beta" 100.00 153 100.00 100.00 1.29e-106 BMRB 434 "interleukin 1-beta" 100.00 153 100.00 100.00 1.29e-106 PDB 1HIB "The Structure Of An Interleukin-1 Beta Mutant With Reduced Bioactivity Shows Multiple Subtle Changes In Conformation That Affec" 100.00 153 99.34 99.34 1.31e-105 PDB 1I1B "Crystal Structure Of Recombinant Human Interleukin-1beta At 2.0 Angstroms Resolution" 100.00 153 100.00 100.00 1.29e-106 PDB 1IOB "Interleukin-1 Beta From Joint X-ray And Nmr Refinement" 100.00 153 100.00 100.00 1.29e-106 PDB 1ITB "Type-1 Interleukin-1 Receptor Complexed With Interleukin-1 Beta" 100.00 153 100.00 100.00 1.29e-106 PDB 1L2H "Crystal Structure Of Interleukin 1-Beta F42wW120F MUTANT" 100.00 153 98.68 100.00 3.19e-104 PDB 1S0L "Interleukin 1 Beta Mutant F42w" 100.00 153 99.34 100.00 6.73e-106 PDB 1T4Q "Interleukin 1 Beta F101w" 100.00 153 99.34 100.00 6.73e-106 PDB 1TOO "Interleukin 1b Mutant F146w" 100.00 153 99.34 100.00 6.73e-106 PDB 1TP0 "Triple Mutation In Interleukin 1 Beta Cavity:replacement Of Phenylalanines With Tryptophan" 100.00 153 98.03 100.00 5.08e-105 PDB 1TWE "Interleukin 1 Beta Mutant F101y" 100.00 153 99.34 100.00 2.84e-106 PDB 1TWM "Interleukin-1 Beta Mutant F146y" 100.00 153 99.34 100.00 2.84e-106 PDB 21BI "Interleukin-1 Beta (Il-1 Beta) (Mutant With Cys 71 Replaced By Ala) (C71a)" 100.00 153 99.34 99.34 1.43e-105 PDB 2I1B "Crystallographic Refinement Of Interleukin-1 Beta At 2.0 Angstroms Resolution" 100.00 153 100.00 100.00 1.29e-106 PDB 2KH2 "Solution Structure Of A Scfv-Il-1b Complex" 100.00 153 100.00 100.00 1.29e-106 PDB 2NVH "Determination Of Solvent Content In Cavities In Interleukin- 1 Using Experimentally-Phased Electron Density" 100.00 153 100.00 100.00 1.29e-106 PDB 31BI "Interleukin-1 Beta (Il-1 Beta) (Mutant With Cys 71 Replaced By Ser) (C71s)" 100.00 153 99.34 99.34 2.12e-105 PDB 3O4O "Crystal Structure Of An Interleukin-1 Receptor Complex" 100.00 158 100.00 100.00 1.99e-106 PDB 41BI "Interleukin-1 Beta (Il-1 Beta) (Mutant With Cys 8 Replaced By Ala (C8a)" 100.00 153 99.34 99.34 1.43e-105 PDB 4DEP "Structure Of The Il-1b Signaling Complex" 100.00 158 100.00 100.00 1.99e-106 PDB 4G6J "Crystal Structure Of Human Il-1beta In Complex With The Therapeutic Antibody Binding Fragment Of Canakinumab" 100.00 158 100.00 100.00 1.69e-106 PDB 4G6M "Crystal Strucure Of Human Il-1beta In Complex With Therapeutic Antibody Binding Fragment Of Gevokizumab" 98.68 150 100.00 100.00 2.72e-105 PDB 4I1B "Functional Implications Of Interleukin-1beta Based On The Three-Dimensional Structure" 100.00 153 100.00 100.00 1.29e-106 PDB 5BVP "The Molecular Mode Of Action And Species Specificity Of Canakinumab, A Human Monoclonal Antibody Neutralizing Il-1beta" 100.00 153 100.00 100.00 1.29e-106 PDB 5I1B "A Comparison Of The High Resolution Structures Of Human And Murine Interleukin-1b" 100.00 153 100.00 100.00 1.29e-106 PDB 6I1B "High-Resolution Three-Dimensional Structure Of Interleukin- 1 Beta In Solution By Three-And Four-Dimensional Nuclear Magnetic R" 100.00 153 100.00 100.00 1.29e-106 PDB 7I1B "High-Resolution Three-Dimensional Structure Of Interleukin- 1 Beta In Solution By Three-And Four-Dimensional Nuclear Magnetic R" 100.00 153 100.00 100.00 1.29e-106 PDB 9ILB "Human Interleukin-1 Beta" 100.00 153 100.00 100.00 1.29e-106 DBJ BAG70308 "interleukin-1 beta precursor [Homo sapiens]" 100.00 153 100.00 100.00 1.29e-106 DBJ BAG73311 "interleukin 1 beta [synthetic construct]" 100.00 269 100.00 100.00 