data_4222 #Corrected using PDB structure: 1IV9A # #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 4.70 5.49 # 63 Y HA 5.50 4.76 # 82 R HA 5.51 4.22 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.00 N/A N/A N/A N/A N/A # #bmr4222.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4222.str file): #HA CA CB CO N HN #N/A N/A N/A N/A N/A N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.05 N/A N/A N/A N/A N/A # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.826 N/A N/A N/A N/A N/A # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.172 N/A N/A N/A N/A N/A # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; High-Resolution Solution Structure of a Sweet Protein Single-Chain Monellin (SCM) determined by Nuclear Magnetic Resonance Spectroscopy and Dynamical Simulated Annealing Calculations ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lee Seok-Yong . . 2 Lee Jung-Hoon . . 3 Chang Ho-Jin . . 4 Cho JM . . 5 Jung Jin-Won . . 6 Lee Weontae . . stop_ _BMRB_accession_number 4222 _BMRB_flat_file_name bmr4222.str _Entry_type new _Submission_date 1998-08-06 _Accession_date 1998-08-06 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 465 '15N chemical shifts' 86 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Solution structure of a sweet protein single-chain monellin determined by nuclear magnetic resonance and dynamical simulated annealing calculations ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 99155206 _PubMed_ID 10029527 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lee Seok-Yong . . 2 Lee Jung-Hoon . . 3 Chang Ho-Jin . . 4 Cho JM . . 5 Jung Jin-Won . . 6 Lee Weontae . . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 38 _Journal_issue ? _Page_first 2340 _Page_last 2346 _Year 1999 loop_ _Keyword 'sweet protein' 'sweet receptor binding' 'alpha/beta motif' stop_ save_ ################################## # Molecular system description # ################################## save_system_monellin _Saveframe_category molecular_system _Mol_system_name monellin _Abbreviation_common monellin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label monellin $monellin stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1MOL "A Chain A, Monellin (Single-Chain, Fused)" . PDB 1MNL "High-Resolution Solution Structure Of A Sweet Protein Single-Chain Monellin (Scm) Determined By Nuclear Magnetic Resonance Spectroscopy And