data_5670 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structural Characterization of Hellethionins from helleborus purpurascens ; _BMRB_accession_number 5670 _BMRB_flat_file_name bmr5670.str _Entry_type original _Submission_date 2003-01-23 _Accession_date 2003-01-23 _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 Milbradt Alexander G. . 2 Kerek Franz . . 3 Moroder Luis . . 4 Renner Christian . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 253 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-04-30 original author . stop_ _Original_release_date 2003-04-30 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural Characterization of Hellethionins from helleborus purpurascens' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12600207 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Milbradt Alexander G. . 2 Kerek Franz . . 3 Moroder Luis . . 4 Renner Christian . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 42 _Journal_issue 8 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2404 _Page_last 2411 _Year 2003 _Details . loop_ _Keyword 'Helleborus Hellethionin Thionins' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref-1 _Saveframe_category citation _Citation_full ; Goddard T.D. and Kneller D.G.; Sparky 3; University of California, San Francisco ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _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 . _Page_last . _Year . _Details . save_ save_ref-2 _Saveframe_category citation _Citation_full ; Koradi R, Billeter M, Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph. 1996 Feb;14(1):51-5, 29-32. ; _Citation_title 'MOLMOL: a program for display and analysis of macromolecular structures.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8744573 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Koradi R. . . 2 Billeter M. . . 3 Wuthrich K. . . stop_ _Journal_abbreviation . _Journal_name_full 'Journal of molecular graphics' _Journal_volume 14 _Journal_issue 1 _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 51 _Page_last 32 _Year 1996 _Details ; MOLMOL is a molecular graphics program for display, analysis, and manipulation of three-dimensional structures of biological macromolecules, with special emphasis on nuclear magnetic resonance (NMR) solution structures of proteins and nucleic acids. MOLMOL has a graphical user interface with menus, dialog boxes, and on-line help. The display possibilities include conventional presentation, as well as novel schematic drawings, with the option of combining different presentations in one view of a molecule. Covalent molecular structures can be modified by addition or removal of individual atoms and bonds, and three-dimensional structures can be manipulated by interactive rotation about individual bonds. Special efforts were made to allow for appropriate display and analysis of the sets of typically 20-40 conformers that are conventionally used to represent the result of an NMR structure determination, using functions for superimposing sets of conformers, calculation of root mean square distance (RMSD) values, identification of hydrogen bonds, checking and displaying violations of NMR constraints, and identification and listing of short distances between pairs of hydrogen atoms. ; save_ save_ref-3 _Saveframe_category citation _Citation_full ; Laskowski RA, Rullmannn JA, MacArthur MW, Kaptein R, Thornton JM. