data_4638 #Corrected using PDB structure: 1IV7A # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 3 W HA 4.73 5.57 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.09 N/A N/A N/A -1.00 -0.15 # #bmr4638.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4638.str file): #HA CA CB CO N HN #N/A N/A N/A N/A -1.00 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.03 N/A N/A N/A +/-0.33 +/-0.05 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.878 N/A N/A N/A 0.916 0.805 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.151 N/A N/A N/A 1.552 0.252 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; SOLUTION STRUCTURE OF MNEI, A SWEET PROTEIN ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Temussi P. A. . 2 Spadaccini R. . . stop_ _BMRB_accession_number 4638 _BMRB_flat_file_name bmr4638.str _Entry_type new _Submission_date 2000-07-12 _Accession_date 2001-03-16 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 3 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 522 '15N chemical shifts' 102 'coupling constants' 114 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Solution structure of a sweet protein: NMR study of MNEI, a single chain monellin ; _Citation_status published _Citation_type Journal _MEDLINE_UI_code . _PubMed_ID 11152608 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Spadaccini R. . . 2 Crescenzi O. O. . 3 tancredi T. . . 4 "De casamassimi" N. . . 5 saviano G. . . 6 scognamiglio R. . . 7 "Di Donato" A. . . 8 Temussi P. A. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full . _Journal_volume 305 _Page_first 505 _Page_last 514 _Year 2001 loop_ _Keyword "5 stranded beta sheet " "1 helix " stop_ save_ ################################## # Molecular system description # ################################## save_system_MNEI _Saveframe_category molecular_system _Mol_system_name "MNEI, A SINGLE CHAIN SWEET PROTEIN" _Abbreviation_common MNEI loop_ _Mol_system_component_name _Mol_label MNEI $MNEI stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1FA3 ? . stop_ save_ ######################## # Monomeric polymers # ######################## save_MNEI _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "MNEI SWEET PROTEIN RELATED TO MONELLIN" _Name_variant . _Abbreviation_common MNEI _Mol_thiol_state 'all free' ############################## # Polymer residue sequence # ############################## _Residue_count 96 _Mol_residue_sequence ; GEWEIIDIGPFTQNLGKFAV DEENKIGQYGRLTFNKVIRP CMKKTIYENEGFREIKGYEY QLYVYASDKLFRADISEDYK TRGRKLLRFNGPVPPP ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 GLU 3 TRP 4 GLU 5 ILE 6 ILE 7 ASP 8 ILE 9 GLY 10 PRO 11 PHE 12 THR 13 GLN 14 ASN 15 LEU 16 GLY 17 LYS 18 PHE 19 ALA 20 VAL 21 ASP 22 GLU 23 GLU 24 ASN 25 LYS 26 ILE 27 GLY 28 GLN 29 TYR 30 GLY 31 ARG 32 LEU 33 THR 34 PHE 35 ASN 36 LYS 37 VAL 38 ILE 39 ARG 40 PRO 41 CYS 42 MET 43 LYS 44 LYS 45 THR 46 ILE 47 TYR 48 GLU 49 ASN 50 GLU 51 GLY 52 PHE 53 ARG 54 GLU 55 ILE 56 LYS 57 GLY 58 TYR 59 GLU 60 TYR 61 GLN 62 LEU 63 TYR 64 VAL 65 TYR 66 ALA 67 SER 68 ASP 69 LYS 70 LEU 71 PHE 72 ARG 73 ALA 74 ASP 75 ILE 76 SER 77 GLU 78 ASP 79 TYR 80 LYS 81 THR 82 ARG 83 GLY 84 ARG 85 LYS 86 LEU 87 LEU 88 ARG 89 PHE 90 ASN 91 GLY 92 PRO 93 VAL 94 PRO 95 PRO 96 PRO stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-07-16 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 1N98 "B Chain B, Crystal Structure Of All-DMonellin At 1.8 A Resolution" 200.00 48 100 100 4e-22 PDB 1KRL "B Chain B, Crystal Structure Of RacemicDl-Monellin In P-1" 192.00 50 100 100 4e-22 PDB 3MON "B Chain B, Monellin" 192.00 50 100 100 2e-23 PDB 4MON "B Chain B, Orthorhombic Monellin" 192.00 50 100 100 2e-23 PDB 