Dynamical Simulated Annealing Calculations, 21 Structures" . stop_ save_ ######################## # Monomeric polymers # ######################## save_monellin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common monellin _Name_variant . _Abbreviation_common monellin _Mol_thiol_state 'not reported' ############################## # Polymer residue sequence # ############################## _Residue_count 94 _Mol_residue_sequence ; GEWEIIDIGPFTQNLGKFAV DEENKIGQYGRLTFNKVIRP CMKKTIYENEREIKGYEYQL YVYASDKLFRADISEDYKTR GRKLLRFNGPVPPP ; 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 ARG 52 GLU 53 ILE 54 LYS 55 GLY 56 TYR 57 GLU 58 TYR 59 GLN 60 LEU 61 TYR 62 VAL 63 TYR 64 ALA 65 SER 66 ASP 67 LYS 68 LEU 69 PHE 70 ARG 71 ALA 72 ASP 73 ILE 74 SER 75 GLU 76 ASP 77 TYR 78 LYS 79 THR 80 ARG 81 GLY 82 ARG 83 LYS 84 LEU 85 LEU 86 ARG 87 PHE 88 ASN 89 GLY 90 PRO 91 VAL 92 PRO 93 PRO 94 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" 195.83 48 100 100 4e-22 PDB 1KRL "B Chain B, Crystal Structure Of RacemicDl-Monellin In P-1" 188.00 50 100 100 4e-22 PDB 3MON "B Chain B, Monellin" 188.00 50 100 100 2e-23 PDB 4MON "B Chain B, Orthorhombic Monellin" 188.00 50 100 100 2e-23 PDB 1FUW "A Chain A, Solution Structure And BackboneDynamics Of A Double Mutant Single-Chain Monellin(Scm)Determined By Nuclear Magnetic Resonance Spectroscopy" 103.30 91 98 100 2e-47 PDB 1MNL "High-Resolution Solution Structure Of ASweet Protein Single-Chain Monellin (Scm) Determined ByNuclear Magnetic Resonance Spectroscopy And DynamicalSimulated Annealing Calculations, 21 Structures" 100.00 94 100 100 10e-51 PDB 1MOL "A Chain A, Monellin (Single-Chain, Fused)" 100.00 94 100 100 10e-51 PDB 1FA3 "A Chain A, Solution Structure Of Mnei, ASweet Protein" 97.92 96 98 98 3e-49 PDB 1IV7 "A Chain A, Crystal Structure Of Single ChainMonellin" 97.92 96 98 98 3e-49 GenBank AAG21344.1 "monellin [synthetic construct]" 101.08 93 98 98 5e-48 PIR MLDIB "monellin chain B [validated] - serendipityberry" 184.31 51 100 100 4e-22 PRF 761801B "monellin B" 188.00 50 100 100 2e-23 SWISS-PROT P02882 "MONB_DIOCU Monellin chain B (Monellin chainII)" 188.00 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 $monellin 'Serendipity Berry' 3457 Eukaryota . Dioscoreophyllum cumminsii 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 $monellin 'recombinant technology' "baker's yeast" Saccharomyces cerevisiae . . 