data_4199 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Determination of the Solution Structure of the N-Domain Plus Linker of Antarctic Eel Pout Antifreeze Protein RD3 ; _BMRB_accession_number 4199 _BMRB_flat_file_name bmr4199.str _Entry_type original _Submission_date 1998-09-10 _Accession_date 1998-09-10 _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 Miura Kazunori . . 2 Ohgiya Satoru . . 3 Hoshino Tamotsu . . 4 Nemoto Nobuaki . . 5 Odaira Masato . . 6 Nitta Katsutoshi . . 7 Tsuda Sakae . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 415 "15N chemical shifts" 74 "coupling constants" 50 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-12-22 original author . stop_ _Original_release_date 1999-12-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Determination of the Solution Structure of the N-Domain Plus Linker of Antarctic Eel Pout Antifreeze Protein RD3 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99353969 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Miura Kazunori . . 2 Ohgiya Satoru . . 3 Hoshino Tamotsu . . 4 Nemoto Nobuaki . . 5 Odaira Masato . . 6 Nitta Katsutoshi . . 7 Tsuda Sakae . . stop_ _Journal_abbreviation 'J. Biochem.' _Journal_name_full 'Journal of Biochemistry' _Journal_volume 126 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 387 _Page_last 394 _Year 1999 _Details . loop_ _Keyword 'antifreeze protein, thermal hysteresis protein, ice binding protein' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full ; Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995). ; _Citation_title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8589602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D S' S. . 2 Bigam 'C G' G. . 3 Yao J . . 4 Abildgaard F . . 5 Dyson 'H J' J. . 6 Oldfield E . . 7 Markley 'J L' L. . 8 Sykes 'B D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 2 _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 135 _Page_last 140 _Year 1995 _Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; save_ ################################## # Molecular system description # ################################## save_system_N-term_linker_Type_III_Antifreeze_protein_RD3 _Saveframe_category molecular_system _Mol_system_name 'N-term linker Type III Antifreeze protein RD3' _Abbreviation_common RD3-Nl _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label RD3-N1 $RD3-N1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_RD3-N1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'N-term. domain with linker Type III Antifreeze protein RD3' _Molecular_mass . _Mol_thiol_state . _Details ; The region of 65-73 (DGTTSPGLK) is a linker portion which connects N- and C-domains of RD3. ; ############################## # Polymer residue sequence # ############################## _Residue_count 73 _Mol_residue_sequence ; NKASVVANQLIPINTALTLI MMKAEVVTPMGIPAEEIPNL VGMQVNRAVPLGTTLMPDMV KNYEDGTTSPGLK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 ASN 2 2 LYS 3 3 ALA 4 4 SER 5 5 VAL 6 6 VAL 7 7 ALA 8 8 ASN 9 9 GLN 10 10 LEU 11 11 ILE 12 12 PRO 13 13 ILE 14 14 ASN 15 15 THR 16 16 ALA 17 17 LEU 18 18 THR 19 19 LEU 20 20 ILE 21 21 MET 22 22 MET 23 23 LYS 24 24 ALA 25 25 GLU 26 26 VAL 27 27 VAL 28 28 THR 29 29 PRO 30 30 MET 31 31 GLY 32 32 ILE 33 33 PRO 34 34 ALA 35 35 GLU 36 36 GLU 37 37 ILE 38 38 PRO 39 39 ASN 40 40 LEU 41 41 VAL 42 42 GLY 43 43 MET 44 44 GLN 45 45 VAL 46 46 ASN 47 47 ARG 48 48 ALA 49 49 VAL 50 50 PRO 51 51 LEU 52 52 GLY 53 53 THR 54 54 THR 55 55 LEU 56 56 MET 57 57 PRO 58 58 ASP 59 59 MET 60 60 VAL 61 61 LYS 62 62 ASN 63 63 TYR 64 64 GLU 65 65 ASP 66 66 GLY 67 67 THR 68 68 THR 69 69 SER 70 70 PRO 71 71 GLY 72 72 LEU 73 73 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-14 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 1UCS "Type Iii Antifreeze Protein Rd1 From An Antarctic Eel Pout" 87.67 64 98.44 98.44 1.85e-34 PDB 3NLA "Nmr Structure Of The N-Terminal Domain With A Linker Portion Of Antarctic Eel Pout Antifreeze Protein Rd3, 40 Structures" 100.00 74 100.00 100.00 2.19e-42 PDB 3RDN "Nmr Structure Of The N-Terminal Domain With A Linker Portion Of Antarctic Eel Pout Antifreeze Protein Rd3, Minimized Average St" 100.00 74 100.00 100.00 2.19e-42 GB AFU88733 "AFPIII-3 [Lycodichthys dearborni]" 87.67 87 98.44 98.44 6.78e-35 GB AFU88737 "AFPIII-21 [Lycodichthys dearborni]" 87.67 87 98.44 98.44 6.78e-35 GB AFU88748 "AFPIII-6 [Lycodichthys dearborni]" 87.67 87 98.44 98.44 6.78e-35 PRF 2109220A "antifreeze peptide:ISOTYPE=RD1 [Lycodichthys dearborni]" 87.67 64 98.44 98.44 1.85e-34 SP P35751 "RecName: Full=Ice-structuring protein RD1; Short=ISP RD1; AltName: Full=Antifreeze peptide RD1" 87.67 64 98.44 98.44 1.85e-34 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Variant _Tissue $RD3-N1 'antarctic eel pout' 8201 Eukaryota Metazoa Lycodichthys dearborni RD3 blood_plasma stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $RD3-N1 'recombinant technology' 'Escherichia coli' Escherichia coli JM105 Plasmid pKK223-3UC stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $RD3-N1 1.0 mM . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $RD3-N1 1.0 mM [U-15N] stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 500 _Details . save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer JEOL _Model JEOL _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_DQFCOSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name DQFCOSY _Sample_label $sample_two save_ save_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label $sample_two save_ save_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label $sample_two save_ save_15N-HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HSQC _Sample_label $sample_two save_ save_15N_TOCSYHSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name 15N_TOCSYHSQC _Sample_label $sample_two save_ save_15N-NOESYHSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-NOESYHSQC _Sample_label $sample_two save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.05 0.01 M pH 6.7 0.2 n/a temperature 277 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_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 _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.00 . direct . . . . $citation_one DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 $citation_one 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_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_two stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name RD3-N1 _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 ASN HA H 4.82 . 1 2 . 1 ASN HB2 H 2.74 . 2 3 . 1 ASN HB3 H 2.97 . 2 4 . 1 ASN HD21 H 7.10 . 2 5 . 1 ASN HD22 H 7.66 . 2 6 . 1 ASN ND2 N 113.69 . 1 7 . 2 LYS H H 8.40 . 1 8 . 2 LYS HA H 4.42 . 1 9 . 2 LYS HB2 H 2.10 . 1 10 . 2 LYS HB3 H 2.10 . 1 11 . 2 LYS HG2 H 1.83 . 1 12 . 2 LYS HG3 H 1.83 . 1 13 . 2 LYS HE2 H 3.06 . 1 14 . 2 LYS HE3 H 3.06 . 1 15 . 2 LYS N N 120.15 . 1 16 . 3 ALA H H 8.83 . 1 17 . 3 ALA HA H 4.33 . 1 18 . 3 ALA HB H 1.32 . 1 19 . 3 ALA N N 124.15 . 1 20 . 4 SER H H 9.05 . 1 21 . 4 SER HA H 5.45 . 1 22 . 4 SER HB2 H 3.70 . 1 23 . 4 SER HB3 H 3.70 . 1 24 . 4 SER N N 119.66 . 1 25 . 5 VAL H H 8.40 . 1 26 . 5 VAL HA H 4.15 . 1 27 . 5 VAL HB H 1.93 . 1 28 . 5 VAL HG1 H 0.83 . 1 29 . 5 VAL HG2 H 0.83 . 1 30 . 5 VAL N N 122.39 . 1 31 . 6 VAL H H 9.28 . 1 32 . 6 VAL HA H 4.61 . 1 33 . 6 VAL HB H 1.57 . 1 34 . 6 VAL HG1 H 0.73 . 2 35 . 6 VAL HG2 H 0.84 . 2 36 . 6 VAL N N 128.10 . 1 37 . 7 ALA H H 8.43 . 1 38 . 7 ALA HA H 4.54 . 1 39 . 7 ALA HB H 1.72 . 1 40 . 7 ALA N N 128.07 . 1 41 . 8 ASN H H 9.19 . 1 42 . 8 ASN HA H 4.78 . 1 43 . 8 ASN HB2 H 2.68 . 1 44 . 8 ASN HB3 H 2.68 . 1 45 . 8 ASN HD21 H 7.00 . 1 46 . 8 ASN HD22 H 7.00 . 1 47 . 8 ASN N N 126.43 . 1 48 . 8 ASN ND2 N 113.62 . 1 49 . 9 GLN H H 7.84 . 1 50 . 9 GLN HA H 4.43 . 1 51 . 9 GLN HB2 H 2.02 . 2 52 . 9 GLN HB3 H 1.86 . 2 53 . 9 GLN HG2 H 2.14 . 2 54 . 9 GLN HG3 H 3.35 . 2 55 . 9 GLN HE21 H 6.94 . 2 56 . 9 GLN HE22 H 7.52 . 2 57 . 9 GLN N N 112.72 . 1 58 . 9 GLN NE2 N 111.98 . 1 59 . 10 LEU H H 8.48 . 1 60 . 10 LEU HA H 4.76 . 1 61 . 10 LEU HB2 H 1.71 . 1 62 . 10 LEU HB3 H 1.71 . 1 63 . 10 LEU HG H 1.15 . 1 64 . 10 LEU HD1 H 0.80 . 2 65 . 10 LEU HD2 H 0.83 . 2 66 . 10 LEU N N 121.13 . 1 67 . 11 ILE H H 9.36 . 1 68 . 11 ILE HA H 4.62 . 1 69 . 