data_18348 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for EB1 CH domain ; _BMRB_accession_number 18348 _BMRB_flat_file_name bmr18348.str _Entry_type original _Submission_date 2012-03-26 _Accession_date 2012-03-26 _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 Kanaba Teppei . . 2 Mishima Masaki . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 126 "13C chemical shifts" 367 "15N chemical shifts" 126 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-02-11 update BMRB 'update entry citation' 2012-11-15 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Microtubule-binding sites of the CH domain of EB1 and its autoinhibition revealed by NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23128140 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kanaba Teppei . . 2 Maesaki Ryoko . . 3 Mori Tomoyuki . . 4 Ito Yutaka . . 5 Hakoshima Toshio . . 6 Mishima Masaki . . stop_ _Journal_abbreviation 'Biochim. Biophys. Acta' _Journal_name_full 'Biochimica et biophysica acta' _Journal_volume 1834 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 499 _Page_last 507 _Year 2013 _Details . loop_ _Keyword 'CH domain' EB1 microtubule stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'EB1 CH domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'EB1 CH domain' $EB1_CH_domain stop_ _System_molecular_weight 15000 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_EB1_CH_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common EB1_CH_domain _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 133 _Mol_residue_sequence ; GPGMAVNVYSTSVTSDNLSR HDMLAWINESLQLNLTKIEQ LCSGAAYCQFMDMLFPGSIA LKKVKFQAKLEHEYIQNFKI LQAGFKRMGVDKIIPVDKLV KGKFQDNFEFVQWFKKFFDA NYDGKDYDPVAAR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -2 GLY 2 -1 PRO 3 0 GLY 4 1 MET 5 2 ALA 6 3 VAL 7 4 ASN 8 5 VAL 9 6 TYR 10 7 SER 11 8 THR 12 9 SER 13 10 VAL 14 11 THR 15 12 SER 16 13 ASP 17 14 ASN 18 15 LEU 19 16 SER 20 17 ARG 21 18 HIS 22 19 ASP 23 20 MET 24 21 LEU 25 22 ALA 26 23 TRP 27 24 ILE 28 25 ASN 29 26 GLU 30 27 SER 31 28 LEU 32 29 GLN 33 30 LEU 34 31 ASN 35 32 LEU 36 33 THR 37 34 LYS 38 35 ILE 39 36 GLU 40 37 GLN 41 38 LEU 42 39 CYS 43 40 SER 44 41 GLY 45 42 ALA 46 43 ALA 47 44 TYR 48 45 CYS 49 46 GLN 50 47 PHE 51 48 MET 52 49 ASP 53 50 MET 54 51 LEU 55 52 PHE 56 53 PRO 57 54 GLY 58 55 SER 59 56 ILE 60 57 ALA 61 58 LEU 62 59 LYS 63 60 LYS 64 61 VAL 65 62 LYS 66 63 PHE 67 64 GLN 68 65 ALA 69 66 LYS 70 67 LEU 71 68 GLU 72 69 HIS 73 70 GLU 74 71 TYR 75 72 ILE 76 73 GLN 77 74 ASN 78 75 PHE 79 76 LYS 80 77 ILE 81 78 LEU 82 79 GLN 83 80 ALA 84 81 GLY 85 82 PHE 86 83 LYS 87 84 ARG 88 85 MET 89 86 GLY 90 87 VAL 91 88 ASP 92 89 LYS 93 90 ILE 94 91 ILE 95 92 PRO 96 93 VAL 97 94 ASP 98 95 LYS 99 96 LEU 100 97 VAL 101 98 LYS 102 99 GLY 103 100 LYS 104 101 PHE 105 102 GLN 106 103 ASP 107 104 ASN 108 105 PHE 109 106 GLU 110 107 PHE 111 108 VAL 112 109 GLN 113 110 TRP 114 111 PHE 115 112 LYS 116 113 LYS 117 114 PHE 118 115 PHE 119 116 ASP 120 117 ALA 121 118 ASN 122 119 TYR 123 120 ASP 124 121 GLY 125 122 LYS 126 123 ASP 127 124 TYR 128 125 ASP 129 126 PRO 130 127 VAL 131 128 ALA 132 129 ALA 133 130 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-12 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 1PA7 "Crystal Structure Of Amino-Terminal Microtubule Binding Domain Of Eb1" 97.74 130 100.00 100.00 3.82e-90 PDB 1UEG "Crystal Structure Of Amino-Terminal