data_16104 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; THE DYNAMIC ALPHA-HELIX STRUCTURE OF MICELLE-BOUND HUMAN AMYLIN. ; _BMRB_accession_number 16104 _BMRB_flat_file_name bmr16104.str _Entry_type original _Submission_date 2009-01-02 _Accession_date 2009-01-02 _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 Patil Sharadrao M. . 2 Xu Shihao . . 3 Sheftic Sarah R. . 4 Alexandrescu Andrei T. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 160 "15N chemical shifts" 44 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-05-27 update BMRB 'edit entity/assembly name' 2009-04-30 update BMRB 'complete entry citation' 2009-03-17 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'THE DYNAMIC ALPHA-HELIX STRUCTURE OF MICELLE-BOUND HUMAN AMYLIN.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19244249 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Patil Sharadrao M. . 2 Xu Shihao . . 3 Sheftic Sarah R. . 4 Alexandrescu Andrei T. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 284 _Journal_issue 18 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 11982 _Page_last 11991 _Year 2009 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name AMYLIN _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label alpha-helix $entity stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common alpha-helix _Molecular_mass 3909.330 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 37 _Mol_residue_sequence ; KCNTATCATQRLANFLVHSS NNFGAILSSTNVGSNTY ; loop_ _Residue_seq_code _Residue_label 1 LYS 2 CYS 3 ASN 4 THR 5 ALA 6 THR 7 CYS 8 ALA 9 THR 10 GLN 11 ARG 12 LEU 13 ALA 14 ASN 15 PHE 16 LEU 17 VAL 18 HIS 19 SER 20 SER 21 ASN 22 ASN 23 PHE 24 GLY 25 ALA 26 ILE 27 LEU 28 SER 29 SER 30 THR 31 ASN 32 VAL 33 GLY 34 SER 35 ASN 36 THR 37 TYR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-06-13 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 16105 alpha-helix 100.00 37 100.00 100.00 4.86e-16 BMRB 17394 entity 100.00 37 100.00 100.00 4.86e-16 BMRB 18795 Amylin 100.00 37 100.00 100.00 4.86e-16 BMRB 20045 IAPP 51.35 19 100.00 100.00 1.92e-03 PDB 2G48 "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amylin" 100.00 37 100.00 100.00 4.86e-16 PDB 2KB8 "The Dynamic Alpha-Helix Structure Of Micelle-Bound Human Amylin" 97.30 37 100.00 100.00 6.11e-15 PDB 2L86 "Solution Nmr Structure Of Human Amylin In Sds Micelles At Ph 7.3" 100.00 38 100.00 100.00 4.93e-16 PDB 3G7V "Islet Amyloid Polypeptide (iapp Or Amylin) Fused To Maltose Binding Protein" 100.00 408 100.00 100.00 4.45e-16 PDB 3G7W "Islet Amyloid Polypeptide (Iapp Or Amylin) Residues 1 To 22 Fused To Maltose Binding Protein" 59.46 393 100.00 