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J Biomol NMR. 1996 Dec;8(4):477-86. ; _Citation_title 'AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9008363 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Laskowski 'R. A.' A. . 2 Rullmannn 'J. A.' A. . 3 MacArthur 'M. W.' W. . 4 Kaptein R. . . 5 Thornton 'J. M.' M. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 8 _Journal_issue 4 _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 477 _Page_last 486 _Year 1996 _Details ; The AQUA and PROCHECK-NMR programs provide a means of validating the geometry and restraint violations of an ensemble of protein structures solved by solution NMR. The outputs include a detailed breakdown of the restraint violations, a number of plots in PostScript format and summary statistics. These various analyses indicate both the degree of agreement of the model structures with the experimental dat, and the quality of their geometrical properties. They are intended to be of use both to support ongoing NMR structure determination and in the validation of the final results. ; save_ ################################## # Molecular system description # ################################## save_system_Hellethionin_D _Saveframe_category molecular_system _Mol_system_name 'Hellethionin D' _Abbreviation_common 'Hellethionin D' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Hellethionin D' $Hellethionin_D 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_Hellethionin_D _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Hellethionin D' _Abbreviation_common 'Hel D' _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details TTTT ############################## # Polymer residue sequence # ############################## _Residue_count 46 _Mol_residue_sequence ; KSCCRNTLARNCYNACRFTG GSQPTCGILCDCIHVTTTTC PSSHPS ; loop_ _Residue_seq_code _Residue_label 1 LYS 2 SER 3 CYS 4 CYS 5 ARG 6 ASN 7 THR 8 LEU 9 ALA 10 ARG 11 ASN 12 CYS 13 TYR 14 ASN 15 ALA 16 CYS 17 ARG 18 PHE 19 THR 20 GLY 21 GLY 22 SER 23 GLN 24 PRO 25 THR 26 CYS 27 GLY 28 ILE 29 LEU 30 CYS 31 ASP 32 CYS 33 ILE 34 HIS 35 VAL 36 THR 37 THR 38 THR 39 THR 40 CYS 41 PRO 42 SER 43 SER 44 HIS 45 PRO 46 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-26 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1NBL "Nmr Structure Of Hellethionin D" 100.00 46 100.00 100.00 1.93e-23 PDB 3SZS "Crystal Structure Analysis Of Hellethionin D" 100.00 46 100.00 100.00 1.93e-23 SP P60057 "RecName: Full=Hellethionin-D [Helleborus purpurascens]" 100.00 46 100.00 100.00 1.93e-23 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Hellethionin_D 'Helleborus purpurascens' 171899 Eukaryota Viridiplantae Helleborus purpurascens 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 $Hellethionin_D 'purified from the natural source' . . . . . 