11 ILE HB H 2.04 . 1 70 . 11 ILE HG12 H 0.94 . 2 71 . 11 ILE HG13 H 1.09 . 2 72 . 11 ILE N N 134.53 . 1 73 . 12 PRO HA H 4.48 . 1 74 . 12 PRO HB2 H 1.72 . 2 75 . 12 PRO HB3 H 2.37 . 2 76 . 12 PRO HG2 H 1.79 . 1 77 . 12 PRO HG3 H 1.79 . 1 78 . 12 PRO HD2 H 4.34 . 1 79 . 12 PRO HD3 H 4.34 . 1 80 . 13 ILE H H 8.46 . 1 81 . 13 ILE HA H 3.42 . 1 82 . 13 ILE HB H 1.69 . 1 83 . 13 ILE HG12 H 0.97 . 1 84 . 13 ILE HG13 H 0.97 . 1 85 . 13 ILE HG2 H 0.90 . 1 86 . 13 ILE HD1 H 0.90 . 1 87 . 13 ILE N N 121.63 . 1 88 . 14 ASN H H 7.56 . 1 89 . 14 ASN HA H 4.55 . 1 90 . 14 ASN HB2 H 3.03 . 2 91 . 14 ASN HB3 H 3.13 . 2 92 . 14 ASN HD21 H 7.18 . 2 93 . 14 ASN HD22 H 7.52 . 2 94 . 14 ASN N N 117.77 . 1 95 . 14 ASN ND2 N 117.01 . 1 96 . 15 THR H H 7.53 . 1 97 . 15 THR HA H 4.07 . 1 98 . 15 THR HB H 3.96 . 1 99 . 15 THR HG1 H 5.46 . 1 100 . 15 THR HG2 H 1.23 . 1 101 . 15 THR N N 117.67 . 1 102 . 16 ALA H H 8.64 . 1 103 . 16 ALA HA H 4.33 . 1 104 . 16 ALA HB H 1.28 . 1 105 . 16 ALA N N 129.04 . 1 106 . 17 LEU H H 9.28 . 1 107 . 17 LEU HA H 4.64 . 1 108 . 17 LEU HB2 H 2.26 . 1 109 . 17 LEU HB3 H 2.26 . 1 110 . 17 LEU HG H 1.97 . 1 111 . 17 LEU HD1 H 0.96 . 2 112 . 17 LEU HD2 H 1.05 . 2 113 . 17 LEU N N 125.65 . 1 114 . 18 THR H H 8.12 . 1 115 . 18 THR HA H 4.73 . 1 116 . 18 THR HB H 4.56 . 1 117 . 18 THR HG2 H 1.30 . 1 118 . 18 THR N N 114.76 . 1 119 . 19 LEU H H 8.93 . 1 120 . 19 LEU HA H 3.85 . 1 121 . 19 LEU HB2 H 1.58 . 2 122 . 19 LEU HB3 H 1.75 . 2 123 . 19 LEU HG H 1.74 . 1 124 . 19 LEU HD1 H 0.81 . 2 125 . 19 LEU HD2 H 0.94 . 2 126 . 19 LEU N N 121.37 . 1 127 . 20 ILE H H 7.75 . 1 128 . 20 ILE HA H 4.27 . 1 129 . 20 ILE HB H 1.96 . 1 130 . 20 ILE HG12 H 1.35 . 2 131 . 20 ILE HG13 H 1.39 . 2 132 . 20 ILE HG2 H 0.83 . 1 133 . 20 ILE HD1 H 0.95 . 1 134 . 20 ILE N N 113.75 . 1 135 . 21 MET H H 7.65 . 1 136 . 21 MET HA H 4.01 . 1 137 . 21 MET HB2 H 2.49 . 2 138 . 21 MET HB3 H 2.89 . 2 139 . 21 MET HG2 H 2.22 . 1 140 . 21 MET HG3 H 2.22 . 1 141 . 21 MET N N 118.85 . 1 142 . 22 MET H H 7.76 . 1 143 . 22 MET HA H 4.90 . 1 144 . 22 MET HB2 H 1.80 . 2 145 . 22 MET HB3 H 2.11 . 2 146 . 22 MET HG2 H 2.32 . 1 147 . 22 MET HG3 H 2.32 . 1 148 . 22 MET N N 118.57 . 1 149 . 23 LYS H H 9.14 . 1 150 . 23 LYS HA H 4.76 . 1 151 . 23 LYS HB2 H 2.02 . 1 152 . 23 LYS HB3 H 2.02 . 1 153 . 23 LYS HG2 H 1.64 . 2 154 . 23 LYS HG3 H 1.74 . 2 155 . 23 LYS HD2 H 1.82 . 1 156 . 23 LYS HD3 H 1.82 . 1 157 . 23 LYS HE2 H 2.90 . 1 158 . 23 LYS HE3 H 2.90 . 1 159 . 23 LYS N N 121.26 . 1 160 . 24 ALA H H 8.55 . 1 161 . 24 ALA HA H 5.22 . 1 162 . 24 ALA HB H 1.18 . 1 163 . 24 ALA N N 125.06 . 1 164 . 25 GLU H H 9.03 . 1 165 . 25 GLU HA H 4.62 . 1 166 . 25 GLU HB2 H 1.77 . 2 167 . 25 GLU HB3 H 1.90 . 2 168 . 25 GLU HG2 H 2.15 . 1 169 . 25 GLU HG3 H 2.15 . 1 170 . 