data_4639 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR structure of the hRap1 Myb motif reveals a canonical three helix bundle lacking the positive surface charge typical of Myb DNA binding domains ; _BMRB_accession_number 4639 _BMRB_flat_file_name bmr4639.str _Entry_type original _Submission_date 2000-07-24 _Accession_date 2001-03-16 _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 Hanaoka S . . 2 Nagadoi A . . 3 Yoshimura S . . 4 Aimoto S . . 5 Li B . . 6 'de Lange' T . . 7 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" 325 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-04-03 original author . stop_ _Original_release_date 2002-04-03 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR structure of the hRap1 Myb motif reveals a canonical three helix bundle lacking the positive surface charge typical of Myb DNA binding domains ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hanaoka S . . 2 Nagadoi A . . 3 Yoshimura S . . 4 Aimoto S . . 5 Li B . . 6 'de Lange' T . . 7 Nishimura Y . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 312 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 167 _Page_last 175 _Year 2001 _Details . loop_ _Keyword NMR telomere 'Myb motif' stop_ save_ ################################## # Molecular system description # ################################## save_system_RAP1 _Saveframe_category molecular_system _Mol_system_name 'human Rap1' _Abbreviation_common hRap1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'hRap1 Myb domain' $RAP1 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_RAP1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'TRF2-INTERACTING TELOMERIC RAP1 PROTEIN' _Abbreviation_common RAP1 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 59 _Mol_residue_sequence ; GRIAFTDADDVAILTYVKEN ARSPSSVTGNALWKAMEKSS LTQHSWQSLKDRYLKHLRG ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 ARG 3 ILE 4 ALA 5 PHE 6 THR 7 ASP 8 ALA 9 ASP 10 ASP 11 VAL 12 ALA 13 ILE 14 LEU 15 THR 16 TYR 17 VAL 18 LYS 19 GLU 20 ASN 21 ALA 22 ARG 23 SER 24 PRO 25 SER 26 SER 27 VAL 28 THR 29 GLY 30 ASN 31 ALA 32 LEU 33 TRP 34 LYS 35 ALA 36 MET 37 GLU 38 LYS 39 SER 40 SER 41 LEU 42 THR 43 GLN 44 HIS 45 SER 46 TRP 47 GLN 48 SER 49 LEU 50 LYS 51 ASP 52 ARG 53 TYR 54 LEU 55 LYS 56 HIS 57 LEU 58 ARG 59 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-02-24 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 1FEX "Solution Structure Of Myb-Domain Of Human Rap1" 