data_6302 #Corrected using PDB structure: 1MFTA # #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 # 21 A HA 3.20 4.00 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.05 N/A N/A N/A N/A -0.05 # #bmr6302.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr6302.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 #+/-0.04 N/A N/A N/A N/A +/-0.07 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.748 N/A N/A N/A N/A 0.612 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.147 N/A N/A N/A N/A 0.241 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of a diiron protein model: Due DF2-TURN_MUTANTturn mutant ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Maglio O. . . 2 Nastri F. . . 3 Calhoun J. R. . 4 Lahr S. . . 5 Pavone V. . . 6 DeGrado W. F. . 7 Lombardi A. . . stop_ _BMRB_accession_number 6302 _BMRB_flat_file_name bmr6302.str _Entry_type new _Submission_date 2004-08-26 _Accession_date 2004-08-26 _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' 348 stop_ loop_ _Related_BMRB_accession_number _Relationship 6303 "DIIRON in DF2" stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Artificial diiron proteins: From structure to function ; _Citation_status published _Citation_type journal _MEDLINE_UI_code . _PubMed_ID 15700297 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Calhoun J. R. . 2 Nastri F. . . 3 Maglio O. . . 4 Pavone V. . . 5 Lombardi A. . . 6 DeGrado W. F. . stop_ _Journal_abbreviation Biopolymers _Journal_volume 80 _Journal_issue 2-3 _Page_first 264 _Page_last 278 _Year 2005 loop_ _Keyword "Diiron proteins" "four-helix bundle" "protein design" "inter-helical loops" stop_ save_ ################################## # Molecular system description # ################################## save_system_DF2-TURN_MUTANT _Saveframe_category molecular_system _Mol_system_name "Four-helix bundle model" _Abbreviation_common "Four-helix bundle model" _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label "Four-helix bundle chain A" $DF2-TURN_MUTANT "Four-helix bundle chain B" $DF2-TURN_MUTANT 'ZINC (II) ION 1' $ZN_2+ 'ZINC (II) ION 2' $ZN_2+ stop_ _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1U7M ? . stop_ save_ ######################## # Monomeric polymers # ######################## save_DF2-TURN_MUTANT _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "Four-helix bundle model" _Name_variant . _Abbreviation_common "Four-helix bundle model" _Mol_thiol_state 'not present' ############################## # Polymer residue sequence # ############################## _Residue_count 53 _Mol_residue_sequence ; MDYLRELYKLEQQAMKLYRE ASEKARNPEKKSVLQKILED EEKHIEWLETING ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASP 3 TYR 4 LEU 5 ARG 6 GLU 7 LEU 8 TYR 9 LYS 10 LEU 11 GLU 12 GLN 13 GLN 14 ALA 15 MET 16 LYS 17 LEU 18 TYR 