25 GLU N N 123.66 . 1 171 . 26 VAL H H 9.22 . 1 172 . 26 VAL HA H 4.03 . 1 173 . 26 VAL HB H 2.09 . 1 174 . 26 VAL HG1 H 0.79 . 2 175 . 26 VAL HG2 H 0.90 . 2 176 . 26 VAL N N 127.58 . 1 177 . 27 VAL H H 8.60 . 1 178 . 27 VAL HA H 4.76 . 1 179 . 27 VAL HB H 2.09 . 1 180 . 27 VAL HG1 H 0.78 . 2 181 . 27 VAL HG2 H 0.91 . 2 182 . 27 VAL N N 125.01 . 1 183 . 28 THR H H 8.46 . 1 184 . 28 THR HA H 4.38 . 1 185 . 28 THR HB H 3.93 . 1 186 . 28 THR HG2 H 1.20 . 1 187 . 28 THR N N 118.10 . 1 188 . 29 PRO HA H 4.78 . 1 189 . 29 PRO HB2 H 2.11 . 2 190 . 29 PRO HB3 H 2.50 . 2 191 . 29 PRO HG2 H 1.80 . 2 192 . 29 PRO HG3 H 1.97 . 2 193 . 29 PRO HD2 H 3.51 . 2 194 . 29 PRO HD3 H 3.67 . 2 195 . 30 MET H H 8.66 . 1 196 . 30 MET HA H 4.10 . 1 197 . 30 MET HB2 H 2.00 . 2 198 . 30 MET HB3 H 2.19 . 2 199 . 30 MET HG2 H 2.83 . 1 200 . 30 MET HG3 H 2.83 . 1 201 . 30 MET HE H 1.17 . 1 202 . 30 MET N N 120.90 . 1 203 . 31 GLY H H 8.48 . 1 204 . 31 GLY HA2 H 3.51 . 2 205 . 31 GLY HA3 H 5.05 . 2 206 . 31 GLY N N 112.90 . 1 207 . 32 ILE H H 8.68 . 1 208 . 32 ILE HA H 4.03 . 1 209 . 32 ILE HB H 1.33 . 1 210 . 32 ILE HG12 H 1.02 . 2 211 . 32 ILE HG13 H 1.17 . 2 212 . 32 ILE HG2 H 0.57 . 1 213 . 32 ILE HD1 H 0.19 . 1 214 . 32 ILE N N 127.60 . 1 215 . 33 PRO HA H 4.60 . 1 216 . 33 PRO HB2 H 2.05 . 2 217 . 33 PRO HB3 H 2.60 . 2 218 . 34 ALA H H 8.52 . 1 219 . 34 ALA HA H 3.91 . 1 220 . 34 ALA HB H 1.25 . 1 221 . 34 ALA N N 125.28 . 1 222 . 35 GLU H H 9.54 . 1 223 . 35 GLU HA H 4.08 . 1 224 . 35 GLU HB2 H 2.10 . 1 225 . 35 GLU HB3 H 2.10 . 1 226 . 35 GLU HG2 H 2.37 . 2 227 . 35 GLU HG3 H 2.41 . 2 228 . 35 GLU N N 120.16 . 1 229 . 36 GLU H H 8.23 . 1 230 . 36 GLU HA H 4.38 . 1 231 . 36 GLU HB2 H 2.06 . 1 232 . 36 GLU HB3 H 2.06 . 1 233 . 36 GLU HG2 H 2.25 . 2 234 . 36 GLU HG3 H 2.45 . 2 235 . 36 GLU N N 116.82 . 1 236 . 37 ILE H H 7.59 . 1 237 . 37 ILE HA H 3.71 . 1 238 . 37 ILE HB H 1.91 . 1 239 . 37 ILE HG12 H 1.27 . 1 240 . 37 ILE HG13 H 1.27 . 1 241 . 37 ILE HG2 H 0.84 . 1 242 . 37 ILE HD1 H 0.87 . 1 243 . 37 ILE N N 121.02 . 1 244 . 38 PRO HA H 4.22 . 1 245 . 38 PRO HB2 H 1.81 . 2 246 . 38 PRO HB3 H 2.36 . 2 247 . 38 PRO HG2 H 2.01 . 1 248 . 38 PRO HG3 H 2.01 . 1 249 . 38 PRO HD2 H 3.52 . 2 250 . 38 PRO HD3 H 3.69 . 2 251 . 39 ASN H H 7.60 . 1 252 . 39 ASN HA H 4.64 . 1 253 . 39 ASN HB2 H 3.02 . 1 254 . 39 ASN HB3 H 3.02 . 1 255 . 39 ASN HD21 H 7.03 . 2 256 . 39 ASN HD22 H 8.13 . 2 257 . 39 ASN N N 115.23 . 1 258 . 39 ASN ND2 N 114.85 . 1 259 . 40 LEU H H 7.84 . 1 260 . 40 LEU HA H 4.26 . 1 261 . 40 LEU HB2 H 1.76 . 1 262 . 40 LEU HB3 H 1.76 . 1 263 . 40 LEU HG H 1.45 . 1 264 . 40 LEU HD1 H 0.81 . 2 265 . 40 LEU HD2 H 0.86 . 2 266 . 40 LEU N N 120.67 . 1 267 . 41 VAL H H 6.71 . 1 268 . 41 VAL HA H 3.26 . 1 269 . 41 VAL HB H 1.98 . 1 270 . 