1.76e-104 EMBL CAA26372 "unnamed protein product [Homo sapiens]" 100.00 269 100.00 100.00 1.76e-104 EMBL CAA28185 "prointerleukin-1-beta [Homo sapiens]" 100.00 269 100.00 100.00 1.76e-104 EMBL CAA39567 "prointerleukin-1 beta [Homo sapiens]" 100.00 269 100.00 100.00 1.76e-104 EMBL CAG28607 "IL1B [Homo sapiens]" 100.00 269 100.00 100.00 1.56e-104 GB AAA36106 "interleukin 1 precursor polypeptide [Homo sapiens]" 100.00 269 100.00 100.00 1.56e-104 GB AAA59135 "interleukin 1-beta [Homo sapiens]" 100.00 269 100.00 100.00 1.76e-104 GB AAA59136 "interleukin 1 precursor [Homo sapiens]" 100.00 269 98.68 98.68 2.18e-102 GB AAA72561 "interleukin 1-beta [synthetic construct]" 100.00 154 99.34 99.34 1.22e-105 GB AAA72849 "growth hormone:interleukin 1-beta fusion protein [synthetic construct]" 100.00 179 100.00 100.00 1.93e-106 PRF 1107273B "interleukin 1beta" 100.00 269 100.00 100.00 1.76e-104 REF NP_000567 "interleukin-1 beta proprotein [Homo sapiens]" 100.00 269 100.00 100.00 1.76e-104 REF XP_001147075 "PREDICTED: interleukin-1 beta [Pan troglodytes]" 100.00 269 100.00 100.00 2.07e-104 REF XP_002811835 "PREDICTED: interleukin-1 beta [Pongo abelii]" 100.00 268 99.34 100.00 4.08e-104 REF XP_003277734 "PREDICTED: interleukin-1 beta isoform X3 [Nomascus leucogenys]" 100.00 269 99.34 100.00 4.75e-104 REF XP_003804551 "PREDICTED: interleukin-1 beta [Pan paniscus]" 100.00 269 100.00 100.00 2.07e-104 SP P01584 "RecName: Full=Interleukin-1 beta; Short=IL-1 beta; AltName: Full=Catabolin; Flags: Precursor" 100.00 269 100.00 100.00 1.76e-104 TPE CAD29872 "TPA: pro-interleukin-1-beta [Homo sapiens]" 100.00 269 100.00 100.00 1.76e-104 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $interleukin_1-beta human 9606 Eukaryota Metazoa Homo sapiens generic 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 $interleukin_1-beta 'not available' . Escherichia coli generic . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.4 . na temperature 309 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H . . ppm 0 . . . . . $entry_citation $entry_citation '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 'interleukin 1-beta' _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 PRO HA H 4.5 . 1 2 . 1 PRO HD2 H 3.68 . 2 3 . 1 PRO HD3 H 3.59 . 2 4 . 2 VAL H H 8 . 1 5 . 2 VAL HA H 4.15 . 1 6 . 2 VAL HB H 1.93 . 1 7 . 2 VAL HG1 H .83 . 1 8 . 2 VAL HG2 H .83 . 1 9 . 2 VAL N N 119.1 . 1 10 . 3 ARG H H 9 . 1 11 . 3 ARG HA H 4.47 . 1 12 . 3 ARG N N 128.3 . 1 13 . 4 SER H H 8.28 . 1 14 . 4 SER N N 118.4 . 1 15 . 5 LEU H H 9.03 . 1 16 . 5 LEU HA H 4.78 . 1 17 . 5 LEU HB2 H 1.82 . 2 18 . 5 LEU HB3 H 1.81 . 2 19 . 5 LEU HG H 1.84 . 1 20 . 5 LEU HD1 H 1.02 . 2 21 . 5 LEU HD2 H .98 . 2 22 . 5 LEU N N 122.4 . 1 23 . 6 ASN H H 8.78 . 1 24 . 6 ASN HA H 6.25 . 1 25 . 6 ASN HB2 H 2.86 . 2 26 . 6 ASN HB3 H 2.32 . 2 27 . 6 ASN N N 120.9 . 1 28 . 7 CYS H H 9.59 . 1 29 . 7 CYS HA H 5.76 . 1 30 . 7 CYS HB2 H 2.96 . 2 31 . 7 CYS HB3 H 2.86 . 2 32 . 7 CYS N N 117.8 . 1 33 . 8 THR H H 8.93 . 1 34 . 8 THR HA H 5.06 . 1 35 . 8 THR HB H 4.39 . 1 36 . 8 THR HG2 H 1.18 . 1 37 . 8 THR N N 109.5 . 1 38 . 9 LEU H H 9.41 . 1 39 . 9 LEU HA H 5.45 . 1 40 . 9 LEU HB2 H 1.53 . 2 41 . 9 LEU HB3 H 1.07 . 2 42 . 9 LEU HG H 1.18 . 1 43 . 9 LEU HD1 H .58 . 2 44 . 9 LEU HD2 H .4 . 2 45 . 9 LEU N N 120.7 . 1 46 . 10 ARG H H 8.62 . 1 47 . 10 ARG HA H 5.28 . 1 48 . 10 ARG HB2 H 1.66 . 2 49 . 10 ARG HB3 H 1.6 . 2 50 . 10 ARG N N 119.6 . 1 51 . 11 ASP H H 8.71 . 1 52 . 