data_16930 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shift assignments of the Talin F2 domain (residues 196-309) ; _BMRB_accession_number 16930 _BMRB_flat_file_name bmr16930.str _Entry_type original _Submission_date 2010-05-14 _Accession_date 2010-05-14 _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 Goult Ben T. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 113 "13C chemical shifts" 343 "15N chemical shifts" 113 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-10-19 update BMRB 'update entry citation' 2010-10-14 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 15457 'domain, 1655-1822' 15458 'F0 domain (residues 1-85)' 15615 'F0F1 double domain' 15616 F1 15625 'Residues 1815-1973' 16932 'F2F3 domain (residues 196-405)' 16959 'F1F2 double domain (residues 86-303)' 17070 'domain C' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'The structure of the talin/integrin complex at a lipid bilayer: an NMR and MD simulation study.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20947017 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kalli Antreas C. . 2 Wegener Kate L. . 3 Goult Benjamin T. . 4 Anthis Nicholas J. . 5 Campbell Iain D. . 6 Sansom Mark S.P. . stop_ _Journal_abbreviation Structure _Journal_name_full 'Structure (London, England : 1993)' _Journal_volume 18 _Journal_issue 10 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1280 _Page_last 1288 _Year 2010 _Details . loop_ _Keyword F2 FERM 'Focal adhesion' phospholipid talin stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name F2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label F2 $F2 stop_ _System_molecular_weight 13847 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_F2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common F2 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 120 _Mol_residue_sequence ; GIDPFTKFFYSDQNVDSRDP VQLNLLYVQARDDILNGSHP VSFDKACEFAGFQCQIQFGP HNEQKHKAGFLDLKDFLPKE YVKQKGERKIFQAHKNCGQM SEIEAKVRYVKLARSLKTYG ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 ILE 3 ASP 4 PRO 5 PHE 6 THR 7 LYS 8 PHE 9 PHE 10 TYR 11 SER 12 ASP 13 GLN 14 ASN 15 VAL 16 ASP 17 SER 18 ARG 19 ASP 20 PRO 21 VAL 22 GLN 23 LEU 24 ASN 25 LEU 26 LEU 27 TYR 28 VAL 29 GLN 30 ALA 31 ARG 32 ASP 33 ASP 34 ILE 35 LEU 36 ASN 37 GLY 38 SER 39 HIS 40 PRO 41 VAL 42 SER 43 PHE 44 ASP 45 LYS 46 ALA 47 CYS 48 GLU 49 PHE 50 ALA 51 GLY 52 PHE 53 GLN 54 CYS 55 GLN 56 ILE 57 GLN 58 PHE 59 GLY 60 PRO 61 HIS 62 ASN 63 GLU 64 GLN 65 LYS 66 HIS 67 LYS 68 ALA 69 GLY 70 PHE 71 LEU 72 ASP 73 LEU 74 LYS 75 ASP 76 PHE 77 LEU 78 PRO 79 LYS 80 GLU 81 TYR 82 VAL 83 LYS 84 GLN 85 LYS 86 GLY 87 GLU 88 ARG 89 LYS 90 ILE 91 PHE 92 GLN 93 ALA 94 HIS 