41 VAL HG1 H 1.01 . 2 271 . 41 VAL HG2 H 1.02 . 2 272 . 41 VAL N N 118.07 . 1 273 . 42 GLY H H 9.46 . 1 274 . 42 GLY HA2 H 3.62 . 2 275 . 42 GLY HA3 H 4.52 . 2 276 . 42 GLY N N 117.69 . 1 277 . 43 MET H H 8.58 . 1 278 . 43 MET HA H 4.52 . 1 279 . 43 MET HB2 H 2.24 . 1 280 . 43 MET HB3 H 2.24 . 1 281 . 43 MET HG2 H 2.45 . 2 282 . 43 MET HG3 H 2.67 . 2 283 . 43 MET HE H 0.98 . 1 284 . 43 MET N N 122.22 . 1 285 . 44 GLN H H 8.98 . 1 286 . 44 GLN HA H 5.32 . 1 287 . 44 GLN HB2 H 1.80 . 1 288 . 44 GLN HB3 H 1.80 . 1 289 . 44 GLN HG2 H 2.15 . 2 290 . 44 GLN HG3 H 2.29 . 2 291 . 44 GLN HE21 H 6.92 . 2 292 . 44 GLN HE22 H 7.61 . 2 293 . 44 GLN N N 119.18 . 1 294 . 44 GLN NE2 N 112.22 . 1 295 . 45 VAL H H 7.65 . 1 296 . 45 VAL HA H 5.39 . 1 297 . 45 VAL HB H 2.53 . 1 298 . 45 VAL HG1 H 1.04 . 2 299 . 45 VAL HG2 H 1.12 . 2 300 . 45 VAL N N 111.77 . 1 301 . 46 ASN H H 8.64 . 1 302 . 46 ASN HA H 4.71 . 1 303 . 46 ASN HB2 H 2.44 . 2 304 . 46 ASN HB3 H 3.27 . 2 305 . 46 ASN HD21 H 7.33 . 2 306 . 46 ASN HD22 H 7.40 . 2 307 . 46 ASN N N 119.19 . 1 308 . 46 ASN ND2 N 112.44 . 1 309 . 47 ARG H H 7.88 . 1 310 . 47 ARG HA H 4.43 . 1 311 . 47 ARG HB2 H 1.87 . 2 312 . 47 ARG HB3 H 2.11 . 2 313 . 47 ARG HG2 H 1.52 . 2 314 . 47 ARG HG3 H 1.63 . 2 315 . 47 ARG HD2 H 3.23 . 1 316 . 47 ARG HD3 H 3.23 . 1 317 . 47 ARG HE H 7.22 . 1 318 . 47 ARG N N 115.74 . 1 319 . 47 ARG NE N 114.63 . 1 320 . 48 ALA H H 8.60 . 1 321 . 48 ALA HA H 4.77 . 1 322 . 48 ALA HB H 1.34 . 1 323 . 48 ALA N N 121.30 . 1 324 . 49 VAL H H 9.34 . 1 325 . 49 VAL HA H 4.50 . 1 326 . 49 VAL HB H 2.28 . 1 327 . 49 VAL HG1 H 0.93 . 2 328 . 49 VAL HG2 H 1.05 . 2 329 . 49 VAL N N 126.08 . 1 330 . 50 PRO HA H 4.34 . 1 331 . 50 PRO HB2 H 2.08 . 1 332 . 50 PRO HB3 H 2.08 . 1 333 . 50 PRO HG2 H 2.38 . 1 334 . 50 PRO HG3 H 2.38 . 1 335 . 51 LEU H H 8.31 . 1 336 . 51 LEU HA H 3.41 . 1 337 . 51 LEU HB2 H 1.58 . 1 338 . 51 LEU HB3 H 1.58 . 1 339 . 51 LEU HG H 1.34 . 1 340 . 51 LEU HD1 H 0.72 . 2 341 . 51 LEU HD2 H 0.83 . 2 342 . 51 LEU N N 125.21 . 1 343 . 52 GLY H H 8.86 . 1 344 . 52 GLY HA2 H 3.62 . 2 345 . 52 GLY HA3 H 4.26 . 2 346 . 52 GLY N N 115.86 . 1 347 . 53 THR H H 7.87 . 1 348 . 53 THR HA H 4.28 . 1 349 . 53 THR HB H 4.14 . 1 350 . 53 THR HG1 H 5.68 . 1 351 . 53 THR HG2 H 1.31 . 1 352 . 53 THR N N 119.72 . 1 353 . 54 THR H H 8.94 . 1 354 . 54 THR HA H 4.30 . 1 355 . 54 THR HB H 3.99 . 1 356 . 54 THR HG1 H 6.15 . 1 357 . 54 THR HG2 H 1.17 . 1 358 . 54 THR N N 125.64 . 1 359 . 55 LEU H H 9.16 . 1 360 . 55 LEU HA H 4.39 . 1 361 . 55 LEU HB2 H 1.14 . 2 362 . 55 LEU HB3 H 1.56 . 2 363 . 55 LEU HG H 1.42 . 1 364 . 55 LEU HD1 H 0.68 . 2 365 . 55 LEU HD2 H 0.83 . 2 366 . 55 LEU N N 132.20 . 1 367 . 56 MET H H 7.91 . 1 368 . 56 MET HA H 5.11 . 1 369 . 56 MET HB2 H 1.87 . 2 370 . 