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 $Hellethionin_D 3.0 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Hellethionin_D 5.0 mM . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 3.0 loop_ _Task 'data acquisition' 'data processing' stop_ _Details . save_ save_INSIGHT _Saveframe_category software _Name INSIGHT _Version 98 loop_ _Task 'structure calculation' stop_ _Details . save_ save_Sparky _Saveframe_category software _Name Sparky _Version 3 loop_ _Task 'peak assignment' stop_ _Details . _Citation_label $ref-1 save_ save_MOLMOL _Saveframe_category software _Name MOLMOL _Version . loop_ _Task visualization stop_ _Details . _Citation_label $ref-2 save_ save_PROCHECK _Saveframe_category software _Name PROCHECK _Version . loop_ _Task 'checking the quality of the protein structure' stop_ _Details . _Citation_label $ref-3 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _Sample_label . save_ save_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H TOCSY' _Sample_label . save_ save_1H-1H_COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H COSY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2.5 0.1 n/a temperature 293 0.5 K stop_ save_ save_cond_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2.5 0.1 n/a temperature 283 0.5 K stop_ save_ save_cond_3 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2.5 0.1 n/a temperature 303 0.5 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_shift1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Hellethionin D' _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 HA H 3.72 0.01 1 2 . 1 LYS HB2 H 1.48 0.01 2 3 . 1 LYS HB3 H 1.35 0.01 2 4 . 1 LYS HG2 H 0.83 0.01 1 5 . 1 LYS HG3 H 0.83 0.01 1 6 . 1 LYS HD2 H 1.03 0.01 2 7 . 1 LYS HD3 H 1.1 0.01 2 8 . 1 LYS HE2 H 2.64 0.01 1 9 . 1 LYS HE3 H 2.64 0.01 1 10 . 1 LYS HZ H 7.17 0.01 1 11 . 2 SER H H 8.52 0.01 1 12 . 2 SER HA H 4.65 0.01 1 13 . 2 SER HB2 H 3.41 0.01 2 14 . 2 SER HB3 H 2.96 0.01 2 15 . 3 CYS H H 8.45 0.01 1 16 . 3 CYS HA H 4.60 0.01 1 17 . 3 CYS HB2 H 4.22 0.01 2 18 . 3 CYS HB3 H 1.93 0.01 2 19 . 4 CYS H H 9.47 0.01 1 20 . 4 CYS HA H 4.90 0.01 1 21 . 4 CYS HB2 H 2.60 0.01 2 22 . 4 CYS HB3 H 2.14 0.01 2 23 . 5 ARG H H 7.52 0.01 1 24 . 5 ARG HA H 3.51 0.01 1 25 . 5 ARG HB2 H 1.65 0.01 1 26 . 5 ARG HB3 H 1.65 0.01 1 27 . 5 ARG HG2 H 1.35 0.01 2 28 . 5 ARG HG3 H 1.30 0.01 2 29 . 5 ARG HD2 H 2.93 0.01 2 30 . 5 ARG HD3 H 2.62 0.01 2 31 . 5 ARG HE H 6.72 0.01 1 32 . 5 ARG HH11 H 6.10 0.01 4 33 . 5 ARG HH12 H 6.10 0.01 4 34 . 5 ARG HH21 H 6.10 0.01 4 35 . 5 ARG HH22 H 6.10 0.01 4 36 . 6 ASN H H 6.82 0.01 1 37 . 6 ASN HA H 4.46 0.01 1 38 . 6 ASN HB2 H 3.01 0.01 1 39 . 6 ASN HB3 H 3.01 0.01 1 40 . 6 ASN HD21 H 7.51 0.01 2 41 . 6 ASN HD22 H 6.45 0.01 2 42 . 7 THR H H 8.30 0.01 1 43 . 7 THR HA H 3.58 0.01 1 44 . 7 THR HB H 3.79 0.01 1 45 . 7 THR HG2 H 0.94 0.01 1 46 . 8 LEU H H 7.65 0.01 1 47 . 8 LEU HA H 3.77 0.01 1 48 . 8 LEU HB2 H 1.38 0.01 2 49 . 8 LEU HB3 H 1.29 0.01 2 50 . 8 LEU HD1 H 0.57 0.01 2 51 . 8 LEU HD2 H 0.61 0.01 2 52 . 9 ALA H H 8.02 0.01 1 53 . 9 ALA HA H 4.07 0.01 1 54 . 