data_4145 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignment of 1H and 15N Resonances of Murine Tec SH3 Domain ; _BMRB_accession_number 4145 _BMRB_flat_file_name bmr4145.str _Entry_type original _Submission_date 1998-05-27 _Accession_date 1998-05-27 _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 Pursglove Sharon E. . 2 Mulhern Terrence D. . 3 Booker Grant W. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 401 "15N chemical shifts" 76 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-02-03 original author . stop_ _Original_release_date 1999-02-03 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Pursglove, S. E., Mulhern, T. D., Hinds, M. G., Norton, R. S., and Booker, G. W., "Assignment of 1H and 15N Resonances of Murine Tec SH3 Domain," J. Biomol. NMR 12, 461-462 (1998). ; _Citation_title 'Assignment of 1H and 15N Resonances of Murine Tec SH3 Domain' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99052120 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pursglove Sharon E. . 2 Mulhern Terrence D. . 3 Hinds Mark G. . 4 Norton Raymond S. . 5 Booker Grant W. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 12 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 461 _Page_last 462 _Year 1998 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full ; Bartel, Ch., Xia, T.H., Billeter, P., Guntert, P. and Wuthrich K. J. Biomol. NMR 5, 1-10 (1995). ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_citation_two _Saveframe_category citation _Citation_full ; Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995). ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_Tec_SH3 _Saveframe_category molecular_system _Mol_system_name 'Tec Src Homology 3 (SH3) domain' _Abbreviation_common 'Tec SH3' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Tec_SH3 $Tec_SH3 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Tec_SH3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Tec src homology 3 (SH3) domain' _Abbreviation_common 'Tec SH3' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 67 _Mol_residue_sequence ; GSEIVVAMYDFQATEAHDLR LERGQEYIILEKNDLHWWRA RDKYGSEGYIPSNYVTGKKS NNLDQYD ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 GLU 4 ILE 5 VAL 6 VAL 7 ALA 8 MET 9 TYR 10 ASP 11 PHE 12 GLN 13 ALA 14 THR 15 GLU 16 ALA 17 HIS 18 ASP 19 LEU 20 ARG 21 LEU 22 GLU 23 ARG 24 GLY 25 GLN 26 GLU 27 TYR 28 ILE 29 ILE 30 LEU 31 GLU 32 LYS 33 ASN 34 ASP 35 LEU 36 HIS 37 TRP 38 TRP 39 ARG 40 ALA 41 ARG 42 ASP 43 LYS 44 TYR 45 GLY 46 SER 47 GLU 48 GLY 49 TYR 50 ILE 51 PRO 52 SER 53 ASN 54 TYR 55 VAL 56 THR 57 GLY 58 LYS 59 LYS 60 SER 61 ASN 62 ASN 63 LEU 64 ASP 65 GLN 66 TYR 67 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-14 