data_4210 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; DNA-binding domain of human telomeric protein, hTRF1 ; _BMRB_accession_number 4210 _BMRB_flat_file_name bmr4210.str _Entry_type original _Submission_date 1998-04-23 _Accession_date 1998-04-23 _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 Nishikawa T. . . 2 Nagadoi A. . . 3 Yoshimura S. . . 4 Aimoto S. . . 5 Nishimura Y. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 326 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-03-10 original author . stop_ _Original_release_date 2000-03-10 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Nishikawa T, Nagadoi A, Yoshimura S, Aimoto S, Nishimura Y. Solution structure of the DNA-binding domain of human telomeric protein, hTRF1. Structure 6, 1057-1065 (1998). ; _Citation_title 'Solution structure of the DNA-binding domain of human telomeric protein, hTRF1' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98416700 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Nishikawa T. . . 2 Nagadoi A. . . 3 Yoshimura S. . . 4 Aimoto S. . . 5 Nishimura Y. . . stop_ _Journal_abbreviation Structure _Journal_volume 6 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1057 _Page_last 1065 _Year 1998 _Details . loop_ _Keyword 'DNA-binding domain' 'Myb repeats' NMR telomeres TRF stop_ save_ ################################## # Molecular system description # ################################## save_system_hTRF1 _Saveframe_category molecular_system _Mol_system_name hTRF1 _Abbreviation_common hTRF1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label hTRF1 $hTRF1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_hTRF1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common hTRF1 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 53 _Mol_residue_sequence ; RKRQAWLWEEDKNLRSGVRK YGEGNWSKILLHYKFNNRTS VMLKDRWRTMKKL ; loop_ _Residue_seq_code _Residue_label 1 ARG 2 LYS 3 ARG 4 GLN 5 ALA 6 TRP 7 LEU 8 TRP 9 GLU 10 GLU 11 ASP 12 LYS 13 ASN 14 LEU 15 ARG 16 SER 17 GLY 18 VAL 19 ARG 20 LYS 21 TYR 22 GLY 23 GLU 24 GLY 25 ASN 26 TRP 27 SER 28 LYS 29 ILE 30 LEU 31 LEU 32 HIS 33 TYR 34 LYS 35 PHE 36 ASN 37 ASN 38 ARG 39 THR 40 SER 41 VAL 42 MET 43 LEU 44 LYS 45 ASP 46 ARG 47 TRP 48 ARG 49 THR 50 MET 51 LYS 52 LYS 53 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-13 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 BMRB 26594 hTRF1 