1MNL "High-Resolution Solution Structure Of ASweet Protein Single-Chain Monellin (Scm) Determined ByNuclear Magnetic Resonance Spectroscopy And DynamicalSimulated Annealing Calculations, 21 Structures" 102.13 94 98 98 3e-49 PDB 1MOL "A Chain A, Monellin (Single-Chain, Fused)" 102.13 94 98 98 3e-49 PDB 1FA3 "A Chain A, Solution Structure Of Mnei, ASweet Protein" 100.00 96 100 100 4e-52 PDB 1IV7 "A Chain A, Crystal Structure Of Single ChainMonellin" 100.00 96 100 100 4e-52 PDB 1IV9 "A Chain A, Crystal Structure Of Single ChainMonellin" 100.00 96 98 98 8e-51 PDB 1M9G "A Chain A, Solution Structure Of G16a-Mnei,A Structural Mutant Of Single Chain Monellin Mnei" 98.97 97 99 99 2e-51 PIR MLDIB "monellin chain B [validated] - serendipityberry" 188.24 51 100 100 4e-22 PRF 761801B "monellin B" 192.00 50 100 100 2e-23 SWISS-PROT P02882 "MONB_DIOCU Monellin chain B (Monellin chainII)" 192.00 50 100 100 4e-22 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $MNEI "serendipity berry" . Eukaryota Viridiplantae Discoreophyllum cuminsii 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 $MNEI 'recombinant technology' 'E. coli' Escherichia coli . PET-22B+ stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $MNEI 2 mM [U-15N] "phosphate buffer K" 18.5 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $MNEI 2 mM . "phosphate buffer K" 18.5 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $MNEI 2 mM . "phosphate buffer K" 18.5 mM . D2O 100 % . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 1.7 loop_ _Task processing stop_ _Details Delaglio save_ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task "structure solution" stop_ _Details Guentert save_ save_AMBER_ _Saveframe_category software _Name "AMBER " _Version 5.0 loop_ _Task refinement stop_ _Details Kollman save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Details ; 3D 15N-separated NOESY HNHA HSQC HNHB E-COSY 2D NOESY ; save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2.9 . n/a temperature 308 . K 'ionic strength' 18.5 . mM pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_ref_1 _Saveframe_category chemical_shift_reference 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 . H 1 . ppm . . . . . . . . N 15 . ppm . . . . . . . stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_ref_1 _Mol_system_component_name MNEI loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 GLY HA2 H 4.17 0.000 . 2 1 GLY H H 8.97 0.000 . 3 1 GLY N N 111.88 0.000 . 4 2 GLU HA H 4.44 0.000 . 5 2 GLU HB2 H 2.16 0.000 . 6 2 GLU HB3 H 2.06 0.000 . 7 2 GLU HG2 H 2.43 0.000 . 8 2 GLU H H 8.62 0.000 . 9 2 GLU N N 119.76 0.000 . 10 3 TRP HA H 4.82 0.000 . 11 3 TRP HB2 H 3.17 0.000 . 12 3 TRP HD1 H 7.42 0.000 . 13 3 TRP HE1 H 10.11 0.000 . 14 3 TRP HE3 H 7.33 0.000 . 15 3 TRP H H 8.24 0.000 . 16 3 TRP HZ2 H 6.91 0.000 . 17 3 TRP HZ3 H 6.92 0.000 . 18 3 TRP NE1 N 130.03 0.000 . 19 3 TRP N N 120.01 0.000 . 20 4 GLU HA H 4.93 0.000 . 21 4 GLU HB2 H 2.25 0.000 . 22 4 GLU HB3 H 2.13 0.000 . 23 4 GLU HG2 H 2.58 0.000 . 24 4 GLU H H 9.51 0.000 . 25 4 GLU N N 121.85 0.000 . 26 5 ILE HA H 4.85 0.000 . 27 5 ILE HB H 1.97 0.000 . 28 5 ILE HG12 H 1.78 0.000 . 29 5 ILE HG13 H 1.38 0.000 . 30 5 ILE H H 8.75 0.000 . 31 5 ILE HD1 H 0.99 0.000 1 32 5 ILE HG2 H 1.12 0.000 1 33 5 ILE N N 124.47 0.000 . 34 6 ILE HA H 4.88 0.000 . 35 6 ILE HB H 2.11 0.000 . 36 6 ILE HG12 H 1.54 0.000 . 37 6 ILE H H 8.57 0.000 . 38 6 ILE HD1 H 1.11 0.000 1 39 6 ILE HG2 H 1.04 0.000 1 40 6 ILE N N 122.24 0.000 . 41 7 ASP HA H 4.79 0.000 . 42 7 ASP HB2 H 2.88 0.000 . 43 7 ASP H H 8.35 0.000 . 44 7 ASP N N 119.64 0.000 . 45 8 ILE HA H 4.58 0.000 . 46 8 ILE HB H 2.01 0.000 . 47 8 ILE HG12 H 1.58 0.000 . 