Microtubule Binding Domain Of Eb1" 97.74 130 100.00 100.00 3.82e-90 PDB 1VKA "Southeast Collaboratory For Structural Genomics: Hypothetical Human Protein Q15691 N-Terminal Fragment" 100.00 153 97.74 97.74 5.39e-90 PDB 2R8U "Structure Of Fragment Of Human End-Binding Protein 1 (Eb1) Containing The N-Terminal Domain At 1.35 A Resolution" 97.74 268 100.00 100.00 1.27e-89 DBJ BAE32461 "unnamed protein product [Mus musculus]" 97.74 268 99.23 100.00 4.00e-89 DBJ BAE89438 "unnamed protein product [Macaca fascicularis]" 97.74 268 100.00 100.00 1.38e-89 DBJ BAG35484 "unnamed protein product [Homo sapiens]" 97.74 268 100.00 100.00 1.27e-89 DBJ BAG73401 "microtubule-associated protein, RP/EB family, member 1 [synthetic construct]" 97.74 268 100.00 100.00 1.27e-89 EMBL CAG31466 "hypothetical protein RCJMB04_6l6 [Gallus gallus]" 97.74 258 96.92 99.23 8.56e-88 EMBL CAH92115 "hypothetical protein [Pongo abelii]" 97.74 268 100.00 100.00 1.48e-89 GB AAA96320 "APC-binding protein EB1 homolog [Mus musculus]" 97.74 268 99.23 100.00 4.00e-89 GB AAC09471 "EB1 [Homo sapiens]" 97.74 268 100.00 100.00 1.27e-89 GB AAH52405 "Mapre1 protein, partial [Mus musculus]" 99.25 271 98.48 99.24 5.88e-90 GB AAH64444 "Mapre1 protein [Mus musculus]" 97.74 268 99.23 100.00 4.00e-89 GB AAH81726 "Microtubule-associated protein, RP/EB family, member 1 [Rattus norvegicus]" 97.74 268 99.23 100.00 6.31e-89 REF NP_001026031 "microtubule-associated protein RP/EB family member 1 [Gallus gallus]" 97.74 258 96.92 99.23 8.56e-88 REF NP_001038078 "microtubule-associated protein RP/EB family member 1 [Sus scrofa]" 97.74 268 100.00 100.00 1.75e-89 REF NP_001068802 "microtubule-associated protein RP/EB family member 1 [Bos taurus]" 97.74 268 99.23 100.00 4.36e-89 REF NP_001126236 "microtubule-associated protein RP/EB family member 1 [Pongo abelii]" 97.74 268 100.00 100.00 1.48e-89 REF NP_001238875 "microtubule-associated protein RP/EB family member 1 [Canis lupus familiaris]" 97.74 268 100.00 100.00 1.39e-89 SP Q15691 "RecName: Full=Microtubule-associated protein RP/EB family member 1; AltName: Full=APC-binding protein EB1; AltName: Full=End-bi" 97.74 268 100.00 100.00 1.27e-89 SP Q3ZBD9 "RecName: Full=Microtubule-associated protein RP/EB family member 1; AltName: Full=APC-binding protein EB1; AltName: Full=End-bi" 97.74 268 99.23 100.00 4.36e-89 SP Q5R7Z5 "RecName: Full=Microtubule-associated protein RP/EB family member 1; AltName: Full=APC-binding protein EB1; AltName: Full=End-bi" 97.74 268 100.00 100.00 1.48e-89 SP Q5ZLC7 "RecName: Full=Microtubule-associated protein RP/EB family member 1" 97.74 258 96.92 99.23 8.56e-88 SP Q61166 "RecName: Full=Microtubule-associated protein RP/EB family member 1; AltName: Full=APC-binding protein EB1; AltName: Full=End-bi" 97.74 268 99.23 100.00 4.00e-89 TPG DAA23186 "TPA: microtubule-associated protein RP/EB family member 1 [Bos taurus]" 97.74 270 99.23 100.00 6.80e-89 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $EB1_CH_domain 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 $EB1_CH_domain 'recombinant technology' . Escherichia coli . pET47b 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 $EB1_CH_domain 1.0 mM '[U-13C; U-15N]' H2O 93 % 'natural abundance' D2O 7 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.4 . M pH 7.0 . pH pressure 1 . atm temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCACB' '3D CBCA(CO)NH' '3D HN(CA)CO' '3D