100.00 53 100.00 100.00 1.79e-28 BMRB 26595 hTRF1 100.00 53 100.00 100.00 1.79e-28 PDB 1BA5 "Dna-Binding Domain Of Human Telomeric Protein, Htrf1, Nmr, 18 Structures" 100.00 53 100.00 100.00 1.79e-28 PDB 1ITY "Solution Structure Of The Dna Binding Domain Of Human Trf1" 100.00 69 100.00 100.00 7.59e-29 PDB 1IV6 "Solution Structure Of The Dna Complex Of Human Trf1" 100.00 70 100.00 100.00 6.47e-29 PDB 1W0T "Htrf1 Dna-Binding Domain In Complex With Telomeric Dna" 98.11 53 100.00 100.00 7.17e-28 DBJ BAE88046 "unnamed protein product [Macaca fascicularis]" 100.00 282 98.11 100.00 3.74e-28 DBJ BAF85218 "unnamed protein product [Homo sapiens]" 100.00 439 100.00 100.00 1.15e-28 EMBL CAA63768 "telomeric DNA binding protein [Homo sapiens]" 100.00 111 100.00 100.00 9.18e-30 EMBL CAH92488 "hypothetical protein [Pongo abelii]" 100.00 436 100.00 100.00 1.62e-28 GB AAB53363 "telomeric repeat DNA-binding protein [Homo sapiens]" 100.00 419 100.00 100.00 1.33e-28 GB AAB54036 "telomeric repeat binding factor [Homo sapiens]" 100.00 439 100.00 100.00 1.08e-28 GB AAB81137 "TTAGGG repeat binding factor 1 [Homo sapiens]" 100.00 419 100.00 100.00 1.33e-28 GB AAC02531 "telomeric repeat binding factor 1 [Cricetulus griseus]" 100.00 438 100.00 100.00 1.13e-28 GB AAH29378 "Telomeric repeat binding factor (NIMA-interacting) 1 [Homo sapiens]" 100.00 419 100.00 100.00 1.28e-28 REF NP_001126467 "telomeric repeat-binding factor 1 [Pongo abelii]" 100.00 436 100.00 100.00 1.62e-28 REF NP_003209 "telomeric repeat-binding factor 1 isoform 2 [Homo sapiens]" 100.00 419 100.00 100.00 1.28e-28 REF NP_059523 "telomeric repeat-binding factor 1 isoform 1 [Homo sapiens]" 100.00 439 100.00 100.00 1.12e-28 REF XP_001083645 "PREDICTED: telomeric repeat-binding factor 1 isoform 1 [Macaca mulatta]" 100.00 438 98.11 100.00 4.35e-28 REF XP_001164723 "PREDICTED: telomeric repeat-binding factor 1 isoform X1 [Pan troglodytes]" 100.00 439 100.00 100.00 1.15e-28 SP O55036 "RecName: Full=Telomeric repeat-binding factor 1; AltName: Full=TTAGGG repeat-binding factor 1" 100.00 438 100.00 100.00 1.13e-28 SP P54274 "RecName: Full=Telomeric repeat-binding factor 1; AltName: Full=NIMA-interacting protein 2; AltName: Full=TTAGGG repeat-binding " 100.00 439 100.00 100.00 1.12e-28 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Fraction $hTRF1 Human 9606 . . Homo sapiens nucleus 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 $hTRF1 'chemical synthesis' . . . . . 