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 $monellin . mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Details ; TOCSY NOESY DQF-COSY 1H-15N HSQC 1H-15N HMQC-J 1H-15N NOESY-HSQC 1H-15N HOHAHA-HMQC ; save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 . n/a temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 _Indirect_shift_ratio_citation_label . H 1 . . . . . . . . . . . N 15 . . . . . . . . . . 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_chem_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_reference _Mol_system_component_name monellin 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 2 GLU N N 118.72 . . 2 2 GLU H H 8.26 . . 3 2 GLU HA H 4.23 . . 4 2 GLU HB2 H 0.83 . . 5 2 GLU HB3 H 0.83 . . 6 3 TRP N N 118.82 . . 7 3 TRP H H 8.20 . . 8 3 TRP HA H 4.70 . . 9 3 TRP HB2 H 3.00 . . 10 3 TRP HB3 H 3.00 . . 11 3 TRP HD1 H 7.22 . . 12 3 TRP HE1 H 10.10 . . 13 4 GLU N N 123.00 . . 14 4 GLU H H 9.41 . . 15 4 GLU HA H 4.80 . . 16 4 GLU HB2 H 1.98 . . 17 4 GLU HB3 H 1.98 . . 18 4 GLU HG2 H 2.30 . . 19 4 GLU HG3 H 2.30 . . 20 5 ILE N N 121.25 . . 21 5 ILE H H 9.20 . . 22 5 ILE HA H 4.82 . . 23 5 ILE HG12 H 0.95 . . 24 5 ILE HG13 H 0.95 . . 25 6 ILE N N 120.22 . . 26 6 ILE H H 8.22 . . 27 6 ILE HA H 4.73 . . 28 6 ILE HB H 2.72 . . 29 6 ILE HG12 H 2.00 . . 30 6 ILE HG13 H 2.00 . . 31 6 ILE HD1 H 2.56 . . 32 7 ASP N N 120.39 . . 33 7 ASP H H 8.65 . . 34 7 ASP HA H 4.72 . . 35 7 ASP HB2 H 1.40 . . 36 7 ASP HB3 H 1.40 . . 37 8 ILE N N 126.62 . . 38 8 ILE H H 8.60 . . 39 8 ILE HA H 5.21 . . 40 8 ILE HB H 1.50 . . 41 8 ILE HG12 H 0.57 . . 42 8 ILE HG13 H 0.57 . . 44 9 GLY H H 8.21 . . 45 9 GLY HA2 H 4.23 . . 46 9 GLY HA3 H 4.23 . . 47 10 PRO HA H 4.46 . . 48 10 PRO HB2 H 2.05 . . 49 10 PRO HB3 H 2.05 . . 50 10 PRO HG2 H 1.97 . . 51 10 PRO HG3 H 1.97 . . 52 10 PRO HD2 H 3.66 . . 53 10 PRO HD3 H 3.66 . . 54 11 PHE N N 120.70 . . 55 11 PHE H H 8.53 . . 56 11 PHE HA H 4.22 . . 57 11 PHE HB2 H 2.10 . . 58 11 PHE HB3 H 2.10 . . 59 11 PHE HD1 H 7.10 . . 60 11 PHE HD2 H 7.10 . . 61 12 THR N N 113.95 . . 62 12 THR H H 7.68 . . 63 12 THR HA H 3.70 . . 64 12 THR HB H 4.23 . . 65 12 THR HG2 H 1.41 . . 66 13 GLN N N 121.20 . . 67 13 GLN H H 8.52 . . 68 13 GLN HA H 4.21 . . 69 13 GLN HB2 H 2.63 . . 70 13 GLN HB3 H 2.63 . . 71 14 ASN N N 116.60 . . 72 14 ASN H H 8.00 . . 73 14 ASN HA H 4.20 . . 74 14 ASN HB2 H 2.75 . . 75 14 ASN HB3 H 2.58 . . 