data_5782 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H chemical shift assignment for the truncated form of the human beta2-microglobulin lacking of the first 3 residues ; _BMRB_accession_number 5782 _BMRB_flat_file_name bmr5782.str _Entry_type original _Submission_date 2003-04-24 _Accession_date 2003-04-24 _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 Viglino Paolo . . 2 Corazza Alessandra . . 3 Pettirossi Fabio . . 4 Verdone Giuliana . . 5 Esposito Gennaro . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 618 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-02-12 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 5169 'beta2-microglobulin with the first 3 residues' 5783 'DN3 beta2-microglobulin (R3A mutant and with the first 3 residues)' 5784 'DN3 beta2-microglobulin (H31Y mutant and with the first 3 residues)' stop_ _Original_release_date 2003-04-24 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Properties of some variants of human beta2-microglobulin and amyloidogenesis ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 14660575 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Corazza Alessandra . . 2 Pettirossi Fabio . . 3 Viglino Paolo . . 4 Verdone Giuliana . . 5 Garcia Julian . . 6 Dumy Pascal . . 7 Giorgetti Sofia . . 8 Mangione Palma . . 9 Andreola Alessia . . 10 Stoppini Monica . . 11 Bellotti Vittorio . . 12 Esposito Gennaro . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _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 amyloidosis beta2-microglobulin stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Verdone G, Corazza A, Viglino P, Pettirossi F, Giorgetti S, Mangione P, Andreola A, Stoppini M, Bellotti V, Esposito G. Protein Sci 2002 11(3):487-99 The solution structure of human beta2-microglobulin reveals the prodromes of its amyloid transition. ; _Citation_title ; The solution structure of human beta2-microglobulin reveals the prodromes of its amyloid transition. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11847272 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Verdone Giuliana . . 2 Corazza Alessandra . . 3 Viglino Paolo . . 4 Pettirossi Fabio . . 5 Giorgetti Sofia . . 6 Mangione Palma . . 7 Andreola Alessia . . 8 Stoppini Monica . . 9 Bellotti Vittorio . . 10 Esposito Gennaro . . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_name_full 'Protein science : a publication of the Protein Society' _Journal_volume 11 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 487 _Page_last 499 _Year 2002 _Details ; The solution structure of human beta2-microglobulin (beta2-m), the nonpolymorphic component of class I major histocompatibility complex (MHC-I), was determined by (1)H NMR spectroscopy and restrained modeling calculations. Compared to previous structural data obtained from the NMR secondary structure of the isolated protein and the crystal structure of MHC-I, in which the protein is associated to the heavy-chain component, several differences are observed. The most important rearrangements were observed for (1) strands V and VI (loss of the C-terminal and N-terminal end, respectively), (2) interstrand loop V-VI, and (3) strand I, including the N-terminal segment (displacement outward of the molecular core). These modifications can be considered as the prodromes of the amyloid transition. Solvation of the protected regions in MHC-I decreases the tertiary packing by breaking the contiguity of the surface hydrophobic patches at the interface with heavy chain and the nearby region at the surface charge cluster of the C-terminal segment. As a result, the molecule is placed in a state in which even minor