100.00 59 100.00 100.00 1.14e-34 DBJ BAA91317 "unnamed protein product [Homo sapiens]" 100.00 298 100.00 100.00 1.38e-31 DBJ BAE00469 "unnamed protein product [Macaca fascicularis]" 88.14 238 100.00 100.00 9.53e-28 DBJ BAE01995 "unnamed protein product [Macaca fascicularis]" 100.00 400 100.00 100.00 4.01e-33 DBJ BAE87910 "unnamed protein product [Macaca fascicularis]" 100.00 398 100.00 100.00 3.81e-33 DBJ BAE88172 "unnamed protein product [Macaca fascicularis]" 100.00 241 100.00 100.00 8.04e-34 GB AAF72711 "TRF2-interacting telomeric RAP1 protein [Homo sapiens]" 100.00 399 100.00 100.00 4.44e-33 GB AAH04465 "Telomeric repeat binding factor 2, interacting protein [Homo sapiens]" 100.00 399 100.00 100.00 4.44e-33 GB AAH05841 "Telomeric repeat binding factor 2, interacting protein [Homo sapiens]" 100.00 399 100.00 100.00 4.44e-33 GB AAH22428 "Telomeric repeat binding factor 2, interacting protein [Homo sapiens]" 100.00 399 100.00 100.00 4.44e-33 GB AAH78171 "Telomeric repeat binding factor 2, interacting protein [Homo sapiens]" 100.00 399 100.00 100.00 4.44e-33 REF NP_001267142 "telomeric repeat-binding factor 2-interacting protein 1 [Pan troglodytes]" 100.00 399 100.00 100.00 7.59e-31 REF NP_061848 "telomeric repeat-binding factor 2-interacting protein 1 [Homo sapiens]" 100.00 399 100.00 100.00 4.44e-33 REF XP_001110856 "PREDICTED: telomeric repeat-binding factor 2-interacting protein 1 [Macaca mulatta]" 100.00 398 100.00 100.00 3.81e-33 REF XP_003780774 "PREDICTED: LOW QUALITY PROTEIN: telomeric repeat-binding factor 2-interacting protein 1 [Pongo abelii]" 100.00 377 100.00 100.00 2.86e-31 REF XP_003829596 "PREDICTED: LOW QUALITY PROTEIN: telomeric repeat-binding factor 2-interacting protein 1 [Pan paniscus]" 100.00 399 100.00 100.00 7.82e-31 SP Q4R4I0 "RecName: Full=Telomeric repeat-binding factor 2-interacting protein 1; Short=TERF2-interacting telomeric protein 1; Short=TRF2-" 100.00 400 100.00 100.00 4.01e-33 SP Q9NYB0 "RecName: Full=Telomeric repeat-binding factor 2-interacting protein 1; Short=TERF2-interacting telomeric protein 1; Short=TRF2-" 100.00 399 100.00 100.00 4.44e-33 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $RAP1 Human 9606 Eukaryota Metazoa Homo sapiens 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 $RAP1 '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 $RAP1 1.0 mM . 