19 ARG 20 GLU 21 ALA 22 SER 23 GLU 24 LYS 25 ALA 26 ARG 27 ASN 28 PRO 29 GLU 30 LYS 31 LYS 32 SER 33 VAL 34 LEU 35 GLN 36 LYS 37 ILE 38 LEU 39 GLU 40 ASP 41 GLU 42 GLU 43 LYS 44 HIS 45 ILE 46 GLU 47 TRP 48 LEU 49 GLU 50 THR 51 ILE 52 ASN 53 GLY stop_ _Sequence_homology_query_date 2005-09-22 _Sequence_homology_query_revised_last_date 2005-08-25 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 1MFT "A Chain A, Crystal Structure Of Four-HelixBundle Model" 100.00 53 100 100 3e-23 PDB 1U7M "A Chain A, Solution Structure Of A DiironProtein Model: Due Ferri(Ii) Turn Mutant" 100.00 53 100 100 3e-23 stop_ save_ ############# # Ligands # ############# save_ZN_2+ _Saveframe_category ligand _Mol_type non-polymer _Name_common 'ZINC (II) ION' _Abbreviation_common Zn _Name_IUPAC . _BMRB_code ZN_2+ _PDB_code ZN _Mol_empirical_formula ZN1 _Mol_charge 2+ _Mol_paramagnetic no _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN ? 2+ 2+ 0 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $DF2-TURN_MUTANT "E. coli" 562 Eubacteria . Escherichia coli 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 $DF2-TURN_MUTANT 'recombinant technology' Bacteria Escherichia coli BL21(DE3) 'Plasmid PET28A' 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 $DF2-TURN_MUTANT 0.5 mM . 'phosphate buffer' 50 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 1.7 loop_ _Task processing stop_ _Details "Delaglio et al." save_ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task "structure solution" stop_ _Details "Guentert et al." save_ save_AMBER _Saveframe_category software _Name AMBER _Version 7.0 loop_ _Task refinement stop_ _Details "Case et al." save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 800 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 2D TOCSY 2D NOESY DQF-COSY ; save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.1 . pH temperature 298 . K pressure 1 . atm 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 TSP H 1 'methyl protons' ppm 0.0 internal . . . . 1.0 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique (geminal atoms and geminal methyl # # groups with identical chemical shifts # # are assumed to be assigned to # # stereospecific atoms) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 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) # # 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_reference _Mol_system_component_name "Four-helix bundle chain A" 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 3 TYR H H 8.14 . 1 2 3 TYR HA H 3.97 . 1 3 3 TYR HB2 H 2.94 . 1 4 3 TYR HB3 H 2.94 . 1 5 3 TYR HD1 H 7.13 . 1 6 3 TYR HD2 H 7.13 . 1 7 3 TYR HE1 H 6.85 . 1 8 3 TYR HE2 H 6.85 . 1 9 4 LEU H H 8.22 . 1 10 4 LEU HA H 4.09 . 1 11 4 LEU HB2 H 1.97 . 1 12 4 LEU HB3 H 1.97 . 1 13 4 LEU HG H 1.62 . 1 14 4 LEU HD1 H 0.96 . 