11 ASP HA H 4.65 . 1 53 . 11 ASP N N 121.2 . 1 54 . 12 SER H H 7.42 . 1 55 . 12 SER HA H 3.99 . 1 56 . 12 SER HB2 H 3.95 . 2 57 . 12 SER HB3 H 3.56 . 2 58 . 12 SER N N 114.4 . 1 59 . 13 GLN H H 8.02 . 1 60 . 13 GLN HA H 4.55 . 1 61 . 13 GLN HB2 H 2.56 . 2 62 . 13 GLN HB3 H 1.59 . 2 63 . 13 GLN N N 120.4 . 1 64 . 14 GLN H H 8.44 . 1 65 . 14 GLN HA H 3.71 . 1 66 . 14 GLN HB2 H 2.62 . 1 67 . 14 GLN HB3 H 2.62 . 1 68 . 14 GLN N N 111.6 . 1 69 . 15 LYS H H 8.48 . 1 70 . 15 LYS HA H 3.55 . 1 71 . 15 LYS HB2 H 1.97 . 1 72 . 15 LYS HB3 H 1.97 . 1 73 . 15 LYS N N 120.2 . 1 74 . 16 SER H H 8.27 . 1 75 . 16 SER HA H 4.91 . 1 76 . 16 SER HB2 H 4.03 . 2 77 . 16 SER HB3 H 3.76 . 2 78 . 16 SER N N 119.5 . 1 79 . 17 LEU H H 8.82 . 1 80 . 17 LEU HA H 5.38 . 1 81 . 17 LEU HB2 H 2.15 . 2 82 . 17 LEU HB3 H 1.4 . 2 83 . 17 LEU N N 122.4 . 1 84 . 18 VAL H H 8.8 . 1 85 . 18 VAL HA H 4.68 . 1 86 . 18 VAL HB H 2.03 . 1 87 . 18 VAL HG1 H .78 . 2 88 . 18 VAL HG2 H .66 . 2 89 . 18 VAL N N 115.5 . 1 90 . 19 MET H H 8.68 . 1 91 . 19 MET HA H 4.9 . 1 92 . 19 MET HB2 H 2.19 . 2 93 . 19 MET HB3 H 1.7 . 2 94 . 19 MET HG2 H 2.5 . 2 95 . 19 MET HG3 H 2.36 . 2 96 . 19 MET N N 120.9 . 1 97 . 20 SER H H 8.59 . 1 98 . 20 SER HA H 4.52 . 1 99 . 20 SER HB2 H 3.6 . 2 100 . 20 SER HB3 H 3.52 . 2 101 . 20 SER N N 120 . 1 102 . 21 GLY H H 8.11 . 1 103 . 21 GLY HA2 H 4.12 . 2 104 . 21 GLY HA3 H 3.97 . 2 105 . 21 GLY N N 111.7 . 1 106 . 22 PRO HA H 4.02 . 1 107 . 22 PRO HD2 H 3.59 . 2 108 . 22 PRO HD3 H 3.44 . 2 109 . 23 TYR H H 8 . 1 110 . 23 TYR HA H 4.78 . 1 111 . 23 TYR HB2 H 3.54 . 2 112 . 23 TYR HB3 H 2.76 . 2 113 . 23 TYR HD1 H 7.09 . 1 114 . 23 TYR HD2 H 7.09 . 1 115 . 23 TYR HE1 H 6.78 . 1 116 . 23 TYR HE2 H 6.78 . 1 117 . 23 TYR N N 110.6 . 1 118 . 24 GLU H H 7.2 . 1 119 . 24 GLU HA H 4.67 . 1 120 . 24 GLU HB2 H 2.04 . 2 121 . 24 GLU HB3 H 1.94 . 2 122 . 24 GLU HG2 H 2.3 . 2 123 . 24 GLU HG3 H 2.24 . 2 124 . 24 GLU N N 119.3 . 1 125 . 25 LEU H H 8.57 . 1 126 . 25 LEU HA H 5.24 . 1 127 . 25 LEU HB2 H 1.63 . 1 128 . 25 LEU HB3 H 1.63 . 1 129 . 25 LEU N N 123 . 1 130 . 26 LYS H H 9.18 . 1 131 . 26 LYS HA H 5.14 . 1 132 . 26 LYS HB2 H 1.48 . 2 133 . 26 LYS HB3 H 1.43 . 2 134 . 26 LYS N N 119.8 . 1 135 . 27 ALA H H 7.62 . 1 136 . 27 ALA HA H 6.16 . 1 137 . 27 ALA HB H 1.31 . 1 138 . 27 ALA N N 118.9 . 1 139 . 28 LEU H H 9.42 . 1 140 . 28 LEU HA H 4.87 . 1 141 . 28 LEU HB2 H 1.95 . 2 142 . 28 LEU HB3 H 1.58 . 2 143 . 28 LEU N N 125.6 . 1 144 . 29 HIS H H 10.19 . 1 145 . 29 HIS HA H 4.69 . 1 146 . 29 HIS HB2 H 3.23 . 2 147 . 29 HIS HB3 H 3.16 . 2 148 . 29 HIS N N 122 . 1 149 . 30 LEU H H 8.4 . 1 150 . 30 LEU HA H 4.67 . 1 151 . 30 LEU HB2 H 1.7 . 2 152 . 30 LEU HB3 H 1.3 . 2 153 . 30 LEU N N 126 . 1 154 . 31 GLN H H 8.88 . 1 155 . 31 GLN HA H 4.53 . 1 156 . 31 GLN HB2 H 2.19 . 2 157 . 31 GLN HB3 H 1.98 . 2 158 . 31 GLN HG2 H 2.31 . 2 159 . 31 GLN HG3 H 2.25 . 2 160 . 31 GLN N N 120.2 . 1 161 . 32 GLY H H 8.72 . 1 162 . 32 GLY HA2 H 3.99 . 2 163 . 32 GLY HA3 H 3.77 . 2 164 . 32 GLY N N 109.5 . 1 165 . 33 GLN H H 8.83 . 1 166 . 33 GLN HA H 4.27 . 1 167 . 33 GLN HB2 H 2.1 . 1 168 . 33 GLN HB3 H 2.1 . 1 169 . 33 GLN N N 121.7 . 1 170 . 34 ASP H H 7.86 . 1 171 . 34 ASP HA H 4.75 . 1 172 . 34 ASP HB2 H 2.89 . 2 173 . 34 ASP HB3 H 2.79 . 2 174 . 34 ASP N N 119 . 1 175 . 35 MET H H 7.68 . 1 176 . 35 MET HA H 4.21 . 1 177 . 35 MET HB2 H 2.05 . 1 178 . 35 MET HB3 H 2.05 . 1 179 . 35 MET N N 118.3 . 1 180 . 36 GLU H H 8.07 . 1 181 . 36 GLU HA H 4.22 . 1 182 . 