'potassium phosphate' 100 mM . NaN3 1.0 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 4.2.5 loop_ _Task processing stop_ _Details 'Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu,G., Pfeifer, J. and Bax,A.' save_ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.851 loop_ _Task 'structure solution' stop_ _Details Brunger,A.T. save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_DQF-COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H DQF-COSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_1H-1H_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.5 . pH temperature 300 . K pressure 1 . atm 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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 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 'hRap1 Myb domain' _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 . 2 ARG H H 8.221 . 1 2 . 2 ARG HA H 4.187 . 1 3 . 2 ARG HB2 H 1.545 . 2 4 . 2 ARG HB3 H 1.685 . 2 5 . 2 ARG HG2 H 1.43 . 1 6 . 2 ARG HG3 H 1.43 . 1 7 . 2 ARG HD2 H 3.025 . 1 8 . 2 ARG HD3 H 3.025 . 1 9 . 3 ILE H H 8.098 . 1 10 . 3 ILE HA H 3.978 . 1 11 . 3 ILE HB H 1.568 . 1 12 . 3 ILE HG12 H 1.221 . 1 13 . 3 ILE HG13 H 1.221 . 1 14 . 3 ILE HG2 H 0.938 . 1 15 . 3 ILE HD1 H 0.569 . 1 16 . 4 ALA H H 8.274 . 1 17 . 4 ALA HA H 4.188 . 1 18 . 4 ALA HB H 1.199 . 1 19 . 5 PHE H H 8.517 . 1 20 . 5 PHE HB2 H 2.758 . 1 21 . 5 PHE HB3 H 2.588 . 1 22 . 5 PHE HD1 H 6.927 . 1 23 . 5 PHE HD2 H 6.927 . 1 24 . 5 PHE HE1 H 6.688 . 1 25 . 5 PHE HE2 H 6.688 . 1 26 . 5 PHE HZ H 6.468 . 1 27 . 6 THR H H 8.835 . 1 28 . 6 THR HA H 4.525 . 1 29 . 6 THR HG2 H 1.116 . 1 30 . 7 ASP H H 8.709 . 1 31 . 7 ASP HA H 4.278 . 1 32 . 7 ASP HB2 H 2.631 . 1 33 . 7 ASP HB3 H 2.536 . 1 34 . 8 ALA H H 8.031 . 1 35 . 8 ALA HA H 3.998 . 1 36 . 8 ALA HB H 1.291 . 1 37 . 9 ASP H H 7.956 . 1 38 . 9 ASP HA H 4.166 . 1 39 . 9 ASP HB2 H 2.499 . 1 40 . 9 ASP HB3 H 3.338 . 1 41 . 10 ASP H H 7.763 . 1 42 . 10 ASP HA H 4.392 . 1 43 . 10 ASP HB2 H 2.782 . 1 44 . 10 ASP HB3 H 2.439 . 1 45 . 11 VAL H H 8.147 . 1 46 . 11 VAL HA H 3.595 . 1 47 . 11 VAL HB H 1.994 . 1 48 . 11 VAL HG1 H 0.845 . 1 49 . 11 VAL HG2 H 0.979 . 1 50 . 12 ALA H H 8.150 . 1 51 . 12 ALA HA H 4.091 . 1 52 . 12 ALA HB H 1.483 . 1 53 . 13 ILE H H 8.524 . 1 54 . 13 ILE HA H 3.646 . 1 55 . 13 ILE HB H 2.096 . 1 56 . 13 ILE HG12 H 1.067 . 1 57 . 13 ILE HG13 H 1.067 . 1 58 . 13 ILE HG2 H 0.839 . 1 59 . 14 LEU H H 8.407 . 1 60 . 14 LEU HA H 3.891 . 1 61 . 14 LEU HB2 H 1.947 . 1 62 . 14 LEU HB3 H 1.947 . 1 63 . 14 LEU HG H 1.458 . 1 64 . 14 LEU HD1 H 0.884 . 1 65 . 14 LEU HD2 H 0.997 . 