data_6303 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of a diiron protein model ; _BMRB_accession_number 6303 _BMRB_flat_file_name bmr6303.str _Entry_type original _Submission_date 2004-08-26 _Accession_date 2004-08-26 _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 Maglio O. . . 2 Nastri F. . . 3 Calhoun J. R. . 4 Lahr S. . . 5 Pavone V. . . 6 DeGrado W. F. . 7 Lombardi A. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 305 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-05-19 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 6302 'DF2-TURN MUTANT' stop_ _Original_release_date 2005-05-19 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Artificial diiron proteins: From structure to function' _Citation_status published _Citation_type journal _CAS_abstract_code . _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 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 264 _Page_last 278 _Year 2005 _Details . loop_ _Keyword 'Diiron proteins' 'four-helix bundle' 'inter-helical loops' 'protein design' stop_ save_ ################################## # Molecular system description # ################################## save_system_DF2 _Saveframe_category molecular_system _Mol_system_name 'Four-helix bundle' _Abbreviation_common 'Four-helix bundle' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Four-helix bundle chain A' $DF2 'Four-helix bundle chain B' $DF2 'ZINC (II) ION 1' $ZN 'ZINC (II) ION 2' $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'Four-helix bundle chain A' 1 'Four-helix bundle chain B' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_DF2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Four-helix bundle' _Abbreviation_common 'Four-helix bundle' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 49 _Mol_residue_sequence ; MDYLRELYKLEQQAMKLYRE ASERVGDPVLAKILEDEEKH IEWLETING ; 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 ARG 25 VAL 26 GLY 27 ASP 28 PRO 29 VAL 30 LEU 31 ALA 32 LYS 33 ILE 34 LEU 35 GLU 36 ASP 37 GLU 38 GLU 39 LYS 40 HIS 41 ILE 42 GLU 43 TRP 44 LEU 45 GLU 46 THR 47 ILE 48 ASN 49 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 1U7J "Solution Structure Of A Diiron Protein Model" 100.00 49 100.00 100.00 1.35e-25 PDB 1Y47 "Structural Studies Of Designed Alpha-Helical Hairpins" 93.88 46 100.00 100.00 1.18e-22 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jun 15 12:20:01 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $DF2 'E. coli' 562 Bacteria . 