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 1GL5 "Nmr Structure Of The Sh3 Domain From The Tec Protein Tyrosine Kinase" 100.00 67 100.00 100.00 2.69e-41 DBJ BAE23957 "unnamed protein product [Mus musculus]" 97.01 630 98.46 100.00 2.07e-36 DBJ BAE32599 "unnamed protein product [Mus musculus]" 97.01 630 98.46 100.00 2.07e-36 DBJ BAE40357 "unnamed protein product [Mus musculus]" 62.69 608 100.00 100.00 5.23e-20 DBJ BAE41897 "unnamed protein product [Mus musculus]" 62.69 608 100.00 100.00 5.83e-20 EMBL CAA39196 "protein-tyrosine kinase [Mus musculus]" 62.69 527 100.00 100.00 4.43e-20 GB AAA13515 "protein tyrosine kinase [Mus sp.]" 97.01 630 98.46 100.00 2.16e-36 GB AAD43402 "protein tyrosine kinase TecIV [Mus musculus]" 97.01 630 98.46 100.00 2.07e-36 GB AAD43405 "protein tyrosine kinase TecIIB [Mus musculus]" 97.01 624 98.46 100.00 1.79e-36 GB AAD43406 "protein tyrosine kinase TecIII [Mus musculus]" 62.69 608 100.00 100.00 5.83e-20 GB AAD43407 "protein tyrosine kinase TecIIA [Mus musculus]" 62.69 602 100.00 100.00 4.22e-20 REF NP_001106931 "tyrosine-protein kinase Tec isoform a [Mus musculus]" 97.01 630 98.46 100.00 2.07e-36 REF NP_001106932 "tyrosine-protein kinase Tec isoform b [Mus musculus]" 62.69 608 100.00 100.00 5.83e-20 REF NP_001106935 "tyrosine-protein kinase Tec isoform a [Mus musculus]" 97.01 630 98.46 100.00 2.07e-36 REF NP_038717 "tyrosine-protein kinase Tec isoform c [Mus musculus]" 62.69 527 100.00 100.00 4.66e-20 REF NP_445884 "tyrosine-protein kinase Tec [Rattus norvegicus]" 97.01 629 96.92 98.46 1.20e-35 SP P24604 "RecName: Full=Tyrosine-protein kinase Tec" 97.01 630 98.46 100.00 2.16e-36 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Tec_SH3 mouse 10090 Eukaryota Metazoa Mus musculus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_type _Vector_name $Tec_SH3 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) pGex-4T-2 plasmid . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Tec_SH3 . mM 1.25 2 [U-15N] stop_ save_ ############################ # Computer software used # ############################ save_software_one _Saveframe_category software _Name XEASY _Version . _Details . _Citation_label $citation_one save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 600 _Details . save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ save_NMR_spectrometer_three _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label $sample_one save_ save_1H-15N_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label $sample_one save_ save_H20_TOCSY,_NOESY,_COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name 'H20 TOCSY, NOESY, COSY' _Sample_label $sample_one save_ save_D20_TOCSY,_NOESY,_COSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name 'D20 TOCSY, NOESY, COSY' _Sample_label $sample_one save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name 'H20 TOCSY, NOESY, COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name 'D20 TOCSY, NOESY, COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.1 n/a temperature 298 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _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 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.0 $citation_two DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 $citation_two 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_assigned_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name Tec_SH3 _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 SER HA H 4.622 0.001 1 2 . 2 SER HB2 H 3.926 0.007 2 3 . 2 SER HB3 H 3.792 0.003 2 4 . 3 GLU H H 8.865 0.000 1 5 . 3 GLU HA H 4.456 0.001 1 6 . 3 GLU HB2 H 1.978 0.000 1 7 . 3 GLU HB3 H 1.978 0.000 1 8 . 3 GLU HG2 H 2.104 0.003 1 9 . 3 GLU HG3 H 2.104 0.003 1 10 . 3 GLU N N 125.52 0.000 1 11 . 4 ILE H H 8.346 0.000 1 12 . 4 ILE HA H 5.052 0.004 1 13 . 4 ILE HB H 1.824 0.011 1 14 . 4 ILE HG12 H 1.608 0.005 2 15 . 4 ILE HG13 H 1.201 0.005 2 16 . 4 ILE HG2 H 0.982 0.001 1 17 . 4 ILE HD1 H 0.890 0.007 1 18 . 4 ILE N N 125.22 0.000 1 19 . 5 VAL H H 9.261 0.000 1 20 . 5 VAL HA H 5.266 0.000 1 21 . 5 VAL HB H 2.293 0.001 1 22 . 5 VAL HG1 H 1.029 0.001 2 23 . 5 VAL HG2 H 0.986 0.001 2 24 . 5 VAL N N 119.35 0.000 1 25 . 6 VAL H H 9.309 0.004 1 26 . 6 VAL HA H 5.270 0.001 1 27 . 6 VAL HB H 1.893 0.008 1 28 . 6 VAL HG1 H 0.979 0.009 2 29 . 6 VAL HG2 H 0.935 0.008 2 30 . 6 VAL N N 118.98 0.000 1 31 . 7 ALA H H 8.687 0.002 1 32 . 7 ALA HA H 4.859 0.006 1 33 . 7 ALA HB H 1.840 0.008 1 34 . 7 ALA N N 126.03 0.000 1 35 . 8 MET H H 9.534 0.017 1 36 . 8 MET HA H 4.262 0.001 1 37 . 8 MET HB2 H 1.403 0.001 1 38 . 8 MET HB3 H 1.403 0.001 1 39 . 8 MET HG2 H 2.274 0.004 1 40 . 8 MET HG3 H 2.274 0.004 1 41 . 8 MET HE H 1.842 0.000 1 42 . 8 MET N N 124.63 0.000 1 43 . 9 TYR H H 7.205 0.002 1 44 . 9 TYR HA H 4.851 0.001 1 45 . 9 TYR HB2 H 3.241 0.001 2 46 . 9 TYR HB3 H 2.333 0.002 2 47 . 9 TYR HD1 H 6.770 0.002 1 48 . 9 TYR HD2 H 6.770 0.002 1 49 . 9 TYR HE1 H 6.748 0.002 1 50 . 9 TYR HE2 H 6.748 0.002 1 51 . 9 TYR N N 113.06 0.000 1 52 . 10 ASP H H 8.390 0.000 1 53 . 10 ASP HA H 4.813 0.006 1 54 . 10 ASP HB2 H 2.671 0.006 2 55 . 10 ASP N N 117.69 0.000 1 56 . 11 PHE H H 8.911 0.000 1 57 . 11 PHE HA H 5.140 0.002 1 58 . 11 PHE HB2 H 2.892 0.002 2 59 . 11 PHE HD1 H 7.496 0.005 1 60 . 11 PHE HD2 H 7.496 0.005 1 61 . 11 PHE HE1 H 7.558 0.004 1 62 . 11 PHE HE2 H 7.558 0.004 1 63 . 