36 GLU HB2 H 2.1 . 2 183 . 36 GLU HB3 H 2.02 . 2 184 . 36 GLU N N 117.6 . 1 185 . 37 GLN H H 7.94 . 1 186 . 37 GLN HA H 4.21 . 1 187 . 37 GLN HB2 H 2.23 . 2 188 . 37 GLN HB3 H 1.97 . 2 189 . 37 GLN N N 117 . 1 190 . 38 GLN H H 7.53 . 1 191 . 38 GLN HA H 4.42 . 1 192 . 38 GLN N N 117.3 . 1 193 . 39 VAL H H 8.3 . 1 194 . 39 VAL HA H 3.78 . 1 195 . 39 VAL HB H 1.58 . 1 196 . 39 VAL HG1 H .62 . 2 197 . 39 VAL HG2 H .19 . 2 198 . 39 VAL N N 122.7 . 1 199 . 40 VAL H H 7.69 . 1 200 . 40 VAL HA H 4.24 . 1 201 . 40 VAL HB H 1.83 . 1 202 . 40 VAL HG1 H .85 . 1 203 . 40 VAL HG2 H .85 . 1 204 . 40 VAL N N 123.9 . 1 205 . 41 PHE H H 9.58 . 1 206 . 41 PHE HA H 5.04 . 1 207 . 41 PHE HB2 H 3.07 . 2 208 . 41 PHE HB3 H 2.57 . 2 209 . 41 PHE HD1 H 6.9 . 1 210 . 41 PHE HD2 H 6.9 . 1 211 . 41 PHE HE1 H 7 . 1 212 . 41 PHE HE2 H 7 . 1 213 . 41 PHE HZ H 6.62 . 1 214 . 41 PHE N N 127.3 . 1 215 . 42 SER H H 9.17 . 1 216 . 42 SER HA H 5.16 . 1 217 . 42 SER HB2 H 3.61 . 2 218 . 42 SER HB3 H 3.45 . 2 219 . 42 SER N N 115.6 . 1 220 . 43 MET H H 9.57 . 1 221 . 43 MET HA H 5.3 . 1 222 . 43 MET HB2 H 2.23 . 1 223 . 43 MET HB3 H 2.23 . 1 224 . 43 MET N N 131.3 . 1 225 . 44 SER H H 8.88 . 1 226 . 44 SER HA H 5.36 . 1 227 . 44 SER HB2 H 3.71 . 2 228 . 44 SER HB3 H 3.58 . 2 229 . 44 SER N N 121.1 . 1 230 . 45 PHE H H 8.46 . 1 231 . 45 PHE HA H 4.77 . 1 232 . 45 PHE HB2 H 3.37 . 2 233 . 45 PHE HB3 H 2.98 . 2 234 . 45 PHE HD1 H 7.23 . 1 235 . 45 PHE HD2 H 7.23 . 1 236 . 45 PHE HE1 H 7.13 . 1 237 . 45 PHE HE2 H 7.13 . 1 238 . 45 PHE N N 123.2 . 1 239 . 46 VAL H H 7.45 . 1 240 . 46 VAL HA H 4.66 . 1 241 . 46 VAL N N 118.6 . 1 242 . 47 GLN H H 8.56 . 1 243 . 47 GLN N N 120.5 . 1 244 . 48 GLY H H 8.33 . 1 245 . 48 GLY HA2 H 4.12 . 2 246 . 48 GLY HA3 H 3.94 . 2 247 . 48 GLY N N 111.6 . 1 248 . 49 GLU H H 8.47 . 1 249 . 49 GLU HA H 4.35 . 1 250 . 49 GLU HB2 H 2.06 . 2 251 . 49 GLU HB3 H 1.92 . 2 252 . 49 GLU N N 121.3 . 1 253 . 50 GLU H H 8.51 . 1 254 . 50 GLU HA H 4.5 . 1 255 . 50 GLU HB2 H 2.09 . 2 256 . 50 GLU HB3 H 2.01 . 2 257 . 50 GLU HG2 H 2.34 . 2 258 . 50 GLU HG3 H 2.27 . 2 259 . 50 GLU N N 122.6 . 1 260 . 51 SER H H 8.39 . 1 261 . 51 SER HA H 4.63 . 1 262 . 51 SER HB2 H 3.97 . 2 263 . 51 SER HB3 H 3.88 . 2 264 . 51 SER N N 116.8 . 1 265 . 52 ASN H H 8.61 . 1 266 . 52 ASN HA H 4.6 . 1 267 . 52 ASN HB2 H 2.9 . 2 268 . 52 ASN HB3 H 2.83 . 2 269 . 52 ASN N N 119.7 . 1 270 . 53 ASP H H 8.53 . 1 271 . 53 ASP HA H 4.59 . 1 272 . 53 ASP HB2 H 2.77 . 1 273 . 53 ASP HB3 H 2.77 . 1 274 . 53 ASP N N 116.2 . 1 275 . 54 LYS H H 7.6 . 1 276 . 54 LYS HA H 4.69 . 1 277 . 54 LYS HB2 H 1.74 . 2 278 . 54 LYS HB3 H 1.51 . 2 279 . 54 LYS N N 118.8 . 1 280 . 55 ILE H H 8.37 . 1 281 . 55 ILE HA H 4.86 . 1 282 . 55 ILE HB H 2.09 . 1 283 . 55 ILE HG2 H 1.16 . 1 284 . 55 ILE N N 122.7 . 1 285 . 56 PRO HA H 5.37 . 1 286 . 56 PRO HB2 H 2.15 . 2 287 . 56 PRO HB3 H 1.83 . 2 288 . 56 PRO HG2 H 1.86 . 1 289 . 56 PRO HG3 H 1.86 . 1 290 . 56 PRO HD2 H 4 . 2 291 . 56 PRO HD3 H 3.96 . 2 292 . 57 VAL H H 10.01 . 1 293 . 57 VAL HA H 5.64 . 1 294 . 57 VAL HB H 2.08 . 1 295 . 57 VAL HG1 H .82 . 2 296 . 57 VAL HG2 H .73 . 2 297 . 57 VAL N N 117.8 . 1 298 . 58 ALA H H 8.68 . 1 299 . 58 ALA HA H 5.42 . 1 300 . 58 ALA HB H 1.51 . 1 301 . 58 ALA N N 120.9 . 1 302 . 59 LEU H H 10.53 . 1 303 . 59 LEU HA H 4.86 . 1 304 . 59 LEU HB2 H 1.51 . 2 305 . 59 LEU HB3 H .86 . 2 306 . 59 LEU N N 124.3 . 1 307 . 60 GLY H H 8.26 . 1 308 . 60 GLY HA2 H 4.15 . 2 309 . 60 GLY HA3 H 2.38 . 2 310 . 