HNCO' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'EB1 CH 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 1 4 MET H H 7.814 0.04 1 2 1 4 MET C C 175.493 0.40 1 3 1 4 MET CA C 54.471 0.40 1 4 1 4 MET CB C 34.225 0.40 1 5 1 4 MET N N 119.946 0.40 1 6 2 5 ALA H H 8.232 0.04 1 7 2 5 ALA C C 176.777 0.40 1 8 2 5 ALA CA C 52.210 0.40 1 9 2 5 ALA CB C 20.441 0.40 1 10 2 5 ALA N N 124.213 0.40 1 11 3 6 VAL H H 9.422 0.04 1 12 3 6 VAL C C 176.051 0.40 1 13 3 6 VAL CA C 62.726 0.40 1 14 3 6 VAL CB C 32.014 0.40 1 15 3 6 VAL N N 124.566 0.40 1 16 4 7 ASN H H 8.383 0.04 1 17 4 7 ASN C C 174.682 0.40 1 18 4 7 ASN CA C 53.914 0.40 1 19 4 7 ASN CB C 41.174 0.40 1 20 4 7 ASN N N 125.237 0.40 1 21 5 8 VAL H H 8.655 0.04 1 22 5 8 VAL C C 174.914 0.40 1 23 5 8 VAL CA C 61.161 0.40 1 24 5 8 VAL CB C 34.709 0.40 1 25 5 8 VAL N N 119.368 0.40 1 26 6 9 TYR H H 8.652 0.04 1 27 6 9 TYR C C 175.967 0.40 1 28 6 9 TYR CA C 57.410 0.40 1 29 6 9 TYR CB C 39.918 0.40 1 30 6 9 TYR N N 126.409 0.40 1 31 8 11 THR H H 8.118 0.04 1 32 8 11 THR C C 174.710 0.40 1 33 8 11 THR CA C 61.599 0.40 1 34 8 11 THR CB C 69.861 0.40 1 35 8 11 THR N N 115.754 0.40 1 36 9 12 SER H H 8.218 0.04 1 37 9 12 SER C C 174.420 0.40 1 38 9 12 SER CA C 58.983 0.40 1 39 9 12 SER CB C 63.579 0.40 1 40 9 12 SER N N 118.906 0.40 1 41 10 13 VAL H H 8.067 0.04 1 42 10 13 VAL C C 176.428 0.40 1 43 10 13 VAL CA C 62.672 0.40 1 44 10 13 VAL CB C 32.301 0.40 1 45 10 13 VAL N N 123.058 0.40 1 46 11 14 THR H H 8.148 0.04 1 47 11 14 THR C C 174.944 0.40 1 48 11 14 THR CA C 61.873 0.40 1 49 11 14 THR CB C 69.830 0.40 1 50 11 14 THR N N 118.326 0.40 1 51 12 15 SER H H 8.134 0.04 1 52 12 15 SER C C 173.964 0.40 1 53 12 15 SER CA C 58.851 0.40 1 54 12 15 SER CB C 63.624 0.40 1 55 12 15 SER N N 118.858 0.40 1 56 13 16 ASP H H 8.190 0.04 1 57 13 16 ASP C C 175.767 0.40 1 58 13 16 ASP CA C 54.256 0.40 1 59 13 16 ASP CB C 40.819 0.40 1 60 13 16 ASP N N 122.956 0.40 1 61 14 17 ASN H H 8.117 0.04 1 62 14 17 ASN C C 175.299 0.40 1 63 14 17 ASN CA C 53.262 0.40 1 64 14 17 ASN CB C 38.985 0.40 1 65 14 17 ASN N N 121.010 0.40 1 66 15 18 LEU H H 8.188 0.04 1 67 15 18 LEU C C 177.982 0.40 1 68 15 18 LEU CA C 54.974 0.40 1 69 15 18 LEU CB C 43.674 0.40 1 70 15 18 LEU N N 123.978 0.40 1 71 16 19 SER H H 9.195 0.04 1 72 16 19 SER C C 175.169 0.40 1 73 16 19 SER CA C 57.639 0.40 1 74 16 19 SER CB C 65.297 0.40 1 75 16 19 SER N N 119.715 0.40 1 76 17 20 ARG H H 9.277 0.04 1 77 17 20 ARG C C 177.055 0.40 1 78 17 20 ARG CA C 60.425 0.40 1 79 17 20 ARG CB C 29.576 0.40 1 80 17 20 ARG N N 122.520 0.40 1 81 18 21 HIS H H 8.015 0.04 1 82 18 21 HIS C C 178.217 0.40 1 83 18 21 HIS CA C 59.668 0.40 1 84 18 21 HIS CB C 29.860 0.40 1 85 18 21 HIS N N 118.697 0.40 1 86 19 22 ASP H H 7.970 0.04 1 87 19 22 ASP C C 179.100 0.40 1 88 19 22 ASP CA C 57.247 0.40 1 89 19 22 ASP CB C 40.215 0.40 1 90 19 22 ASP N N 123.307 0.40 1 91 20 23 MET H H 8.787 0.04 1 92 20 23 MET C C 178.084 0.40 1 93 20 23 MET CA C 57.666 0.40 1 94 20 23 MET CB C 31.784 0.40 1 95 20 23 MET N N 123.297 0.40 1 96 21 24 LEU H H 8.062 0.04 1 97 21 24 LEU C C 177.687 0.40 1 98 21 24 LEU CA C 58.057 0.40 1 99 21 24 LEU CB C 41.505 0.40 1 100 21 24 LEU N N 120.356 0.40 1 101 22 25 ALA H H 7.904 0.04 1 102 22 25 ALA C C 179.820 0.40 1 103 22 25 ALA CA C 55.509 0.40 1 104 22 25 ALA CB C 17.805 0.40 1 105 22 25 ALA N N 121.660 0.40 1 106 23 26 TRP H H 7.760 0.04 1 107 23 26 TRP