76 15 LEU N N 121.67 . . 77 15 LEU H H 7.35 . . 78 15 LEU HA H 3.70 . . 79 15 LEU HB2 H 1.80 . . 80 15 LEU HB3 H 1.80 . . 81 15 LEU HG H 1.00 . . 82 15 LEU HD1 H 0.09 . . 83 15 LEU HD2 H 0.09 . . 84 16 GLY N N 106.33 . . 85 16 GLY H H 7.83 . . 86 16 GLY HA2 H 3.38 . . 87 16 GLY HA3 H 3.38 . . 88 17 LYS N N 122.57 . . 89 17 LYS H H 7.40 . . 90 17 LYS HA H 2.90 . . 91 17 LYS HB2 H 1.22 . . 92 17 LYS HB3 H 1.22 . . 93 17 LYS HG2 H 0.78 . . 94 17 LYS HG3 H 0.78 . . 95 17 LYS HD2 H 1.53 . . 96 17 LYS HD3 H 1.53 . . 97 17 LYS HE2 H 2.97 . . 98 17 LYS HE3 H 2.97 . . 99 18 PHE N N 119.19 . . 100 18 PHE H H 7.48 . . 101 18 PHE HA H 4.23 . . 102 18 PHE HB2 H 3.22 . . 103 18 PHE HB3 H 3.22 . . 104 19 ALA N N 119.96 . . 105 19 ALA H H 8.13 . . 106 19 ALA HA H 3.50 . . 107 20 VAL N N 115.94 . . 108 20 VAL H H 7.78 . . 109 20 VAL HA H 2.93 . . 110 20 VAL HB H 2.00 . . 111 20 VAL HG1 H 0.70 . . 112 20 VAL HG2 H 0.70 . . 113 21 ASP N N 122.50 . . 114 21 ASP H H 8.59 . . 115 21 ASP HA H 3.82 . . 116 22 GLU N N 118.25 . . 117 22 GLU H H 8.25 . . 118 22 GLU HA H 3.62 . . 119 22 GLU HB2 H 0.92 . . 120 22 GLU HB3 H 0.92 . . 121 22 GLU HG2 H 1.66 . . 122 22 GLU HG3 H 1.34 . . 123 23 GLU N N 123.18 . . 124 23 GLU H H 8.38 . . 125 23 GLU HA H 3.83 . . 126 24 ASN N N 121.55 . . 127 24 ASN H H 8.79 . . 128 24 ASN HA H 4.48 . . 129 24 ASN HB2 H 2.62 . . 130 24 ASN HB3 H 2.82 . . 131 25 LYS N N 118.91 . . 132 25 LYS H H 7.18 . . 133 25 LYS HA H 3.92 . . 134 25 LYS HB2 H 1.84 . . 135 25 LYS HB3 H 1.84 . . 136 26 ILE N N 119.02 . . 137 26 ILE H H 7.21 . . 138 26 ILE HA H 3.73 . . 139 26 ILE HB H 1.87 . . 140 26 ILE HG12 H 1.02 . . 141 26 ILE HG13 H 1.82 . . 142 27 GLY N N 104.24 . . 143 27 GLY H H 8.19 . . 144 27 GLY HA2 H 3.95 . . 145 27 GLY HA3 H 3.70 . . 146 28 GLN N N 119.49 . . 147 28 GLN H H 7.00 . . 148 28 GLN HA H 3.83 . . 149 28 GLN HB2 H 1.60 . . 150 28 GLN HB3 H 1.60 . . 151 28 GLN HG2 H 1.80 . . 152 28 GLN HG3 H 1.80 . . 153 29 TYR N N 116.70 . . 154 29 TYR H H 8.60 . . 155 29 TYR HA H 4.70 . . 156 29 TYR HB2 H 3.38 . . 157 29 TYR HB3 H 3.38 . . 158 30 GLY N N 106.44 . . 159 30 GLY H H 7.26 . . 160 30 GLY HA2 H 4.04 . . 161 30 GLY HA3 H 3.62 . . 162 31 ARG N N 122.80 . . 163 31 ARG H H 8.46 . . 164 31 ARG HA H 3.70 . . 165 32 LEU N N 126.15 . . 166 32 LEU H H 9.45 . . 167 32 LEU HA H 4.80 . . 168 32 LEU HB2 H 1.74 . . 169 32 LEU HB3 H 1.74 . . 170 32 LEU HG H 1.32 . . 171 32 LEU HD1 H 0.80 . . 