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 $hTRF1 1.6 mM . 'Phosphate potassium' 100 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX2 _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name COSY _Sample_label . save_ save_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label . save_ save_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 . n/a pressure 1 . atm temperature 300 . 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 Dioxane H 1 'methylene protons' ppm 3.66 external direct . . . 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_chem_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 hTRF1 _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 ARG H H 8.69 . 1 2 . 3 ARG HA H 4.34 . 1 3 . 3 ARG HB2 H 1.83 . 1 4 . 3 ARG HB3 H 1.83 . 1 5 . 3 ARG HG2 H 1.69 . 2 6 . 3 ARG HG3 H 1.65 . 2 7 . 4 GLN H H 8.70 . 1 8 . 4 GLN HA H 4.34 . 1 9 . 4 GLN HB2 H 1.97 . 1 10 . 4 GLN HB3 H 1.97 . 1 11 . 4 GLN HG2 H 2.36 . 1 12 . 4 GLN HG3 H 2.36 . 1 13 . 5 ALA H H 8.53 . 1 14 . 5 ALA HA H 4.39 . 1 15 . 5 ALA HB H 1.46 . 1 16 . 6 TRP H H 9.10 . 1 17 . 6 TRP HA H 4.54 . 1 18 . 6 TRP HB2 H 3.01 . 1 19 . 6 TRP HB3 H 3.31 . 1 20 . 6 TRP HD1 H 7.34 . 1 21 . 6 TRP HE1 H 9.96 . 1 22 . 6 TRP HE3 H 7.76 . 1 23 . 6 TRP HZ2 H 7.09 . 1 24 . 6 TRP HZ3 H 6.99 . 1 25 . 6 TRP HH2 H 6.67 . 1 26 . 7 LEU H H 9.18 . 1 27 . 7 LEU HA H 4.71 . 1 28 . 7 LEU HB2 H 2.01 . 2 29 . 7 LEU HB3 H 1.84 . 2 30 . 7 LEU HG H 1.84 . 1 31 . 7 LEU HD1 H 0.95 . 1 32 . 7 LEU HD2 H 0.95 . 1 33 . 8 TRP H H 9.10 . 1 34 . 8 TRP HA H 4.54 . 1 35 . 8 TRP HB3 H 3.34 . 2 36 . 8 TRP HB2 H 3.65 . 2 37 . 8 TRP HD1 H 7.44 . 1 38 . 8 TRP HE1 H 10.26 . 1 39 . 8 TRP HE3 H 7.64 . 1 40 . 8 TRP HZ2 H 7.55 . 1 41 . 8 TRP HZ3 H 7.20 . 1 42 . 8 TRP HH2 H 7.27 . 1 43 . 9 GLU H H 8.98 . 1 44 . 9 GLU HA H 3.61 . 1 45 . 9 GLU HB2 H 1.85 . 1 46 . 9 GLU HB3 H 1.85 . 1 47 . 9 GLU HG2 H 2.21 . 2 48 . 9 GLU HG3 H 2.11 . 2 49 . 10 GLU H H 7.16 . 1 50 . 10 GLU HA H 4.03 . 1 51 . 10 GLU HB2 H 2.96 . 1 52 . 10 GLU HB3 H 2.66 . 1 53 . 10 GLU HG2 H 2.51 . 2 54 . 10 GLU HG3 H 2.18 . 2 55 . 11 ASP H H 7.98 . 1 56 . 11 ASP HA H 4.62 . 1 57 . 11 ASP HB2 H 2.78 . 2 58 . 11 ASP HB3 H 2.51 . 2 59 . 12 LYS H H 8.19 . 1 60 . 12 LYS HA H 3.99 . 1 61 . 12 LYS HB2 H 1.62 . 4 62 . 12 LYS HB3 H 1.62 . 4 63 . 12 LYS HG2 H 1.37 . 4 64 . 12 LYS HG3 H 1.37 . 4 65 . 