C C 178.795 0.40 1 108 23 26 TRP CA C 60.854 0.40 1 109 23 26 TRP CB C 26.599 0.40 1 110 23 26 TRP N N 121.016 0.40 1 111 24 27 ILE H H 8.025 0.04 1 112 24 27 ILE C C 176.827 0.40 1 113 24 27 ILE CA C 65.415 0.40 1 114 24 27 ILE CB C 38.190 0.40 1 115 24 27 ILE N N 124.389 0.40 1 116 25 28 ASN H H 8.642 0.04 1 117 25 28 ASN C C 179.415 0.40 1 118 25 28 ASN CA C 55.909 0.40 1 119 25 28 ASN CB C 37.318 0.40 1 120 25 28 ASN N N 119.237 0.40 1 121 26 29 GLU H H 8.448 0.04 1 122 26 29 GLU C C 178.967 0.40 1 123 26 29 GLU CA C 58.761 0.40 1 124 26 29 GLU CB C 29.617 0.40 1 125 26 29 GLU N N 120.897 0.40 1 126 27 30 SER H H 7.760 0.04 1 127 27 30 SER C C 175.083 0.40 1 128 27 30 SER CA C 62.073 0.40 1 129 27 30 SER CB C 63.457 0.40 1 130 27 30 SER N N 115.427 0.40 1 131 28 31 LEU H H 7.559 0.04 1 132 28 31 LEU C C 175.767 0.40 1 133 28 31 LEU CA C 53.400 0.40 1 134 28 31 LEU CB C 42.301 0.40 1 135 28 31 LEU N N 115.888 0.40 1 136 29 32 GLN H H 7.617 0.04 1 137 29 32 GLN C C 175.054 0.40 1 138 29 32 GLN CA C 56.829 0.40 1 139 29 32 GLN CB C 25.449 0.40 1 140 29 32 GLN N N 120.059 0.40 1 141 30 33 LEU H H 7.502 0.04 1 142 30 33 LEU C C 175.220 0.40 1 143 30 33 LEU CA C 52.920 0.40 1 144 30 33 LEU CB C 45.655 0.40 1 145 30 33 LEU N N 119.776 0.40 1 146 31 34 ASN H H 8.010 0.04 1 147 31 34 ASN C C 175.218 0.40 1 148 31 34 ASN CA C 52.495 0.40 1 149 31 34 ASN CB C 38.801 0.40 1 150 31 34 ASN N N 120.391 0.40 1 151 32 35 LEU H H 9.242 0.04 1 152 32 35 LEU C C 178.970 0.40 1 153 32 35 LEU CA C 56.845 0.40 1 154 32 35 LEU CB C 41.847 0.40 1 155 32 35 LEU N N 123.315 0.40 1 156 33 36 THR H H 9.351 0.04 1 157 33 36 THR C C 174.817 0.40 1 158 33 36 THR CA C 61.428 0.40 1 159 33 36 THR CB C 70.579 0.40 1 160 33 36 THR N N 112.419 0.40 1 161 34 37 LYS H H 7.978 0.04 1 162 34 37 LYS C C 176.287 0.40 1 163 34 37 LYS CA C 55.352 0.40 1 164 34 37 LYS CB C 35.914 0.40 1 165 34 37 LYS N N 123.055 0.40 1 166 35 38 ILE H H 9.403 0.04 1 167 35 38 ILE C C 177.313 0.40 1 168 35 38 ILE CA C 61.005 0.40 1 169 35 38 ILE CB C 35.875 0.40 1 170 35 38 ILE N N 127.997 0.40 1 171 36 39 GLU H H 11.378 0.04 1 172 36 39 GLU N N 121.109 0.40 1 173 37 40 GLN H H 7.586 0.04 1 174 37 40 GLN C C 178.038 0.40 1 175 37 40 GLN CA C 58.315 0.40 1 176 37 40 GLN CB C 29.189 0.40 1 177 37 40 GLN N N 117.740 0.40 1 178 38 41 LEU H H 8.174 0.04 1 179 38 41 LEU C C 177.351 0.40 1 180 38 41 LEU CA C 56.167 0.40 1 181 38 41 LEU CB C 41.287 0.40 1 182 38 41 LEU N N 122.249 0.40 1 183 39 42 CYS H H 7.549 0.04 1 184 39 42 CYS C C 172.096 0.40 1 185 39 42 CYS CA C 59.297 0.40 1 186 39 42 CYS CB C 28.560 0.40 1 187 39 42 CYS N N 118.394 0.40 1 188 40 43 SER H H 6.502 0.04 1 189 40 43 SER C C 176.101 0.40 1 190 40 43 SER CA C 56.517 0.40 1 191 40 43 SER CB C 65.575 0.40 1 192 40 43 SER N N 113.710 0.40 1 193 41 44 GLY H H 7.534 0.04 1 194 41 44 GLY C C 173.305 0.40 1 195 41 44 GLY CA C 46.598 0.40 1 196 41 44 GLY N N 110.417 0.40 1 197 42 45 ALA H H 6.784 0.04 1 198 42 45 ALA C C 178.314 0.40 1 199 42 45 ALA CA C 55.770 0.40 1 200 42 45 ALA CB C 18.813 0.40 1 201 42 45 ALA N N 124.224 0.40 1 202 43 46 ALA H H 7.760 0.04 1 203 43 46 ALA C C 179.087 0.40 1 204 43 46 ALA CA C 55.170 0.40 1 205 43 46 ALA CB C 15.797 0.40 1 206 43 46 ALA N N 120.664 0.40 1 207 44 47 TYR H H 7.177 0.04 1 208 44 47 TYR C C 178.288 0.40 1 209 44 47 TYR CA C 60.798 0.40 1 210 44 47 TYR CB C 38.945 0.40 1 211 44 47 TYR N N 115.380 0.40 