1 66 . 15 THR H H 8.748 . 1 67 . 15 THR HA H 3.746 . 1 68 . 15 THR HB H 4.194 . 1 69 . 15 THR HG2 H 1.089 . 1 70 . 16 TYR H H 8.343 . 1 71 . 16 TYR HA H 3.749 . 1 72 . 16 TYR HB2 H 3.053 . 1 73 . 16 TYR HB3 H 3.053 . 1 74 . 16 TYR HD1 H 6.582 . 1 75 . 16 TYR HD2 H 6.582 . 1 76 . 16 TYR HE1 H 6.476 . 1 77 . 16 TYR HE2 H 6.476 . 1 78 . 17 VAL H H 8.566 . 1 79 . 17 VAL HA H 3.018 . 1 80 . 17 VAL HB H 1.856 . 1 81 . 17 VAL HG1 H 0.562 . 1 82 . 17 VAL HG2 H 0.453 . 1 83 . 18 LYS H H 7.82 . 1 84 . 18 LYS HA H 3.811 . 1 85 . 18 LYS HB2 H 1.572 . 1 86 . 18 LYS HB3 H 1.858 . 1 87 . 18 LYS HG2 H 1.281 . 2 88 . 18 LYS HG3 H 1.385 . 2 89 . 19 GLU H H 7.823 . 1 90 . 19 GLU HA H 3.909 . 1 91 . 19 GLU HB2 H 1.631 . 1 92 . 19 GLU HB3 H 1.631 . 1 93 . 19 GLU HG2 H 2.228 . 2 94 . 19 GLU HG3 H 2.001 . 2 95 . 20 ASN H H 7.631 . 1 96 . 20 ASN HA H 4.523 . 1 97 . 20 ASN HB2 H 1.771 . 1 98 . 20 ASN HB3 H 2.908 . 1 99 . 20 ASN HD21 H 5.692 . 2 100 . 20 ASN HD22 H 6.678 . 2 101 . 21 ALA H H 8.262 . 1 102 . 21 ALA HA H 4.159 . 1 103 . 21 ALA HB H 1.170 . 1 104 . 22 ARG H H 8.137 . 1 105 . 22 ARG HA H 4.139 . 1 106 . 22 ARG HB2 H 1.790 . 1 107 . 22 ARG HB3 H 1.590 . 1 108 . 22 ARG HG2 H 1.398 . 1 109 . 22 ARG HG3 H 1.398 . 1 110 . 22 ARG HD2 H 3.003 . 2 111 . 22 ARG HD3 H 1.468 . 2 112 . 22 ARG HE H 7.103 . 1 113 . 23 SER H H 7.869 . 1 114 . 23 SER HA H 4.841 . 1 115 . 23 SER HB2 H 3.946 . 2 116 . 23 SER HB3 H 3.700 . 2 117 . 24 PRO HA H 4.331 . 1 118 . 24 PRO HB2 H 2.331 . 2 119 . 24 PRO HB3 H 2.035 . 2 120 . 24 PRO HG2 H 1.892 . 1 121 . 24 PRO HG3 H 1.892 . 1 122 . 24 PRO HD2 H 3.780 . 1 123 . 24 PRO HD3 H 3.780 . 1 124 . 25 SER H H 7.974 . 1 125 . 25 SER HA H 4.347 . 1 126 . 25 SER HB2 H 3.810 . 2 127 . 25 SER HB3 H 3.765 . 2 128 . 26 SER H H 8.082 . 1 129 . 26 SER HA H 4.136 . 1 130 . 26 SER HB2 H 3.838 . 1 131 . 26 SER HB3 H 3.838 . 1 132 . 27 VAL H H 7.590 . 1 133 . 27 VAL HA H 4.082 . 1 134 . 27 VAL HB H 2.484 . 1 135 . 27 VAL HG1 H 0.877 . 1 136 . 27 VAL HG2 H 1.107 . 1 137 . 28 THR H H 7.450 . 1 138 . 28 THR HA H 4.444 . 1 139 . 28 THR HG2 H 1.200 . 1 140 . 29 GLY H H 7.537 . 1 141 . 29 GLY HA2 H 3.815 . 1 142 . 29 GLY HA3 H 4.358 . 1 143 . 30 ASN H H 8.449 . 1 144 . 30 ASN HA H 4.988 . 1 145 . 30 ASN HB2 H 2.372 . 1 146 . 30 ASN HB3 H 1.894 . 1 147 . 30 ASN HD21 H 7.008 . 2 148 . 30 ASN HD22 H 7.385 . 2 149 . 31 ALA H H 8.182 . 1 150 . 31 ALA HA H 3.651 . 1 151 . 31 ALA HB H 1.256 . 1 152 . 32 LEU H H 8.822 . 1 153 . 32 LEU HA H 3.713 . 