100.00 4.63e-06 PDB 3HGZ "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amylin" 100.00 37 100.00 100.00 4.86e-16 DBJ BAG73319 "islet amyloid polypeptide [synthetic construct]" 100.00 89 100.00 100.00 1.75e-16 EMBL CAA33032 "unnamed protein product [Homo sapiens]" 100.00 89 100.00 100.00 1.75e-16 EMBL CAA37002 "islet amyloid polypeptide [Homo sapiens]" 100.00 89 100.00 100.00 1.75e-16 EMBL CAA39504 "IAPP [Homo sapiens]" 100.00 89 97.30 97.30 1.77e-15 EMBL CAA48724 "islet amyloid polypeptide (IAAP) [Homo sapiens]" 100.00 89 100.00 100.00 1.75e-16 EMBL CAB57803 "prepro-IAPP [Homo sapiens]" 100.00 62 100.00 100.00 2.29e-16 GB AAA35524 "amylin, partial [Homo sapiens]" 100.00 62 100.00 100.00 2.29e-16 GB AAA35983 "islet amyloid polypeptide (hIAPP), partial [Homo sapiens]" 100.00 89 100.00 100.00 1.75e-16 GB AAA51728 "amyloid protein, partial [Homo sapiens]" 100.00 62 100.00 100.00 2.29e-16 GB AAA52281 "islet amyloid polypeptide [Homo sapiens]" 100.00 89 100.00 100.00 1.75e-16 GB AAI11850 "IAPP protein, partial [synthetic construct]" 100.00 89 100.00 100.00 1.75e-16 REF NP_000406 "islet amyloid polypeptide precursor [Homo sapiens]" 100.00 89 100.00 100.00 1.75e-16 REF XP_001144800 "PREDICTED: islet amyloid polypeptide [Pan troglodytes]" 100.00 89 97.30 97.30 3.18e-15 REF XP_003265632 "PREDICTED: islet amyloid polypeptide [Nomascus leucogenys]" 100.00 89 97.30 97.30 3.18e-15 REF XP_003265633 "PREDICTED: islet amyloid polypeptide [Nomascus leucogenys]" 100.00 89 97.30 97.30 3.18e-15 REF XP_003828947 "PREDICTED: islet amyloid polypeptide [Pan paniscus]" 100.00 89 97.30 97.30 3.18e-15 SP P10997 "RecName: Full=Islet amyloid polypeptide; AltName: Full=Amylin; AltName: Full=Diabetes-associated peptide; Short=DAP; AltName: F" 100.00 89 100.00 100.00 1.75e-16 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $entity Human 9606 Eukaryota Metazoa Homo sapiens 'Our recombinant peptide differs from human amylin by not having an amidated C-terminus' 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 _Details $entity 'recombinant technology' . Escherichia coli . 'purchased from rPeptide' ; Recombinant 15N-labeled amylin was purchased from rPeptide: http://www.rpeptide.com We don't have the details of the expression system. ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_2 _Saveframe_category sample _Sample_type solution _Details ; 0.5 mg unlabled amylin (from rPeptide lot 70507 AM) was dissolved in 0.25 ml of 100 mM SDS-d25, containing 60 mM d4-acetic acid in 99.96% D2O. Final protein concentration was 0.5 mM, sample pD 4.2, all experiments done at 37 oC. This sample was used for NOESY experiments in D2O. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity 0.5 mM '[U-100% 15N]' 'sodium dodecyl sulfate' 100 mM '[U-99% 2H]' 'acetic acid' 60 mM '[U-99% 2H]' stop_ save_ save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; 0.5 mg 15N-amylin (from rPeptide, lot 718071NAM)was dissolved in 100 mM d25-SDS, 60 mM acetic acid, 90% H2O/ 10% D2O. The final peptide concentration was 0.5 mM, pH 4.6. All experiments were done at 37 C. This sample was used for all NMR assignment data and for collecting structure data. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity 0.5 mM '[U-99% 15N]' SDS 100 mM [U-2H] 'acetic acid' 60 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.851 loop_ _Vendor _Address _Electronic_address Brunger . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_1H-15N_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNHB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHB' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_3D_TROSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY' _Sample_label $sample_1 save_ save_3D_TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TOCSY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 60 . mM pH 4.6 . pH pressure 1.0 . atm temperature 310 . K stop_ save_ save_sample_conditions_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 60 . mM pH* 4.2 . pH temperature 310 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D 1H-15N NOESY' '3D HNCA' '3D HNHB' '2D 1H-1H NOESY' '3D TROSY' '3D TOCSY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name alpha-helix _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 1 LYS HA H 4.105 0.05 1 2 2 2 CYS H H 8.735 0.05 1 3 2 2 CYS HA H 4.815 0.05 1 4 2 2 CYS HB2 H 3.215 0.05 2 5 2 2 CYS HB3 H 3.155 0.05 2 6 2 2 CYS N N 122.02 0.3 1 7 3 3 ASN H H 8.635 0.05 1 8 3 3 ASN HA H 4.795 0.05 1 9 3 3 ASN HB2 H 2.835 0.05 2 10 3 3 ASN HB3 H 2.985 0.05 2 11 3 3 ASN HD21 H 7.635 0.05 2 12 3 3 ASN HD22 H 6.925 0.05 2 13 3 3 ASN N N 119.65 0.3 1 14 3 3 ASN ND2 N 113.04 0.3 1 15 4 4 THR H H 7.432 0.05 1 16 4 4 THR HA H 4.695 0.05 1 17 4 4 THR HG2 H 1.295 0.05 1 18 4 4 THR N N 107.81 0.3 1 19 5 5 ALA H H 8.745 0.05 1 20 5 5 ALA HA H 4.145 0.05 1 21 5 5 ALA HB H 1.535 0.05 1 22 5 5 ALA N N 123.22 0.3 1 23 6 6 THR H H 7.991 0.05 1 24 6 6 THR HA H 4.225 0.05 1 25 6 6 THR HG2 H 1.255 0.05 . 