1 212 45 48 CYS H H 7.420 0.04 1 213 45 48 CYS C C 176.237 0.40 1 214 45 48 CYS CA C 64.890 0.40 1 215 45 48 CYS CB C 27.577 0.40 1 216 45 48 CYS N N 116.838 0.40 1 217 46 49 GLN H H 7.882 0.04 1 218 46 49 GLN C C 178.753 0.40 1 219 46 49 GLN CA C 60.465 0.40 1 220 46 49 GLN CB C 27.880 0.40 1 221 46 49 GLN N N 120.448 0.40 1 222 47 50 PHE H H 8.846 0.04 1 223 47 50 PHE C C 178.840 0.40 1 224 47 50 PHE CA C 61.878 0.40 1 225 47 50 PHE CB C 40.493 0.40 1 226 47 50 PHE N N 120.235 0.40 1 227 48 51 MET H H 8.403 0.04 1 228 48 51 MET C C 177.269 0.40 1 229 48 51 MET CA C 57.880 0.40 1 230 48 51 MET CB C 31.027 0.40 1 231 48 51 MET N N 119.781 0.40 1 232 49 52 ASP H H 7.568 0.04 1 233 49 52 ASP C C 175.782 0.40 1 234 49 52 ASP CA C 57.595 0.40 1 235 49 52 ASP CB C 43.517 0.40 1 236 49 52 ASP N N 121.456 0.40 1 237 50 53 MET H H 7.630 0.04 1 238 50 53 MET C C 177.820 0.40 1 239 50 53 MET CA C 58.833 0.40 1 240 50 53 MET CB C 33.447 0.40 1 241 50 53 MET N N 117.800 0.40 1 242 51 54 LEU H H 8.190 0.04 1 243 51 54 LEU C C 177.317 0.40 1 244 51 54 LEU CA C 56.848 0.40 1 245 51 54 LEU CB C 44.983 0.40 1 246 51 54 LEU N N 118.930 0.40 1 247 52 55 PHE H H 8.422 0.04 1 248 52 55 PHE C C 171.728 0.40 1 249 52 55 PHE CA C 53.624 0.40 1 250 52 55 PHE CB C 39.486 0.40 1 251 52 55 PHE N N 117.449 0.40 1 252 54 57 GLY H H 9.249 0.04 1 253 54 57 GLY C C 175.792 0.40 1 254 54 57 GLY CA C 45.561 0.40 1 255 54 57 GLY N N 116.779 0.40 1 256 55 58 SER H H 8.812 0.04 1 257 55 58 SER C C 174.073 0.40 1 258 55 58 SER CA C 61.354 0.40 1 259 55 58 SER CB C 63.954 0.40 1 260 55 58 SER N N 118.234 0.40 1 261 56 59 ILE H H 7.696 0.04 1 262 56 59 ILE C C 175.109 0.40 1 263 56 59 ILE CA C 57.783 0.40 1 264 56 59 ILE CB C 41.966 0.40 1 265 56 59 ILE N N 118.263 0.40 1 266 57 60 ALA H H 8.010 0.04 1 267 57 60 ALA C C 176.494 0.40 1 268 57 60 ALA CA C 50.572 0.40 1 269 57 60 ALA CB C 16.648 0.40 1 270 57 60 ALA N N 130.591 0.40 1 271 58 61 LEU H H 8.039 0.04 1 272 58 61 LEU C C 178.904 0.40 1 273 58 61 LEU CA C 57.890 0.40 1 274 58 61 LEU CB C 42.499 0.40 1 275 58 61 LEU N N 128.062 0.40 1 276 59 62 LYS H H 8.530 0.04 1 277 59 62 LYS C C 177.542 0.40 1 278 59 62 LYS CA C 57.932 0.40 1 279 59 62 LYS CB C 31.692 0.40 1 280 59 62 LYS N N 116.643 0.40 1 281 60 63 LYS H H 7.748 0.04 1 282 60 63 LYS C C 176.265 0.40 1 283 60 63 LYS CA C 55.804 0.40 1 284 60 63 LYS CB C 33.108 0.40 1 285 60 63 LYS N N 118.421 0.40 1 286 61 64 VAL H H 7.382 0.04 1 287 61 64 VAL C C 175.059 0.40 1 288 61 64 VAL CA C 62.963 0.40 1 289 61 64 VAL CB C 31.966 0.40 1 290 61 64 VAL N N 123.840 0.40 1 291 62 65 LYS H H 8.973 0.04 1 292 62 65 LYS C C 177.218 0.40 1 293 62 65 LYS CA C 54.380 0.40 1 294 62 65 LYS CB C 31.900 0.40 1 295 62 65 LYS N N 128.975 0.40 1 296 63 66 PHE H H 8.582 0.04 1 297 63 66 PHE C C 177.007 0.40 1 298 63 66 PHE CA C 62.050 0.40 1 299 63 66 PHE CB C 38.871 0.40 1 300 63 66 PHE N N 126.892 0.40 1 301 64 67 GLN H H 8.816 0.04 1 302 64 67 GLN C C 174.970 0.40 1 303 64 67 GLN N N 121.175 0.40 1 304 65 68 ALA H H 6.854 0.04 1 305 65 68 ALA C C 177.078 0.40 1 306 65 68 ALA CA C 53.047 0.40 1 307 65 68 ALA CB C 20.800 0.40 1 308 65 68 ALA N N 122.981 0.40 1 309 66 69 LYS H H 8.954 0.04 1 310 66 69 LYS C C 174.634 0.40 1 311 66 69 LYS CA C 56.077 0.40 1 312 66 69 LYS CB C 35.792 0.40 1 313 66 69 LYS N N 121.685 0.40 1 314 67 70 LEU H H 7.586 0.04 1 315 67 70 LEU C C 176.781 0.40 1 316 67 70 LEU