95 LYS 96 ASN 97 CYS 98 GLY 99 GLN 100 MET 101 SER 102 GLU 103 ILE 104 GLU 105 ALA 106 LYS 107 VAL 108 ARG 109 TYR 110 VAL 111 LYS 112 LEU 113 ALA 114 ARG 115 SER 116 LEU 117 LYS 118 THR 119 TYR 120 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-08 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 15792 talin-F2F3 87.50 201 100.00 100.00 1.90e-70 BMRB 16932 F2F3 100.00 216 100.00 100.00 1.25e-82 BMRB 16959 F1F2 90.00 194 100.00 100.00 7.22e-73 PDB 1Y19 "Structural Basis For Phosphatidylinositol Phosphate Kinase Type I-Gamma Binding To Talin At Focal Adhesions" 84.17 202 100.00 100.00 5.87e-67 PDB 3IVF "Crystal Structure Of The Talin Head Ferm Domain" 95.00 371 100.00 100.00 4.27e-76 DBJ BAA82979 "KIAA1027 protein [Homo sapiens]" 95.00 2550 100.00 100.00 2.31e-73 DBJ BAC30516 "unnamed protein product [Mus musculus]" 95.00 300 100.00 100.00 3.87e-77 DBJ BAC65702 "mKIAA1027 protein [Mus musculus]" 95.00 2564 100.00 100.00 3.35e-73 DBJ BAE27781 "unnamed protein product [Mus musculus]" 95.00 2541 100.00 100.00 3.32e-73 DBJ BAG09941 "talin-1 [synthetic construct]" 95.00 2541 100.00 100.00 2.66e-73 EMBL CAA39588 "talin [Mus musculus]" 95.00 2541 100.00 100.00 3.32e-73 GB AAD13152 "talin [Homo sapiens]" 95.00 2541 100.00 100.00 2.66e-73 GB AAF23322 "talin [Homo sapiens]" 95.00 2541 100.00 100.00 2.66e-73 GB AAF27330 "talin [Homo sapiens]" 95.00 2540 100.00 100.00 2.66e-73 GB AAH42923 "Talin 1 [Homo sapiens]" 95.00 2541 100.00 100.00 2.21e-73 GB AAI22767 "TLN1 protein [Bos taurus]" 95.00 407 100.00 100.00 4.66e-76 PRF 1617167A talin 95.00 2541 100.00 100.00 3.32e-73 REF NP_001034114 "talin-1 [Rattus norvegicus]" 95.00 2541 100.00 100.00 2.93e-73 REF NP_001192357 "talin-1 [Bos taurus]" 95.00 2541 100.00 100.00 2.21e-73 REF NP_006280 "talin-1 [Homo sapiens]" 95.00 2541 100.00 100.00 2.66e-73 REF NP_035732 "talin-1 [Mus musculus]" 95.00 2541 100.00 100.00 3.32e-73 REF XP_001084941 "PREDICTED: talin-1 [Macaca mulatta]" 95.00 2428 100.00 100.00 2.00e-73 SP P26039 "RecName: Full=Talin-1" 95.00 2541 100.00 100.00 3.32e-73 SP Q9Y490 "RecName: Full=Talin-1" 95.00 2541 100.00 100.00 2.66e-73 TPG DAA26829 "TPA: talin 1 [Bos taurus]" 95.00 2541 100.00 100.00 2.30e-73 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $F2 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 _Vector_name $F2 'recombinant technology' . Escherichia coli 'BL21 (DE3)' PET-151 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 $F2 1 mM 'natural abundance' DTT 2 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' 'sodium phosphate' 20 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 2 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_Analysis _Saveframe_category