56 MET HB3 H 2.26 . 2 371 . 56 MET HG2 H 2.61 . 2 372 . 56 MET HG3 H 2.92 . 2 373 . 56 MET HE H 2.17 . 1 374 . 56 MET N N 126.97 . 1 375 . 57 PRO HA H 3.70 . 1 376 . 57 PRO HB2 H 2.09 . 1 377 . 57 PRO HB3 H 2.09 . 1 378 . 57 PRO HG2 H 2.36 . 1 379 . 57 PRO HG3 H 2.36 . 1 380 . 58 ASP H H 7.96 . 1 381 . 58 ASP HA H 4.49 . 1 382 . 58 ASP HB2 H 2.67 . 2 383 . 58 ASP HB3 H 2.94 . 2 384 . 58 ASP N N 111.16 . 1 385 . 59 MET H H 8.17 . 1 386 . 59 MET HA H 4.60 . 1 387 . 59 MET HB2 H 2.17 . 2 388 . 59 MET HB3 H 2.18 . 2 389 . 59 MET HG2 H 2.34 . 2 390 . 59 MET HG3 H 2.71 . 2 391 . 59 MET HE H 1.86 . 1 392 . 59 MET N N 118.68 . 1 393 . 60 VAL H H 7.22 . 1 394 . 60 VAL HA H 4.42 . 1 395 . 60 VAL HB H 1.86 . 1 396 . 60 VAL HG1 H 0.62 . 2 397 . 60 VAL HG2 H 0.97 . 2 398 . 60 VAL N N 119.22 . 1 399 . 61 LYS H H 9.17 . 1 400 . 61 LYS HA H 4.15 . 1 401 . 61 LYS HB2 H 1.78 . 1 402 . 61 LYS HB3 H 1.78 . 1 403 . 61 LYS HG2 H 1.29 . 2 404 . 61 LYS HG3 H 1.48 . 2 405 . 61 LYS HD2 H 1.64 . 1 406 . 61 LYS HD3 H 1.64 . 1 407 . 61 LYS HE2 H 2.82 . 2 408 . 61 LYS HE3 H 2.97 . 2 409 . 61 LYS N N 129.68 . 1 410 . 62 ASN H H 9.30 . 1 411 . 62 ASN HA H 4.43 . 1 412 . 62 ASN HB2 H 3.09 . 1 413 . 62 ASN HB3 H 3.09 . 1 414 . 62 ASN HD21 H 7.05 . 2 415 . 62 ASN HD22 H 7.76 . 2 416 . 62 ASN N N 119.06 . 1 417 . 62 ASN ND2 N 114.11 . 1 418 . 63 TYR H H 7.76 . 1 419 . 63 TYR HA H 4.14 . 1 420 . 63 TYR HB2 H 2.86 . 2 421 . 63 TYR HB3 H 3.11 . 2 422 . 63 TYR HD1 H 6.95 . 1 423 . 63 TYR HD2 H 6.95 . 1 424 . 63 TYR HE1 H 6.72 . 1 425 . 63 TYR HE2 H 6.72 . 1 426 . 63 TYR N N 121.65 . 1 427 . 64 GLU H H 8.44 . 1 428 . 64 GLU HA H 4.18 . 1 429 . 64 GLU HB2 H 1.86 . 2 430 . 64 GLU HB3 H 2.00 . 2 431 . 64 GLU HG2 H 2.15 . 2 432 . 64 GLU HG3 H 2.22 . 2 433 . 64 GLU N N 123.63 . 1 434 . 65 ASP H H 8.24 . 1 435 . 65 ASP HA H 4.52 . 1 436 . 65 ASP HB2 H 2.75 . 1 437 . 65 ASP HB3 H 2.75 . 1 438 . 65 ASP N N 122.55 . 1 439 . 66 GLY H H 8.56 . 1 440 . 66 GLY HA2 H 3.96 . 2 441 . 66 GLY HA3 H 5.02 . 2 442 . 66 GLY N N 110.05 . 1 443 . 67 THR H H 8.29 . 1 444 . 67 THR HA H 4.36 . 1 445 . 67 THR HB H 4.26 . 1 446 . 67 THR HG1 H 5.02 . 1 447 . 67 THR HG2 H 1.12 . 1 448 . 67 THR N N 114.45 . 1 449 . 68 THR H H 8.28 . 1 450 . 68 THR HA H 4.36 . 1 451 . 68 THR HB H 4.24 . 1 452 . 68 THR HG1 H 5.02 . 1 453 . 68 THR HG2 H 1.22 . 1 454 . 68 THR N N 117.23 . 1 455 . 69 SER H H 8.49 . 1 456 . 69 SER HA H 5.02 . 1 457 . 69 SER HB2 H 3.87 . 2 458 . 69 SER HB3 H 4.79 . 2 459 . 69 SER N N 120.75 . 1 460 . 70 PRO HA H 4.48 . 1 461 . 70 PRO HB2 H 2.06 . 2 462 . 70 PRO HB3 H 2.29 . 2 463 . 70 PRO HG2 H 2.13 . 1 464 . 70 PRO HG3 H 2.13 . 1 465 . 70 PRO HD2 H 3.75 . 2 466 . 70 PRO HD3 H 3.84 . 2 467 . 71 GLY H H 8.56 . 1 468 . 71 GLY HA2 H 3.96 . 2 469 . 71 GLY HA3 H 5.02 . 2 470 . 