CA C 52.686 0.40 1 317 67 70 LEU CB C 45.007 0.40 1 318 67 70 LEU N N 120.995 0.40 1 319 68 71 GLU H H 8.612 0.04 1 320 68 71 GLU C C 177.849 0.40 1 321 68 71 GLU CA C 60.995 0.40 1 322 68 71 GLU CB C 29.869 0.40 1 323 68 71 GLU N N 124.510 0.40 1 324 69 72 HIS H H 8.306 0.04 1 325 69 72 HIS C C 178.163 0.40 1 326 69 72 HIS CA C 59.599 0.40 1 327 69 72 HIS CB C 29.354 0.40 1 328 69 72 HIS N N 115.001 0.40 1 329 70 73 GLU H H 6.872 0.04 1 330 70 73 GLU C C 178.290 0.40 1 331 70 73 GLU CA C 58.206 0.40 1 332 70 73 GLU CB C 31.115 0.40 1 333 70 73 GLU N N 122.285 0.40 1 334 71 74 TYR H H 7.590 0.04 1 335 71 74 TYR C C 179.329 0.40 1 336 71 74 TYR CA C 56.616 0.40 1 337 71 74 TYR CB C 36.337 0.40 1 338 71 74 TYR N N 121.820 0.40 1 339 72 75 ILE H H 8.454 0.04 1 340 72 75 ILE C C 178.039 0.40 1 341 72 75 ILE CA C 66.194 0.40 1 342 72 75 ILE CB C 38.239 0.40 1 343 72 75 ILE N N 119.437 0.40 1 344 73 76 GLN H H 7.530 0.04 1 345 73 76 GLN C C 178.847 0.40 1 346 73 76 GLN CA C 59.496 0.40 1 347 73 76 GLN CB C 27.788 0.40 1 348 73 76 GLN N N 120.511 0.40 1 349 74 77 ASN H H 7.925 0.04 1 350 74 77 ASN C C 177.976 0.40 1 351 74 77 ASN CA C 55.533 0.40 1 352 74 77 ASN CB C 36.970 0.40 1 353 74 77 ASN N N 120.641 0.40 1 354 75 78 PHE H H 8.454 0.04 1 355 75 78 PHE C C 178.450 0.40 1 356 75 78 PHE CA C 63.715 0.40 1 357 75 78 PHE CB C 39.999 0.40 1 358 75 78 PHE N N 119.886 0.40 1 359 76 79 LYS H H 8.716 0.04 1 360 76 79 LYS C C 180.592 0.40 1 361 76 79 LYS CA C 60.055 0.40 1 362 76 79 LYS CB C 32.003 0.40 1 363 76 79 LYS N N 124.466 0.40 1 364 77 80 ILE H H 7.677 0.04 1 365 77 80 ILE C C 179.187 0.40 1 366 77 80 ILE CA C 65.121 0.40 1 367 77 80 ILE CB C 37.262 0.40 1 368 77 80 ILE N N 125.530 0.40 1 369 78 81 LEU H H 7.764 0.04 1 370 78 81 LEU C C 178.114 0.40 1 371 78 81 LEU CA C 58.205 0.40 1 372 78 81 LEU CB C 41.482 0.40 1 373 78 81 LEU N N 124.509 0.40 1 374 79 82 GLN H H 8.950 0.04 1 375 79 82 GLN C C 178.639 0.40 1 376 79 82 GLN CA C 58.897 0.40 1 377 79 82 GLN CB C 29.584 0.40 1 378 79 82 GLN N N 119.917 0.40 1 379 80 83 ALA H H 7.935 0.04 1 380 80 83 ALA C C 181.017 0.40 1 381 80 83 ALA CA C 55.250 0.40 1 382 80 83 ALA CB C 17.810 0.40 1 383 80 83 ALA N N 124.139 0.40 1 384 81 84 GLY H H 8.202 0.04 1 385 81 84 GLY C C 175.413 0.40 1 386 81 84 GLY CA C 47.970 0.40 1 387 81 84 GLY N N 110.727 0.40 1 388 82 85 PHE H H 9.138 0.04 1 389 82 85 PHE C C 178.291 0.40 1 390 82 85 PHE CA C 59.128 0.40 1 391 82 85 PHE CB C 37.143 0.40 1 392 82 85 PHE N N 124.725 0.40 1 393 83 86 LYS H H 8.338 0.04 1 394 83 86 LYS C C 180.249 0.40 1 395 83 86 LYS CA C 59.424 0.40 1 396 83 86 LYS CB C 32.111 0.40 1 397 83 86 LYS N N 121.480 0.40 1 398 84 87 ARG H H 8.142 0.04 1 399 84 87 ARG C C 177.733 0.40 1 400 84 87 ARG CA C 59.215 0.40 1 401 84 87 ARG CB C 30.324 0.40 1 402 84 87 ARG N N 121.669 0.40 1 403 85 88 MET H H 7.507 0.04 1 404 85 88 MET C C 175.715 0.40 1 405 85 88 MET CA C 52.635 0.40 1 406 85 88 MET CB C 30.090 0.40 1 407 85 88 MET N N 113.795 0.40 1 408 86 89 GLY H H 7.664 0.04 1 409 86 89 GLY C C 175.166 0.40 1 410 86 89 GLY CA C 46.929 0.40 1 411 86 89 GLY N N 109.819 0.40 1 412 87 90 VAL H H 8.549 0.04 1 413 87 90 VAL C C 176.392 0.40 1 414 87 90 VAL CA C 62.070 0.40 1 415 87 90 VAL CB C 31.170 0.40 1 416 87 90 VAL N N 123.564 0.40 1 417 88 91 ASP H H 8.813 0.04 1 418 88 91 ASP C C 174.692 0.40 1 419 88 91 ASP CA C 53.012 0.40 1 420 88 91 ASP CB C 39.656 0.40 