48 8 ILE HG13 H 1.38 0.000 . 49 8 ILE H H 8.13 0.000 . 50 8 ILE HD1 H 0.95 0.000 1 51 8 ILE HG2 H 0.99 0.000 1 52 8 ILE N N 116.86 0.000 . 53 9 GLY HA2 H 4.32 0.000 . 54 9 GLY H H 8.12 0.000 . 55 9 GLY N N 112.66 0.000 . 56 10 PRO HA H 4.29 0.000 . 57 10 PRO HB2 H 2.30 0.000 . 58 10 PRO HB3 H 2.51 0.000 . 59 10 PRO HD2 H 3.89 0.000 . 60 10 PRO HD3 H 3.76 0.000 . 61 10 PRO HG2 H 2.14 0.000 . 62 11 PHE HA H 4.33 0.000 . 63 11 PHE HB2 H 3.33 0.000 . 64 11 PHE HB3 H 3.13 0.000 . 65 11 PHE HD1 H 7.16 0.000 1 66 11 PHE HD2 H 7.16 0.000 1 67 11 PHE H H 8.58 0.000 . 68 11 PHE N N 117.37 0.000 . 69 12 THR HA H 3.75 0.000 . 70 12 THR HB H 4.39 0.000 . 71 12 THR H H 7.79 0.000 . 72 12 THR HG2 H 1.51 0.000 1 73 12 THR N N 112.47 0.000 . 74 13 GLN HA H 4.29 0.000 . 75 13 GLN HB2 H 2.40 0.000 . 76 13 GLN HB3 H 2.23 0.000 . 77 13 GLN HG2 H 2.63 0.000 . 78 13 GLN H H 8.51 0.000 . 79 13 GLN N N 120.81 0.000 . 80 14 ASN HA H 4.31 0.000 . 81 14 ASN HB2 H 2.88 0.000 . 82 14 ASN HB3 H 2.71 0.000 . 83 14 ASN HD21 H 7.48 0.000 . 84 14 ASN HD22 H 6.95 0.000 . 85 14 ASN H H 8.05 0.000 . 86 14 ASN ND2 N 113.13 0.000 . 87 14 ASN N N 116.73 0.000 . 88 15 LEU HA H 3.89 0.000 . 89 15 LEU HB2 H 1.85 0.000 . 90 15 LEU HG H 1.10 0.000 . 91 15 LEU H H 7.54 0.000 . 92 15 LEU HD1 H 0.24 0.000 1 93 15 LEU HD2 H -0.03 0.000 1 94 15 LEU N N 121.62 0.000 . 95 16 GLY HA2 H 3.56 0.000 . 96 16 GLY H H 7.98 0.000 . 97 16 GLY N N 106.65 0.000 . 98 17 LYS HA H 3.14 0.000 . 99 17 LYS HB2 H 1.23 0.000 . 100 17 LYS HD2 H 1.61 0.000 . 101 17 LYS HG2 H 0.83 0.000 . 102 17 LYS H H 7.61 0.000 . 103 17 LYS N N 122.49 0.000 . 104 18 PHE HA H 4.29 0.000 . 105 18 PHE HB2 H 3.29 0.000 . 106 18 PHE HD1 H 7.24 0.000 1 107 18 PHE HD2 H 7.24 0.000 1 108 18 PHE HE1 H 7.16 0.000 1 109 18 PHE HE2 H 7.16 0.000 1 110 18 PHE H H 7.81 0.000 . 111 18 PHE HZ H 7.11 0.000 . 112 18 PHE N N 119.50 0.000 . 113 19 ALA HA H 3.66 0.000 . 114 19 ALA H H 8.21 0.000 . 115 19 ALA HB H 1.64 0.000 1 116 19 ALA N N 120.42 0.000 . 117 20 VAL HA H 3.06 0.000 . 118 20 VAL HB H 2.12 0.000 . 119 20 VAL H H 7.84 0.000 . 120 20 VAL HG1 H 1.20 0.000 1 121 20 VAL HG2 H 0.82 0.000 1 122 20 VAL N N 115.96 0.000 . 123 21 ASP HA H 4.33 0.000 . 124 21 ASP HB2 H 2.92 0.000 . 125 21 ASP HB3 H 2.71 0.000 . 126 21 ASP H H 8.55 0.000 . 127 21 ASP N N 120.01 0.000 . 128 22 GLU HA H 3.90 0.000 . 129 22 GLU HB2 H 1.65 0.000 . 130 22 GLU HB3 H 1.77 0.000 . 131 22 GLU H H 8.32 0.000 . 132 22 GLU N N 118.22 0.000 . 133 23 GLU HA H 3.88 0.000 . 134 23 GLU HB2 H 1.22 0.000 . 135 23 GLU HB3 H 1.08 0.000 . 136 23 GLU HG2 H 1.79 0.000 . 137 23 GLU H H 8.37 0.000 . 138 23 GLU N N 121.96 0.000 . 139 24 ASN HA H 4.64 0.000 . 140 24 ASN HB2 H 2.98 0.000 . 141 24 ASN HB3 H 2.72 0.000 . 142 24 ASN H H 8.76 0.000 . 143 24 ASN N N 121.66 0.000 . 144 25 LYS HA H 4.12 0.000 . 145 25 LYS HB2 H 1.97 0.000 . 146 25 LYS HD2 H 1.67 0.000 . 147 25 LYS HE2 H 2.95 0.000 . 148 25 LYS HG2 H 1.44 0.000 . 149 25 LYS H H 7.25 0.000 . 150 25 LYS N N 119.09 0.000 . 151 26 ILE HA H 3.92 0.000 . 152 26 ILE HB H 1.92 0.000 . 153 26 ILE HG12 H 1.65 0.000 . 154 26 ILE HG13 H 1.20 0.000 . 155 26 ILE H H 7.35 0.000 . 156 26 ILE HD1 H 0.88 0.000 1 157 26 ILE HG2 H 1.04 0.000 1 158 26 ILE N N 118.80 0.000 . 159 27 GLY HA2 H 4.14 0.000 . 160 27 GLY HA3 H 3.84 0.000 . 161 27 GLY H H 8.22 0.000 . 162 27 GLY N N 103.90 0.000 . 163 28 GLN HA H 4.01 0.000 . 164 28 GLN HB2 H 1.78 0.000 . 165 28 GLN HG2 H 2.00 0.000 . 166 28 GLN H H 6.86 0.000 . 167 28 GLN N N 118.64 0.000 . 168 29 TYR HA H 4.78 0.000 . 169 29 TYR HB2 H 3.50 0.000 . 170 29 TYR HB3 H 2.39 0.000 . 171 29 TYR HD1 H 7.15 0.000 1 172 29 TYR HD2 H 7.15 0.000 1 173 29 TYR HE1 H 7.17 0.000 1 174 29 TYR HE2 H 7.17 0.000 1 175 29 TYR H H 8.55 0.000 . 