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 'recombinant technology' Bacteria Escherichia coli BL21(DE3) 'Plasmid PET15B' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DF2 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 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label $sample_1 save_ save_DQF-COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label $sample_1 save_ save_2D_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.1 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label TSP H 1 'methyl protons' ppm 0.0 internal . . . . 1.0 $entry_citation $entry_citation 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_set_1 _Saveframe_category assigned_chemical_shifts _Details . 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' _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 . 3 TYR H H 8.12 . 1 2 . 3 TYR HA H 3.96 . 1 3 . 3 TYR HB2 H 2.91 . 1 4 . 3 TYR HB3 H 2.91 . 1 5 . 3 TYR HD1 H 7.12 . 1 6 . 3 TYR HD2 H 7.12 . 1 7 . 3 TYR HE1 H 6.84 . 1 8 . 3 TYR HE2 H 6.84 . 1 9 . 4 LEU H H 8.21 . 1 10 . 4 LEU HA H 4.10 . 1 11 . 4 LEU HB2 H 1.85 . 2 12 . 4 LEU HB3 H 1.77 . 2 13 . 4 LEU HG H 1.62 . 1 14 . 4 LEU HD1 H 1.04 . 1 15 . 4 LEU HD2 H 1.04 . 1 16 . 5 ARG H H 7.67 . 1 17 . 5 ARG HA H 4.12 . 1 18 . 5 ARG HB2 H 1.77 . 1 19 . 5 ARG HB3 H 1.77 . 1 20 . 5 ARG HG2 H 1.89 . 1 21 . 5 ARG HG3 H 1.89 . 1 22 . 5 ARG HD2 H 3.23 . 1 23 . 5 ARG HD3 H 3.23 . 1 24 . 6 GLU H H 8.03 . 1 25 . 6 GLU HA H 4.14 . 1 26 . 6 GLU HB2 H 2.05 . 2 27 . 6 GLU HB3 H 1.89 . 2 28 . 6 GLU HG2 H 2.39 . 2 29 . 6 GLU HG3 H 2.33 . 2 30 . 7 LEU H H 8.54 . 1 31 . 7 LEU HA H 3.92 . 1 32 . 7 LEU HB2 H 1.95 . 2 33 . 7 LEU HB3 H 1.66 . 2 34 . 7 LEU HG H 1.39 . 1 35 . 7 LEU HD1 H 0.56 . 2 36 . 7 LEU HD2 H -0.06 . 2 37 . 8 TYR H H 8.10 . 1 38 . 8 TYR HA H 3.96 . 1 39 . 8 TYR HB2 H 3.22 . 2 40 . 8 TYR HB3 H 3.16 . 2 41 . 8 TYR HD1 H 7.09 . 1 42 . 8 TYR HD2 H 7.09 . 1 43 . 8 TYR HE1 H 6.92 . 1 44 . 8 TYR HE2 H 6.92 . 1 45 . 9 LYS H H 7.78 . 1 46 . 9 LYS HA H 4.08 . 1 47 . 9 LYS HB2 H 1.93 . 1 48 . 9 LYS HB3 H 1.93 . 1 49 . 9 LYS HG2 H 1.51 . 1 50 . 9 LYS HG3 H 1.51 . 1 51 . 9 LYS HD2 H 1.75 . 1 52 . 