charge and solvation changes in response to pH or ionic-strength variations can easily compromise the hydrophobic/hydrophilic balance and trigger the transition into a partially unfolded intermediate that starts with unpairing of strand I and leads to polymerization and precipitation into fibrils or amorphous aggregates. The same mechanism accounts for the partial unfolding and fiber formation subsequent to Cu(2+) binding, which is shown to occur primarily at His 31 and involve partially also His 13, the next available His residue along the partial unfolding pathway. ; save_ save_ref_2 _Saveframe_category citation _Citation_full ; Esposito G, Michelutti R, Verdone G, Viglino P, Hernandez H, Robinson CV, Amoresano A, Dal Piaz F, Monti M, Pucci P, Mangione P, Stoppini M, Merlini G, Ferri G, Bellotti V. Protein Sci 2000 9(5):831-45 Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation. ; _Citation_title ; Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10850793 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Esposito G . . 2 Michelutti R . . 3 Verdone G . . 4 Viglino P . . 5 Hernandez H . . 6 Robinson C.V. V. . 7 Amoresano A . . 8 'Dal Piaz' F . . 9 Monti M . . 10 Pucci P . . 11 Mangione P . . 12 Stoppini M . . 13 Merlini G . . 14 Ferri G . . 15 Bellotti V . . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_name_full 'Protein science : a publication of the Protein Society' _Journal_volume 9 _Journal_issue 5 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 831 _Page_last 845 _Year 2000 _Details ; The solution structure and stability of N-terminally truncated beta2-microglobulin (deltaN6beta2-m), the major modification in ex vivo fibrils, have been investigated by a variety of biophysical techniques. The results show that deltaN6beta2-m has a free energy of stabilization that is reduced by 2.5 kcal/mol compared to the intact protein. Hydrogen exchange of a mixture of the truncated and full-length proteins at microM concentrations at pH 6.5 monitored by electrospray mass spectrometry reveals that deltaN6beta2-m is significantly less protected than its wild-type counterpart. Analysis of deltaN6beta2-m by NMR shows that this loss of protection occurs in beta strands I, III, and part of II. At mM concentration gel filtration analysis shows that deltaN6beta2-m forms a series of oligomers, including trimers and tetramers, and NMR analysis indicates that strand V is involved in intermolecular interactions that stabilize this association. The truncated species of beta2-microglobulin was found to have a higher tendency to self-associate than the intact molecule, and unlike wild-type protein, is able to form amyloid fibrils at physiological pH. Limited proteolysis experiments and analysis by mass spectrometry support the conformational modifications identified by NMR and suggest that deltaN6beta2-m could be a key intermediate of a proteolytic pathway of beta2-microglobulin. Overall, the data suggest that removal of the six residues from the N-terminus of beta2-microglobulin has a major effect on the stability of the overall fold. Part of the tertiary structure is preserved substantially by the disulfide bridge between Cys25 and Cys80, but the pairing between beta-strands far removed from this constrain is greatly perturbed. ; save_ ################################## # Molecular system description # ################################## save_system_DN3beta2-m _Saveframe_category molecular_system _Mol_system_name DN3beta2-microglobulin _Abbreviation_common DN3beta2-m _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label DN3beta2-microglobulin $D3Nbeta2-m 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_D3Nbeta2-m _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common beta2-microglobulin _Name_variant D3Nbeta2-microglobulin _Abbreviation_common D3Nbeta2-m _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 97 _Mol_residue_sequence ; MTPKIQVYSRHPAENGKSNF LNCYVSGFHPSDIEVDLLKN GERIEKVEHSDLSFSKDWSF YLLYYTEFTPTEKDEYACRV NHVTLSQPKIVKWDRDM ; loop_ _Residue_seq_code _Residue_label 1 MET 2 THR 3 PRO 4 LYS 5 ILE 6 GLN 7 VAL 8 TYR 9 SER 10 ARG 11 HIS 12 PRO 13 ALA 14 GLU 15 ASN 16 GLY 17 LYS 18 SER 19 ASN 20 PHE 21 LEU 22 ASN 23 CYS 24 TYR 25 VAL 26 SER 27 GLY 28 PHE 29 HIS 30 PRO 31 SER 32 ASP 33 ILE 34 GLU 35 VAL 36 ASP 37 LEU 38 LEU 39 LYS 40 ASN 41 GLY 42 GLU 43 ARG 44 ILE 45 GLU 46 LYS 47 VAL 48 GLU 49 HIS 50 SER 51 ASP 52 LEU 53 SER 54 PHE 55 SER 56 LYS 57 ASP 58 TRP 59 SER 60 PHE 61 TYR 62 LEU 63 LEU 64 TYR 65 TYR 66 THR 67 GLU 68 PHE 69 THR 70 PRO 71 THR 72 GLU 73 LYS 74 ASP 75 GLU 76 TYR 77 ALA 78 CYS 79 ARG 80 VAL 81 ASN 82 HIS 83 VAL 84 THR 85 LEU 86 SER 87 GLN 88 PRO 89 LYS 90 ILE 91 VAL 92 LYS 93 TRP 94 ASP 95 ARG 96 ASP 97 MET stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $D3Nbeta2-m 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 $D3Nbeta2-m 'recombinant technology' 'E. coli' Escherichia coli . . 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 $D3Nbeta2-m 0.86 mM . 'sodium phosphate' 70 mM . 'sodium chloride' 100 mM . H2O 100 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $D3Nbeta2-m 0.7 mM . 'sodium phosphate' 70 mM . 'sodium chloride' 100 mM . D2O 95 % . H2O 5 % . stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 2000 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-1H_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H TOCSY' _Sample_label . save_ save_1H-1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _Sample_label . save_ save_1H-1H_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H DQF-COSY' _Sample_label . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.1 na temperature 310 0.1 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 Dioxane H 1 'methylene protons' ppm 3.53 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details 'Principal conformational species (75%).' loop_ _Experiment_label '1H-1H TOCSY' '1H-1H NOESY' '1H-1H DQF-COSY' stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name DN3beta2-microglobulin _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 MET HA H 3.977 0.02 1 2 . 1 MET HB2 H 2.157 0.02 2 3 . 1 MET HB3 H 2.053 0.02 2 4 . 1 MET HG2 H 2.745 0.02 2 5 . 1 MET HG3 H 2.524 0.02 2 6 . 2 THR HA H 5.007 0.02 1 7 . 2 THR HB H 4.135 0.02 1 8 . 2 THR HG2 H 1.348 0.02 1 9 . 3 PRO HA H 4.393 0.02 1 10 . 3 PRO HB2 H 1.507 0.02 1 11 . 3 PRO HD2 H 3.588 0.02 2 12 . 3 PRO HD3 H 3.448 0.02 2 13 . 3 PRO HG2 H 1.679 0.02 2 14 . 3 PRO HG3 H 1.205 0.02 2 15 . 4 LYS H H 9.168 0.02 1 16 . 4 LYS HA H 4.516 0.02 1 17 . 4 LYS HB2 H 1.785 0.02 2 18 . 4 LYS HB3 H 1.523 0.02 2 19 . 4 LYS HG2 H 1.635 0.02 2 20 . 4 LYS HG3 H 1.444 0.02 2 21 . 5 ILE H H 8.446 0.02 1 22 . 5 ILE HA H 4.886 0.02 1 23 . 5 ILE HB H 1.695 0.02 1 24 . 5 ILE HD1 H 0.655 0.02 1 25 . 5 ILE HG12 H 1.426 0.02 1 26 . 5 ILE HG2 H 0.783 0.02 1 27 . 6 GLN H H 9.144 0.02 1 28 . 6 GLN HA H 4.946 0.02 1 29 . 6 GLN HB2 H 2.348 0.02 2 30 . 6 GLN HB3 H 2.189 0.02 2 31 . 6 GLN HE21 H 7.492 0.02 2 32 . 6 GLN HE22 H 6.818 0.02 2 33 . 6 GLN HG2 H 2.414 0.02 1 34 . 7 VAL H H 9.006 0.02 1 35 . 7 VAL HA H 5.360 0.02 1 36 . 7 VAL HB H 2.043 0.02 1 37 . 7 VAL HG1 H 0.983 0.02 2 38 . 7 VAL HG2 H 0.925 0.02 2 39 . 8 TYR H H 8.468 0.02 1 40 . 8 TYR HA H 5.320 0.02 1 41 . 8 TYR HB2 H 3.413 0.02 2 42 . 8 TYR HB3 H 3.183 0.02 2 43 . 8 TYR HD1 H 6.818 0.02 1 44 . 