172 32 LEU HD2 H 0.80 . . 173 33 THR N N 117.33 . . 174 33 THR H H 8.43 . . 175 33 THR HA H 4.15 . . 176 33 THR HB H 3.92 . . 177 33 THR HG2 H 0.80 . . 178 34 PHE N N 117.67 . . 179 34 PHE H H 9.40 . . 180 34 PHE HA H 4.12 . . 181 35 ASN N N 125.48 . . 182 35 ASN H H 8.38 . . 183 35 ASN HA H 4.71 . . 184 35 ASN HB2 H 2.70 . . 185 35 ASN HB3 H 2.50 . . 186 36 LYS N N 110.32 . . 187 36 LYS H H 7.13 . . 188 36 LYS HA H 4.40 . . 189 37 VAL N N 121.48 . . 190 37 VAL H H 9.27 . . 191 37 VAL HA H 4.98 . . 192 37 VAL HB H 1.92 . . 193 37 VAL HG1 H 1.12 . . 194 37 VAL HG2 H 1.22 . . 195 38 ILE N N 117.74 . . 196 38 ILE H H 7.82 . . 197 38 ILE HA H 4.76 . . 198 38 ILE HB H 2.00 . . 199 38 ILE HG12 H 0.90 . . 200 38 ILE HG13 H 0.60 . . 201 38 ILE HD1 H 8.80 . . 203 39 ARG H H 8.70 . . 204 39 ARG HA H 4.74 . . 205 40 PRO HA H 4.32 . . 206 40 PRO HB2 H 2.11 . . 207 40 PRO HB3 H 2.22 . . 208 40 PRO HG2 H 1.98 . . 209 40 PRO HG3 H 1.98 . . 210 40 PRO HD2 H 3.63 . . 211 40 PRO HD3 H 3.63 . . 212 41 CYS N N 124.71 . . 213 41 CYS H H 8.98 . . 214 41 CYS HA H 4.93 . . 215 41 CYS HB2 H 2.80 . . 216 41 CYS HB3 H 2.88 . . 217 41 CYS HG H 1.92 . . 218 42 MET N N 124.08 . . 219 42 MET H H 8.19 . . 220 42 MET HA H 5.72 . . 221 42 MET HB2 H 1.78 . . 222 42 MET HB3 H 1.78 . . 223 42 MET HG2 H 2.12 . . 224 42 MET HG3 H 2.12 . . 225 43 LYS N N 123.20 . . 226 43 LYS H H 9.71 . . 227 43 LYS HA H 5.42 . . 228 43 LYS HB2 H 1.53 . . 229 43 LYS HB3 H 1.53 . . 230 44 LYS N N 130.06 . . 231 44 LYS H H 9.38 . . 232 44 LYS HA H 4.60 . . 233 44 LYS HG2 H 0.65 . . 234 44 LYS HG3 H 0.65 . . 235 45 THR N N 119.12 . . 236 45 THR H H 8.61 . . 237 45 THR HA H 4.72 . . 238 45 THR HB H 4.19 . . 239 45 THR HG2 H 1.30 . . 240 46 ILE N N 127.30 . . 241 46 ILE H H 8.54 . . 242 46 ILE HA H 3.90 . . 243 46 ILE HB H 1.35 . . 244 46 ILE HG12 H 0.90 . . 245 46 ILE HG13 H 0.90 . . 246 46 ILE HD1 H 0.41 . . 247 47 TYR N N 126.66 . . 248 47 TYR H H 8.81 . . 249 47 TYR HA H 4.77 . . 250 47 TYR HB2 H 2.92 . . 251 47 TYR HB3 H 2.49 . . 252 47 TYR HD1 H 6.51 . . 253 47 TYR HD2 H 6.51 . . 254 47 TYR HE1 H 6.80 . . 255 47 TYR HE2 H 6.80 . . 256 48 GLU N N 122.26 . . 257 48 GLU H H 9.14 . . 258 48 GLU HA H 4.40 . . 259 48 GLU HB2 H 1.76 . . 260 48 GLU HB3 H 1.76 . . 261 48 GLU HG2 H 2.15 . . 262 48 GLU HG3 H 2.15 . . 263 49 ASN N N 116.70 . . 264 49 ASN H H 8.49 . . 265 49 ASN HA H 4.40 . . 266 49 ASN HB2 H 1.82 . . 