9 LYS HD3 H 1.75 . 1 53 . 9 LYS HE2 H 2.97 . 1 54 . 9 LYS HE3 H 2.97 . 1 55 . 10 LEU H H 7.90 . 1 56 . 10 LEU HA H 4.20 . 1 57 . 10 LEU HB2 H 1.91 . 1 58 . 10 LEU HB3 H 1.91 . 1 59 . 10 LEU HG H 1.73 . 1 60 . 10 LEU HD1 H 0.91 . 1 61 . 10 LEU HD2 H 0.91 . 1 62 . 11 GLU H H 8.62 . 1 63 . 11 GLU HA H 4.55 . 1 64 . 11 GLU HB2 H 2.15 . 2 65 . 11 GLU HB3 H 2.01 . 2 66 . 11 GLU HG2 H 2.77 . 2 67 . 11 GLU HG3 H 2.37 . 2 68 . 12 GLN H H 8.26 . 1 69 . 12 GLN HA H 3.94 . 1 70 . 12 GLN HB2 H 2.39 . 2 71 . 12 GLN HB3 H 2.18 . 2 72 . 12 GLN HG2 H 2.31 . 2 73 . 12 GLN HG3 H 1.99 . 2 74 . 12 GLN HE21 H 6.96 . 2 75 . 12 GLN HE22 H 6.54 . 2 76 . 13 GLN H H 7.97 . 1 77 . 13 GLN HA H 4.13 . 1 78 . 13 GLN HB2 H 2.42 . 2 79 . 13 GLN HB3 H 2.27 . 2 80 . 13 GLN HG2 H 2.53 . 2 81 . 13 GLN HG3 H 2.16 . 2 82 . 13 GLN HE21 H 7.22 . 2 83 . 13 GLN HE22 H 6.87 . 2 84 . 14 ALA H H 8.96 . 1 85 . 14 ALA HA H 3.98 . 1 86 . 14 ALA HB H 1.62 . 1 87 . 15 MET H H 8.95 . 1 88 . 15 MET HA H 3.97 . 1 89 . 15 MET HB2 H 2.18 . 1 90 . 15 MET HB3 H 2.18 . 1 91 . 15 MET HG2 H 2.58 . 1 92 . 15 MET HG3 H 2.58 . 1 93 . 15 MET HE H 1.97 . 1 94 . 16 LYS H H 7.70 . 1 95 . 16 LYS HA H 3.98 . 1 96 . 16 LYS HB2 H 1.98 . 1 97 . 16 LYS HB3 H 1.98 . 1 98 . 16 LYS HG2 H 1.41 . 1 99 . 16 LYS HG3 H 1.41 . 1 100 . 16 LYS HD2 H 1.70 . 1 101 . 16 LYS HD3 H 1.70 . 1 102 . 16 LYS HE2 H 3.02 . 1 103 . 16 LYS HE3 H 3.02 . 1 104 . 17 LEU H H 8.07 . 1 105 . 17 LEU HA H 4.30 . 1 106 . 17 LEU HB2 H 1.97 . 2 107 . 17 LEU HB3 H 1.54 . 2 108 . 17 LEU HG H 1.72 . 1 109 . 17 LEU HD1 H 0.95 . 1 110 . 17 LEU HD2 H 0.95 . 1 111 . 18 TYR H H 9.47 . 1 112 . 18 TYR HA H 4.12 . 1 113 . 18 TYR HB2 H 3.04 . 2 114 . 18 TYR HB3 H 2.86 . 2 115 . 18 TYR HD1 H 6.98 . 1 116 . 18 TYR HD2 H 6.98 . 1 117 . 18 TYR HE1 H 6.66 . 1 118 . 18 TYR HE2 H 6.66 . 1 119 . 18 TYR HH H 9.93 . 1 120 . 19 ARG H H 8.51 . 1 121 . 19 ARG HA H 3.96 . 1 122 . 19 ARG HB2 H 2.00 . 2 123 . 19 ARG HB3 H 1.81 . 2 124 . 19 ARG HG2 H 1.68 . 1 125 . 19 ARG HG3 H 1.68 . 1 126 . 19 ARG HD2 H 3.22 . 1 127 . 19 ARG HD3 H 3.22 . 1 128 . 20 GLU H H 7.71 . 1 129 . 20 GLU HA H 4.04 . 1 130 . 20 GLU HB2 H 2.19 . 2 131 . 20 GLU HB3 H 1.97 . 2 132 . 20 GLU HG2 H 2.48 . 1 133 . 20 GLU HG3 H 2.48 . 1 134 . 21 ALA H H 8.75 . 1 135 . 21 ALA HA H 3.37 . 1 136 . 21 ALA HB H 1.32 . 1 137 . 22 SER H H 8.74 . 1 138 . 