60 GLY N N 109.9 . 1 311 . 61 LEU H H 8.22 . 1 312 . 61 LEU HA H 4.46 . 1 313 . 61 LEU HB2 H 1.41 . 2 314 . 61 LEU HB3 H 1.34 . 2 315 . 61 LEU N N 121.4 . 1 316 . 62 LYS H H 8.16 . 1 317 . 62 LYS HA H 3.84 . 1 318 . 62 LYS N N 126.3 . 1 319 . 63 GLU H H 8.9 . 1 320 . 63 GLU HA H 3.98 . 1 321 . 63 GLU HB2 H 2.24 . 2 322 . 63 GLU HB3 H 2.09 . 2 323 . 63 GLU N N 118.6 . 1 324 . 64 LYS H H 7.57 . 1 325 . 64 LYS HA H 4.48 . 1 326 . 64 LYS HB2 H 1.47 . 1 327 . 64 LYS HB3 H 1.47 . 1 328 . 64 LYS N N 115.1 . 1 329 . 65 ASN H H 8.4 . 1 330 . 65 ASN HA H 4.41 . 1 331 . 65 ASN HB2 H 3.14 . 2 332 . 65 ASN HB3 H 3.01 . 2 333 . 65 ASN N N 116.2 . 1 334 . 66 LEU H H 6.82 . 1 335 . 66 LEU HA H 5.34 . 1 336 . 66 LEU HB2 H 1.42 . 2 337 . 66 LEU HB3 H 1.17 . 2 338 . 66 LEU N N 115.7 . 1 339 . 67 TYR H H 9.18 . 1 340 . 67 TYR HA H 4.96 . 1 341 . 67 TYR HB2 H 3.08 . 2 342 . 67 TYR HB3 H 2.51 . 2 343 . 67 TYR HD1 H 6.88 . 1 344 . 67 TYR HD2 H 6.88 . 1 345 . 67 TYR HE1 H 6.51 . 1 346 . 67 TYR HE2 H 6.51 . 1 347 . 67 TYR N N 121.5 . 1 348 . 68 LEU H H 8.49 . 1 349 . 68 LEU HA H 4.84 . 1 350 . 68 LEU HB2 H 1.96 . 2 351 . 68 LEU HB3 H 1.66 . 2 352 . 68 LEU N N 121.8 . 1 353 . 69 SER H H 9.17 . 1 354 . 69 SER HA H 5.23 . 1 355 . 69 SER HB2 H 3.66 . 2 356 . 69 SER HB3 H 3.28 . 2 357 . 69 SER N N 115.8 . 1 358 . 70 CYS H H 8.35 . 1 359 . 70 CYS HA H 5.53 . 1 360 . 70 CYS HB2 H 2.86 . 2 361 . 70 CYS HB3 H 2.46 . 2 362 . 70 CYS N N 119.5 . 1 363 . 71 VAL H H 8.8 . 1 364 . 71 VAL HA H 4.58 . 1 365 . 71 VAL HB H 1.99 . 1 366 . 71 VAL HG1 H .71 . 2 367 . 71 VAL HG2 H .55 . 2 368 . 71 VAL N N 117 . 1 369 . 72 LEU H H 8.52 . 1 370 . 72 LEU HA H 4.17 . 1 371 . 72 LEU HB2 H 1.48 . 2 372 . 72 LEU HB3 H 1.36 . 2 373 . 72 LEU HG H 1.35 . 1 374 . 72 LEU HD1 H .59 . 2 375 . 72 LEU HD2 H .43 . 2 376 . 72 LEU N N 123.7 . 1 377 . 73 LYS H H 8.2 . 1 378 . 73 LYS HA H 4.39 . 1 379 . 73 LYS HB2 H 1.8 . 2 380 . 73 LYS HB3 H 1.53 . 2 381 . 73 LYS N N 126.4 . 1 382 . 74 ASP H H 9.22 . 1 383 . 74 ASP HA H 4.15 . 1 384 . 74 ASP HB2 H 2.81 . 2 385 . 74 ASP HB3 H 2.66 . 2 386 . 74 ASP N N 127.5 . 1 387 . 75 ASP H H 8.46 . 1 388 . 75 ASP HA H 4.07 . 1 389 . 75 ASP HB2 H 2.86 . 2 390 . 75 ASP HB3 H 2.79 . 2 391 . 75 ASP N N 109.9 . 1 392 . 76 LYS H H 7.71 . 1 393 . 76 LYS HA H 4.66 . 1 394 . 76 LYS HB2 H 1.67 . 2 395 . 76 LYS HB3 H 1.6 . 2 396 . 76 LYS N N 119.8 . 1 397 . 77 PRO HA H 3.19 . 1 398 . 77 PRO HD2 H 3.07 . 1 399 . 77 PRO HD3 H 3.07 . 1 400 . 78 THR H H 8.83 . 1 401 . 78 THR HA H 4.58 . 1 402 . 78 THR HB H 3.93 . 1 403 . 78 THR HG2 H 1.2 . 1 404 . 78 THR N N 120 . 1 405 . 79 LEU H H 8.83 . 1 406 . 79 LEU HA H 5.13 . 1 407 . 79 LEU HB2 H 2 . 2 408 . 79 LEU HB3 H 1.5 . 2 409 . 79 LEU HG H 1.6 . 1 410 . 79 LEU HD1 H 1.09 . 2 411 . 79 LEU HD2 H .75 . 2 412 . 79 LEU N N 127.1 . 1 413 . 80 GLN H H 9.68 . 1 414 . 80 GLN HA H 4.98 . 1 415 . 80 GLN HB2 H 1.96 . 1 416 . 80 GLN HB3 H 1.96 . 1 417 . 80 GLN N N 126.3 . 1 418 . 81 LEU H H 8.44 . 1 419 . 81 LEU HA H 5.01 . 1 420 . 81 LEU HB2 H 1.83 . 2 421 . 81 LEU HB3 H 1.37 . 2 422 . 81 LEU HG H 1.59 . 1 423 . 81 LEU HD1 H .72 . 2 424 . 81 LEU HD2 H .71 . 2 425 . 81 LEU N N 122 . 1 426 . 82 GLU H H 9.17 . 1 427 . 82 GLU HA H 4.63 . 1 428 . 82 GLU HB2 H 2.1 . 1 429 . 82 GLU HB3 H 2.1 . 1 430 . 82 GLU N N 123.8 . 1 431 . 83 SER H H 8.71 . 1 432 . 83 SER HA H 5.15 . 1 433 . 83 SER HB2 H 3.92 . 2 434 . 83 SER HB3 H 3.9 . 2 435 . 83 SER N N 121.2 . 1 436 . 84 VAL H H 7.92 . 1 437 . 84 VAL HA H 4.59 . 1 438 . 