267 49 ASN HB3 H 1.82 . . 268 50 GLU N N 115.32 . . 269 50 GLU H H 8.72 . . 270 50 GLU HA H 3.72 . . 271 50 GLU HB2 H 2.06 . . 272 50 GLU HB3 H 2.06 . . 273 50 GLU HG2 H 2.27 . . 274 50 GLU HG3 H 2.27 . . 275 51 ARG N N 112.50 . . 276 51 ARG H H 8.22 . . 277 51 ARG HA H 4.31 . . 278 51 ARG HB2 H 1.82 . . 279 51 ARG HB3 H 1.69 . . 280 51 ARG HG2 H 1.56 . . 281 51 ARG HG3 H 1.56 . . 282 52 GLU N N 120.38 . . 283 52 GLU H H 7.92 . . 284 52 GLU HA H 4.42 . . 285 52 GLU HB2 H 1.85 . . 286 52 GLU HB3 H 1.85 . . 287 53 ILE N N 126.03 . . 288 53 ILE H H 8.28 . . 289 53 ILE HA H 3.26 . . 290 53 ILE HB H 0.40 . . 291 53 ILE HG12 H 0.20 . . 292 53 ILE HG13 H 0.20 . . 293 54 LYS N N 127.09 . . 294 54 LYS H H 9.06 . . 295 54 LYS HA H 4.26 . . 296 54 LYS HB2 H 1.34 . . 297 54 LYS HB3 H 1.34 . . 298 54 LYS HG2 H 1.48 . . 299 54 LYS HG3 H 1.48 . . 300 55 GLY N N 106.69 . . 301 55 GLY H H 7.54 . . 302 55 GLY HA2 H 4.43 . . 303 55 GLY HA3 H 3.41 . . 304 56 TYR N N 115.25 . . 305 56 TYR H H 8.99 . . 306 56 TYR HA H 5.50 . . 307 56 TYR HB2 H 2.23 . . 308 56 TYR HB3 H 2.23 . . 309 56 TYR HD1 H 6.97 . . 310 56 TYR HD2 H 6.97 . . 311 56 TYR HE1 H 6.75 . . 312 56 TYR HE2 H 6.75 . . 313 57 GLU N N 123.25 . . 314 57 GLU H H 9.04 . . 315 57 GLU HA H 5.20 . . 316 57 GLU HB2 H 1.90 . . 317 57 GLU HB3 H 1.90 . . 318 58 TYR N N 119.00 . . 319 58 TYR H H 9.55 . . 320 58 TYR HA H 5.87 . . 321 58 TYR HB2 H 2.67 . . 322 58 TYR HB3 H 2.79 . . 323 58 TYR HD1 H 6.84 . . 324 58 TYR HD2 H 6.84 . . 325 58 TYR HE1 H 7.14 . . 326 58 TYR HE2 H 7.14 . . 327 59 GLN N N 120.90 . . 328 59 GLN H H 9.17 . . 329 59 GLN HA H 5.23 . . 330 59 GLN HB2 H 1.70 . . 331 59 GLN HB3 H 1.20 . . 332 59 GLN HG2 H 2.60 . . 333 59 GLN HG3 H 2.60 . . 334 60 LEU N N 123.43 . . 335 60 LEU H H 9.32 . . 336 60 LEU HA H 5.21 . . 337 60 LEU HB2 H 1.78 . . 338 60 LEU HB3 H 1.78 . . 339 60 LEU HG H 0.92 . . 340 61 TYR N N 120.12 . . 341 61 TYR H H 9.58 . . 342 61 TYR HA H 5.50 . . 343 61 TYR HB2 H 2.60 . . 344 61 TYR HB3 H 2.60 . . 345 61 TYR HD1 H 6.90 . . 346 61 TYR HD2 H 6.90 . . 347 61 TYR HE1 H 6.50 . . 348 61 TYR HE2 H 6.50 . . 349 62 VAL N N 124.80 . . 350 62 VAL H H 9.94 . . 351 62 VAL HA H 4.83 . . 352 62 VAL HB H 1.60 . . 353 63 TYR N N 127.26 . . 354 63 TYR H H 9.47 . . 355 63 TYR HA H 5.50 . . 356 63 TYR HB2 H 2.67 . . 357 63 TYR HB3 H 2.67 . . 358 63 TYR HD1 H 6.67 . . 359 63 TYR HD2 H 6.67 . . 360 63 TYR HE1 H 6.83 . . 