11 PHE HZ H 7.614 0.003 1 64 . 11 PHE N N 121.36 0.000 1 65 . 12 GLN H H 8.340 0.000 1 66 . 12 GLN HA H 4.298 0.003 1 67 . 12 GLN HB2 H 1.941 0.000 2 68 . 12 GLN HB3 H 1.887 0.000 2 69 . 12 GLN HG2 H 2.334 0.006 1 70 . 12 GLN HG3 H 2.334 0.006 1 71 . 12 GLN HE21 H 7.623 0.000 2 72 . 12 GLN HE22 H 6.884 0.000 2 73 . 12 GLN N N 127.22 0.000 1 74 . 12 GLN NE2 N 112.40 0.000 1 75 . 13 ALA H H 7.516 0.000 1 76 . 13 ALA HA H 4.016 0.002 1 77 . 13 ALA HB H 1.293 0.002 1 78 . 13 ALA N N 125.97 0.000 1 79 . 14 THR H H 9.087 0.001 1 80 . 14 THR HA H 4.377 0.002 1 81 . 14 THR HB H 4.242 0.003 1 82 . 14 THR HG2 H 1.224 0.006 1 83 . 14 THR N N 116.10 0.000 1 84 . 15 GLU H H 8.312 0.015 1 85 . 15 GLU HA H 4.507 0.005 1 86 . 15 GLU HB2 H 1.776 0.000 2 87 . 15 GLU HB3 H 1.695 0.000 2 88 . 15 GLU HG2 H 1.930 0.000 2 89 . 15 GLU HG3 H 1.870 0.000 2 90 . 15 GLU N N 122.63 0.000 1 91 . 16 ALA H H 8.771 0.001 1 92 . 16 ALA HA H 4.141 0.003 1 93 . 16 ALA HB H 1.431 0.002 1 94 . 16 ALA N N 123.85 0.000 1 95 . 17 HIS H H 8.100 0.002 1 96 . 17 HIS HA H 5.001 0.002 1 97 . 17 HIS HB2 H 3.619 0.001 2 98 . 17 HIS HB3 H 3.401 0.004 2 99 . 17 HIS HD2 H 7.124 0.000 2 100 . 17 HIS N N 110.87 0.000 1 101 . 18 ASP H H 7.808 0.000 1 102 . 18 ASP HA H 5.460 0.009 1 103 . 18 ASP HB2 H 2.947 0.000 2 104 . 18 ASP HB3 H 2.901 0.000 2 105 . 18 ASP N N 122.46 0.000 1 106 . 19 LEU H H 8.910 0.007 1 107 . 19 LEU HA H 4.661 0.002 1 108 . 19 LEU HB2 H 1.856 0.000 2 109 . 19 LEU HB3 H 1.716 0.000 2 110 . 19 LEU HG H 1.707 0.001 1 111 . 19 LEU N N 124.97 0.000 1 112 . 20 ARG H H 8.036 0.002 1 113 . 20 ARG HA H 4.448 0.002 1 114 . 20 ARG HB2 H 2.082 0.004 2 115 . 20 ARG HB3 H 1.942 0.004 2 116 . 20 ARG HG2 H 2.036 0.000 2 117 . 20 ARG HG3 H 1.585 0.000 2 118 . 20 ARG HD2 H 3.358 0.001 1 119 . 20 ARG HD3 H 3.358 0.001 1 120 . 20 ARG HE H 7.506 0.002 1 121 . 20 ARG N N 123.05 0.000 1 122 . 20 ARG NE N 115.13 0.000 1 123 . 21 LEU H H 8.893 0.017 1 124 . 21 LEU HA H 5.206 0.005 1 125 . 21 LEU HB2 H 2.273 0.006 2 126 . 21 LEU HB3 H 1.289 0.007 2 127 . 21 LEU HG H 1.842 0.000 1 128 . 21 LEU HD1 H 0.778 0.002 2 129 . 21 LEU HD2 H 0.056 0.004 2 130 . 21 LEU N N 119.61 0.000 1 131 . 22 GLU H H 8.953 0.002 1 132 . 22 GLU HA H 4.997 0.004 1 133 . 22 GLU HB2 H 2.144 0.000 2 134 . 22 GLU HB3 H 2.011 0.008 2 135 . 22 GLU HG2 H 2.330 0.009 1 136 . 22 GLU HG3 H 2.330 0.009 1 137 . 22 GLU N N 124.13 0.000 1 138 . 23 ARG H H 9.108 0.003 1 139 . 23 ARG HA H 3.549 0.002 1 140 . 23 ARG HB2 H 1.819 0.001 2 141 . 23 ARG HB3 H 1.619 0.005 2 142 . 23 ARG HG2 H 1.538 0.000 2 143 . 23 ARG HG3 H 1.477 0.003 2 144 . 23 ARG HD2 H 3.319 0.007 2 145 . 23 ARG HD3 H 3.272 0.004 2 146 . 23 ARG HE H 7.236 0.001 1 147 . 23 ARG N N 124.66 0.000 1 148 . 