1 15 4 LEU HD2 H 0.96 . 1 16 5 ARG H H 7.69 . 1 17 5 ARG HA H 4.10 . 1 18 5 ARG HB2 H 1.77 . 1 19 5 ARG HB3 H 1.77 . 1 20 5 ARG HG2 H 2.01 . 1 21 5 ARG HG3 H 2.01 . 1 22 5 ARG HD2 H 3.22 . 1 23 5 ARG HD3 H 3.22 . 1 24 5 ARG HE H 7.28 . 1 25 6 GLU H H 7.96 . 1 26 6 GLU HA H 4.12 . 1 27 6 GLU HB2 H 2.03 . 2 28 6 GLU HB3 H 1.85 . 2 29 6 GLU HG2 H 2.37 . 1 30 6 GLU HG3 H 2.37 . 1 31 7 LEU H H 8.64 . 1 32 7 LEU HA H 3.92 . 1 33 7 LEU HB2 H 1.94 . 1 34 7 LEU HB3 H 1.94 . 1 35 7 LEU HG H 1.61 . 1 36 7 LEU HD1 H 0.50 . 2 37 7 LEU HD2 H -0.06 . 2 38 8 TYR H H 8.22 . 1 39 8 TYR HA H 3.94 . 1 40 8 TYR HB2 H 3.22 . 2 41 8 TYR HB3 H 3.18 . 2 42 8 TYR HD1 H 7.07 . 1 43 8 TYR HD2 H 7.07 . 1 44 8 TYR HE1 H 6.89 . 1 45 8 TYR HE2 H 6.89 . 1 46 9 LYS H H 7.77 . 1 47 9 LYS HA H 4.09 . 1 48 9 LYS HB2 H 2.00 . 1 49 9 LYS HB3 H 2.00 . 1 50 9 LYS HG2 H 1.64 . 1 51 9 LYS HG3 H 1.64 . 1 52 9 LYS HD2 H 1.80 . 1 53 9 LYS HD3 H 1.80 . 1 54 9 LYS HE2 H 2.95 . 1 55 9 LYS HE3 H 2.95 . 1 56 10 LEU H H 7.93 . 1 57 10 LEU HA H 4.17 . 1 58 10 LEU HB2 H 2.04 . 1 59 10 LEU HB3 H 2.04 . 1 60 10 LEU HG H 1.75 . 1 61 10 LEU HD1 H 0.97 . 1 62 10 LEU HD2 H 0.97 . 1 63 11 GLU H H 8.58 . 1 64 11 GLU HA H 4.54 . 1 65 11 GLU HB2 H 2.15 . 2 66 11 GLU HB3 H 1.99 . 2 67 11 GLU HG2 H 2.86 . 2 68 11 GLU HG3 H 2.35 . 2 69 12 GLN H H 8.24 . 1 70 12 GLN HA H 3.95 . 1 71 12 GLN HB2 H 2.19 . 2 72 12 GLN HB3 H 2.39 . 2 73 12 GLN HG2 H 2.33 . 2 74 12 GLN HG3 H 1.99 . 2 75 12 GLN HE21 H 6.55 . 2 76 12 GLN HE22 H 6.98 . 2 77 13 GLN H H 8.05 . 1 78 13 GLN HA H 4.13 . 1 79 13 GLN HB2 H 2.26 . 1 80 13 GLN HB3 H 2.26 . 1 81 13 GLN HG2 H 2.52 . 2 82 13 GLN HG3 H 2.41 . 2 83 13 GLN HE21 H 7.18 . 2 84 13 GLN HE22 H 6.88 . 2 85 14 ALA H H 8.98 . 1 86 14 ALA HA H 3.97 . 1 87 14 ALA HB H 1.63 . 1 88 15 MET H H 8.92 . 1 89 15 MET HA H 3.96 . 1 90 15 MET HB2 H 2.24 . 1 91 15 MET HB3 H 2.24 . 1 92 15 MET HG2 H 2.66 . 1 93 15 MET HG3 H 2.66 . 1 94 15 MET HE H 1.99 . 1 95 16 LYS H H 7.68 . 1 96 16 LYS HA H 4.01 . 1 97 16 LYS HB2 H 1.90 . 1 98 16 LYS HB3 H 1.90 . 1 99 16 LYS HG2 H 1.45 . 1 100 16 LYS HG3 H 1.45 . 1 101 16 LYS HD2 H 1.72 . 1 102 16 LYS HD3 H 1.72 . 1 103 16 LYS HE2 H 2.95 . 1 104 16 LYS HE3 H 2.95 . 1 105 17 LEU H H 8.08 . 1 106 17 LEU HA H 4.27 . 1 107 17 LEU HB2 H 1.72 . 2 108 17 LEU HB3 H 1.49 . 2 109 17 LEU HG H 1.98 . 1 110 17 LEU HD1 H 0.94 . 1 111 17 LEU HD2 H 0.94 . 1 112 18 TYR H H 9.47 . 1 113 18 TYR HA H 4.12 . 1 114 18 TYR HB2 H 2.97 . 2 115 18 TYR HB3 H 2.88 . 2 116 18 TYR HD1 H 6.98 . 1 117 18 TYR HD2 H 6.98 . 1 118 18 TYR HE1 H 6.66 . 1 119 18 TYR HE2 H 6.66 . 1 120 18 TYR HH H 10.03 . 1 121 19 ARG H H 8.43 . 1 122 19 ARG HA H 3.91 . 1 123 19 ARG HB2 H 2.01 . 1 124 19 ARG HB3 H 2.01 . 1 125 19 ARG HG2 H 1.71 . 2 126 19 ARG HG3 H 1.64 . 2 127 19 ARG HD2 H 3.23 . 1 128 19 ARG HD3 H 3.23 . 1 129 19 ARG HE H 7.34 . 