176 29 TYR N N 116.31 0.000 . 177 30 GLY HA2 H 4.15 0.000 . 178 30 GLY HA3 H 3.76 0.000 . 179 30 GLY H H 7.34 0.000 . 180 30 GLY N N 106.33 0.000 . 181 31 ARG HA H 4.30 0.000 . 182 31 ARG HB2 H 1.80 0.000 . 183 31 ARG HB3 H 1.69 0.000 . 184 31 ARG HD2 H 3.18 0.000 . 185 31 ARG HG2 H 1.52 0.000 . 186 31 ARG H H 8.45 0.000 . 187 31 ARG HE H 7.16 0.000 . 188 31 ARG NE N 115.14 0.000 . 189 31 ARG N N 122.73 0.000 . 190 32 LEU HA H 4.85 0.000 . 191 32 LEU HB2 H 1.74 0.000 . 192 32 LEU HB3 H 1.01 0.000 . 193 32 LEU HG H 1.59 0.000 . 194 32 LEU H H 9.62 0.000 . 195 32 LEU HD1 H 0.85 0.000 1 196 32 LEU HD2 H 0.30 0.000 1 197 32 LEU N N 129.48 0.000 . 198 33 THR HA H 4.54 0.000 . 199 33 THR HB H 4.02 0.000 . 200 33 THR H H 8.40 0.000 . 201 33 THR HG2 H 1.26 0.000 1 202 33 THR N N 117.00 0.000 . 203 34 PHE HA H 4.10 0.000 . 204 34 PHE HB2 H 3.09 0.000 . 205 34 PHE HB3 H 3.03 0.000 . 206 34 PHE HD1 H 7.07 0.000 1 207 34 PHE HD2 H 7.07 0.000 1 208 34 PHE HE1 H 7.25 0.000 1 209 34 PHE HE2 H 7.25 0.000 1 210 34 PHE H H 9.39 0.000 . 211 34 PHE HZ H 7.73 0.000 . 212 34 PHE N N 127.40 0.000 . 213 35 ASN HA H 4.85 0.000 . 214 35 ASN HB2 H 2.81 0.000 . 215 35 ASN HB3 H 2.60 0.000 . 216 35 ASN HD21 H 7.05 0.000 . 217 35 ASN HD22 H 6.95 0.000 . 218 35 ASN H H 8.45 0.000 . 219 35 ASN ND2 N 108.02 0.000 . 220 35 ASN N N 125.00 0.000 . 221 36 LYS HA H 4.44 0.000 . 222 36 LYS HB2 H 2.16 0.000 . 223 36 LYS HD2 H 1.79 0.000 . 224 36 LYS HG2 H 1.20 0.000 . 225 36 LYS H H 7.14 0.000 . 226 36 LYS N N 110.29 0.000 . 227 37 VAL HA H 5.12 0.000 . 228 37 VAL HB H 2.10 0.000 . 229 37 VAL H H 9.18 0.000 . 230 37 VAL HG1 H 1.37 0.000 1 231 37 VAL HG2 H 1.27 0.000 1 232 37 VAL N N 121.23 0.000 . 233 38 ILE HA H 4.90 0.000 . 234 38 ILE HB H 2.20 0.000 . 235 38 ILE HG12 H 2.21 0.000 . 236 38 ILE HG13 H 1.45 0.000 . 237 38 ILE H H 7.88 0.000 . 238 38 ILE HD1 H 0.79 0.000 1 239 38 ILE HG2 H 1.08 0.000 1 240 38 ILE N N 117.23 0.000 . 241 39 ARG HA H 4.41 0.000 . 242 39 ARG HB2 H 1.83 0.000 . 243 39 ARG HD2 H 3.33 0.000 . 244 39 ARG HG2 H 1.93 0.000 . 245 39 ARG H H 8.26 0.000 . 246 39 ARG HE H 7.42 0.000 . 247 39 ARG NE N 115.83 0.000 . 248 39 ARG N N 118.95 0.000 . 249 40 PRO HA H 4.85 0.000 . 250 40 PRO HB2 H 2.42 0.000 . 251 40 PRO HB3 H 1.95 0.000 . 252 41 CYS HA H 5.02 0.000 . 253 41 CYS HB2 H 3.06 0.000 . 254 41 CYS HB3 H 2.88 0.000 . 255 41 CYS HG H 2.11 0.000 . 256 41 CYS H H 9.19 0.000 . 257 41 CYS N N 124.79 0.000 . 258 42 MET HA H 5.86 0.000 . 259 42 MET HB2 H 1.89 0.000 . 260 42 MET HG2 H 2.46 0.000 . 261 42 MET HG3 H 2.27 0.000 . 262 42 MET H H 8.35 0.000 . 263 42 MET N N 123.01 0.000 . 264 43 LYS HA H 5.70 0.000 . 265 43 LYS HB2 H 1.73 0.000 . 266 43 LYS HB3 H 1.66 0.000 . 267 43 LYS HD2 H 1.46 0.000 . 268 43 LYS HE2 H 2.59 0.000 . 269 43 LYS HE3 H 2.45 0.000 . 270 43 LYS HG2 H 1.11 0.000 . 271 43 LYS HG3 H 0.86 0.000 . 272 43 LYS H H 9.76 0.000 . 273 43 LYS N N 122.92 0.000 . 274 44 LYS HA H 4.75 0.000 . 275 44 LYS HB2 H 0.74 0.000 . 276 44 LYS HB3 H 0.46 0.000 . 277 44 LYS HD2 H 0.59 0.000 . 278 44 LYS HE2 H 2.23 0.000 . 279 44 LYS HE3 H 2.07 0.000 . 280 44 LYS HG2 H 0.56 0.000 . 281 44 LYS H H 9.35 0.000 . 282 44 LYS N N 127.21 0.000 . 283 45 THR HA H 4.33 0.000 . 284 45 THR HB H 3.82 0.000 . 285 45 THR H H 8.60 0.000 . 286 45 THR HG2 H 0.56 0.000 1 287 45 THR N N 121.99 0.000 . 288 46 ILE HA H 4.11 0.000 . 289 46 ILE HB H 1.43 0.000 . 290 46 ILE HG12 H 1.18 0.000 . 291 46 ILE HG13 H 0.97 0.000 . 292 46 ILE H H 8.49 0.000 . 293 46 ILE HD1 H 0.61 0.000 1 294 46 ILE HG2 H 0.81 0.000 1 295 46 ILE N N 126.48 0.000 . 296 47 TYR HA H 4.89 0.000 . 297 47 TYR HB2 H 3.01 0.000 . 