1 421 88 91 ASP N N 131.827 0.40 1 422 89 92 LYS H H 6.878 0.04 1 423 89 92 LYS C C 174.417 0.40 1 424 89 92 LYS CA C 54.795 0.40 1 425 89 92 LYS CB C 35.312 0.40 1 426 89 92 LYS N N 124.297 0.40 1 427 90 93 ILE H H 8.466 0.04 1 428 90 93 ILE C C 176.066 0.40 1 429 90 93 ILE CA C 59.728 0.40 1 430 90 93 ILE CB C 37.073 0.40 1 431 90 93 ILE N N 131.010 0.40 1 432 91 94 ILE H H 8.930 0.04 1 433 91 94 ILE C C 175.705 0.40 1 434 91 94 ILE CA C 59.378 0.40 1 435 91 94 ILE CB C 39.041 0.40 1 436 91 94 ILE N N 131.888 0.40 1 437 93 96 VAL H H 8.064 0.04 1 438 93 96 VAL C C 175.142 0.40 1 439 93 96 VAL CA C 67.592 0.40 1 440 93 96 VAL CB C 32.513 0.40 1 441 93 96 VAL N N 126.618 0.40 1 442 94 97 ASP H H 8.161 0.04 1 443 94 97 ASP C C 177.510 0.40 1 444 94 97 ASP CA C 56.843 0.40 1 445 94 97 ASP CB C 39.877 0.40 1 446 94 97 ASP N N 115.473 0.40 1 447 95 98 LYS H H 7.094 0.04 1 448 95 98 LYS C C 179.413 0.40 1 449 95 98 LYS CA C 57.749 0.40 1 450 95 98 LYS CB C 32.911 0.40 1 451 95 98 LYS N N 116.688 0.40 1 452 96 99 LEU H H 7.857 0.04 1 453 96 99 LEU C C 181.134 0.40 1 454 96 99 LEU CA C 58.134 0.40 1 455 96 99 LEU CB C 41.047 0.40 1 456 96 99 LEU N N 120.624 0.40 1 457 97 100 VAL H H 7.809 0.04 1 458 97 100 VAL C C 175.482 0.40 1 459 97 100 VAL CA C 64.501 0.40 1 460 97 100 VAL CB C 31.888 0.40 1 461 97 100 VAL N N 110.028 0.40 1 462 98 101 LYS H H 6.996 0.04 1 463 98 101 LYS C C 178.761 0.40 1 464 98 101 LYS CA C 55.883 0.40 1 465 98 101 LYS CB C 31.724 0.40 1 466 98 101 LYS N N 118.003 0.40 1 467 99 102 GLY H H 7.990 0.04 1 468 99 102 GLY C C 173.652 0.40 1 469 99 102 GLY CA C 47.162 0.40 1 470 99 102 GLY N N 105.352 0.40 1 471 100 103 LYS H H 8.770 0.04 1 472 100 103 LYS C C 178.847 0.40 1 473 100 103 LYS CA C 55.030 0.40 1 474 100 103 LYS CB C 32.507 0.40 1 475 100 103 LYS N N 118.967 0.40 1 476 101 104 PHE H H 9.242 0.04 1 477 101 104 PHE C C 177.071 0.40 1 478 101 104 PHE CA C 64.061 0.40 1 479 101 104 PHE CB C 39.260 0.40 1 480 101 104 PHE N N 125.853 0.40 1 481 102 105 GLN H H 9.292 0.04 1 482 102 105 GLN C C 178.422 0.40 1 483 102 105 GLN CA C 60.624 0.40 1 484 102 105 GLN CB C 27.637 0.40 1 485 102 105 GLN N N 120.714 0.40 1 486 103 106 ASP H H 7.646 0.04 1 487 103 106 ASP C C 179.044 0.40 1 488 103 106 ASP CA C 56.928 0.40 1 489 103 106 ASP CB C 41.260 0.40 1 490 103 106 ASP N N 115.594 0.40 1 491 104 107 ASN H H 7.285 0.04 1 492 104 107 ASN C C 177.565 0.40 1 493 104 107 ASN CA C 57.075 0.40 1 494 104 107 ASN CB C 39.390 0.40 1 495 104 107 ASN N N 118.147 0.40 1 496 105 108 PHE H H 9.299 0.04 1 497 105 108 PHE C C 176.680 0.40 1 498 105 108 PHE CA C 58.844 0.40 1 499 105 108 PHE CB C 38.552 0.40 1 500 105 108 PHE N N 125.693 0.40 1 501 106 109 GLU H H 8.156 0.04 1 502 106 109 GLU C C 179.843 0.40 1 503 106 109 GLU CA C 59.799 0.40 1 504 106 109 GLU CB C 29.539 0.40 1 505 106 109 GLU N N 119.927 0.40 1 506 107 110 PHE H H 7.658 0.04 1 507 107 110 PHE C C 177.142 0.40 1 508 107 110 PHE CA C 62.581 0.40 1 509 107 110 PHE CB C 39.614 0.40 1 510 107 110 PHE N N 119.758 0.40 1 511 108 111 VAL H H 8.037 0.04 1 512 108 111 VAL C C 176.414 0.40 1 513 108 111 VAL CA C 65.081 0.40 1 514 108 111 VAL CB C 30.382 0.40 1 515 108 111 VAL N N 121.456 0.40 1 516 109 112 GLN H H 7.646 0.04 1 517 109 112 GLN C C 179.409 0.40 1 518 109 112 GLN CA C 59.049 0.40 1 519 109 112 GLN CB C 27.411 0.40 1 520 109 112 GLN N N 122.016 0.40 1 521 110 113 TRP H H 7.154 0.04 