361 63 TYR HE2 H 6.83 . . 362 64 ALA N N 127.86 . . 363 64 ALA H H 9.89 . . 364 64 ALA HA H 5.04 . . 365 64 ALA HB H 1.28 . . 366 65 SER N N 127.50 . . 367 65 SER H H 9.43 . . 368 65 SER HA H 4.08 . . 369 65 SER HB2 H 3.88 . . 370 65 SER HB3 H 3.88 . . 371 66 ASP N N 110.07 . . 372 66 ASP H H 9.13 . . 373 66 ASP HA H 3.88 . . 374 66 ASP HB2 H 2.81 . . 375 66 ASP HB3 H 2.81 . . 376 67 LYS N N 121.13 . . 377 67 LYS H H 8.24 . . 378 67 LYS HA H 4.50 . . 379 67 LYS HB2 H 1.80 . . 380 67 LYS HB3 H 1.80 . . 381 67 LYS HG2 H 1.34 . . 382 67 LYS HG3 H 1.34 . . 383 67 LYS HD2 H 1.04 . . 384 67 LYS HD3 H 1.04 . . 385 68 LEU N N 122.85 . . 386 68 LEU H H 8.07 . . 387 68 LEU HA H 4.20 . . 388 68 LEU HB2 H 1.86 . . 389 68 LEU HB3 H 1.86 . . 390 68 LEU HD1 H 0.45 . . 391 68 LEU HD2 H 0.45 . . 392 69 PHE N N 123.72 . . 393 69 PHE H H 9.02 . . 394 69 PHE HA H 5.23 . . 395 69 PHE HB2 H 1.92 . . 396 69 PHE HB3 H 1.92 . . 397 69 PHE HD1 H 6.86 . . 398 69 PHE HD2 H 6.86 . . 399 69 PHE HE1 H 7.27 . . 400 69 PHE HE2 H 7.27 . . 401 70 ARG N N 123.47 . . 402 70 ARG H H 8.64 . . 403 70 ARG HA H 4.77 . . 404 70 ARG HB2 H 1.83 . . 405 70 ARG HB3 H 1.83 . . 406 70 ARG HG2 H 1.10 . . 407 70 ARG HG3 H 1.10 . . 408 71 ALA N N 129.80 . . 409 71 ALA H H 9.58 . . 410 71 ALA HA H 4.14 . . 411 71 ALA HB H 1.42 . . 413 72 ASP H H 8.63 . . 414 72 ASP HA H 6.20 . . 415 72 ASP HB2 H 2.61 . . 416 72 ASP HB3 H 2.61 . . 417 73 ILE H H 9.50 . . 418 73 ILE HA H 5.30 . . 419 73 ILE HB H 1.89 . . 420 73 ILE HG12 H 1.32 . . 421 73 ILE HG13 H 1.32 . . 422 73 ILE HG2 H 1.07 . . 423 74 SER N N 120.55 . . 424 74 SER H H 9.46 . . 425 74 SER HA H 5.50 . . 426 74 SER HB2 H 3.78 . . 427 74 SER HB3 H 4.08 . . 428 75 GLU N N 121.88 . . 429 75 GLU H H 8.93 . . 430 75 GLU HA H 5.32 . . 431 75 GLU HB2 H 2.37 . . 432 75 GLU HB3 H 2.37 . . 433 75 GLU HG2 H 2.20 . . 434 75 GLU HG3 H 2.20 . . 435 76 ASP N N 127.66 . . 436 76 ASP H H 8.66 . . 437 76 ASP HA H 4.72 . . 438 76 ASP HB2 H 2.63 . . 439 76 ASP HB3 H 2.63 . . 440 77 TYR N N 127.92 . . 441 77 TYR H H 8.53 . . 442 77 TYR HA H 4.12 . . 443 77 TYR HB2 H 2.70 . . 444 77 TYR HB3 H 2.35 . . 445 77 TYR HD1 H 6.94 . . 446 77 TYR HD2 H 6.94 . . 447 77 TYR HE1 H 6.86 . . 448 77 TYR HE2 H 6.86 . . 449 78 LYS N N 116.06 . . 450 78 LYS H H 8.46 . . 451 78 LYS HA H 3.87 . . 452 78 LYS HB2 H 1.65 . . 453 78 LYS HB3 H 1.65 . . 454 78 LYS HG2 H 1.40 . . 455 78 LYS HG3 H 1.40 . . 