1 154 . 32 LEU HB2 H 1.173 . 1 155 . 32 LEU HB3 H 1.173 . 1 156 . 32 LEU HG H 0.646 . 1 157 . 32 LEU HD1 H 0.373 . 1 158 . 32 LEU HD2 H -0.259 . 1 159 . 33 TRP H H 6.134 . 1 160 . 33 TRP HA H 4.163 . 1 161 . 33 TRP HB2 H 4.027 . 1 162 . 33 TRP HB3 H 3.154 . 1 163 . 33 TRP HD1 H 7.935 . 1 164 . 33 TRP HE1 H 10.527 . 1 165 . 33 TRP HE3 H 7.064 . 1 166 . 33 TRP HZ2 H 7.343 . 1 167 . 33 TRP HZ3 H 6.310 . 1 168 . 33 TRP HH2 H 6.676 . 1 169 . 34 LYS H H 8.027 . 1 170 . 34 LYS HA H 3.717 . 1 171 . 34 LYS HB2 H 1.455 . 1 172 . 34 LYS HB3 H 1.302 . 1 173 . 34 LYS HG2 H 0.300 . 2 174 . 34 LYS HG3 H 0.039 . 2 175 . 34 LYS HD2 H 0.866 . 2 176 . 34 LYS HD3 H 1.003 . 2 177 . 34 LYS HE2 H 1.745 . 2 178 . 34 LYS HE3 H 1.981 . 2 179 . 35 ALA H H 7.809 . 1 180 . 35 ALA HA H 3.979 . 1 181 . 35 ALA HB H 1.348 . 1 182 . 36 MET H H 8.112 . 1 183 . 36 MET HA H 3.002 . 1 184 . 36 MET HB2 H 1.652 . 1 185 . 36 MET HB3 H 1.546 . 1 186 . 36 MET HG2 H 1.449 . 1 187 . 36 MET HG3 H 1.411 . 1 188 . 37 GLU H H 8.424 . 1 189 . 37 GLU HA H 3.936 . 1 190 . 37 GLU HB2 H 2.198 . 1 191 . 37 GLU HB3 H 2.095 . 1 192 . 37 GLU HG2 H 2.587 . 1 193 . 37 GLU HG3 H 2.587 . 1 194 . 38 LYS H H 7.592 . 1 195 . 38 LYS HA H 4.073 . 1 196 . 38 LYS HB2 H 1.803 . 1 197 . 38 LYS HB3 H 1.803 . 1 198 . 38 LYS HG2 H 1.547 . 2 199 . 38 LYS HG3 H 1.434 . 2 200 . 39 SER H H 7.766 . 1 201 . 39 SER HA H 4.287 . 1 202 . 39 SER HB2 H 3.883 . 1 203 . 39 SER HB3 H 3.883 . 1 204 . 40 SER H H 7.875 . 1 205 . 40 SER HA H 4.268 . 1 206 . 40 SER HB2 H 3.830 . 2 207 . 40 SER HB3 H 3.800 . 2 208 . 41 LEU H H 7.956 . 1 209 . 41 LEU HA H 4.166 . 1 210 . 41 LEU HB2 H 1.450 . 1 211 . 41 LEU HB3 H 1.450 . 1 212 . 41 LEU HD1 H 0.814 . 1 213 . 41 LEU HD2 H 0.895 . 1 214 . 42 THR H H 7.837 . 1 215 . 42 THR HA H 4.470 . 1 216 . 42 THR HG2 H 1.081 . 1 217 . 43 GLN H H 8.666 . 1 218 . 43 GLN HA H 4.254 . 1 219 . 43 GLN HB2 H 1.444 . 1 220 . 43 GLN HB3 H 1.444 . 1 221 . 43 GLN HG2 H 2.007 . 1 222 . 43 GLN HG3 H 1.914 . 1 223 . 43 GLN HE21 H 6.582 . 2 224 . 43 GLN HE22 H 7.305 . 2 225 . 44 HIS H H 7.674 . 1 226 . 44 HIS HA H 4.495 . 1 227 . 44 HIS HB2 H 2.988 . 1 228 . 44 HIS HB3 H 2.676 . 1 229 . 44 HIS HD1 H 7.115 . 1 230 . 44 HIS HD2 H 6.433 . 1 231 . 45 SER H H 8.494 . 1 232 . 45 SER HA H 4.504 . 1 233 . 45 SER HB2 H 4.120 . 2 234 . 45 SER HB3 H 3.892 . 2 235 . 46 TRP H H 9.259 . 1 236 . 46 TRP HA H 4.262 . 1 237 . 46 TRP HB2 H 3.175 . 1 238 . 46 TRP HB3 H 3.112 . 1 239 . 46 TRP HD1 H 7.654 . 