12 LYS HD2 H 1.22 . 1 66 . 12 LYS HD3 H 1.22 . 1 67 . 13 ASN H H 8.03 . 1 68 . 13 ASN HA H 4.12 . 1 69 . 13 ASN HB2 H 2.69 . 2 70 . 13 ASN HB3 H 2.03 . 2 71 . 13 ASN HD21 H 7.20 . 2 72 . 13 ASN HD22 H 6.94 . 2 73 . 14 LEU H H 8.79 . 1 74 . 14 LEU HA H 4.20 . 1 75 . 14 LEU HB2 H 1.94 . 1 76 . 14 LEU HB3 H 2.91 . 1 77 . 14 LEU HG H 1.87 . 1 78 . 14 LEU HD1 H 1.14 . 1 79 . 14 LEU HD2 H 1.04 . 1 80 . 15 ARG H H 8.17 . 1 81 . 15 ARG HA H 3.81 . 1 82 . 15 ARG HB2 H 2.06 . 4 83 . 15 ARG HB3 H 2.06 . 4 84 . 15 ARG HG2 H 1.79 . 4 85 . 15 ARG HG3 H 1.99 . 4 86 . 15 ARG HD2 H 3.38 . 2 87 . 15 ARG HD3 H 3.28 . 2 88 . 16 SER H H 8.55 . 1 89 . 16 SER HA H 4.11 . 1 90 . 16 SER HB2 H 3.94 . 2 91 . 16 SER HB3 H 3.86 . 2 92 . 17 GLY H H 8.67 . 1 93 . 17 GLY HA2 H 4.05 . 2 94 . 17 GLY HA3 H 3.58 . 2 95 . 18 VAL H H 8.52 . 1 96 . 18 VAL HA H 3.12 . 1 97 . 18 VAL HB H 1.33 . 1 98 . 18 VAL HG1 H 0.29 . 1 99 . 18 VAL HG2 H -0.10 . 1 100 . 19 ARG H H 7.59 . 1 101 . 19 ARG HA H 3.92 . 1 102 . 19 ARG HB2 H 1.94 . 1 103 . 19 ARG HB3 H 1.94 . 1 104 . 19 ARG HG2 H 1.75 . 2 105 . 19 ARG HG3 H 1.61 . 2 106 . 19 ARG HD2 H 3.24 . 1 107 . 19 ARG HD3 H 3.24 . 1 108 . 20 LYS H H 7.76 . 1 109 . 20 LYS HA H 3.92 . 1 110 . 20 LYS HB2 H 1.55 . 2 111 . 20 LYS HB3 H 1.34 . 2 112 . 20 LYS HG2 H 0.78 . 2 113 . 20 LYS HG3 H 0.24 . 2 114 . 21 TYR H H 8.77 . 1 115 . 21 TYR HA H 4.62 . 1 116 . 21 TYR HB2 H 3.09 . 2 117 . 21 TYR HB3 H 2.64 . 2 118 . 21 TYR HD1 H 7.20 . 1 119 . 21 TYR HD2 H 7.20 . 1 120 . 21 TYR HE1 H 6.65 . 1 121 . 21 TYR HE2 H 6.65 . 1 122 . 22 GLY H H 7.89 . 1 123 . 22 GLY HA2 H 4.23 . 2 124 . 22 GLY HA3 H 3.74 . 2 125 . 23 GLU H H 8.38 . 1 126 . 23 GLU HA H 3.04 . 1 127 . 23 GLU HB2 H 2.03 . 2 128 . 23 GLU HB3 H 1.83 . 2 129 . 23 GLU HG2 H 2.26 . 2 130 . 23 GLU HG3 H 2.16 . 2 131 . 24 GLY H H 5.45 . 1 132 . 24 GLY HA2 H 4.12 . 2 133 . 24 GLY HA3 H 3.47 . 2 134 . 25 ASN H H 7.16 . 1 135 . 25 ASN HA H 5.04 . 1 136 . 25 ASN HB2 H 2.66 . 2 137 . 25 ASN HB3 H 2.18 . 2 138 . 25 ASN HD21 H 7.67 . 2 139 . 25 ASN HD22 H 6.98 . 2 140 . 26 TRP H H 6.66 . 1 141 . 26 TRP HA H 4.20 . 1 142 . 26 TRP HB2 H 3.16 . 1 143 . 26 TRP HB3 H 3.51 . 1 144 . 26 TRP HD1 H 7.49 . 1 145 . 26 TRP HE1 H 10.90 . 1 146 . 26 TRP HE3 H 7.23 . 1 147 . 26 TRP HZ2 H 7.77 . 1 148 . 26 TRP HZ3 H 6.48 . 1 149 . 26 TRP HH2 H 6.85 . 1 150 . 27 SER H H 8.78 . 1 151 . 27 SER HA H 3.96 . 1 152 . 27 SER HB2 H 4.19 . 1 153 . 