456 78 LYS HD2 H 1.70 . . 457 78 LYS HD3 H 1.60 . . 458 79 THR N N 116.14 . . 459 79 THR H H 8.26 . . 460 79 THR HA H 4.29 . . 461 79 THR HB H 3.91 . . 462 79 THR HG2 H 1.45 . . 463 80 ARG N N 115.72 . . 464 80 ARG H H 7.70 . . 465 80 ARG HA H 4.22 . . 466 80 ARG HB2 H 2.09 . . 467 80 ARG HB3 H 2.09 . . 468 80 ARG HG2 H 1.46 . . 469 80 ARG HG3 H 1.46 . . 470 80 ARG HD2 H 3.07 . . 471 80 ARG HD3 H 3.07 . . 472 80 ARG HE H 6.99 . . 473 81 GLY N N 106.47 . . 474 81 GLY H H 8.29 . . 475 81 GLY HA2 H 3.83 . . 476 81 GLY HA3 H 3.60 . . 477 82 ARG N N 123.38 . . 478 82 ARG H H 8.41 . . 479 82 ARG HA H 5.51 . . 480 82 ARG HB2 H 0.91 . . 481 82 ARG HB3 H 0.91 . . 482 82 ARG HG2 H 1.20 . . 483 82 ARG HG3 H 1.20 . . 484 82 ARG HD2 H 2.40 . . 485 82 ARG HD3 H 2.40 . . 486 82 ARG HE H 7.22 . . 487 83 LYS N N 117.80 . . 488 83 LYS H H 8.60 . . 489 83 LYS HA H 4.72 . . 490 83 LYS HB2 H 1.68 . . 491 83 LYS HB3 H 1.68 . . 492 83 LYS HG2 H 1.40 . . 493 83 LYS HG3 H 1.40 . . 494 83 LYS HD2 H 1.70 . . 495 83 LYS HD3 H 1.70 . . 496 83 LYS HE2 H 3.02 . . 497 83 LYS HE3 H 3.02 . . 498 84 LEU N N 124.09 . . 499 84 LEU H H 9.32 . . 500 84 LEU HA H 5.24 . . 501 84 LEU HB2 H 1.72 . . 502 84 LEU HB3 H 1.72 . . 503 85 LEU N N 128.94 . . 504 85 LEU H H 9.24 . . 505 85 LEU HA H 4.38 . . 506 85 LEU HB2 H 1.70 . . 507 85 LEU HB3 H 1.70 . . 508 85 LEU HG H 1.44 . . 509 85 LEU HD1 H 0.90 . . 510 85 LEU HD2 H 0.70 . . 511 86 ARG N N 113.87 . . 512 86 ARG H H 7.58 . . 513 86 ARG HA H 4.58 . . 514 86 ARG HB2 H 1.95 . . 515 86 ARG HB3 H 1.70 . . 516 86 ARG HG2 H 1.50 . . 517 86 ARG HG3 H 1.50 . . 518 86 ARG HD2 H 3.40 . . 519 86 ARG HD3 H 3.40 . . 520 86 ARG HE H 7.28 . . 521 87 PHE N N 126.31 . . 522 87 PHE H H 8.68 . . 523 87 PHE HA H 5.03 . . 524 87 PHE HB2 H 3.32 . . 525 87 PHE HB3 H 3.32 . . 526 87 PHE HD1 H 6.72 . . 527 87 PHE HD2 H 6.72 . . 528 87 PHE HE1 H 5.82 . . 529 87 PHE HE2 H 5.82 . . 530 88 ASN N N 124.25 . . 531 88 ASN H H 8.89 . . 532 88 ASN HA H 5.49 . . 533 88 ASN HB2 H 2.61 . . 534 88 ASN HB3 H 2.61 . . 536 89 GLY H H 8.21 . . 537 89 GLY HA2 H 4.63 . . 538 89 GLY HA3 H 3.46 . . 539 90 PRO HA H 4.63 . . 540 90 PRO HB2 H 2.12 . . 541 90 PRO HB3 H 2.38 . . 542 90 PRO HG2 H 2.07 . . 543 90 PRO HG3 H 2.07 . . 544 90 PRO HD2 H 3.86 . . 545 90 PRO HD3 H 3.86 . . 547 91 VAL H H 8.12 . . 548 91 VAL HA H 4.63 . . 549 91 VAL HB H 1.91 . . 550 91 VAL HG1 H 0.90 . . 551 91 VAL HG2 H 0.90 . . stop_ save_