298 47 TYR HB3 H 2.70 0.000 . 299 47 TYR HD1 H 6.88 0.000 1 300 47 TYR HD2 H 6.88 0.000 1 301 47 TYR HE1 H 6.63 0.000 1 302 47 TYR HE2 H 6.63 0.000 1 303 47 TYR H H 8.75 0.000 . 304 47 TYR N N 126.21 0.000 . 305 48 GLU HA H 4.40 0.000 . 306 48 GLU HB2 H 2.00 0.000 . 307 48 GLU HB3 H 2.12 0.000 . 308 48 GLU HG2 H 2.41 0.000 . 309 48 GLU HG3 H 2.36 0.000 . 310 48 GLU H H 8.84 0.000 . 311 48 GLU N N 119.15 0.000 . 312 49 ASN HA H 4.76 0.000 . 313 49 ASN HB2 H 2.95 0.000 . 314 49 ASN HB3 H 2.82 0.000 . 315 49 ASN HD21 H 7.61 0.000 . 316 49 ASN HD22 H 6.85 0.000 . 317 49 ASN H H 8.54 0.000 . 318 49 ASN ND2 N 113.61 0.000 . 319 49 ASN N N 118.10 0.000 . 320 50 GLU HA H 4.33 0.000 . 321 50 GLU HB2 H 2.15 0.000 . 322 50 GLU HB3 H 1.94 0.000 . 323 50 GLU HG2 H 2.37 0.000 . 324 50 GLU H H 8.18 0.000 . 325 50 GLU N N 119.86 0.000 . 326 51 GLY HA2 H 4.00 0.000 . 327 51 GLY HA3 H 3.69 0.000 . 328 51 GLY H H 8.30 0.000 . 329 51 GLY N N 109.63 0.000 . 330 52 PHE HA H 4.46 0.000 . 331 52 PHE HB2 H 3.12 0.000 . 332 52 PHE HB3 H 2.92 0.000 . 333 52 PHE HD1 H 7.12 0.000 1 334 52 PHE HD2 H 7.12 0.000 1 335 52 PHE HE1 H 7.36 0.000 1 336 52 PHE HE2 H 7.36 0.000 1 337 52 PHE H H 7.92 0.000 . 338 52 PHE HZ H 7.34 0.000 . 339 52 PHE N N 118.52 0.000 . 340 53 ARG HA H 4.14 0.000 . 341 53 ARG HB2 H 1.76 0.000 . 342 53 ARG HD2 H 3.00 0.000 . 343 53 ARG HG2 H 1.38 0.000 . 344 53 ARG H H 8.26 0.000 . 345 53 ARG HE H 7.00 0.000 . 346 53 ARG NE N 115.82 0.000 . 347 53 ARG N N 119.84 0.000 . 348 54 GLU HA H 4.59 0.000 . 349 54 GLU HB2 H 2.03 0.000 . 350 54 GLU HG2 H 2.40 0.000 . 351 54 GLU H H 8.30 0.000 . 352 54 GLU N N 120.74 0.000 . 353 55 ILE HA H 3.54 0.000 . 354 55 ILE HB H 0.75 0.000 . 355 55 ILE HG12 H 0.43 0.000 . 356 55 ILE HG13 H 1.45 0.000 . 357 55 ILE H H 8.46 0.000 . 358 55 ILE HD1 H 0.73 0.000 1 359 55 ILE HG2 H 0.18 0.000 1 360 55 ILE N N 126.41 0.000 . 361 56 LYS HA H 4.41 0.000 . 362 56 LYS HB2 H 1.42 0.000 . 363 56 LYS HD2 H 1.59 0.000 . 364 56 LYS HE2 H 2.99 0.000 . 365 56 LYS HG2 H 1.42 0.000 . 366 56 LYS H H 9.08 0.000 . 367 56 LYS N N 126.86 0.000 . 368 57 GLY HA2 H 4.58 0.000 . 369 57 GLY HA3 H 3.61 0.000 . 370 57 GLY H H 7.69 0.000 . 371 57 GLY N N 107.04 0.000 . 372 58 TYR HA H 5.50 0.000 . 373 58 TYR HB2 H 2.62 0.000 . 374 58 TYR HB3 H 2.49 0.000 . 375 58 TYR HD1 H 7.06 0.000 1 376 58 TYR HD2 H 7.06 0.000 1 377 58 TYR HE1 H 6.81 0.000 1 378 58 TYR HE2 H 6.81 0.000 1 379 58 TYR H H 8.92 0.000 . 380 58 TYR N N 115.46 0.000 . 381 59 GLU HA H 5.45 0.000 . 382 59 GLU HB2 H 1.88 0.000 . 383 59 GLU HB3 H 1.82 0.000 . 384 59 GLU HG2 H 2.46 0.000 . 385 59 GLU H H 9.07 0.000 . 386 59 GLU N N 121.91 0.000 . 387 60 TYR HA H 5.96 0.000 . 388 60 TYR HB2 H 2.92 0.000 . 389 60 TYR HB3 H 2.77 0.000 . 390 60 TYR HD1 H 6.96 0.000 1 391 60 TYR HD2 H 6.96 0.000 1 392 60 TYR HE1 H 6.77 0.000 1 393 60 TYR HE2 H 6.77 0.000 1 394 60 TYR H H 9.72 0.000 . 395 60 TYR N N 121.75 0.000 . 396 61 GLN HA H 5.51 0.000 . 397 61 GLN HB2 H 1.59 0.000 . 398 61 GLN HB3 H 1.47 0.000 . 399 61 GLN HG2 H 1.88 0.000 . 400 61 GLN HG3 H 1.83 0.000 . 401 61 GLN H H 9.18 0.000 . 402 61 GLN N N 121.54 0.000 . 403 62 LEU HA H 5.32 0.000 . 404 62 LEU HB2 H 1.73 0.000 . 405 62 LEU HB3 H 1.63 0.000 . 406 62 LEU HG H 1.78 0.000 . 407 62 LEU H H 9.31 0.000 . 408 62 LEU HD1 H 0.97 0.000 1 409 62 LEU HD2 H 0.86 0.000 1 410 62 LEU N N 125.74 0.000 . 411 63 TYR HA H 5.04 0.000 . 412 63 TYR HB2 H 2.86 0.000 . 413 63 TYR HB3 H 2.63 0.000 . 414 63 TYR HD1 H 7.03 0.000 1 415 63 TYR HD2 H 7.03 0.000 1 416 63 TYR HE1 H 6.70 0.000 1 417 63 TYR HE2 H 6.70 0.000 1 418 63 TYR H H 9.71 0.000 . 419 63 TYR N N 123.38 0.000 . 420 64 VAL HA H 4.80 0.000 . 421 64 VAL HB H 1.93 0.000 . 