27 SER HB3 H 4.19 . 1 154 . 28 LYS H H 7.30 . 1 155 . 28 LYS HA H 3.94 . 1 156 . 28 LYS HB2 H 1.47 . 2 157 . 28 LYS HB3 H 1.13 . 2 158 . 28 LYS HG2 H 0.98 . 1 159 . 28 LYS HG3 H 0.98 . 1 160 . 29 ILE H H 7.47 . 1 161 . 29 ILE HA H 3.71 . 1 162 . 29 ILE HB H 2.01 . 1 163 . 29 ILE HG12 H 0.82 . 1 164 . 29 ILE HG13 H 0.82 . 1 165 . 29 ILE HG2 H 1.27 . 1 166 . 29 ILE HD1 H 0.59 . 1 167 . 30 LEU H H 8.01 . 1 168 . 30 LEU HA H 4.29 . 1 169 . 30 LEU HB2 H 1.87 . 1 170 . 30 LEU HB3 H 1.87 . 1 171 . 30 LEU HG H 1.65 . 1 172 . 30 LEU HD1 H 0.86 . 2 173 . 30 LEU HD2 H 0.79 . 2 174 . 31 LEU H H 7.26 . 1 175 . 31 LEU HA H 4.27 . 1 176 . 31 LEU HB2 H 1.66 . 2 177 . 31 LEU HB3 H 1.46 . 2 178 . 31 LEU HG H 1.59 . 1 179 . 31 LEU HD1 H 0.85 . 2 180 . 31 LEU HD2 H 0.81 . 2 181 . 32 HIS H H 7.72 . 1 182 . 32 HIS HA H 4.44 . 1 183 . 32 HIS HB2 H 3.13 . 2 184 . 32 HIS HB3 H 2.90 . 2 185 . 32 HIS HD1 H 8.10 . 1 186 . 32 HIS HD2 H 6.57 . 1 187 . 33 TYR H H 7.90 . 1 188 . 33 TYR HA H 4.62 . 1 189 . 33 TYR HB2 H 2.86 . 2 190 . 33 TYR HB3 H 2.51 . 2 191 . 33 TYR HD1 H 7.46 . 1 192 . 33 TYR HD2 H 7.46 . 1 193 . 33 TYR HE1 H 6.82 . 1 194 . 33 TYR HE2 H 6.82 . 1 195 . 34 LYS H H 7.91 . 1 196 . 34 LYS HA H 4.38 . 1 197 . 34 LYS HB2 H 1.61 . 1 198 . 34 LYS HB3 H 1.61 . 1 199 . 34 LYS HG2 H 1.25 . 4 200 . 34 LYS HG3 H 1.25 . 4 201 . 34 LYS HD2 H 1.37 . 4 202 . 34 LYS HD3 H 1.37 . 4 203 . 35 PHE H H 8.48 . 1 204 . 35 PHE HA H 4.71 . 1 205 . 35 PHE HB2 H 3.09 . 2 206 . 35 PHE HB3 H 2.93 . 2 207 . 35 PHE HD1 H 7.51 . 1 208 . 35 PHE HD2 H 7.51 . 1 209 . 35 PHE HE1 H 7.71 . 1 210 . 35 PHE HE2 H 7.71 . 1 211 . 35 PHE HZ H 6.73 . 1 212 . 36 ASN H H 9.45 . 1 213 . 36 ASN HA H 4.81 . 1 214 . 36 ASN HB2 H 2.75 . 2 215 . 36 ASN HB3 H 2.57 . 2 216 . 36 ASN HD21 H 7.33 . 2 217 . 36 ASN HD22 H 6.79 . 2 218 . 37 ASN H H 8.47 . 1 219 . 37 ASN HA H 4.31 . 1 220 . 37 ASN HB2 H 2.94 . 2 221 . 37 ASN HB3 H 2.63 . 2 222 . 37 ASN HD21 H 7.53 . 2 223 . 37 ASN HD22 H 6.88 . 2 224 . 38 ARG H H 8.06 . 1 225 . 38 ARG HA H 5.08 . 1 226 . 38 ARG HB2 H 1.48 . 1 227 . 38 ARG HB3 H 1.63 . 1 228 . 38 ARG HG2 H 1.30 . 1 229 . 38 ARG HG3 H 1.30 . 1 230 . 38 ARG HD2 H 2.36 . 2 231 . 38 ARG HD3 H 2.75 . 2 232 . 39 THR H H 7.11 . 1 233 . 39 THR HA H 4.72 . 1 234 . 39 THR HB H 4.72 . 1 235 . 39 THR HG2 H 1.26 . 1 236 . 40 SER H H 9.31 . 1 237 . 40 SER HA H 3.82 . 1 238 . 40 SER HB2 H 3.97 . 1 239 . 40 SER HB3 H 3.97 . 1 240 . 