8 TYR HE1 H 6.566 0.02 1 45 . 9 SER H H 9.327 0.02 1 46 . 9 SER HA H 5.299 0.02 1 47 . 9 SER HB2 H 4.426 0.02 2 48 . 9 SER HB3 H 3.675 0.02 2 49 . 10 ARG H H 8.855 0.02 1 50 . 10 ARG HA H 3.940 0.02 1 51 . 10 ARG HB2 H 1.941 0.02 2 52 . 10 ARG HB3 H 1.754 0.02 2 53 . 10 ARG HD2 H 3.065 0.02 2 54 . 10 ARG HD3 H 2.797 0.02 2 55 . 10 ARG HG2 H 1.432 0.02 1 56 . 11 HIS H H 8.326 0.02 1 57 . 11 HIS HA H 5.344 0.02 1 58 . 11 HIS HB2 H 3.262 0.02 2 59 . 11 HIS HB3 H 2.921 0.02 2 60 . 11 HIS HD2 H 7.090 0.02 1 61 . 11 HIS HE1 H 7.879 0.02 1 62 . 12 PRO HA H 4.534 0.02 1 63 . 12 PRO HB2 H 2.438 0.02 2 64 . 12 PRO HB3 H 1.954 0.02 2 65 . 12 PRO HD2 H 4.064 0.02 2 66 . 12 PRO HD3 H 3.797 0.02 2 67 . 12 PRO HG2 H 2.232 0.02 2 68 . 12 PRO HG3 H 2.079 0.02 2 69 . 13 ALA H H 8.979 0.02 1 70 . 13 ALA HA H 4.113 0.02 1 71 . 13 ALA HB H 1.699 0.02 1 72 . 14 GLU H H 8.845 0.02 1 73 . 14 GLU HA H 4.414 0.02 1 74 . 14 GLU HB2 H 1.871 0.02 1 75 . 14 GLU HG2 H 2.167 0.02 1 76 . 15 ASN HA H 4.505 0.02 1 77 . 15 ASN HB2 H 2.787 0.02 2 78 . 15 ASN HB3 H 2.697 0.02 2 79 . 15 ASN HD21 H 7.539 0.02 2 80 . 15 ASN HD22 H 7.099 0.02 2 81 . 16 GLY H H 8.834 0.02 1 82 . 16 GLY HA2 H 4.198 0.02 2 83 . 16 GLY HA3 H 3.536 0.02 2 84 . 17 LYS H H 7.834 0.02 1 85 . 17 LYS HA H 4.674 0.02 1 86 . 17 LYS HB2 H 1.835 0.02 2 87 . 17 LYS HB3 H 1.762 0.02 2 88 . 17 LYS HD2 H 1.655 0.02 2 89 . 17 LYS HD3 H 1.598 0.02 2 90 . 17 LYS HE2 H 2.954 0.02 1 91 . 17 LYS HG2 H 1.386 0.02 2 92 . 17 LYS HG3 H 1.311 0.02 2 93 . 18 SER H H 8.338 0.02 1 94 . 18 SER HA H 4.268 0.02 1 95 . 18 SER HB2 H 3.748 0.02 1 96 . 19 ASN H H 8.887 0.02 1 97 . 19 ASN HA H 4.878 0.02 1 98 . 19 ASN HB2 H 2.765 0.02 2 99 . 19 ASN HB3 H 2.555 0.02 2 100 . 19 ASN HD21 H 7.765 0.02 2 101 . 19 ASN HD22 H 7.445 0.02 2 102 . 20 PHE H H 10.321 0.02 1 103 . 20 PHE HA H 5.439 0.02 1 104 . 20 PHE HB2 H 2.683 0.02 2 105 . 20 PHE HB3 H 2.629 0.02 2 106 . 20 PHE HD1 H 7.017 0.02 1 107 . 20 PHE HE1 H 7.411 0.02 1 108 . 20 PHE HZ H 7.340 0.02 1 109 . 21 LEU H H 8.971 0.02 1 110 . 21 LEU HA H 3.699 0.02 1 111 . 21 LEU HB2 H 0.823 0.02 2 112 . 21 LEU HB3 H 0.811 0.02 2 113 . 21 LEU HD1 H 0.016 0.02 2 114 . 21 LEU HD2 H 0.565 0.02 2 115 . 21 LEU HG H 0.672 0.02 1 116 . 22 ASN H H 8.200 0.02 1 117 . 22 ASN HA H 5.388 0.02 1 118 . 22 ASN HB2 H 1.854 0.02 2 119 . 22 ASN HB3 H 1.470 0.02 2 120 . 22 ASN HD21 H 5.730 0.02 2 121 . 22 ASN HD22 H 5.560 0.02 2 122 . 23 CYS H H 9.630 0.02 1 123 . 23 CYS HA H 5.185 0.02 1 124 . 23 CYS HB2 H 3.282 0.02 2 125 . 23 CYS HB3 H 2.555 0.02 2 126 . 24 TYR H H 9.669 0.02 1 127 . 24 TYR HA H 5.425 0.02 1 128 . 24 TYR HB2 H 3.187 0.02 1 129 . 24 TYR HD1 H 7.153 0.02 1 130 . 24 TYR HE1 H 6.577 0.02 1 131 . 25 VAL H H 8.803 0.02 1 132 . 25 VAL HA H 5.204 0.02 1 133 . 25 VAL HB H 1.914 0.02 1 134 . 25 VAL HG1 H 0.904 0.02 2 135 . 25 VAL HG2 H 0.793 0.02 2 136 . 26 SER H H 8.959 0.02 1 137 . 26 SER HA H 5.718 0.02 1 138 . 26 SER HB2 H 3.859 0.02 2 139 . 26 SER HB3 H 3.472 0.02 2 140 . 27 GLY H H 8.362 0.02 1 141 . 27 GLY HA2 H 4.112 0.02 2 142 . 27 GLY HA3 H 3.887 0.02 2 143 . 28 PHE H H 7.170 0.02 1 144 . 28 PHE HA H 4.971 0.02 1 145 . 28 PHE HB2 H 2.269 0.02 2 146 . 28 PHE HB3 H 1.962 0.02 2 147 . 28 PHE HD1 H 6.961 0.02 1 148 . 28 PHE HE1 H 7.248 0.02 1 149 . 28 PHE HZ H 6.861 0.02 1 150 . 29 HIS H H 8.262 0.02 1 151 . 29 HIS HA H 4.528 0.02 1 152 . 29 HIS HB2 H 3.314 0.02 2 153 . 29 HIS HB3 H 3.114 0.02 2 154 . 29 HIS HD2 H 7.074 0.02 1 155 . 29 HIS HE1 H 7.849 0.02 1 156 . 30 PRO HA H 3.962 0.02 1 157 . 30 PRO HB2 H 2.248 0.02 2 158 . 30 PRO HB3 H 2.013 0.02 2 159 . 30 PRO HD2 H 3.744 0.02 2 160 . 30 PRO HD3 H 3.644 0.02 2 161 . 30 PRO HG2 H 1.817 0.02 1 162 . 