24 GLY H H 9.300 0.005 1 149 . 24 GLY HA2 H 3.704 0.001 2 150 . 24 GLY HA3 H 4.474 0.001 2 151 . 24 GLY N N 113.93 0.000 1 152 . 25 GLN H H 8.378 0.007 1 153 . 25 GLN HA H 4.546 0.003 1 154 . 25 GLN HB2 H 2.864 0.002 2 155 . 25 GLN HB3 H 2.181 0.002 2 156 . 25 GLN HG2 H 2.527 0.002 2 157 . 25 GLN HG3 H 2.334 0.001 2 158 . 25 GLN HE21 H 7.123 0.000 2 159 . 25 GLN HE22 H 7.897 0.000 2 160 . 25 GLN N N 119.27 0.000 1 161 . 25 GLN NE2 N 116.99 0.000 1 162 . 26 GLU H H 8.257 0.001 1 163 . 26 GLU HA H 5.481 0.004 1 164 . 26 GLU HB2 H 1.871 0.002 1 165 . 26 GLU HB3 H 1.871 0.002 1 166 . 26 GLU HG2 H 2.125 0.004 2 167 . 26 GLU N N 117.70 0.000 1 168 . 27 TYR H H 9.198 0.004 1 169 . 27 TYR HA H 4.730 0.004 1 170 . 27 TYR HB2 H 2.814 0.003 2 171 . 27 TYR HB3 H 2.483 0.004 2 172 . 27 TYR HD1 H 6.914 0.002 1 173 . 27 TYR HD2 H 6.914 0.002 1 174 . 27 TYR HE1 H 7.120 0.007 1 175 . 27 TYR HE2 H 7.120 0.007 1 176 . 27 TYR N N 119.86 0.000 1 177 . 28 ILE H H 8.803 0.000 1 178 . 28 ILE HA H 4.803 0.001 1 179 . 28 ILE HB H 1.820 0.004 1 180 . 28 ILE HG12 H 1.634 0.000 2 181 . 28 ILE HG13 H 1.146 0.000 2 182 . 28 ILE HG2 H 0.913 0.002 1 183 . 28 ILE HD1 H 0.886 0.000 1 184 . 28 ILE N N 122.03 0.000 1 185 . 29 ILE H H 9.128 0.001 1 186 . 29 ILE HA H 4.390 0.002 1 187 . 29 ILE HB H 2.173 0.005 1 188 . 29 ILE HG12 H 1.847 0.000 2 189 . 29 ILE HG13 H 1.375 0.000 2 190 . 29 ILE HG2 H 0.655 0.000 1 191 . 29 ILE HD1 H 0.637 0.000 1 192 . 29 ILE N N 125.44 0.000 1 193 . 30 LEU H H 9.407 0.000 1 194 . 30 LEU HA H 4.504 0.004 1 195 . 30 LEU HB2 H 1.399 0.003 1 196 . 30 LEU HB3 H 1.399 0.003 1 197 . 30 LEU HG H 1.654 0.003 1 198 . 30 LEU HD1 H 0.870 0.000 2 199 . 30 LEU HD2 H 0.837 0.000 2 200 . 30 LEU N N 128.68 0.000 1 201 . 31 GLU H H 7.744 0.001 1 202 . 31 GLU HA H 4.456 0.006 1 203 . 31 GLU HB2 H 2.190 0.008 2 204 . 31 GLU HB3 H 2.085 0.002 2 205 . 31 GLU HG2 H 2.319 0.013 1 206 . 31 GLU HG3 H 2.319 0.013 1 207 . 31 GLU N N 116.70 0.000 1 208 . 32 LYS H H 8.674 0.000 1 209 . 32 LYS HA H 4.584 0.000 1 210 . 32 LYS HB2 H 1.125 0.000 2 211 . 32 LYS HB3 H 1.066 0.000 2 212 . 32 LYS HG2 H 0.561 0.000 2 213 . 32 LYS HG3 H -0.264 0.000 2 214 . 32 LYS HD2 H 1.512 0.000 2 215 . 32 LYS HD3 H 0.882 0.000 2 216 . 32 LYS HE2 H 2.191 0.000 1 217 . 32 LYS HE3 H 2.191 0.000 1 218 . 32 LYS N N 124.17 0.000 1 219 . 33 ASN H H 8.739 0.000 1 220 . 33 ASN HA H 4.789 0.005 1 221 . 33 ASN HB2 H 3.071 0.002 2 222 . 33 ASN HB3 H 2.956 0.005 2 223 . 33 ASN HD21 H 7.805 0.000 2 224 . 33 ASN HD22 H 7.053 0.000 2 225 . 33 ASN N N 120.70 0.000 1 226 . 33 ASN ND2 N 113.44 0.000 1 227 . 34 ASP H H 8.330 0.000 1 228 . 34 ASP HA H 4.883 0.008 1 229 . 34 ASP HB2 H 3.554 0.001 2 230 . 