1 130 20 GLU H H 7.74 . 1 131 20 GLU HA H 3.98 . 1 132 20 GLU HB2 H 2.17 . 2 133 20 GLU HB3 H 1.99 . 2 134 20 GLU HG2 H 2.48 . 1 135 20 GLU HG3 H 2.48 . 1 136 21 ALA H H 8.70 . 1 137 21 ALA HA H 3.25 . 1 138 21 ALA HB H 1.21 . 1 139 22 SER H H 8.49 . 1 140 22 SER HA H 4.01 . 1 141 22 SER HB2 H 4.02 . 1 142 22 SER HB3 H 4.02 . 1 143 23 GLU H H 7.63 . 1 144 23 GLU HA H 4.05 . 1 145 23 GLU HB2 H 2.17 . 2 146 23 GLU HB3 H 2.10 . 2 147 23 GLU HG2 H 2.48 . 1 148 23 GLU HG3 H 2.48 . 1 149 24 LYS H H 7.42 . 1 150 24 LYS HA H 4.24 . 1 151 24 LYS HB2 H 1.60 . 1 152 24 LYS HB3 H 1.60 . 1 153 24 LYS HG2 H 2.01 . 1 154 24 LYS HG3 H 2.01 . 1 155 24 LYS HD2 H 1.85 . 2 156 24 LYS HD3 H 1.39 . 2 157 24 LYS HE2 H 3.25 . 1 158 24 LYS HE3 H 3.25 . 1 159 25 ALA H H 7.36 . 1 160 25 ALA HA H 4.25 . 1 161 25 ALA HB H 1.37 . 1 162 26 ARG H H 8.59 . 1 163 26 ARG HA H 4.41 . 1 164 26 ARG HB2 H 1.82 . 1 165 26 ARG HB3 H 1.82 . 1 166 26 ARG HG2 H 2.04 . 1 167 26 ARG HG3 H 2.04 . 1 168 26 ARG HD2 H 2.85 . 2 169 26 ARG HD3 H 2.34 . 2 170 26 ARG HE H 6.98 . 1 171 27 ASN H H 7.99 . 1 172 27 ASN HA H 5.11 . 1 173 27 ASN HB2 H 2.96 . 2 174 27 ASN HB3 H 2.90 . 2 175 27 ASN HD21 H 8.04 . 2 176 27 ASN HD22 H 7.42 . 2 177 28 PRO HA H 4.18 . 1 178 28 PRO HB2 H 2.44 . 1 179 28 PRO HB3 H 2.44 . 1 180 28 PRO HG2 H 2.22 . 1 181 28 PRO HG3 H 2.22 . 1 182 28 PRO HD2 H 4.13 . 2 183 28 PRO HD3 H 3.95 . 2 184 29 GLU H H 8.36 . 1 185 29 GLU HA H 4.17 . 1 186 29 GLU HB2 H 2.20 . 2 187 29 GLU HB3 H 2.08 . 2 188 29 GLU HG2 H 2.34 . 1 189 29 GLU HG3 H 2.34 . 1 190 30 LYS H H 7.79 . 1 191 30 LYS HA H 4.09 . 1 192 30 LYS HB2 H 1.90 . 1 193 30 LYS HB3 H 1.90 . 1 194 30 LYS HG2 H 1.76 . 1 195 30 LYS HG3 H 1.76 . 1 196 30 LYS HE2 H 2.95 . 1 197 30 LYS HE3 H 2.95 . 1 198 31 LYS H H 8.34 . 1 199 31 LYS HA H 3.65 . 1 200 31 LYS HB2 H 2.07 . 2 201 31 LYS HB3 H 1.84 . 2 202 31 LYS HG2 H 1.67 . 1 203 31 LYS HG3 H 1.67 . 1 204 31 LYS HD2 H 1.76 . 1 205 31 LYS HD3 H 1.76 . 1 206 31 LYS HE2 H 2.99 . 1 207 31 LYS HE3 H 2.99 . 1 208 32 SER H H 7.95 . 1 209 32 SER HA H 3.96 . 1 210 32 SER HB2 H 4.13 . 1 211 32 SER HB3 H 4.13 . 1 212 33 VAL H H 7.31 . 1 213 33 VAL HA H 3.41 . 1 214 33 VAL HB H 2.05 . 1 215 33 VAL HG1 H 0.89 . 2 216 33 VAL HG2 H 0.72 . 2 217 34 LEU H H 7.88 . 1 218 34 LEU HA H 3.96 . 1 219 34 LEU HB2 H 1.99 . 1 220 34 LEU HB3 H 1.99 . 1 221 34 LEU HG H 1.41 . 1 222 34 LEU HD1 H 0.96 . 1 223 34 LEU HD2 H 0.96 . 1 224 35 GLN H H 8.39 . 1 225 35 GLN HA H 3.88 . 1 226 35 GLN HB2 H 2.25 . 2 227 35 GLN HB3 H 2.00 . 2 228 35 GLN HG2 H 2.49 . 1 229 35 GLN HG3 H 2.49 . 1 230 35 GLN HE21 H 7.67 . 2 231 35 GLN HE22 H 6.82 . 2 232 36 LYS H H 7.67 . 1 233 36 LYS HA H 4.01 . 1 234 36 LYS HB2 H 2.00 . 1 235 36 LYS HB3 H 2.00 . 1 236 36 LYS HG2 H 1.85 . 1 237 36 LYS HG3 H 1.85 . 1 238 36 LYS HD2 H 1.44 . 1 239 36 LYS HD3 H 1.44 . 