9 ALA HB H 1.52 0.01 1 55 . 10 ARG H H 7.68 0.01 1 56 . 10 ARG HA H 4.16 0.01 1 57 . 10 ARG HB2 H 1.92 0.01 2 58 . 10 ARG HB3 H 1.36 0.01 2 59 . 10 ARG HG2 H 1.59 0.01 1 60 . 10 ARG HG3 H 1.59 0.01 1 61 . 10 ARG HD2 H 3.06 0.01 2 62 . 10 ARG HD3 H 3.00 0.01 2 63 . 10 ARG HE H 8.07 0.01 1 64 . 10 ARG HH11 H 6.79 0.01 4 65 . 10 ARG HH12 H 6.79 0.01 4 66 . 10 ARG HH21 H 6.28 0.01 4 67 . 10 ARG HH22 H 6.28 0.01 4 68 . 11 ASN H H 8.16 0.01 1 69 . 11 ASN HA H 4.21 0.01 1 70 . 11 ASN HB2 H 2.64 0.01 2 71 . 11 ASN HB3 H 2.60 0.01 2 72 . 11 ASN HD21 H 7.29 0.01 2 73 . 11 ASN HD22 H 6.70 0.01 2 74 . 12 CYS H H 8.15 0.01 1 75 . 12 CYS HA H 3.89 0.01 1 76 . 12 CYS HB2 H 3.58 0.01 2 77 . 12 CYS HB3 H 2.72 0.01 2 78 . 13 TYR H H 8.74 0.01 1 79 . 13 TYR HA H 3.36 0.01 1 80 . 13 TYR HB2 H 3.06 0.01 2 81 . 13 TYR HB3 H 2.89 0.01 2 82 . 13 TYR HD1 H 6.4 0.01 4 83 . 13 TYR HD2 H 6.4 0.01 4 84 . 13 TYR HE1 H 6.4 0.01 4 85 . 13 TYR HE2 H 6.4 0.01 4 86 . 14 ASN H H 8.55 0.01 1 87 . 14 ASN HA H 4.00 0.01 1 88 . 14 ASN HB2 H 2.62 0.01 2 89 . 14 ASN HB3 H 2.52 0.01 2 90 . 14 ASN HD21 H 7.6 0.01 1 91 . 14 ASN HD22 H 7.6 0.01 1 92 . 15 ALA H H 7.63 0.01 1 93 . 15 ALA HA H 3.93 0.01 1 94 . 15 ALA HB H 1.19 0.01 1 95 . 16 CYS H H 7.98 0.01 1 96 . 16 CYS HA H 3.80 0.01 1 97 . 16 CYS HB2 H 2.83 0.01 2 98 . 16 CYS HB3 H 2.78 0.01 2 99 . 17 ARG H H 8.26 0.01 1 100 . 17 ARG HA H 3.79 0.01 1 101 . 17 ARG HB2 H 1.48 0.01 2 102 . 17 ARG HB3 H 1.37 0.01 2 103 . 17 ARG HG2 H 0.88 0.01 2 104 . 17 ARG HG3 H 0.62 0.01 2 105 . 17 ARG HD2 H 2.72 0.01 2 106 . 17 ARG HD3 H 2.15 0.01 2 107 . 17 ARG HE H 6.72 0.01 1 108 . 17 ARG HH11 H 6.79 0.01 4 109 . 17 ARG HH12 H 6.79 0.01 4 110 . 17 ARG HH21 H 6.28 0.01 4 111 . 17 ARG HH22 H 6.28 0.01 4 112 . 18 PHE H H 8.00 0.01 1 113 . 18 PHE HA H 4.01 0.01 1 114 . 18 PHE HB2 H 3.07 0.01 2 115 . 18 PHE HB3 H 2.94 0.01 2 116 . 18 PHE HD1 H 7.01 0.01 4 117 . 18 PHE HD2 H 7.01 0.01 4 118 . 18 PHE HE1 H 6.91 0.01 4 119 . 18 PHE HE2 H 6.91 0.01 4 120 . 18 PHE HZ H 6.91 0.01 4 121 . 19 THR H H 7.24 0.01 1 122 . 19 THR HA H 3.94 0.01 1 123 . 19 THR HB H 4.27 0.01 1 124 . 19 THR HG2 H 1.06 0.01 1 125 . 20 GLY H H 7.24 0.01 1 126 . 20 GLY HA2 H 4.04 0.01 2 127 . 20 GLY HA3 H 3.30 0.01 2 128 . 21 GLY H H 7.88 0.01 1 129 . 21 GLY HA2 H 3.73 0.01 2 130 . 21 GLY HA3 H 3.12 0.01 2 131 . 22 SER H H 8.45 0.01 1 132 . 22 SER HA H 4.03 0.01 1 133 . 22 SER HB2 H 3.90 0.01 2 134 . 22 SER HB3 H 3.74 0.01 2 135 . 23 GLN H H 9.01 0.01 1 136 . 23 GLN HA H 3.76 0.01 1 137 . 23 GLN HB2 H 1.84 0.01 2 138 . 23 GLN HB3 H 1.77 0.01 2 139 . 23 GLN HG2 H 2.20 0.01 2 140 . 23 GLN HG3 H 1.95 0.01 2 141 . 23 GLN HE21 H 7.13 0.01 2 142 . 23 GLN HE22 H 6.56 0.01 2 143 . 24 PRO HA H 4.05 0.01 1 144 . 24 PRO HB2 H 1.99 0.01 2 145 . 24 PRO HB3 H 1.56 0.01 2 146 . 24 PRO HG2 H 1.78 0.01 2 147 . 24 PRO HG3 H 1.65 0.01 2 148 . 24 PRO HD2 H 3.54 0.01 2 149 . 24 PRO HD3 H 3.39 0.01 2 150 . 25 THR H H 7.10 0.01 1 151 . 25 THR HA H 3.55 0.01 1 152 . 25 THR HB H 3.80 0.01 1 153 . 25 THR HG2 H 0.84 0.01 1 154 . 26 CYS H H 8.40 0.01 1 155 . 26 CYS HA H 4.28 0.01 1 156 . 26 CYS HB2 H 2.29 0.01 2 157 . 