26 6 6 THR N N 110.78 0.3 1 27 7 7 CYS H H 7.805 0.05 1 28 7 7 CYS HA H 4.465 0.05 1 29 7 7 CYS HB2 H 3.175 0.05 1 30 7 7 CYS HB3 H 3.445 0.05 1 31 7 7 CYS N N 120.81 0.3 1 32 8 8 ALA H H 8.085 0.05 1 33 8 8 ALA HA H 4.045 0.05 1 34 8 8 ALA HB H 1.485 0.05 1 35 8 8 ALA N N 123.57 0.3 1 36 9 9 THR H H 8.39 0.05 1 37 9 9 THR HA H 3.893 0.05 1 38 9 9 THR HB H 4.206 0.05 1 39 9 9 THR HG2 H 1.335 0.05 1 40 9 9 THR N N 109.64 0.3 1 41 10 10 GLN H H 7.715 0.05 1 42 10 10 GLN HA H 4.125 0.05 1 43 10 10 GLN HB2 H 2.055 0.05 2 44 10 10 GLN HB3 H 2.195 0.05 2 45 10 10 GLN HE21 H 7.405 0.05 2 46 10 10 GLN HE22 H 6.755 0.05 2 47 10 10 GLN HG2 H 2.405 0.05 2 48 10 10 GLN HG3 H 2.515 0.05 2 49 10 10 GLN N N 120.96 0.3 1 50 10 10 GLN NE2 N 111.96 0.3 1 51 11 11 ARG H H 7.918 0.05 1 52 11 11 ARG HA H 4.205 0.05 1 53 11 11 ARG HB2 H 2.017 0.05 2 54 11 11 ARG HB3 H 2.105 0.05 2 55 11 11 ARG HD2 H 3.245 0.05 2 56 11 11 ARG HE H 7.125 0.05 1 57 11 11 ARG N N 119.55 0.3 1 58 11 11 ARG NE N 120.54 0.3 1 59 12 12 LEU H H 8.145 0.05 1 60 12 12 LEU HA H 4.115 0.05 1 61 12 12 LEU HB2 H 1.755 0.05 1 62 12 12 LEU HB3 H 1.875 0.05 1 63 12 12 LEU HD1 H 0.945 0.05 2 64 12 12 LEU N N 119.97 0.3 1 65 13 13 ALA H H 8.435 0.05 1 66 13 13 ALA HA H 3.955 0.05 1 67 13 13 ALA HB H 1.548 0.05 1 68 13 13 ALA N N 120.96 0.3 1 69 14 14 ASN H H 8.095 0.05 1 70 14 14 ASN HA H 4.425 0.05 1 71 14 14 ASN HB2 H 2.895 0.05 1 72 14 14 ASN HB3 H 2.975 0.05 1 73 14 14 ASN HD21 H 7.385 0.05 2 74 14 14 ASN HD22 H 6.755 0.05 2 75 14 14 ASN N N 114.80 0.3 1 76 14 14 ASN ND2 N 111.63 0.3 1 77 15 15 PHE H H 8.095 0.05 1 78 15 15 PHE HA H 4.455 0.05 1 79 15 15 PHE HB2 H 3.335 0.05 1 80 15 15 PHE HB3 H 2.595 0.05 1 81 15 15 PHE N N 120.67 0.3 1 82 16 16 LEU H H 8.385 0.05 1 83 16 16 LEU HA H 3.955 0.05 1 84 16 16 LEU HB2 H 1.995 0.05 2 85 16 16 LEU HD1 H 0.945 0.05 2 86 16 16 LEU N N 119.62 0.3 1 87 17 17 VAL H H 8.058 0.05 1 88 17 17 VAL HA H 3.875 0.05 1 89 17 17 VAL HB H 2.115 0.05 1 90 17 17 VAL HG1 H 0.985 0.05 2 91 17 17 VAL HG2 H 0.825 0.05 2 92 17 17 VAL N N 116.51 0.3 1 93 18 18 HIS H H 7.777 0.05 1 94 18 18 HIS HA H 4.615 0.05 1 95 18 18 HIS HB2 H 3.285 0.05 1 96 18 18 HIS HB3 H 3.405 0.05 1 97 18 18 HIS N N 116.79 0.3 1 98 19 19 SER H H 7.87 0.05 1 99 19 19 SER HA H 4.345 0.05 1 100 19 19 SER HB2 H 3.685 0.05 2 101 19 19 SER N N 115.59 0.3 1 102 20 20 SER H H 8.092 0.05 1 103 20 20 SER HA H 4.225 0.05 1 104 20 20 SER HB2 H 3.893 0.05 . 105 20 20 SER N N 117.00 0.3 1 106 21 21 ASN H H 8.123 0.05 1 107 21 21 ASN HA H 4.615 0.05 1 108 21 21 ASN HB2 H 2.665 0.05 2 109 21 21 ASN HD21 H 7.385 0.05 2 110 21 21 ASN HD22 H 6.785 0.05 2 111 21 21 ASN N N 119.55 0.3 1 112 21 21 ASN ND2 N 112.61 0.3 1 113 22 22 ASN H H 8.177 0.05 1 114 22 22 ASN HA H 4.775 0.05 1 115 22 22 ASN HB2 H 2.785 0.05 2 116 22 22 ASN HB3 H 2.625 0.05 2 117 22 22 ASN HD21 H 7.385 0.05 2 118 22 22 ASN HD22 H 6.785 0.05 2 119 22 22 ASN N N 117.85 0.3 1 120 22 22 ASN ND2 N 112.61 0.3 1 121 23 23 PHE H H 8.16 0.05 1 122 23 23 PHE HA H 