34 ASP HB3 H 2.964 0.002 2 231 . 34 ASP N N 119.35 0.000 1 232 . 35 LEU H H 8.285 0.001 1 233 . 35 LEU HA H 4.347 0.003 1 234 . 35 LEU HB2 H 1.648 0.001 2 235 . 35 LEU HB3 H 1.429 0.004 2 236 . 35 LEU HG H 1.280 0.005 1 237 . 35 LEU HD1 H 0.994 0.002 2 238 . 35 LEU HD2 H 0.963 0.001 2 239 . 35 LEU N N 120.24 0.000 1 240 . 36 HIS H H 8.836 0.001 1 241 . 36 HIS HA H 4.421 0.003 1 242 . 36 HIS HB2 H 3.044 0.001 2 243 . 36 HIS HB3 H 2.824 0.001 2 244 . 36 HIS HD2 H 6.732 0.000 2 245 . 36 HIS N N 115.76 0.000 1 246 . 37 TRP H H 8.570 0.006 1 247 . 37 TRP HA H 5.341 0.005 1 248 . 37 TRP HB2 H 3.071 0.005 1 249 . 37 TRP HB3 H 3.071 0.005 1 250 . 37 TRP HD1 H 7.345 0.001 1 251 . 37 TRP HE1 H 10.082 0.017 1 252 . 37 TRP HE3 H 6.681 0.003 1 253 . 37 TRP HZ2 H 7.520 0.006 1 254 . 37 TRP HZ3 H 7.296 0.001 1 255 . 37 TRP HH2 H 7.261 0.005 1 256 . 37 TRP N N 121.99 0.000 1 257 . 37 TRP NE1 N 128.26 0.000 1 258 . 38 TRP H H 9.133 0.004 1 259 . 38 TRP HA H 5.760 0.001 1 260 . 38 TRP HB2 H 3.408 0.003 2 261 . 38 TRP HB3 H 3.017 0.009 2 262 . 38 TRP HD1 H 7.547 0.006 1 263 . 38 TRP HE1 H 9.748 0.000 1 264 . 38 TRP HE3 H 6.934 0.003 1 265 . 38 TRP HZ2 H 7.637 0.006 1 266 . 38 TRP HZ3 H 7.255 0.001 1 267 . 38 TRP HH2 H 7.288 0.002 1 268 . 38 TRP N N 125.59 0.000 1 269 . 38 TRP NE1 N 128.64 0.000 1 270 . 39 ARG H H 9.022 0.004 1 271 . 39 ARG HA H 4.687 0.004 1 272 . 39 ARG HB2 H 1.831 0.000 2 273 . 39 ARG HB3 H 1.593 0.003 2 274 . 39 ARG HG2 H 1.325 0.001 2 275 . 39 ARG HG3 H 0.942 0.005 2 276 . 39 ARG HD2 H 3.095 0.000 2 277 . 39 ARG HD3 H 3.005 0.001 2 278 . 39 ARG HE H 7.473 0.000 1 279 . 39 ARG N N 123.42 0.000 1 280 . 39 ARG NE N 112.79 0.000 1 281 . 40 ALA H H 9.548 0.000 1 282 . 40 ALA HA H 5.753 0.003 1 283 . 40 ALA HB H 1.434 0.008 1 284 . 40 ALA N N 130.96 0.000 1 285 . 41 ARG H H 9.134 0.018 1 286 . 41 ARG HA H 5.800 0.003 1 287 . 41 ARG HB2 H 2.311 0.005 2 288 . 41 ARG HB3 H 1.778 0.006 2 289 . 41 ARG HG2 H 1.873 0.002 2 290 . 41 ARG HG3 H 1.675 0.002 2 291 . 41 ARG HD2 H 3.412 0.005 2 292 . 41 ARG HD3 H 3.255 0.000 2 293 . 41 ARG HE H 7.624 0.000 1 294 . 41 ARG N N 118.67 0.000 1 295 . 41 ARG NE N 114.74 0.000 1 296 . 42 ASP H H 9.067 0.001 1 297 . 42 ASP HA H 5.103 0.002 1 298 . 42 ASP HB2 H 3.095 0.004 2 299 . 42 ASP N N 125.82 0.000 1 300 . 43 LYS H H 9.013 0.016 1 301 . 43 LYS HA H 4.139 0.004 1 302 . 43 LYS HB2 H 1.794 0.004 2 303 . 43 LYS HB3 H 1.686 0.001 2 304 . 43 LYS HG2 H 0.946 0.005 2 305 . 43 LYS HG3 H 0.168 0.005 2 306 . 43 LYS HD2 H 1.565 0.000 2 307 . 43 LYS HD3 H 1.504 0.000 2 308 . 43 LYS HE2 H 2.816 0.001 1 309 . 43 LYS HE3 H 2.816 0.001 1 310 . 43 LYS N N 117.16 0.000 1 311 . 44 TYR H H 8.136 0.009 1 312 . 44 TYR HA H 4.713 0.006 1 313 . 