422 64 VAL H H 9.14 0.000 . 423 64 VAL HG1 H 1.04 0.000 1 424 64 VAL N N 121.34 0.000 . 425 65 TYR HA H 5.59 0.000 . 426 65 TYR HB2 H 3.19 0.000 . 427 65 TYR HB3 H 2.79 0.000 . 428 65 TYR HD1 H 6.75 0.000 1 429 65 TYR HD2 H 6.75 0.000 1 430 65 TYR H H 9.46 0.000 . 431 65 TYR N N 127.01 0.000 . 432 66 ALA HA H 5.14 0.000 . 433 66 ALA H H 9.92 0.000 . 434 66 ALA HB H 1.41 0.000 1 435 66 ALA N N 127.70 0.000 . 436 67 SER HA H 4.20 0.000 . 437 67 SER HB2 H 4.36 0.000 . 438 67 SER HB3 H 4.11 0.000 . 439 67 SER H H 9.48 0.000 . 440 67 SER N N 117.52 0.000 . 441 68 ASP HA H 4.12 0.000 . 442 68 ASP HB2 H 3.21 0.000 . 443 68 ASP HB3 H 3.11 0.000 . 444 68 ASP H H 9.33 0.000 . 445 68 ASP N N 109.46 0.000 . 446 69 LYS HA H 4.62 0.000 . 447 69 LYS HB2 H 1.97 0.000 . 448 69 LYS HD2 H 1.22 0.000 . 449 69 LYS HE2 H 3.18 0.000 . 450 69 LYS HG2 H 1.48 0.000 . 451 69 LYS H H 8.30 0.000 . 452 69 LYS N N 120.97 0.000 . 453 70 LEU HA H 4.36 0.000 . 454 70 LEU HB2 H 1.99 0.000 . 455 70 LEU HG H 1.16 0.000 . 456 70 LEU H H 8.16 0.000 . 457 70 LEU HD1 H 0.68 0.000 1 458 70 LEU HD2 H 0.13 0.000 1 459 70 LEU N N 123.01 0.000 . 460 71 PHE HA H 4.84 0.000 . 461 71 PHE HB2 H 2.06 0.000 . 462 71 PHE HB3 H 1.75 0.000 . 463 71 PHE HD1 H 6.73 0.000 1 464 71 PHE HD2 H 6.73 0.000 1 465 71 PHE HE1 H 6.92 0.000 1 466 71 PHE HE2 H 6.92 0.000 1 467 71 PHE H H 9.01 0.000 . 468 71 PHE N N 123.54 0.000 . 469 72 ARG HA H 4.95 0.000 . 470 72 ARG HB2 H 1.69 0.000 . 471 72 ARG HB3 H 1.27 0.000 . 472 72 ARG HD2 H 2.71 0.000 . 473 72 ARG HG2 H 1.06 0.000 . 474 72 ARG HG3 H 1.00 0.000 . 475 72 ARG H H 8.72 0.000 . 476 72 ARG HE H 6.57 0.000 . 477 72 ARG NE N 114.43 0.000 . 478 72 ARG N N 120.01 0.000 . 479 73 ALA HA H 5.38 0.000 . 480 73 ALA H H 9.08 0.000 . 481 73 ALA HB H 1.27 0.000 1 482 73 ALA N N 127.22 0.000 . 483 74 ASP HA H 6.29 0.000 . 484 74 ASP HB2 H 3.00 0.000 . 485 74 ASP HB3 H 2.69 0.000 . 486 74 ASP H H 8.82 0.000 . 487 74 ASP N N 120.15 0.000 . 488 75 ILE HA H 5.32 0.000 . 489 75 ILE HB H 1.90 0.000 . 490 75 ILE HG12 H 1.76 0.000 . 491 75 ILE HG13 H 1.35 0.000 . 492 75 ILE H H 9.60 0.000 . 493 75 ILE HD1 H 1.08 0.000 1 494 75 ILE HG2 H 1.09 0.000 1 495 75 ILE N N 125.35 0.000 . 496 76 SER HA H 5.65 0.000 . 497 76 SER HB2 H 4.12 0.000 . 498 76 SER HB3 H 3.87 0.000 . 499 76 SER H H 9.59 0.000 . 500 76 SER N N 120.85 0.000 . 501 77 GLU HA H 5.32 0.000 . 502 77 GLU HB2 H 2.32 0.000 . 503 77 GLU HB3 H 2.06 0.000 . 504 77 GLU HG2 H 2.25 0.000 . 505 77 GLU H H 9.16 0.000 . 506 77 GLU N N 123.00 0.000 . 507 78 ASP HA H 4.82 0.000 . 508 78 ASP HB2 H 2.87 0.000 . 509 78 ASP HB3 H 2.81 0.000 . 510 78 ASP H H 8.70 0.000 . 511 78 ASP N N 127.29 0.000 . 512 79 TYR HA H 4.24 0.000 . 513 79 TYR HB2 H 2.76 0.000 . 514 79 TYR HB3 H 2.52 0.000 . 515 79 TYR HD1 H 7.01 0.000 1 516 79 TYR HD2 H 7.01 0.000 1 517 79 TYR HE1 H 6.93 0.000 1 518 79 TYR HE2 H 6.93 0.000 1 519 79 TYR H H 8.56 0.000 . 520 79 TYR N N 126.82 0.000 . 521 80 LYS HA H 4.01 0.000 . 522 80 LYS HB2 H 2.03 0.000 . 523 80 LYS HB3 H 1.98 0.000 . 524 80 LYS HD2 H 1.79 0.000 . 525 80 LYS HD3 H 1.65 0.000 . 526 80 LYS HE2 H 3.11 0.000 . 527 80 LYS HG2 H 1.48 0.000 . 528 80 LYS H H 8.42 0.000 . 529 80 LYS N N 116.80 0.000 . 530 81 THR HA H 4.39 0.000 . 531 81 THR HB H 4.41 0.000 . 532 81 THR H H 8.23 0.000 . 533 81 THR HG1 H 5.04 0.000 . 534 81 THR HG2 H 1.29 0.000 1 535 81 THR N N 106.36 0.000 . 536 82 ARG HA H 4.23 0.000 . 537 82 ARG HB2 H 2.19 0.000 . 538 82 ARG HB3 H 2.10 0.000 . 539 82 ARG HD2 H 3.23 0.000 . 540 82 ARG HD3 H 3.17 0.000 . 541 82 ARG HG2 H 1.60 0.000 . 542 82 ARG H H 7.79 0.000 . 543 82 ARG HE H 7.08 0.000 . 544 82 ARG NE N 115.88 0.000 . 545 82 ARG N N 115.36 0.000 . 