4.465 0.05 1 123 23 23 PHE HB2 H 3.135 0.05 2 124 23 23 PHE HD1 H 7.245 0.05 4 125 23 23 PHE HD2 H 7.555 0.05 4 126 23 23 PHE N N 119.97 0.3 1 127 24 24 GLY H H 8.459 0.05 1 128 24 24 GLY HA2 H 3.725 0.05 1 129 24 24 GLY HA3 H 4.035 0.05 1 130 24 24 GLY N N 107.81 0.3 1 131 25 25 ALA H H 7.894 0.05 1 132 25 25 ALA HA H 4.225 0.05 1 133 25 25 ALA HB H 1.455 0.05 1 134 25 25 ALA N N 123.71 0.3 1 135 26 26 ILE H H 7.845 0.05 1 136 26 26 ILE HA H 3.915 0.05 1 137 26 26 ILE HB H 1.995 0.05 1 138 26 26 ILE HG12 H 1.455 0.05 2 139 26 26 ILE HG13 H 1.255 0.05 2 140 26 26 ILE HG2 H 0.905 0.05 1 141 26 26 ILE N N 118.76 0.3 1 142 27 27 LEU H H 7.975 0.05 1 143 27 27 LEU HA H 4.145 0.05 1 144 27 27 LEU HB2 H 1.725 0.05 1 145 27 27 LEU HB3 H 1.625 0.05 1 146 27 27 LEU HD1 H 0.885 0.05 2 147 27 27 LEU N N 119.61 0.3 1 148 28 28 SER H H 8.004 0.05 1 149 28 28 SER HA H 4.386 0.05 1 150 28 28 SER HB2 H 3.995 0.05 2 151 28 28 SER HB3 H 3.935 0.05 2 152 28 28 SER N N 113.32 0.3 1 153 29 29 SER H H 7.85 0.05 1 154 29 29 SER HA H 4.58 0.05 1 155 29 29 SER HB2 H 4.035 0.05 2 156 29 29 SER HB3 H 4.305 0.05 2 157 29 29 SER N N 116.36 0.3 1 158 30 30 THR H H 7.704 0.05 1 159 30 30 THR HA H 4.505 0.05 1 160 30 30 THR HB H 4.345 0.05 1 161 30 30 THR HG2 H 1.255 0.05 1 162 30 30 THR N N 113.67 0.3 1 163 31 31 ASN H H 8.385 0.05 1 164 31 31 ASN HA H 4.835 0.05 1 165 31 31 ASN HB2 H 2.925 0.05 2 166 31 31 ASN HB3 H 2.795 0.05 2 167 31 31 ASN HD21 H 7.515 0.05 2 168 31 31 ASN HD22 H 6.825 0.05 2 169 31 31 ASN N N 119.68 0.3 1 170 31 31 ASN ND2 N 113.04 0.3 1 171 32 32 VAL H H 7.965 0.05 1 172 32 32 VAL HA H 4.035 0.05 1 173 32 32 VAL HB H 1.705 0.05 1 174 32 32 VAL HG1 H 0.985 0.05 2 175 32 32 VAL N N 119.62 0.3 1 176 33 33 GLY H H 8.346 0.05 1 177 33 33 GLY HA2 H 4.075 0.05 2 178 33 33 GLY HA3 H 3.955 0.05 2 179 33 33 GLY N N 111.06 0.3 1 180 34 34 SER H H 8.014 0.05 1 181 34 34 SER HA H 4.425 0.05 1 182 34 34 SER HB2 H 3.905 0.05 2 183 34 34 SER N N 114.95 0.3 1 184 35 35 ASN H H 8.231 0.05 1 185 35 35 ASN HA H 4.775 0.05 1 186 35 35 ASN HB2 H 2.786 0.05 2 187 35 35 ASN HD21 H 7.445 0.05 2 188 35 35 ASN HD22 H 6.825 0.05 2 189 35 35 ASN N N 119.90 0.3 1 190 35 35 ASN ND2 N 112.61 0.3 1 191 36 36 THR H H 7.924 0.05 1 192 36 36 THR HA H 4.265 0.05 1 193 36 36 THR HB H 4.075 0.05 1 194 36 36 THR HG2 H 1.095 0.05 1 195 36 36 THR N N 113.89 0.3 1 196 37 37 TYR H H 7.905 0.05 1 197 37 37 TYR HA H 4.585 0.05 1 198 37 37 TYR HB2 H 2.895 0.05 1 199 37 37 TYR HB3 H 3.135 0.05 1 200 37 37 TYR HD1 H 7.085 0.05 1 201 37 37 TYR HD2 H 7.085 0.05 1 202 37 37 TYR HE1 H 6.805 0.05 1 203 37 37 TYR HE2 H 6.805 0.05 1 204 37 37 TYR N N 123.15 0.3 1 stop_ save_