84 VAL HB H 1.52 . 1 439 . 84 VAL N N 117.3 . 1 440 . 85 ASP H H 8.04 . 1 441 . 85 ASP HA H 4.9 . 1 442 . 85 ASP HB2 H 2.96 . 2 443 . 85 ASP HB3 H 2.69 . 2 444 . 85 ASP N N 122 . 1 445 . 87 LYS H H 8.38 . 1 446 . 87 LYS HA H 4.2 . 1 447 . 87 LYS HB2 H 1.8 . 2 448 . 87 LYS HB3 H 1.73 . 2 449 . 87 LYS N N 117.1 . 1 450 . 88 ASN H H 7.78 . 1 451 . 88 ASN HA H 4.75 . 1 452 . 88 ASN HB2 H 2.64 . 2 453 . 88 ASN HB3 H 2.5 . 2 454 . 88 ASN N N 114.5 . 1 455 . 89 TYR H H 7.3 . 1 456 . 89 TYR N N 116.7 . 1 457 . 90 PRO HA H 4.25 . 1 458 . 91 LYS H H 7.24 . 1 459 . 91 LYS HA H 4.41 . 1 460 . 91 LYS N N 117.3 . 1 461 . 92 LYS H H 8.29 . 1 462 . 92 LYS N N 119.3 . 1 463 . 93 LYS H H 7.8 . 1 464 . 93 LYS HA H 4.59 . 1 465 . 93 LYS HB2 H 1.75 . 2 466 . 93 LYS HB3 H 1.51 . 2 467 . 93 LYS HG2 H 1.3 . 2 468 . 93 LYS HG3 H 1.26 . 2 469 . 93 LYS N N 118 . 1 470 . 94 MET H H 7.64 . 1 471 . 94 MET HA H 4.23 . 1 472 . 94 MET N N 122.5 . 1 473 . 95 GLU H H 9.14 . 1 474 . 95 GLU HA H 4.09 . 1 475 . 95 GLU HB2 H 2.23 . 2 476 . 95 GLU HB3 H 2.08 . 2 477 . 95 GLU HG2 H 2.72 . 2 478 . 95 GLU HG3 H 2.44 . 2 479 . 95 GLU N N 122.7 . 1 480 . 96 LYS H H 8.23 . 1 481 . 96 LYS HA H 3.71 . 1 482 . 96 LYS HB2 H 1.71 . 2 483 . 96 LYS HB3 H 1.63 . 2 484 . 96 LYS HG2 H 1.3 . 2 485 . 96 LYS HG3 H 1.24 . 2 486 . 96 LYS N N 121.5 . 1 487 . 97 ARG H H 7.88 . 1 488 . 97 ARG HA H 3.91 . 1 489 . 97 ARG HB2 H 1.56 . 2 490 . 97 ARG HB3 H 1.49 . 2 491 . 97 ARG N N 114.2 . 1 492 . 98 PHE H H 7.84 . 1 493 . 98 PHE HA H 5.16 . 1 494 . 98 PHE HB2 H 3.69 . 2 495 . 98 PHE HB3 H 2.87 . 2 496 . 98 PHE HD1 H 7.51 . 1 497 . 98 PHE HD2 H 7.51 . 1 498 . 98 PHE HE1 H 7.04 . 1 499 . 98 PHE HE2 H 7.04 . 1 500 . 98 PHE HZ H 6.89 . 1 501 . 98 PHE N N 116.6 . 1 502 . 99 VAL H H 7.45 . 1 503 . 99 VAL HA H 4.36 . 1 504 . 99 VAL HB H 1.92 . 1 505 . 99 VAL HG1 H .9 . 2 506 . 99 VAL HG2 H .82 . 2 507 . 99 VAL N N 117.8 . 1 508 . 100 PHE H H 9.83 . 1 509 . 100 PHE HA H 5.15 . 1 510 . 100 PHE HB2 H 2.7 . 2 511 . 100 PHE HB3 H 2.67 . 2 512 . 100 PHE HD1 H 6.98 . 1 513 . 100 PHE HD2 H 6.98 . 1 514 . 100 PHE HE1 H 7.06 . 1 515 . 100 PHE HE2 H 7.06 . 1 516 . 100 PHE HZ H 6.81 . 1 517 . 100 PHE N N 127.2 . 1 518 . 101 ASN H H 10.38 . 1 519 . 101 ASN HA H 5.01 . 1 520 . 101 ASN HB2 H 2.92 . 2 521 . 101 ASN HB3 H 2.29 . 2 522 . 101 ASN N N 121.1 . 1 523 . 102 LYS H H 9.38 . 1 524 . 102 LYS HA H 4.64 . 1 525 . 102 LYS N N 127.7 . 1 526 . 103 ILE H H 9.23 . 1 527 . 103 ILE HA H 4.45 . 1 528 . 103 ILE HB H 1.74 . 1 529 . 103 ILE HG2 H .9 . 1 530 . 103 ILE N N 133.7 . 1 531 . 104 GLU H H 8.48 . 1 532 . 104 GLU HA H 5.14 . 1 533 . 104 GLU HB2 H 1.94 . 2 534 . 104 GLU HB3 H 1.73 . 2 535 . 104 GLU HG2 H 2.14 . 2 536 . 104 GLU HG3 H 2.05 . 2 537 . 104 GLU N N 126.8 . 1 538 . 105 ILE H H 8.67 . 1 539 . 105 ILE HA H 4.33 . 1 540 . 105 ILE HB H 1.68 . 1 541 . 105 ILE HG12 H 1.36 . 2 542 . 105 ILE HG13 H 1.03 . 2 543 . 105 ILE HG2 H .8 . 1 544 . 105 ILE HD1 H .78 . 1 545 . 105 ILE N N 125.6 . 1 546 . 106 ASN H H 9.28 . 1 547 . 106 ASN HA H 4.27 . 1 548 . 106 ASN HB2 H 2.99 . 2 549 . 106 ASN HB3 H 2.72 . 2 550 . 106 ASN N N 126.4 . 1 551 . 107 ASN H H 8.81 . 1 552 . 107 ASN HA H 4.38 . 1 553 . 107 ASN HB2 H 3.02 . 1 554 . 107 ASN HB3 H 3.02 . 1 555 . 107 ASN N N 110.7 . 1 556 . 108 LYS H H 8.03 . 1 557 . 108 LYS HA H 4.78 . 1 558 . 108 LYS HB2 H 1.85 . 2 559 . 108 LYS HB3 H 1.83 . 2 560 . 108 LYS N N 120.1 . 1 561 . 109 LEU H H 9.43 . 1 562 . 109 LEU HA H 5.42 . 1 563 . 109 LEU HB2 H 1.36 . 