546 83 GLY HA2 H 4.03 0.000 . 547 83 GLY HA3 H 3.71 0.000 . 548 83 GLY H H 8.36 0.000 . 549 83 GLY N N 106.82 0.000 . 550 84 ARG HA H 5.50 0.000 . 551 84 ARG HB2 H 1.01 0.000 . 552 84 ARG HD2 H 2.46 0.000 . 553 84 ARG HG2 H 1.55 0.000 . 554 84 ARG HG3 H 1.22 0.000 . 555 84 ARG H H 8.36 0.000 . 556 84 ARG HE H 7.08 0.000 . 557 84 ARG NE N 115.76 0.000 . 558 84 ARG N N 122.71 0.000 . 559 85 LYS HA H 4.85 0.000 . 560 85 LYS HB2 H 1.86 0.000 . 561 85 LYS HD2 H 1.74 0.000 . 562 85 LYS HE2 H 3.04 0.000 . 563 85 LYS HG2 H 1.48 0.000 . 564 85 LYS HG3 H 1.36 0.000 . 565 85 LYS H H 8.74 0.000 . 566 85 LYS N N 119.75 0.000 . 567 86 LEU HA H 4.76 0.000 . 568 86 LEU HB2 H 2.18 0.000 . 569 86 LEU HB3 H 1.13 0.000 . 570 86 LEU HG H 1.51 0.000 . 571 86 LEU H H 9.50 0.000 . 572 86 LEU HD1 H 1.27 0.000 1 573 86 LEU HD2 H 1.01 0.000 1 574 86 LEU N N 126.48 0.000 . 575 87 LEU HA H 4.54 0.000 . 576 87 LEU HB2 H 1.74 0.000 . 577 87 LEU HB3 H 1.63 0.000 . 578 87 LEU HG H 1.76 0.000 . 579 87 LEU H H 9.21 0.000 . 580 87 LEU HD1 H 0.93 0.000 1 581 87 LEU N N 128.89 0.000 . 582 88 ARG HA H 4.68 0.000 . 583 88 ARG HB2 H 1.96 0.000 . 584 88 ARG HD2 H 3.27 0.000 . 585 88 ARG HG2 H 1.71 0.000 . 586 88 ARG H H 7.78 0.000 . 587 88 ARG HE H 7.27 0.000 . 588 88 ARG NE N 115.24 0.000 . 589 88 ARG N N 114.45 0.000 . 590 89 PHE HA H 5.12 0.000 . 591 89 PHE HB2 H 3.40 0.000 . 592 89 PHE HB3 H 2.75 0.000 . 593 89 PHE HD1 H 6.83 0.000 1 594 89 PHE HD2 H 6.83 0.000 1 595 89 PHE HE1 H 5.97 0.000 1 596 89 PHE HE2 H 5.97 0.000 1 597 89 PHE H H 8.77 0.000 . 598 89 PHE HZ H 6.13 0.000 . 599 89 PHE N N 127.13 0.000 . 600 90 ASN HA H 5.61 0.000 . 601 90 ASN HB2 H 2.83 0.000 . 602 90 ASN HB3 H 2.68 0.000 . 603 90 ASN HD21 H 7.62 0.000 . 604 90 ASN HD22 H 6.92 0.000 . 605 90 ASN H H 8.83 0.000 . 606 90 ASN ND2 N 112.80 0.000 . 607 90 ASN N N 123.67 0.000 . 608 91 GLY HA2 H 4.41 0.000 . 609 91 GLY HA3 H 3.61 0.000 . 610 91 GLY H H 8.21 0.000 . 611 91 GLY N N 107.35 0.000 . 612 92 PRO HA H 4.53 0.000 . 613 92 PRO HB2 H 2.12 0.000 . 614 92 PRO HB3 H 1.94 0.000 . 615 92 PRO HD2 H 3.16 0.000 . 616 92 PRO HD3 H 2.95 0.000 . 617 93 VAL HA H 4.89 0.000 . 618 93 VAL HB H 2.30 0.000 . 619 93 VAL H H 8.62 0.000 . 620 93 VAL HG1 H 0.97 0.000 1 621 93 VAL HG2 H 0.70 0.000 1 622 93 VAL N N 118.30 0.000 . 623 94 PRO HD2 H 3.81 0.000 . 624 94 PRO HD3 H 3.61 0.000 . stop_ save_ ######################## # Coupling constants # ######################## save_JHNHA _Saveframe_category coupling_constants loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Spectrometer_frequency_1H 600 _Mol_system_component_name MNEI 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_value_error 1 3JHNHA 4 GLU H 4 GLU HA 10.74 . 2 3JHNHA 6 ILE H 6 ILE HA 9.94 . 3 3JHNHA 11 PHE H 11 PHE HA 3.91 . 4 3JHNHA 13 GLN H 13 GLN HA 4.68 . 5 3JHNHA 14 ASN H 14 ASN HA 4.38 . 6 3JHNHA 15 LEU H 15 LEU HA 4.87 . 7 3JHNHA 17 LYS H 17 LYS HA 3.48 . 8 3JHNHA 18 PHE H 18 PHE HA 3.82 . 9 3JHNHA 19 ALA H 19 ALA HA 3.38 . 10 3JHNHA 21 ASP H 21 ASP HA 3.67 . 11 3JHNHA 23 GLU H 23 GLU HA 4.81 . 12 3JHNHA 24 ASN H 24 ASN HA 3.82 . 13 3JHNHA 28 GLN H 28 GLN HA 4.42 . 14 3JHNHA 29 TYR H 29 TYR HA 9.47 . 15 3JHNHA 32 LEU H 32 LEU HA 8.96 . 16 3JHNHA 33 THR H 33 THR HA 8.96 . 17 3JHNHA 34 PHE H 34 PHE HA 3.15 . 18 3JHNHA 35 ASN H 35 ASN HA 11.13 . 19 3JHNHA 36 LYS H 36 LYS HA 4.11 . 20 3JHNHA 38 ILE H 38 ILE HA 10.15 . 21 3JHNHA 39 ARG H 39 ARG HA 5.15 . 22 3JHNHA 41 CYS H 41 CYS HA 9.42 . 23 3JHNHA 42 MET H 42 MET HA 9.32 . 24 3JHNHA 43 LYS H 43 LYS HA 9.52 . 25 3JHNHA 44 LYS H 44 LYS HA 10.37 . 26 3JHNHA 45 THR H 45 THR HA 8.61 . 27 3JHNHA 46 ILE H 46 ILE HA 8.71 . 28 3JHNHA 47 TYR H 47 TYR HA 9.79 . 29 3JHNHA 52 PHE H 52 PHE HA 9.04 . 