22 SER HA H 4.08 . 1 139 . 22 SER HB2 H 3.99 . 2 140 . 22 SER HB3 H 3.94 . 2 141 . 23 GLU H H 7.48 . 1 142 . 23 GLU HA H 4.10 . 1 143 . 23 GLU HB2 H 2.13 . 2 144 . 23 GLU HB3 H 1.73 . 2 145 . 23 GLU HG2 H 2.48 . 1 146 . 23 GLU HG3 H 2.48 . 1 147 . 24 ARG H H 7.77 . 1 148 . 24 ARG HA H 4.30 . 1 149 . 24 ARG HB2 H 1.73 . 1 150 . 24 ARG HB3 H 1.73 . 1 151 . 24 ARG HG2 H 1.79 . 1 152 . 24 ARG HG3 H 1.79 . 1 153 . 24 ARG HD2 H 3.22 . 1 154 . 24 ARG HD3 H 3.22 . 1 155 . 25 VAL H H 8.63 . 1 156 . 25 VAL HA H 4.14 . 1 157 . 25 VAL HB H 2.11 . 1 158 . 25 VAL HG1 H 1.09 . 2 159 . 25 VAL HG2 H 1.02 . 2 160 . 26 GLY H H 7.86 . 1 161 . 26 GLY HA2 H 4.12 . 2 162 . 26 GLY HA3 H 3.94 . 2 163 . 27 ASP H H 6.63 . 1 164 . 27 ASP HA H 4.96 . 1 165 . 27 ASP HB2 H 2.60 . 1 166 . 27 ASP HB3 H 2.60 . 1 167 . 28 PRO HA H 4.38 . 1 168 . 28 PRO HB2 H 2.41 . 1 169 . 28 PRO HB3 H 2.41 . 1 170 . 28 PRO HG2 H 2.06 . 2 171 . 28 PRO HG3 H 1.95 . 2 172 . 28 PRO HD2 H 4.06 . 2 173 . 28 PRO HD3 H 3.90 . 2 174 . 29 VAL H H 9.01 . 1 175 . 29 VAL HA H 3.52 . 1 176 . 29 VAL HB H 1.89 . 1 177 . 29 VAL HG1 H 0.80 . 2 178 . 29 VAL HG2 H 0.60 . 2 179 . 30 LEU H H 7.60 . 1 180 . 30 LEU HA H 3.92 . 1 181 . 30 LEU HB2 H 1.97 . 2 182 . 30 LEU HB3 H 1.79 . 2 183 . 30 LEU HG H 1.47 . 1 184 . 30 LEU HD1 H 0.98 . 1 185 . 30 LEU HD2 H 0.98 . 1 186 . 31 ALA H H 7.03 . 1 187 . 31 ALA HA H 4.01 . 1 188 . 31 ALA HB H 1.44 . 1 189 . 32 LYS H H 7.26 . 1 190 . 32 LYS HA H 4.05 . 1 191 . 32 LYS HB2 H 1.81 . 1 192 . 32 LYS HB3 H 1.81 . 1 193 . 32 LYS HG2 H 1.86 . 1 194 . 32 LYS HG3 H 1.86 . 1 195 . 32 LYS HD2 H 1.43 . 1 196 . 32 LYS HD3 H 1.43 . 1 197 . 32 LYS HE2 H 2.74 . 1 198 . 32 LYS HE3 H 2.74 . 1 199 . 33 ILE H H 8.02 . 1 200 . 33 ILE HA H 2.97 . 1 201 . 33 ILE HB H 1.07 . 1 202 . 33 ILE HG2 H -0.63 . 1 203 . 33 ILE HG12 H 1.07 . 1 204 . 33 ILE HG13 H 1.07 . 1 205 . 33 ILE HD1 H -0.63 . 1 206 . 34 LEU H H 7.73 . 1 207 . 34 LEU HA H 3.52 . 1 208 . 34 LEU HB2 H 1.49 . 1 209 . 34 LEU HB3 H 1.49 . 1 210 . 34 LEU HG H 1.44 . 1 211 . 34 LEU HD1 H 0.89 . 1 212 . 34 LEU HD2 H 0.89 . 1 213 . 35 GLU H H 7.21 . 1 214 . 35 GLU HA H 3.96 . 1 215 . 35 GLU HB2 H 2.12 . 2 216 . 35 GLU HB3 H 1.91 . 2 217 . 35 GLU HG2 H 2.46 . 2 218 . 35 GLU HG3 H 2.20 . 2 219 . 36 ASP H H 7.53 . 1 220 . 36 ASP HA H 4.13 . 1 221 . 36 ASP HB2 H 3.13 . 2 222 . 