41 VAL H H 7.52 . 1 241 . 41 VAL HA H 3.59 . 1 242 . 41 VAL HB H 1.96 . 1 243 . 41 VAL HG1 H 1.02 . 2 244 . 41 VAL HG2 H 0.92 . 2 245 . 42 MET H H 7.36 . 1 246 . 42 MET HA H 4.31 . 1 247 . 42 MET HB2 H 2.34 . 1 248 . 42 MET HB3 H 2.34 . 1 249 . 42 MET HG2 H 2.90 . 1 250 . 42 MET HG3 H 2.90 . 1 251 . 43 LEU H H 7.55 . 1 252 . 43 LEU HA H 3.82 . 1 253 . 43 LEU HB2 H 1.86 . 1 254 . 43 LEU HB3 H 1.41 . 1 255 . 43 LEU HG H 1.68 . 1 256 . 43 LEU HD1 H 0.64 . 1 257 . 43 LEU HD2 H 0.34 . 1 258 . 44 LYS H H 6.88 . 1 259 . 44 LYS HA H 2.11 . 1 260 . 44 LYS HB2 H 1.44 . 2 261 . 44 LYS HB3 H 0.33 . 2 262 . 44 LYS HG2 H 1.24 . 2 263 . 44 LYS HG3 H 1.06 . 2 264 . 45 ASP H H 8.03 . 1 265 . 45 ASP HA H 4.25 . 1 266 . 45 ASP HB2 H 2.60 . 2 267 . 45 ASP HB3 H 2.56 . 2 268 . 46 ARG H H 7.96 . 1 269 . 46 ARG HA H 3.71 . 1 270 . 46 ARG HB2 H 1.35 . 2 271 . 46 ARG HB3 H 0.85 . 2 272 . 46 ARG HG2 H -0.25 . 2 273 . 46 ARG HG3 H 0.73 . 2 274 . 47 TRP H H 8.42 . 1 275 . 47 TRP HA H 4.42 . 1 276 . 47 TRP HB2 H 3.19 . 1 277 . 47 TRP HB3 H 3.19 . 1 278 . 47 TRP HD1 H 7.43 . 1 279 . 47 TRP HE1 H 10.53 . 1 280 . 47 TRP HE3 H 7.52 . 1 281 . 47 TRP HZ2 H 7.55 . 1 282 . 47 TRP HZ3 H 6.88 . 1 283 . 47 TRP HH2 H 7.26 . 1 284 . 48 ARG H H 7.68 . 1 285 . 48 ARG HA H 3.75 . 1 286 . 48 ARG HB2 H 1.96 . 1 287 . 48 ARG HB3 H 1.96 . 1 288 . 48 ARG HG2 H 1.59 . 2 289 . 48 ARG HG3 H 1.80 . 2 290 . 48 ARG HD2 H 3.24 . 1 291 . 48 ARG HD3 H 3.24 . 1 292 . 49 THR H H 7.52 . 1 293 . 49 THR HA H 3.88 . 1 294 . 49 THR HB H 4.18 . 1 295 . 49 THR HG2 H 1.13 . 1 296 . 50 MET H H 8.04 . 1 297 . 50 MET HA H 3.86 . 1 298 . 50 MET HB2 H 1.71 . 1 299 . 50 MET HB3 H 1.71 . 1 300 . 50 MET HG2 H 2.40 . 2 301 . 50 MET HG3 H 2.24 . 2 302 . 51 LYS H H 7.85 . 1 303 . 51 LYS HA H 3.60 . 1 304 . 51 LYS HB2 H 1.34 . 1 305 . 51 LYS HB3 H 1.34 . 1 306 . 51 LYS HG2 H 1.55 . 4 307 . 51 LYS HG3 H 1.55 . 4 308 . 51 LYS HD2 H 1.00 . 4 309 . 51 LYS HD3 H 1.00 . 4 310 . 51 LYS HE2 H 2.91 . 2 311 . 51 LYS HE3 H 2.85 . 2 312 . 52 LYS H H 7.49 . 1 313 . 52 LYS HA H 4.10 . 1 314 . 52 LYS HB2 H 1.86 . 4 315 . 52 LYS HB3 H 1.79 . 4 316 . 52 LYS HG2 H 1.45 . 4 317 . 52 LYS HG3 H 1.37 . 4 318 . 52 LYS HD2 H 1.62 . 1 319 . 52 LYS HD3 H 1.62 . 1 320 . 53 LEU H H 7.70 . 1 321 . 53 LEU HA H 4.20 . 1 322 . 53 LEU HB2 H 1.69 . 4 323 . 53 LEU HB3 H 1.69 . 4 324 . 53 LEU HG H 1.56 . 4 325 . 53 LEU HD1 H 0.87 . 1 326 . 53 LEU HD2 H 0.83 . 1 stop_ save_