2 564 . 109 LEU HB3 H .94 . 2 565 . 109 LEU HG H 1.54 . 1 566 . 109 LEU HD1 H .77 . 2 567 . 109 LEU HD2 H .73 . 2 568 . 109 LEU N N 121 . 1 569 . 110 GLU H H 8.76 . 1 570 . 110 GLU HA H 5 . 1 571 . 110 GLU HB2 H 1.99 . 1 572 . 110 GLU HB3 H 1.99 . 1 573 . 110 GLU N N 117.8 . 1 574 . 111 PHE H H 10.28 . 1 575 . 111 PHE HA H 5.23 . 1 576 . 111 PHE HB2 H 2.54 . 2 577 . 111 PHE HB3 H 2.36 . 2 578 . 111 PHE HD1 H 6.62 . 1 579 . 111 PHE HD2 H 6.62 . 1 580 . 111 PHE HE1 H 6.65 . 1 581 . 111 PHE HE2 H 6.65 . 1 582 . 111 PHE N N 119.5 . 1 583 . 112 GLU H H 8.82 . 1 584 . 112 GLU HA H 4.47 . 1 585 . 112 GLU N N 126.2 . 1 586 . 113 SER H H 9.14 . 1 587 . 113 SER HA H 3.9 . 1 588 . 113 SER HB2 H 4.37 . 2 589 . 113 SER HB3 H 4.1 . 2 590 . 113 SER N N 121.9 . 1 591 . 114 ALA H H 8.12 . 1 592 . 114 ALA HA H 4.05 . 1 593 . 114 ALA HB H 1.17 . 1 594 . 114 ALA N N 128.5 . 1 595 . 115 GLN H H 7.87 . 1 596 . 115 GLN HA H 3.61 . 1 597 . 115 GLN HB2 H 1.42 . 2 598 . 115 GLN HB3 H .98 . 2 599 . 115 GLN N N 116.9 . 1 600 . 116 PHE H H 7.38 . 1 601 . 116 PHE HA H 4.86 . 1 602 . 116 PHE HB2 H 2.64 . 2 603 . 116 PHE HB3 H 2.58 . 2 604 . 116 PHE HD1 H 6.91 . 1 605 . 116 PHE HD2 H 6.91 . 1 606 . 116 PHE HE1 H 6.81 . 1 607 . 116 PHE HE2 H 6.81 . 1 608 . 116 PHE N N 116.9 . 1 609 . 117 PRO HA H 4.4 . 1 610 . 117 PRO HB2 H 2.29 . 1 611 . 117 PRO HB3 H 2.29 . 1 612 . 117 PRO HG2 H 3.54 . 2 613 . 117 PRO HG3 H 3.31 . 2 614 . 117 PRO HD2 H 2 . 2 615 . 117 PRO HD3 H 1.87 . 2 616 . 118 ASN H H 10.23 . 1 617 . 118 ASN HA H 4.04 . 1 618 . 118 ASN HB2 H 3.37 . 2 619 . 118 ASN HB3 H 3.03 . 2 620 . 118 ASN N N 114.1 . 1 621 . 119 TRP H H 8.11 . 1 622 . 119 TRP HA H 4.98 . 1 623 . 119 TRP HB2 H 3.67 . 2 624 . 119 TRP HB3 H 2.92 . 2 625 . 119 TRP HD1 H 7.3 . 1 626 . 119 TRP HE1 H 10.01 . 1 627 . 119 TRP HE3 H 7.1 . 1 628 . 119 TRP HZ2 H 7.45 . 1 629 . 119 TRP HZ3 H 7.21 . 1 630 . 119 TRP HH2 H 7.21 . 1 631 . 119 TRP N N 119.7 . 1 632 . 120 TYR H H 9.4 . 1 633 . 120 TYR HA H 5.64 . 1 634 . 120 TYR HB2 H 3.5 . 2 635 . 120 TYR HB3 H 2.41 . 2 636 . 120 TYR HD1 H 7.01 . 1 637 . 120 TYR HD2 H 7.01 . 1 638 . 120 TYR HE1 H 6.63 . 1 639 . 120 TYR HE2 H 6.63 . 1 640 . 120 TYR N N 119.4 . 1 641 . 121 ILE H H 8.65 . 1 642 . 121 ILE HA H 3.84 . 1 643 . 121 ILE HB H 1.62 . 1 644 . 121 ILE HG2 H .41 . 1 645 . 121 ILE N N 124.6 . 1 646 . 122 SER H H 8.98 . 1 647 . 122 SER HA H 5.82 . 1 648 . 122 SER HB2 H 3 . 2 649 . 122 SER HB3 H 2.06 . 2 650 . 122 SER N N 122.5 . 1 651 . 123 THR H H 8.99 . 1 652 . 123 THR HA H 4.83 . 1 653 . 123 THR HB H 4.39 . 1 654 . 123 THR HG2 H 1.16 . 1 655 . 123 THR N N 109.9 . 1 656 . 124 SER H H 9.55 . 1 657 . 124 SER HA H 4.97 . 1 658 . 124 SER HB2 H 3.98 . 2 659 . 124 SER HB3 H 3.93 . 2 660 . 124 SER N N 113.8 . 1 661 . 125 GLN H H 8.87 . 1 662 . 125 GLN HA H 3.98 . 1 663 . 125 GLN HB2 H 2.24 . 2 664 . 125 GLN HB3 H 2.01 . 2 665 . 125 GLN HG2 H 2.63 . 2 666 . 125 GLN HG3 H 2.38 . 2 667 . 125 GLN N N 122.1 . 1 668 . 126 ALA H H 8.17 . 1 669 . 126 ALA HA H 4.38 . 1 670 . 126 ALA HB H 1.44 . 1 671 . 126 ALA N N 120 . 1 672 . 127 GLU H H 8.44 . 1 673 . 127 GLU HA H 4.04 . 1 674 . 127 GLU HB2 H 2.27 . 2 675 . 127 GLU HB3 H 1.96 . 2 676 . 127 GLU N N 117.2 . 1 677 . 128 ASN H H 8.06 . 1 678 . 128 ASN HA H 4.18 . 1 679 . 128 ASN HB2 H 3.31 . 2 680 . 128 ASN HB3 H 2.55 . 2 681 . 128 ASN N N 114.1 . 1 682 . 129 MET H H 8.84 . 1 683 . 129 MET HA H 5.23 . 1 684 . 129 MET HB2 H 2.36 . 2 685 . 129 MET HB3 H 2.15 . 2 686 . 129 MET N N 117.7 . 