31 SER H H 8.262 0.02 1 163 . 31 SER HA H 3.621 0.02 1 164 . 31 SER HB2 H 3.314 0.02 2 165 . 31 SER HB3 H 1.895 0.02 2 166 . 32 ASP H H 7.211 0.02 1 167 . 32 ASP HA H 4.428 0.02 1 168 . 32 ASP HB2 H 2.414 0.02 2 169 . 32 ASP HB3 H 2.351 0.02 2 170 . 33 ILE H H 7.956 0.02 1 171 . 33 ILE HA H 4.512 0.02 1 172 . 33 ILE HB H 1.406 0.02 1 173 . 33 ILE HD1 H 0.444 0.02 1 174 . 33 ILE HG12 H 1.462 0.02 2 175 . 33 ILE HG13 H 0.694 0.02 2 176 . 33 ILE HG2 H 0.571 0.02 1 177 . 34 GLU H H 7.963 0.02 1 178 . 34 GLU HA H 4.588 0.02 1 179 . 34 GLU HB2 H 1.939 0.02 2 180 . 34 GLU HB3 H 1.785 0.02 2 181 . 34 GLU HG2 H 2.111 0.02 2 182 . 34 GLU HG3 H 2.077 0.02 2 183 . 35 VAL H H 7.929 0.02 1 184 . 35 VAL HA H 4.674 0.02 1 185 . 35 VAL HB H 0.450 0.02 1 186 . 35 VAL HG1 H 0.490 0.02 2 187 . 35 VAL HG2 H 0.249 0.02 2 188 . 36 ASP H H 8.866 0.02 1 189 . 36 ASP HA H 4.947 0.02 1 190 . 36 ASP HB2 H 2.404 0.02 2 191 . 36 ASP HB3 H 2.206 0.02 2 192 . 37 LEU H H 9.027 0.02 1 193 . 37 LEU HA H 5.013 0.02 1 194 . 37 LEU HB2 H 1.635 0.02 2 195 . 37 LEU HB3 H 1.239 0.02 2 196 . 37 LEU HD1 H 0.748 0.02 1 197 . 37 LEU HG H 1.597 0.02 1 198 . 38 LEU H H 8.969 0.02 1 199 . 38 LEU HA H 5.006 0.02 1 200 . 38 LEU HB2 H 1.577 0.02 2 201 . 38 LEU HB3 H 0.829 0.02 2 202 . 38 LEU HD1 H 0.602 0.02 2 203 . 38 LEU HD2 H 0.406 0.02 2 204 . 38 LEU HG H 1.207 0.02 1 205 . 39 LYS H H 8.845 0.02 1 206 . 39 LYS HA H 4.414 0.02 1 207 . 39 LYS HB2 H 1.752 0.02 2 208 . 39 LYS HB3 H 1.457 0.02 2 209 . 39 LYS HD2 H 1.774 0.02 2 210 . 39 LYS HD3 H 1.578 0.02 2 211 . 39 LYS HE2 H 2.845 0.02 1 212 . 39 LYS HG2 H 0.555 0.02 2 213 . 39 LYS HG3 H 0.831 0.02 2 214 . 40 ASN H H 9.731 0.02 1 215 . 40 ASN HA H 4.363 0.02 1 216 . 40 ASN HB2 H 2.859 0.02 2 217 . 40 ASN HB3 H 2.909 0.02 2 218 . 40 ASN HD21 H 7.980 0.02 2 219 . 40 ASN HD22 H 7.730 0.02 2 220 . 41 GLY H H 8.791 0.02 1 221 . 41 GLY HA2 H 4.198 0.02 2 222 . 41 GLY HA3 H 3.333 0.02 2 223 . 42 GLU H H 7.832 0.02 1 224 . 42 GLU HA H 4.582 0.02 1 225 . 42 GLU HB2 H 2.060 0.02 2 226 . 42 GLU HB3 H 1.963 0.02 2 227 . 42 GLU HG2 H 2.287 0.02 2 228 . 42 GLU HG3 H 2.177 0.02 2 229 . 43 ARG H H 8.651 0.02 1 230 . 43 ARG HA H 4.181 0.02 1 231 . 43 ARG HB2 H 1.639 0.02 1 232 . 43 ARG HD2 H 3.139 0.02 2 233 . 43 ARG HD3 H 3.083 0.02 2 234 . 43 ARG HG2 H 1.544 0.02 2 235 . 43 ARG HG3 H 1.345 0.02 2 236 . 44 ILE H H 8.793 0.02 1 237 . 44 ILE HA H 4.000 0.02 1 238 . 44 ILE HB H 1.547 0.02 1 239 . 44 ILE HD1 H 0.903 0.02 1 240 . 44 ILE HG12 H 1.702 0.02 2 241 . 44 ILE HG13 H 1.038 0.02 2 242 . 44 ILE HG2 H 0.983 0.02 1 243 . 45 GLU H H 8.491 0.02 1 244 . 45 GLU HA H 4.181 0.02 1 245 . 45 GLU HB2 H 2.109 0.02 2 246 . 45 GLU HB3 H 2.031 0.02 2 247 . 45 GLU HG2 H 2.374 0.02 2 248 . 45 GLU HG3 H 2.251 0.02 2 249 . 46 LYS H H 7.923 0.02 1 250 . 46 LYS HA H 4.512 0.02 1 251 . 46 LYS HB2 H 1.943 0.02 2 252 . 46 LYS HB3 H 1.785 0.02 2 253 . 46 LYS HE2 H 3.040 0.02 1 254 . 46 LYS HG2 H 1.445 0.02 2 255 . 46 LYS HG3 H 1.407 0.02 2 256 . 47 VAL H H 7.829 0.02 1 257 . 47 VAL HA H 4.398 0.02 1 258 . 47 VAL HB H 2.115 0.02 1 259 . 47 VAL HG1 H 1.099 0.02 2 260 . 47 VAL HG2 H 1.028 0.02 2 261 . 48 GLU H H 8.441 0.02 1 262 . 48 GLU HA H 4.492 0.02 1 263 . 48 GLU HB2 H 1.589 0.02 2 264 . 48 GLU HB3 H 0.755 0.02 2 265 . 48 GLU HG2 H 2.075 0.02 1 266 . 49 HIS H H 8.126 0.02 1 267 . 49 HIS HA H 5.494 0.02 1 268 . 49 HIS HB2 H 2.462 0.02 2 269 . 49 HIS HB3 H 1.985 0.02 2 270 . 49 HIS HD2 H 7.017 0.02 1 271 . 49 HIS HE1 H 8.503 0.02 1 272 . 50 SER H H 9.114 0.02 1 273 . 50 SER HA H 4.662 0.02 1 274 . 50 SER HB2 H 4.469 0.02 2 275 . 50 SER HB3 H 4.099 0.02 2 276 . 51 ASP HA H 4.808 0.02 1 277 . 51 ASP HB2 H 2.754 0.02 2 278 . 