1 240 36 LYS HE2 H 3.39 . 1 241 36 LYS HE3 H 3.39 . 1 242 37 ILE H H 8.06 . 1 243 37 ILE HA H 2.94 . 1 244 37 ILE HB H 1.04 . 1 245 37 ILE HG2 H -0.61 . 1 246 37 ILE HG12 H 0.95 . 1 247 37 ILE HG13 H 0.95 . 1 248 37 ILE HD1 H -0.61 . 1 249 38 LEU H H 7.96 . 1 250 38 LEU HA H 3.52 . 1 251 38 LEU HB2 H 2.04 . 1 252 38 LEU HB3 H 2.04 . 1 253 38 LEU HG H 1.48 . 1 254 38 LEU HD1 H 0.98 . 1 255 38 LEU HD2 H 0.98 . 1 256 39 GLU H H 7.59 . 1 257 39 GLU HA H 3.93 . 1 258 39 GLU HB2 H 2.26 . 2 259 39 GLU HB3 H 2.08 . 2 260 39 GLU HG2 H 2.54 . 1 261 39 GLU HG3 H 2.54 . 1 262 40 ASP H H 7.61 . 1 263 40 ASP HA H 4.15 . 1 264 40 ASP HB2 H 3.17 . 2 265 40 ASP HB3 H 2.12 . 2 266 41 GLU H H 8.29 . 1 267 41 GLU HA H 4.43 . 1 268 41 GLU HB2 H 1.73 . 1 269 41 GLU HB3 H 1.73 . 1 270 41 GLU HG2 H 2.73 . 1 271 41 GLU HG3 H 2.73 . 1 272 42 GLU H H 7.93 . 1 273 42 GLU HA H 3.92 . 1 274 42 GLU HB2 H 2.12 . 2 275 42 GLU HB3 H 1.99 . 2 276 42 GLU HG2 H 2.38 . 1 277 42 GLU HG3 H 2.38 . 1 278 43 LYS H H 7.31 . 1 279 43 LYS HA H 3.75 . 1 280 43 LYS HB2 H 1.63 . 2 281 43 LYS HB3 H 1.38 . 2 282 43 LYS HG2 H 1.98 . 1 283 43 LYS HG3 H 1.98 . 1 284 43 LYS HD2 H 0.74 . 1 285 43 LYS HD3 H 0.74 . 1 286 44 HIS H H 8.19 . 1 287 44 HIS HA H 4.13 . 1 288 44 HIS HB2 H 3.56 . 2 289 44 HIS HB3 H 3.11 . 2 290 44 HIS HD2 H 6.26 . 1 291 44 HIS HE1 H 7.43 . 1 292 44 HIS HE2 H 15.00 . 1 293 45 ILE H H 7.94 . 1 294 45 ILE HA H 3.69 . 1 295 45 ILE HB H 1.75 . 1 296 45 ILE HG2 H 0.97 . 1 297 45 ILE HG12 H 0.67 . 1 298 45 ILE HG13 H 0.67 . 1 299 45 ILE HD1 H 0.97 . 1 300 46 GLU H H 7.47 . 1 301 46 GLU HA H 4.13 . 1 302 46 GLU HB2 H 2.26 . 2 303 46 GLU HB3 H 2.06 . 2 304 46 GLU HG2 H 2.22 . 1 305 46 GLU HG3 H 2.22 . 1 306 47 TRP H H 8.98 . 1 307 47 TRP HA H 4.74 . 1 308 47 TRP HB2 H 3.61 . 2 309 47 TRP HB3 H 3.16 . 2 310 47 TRP HD1 H 7.22 . 1 311 47 TRP HE3 H 7.43 . 1 312 47 TRP HE1 H 10.27 . 1 313 47 TRP HZ3 H 6.85 . 1 314 47 TRP HZ2 H 7.60 . 1 315 47 TRP HH2 H 7.29 . 1 316 48 LEU H H 9.07 . 1 317 48 LEU HA H 4.15 . 1 318 48 LEU HB2 H 2.40 . 2 319 48 LEU HB3 H 2.29 . 2 320 48 LEU HG H 1.51 . 1 321 48 LEU HD1 H 1.10 . 2 322 48 LEU HD2 H 0.98 . 2 323 49 GLU H H 8.25 . 1 324 49 GLU HA H 4.10 . 1 325 49 GLU HB2 H 2.44 . 2 326 49 GLU HB3 H 2.18 . 2 327 49 GLU HG2 H 2.87 . 1 328 49 GLU HG3 H 2.87 . 1 329 50 THR H H 7.90 . 1 330 50 THR HA H 4.37 . 1 331 50 THR HB H 4.50 . 1 332 50 THR HG2 H 1.44 . 1 333 51 ILE H H 7.58 . 1 334 51 ILE HA H 4.43 . 1 335 51 ILE HB H 2.12 . 1 336 51 ILE HG2 H 0.91 . 1 337 51 ILE HG12 H 1.60 . 1 338 51 ILE HG13 H 1.60 . 1 339 51 ILE HD1 H 0.91 . 1 340 52 ASN H H 7.89 . 1 341 52 ASN HA H 4.79 . 1 342 52 ASN HB2 H 2.87 . 2 343 52 ASN HB3 H 2.77 . 2 344 52 ASN HD21 H 7.58 . 2 345 52 ASN HD22 H 6.66 . 2 346 53 GLY H H 7.82 . 1 347 53 GLY HA2 H 3.79 . 1 348 53 GLY HA3 H 3.79 . 1 stop_ save_