36 ASP HB3 H 2.09 . 2 223 . 37 GLU H H 8.23 . 1 224 . 37 GLU HA H 4.34 . 1 225 . 37 GLU HB2 H 1.69 . 1 226 . 37 GLU HB3 H 1.69 . 1 227 . 37 GLU HG2 H 2.61 . 1 228 . 37 GLU HG3 H 2.61 . 1 229 . 38 GLU H H 7.95 . 1 230 . 38 GLU HA H 3.93 . 1 231 . 38 GLU HB2 H 2.15 . 2 232 . 38 GLU HB3 H 1.95 . 2 233 . 38 GLU HG2 H 2.47 . 1 234 . 38 GLU HG3 H 2.47 . 1 235 . 39 LYS H H 7.32 . 1 236 . 39 LYS HA H 3.81 . 1 237 . 39 LYS HB2 H 1.66 . 1 238 . 39 LYS HB3 H 1.66 . 1 239 . 39 LYS HG2 H 1.36 . 2 240 . 39 LYS HG3 H 1.29 . 2 241 . 39 LYS HD2 H 0.67 . 1 242 . 39 LYS HD3 H 0.67 . 1 243 . 40 HIS H H 8.21 . 1 244 . 40 HIS HA H 4.16 . 1 245 . 40 HIS HB2 H 3.56 . 2 246 . 40 HIS HB3 H 3.13 . 2 247 . 40 HIS HD2 H 6.33 . 1 248 . 40 HIS HE1 H 7.43 . 1 249 . 40 HIS HE2 H 14.98 . 1 250 . 41 ILE H H 7.96 . 1 251 . 41 ILE HA H 3.70 . 1 252 . 41 ILE HB H 2.01 . 1 253 . 41 ILE HG2 H 0.96 . 1 254 . 41 ILE HG12 H 0.96 . 1 255 . 41 ILE HG13 H 0.96 . 1 256 . 41 ILE HD1 H 0.69 . 1 257 . 42 GLU H H 7.47 . 1 258 . 42 GLU HA H 4.14 . 1 259 . 42 GLU HB2 H 2.21 . 1 260 . 42 GLU HB3 H 2.21 . 1 261 . 42 GLU HG2 H 2.02 . 1 262 . 42 GLU HG3 H 2.02 . 1 263 . 43 TRP H H 8.87 . 1 264 . 43 TRP HA H 4.70 . 1 265 . 43 TRP HB2 H 3.56 . 2 266 . 43 TRP HB3 H 3.26 . 2 267 . 43 TRP HD1 H 7.22 . 1 268 . 43 TRP HE3 H 7.42 . 1 269 . 43 TRP HE1 H 10.28 . 1 270 . 43 TRP HZ3 H 6.84 . 1 271 . 43 TRP HZ2 H 7.54 . 1 272 . 43 TRP HH2 H 7.24 . 1 273 . 44 LEU H H 8.96 . 1 274 . 44 LEU HA H 4.10 . 1 275 . 44 LEU HB2 H 2.36 . 2 276 . 44 LEU HB3 H 2.28 . 2 277 . 44 LEU HG H 1.08 . 1 278 . 44 LEU HD1 H 0.91 . 1 279 . 44 LEU HD2 H 0.91 . 1 280 . 45 GLU H H 8.26 . 1 281 . 45 GLU HA H 4.11 . 1 282 . 45 GLU HB2 H 2.39 . 2 283 . 45 GLU HB3 H 2.19 . 2 284 . 45 GLU HG2 H 2.84 . 1 285 . 45 GLU HG3 H 2.84 . 1 286 . 46 THR H H 7.82 . 1 287 . 46 THR HA H 4.34 . 1 288 . 46 THR HB H 4.49 . 1 289 . 46 THR HG2 H 1.42 . 1 290 . 47 ILE H H 7.43 . 1 291 . 47 ILE HA H 4.12 . 1 292 . 47 ILE HB H 1.91 . 1 293 . 47 ILE HG2 H 0.89 . 1 294 . 47 ILE HG12 H 1.60 . 1 295 . 47 ILE HG13 H 1.60 . 1 296 . 47 ILE HD1 H 0.81 . 1 297 . 48 ASN H H 8.31 . 1 298 . 48 ASN HA H 4.75 . 1 299 . 48 ASN HB2 H 2.83 . 2 300 . 48 ASN HB3 H 2.71 . 2 301 . 48 ASN HD21 H 7.50 . 2 302 . 48 ASN HD22 H 6.60 . 2 303 . 49 GLY H H 7.82 . 1 304 . 49 GLY HA2 H 3.81 . 2 305 . 49 GLY HA3 H 3.77 . 2 stop_ save_