1 687 . 130 PRO HA H 5.2 . 1 688 . 130 PRO HD2 H 3.94 . 2 689 . 130 PRO HD3 H 3.78 . 2 690 . 131 VAL H H 8.01 . 1 691 . 131 VAL HA H 4.42 . 1 692 . 131 VAL HB H 1.75 . 1 693 . 131 VAL HG1 H .86 . 1 694 . 131 VAL HG2 H .86 . 1 695 . 131 VAL N N 125.4 . 1 696 . 132 PHE H H 8.65 . 1 697 . 132 PHE HA H 5.27 . 1 698 . 132 PHE HB2 H 3.3 . 2 699 . 132 PHE HB3 H 2.97 . 2 700 . 132 PHE HD1 H 7.31 . 1 701 . 132 PHE HD2 H 7.31 . 1 702 . 132 PHE HE1 H 7.23 . 1 703 . 132 PHE HE2 H 7.23 . 1 704 . 132 PHE HZ H 7.13 . 1 705 . 132 PHE N N 124.6 . 1 706 . 133 LEU H H 8.58 . 1 707 . 133 LEU HA H 5.21 . 1 708 . 133 LEU N N 119.7 . 1 709 . 134 GLY H H 9.34 . 1 710 . 134 GLY HA2 H 4.92 . 2 711 . 134 GLY HA3 H 4.02 . 2 712 . 134 GLY N N 114.9 . 1 713 . 135 GLY H H 8.75 . 1 714 . 135 GLY HA2 H 3.84 . 2 715 . 135 GLY HA3 H 2.93 . 2 716 . 135 GLY N N 111.2 . 1 717 . 136 THR H H 7.46 . 1 718 . 136 THR HA H 4.31 . 1 719 . 136 THR HB H 3.99 . 1 720 . 136 THR HG2 H .96 . 1 721 . 136 THR N N 112.1 . 1 722 . 137 LYS H H 8.37 . 1 723 . 137 LYS HA H 4.29 . 1 724 . 137 LYS HB2 H 1.56 . 2 725 . 137 LYS HB3 H 1.53 . 2 726 . 137 LYS N N 124.4 . 1 727 . 138 GLY H H 8.63 . 1 728 . 138 GLY HA2 H 4.02 . 2 729 . 138 GLY HA3 H 3.83 . 2 730 . 138 GLY N N 111.5 . 1 731 . 139 GLY H H 8.15 . 1 732 . 139 GLY HA2 H 4.2 . 2 733 . 139 GLY HA3 H 3.78 . 2 734 . 139 GLY N N 109 . 1 735 . 140 GLN H H 8.4 . 1 736 . 140 GLN HA H 4.29 . 1 737 . 140 GLN HB2 H 2.2 . 2 738 . 140 GLN HB3 H 2 . 2 739 . 140 GLN N N 119.7 . 1 740 . 141 ASP H H 7.79 . 1 741 . 141 ASP HA H 4.93 . 1 742 . 141 ASP HB2 H 2.82 . 2 743 . 141 ASP HB3 H 2.57 . 2 744 . 141 ASP N N 119.6 . 1 745 . 142 ILE H H 9.18 . 1 746 . 142 ILE HA H 3.92 . 1 747 . 142 ILE HB H 2.41 . 1 748 . 142 ILE HG2 H .78 . 1 749 . 142 ILE N N 125.5 . 1 750 . 143 THR H H 8.12 . 1 751 . 143 THR HA H 4.99 . 1 752 . 143 THR HB H 4.39 . 1 753 . 143 THR HG2 H .96 . 1 754 . 143 THR N N 111.8 . 1 755 . 144 ASP H H 7.1 . 1 756 . 144 ASP HA H 5.58 . 1 757 . 144 ASP HB2 H 2.54 . 2 758 . 144 ASP HB3 H 2.42 . 2 759 . 144 ASP N N 120.6 . 1 760 . 145 PHE H H 9.55 . 1 761 . 145 PHE HA H 5.22 . 1 762 . 145 PHE HB2 H 3.09 . 2 763 . 145 PHE HB3 H 2.63 . 2 764 . 145 PHE HD1 H 7.01 . 1 765 . 145 PHE HD2 H 7.01 . 1 766 . 145 PHE HE1 H 7.11 . 1 767 . 145 PHE HE2 H 7.11 . 1 768 . 145 PHE HZ H 6.81 . 1 769 . 145 PHE N N 118 . 1 770 . 146 THR H H 9.47 . 1 771 . 146 THR HA H 4.74 . 1 772 . 146 THR HB H 4.19 . 1 773 . 146 THR HG2 H 1.22 . 1 774 . 146 THR N N 110 . 1 775 . 147 MET H H 8.67 . 1 776 . 147 MET HA H 5.39 . 1 777 . 147 MET HB2 H 1.78 . 1 778 . 147 MET HB3 H 1.78 . 1 779 . 147 MET N N 121.3 . 1 780 . 148 GLN H H 8.43 . 1 781 . 148 GLN HA H 4.63 . 1 782 . 148 GLN HB2 H 2.07 . 1 783 . 148 GLN HB3 H 2.07 . 1 784 . 148 GLN N N 123.7 . 1 785 . 149 PHE H H 8.72 . 1 786 . 149 PHE HA H 4.77 . 1 787 . 149 PHE HB2 H 3.26 . 2 788 . 149 PHE HB3 H 3.03 . 2 789 . 149 PHE HD1 H 7.33 . 1 790 . 149 PHE HD2 H 7.33 . 1 791 . 149 PHE HE1 H 7.39 . 1 792 . 149 PHE HE2 H 7.39 . 1 793 . 149 PHE N N 123.7 . 1 794 . 150 VAL H H 8.05 . 1 795 . 150 VAL HA H 4.36 . 1 796 . 150 VAL HB H 1.84 . 1 797 . 150 VAL HG1 H .95 . 2 798 . 150 VAL HG2 H .9 . 2 799 . 150 VAL N N 122.6 . 1 800 . 151 SER H H 8.39 . 1 801 . 151 SER HA H 4.48 . 1 802 . 151 SER HB2 H 3.94 . 1 803 . 151 SER HB3 H 3.94 . 1 804 . 151 SER N N 119.4 . 1 805 . 152 SER H H 7.98 . 1 806 . 152 SER HA H 4.31 . 1 807 . 152 SER HB2 H 3.89 . 1 808 . 152 SER HB3 H 3.89 . 1 809 . 152 SER N N 122.5 . 1 stop_ save_