26 CYS HB3 H 2.16 0.01 2 158 . 27 GLY H H 8.42 0.01 1 159 . 27 GLY HA2 H 3.83 0.01 2 160 . 27 GLY HA3 H 3.45 0.01 2 161 . 28 ILE H H 7.44 0.01 1 162 . 28 ILE HA H 3.66 0.01 1 163 . 28 ILE HB H 1.67 0.01 1 164 . 28 ILE HG12 H 1.41 0.01 2 165 . 28 ILE HG13 H 1.00 0.01 2 166 . 28 ILE HG2 H 0.66 0.01 1 167 . 28 ILE HD1 H 0.56 0.01 1 168 . 29 LEU H H 7.81 0.01 1 169 . 29 LEU HA H 3.81 0.01 1 170 . 29 LEU HB2 H 1.40 0.01 1 171 . 29 LEU HB3 H 1.40 0.01 1 172 . 29 LEU HG H 1.28 0.01 1 173 . 29 LEU HD1 H 0.57 0.01 1 174 . 29 LEU HD2 H 0.57 0.01 1 175 . 30 CYS H H 7.40 0.01 1 176 . 30 CYS HA H 4.51 0.01 1 177 . 30 CYS HB2 H 3.54 0.01 2 178 . 30 CYS HB3 H 2.65 0.01 2 179 . 31 ASP H H 7.70 0.01 1 180 . 31 ASP HA H 4.27 0.01 1 181 . 31 ASP HB2 H 3.36 0.01 2 182 . 31 ASP HB3 H 2.62 0.01 2 183 . 32 CYS H H 8.84 0.01 1 184 . 32 CYS HA H 5.24 0.01 1 185 . 32 CYS HB2 H 2.64 0.01 2 186 . 32 CYS HB3 H 1.79 0.01 2 187 . 33 ILE H H 8.64 0.01 1 188 . 33 ILE HA H 4.25 0.01 1 189 . 33 ILE HB H 1.40 0.01 1 190 . 33 ILE HG12 H 0.573 0.01 2 191 . 33 ILE HG13 H -0.07 0.01 2 192 . 33 ILE HG2 H 0.03 0.01 1 193 . 33 ILE HD1 H -0.01 0.01 1 194 . 34 HIS H H 8.52 0.01 1 195 . 34 HIS HA H 4.82 0.01 1 196 . 34 HIS HB2 H 2.73 0.01 2 197 . 34 HIS HB3 H 2.69 0.01 2 198 . 34 HIS HD1 H 8.52 0.01 4 199 . 35 VAL H H 7.96 0.01 1 200 . 35 VAL HA H 4.44 0.01 1 201 . 35 VAL HB H 1.99 0.01 1 202 . 35 VAL HG1 H 0.44 0.01 2 203 . 35 VAL HG2 H 0.39 0.01 2 204 . 36 THR H H 8.54 0.01 1 205 . 36 THR HA H 4.15 0.01 5 206 . 37 THR H H 6.65 0.01 1 207 . 37 THR HA H 4.17 0.01 1 208 . 37 THR HB H 4.31 0.01 1 209 . 37 THR HG2 H 0.91 0.01 1 210 . 38 THR H H 8.22 0.01 1 211 . 38 THR HA H 3.79 0.01 1 212 . 38 THR HB H 4.02 0.01 1 213 . 38 THR HG2 H 0.93 0.01 1 214 . 39 THR H H 6.78 0.01 1 215 . 39 THR HA H 4.16 0.01 1 216 . 39 THR HB H 3.79 0.01 1 217 . 39 THR HG2 H 0.82 0.01 1 218 . 40 CYS H H 8.57 0.01 1 219 . 40 CYS HA H 4.59 0.01 1 220 . 40 CYS HB2 H 3.55 0.01 2 221 . 40 CYS HB3 H 2.14 0.01 2 222 . 41 PRO HA H 4.29 0.01 1 223 . 41 PRO HB2 H 1.98 0.01 2 224 . 41 PRO HB3 H 1.84 0.01 2 225 . 41 PRO HG2 H 1.50 0.01 1 226 . 41 PRO HG3 H 1.50 0.01 1 227 . 41 PRO HD2 H 3.51 0.01 2 228 . 41 PRO HD3 H 3.30 0.01 2 229 . 42 SER H H 8.55 0.01 1 230 . 42 SER HA H 3.71 0.01 4 231 . 42 SER HB2 H 3.59 0.01 4 232 . 42 SER HB3 H 3.59 0.01 4 233 . 43 SER H H 7.62 0.01 1 234 . 43 SER HA H 3.87 0.01 1 235 . 43 SER HB2 H 3.76 0.01 2 236 . 43 SER HB3 H 3.65 0.01 2 237 . 44 HIS H H 7.41 0.01 1 238 . 44 HIS HA H 4.37 0.01 1 239 . 44 HIS HB2 H 2.21 0.01 2 240 . 44 HIS HB3 H 2.01 0.01 2 241 . 44 HIS HD2 H 6.72 0.01 1 242 . 44 HIS HE1 H 8.44 0.01 1 243 . 45 PRO HA H 4.00 0.01 1 244 . 45 PRO HB2 H 1.66 0.01 4 245 . 45 PRO HB3 H 1.66 0.01 4 246 . 45 PRO HG2 H 1.66 0.01 4 247 . 45 PRO HG3 H 1.66 0.01 4 248 . 45 PRO HD2 H 3.42 0.01 2 249 . 45 PRO HD3 H 3.07 0.01 2 250 . 46 SER H H 7.78 0.01 1 251 . 46 SER HA H 4.04 0.01 1 252 . 46 SER HB2 H 3.42 0.01 2 253 . 46 SER HB3 H 2.56 0.01 2 stop_ loop_ _Atom_shift_assign_ID_ambiguity 35 '34,33,32' '67,66,65,64' '85,84,83,82' '111,110,109,108' '120,119,118,117,116' '232,231,230' '247,246,245,244' stop_ save_