30 3JHNHA 56 LYS H 56 LYS HA 10.62 . 31 3JHNHA 58 TYR H 58 TYR HA 10.67 . 32 3JHNHA 59 GLU H 59 GLU HA 9.77 . 33 3JHNHA 60 TYR H 60 TYR HA 10.15 . 34 3JHNHA 61 GLN H 61 GLN HA 9.87 . 35 3JHNHA 62 LEU H 62 LEU HA 9.78 . 36 3JHNHA 63 TYR H 63 TYR HA 10.70 . 37 3JHNHA 65 TYR H 65 TYR HA 8.66 . 38 3JHNHA 66 ALA H 66 ALA HA 9.00 . 39 3JHNHA 69 LYS H 69 LYS HA 9.33 . 40 3JHNHA 71 PHE H 71 PHE HA 9.69 . 41 3JHNHA 72 ARG H 72 ARG HA 9.48 . 42 3JHNHA 73 ALA H 73 ALA HA 9.86 . 43 3JHNHA 74 ASP H 74 ASP HA 10.63 . 44 3JHNHA 75 ILE H 75 ILE HA 10.13 . 45 3JHNHA 76 SER H 76 SER HA 9.66 . 46 3JHNHA 77 GLU H 77 GLU HA 8.84 . 47 3JHNHA 79 TYR H 79 TYR HA 3.93 . 48 3JHNHA 84 ARG H 84 ARG HA 10.21 . 49 3JHNHA 85 LYS H 85 LYS HA 9.45 . 50 3JHNHA 87 LEU H 87 LEU HA 9.48 . 51 3JHNHA 89 PHE H 89 PHE HA 8.52 . 52 3JHNHA 90 ASN H 90 ASN HA 9.35 . 53 3JHNHA 93 VAL H 93 VAL HA 9.69 . stop_ save_ save_JHAHB _Saveframe_category coupling_constants loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Spectrometer_frequency_1H 600 _Mol_system_component_name MNEI 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_value_error 1 3JHAHB 22 GLU HA 22 GLU HB2 5.9 . 2 3JHAHB 24 ASN HA 24 ASN HB2 8.7 . 3 3JHAHB 24 ASN HA 24 ASN HB3 4.6 . 4 3JHAHB 29 TYR HA 29 TYR HB3 10.3 . 5 3JHAHB 31 ARG HA 31 ARG HB2 9.6 . 6 3JHAHB 32 LEU HA 32 LEU HB2 11.2 . 7 3JHAHB 35 ASN HA 35 ASN HB2 8.0 . 8 3JHAHB 41 CYS HA 41 CYS HB3 8.5 . 9 3JHAHB 44 LYS HA 44 LYS HB3 13.1 . 10 3JHAHB 47 TYR HA 47 TYR HB2 7.0 . 11 3JHAHB 52 PHE HA 52 PHE HB2 7.2 . 12 3JHAHB 52 PHE HA 52 PHE HB3 8.8 . 13 3JHAHB 58 TYR HA 58 TYR HB2 6.1 . 14 3JHAHB 58 TYR HA 58 TYR HB3 11.1 . 15 3JHAHB 59 GLU HA 59 GLU HB2 10.2 . 16 3JHAHB 59 GLU HA 59 GLU HB3 6.5 . 17 3JHAHB 60 TYR HA 60 TYR HB2 6.0 . 18 3JHAHB 60 TYR HA 60 TYR HB3 10.8 . 19 3JHAHB 62 LEU HA 62 LEU HB2 5.7 . 20 3JHAHB 62 LEU HA 62 LEU HB3 11.8 . 21 3JHAHB 65 TYR HA 65 TYR HB3 9.9 . 22 3JHAHB 68 ASP HA 68 ASP HB3 9.1 . 23 3JHAHB 72 ARG HA 72 ARG HB2 10.0 . 24 3JHAHB 72 ARG HA 72 ARG HB3 6.2 . 25 3JHAHB 74 ASP HA 74 ASP HB2 7.7 . 26 3JHAHB 74 ASP HA 74 ASP HB3 10.5 . 27 3JHAHB 77 GLU HA 77 GLU HB2 10.5 . 28 3JHAHB 77 GLU HA 77 GLU HB3 7.2 . 29 3JHAHB 86 LEU HA 86 LEU HB2 10.8 . 30 3JHAHB 86 LEU HA 86 LEU HB3 7.2 . 31 3JHAHB 87 LEU HA 87 LEU HB2 10.8 . 32 3JHAHB 87 LEU HA 87 LEU HB3 6.6 . 33 3JHAHB 89 PHE HA 89 PHE HB2 10.5 . 34 3JHAHB 89 PHE HA 89 PHE HB3 6.2 . stop_ save_ save_JNHB _Saveframe_category coupling_constants loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Spectrometer_frequency_1H 600 _Mol_system_component_name MNEI 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_value_error 1 3JNHB 5 ILE N 5 ILE HB -1.83 1.0 2 3JNHB 8 ILE N 8 ILE HB -4.55 1.0 3 3JNHB 11 PHE N 11 PHE HB2 -0.96 1.0 4 3JNHB 11 PHE N 11 PHE HB3 -1.18 1.0 5 3JNHB 12 THR N 12 THR HB -0.64 1.0 6 3JNHB 14 ASN N 14 ASN HB2 -1.28 1.0 7 3JNHB 14 ASN N 14 ASN HB3 -3.49 1.0 8 3JNHB 24 ASN N 24 ASN HB2 -2.01 1.0 9 3JNHB 24 ASN N 24 ASN HB3 -3.95 1.0 10 3JNHB 26 ILE N 26 ILE HB -1.57 1.0 11 3JNHB 29 TYR N 29 TYR HB2 -4.62 1.0 12 3JNHB 29 TYR N 29 TYR HB3 -0.99 1.0 13 3JNHB 32 LEU N 32 LEU HB2 -1.25 1.0 14 3JNHB 32 LEU N 32 LEU HB3 -3.49 1.0 15 3JNHB 35 ASN N 35 ASN HB2 -4.95 1.0 16 3JNHB 35 ASN N 35 ASN HB3 -0.96 1.0 17 3JNHB 38 ILE N 38 ILE HB -3.48 1.0 18 3JNHB 41 CYS N 41 CYS HB2 -0.91 1.0 19 3JNHB 41 CYS N 41 CYS HB3 -2.17 1.0 20 3JNHB 52 PHE N 52 PHE HB2 -2.77 1.0 21 3JNHB 52 PHE N 52 PHE HB3 -1.47 1.0 22 3JNHB 67 SER N 67 SER HB3 -1.12 1.0 23 3JNHB 71 PHE N 71 PHE HB2 -1.53 1.0 24 3JNHB 71 PHE N 71 PHE HB3 -4.02 1.0 25 3JNHB 75 ILE N 75 ILE HB -1.75 1.0 26 3JNHB 76 SER N 76 SER HB2 -2.19 1.0 27 3JNHB 76 SER N 76 SER HB3 -1.09 1.0 stop_ save_