software _Name Analysis _Version 2.1.3 loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _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_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _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' 50 0.5 M pH 6.5 0.1 pH pressure 1 . atm temperature 298 0.5 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_ _Software_label $Analysis stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCA' '3D HNCACB' 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 F2 _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 2 ILE C C 176.435 0.2 1 2 2 2 ILE CA C 60.834 0.2 1 3 2 2 ILE CB C 39.021 0.2 1 4 3 3 ASP H H 8.419 0.02 1 5 3 3 ASP CA C 51.979 0.2 1 6 3 3 ASP CB C 41.388 0.2 1 7 3 3 ASP N N 126.705 0.2 1 8 4 4 PRO C C 174.908 0.2 1 9 4 4 PRO CA C 63.728 0.2 1 10 4 4 PRO CB C 31.904 0.2 1 11 5 5 PHE H H 8.235 0.02 1 12 5 5 PHE C C 175.616 0.2 1 13 5 5 PHE CA C 58.639 0.2 1 14 5 5 PHE CB C 38.756 0.2 1 15 5 5 PHE N N 118.355 0.2 1 16 6 6 THR H H 7.743 0.02 1 17 6 6 THR C C 177.309 0.2 1 18 6 6 THR CA C 63.055 0.2 1 19 6 6 THR CB C 69.585 0.2 1 20 6 6 THR N N 114.685 0.2 1 21 7 7 LYS H H 8.013 0.02 1 22 7 7 LYS C C 175.679 0.2 1 23 7 7 LYS CA C 57.064 0.2 1 24 7 7 LYS CB C 32.537 0.2 1 25 7 7 LYS N N 122.257 0.2 1 26 8 8 PHE H H 7.896 0.02 1 27 8 8 PHE C C 176.651 0.2 1 28 8 8 PHE CA C 58.124 0.2 1 29 8 8 PHE CB C 39.525 0.2 1 30 8 8 PHE N N 119.713 0.2 1 31 9 9 PHE H H 7.937 0.02 1 32 9 9 PHE C C 177.085 0.2 1 33 9 9 PHE CA C 58.113 0.2 1 34 9 9 PHE CB C 39.714 0.2 1 35 9 9 PHE N N 121.224 0.2 1 36 10 10 TYR H H 7.823 0.02 1 37 10 10 TYR C C 176.857 0.2 1 38 10 10 TYR CA C 58.065 0.2 1 39 10 10 TYR CB C 39.053 0.2 1 40 10 10 TYR N N 120.533 0.2 1 41 11 11 SER H H 7.833 0.02 1 42 11 11 SER C C 177.980 0.2 1 43 11 11 SER CA C 58.168 0.2 1 44 11 11 SER CB C 64.190 0.2 1 45 11 11 SER N N 116.903 0.2 1 46 12 12 ASP H H 8.293 0.02 1 47 12 12 ASP C C 175.800 0.2 1 48 12 12 ASP CA C 54.421 0.2 1 49 12 12 ASP CB C 40.851 0.2 1 50 12 12 ASP N N 122.234 0.2 1 51 13 13 GLN H H 8.092 0.02 1 52 13 13 GLN C C 176.197 0.2 1 53 13 13 GLN CA C 56.251 0.2 1 54 13 13 GLN CB C 29.051 0.2 1 55 13 13 GLN N N 118.782 0.2 1 56 14 14 ASN H H 8.284 0.02 1 57 14 14 ASN C C 177.057 0.2 1 58 14 14 ASN CA C 53.545 0.2 1 59 14 14 ASN CB C 38.976 0.2 1 60 14 14 ASN N N 118.859 0.2 1 61 15 15 VAL H H 7.989 0.02 1 62 15 15 VAL C C 177.241 0.2 1 63 15 15 VAL CA C 62.612 0.2 1 64 15 15 VAL CB C 32.589 0.2 1 65 15 15 VAL N N 120.850 0.2 1 66 16 16 ASP H H 8.337 0.02 1 67 16 16 ASP C C 175.649 0.2 1 68 16 16 ASP CA C 54.191 0.2 1 69 16 16 ASP CB C 41.687 0.2 1 70 16 16 ASP N N 123.743 0.2 1 71 17 17 SER H H 8.193 0.02 1 72 