51 ASP HB3 H 2.579 0.02 2 279 . 52 LEU HA H 4.318 0.02 1 280 . 52 LEU HB2 H 1.809 0.02 1 281 . 52 LEU HD1 H 1.054 0.02 2 282 . 52 LEU HD2 H 0.871 0.02 2 283 . 52 LEU HG H 1.659 0.02 1 284 . 53 SER H H 8.033 0.02 1 285 . 53 SER HA H 4.767 0.02 1 286 . 53 SER HB2 H 3.421 0.02 2 287 . 53 SER HB3 H 2.741 0.02 2 288 . 54 PHE H H 8.158 0.02 1 289 . 54 PHE HA H 5.047 0.02 1 290 . 54 PHE HB2 H 2.680 0.02 1 291 . 54 PHE HD1 H 6.346 0.02 1 292 . 54 PHE HE1 H 7.004 0.02 1 293 . 54 PHE HZ H 7.099 0.02 1 294 . 55 SER H H 8.217 0.02 1 295 . 55 SER HA H 4.537 0.02 1 296 . 55 SER HB2 H 3.913 0.02 2 297 . 55 SER HB3 H 3.653 0.02 2 298 . 56 LYS HA H 3.828 0.02 1 299 . 56 LYS HB2 H 1.742 0.02 1 300 . 56 LYS HD2 H 1.646 0.02 1 301 . 56 LYS HE2 H 2.978 0.02 1 302 . 56 LYS HG2 H 1.397 0.02 1 303 . 57 ASP H H 7.693 0.02 1 304 . 57 ASP HA H 4.366 0.02 1 305 . 57 ASP HB2 H 2.278 0.02 1 306 . 58 TRP H H 7.285 0.02 1 307 . 58 TRP HA H 4.655 0.02 1 308 . 58 TRP HB2 H 3.039 0.02 2 309 . 58 TRP HB3 H 3.180 0.02 2 310 . 58 TRP HD1 H 6.875 0.02 1 311 . 58 TRP HE1 H 9.641 0.02 1 312 . 58 TRP HE3 H 6.968 0.02 1 313 . 58 TRP HH2 H 7.094 0.02 1 314 . 58 TRP HZ2 H 7.341 0.02 1 315 . 58 TRP HZ3 H 6.852 0.02 1 316 . 59 SER H H 7.601 0.02 1 317 . 59 SER HA H 3.878 0.02 1 318 . 59 SER HB2 H 3.776 0.02 2 319 . 59 SER HB3 H 3.725 0.02 2 320 . 60 PHE H H 7.708 0.02 1 321 . 60 PHE HA H 5.252 0.02 1 322 . 60 PHE HB2 H 2.488 0.02 2 323 . 60 PHE HB3 H 1.793 0.02 2 324 . 60 PHE HD1 H 7.396 0.02 1 325 . 60 PHE HE1 H 7.271 0.02 1 326 . 60 PHE HZ H 7.138 0.02 1 327 . 61 TYR H H 8.237 0.02 1 328 . 61 TYR HA H 5.552 0.02 1 329 . 61 TYR HB2 H 2.995 0.02 2 330 . 61 TYR HB3 H 2.817 0.02 2 331 . 61 TYR HD1 H 6.989 0.02 1 332 . 61 TYR HE1 H 6.649 0.02 1 333 . 62 LEU H H 9.093 0.02 1 334 . 62 LEU HA H 4.637 0.02 1 335 . 62 LEU HB2 H 1.969 0.02 2 336 . 62 LEU HB3 H 1.757 0.02 2 337 . 62 LEU HD1 H 1.007 0.02 2 338 . 62 LEU HD2 H 0.967 0.02 2 339 . 63 LEU H H 8.128 0.02 1 340 . 63 LEU HA H 5.480 0.02 1 341 . 63 LEU HB2 H 1.987 0.02 2 342 . 63 LEU HB3 H 1.573 0.02 2 343 . 63 LEU HD1 H 1.033 0.02 2 344 . 63 LEU HD2 H 0.840 0.02 2 345 . 64 TYR H H 9.137 0.02 1 346 . 64 TYR HA H 5.353 0.02 1 347 . 64 TYR HB2 H 3.044 0.02 2 348 . 64 TYR HB3 H 2.665 0.02 2 349 . 64 TYR HD1 H 6.993 0.02 1 350 . 64 TYR HE1 H 6.690 0.02 1 351 . 65 TYR H H 8.921 0.02 1 352 . 65 TYR HA H 5.981 0.02 1 353 . 65 TYR HB2 H 3.223 0.02 2 354 . 65 TYR HB3 H 2.658 0.02 2 355 . 65 TYR HD1 H 6.699 0.02 1 356 . 65 TYR HE1 H 6.547 0.02 1 357 . 66 THR H H 8.294 0.02 1 358 . 66 THR HA H 4.869 0.02 1 359 . 66 THR HB H 4.120 0.02 1 360 . 66 THR HG2 H 0.959 0.02 1 361 . 67 GLU H H 8.477 0.02 1 362 . 67 GLU HA H 4.329 0.02 1 363 . 67 GLU HB2 H 1.838 0.02 2 364 . 67 GLU HB3 H 1.697 0.02 2 365 . 67 GLU HG2 H 1.893 0.02 1 366 . 68 PHE H H 8.750 0.02 1 367 . 68 PHE HA H 4.845 0.02 1 368 . 68 PHE HB2 H 2.794 0.02 2 369 . 68 PHE HB3 H 2.704 0.02 2 370 . 68 PHE HD1 H 6.208 0.02 1 371 . 68 PHE HZ H 5.744 0.02 1 372 . 69 THR H H 8.194 0.02 1 373 . 69 THR HA H 4.472 0.02 1 374 . 69 THR HB H 3.881 0.02 1 375 . 69 THR HG2 H 0.865 0.02 1 376 . 70 PRO HA H 4.579 0.02 1 377 . 70 PRO HB2 H 2.389 0.02 2 378 . 70 PRO HB3 H 1.988 0.02 2 379 . 70 PRO HD2 H 3.977 0.02 2 380 . 70 PRO HD3 H 2.204 0.02 2 381 . 70 PRO HG2 H 1.413 0.02 1 382 . 71 THR H H 8.060 0.02 1 383 . 71 THR HA H 4.690 0.02 1 384 . 71 THR HB H 4.538 0.02 1 385 . 71 THR HG2 H 1.325 0.02 1 386 . 72 GLU H H 9.087 0.02 1 387 . 72 GLU HA H 4.224 0.02 1 388 . 72 GLU HB2 H 2.289 0.02 2 389 . 72 GLU HB3 H 2.079 0.02 2 390 . 72 GLU HG2 H 2.327 0.02 1 391 . 73 LYS H H 7.799 0.02 1 392 . 73 LYS HA H 4.467 0.02 1 393 . 73 LYS HB2 H 1.873 0.02 2 394 . 73 LYS HB3 H 1.786 0.02 2 395 . 