71 GLY N N 110.05 . 1 471 . 72 LEU H H 8.23 . 1 472 . 72 LEU HA H 4.40 . 1 473 . 72 LEU HB2 H 1.66 . 1 474 . 72 LEU HB3 H 1.66 . 1 475 . 72 LEU HG H 1.71 . 1 476 . 72 LEU HD1 H 0.90 . 2 477 . 72 LEU HD2 H 0.93 . 2 478 . 72 LEU N N 123.17 . 1 479 . 73 LYS H H 8.04 . 1 480 . 73 LYS HA H 4.21 . 1 481 . 73 LYS HB2 H 1.75 . 1 482 . 73 LYS HB3 H 1.75 . 1 483 . 73 LYS HG2 H 1.42 . 1 484 . 73 LYS HG3 H 1.42 . 1 485 . 73 LYS HD2 H 1.62 . 2 486 . 73 LYS HD3 H 1.66 . 2 487 . 73 LYS HE2 H 3.02 . 1 488 . 73 LYS HE3 H 3.02 . 1 489 . 73 LYS N N 128.50 . 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants_1 _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_two stop_ _Sample_conditions_label $sample_conditions _Spectrometer_frequency_1H 500 _Mol_system_component_name RD3-N1 _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 2 LYS H 2 LYS HA 7.2 . . . 2 3JHNHA 3 ALA H 3 ALA HA 5.2 . . . 3 3JHNHA 4 SER H 4 SER HA 9.3 . . . 4 3JHNHA 5 VAL H 5 VAL HA 6.0 . . . 5 3JHNHA 6 VAL H 6 VAL HA 9.2 . . . 6 3JHNHA 7 ALA H 7 ALA HA 4.2 . . . 7 3JHNHA 8 ASN H 8 ASN HA 8.2 . . . 8 3JHNHA 9 GLN H 9 GLN HA 6.3 . . . 9 3JHNHA 10 LEU H 10 LEU HA 6.7 . . . 10 3JHNHA 11 ILE H 11 ILE HA 8.9 . . . 11 3JHNHA 14 ASN H 14 ASN HA 6.4 . . . 12 3JHNHA 15 THR H 15 THR HA 6.5 . . . 13 3JHNHA 16 ALA H 16 ALA HA 6.1 . . . 14 3JHNHA 18 THR H 18 THR HA 10.1 . . . 15 3JHNHA 20 ILE H 20 ILE HA 4.3 . . . 16 3JHNHA 21 MET H 21 MET HA 6.4 . . . 17 3JHNHA 22 MET H 22 MET HA 8.7 . . . 18 3JHNHA 23 LYS H 23 LYS HA 8.6 . . . 19 3JHNHA 24 ALA H 24 ALA HA 7.4 . . . 20 3JHNHA 25 GLU H 25 GLU HA 8.1 . . . 21 3JHNHA 26 VAL H 26 VAL HA 6.5 . . . 22 3JHNHA 28 THR H 28 THR HA 8.5 . . . 23 3JHNHA 30 MET H 30 MET HA 4.5 . . . 24 3JHNHA 35 GLU H 35 GLU HA 3.7 . . . 25 3JHNHA 36 GLU H 36 GLU HA 7.3 . . . 26 3JHNHA 39 ASN H 39 ASN HA 8.2 . . . 27 3JHNHA 40 LEU H 40 LEU HA 3.7 . . . 28 3JHNHA 43 MET H 43 MET HA 7.4 . . . 29 3JHNHA 44 GLN H 44 GLN HA 7.9 . . . 30 3JHNHA 45 VAL H 45 VAL HA 8.6 . . . 31 3JHNHA 46 ASN H 46 ASN HA 8.0 . . . 32 3JHNHA 47 ARG H 47 ARG HA 6.4 . . . 33 3JHNHA 48 ALA H 48 ALA HA 4.9 . . . 34 3JHNHA 49 VAL H 49 VAL HA 9.3 . . . 35 3JHNHA 53 THR H 53 THR HA 6.3 . . . 36 3JHNHA 54 THR H 54 THR HA 4.8 . . . 37 3JHNHA 55 LEU H 55 LEU HA 7.0 . . . 38 3JHNHA 56 MET H 56 MET HA 8.1 . . . 39 3JHNHA 58 ASP H 58 ASP HA 5.6 . . . 40 3JHNHA 59 MET H 59 MET HA 8.2 . . . 41 3JHNHA 60 VAL H 60 VAL HA 9.1 . . . 42 3JHNHA 61 LYS H 61 LYS HA 4.2 . . . 43 3JHNHA 62 ASN H 62 ASN HA 6.8 . . . 44 3JHNHA 63 TYR H 63 TYR HA 4.7 . . . 45 3JHNHA 64 GLU H 64 GLU HA 7.3 . . . 46 3JHNHA 65 ASP H 65 ASP HA 6.7 . . . 47 3JHNHA 67 THR H 67 THR HA 7.6 . . . 48 3JHNHA 68 THR H 68 THR HA 7.9 . . . 49 3JHNHA 72 LEU H 72 LEU HA 7.2 . . . 50 3JHNHA 73 LYS H 73 LYS HA 7.8 . . . stop_ save_