44 TYR HB2 H 3.486 0.007 2 314 . 44 TYR HB3 H 3.251 0.009 2 315 . 44 TYR HD1 H 6.972 0.003 1 316 . 44 TYR HD2 H 6.972 0.003 1 317 . 44 TYR HE1 H 7.344 0.002 1 318 . 44 TYR HE2 H 7.344 0.002 1 319 . 44 TYR N N 120.97 0.000 1 320 . 45 GLY H H 8.276 0.001 1 321 . 45 GLY HA2 H 3.617 0.002 2 322 . 45 GLY HA3 H 4.555 0.002 2 323 . 45 GLY N N 108.18 0.000 1 324 . 46 SER H H 8.979 0.001 1 325 . 46 SER HA H 4.672 0.003 1 326 . 46 SER HB2 H 3.996 0.006 2 327 . 46 SER N N 121.32 0.000 1 328 . 47 GLU H H 8.587 0.000 1 329 . 47 GLU HA H 5.993 0.003 1 330 . 47 GLU HB2 H 1.964 0.004 2 331 . 47 GLU HB3 H 1.929 0.002 2 332 . 47 GLU HG2 H 2.487 0.004 2 333 . 47 GLU HG3 H 2.186 0.001 2 334 . 47 GLU N N 119.90 0.000 1 335 . 48 GLY H H 8.717 0.002 1 336 . 48 GLY HA2 H 4.047 0.001 2 337 . 48 GLY HA3 H 4.139 0.001 2 338 . 48 GLY N N 107.62 0.000 1 339 . 49 TYR H H 9.315 0.010 1 340 . 49 TYR HA H 5.582 0.007 1 341 . 49 TYR HB2 H 3.140 0.000 2 342 . 49 TYR HB3 H 3.098 0.000 2 343 . 49 TYR HD1 H 6.921 0.002 1 344 . 49 TYR HD2 H 6.921 0.002 1 345 . 49 TYR HE1 H 7.122 0.005 1 346 . 49 TYR HE2 H 7.122 0.005 1 347 . 49 TYR N N 119.79 0.000 1 348 . 50 ILE H H 9.558 0.003 1 349 . 50 ILE HA H 5.067 0.000 1 350 . 50 ILE HB H 1.850 0.005 1 351 . 50 ILE HG12 H 1.531 0.003 2 352 . 50 ILE HG13 H 1.034 0.007 2 353 . 50 ILE HG2 H 1.467 0.001 1 354 . 50 ILE HD1 H 0.651 0.002 1 355 . 50 ILE N N 113.15 0.000 1 356 . 51 PRO HA H 3.759 0.004 1 357 . 51 PRO HB2 H 1.245 0.000 2 358 . 51 PRO HB3 H 0.887 0.000 2 359 . 51 PRO HG2 H 0.677 0.000 2 360 . 51 PRO HG3 H 0.307 0.000 2 361 . 51 PRO HD2 H 2.633 0.000 2 362 . 51 PRO HD3 H 2.529 0.000 2 363 . 52 SER H H 8.069 0.001 1 364 . 52 SER HA H 2.739 0.000 1 365 . 52 SER HB2 H 1.879 0.000 2 366 . 52 SER HB3 H 1.511 0.000 2 367 . 52 SER N N 122.27 0.000 1 368 . 53 ASN H H 8.261 0.002 1 369 . 53 ASN HA H 4.668 0.004 1 370 . 53 ASN HB2 H 3.007 0.006 2 371 . 53 ASN HB3 H 2.763 0.003 2 372 . 53 ASN HD21 H 6.813 0.007 2 373 . 53 ASN HD22 H 7.539 0.008 2 374 . 53 ASN N N 114.83 0.000 1 375 . 53 ASN ND2 N 112.20 0.000 1 376 . 54 TYR H H 7.839 0.020 1 377 . 54 TYR HA H 4.803 0.004 1 378 . 54 TYR HB2 H 3.346 0.006 2 379 . 54 TYR HB3 H 3.063 0.002 2 380 . 54 TYR HD1 H 7.015 0.001 1 381 . 54 TYR HD2 H 7.015 0.001 1 382 . 54 TYR HE1 H 6.993 0.004 1 383 . 54 TYR HE2 H 6.993 0.004 1 384 . 54 TYR N N 119.33 0.000 1 385 . 55 VAL H H 7.258 0.006 1 386 . 55 VAL HA H 5.522 0.002 1 387 . 55 VAL HB H 2.086 0.005 1 388 . 55 VAL HG1 H 0.929 0.005 2 389 . 55 VAL HG2 H 0.740 0.004 2 390 . 55 VAL N N 109.56 0.000 1 391 . 56 THR H H 8.713 0.003 1 392 . 56 THR HA H 4.896 0.008 1 393 . 56 THR HB H 4.232 0.005 1 394 . 56 THR HG2 H 1.256 0.004 1 395 . 56 THR N N 114.08 0.000 1 396 . 