1 522 110 113 TRP C C 176.378 0.40 1 523 110 113 TRP CA C 62.274 0.40 1 524 110 113 TRP CB C 27.199 0.40 1 525 110 113 TRP N N 121.373 0.40 1 526 111 114 PHE H H 8.953 0.04 1 527 111 114 PHE C C 176.815 0.40 1 528 111 114 PHE CA C 61.747 0.40 1 529 111 114 PHE CB C 39.825 0.40 1 530 111 114 PHE N N 122.723 0.40 1 531 112 115 LYS H H 8.702 0.04 1 532 112 115 LYS C C 176.912 0.40 1 533 112 115 LYS CA C 58.280 0.40 1 534 112 115 LYS CB C 31.622 0.40 1 535 112 115 LYS N N 120.774 0.40 1 536 113 116 LYS H H 6.603 0.04 1 537 113 116 LYS C C 179.428 0.40 1 538 113 116 LYS CA C 59.112 0.40 1 539 113 116 LYS CB C 31.841 0.40 1 540 113 116 LYS N N 119.637 0.40 1 541 114 117 PHE H H 7.681 0.04 1 542 114 117 PHE C C 176.963 0.40 1 543 114 117 PHE CA C 60.938 0.40 1 544 114 117 PHE CB C 37.837 0.40 1 545 114 117 PHE N N 124.248 0.40 1 546 115 118 PHE H H 9.115 0.04 1 547 115 118 PHE C C 177.234 0.40 1 548 115 118 PHE CA C 61.303 0.40 1 549 115 118 PHE CB C 39.197 0.40 1 550 115 118 PHE N N 125.786 0.40 1 551 116 119 ASP H H 8.668 0.04 1 552 116 119 ASP C C 178.471 0.40 1 553 116 119 ASP CA C 57.102 0.40 1 554 116 119 ASP CB C 39.456 0.40 1 555 116 119 ASP N N 121.680 0.40 1 556 117 120 ALA H H 7.296 0.04 1 557 117 120 ALA C C 177.486 0.40 1 558 117 120 ALA CA C 53.342 0.40 1 559 117 120 ALA CB C 18.712 0.40 1 560 117 120 ALA N N 120.370 0.40 1 561 118 121 ASN H H 7.017 0.04 1 562 118 121 ASN C C 173.960 0.40 1 563 118 121 ASN CA C 54.002 0.40 1 564 118 121 ASN CB C 42.887 0.40 1 565 118 121 ASN N N 115.061 0.40 1 566 119 122 TYR H H 7.945 0.04 1 567 119 122 TYR C C 175.269 0.40 1 568 119 122 TYR CA C 58.045 0.40 1 569 119 122 TYR CB C 37.705 0.40 1 570 119 122 TYR N N 124.782 0.40 1 571 120 123 ASP H H 7.919 0.04 1 572 120 123 ASP C C 176.691 0.40 1 573 120 123 ASP CA C 53.182 0.40 1 574 120 123 ASP CB C 41.048 0.40 1 575 120 123 ASP N N 129.605 0.40 1 576 121 124 GLY H H 5.417 0.04 1 577 121 124 GLY C C 174.345 0.40 1 578 121 124 GLY CA C 46.122 0.40 1 579 121 124 GLY N N 107.007 0.40 1 580 122 125 LYS H H 7.446 0.04 1 581 122 125 LYS C C 176.282 0.40 1 582 122 125 LYS CA C 56.572 0.40 1 583 122 125 LYS CB C 31.728 0.40 1 584 122 125 LYS N N 120.810 0.40 1 585 123 126 ASP H H 8.466 0.04 1 586 123 126 ASP C C 175.436 0.40 1 587 123 126 ASP CA C 54.817 0.40 1 588 123 126 ASP CB C 41.130 0.40 1 589 123 126 ASP N N 124.188 0.40 1 590 124 127 TYR H H 8.308 0.04 1 591 124 127 TYR C C 173.656 0.40 1 592 124 127 TYR CA C 58.055 0.40 1 593 124 127 TYR CB C 41.161 0.40 1 594 124 127 TYR N N 124.590 0.40 1 595 125 128 ASP H H 7.867 0.04 1 596 125 128 ASP C C 174.577 0.40 1 597 125 128 ASP CA C 50.142 0.40 1 598 125 128 ASP CB C 41.192 0.40 1 599 125 128 ASP N N 128.008 0.40 1 600 127 130 VAL H H 7.565 0.04 1 601 127 130 VAL C C 177.435 0.40 1 602 127 130 VAL CA C 64.264 0.40 1 603 127 130 VAL CB C 31.826 0.40 1 604 127 130 VAL N N 120.620 0.40 1 605 128 131 ALA H H 7.237 0.04 1 606 128 131 ALA C C 177.787 0.40 1 607 128 131 ALA CA C 53.084 0.40 1 608 128 131 ALA CB C 18.752 0.40 1 609 128 131 ALA N N 124.556 0.40 1 610 129 132 ALA H H 7.184 0.04 1 611 129 132 ALA C C 176.412 0.40 1 612 129 132 ALA CA C 52.691 0.40 1 613 129 132 ALA CB C 19.932 0.40 1 614 129 132 ALA N N 120.445 0.40 1 615 130 133 ARG H H 7.028 0.04 1 616 130 133 ARG C C 180.470 0.40 1 617 130 133 ARG CA C 57.394 0.40 1 618 130 133 ARG CB C 31.958 0.40 1 619 130 133 ARG N N 123.750 0.40 1 stop_ save_