73 LYS HD2 H 1.693 0.02 1 396 . 73 LYS HE2 H 3.000 0.02 1 397 . 73 LYS HG2 H 1.400 0.02 1 398 . 74 ASP H H 7.121 0.02 1 399 . 74 ASP HA H 5.130 0.02 1 400 . 74 ASP HB2 H 2.818 0.02 2 401 . 74 ASP HB3 H 2.165 0.02 2 402 . 75 GLU H H 8.604 0.02 1 403 . 75 GLU HA H 4.813 0.02 1 404 . 75 GLU HB2 H 2.109 0.02 2 405 . 75 GLU HB3 H 2.016 0.02 2 406 . 75 GLU HG2 H 2.378 0.02 1 407 . 76 TYR H H 9.458 0.02 1 408 . 76 TYR HA H 5.615 0.02 1 409 . 76 TYR HB2 H 2.731 0.02 2 410 . 76 TYR HB3 H 2.834 0.02 2 411 . 76 TYR HD1 H 7.102 0.02 1 412 . 76 TYR HE1 H 6.897 0.02 1 413 . 77 ALA H H 8.790 0.02 1 414 . 77 ALA HA H 5.060 0.02 1 415 . 77 ALA HB H 1.211 0.02 1 416 . 78 CYS H H 9.109 0.02 1 417 . 78 CYS HA H 5.123 0.02 1 418 . 78 CYS HB2 H 3.052 0.02 2 419 . 78 CYS HB3 H 2.630 0.02 2 420 . 79 ARG H H 9.400 0.02 1 421 . 79 ARG HA H 5.390 0.02 1 422 . 79 ARG HB2 H 1.798 0.02 2 423 . 79 ARG HB3 H 1.186 0.02 2 424 . 79 ARG HD2 H 3.081 0.02 2 425 . 79 ARG HD3 H 2.925 0.02 2 426 . 79 ARG HE H 7.088 0.02 1 427 . 79 ARG HG2 H 1.328 0.02 2 428 . 79 ARG HG3 H 1.235 0.02 2 429 . 80 VAL H H 9.044 0.02 1 430 . 80 VAL HA H 4.918 0.02 1 431 . 80 VAL HB H 1.683 0.02 1 432 . 80 VAL HG1 H 0.814 0.02 2 433 . 80 VAL HG2 H 0.608 0.02 2 434 . 81 ASN H H 9.019 0.02 1 435 . 81 ASN HA H 5.180 0.02 1 436 . 81 ASN HB2 H 2.826 0.02 2 437 . 81 ASN HB3 H 2.385 0.02 2 438 . 81 ASN HD21 H 7.430 0.02 2 439 . 81 ASN HD22 H 6.649 0.02 2 440 . 82 HIS H H 7.756 0.02 1 441 . 82 HIS HA H 4.584 0.02 1 442 . 82 HIS HB2 H 2.889 0.02 2 443 . 82 HIS HB3 H 2.451 0.02 2 444 . 82 HIS HD2 H 7.512 0.02 1 445 . 82 HIS HE1 H 8.157 0.02 1 446 . 83 VAL H H 7.920 0.02 1 447 . 83 VAL HA H 4.020 0.02 1 448 . 83 VAL HB H 2.017 0.02 1 449 . 83 VAL HG1 H 0.888 0.02 2 450 . 83 VAL HG2 H 0.691 0.02 2 451 . 84 THR H H 7.835 0.02 1 452 . 84 THR HA H 4.257 0.02 1 453 . 84 THR HB H 4.535 0.02 1 454 . 84 THR HG2 H 1.596 0.02 1 455 . 85 LEU H H 8.025 0.02 1 456 . 85 LEU HA H 4.752 0.02 1 457 . 85 LEU HB2 H 2.068 0.02 2 458 . 85 LEU HB3 H 1.851 0.02 2 459 . 85 LEU HD1 H 1.017 0.02 1 460 . 85 LEU HG H 1.759 0.02 1 461 . 86 SER HA H 4.270 0.02 1 462 . 86 SER HB2 H 4.004 0.02 2 463 . 86 SER HB3 H 3.969 0.02 2 464 . 87 GLN H H 7.543 0.02 1 465 . 87 GLN HA H 4.763 0.02 1 466 . 87 GLN HB2 H 2.319 0.02 2 467 . 87 GLN HB3 H 2.175 0.02 2 468 . 87 GLN HG2 H 2.269 0.02 1 469 . 87 GLN HE22 H 6.818 0.02 2 470 . 87 GLN HE21 H 7.492 0.02 2 471 . 88 PRO HA H 4.475 0.02 1 472 . 88 PRO HB2 H 1.859 0.02 2 473 . 88 PRO HB3 H 1.512 0.02 2 474 . 88 PRO HD2 H 3.745 0.02 2 475 . 88 PRO HD3 H 3.543 0.02 2 476 . 88 PRO HG2 H 2.003 0.02 2 477 . 88 PRO HG3 H 1.783 0.02 2 478 . 89 LYS H H 8.706 0.02 1 479 . 89 LYS HA H 4.556 0.02 1 480 . 89 LYS HB2 H 1.746 0.02 2 481 . 89 LYS HB3 H 1.663 0.02 2 482 . 89 LYS HG2 H 1.441 0.02 2 483 . 89 LYS HG3 H 1.366 0.02 2 484 . 90 ILE H H 8.482 0.02 1 485 . 90 ILE HA H 4.819 0.02 1 486 . 90 ILE HB H 1.705 0.02 1 487 . 90 ILE HD1 H 0.755 0.02 1 488 . 90 ILE HG12 H 1.428 0.02 1 489 . 90 ILE HG2 H 0.632 0.02 1 490 . 91 VAL H H 9.034 0.02 1 491 . 91 VAL HA H 4.336 0.02 1 492 . 91 VAL HB H 1.894 0.02 1 493 . 91 VAL HG1 H 1.049 0.02 2 494 . 91 VAL HG2 H 0.937 0.02 2 495 . 92 LYS H H 8.763 0.02 1 496 . 92 LYS HA H 4.472 0.02 1 497 . 92 LYS HB2 H 1.861 0.02 1 498 . 92 LYS HE2 H 3.008 0.02 1 499 . 92 LYS HG2 H 1.565 0.02 2 500 . 92 LYS HG3 H 1.443 0.02 2 501 . 93 TRP H H 8.700 0.02 1 502 . 93 TRP HA H 4.665 0.02 1 503 . 93 TRP HB2 H 3.515 0.02 2 504 . 93 TRP HB3 H 2.621 0.02 2 505 . 93 TRP HD1 H 7.131 0.02 1 506 . 93 TRP HE1 H 10.472 0.02 1 507 . 93 TRP HE3 H 7.980 0.02 1 508 . 93 TRP HH2 H 6.983 0.02 1 509 . 93 TRP HZ2 H 7.640 0.02 1 510 . 93 TRP HZ3 H 7.478 0.02 1 511 . 