57 GLY H H 8.674 0.004 1 397 . 57 GLY HA2 H 3.994 0.000 2 398 . 57 GLY HA3 H 4.387 0.002 2 399 . 57 GLY N N 112.27 0.000 1 400 . 58 LYS H H 8.395 0.000 1 401 . 58 LYS HA H 4.349 0.003 1 402 . 58 LYS HB2 H 1.857 0.007 1 403 . 58 LYS HB3 H 1.857 0.007 1 404 . 58 LYS HG2 H 1.449 0.001 1 405 . 58 LYS HG3 H 1.449 0.001 1 406 . 58 LYS HD2 H 1.607 0.006 1 407 . 58 LYS HD3 H 1.607 0.006 1 408 . 58 LYS HE2 H 2.980 0.008 1 409 . 58 LYS HE3 H 2.980 0.008 1 410 . 58 LYS N N 123.83 0.000 1 411 . 59 LYS H H 8.735 0.006 1 412 . 59 LYS HA H 4.510 0.006 1 413 . 59 LYS HB2 H 1.937 0.000 2 414 . 59 LYS HB3 H 1.835 0.000 2 415 . 59 LYS HG2 H 1.543 0.001 2 416 . 59 LYS HG3 H 1.500 0.002 2 417 . 59 LYS HD2 H 1.775 0.002 1 418 . 59 LYS HD3 H 1.775 0.002 1 419 . 59 LYS HE2 H 3.088 0.000 1 420 . 59 LYS HE3 H 3.088 0.000 1 421 . 59 LYS N N 126.02 0.000 1 422 . 60 SER H H 8.525 0.002 1 423 . 60 SER HA H 4.546 0.001 1 424 . 60 SER HB2 H 3.982 0.002 2 425 . 60 SER HB3 H 3.930 0.001 2 426 . 60 SER N N 117.47 0.000 1 427 . 61 ASN H H 8.222 0.002 1 428 . 61 ASN HA H 4.592 0.011 1 429 . 61 ASN HB2 H 2.919 0.000 2 430 . 61 ASN HB3 H 2.799 0.000 2 431 . 61 ASN HD21 H 7.680 0.000 2 432 . 61 ASN HD22 H 6.988 0.000 2 433 . 61 ASN N N 125.91 0.000 1 434 . 61 ASN ND2 N 112.96 0.000 1 435 . 62 ASN H H 8.529 0.003 1 436 . 62 ASN HA H 4.765 0.012 1 437 . 62 ASN HB2 H 2.913 0.005 2 438 . 62 ASN HB3 H 2.814 0.001 2 439 . 62 ASN HD21 H 7.682 0.013 2 440 . 62 ASN HD22 H 6.989 0.011 2 441 . 62 ASN N N 118.88 0.000 1 442 . 62 ASN ND2 N 112.96 0.000 1 443 . 63 LEU H H 8.319 0.015 1 444 . 63 LEU HA H 4.422 0.004 1 445 . 63 LEU HB2 H 1.750 0.002 1 446 . 63 LEU HB3 H 1.750 0.002 1 447 . 63 LEU HG H 1.692 0.008 1 448 . 63 LEU HD1 H 1.025 0.000 2 449 . 63 LEU HD2 H 0.962 0.001 2 450 . 63 LEU N N 121.69 0.000 1 451 . 64 ASP H H 8.326 0.003 1 452 . 64 ASP HA H 4.609 0.004 1 453 . 64 ASP HB2 H 2.717 0.009 1 454 . 64 ASP HB3 H 2.717 0.009 1 455 . 64 ASP N N 120.40 0.000 1 456 . 65 GLN H H 8.022 0.001 1 457 . 65 GLN HA H 4.359 0.005 1 458 . 65 GLN HB2 H 2.065 0.006 2 459 . 65 GLN HB3 H 1.962 0.003 2 460 . 65 GLN HG2 H 2.264 0.004 1 461 . 65 GLN HG3 H 2.264 0.004 1 462 . 65 GLN N N 119.41 0.000 1 463 . 65 GLN NE2 N 112.80 0.000 1 464 . 66 TYR H H 8.305 0.001 1 465 . 66 TYR HA H 4.743 0.004 1 466 . 66 TYR HB2 H 3.277 0.002 2 467 . 66 TYR HB3 H 2.955 0.004 2 468 . 66 TYR HD1 H 7.226 0.000 1 469 . 66 TYR HD2 H 7.226 0.000 1 470 . 66 TYR HE1 H 6.908 0.000 1 471 . 66 TYR HE2 H 6.908 0.000 1 472 . 66 TYR N N 121.67 0.000 1 473 . 67 ASP H H 8.041 0.000 1 474 . 67 ASP HA H 4.485 0.002 1 475 . 67 ASP HB2 H 2.761 0.000 2 476 . 67 ASP HB3 H 2.670 0.000 2 477 . 67 ASP N N 126.80 0.000 1 stop_ save_