1 240 . 46 TRP HE1 H 10.085 . 1 241 . 46 TRP HE3 H 7.349 . 1 242 . 46 TRP HZ2 H 7.156 . 1 243 . 46 TRP HZ3 H 7.029 . 1 244 . 46 TRP HH2 H 6.901 . 1 245 . 47 GLN H H 7.719 . 1 246 . 47 GLN HA H 3.078 . 1 247 . 47 GLN HB2 H 1.212 . 1 248 . 47 GLN HB3 H 0.988 . 1 249 . 47 GLN HG2 H 0.247 . 1 250 . 47 GLN HG3 H 1.499 . 1 251 . 47 GLN HE21 H 6.244 . 2 252 . 47 GLN HE22 H 6.945 . 2 253 . 48 SER H H 7.605 . 1 254 . 48 SER HA H 3.968 . 1 255 . 48 SER HB2 H 3.868 . 2 256 . 48 SER HB3 H 3.968 . 2 257 . 49 LEU H H 8.125 . 1 258 . 49 LEU HA H 3.748 . 1 259 . 49 LEU HB2 H 2.238 . 1 260 . 49 LEU HB3 H 1.793 . 1 261 . 49 LEU HG H 1.622 . 1 262 . 50 LYS H H 7.636 . 1 263 . 50 LYS HB2 H 1.548 . 1 264 . 50 LYS HB3 H 1.548 . 1 265 . 50 LYS HG2 H 1.362 . 1 266 . 50 LYS HG3 H 0.925 . 1 267 . 50 LYS HD2 H 0.389 . 1 268 . 50 LYS HD3 H 0.389 . 1 269 . 51 ASP H H 7.491 . 1 270 . 51 ASP HA H 4.007 . 1 271 . 51 ASP HB2 H 2.398 . 1 272 . 51 ASP HB3 H 2.273 . 1 273 . 52 ARG H H 7.819 . 1 274 . 52 ARG HA H 3.512 . 1 275 . 52 ARG HB2 H 0.883 . 1 276 . 52 ARG HB3 H 0.883 . 1 277 . 52 ARG HG2 H 0.777 . 1 278 . 52 ARG HG3 H 0.777 . 1 279 . 52 ARG HD2 H 2.244 . 1 280 . 52 ARG HD3 H 2.244 . 1 281 . 52 ARG HE H 9.453 . 1 282 . 53 TYR H H 8.013 . 1 283 . 53 TYR HA H 3.945 . 1 284 . 53 TYR HB2 H 2.731 . 1 285 . 53 TYR HB3 H 2.913 . 1 286 . 53 TYR HD1 H 6.947 . 1 287 . 53 TYR HD2 H 6.947 . 1 288 . 53 TYR HE1 H 6.724 . 1 289 . 53 TYR HE2 H 6.724 . 1 290 . 54 LEU H H 8.659 . 1 291 . 54 LEU HA H 3.540 . 1 292 . 54 LEU HB2 H 1.663 . 1 293 . 54 LEU HB3 H 1.663 . 1 294 . 54 LEU HG H 1.914 . 1 295 . 55 LYS H H 8.376 . 1 296 . 55 LYS HA H 4.086 . 1 297 . 55 LYS HB2 H 1.617 . 1 298 . 55 LYS HB3 H 1.380 . 1 299 . 55 LYS HG2 H 1.243 . 1 300 . 55 LYS HG3 H 1.243 . 1 301 . 55 LYS HD2 H 1.060 . 1 302 . 55 LYS HD3 H 1.060 . 1 303 . 56 HIS H H 7.298 . 1 304 . 56 HIS HA H 3.079 . 1 305 . 56 HIS HB2 H 2.968 . 1 306 . 56 HIS HB3 H 2.968 . 1 307 . 57 LEU H H 7.816 . 1 308 . 57 LEU HA H 4.213 . 1 309 . 57 LEU HB2 H 1.787 . 1 310 . 57 LEU HB3 H 1.787 . 1 311 . 57 LEU HG H 1.455 . 1 312 . 57 LEU HD1 H 0.693 . 1 313 . 57 LEU HD2 H 0.937 . 1 314 . 58 ARG H H 7.874 . 1 315 . 58 ARG HA H 3.657 . 1 316 . 58 ARG HB2 H 1.337 . 1 317 . 58 ARG HB3 H 1.283 . 1 318 . 58 ARG HG2 H 1.089 . 1 319 . 58 ARG HG3 H 1.089 . 1 320 . 58 ARG HD2 H 2.940 . 1 321 . 58 ARG HD3 H 2.940 . 1 322 . 58 ARG HE H 7.193 . 1 323 . 59 GLY H H 7.952 . 1 324 . 59 GLY HA2 H 3.589 . 1 325 . 59 GLY HA3 H 3.589 . 1 stop_ save_