94 ASP H H 8.432 0.02 1 512 . 94 ASP HA H 4.492 0.02 1 513 . 94 ASP HB2 H 2.760 0.02 2 514 . 94 ASP HB3 H 2.472 0.02 2 515 . 95 ARG H H 7.410 0.02 1 516 . 95 ARG HA H 3.388 0.02 1 517 . 95 ARG HB2 H 1.423 0.02 2 518 . 95 ARG HB3 H 1.149 0.02 2 519 . 95 ARG HD2 H 2.953 0.02 1 520 . 95 ARG HG3 H 0.946 0.02 1 521 . 96 ASP H H 8.192 0.02 1 522 . 96 ASP HA H 4.663 0.02 1 523 . 96 ASP HB2 H 2.783 0.02 2 524 . 96 ASP HB3 H 2.611 0.02 2 525 . 97 MET H H 7.586 0.02 1 526 . 97 MET HA H 4.294 0.02 1 527 . 97 MET HB2 H 2.172 0.02 2 528 . 97 MET HB3 H 2.027 0.02 2 529 . 97 MET HG2 H 2.172 0.02 2 530 . 97 MET HG3 H 2.542 0.02 2 stop_ save_ save_shift_set_2 _Saveframe_category assigned_chemical_shifts _Details ; For several residues a second chemical shift is observed, indicating a minor conformational species (25%). ; loop_ _Experiment_label '1H-1H TOCSY' '1H-1H NOESY' '1H-1H DQF-COSY' stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name DN3beta2-microglobulin _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 . 5 ILE H H 8.344 0.02 1 2 . 5 ILE HA H 4.848 0.02 1 3 . 5 ILE HB H 1.656 0.02 1 4 . 6 GLN H H 9.205 0.02 1 5 . 6 GLN HA H 4.942 0.02 1 6 . 6 GLN HB2 H 2.348 0.02 2 7 . 6 GLN HB3 H 2.214 0.02 2 8 . 7 VAL H H 8.872 0.02 1 9 . 7 VAL HA H 5.396 0.02 1 10 . 7 VAL HB H 1.975 0.02 1 11 . 7 VAL HG1 H 0.886 0.02 2 12 . 7 VAL HG2 H 0.951 0.02 2 13 . 8 TYR H H 8.595 0.02 1 14 . 8 TYR HA H 5.299 0.02 1 15 . 20 PHE H H 10.362 0.02 1 16 . 20 PHE HA H 5.434 0.02 1 17 . 20 PHE HB2 H 2.658 0.02 1 18 . 20 PHE HD1 H 7.017 0.02 1 19 . 23 CYS H H 9.622 0.02 1 20 . 24 TYR H H 9.586 0.02 1 21 . 24 TYR HA H 5.403 0.02 1 22 . 24 TYR HB2 H 3.018 0.02 1 23 . 35 VAL H H 8.140 0.02 1 24 . 35 VAL HA H 4.793 0.02 1 25 . 35 VAL HB H 0.617 0.02 1 26 . 35 VAL HG1 H 0.451 0.02 2 27 . 35 VAL HG2 H 0.200 0.02 2 28 . 36 ASP H H 8.909 0.02 1 29 . 36 ASP HA H 5.032 0.02 1 30 . 36 ASP HB2 H 2.183 0.02 1 31 . 47 VAL H H 7.939 0.02 1 32 . 47 VAL HA H 4.507 0.02 1 33 . 47 VAL HB H 2.053 0.02 1 34 . 47 VAL HG1 H 1.070 0.02 2 35 . 47 VAL HG2 H 0.986 0.02 2 36 . 48 GLU H H 8.532 0.02 1 37 . 48 GLU HA H 4.507 0.02 1 38 . 48 GLU HB2 H 1.581 0.02 2 39 . 48 GLU HB3 H 0.713 0.02 2 40 . 53 SER H H 8.079 0.02 1 41 . 53 SER HA H 4.709 0.02 1 42 . 53 SER HB3 H 2.674 0.02 1 43 . 64 TYR H H 9.067 0.02 1 44 . 64 TYR HA H 5.345 0.02 1 45 . 64 TYR HB2 H 2.840 0.02 2 46 . 64 TYR HB3 H 2.642 0.02 2 47 . 65 TYR H H 8.967 0.02 1 48 . 65 TYR HA H 6.056 0.02 1 49 . 65 TYR HB2 H 3.046 0.02 2 50 . 65 TYR HB3 H 2.735 0.02 2 51 . 67 GLU H H 8.466 0.02 1 52 . 67 GLU HA H 4.361 0.02 1 53 . 67 GLU HB2 H 1.857 0.02 1 54 . 76 TYR H H 9.447 0.02 1 55 . 76 TYR HA H 5.686 0.02 1 56 . 76 TYR HB2 H 2.824 0.02 2 57 . 76 TYR HB3 H 2.752 0.02 2 58 . 77 ALA H H 8.790 0.02 1 59 . 77 ALA HA H 5.059 0.02 1 60 . 77 ALA HB H 1.218 0.02 1 61 . 79 ARG H H 9.363 0.02 1 62 . 79 ARG HA H 5.379 0.02 1 63 . 79 ARG HB2 H 1.830 0.02 2 64 . 79 ARG HB3 H 1.174 0.02 2 65 . 81 ASN H H 8.931 0.02 1 66 . 81 ASN HA H 5.167 0.02 1 67 . 81 ASN HB2 H 2.810 0.02 2 68 . 81 ASN HB3 H 2.413 0.02 2 69 . 82 HIS H H 7.790 0.02 1 70 . 82 HIS HA H 4.588 0.02 1 71 . 83 VAL H H 7.950 0.02 1 72 . 87 GLN H H 7.527 0.02 1 73 . 87 GLN HA H 4.798 0.02 1 74 . 89 LYS H H 8.563 0.02 1 75 . 89 LYS HA H 4.556 0.02 1 76 . 89 LYS HB2 H 1.742 0.02 1 77 . 89 LYS HG2 H 1.440 0.02 1 78 . 91 VAL H H 8.987 0.02 1 79 . 91 VAL HA H 4.294 0.02 1 80 . 91 VAL HB H 1.885 0.02 1 81 . 91 VAL HG1 H 1.024 0.02 1 82 . 94 ASP H H 8.506 0.02 1 83 . 94 ASP HA H 4.521 0.02 1 84 . 94 ASP HB2 H 2.779 0.02 2 85 . 94 ASP HB3 H 2.491 0.02 2 86 . 95 ARG H H 7.442 0.02 1 87 . 95 ARG HA H 3.407 0.02 1 88 . 95 ARG HB3 H 1.147 0.02 1 stop_ save_