17 17 SER C C 177.579 0.2 1 73 17 17 SER CA C 58.596 0.2 1 74 17 17 SER CB C 63.663 0.2 1 75 17 17 SER N N 115.756 0.2 1 76 18 18 ARG H H 8.099 0.02 1 77 18 18 ARG C C 176.212 0.2 1 78 18 18 ARG CA C 57.093 0.2 1 79 18 18 ARG CB C 30.082 0.2 1 80 18 18 ARG N N 120.634 0.2 1 81 19 19 ASP H H 7.860 0.02 1 82 19 19 ASP CA C 57.094 0.2 1 83 19 19 ASP CB C 41.597 0.2 1 84 19 19 ASP N N 118.986 0.2 1 85 20 20 PRO C C 173.143 0.2 1 86 20 20 PRO CA C 64.847 0.2 1 87 20 20 PRO CB C 32.272 0.2 1 88 21 21 VAL H H 7.877 0.02 1 89 21 21 VAL C C 173.163 0.2 1 90 21 21 VAL CA C 66.146 0.2 1 91 21 21 VAL CB C 31.275 0.2 1 92 21 21 VAL N N 120.851 0.2 1 93 22 22 GLN H H 7.539 0.02 1 94 22 22 GLN C C 173.428 0.2 1 95 22 22 GLN CA C 58.160 0.2 1 96 22 22 GLN CB C 28.385 0.2 1 97 22 22 GLN N N 120.719 0.2 1 98 23 23 LEU H H 8.243 0.02 1 99 23 23 LEU C C 173.821 0.2 1 100 23 23 LEU CA C 57.873 0.2 1 101 23 23 LEU CB C 41.542 0.2 1 102 23 23 LEU N N 119.102 0.2 1 103 24 24 ASN H H 7.775 0.02 1 104 24 24 ASN C C 175.736 0.2 1 105 24 24 ASN CA C 57.806 0.2 1 106 24 24 ASN CB C 38.820 0.2 1 107 24 24 ASN N N 115.379 0.2 1 108 25 25 LEU H H 7.499 0.02 1 109 25 25 LEU C C 172.232 0.2 1 110 25 25 LEU CA C 58.323 0.2 1 111 25 25 LEU CB C 41.407 0.2 1 112 25 25 LEU N N 118.134 0.2 1 113 26 26 LEU H H 7.918 0.02 1 114 26 26 LEU C C 172.296 0.2 1 115 26 26 LEU CA C 57.588 0.2 1 116 26 26 LEU CB C 42.385 0.2 1 117 26 26 LEU N N 118.979 0.2 1 118 27 27 TYR H H 8.468 0.02 1 119 27 27 TYR C C 177.329 0.2 1 120 27 27 TYR CA C 60.774 0.2 1 121 27 27 TYR CB C 37.863 0.2 1 122 27 27 TYR N N 120.943 0.2 1 123 28 28 VAL H H 8.361 0.02 1 124 28 28 VAL C C 174.718 0.2 1 125 28 28 VAL CA C 66.878 0.2 1 126 28 28 VAL CB C 31.315 0.2 1 127 28 28 VAL N N 118.390 0.2 1 128 29 29 GLN H H 7.287 0.02 1 129 29 29 GLN C C 174.428 0.2 1 130 29 29 GLN CA C 58.651 0.2 1 131 29 29 GLN CB C 28.674 0.2 1 132 29 29 GLN N N 116.015 0.2 1 133 30 30 ALA H H 7.673 0.02 1 134 30 30 ALA C C 172.731 0.2 1 135 30 30 ALA CA C 54.886 0.2 1 136 30 30 ALA CB C 17.946 0.2 1 137 30 30 ALA N N 120.640 0.2 1 138 31 31 ARG H H 8.596 0.02 1 139 31 31 ARG C C 173.199 0.2 1 140 31 31 ARG CA C 57.020 0.2 1 141 31 31 ARG CB C 29.170 0.2 1 142 31 31 ARG N N 119.524 0.2 1 143 32 32 ASP H H 8.550 0.02 1 144 32 32 ASP C C 173.386 0.2 1 145 32 32 ASP CA C 57.607 0.2 1 146 32 32 ASP CB C 38.522 0.2 1 147 32 32 ASP N N 120.047 0.2 1 148 33 33 ASP H H 7.650 0.02 1 149 33 33 ASP C C 173.181 0.2 1 150 33 33 ASP CA C 56.798 0.2 1 151 33 33 ASP CB C 40.097 0.2 1 152 33 33 ASP N N 119.151 0.2 1 153 34 34 ILE H H 7.572 0.02 1 154 34 34 ILE C C 171.822 0.2 1 155 34 34 ILE CA C 63.944 0.2 1 156 34 34 ILE CB C 37.057 0.2 1 157 34 34 ILE N N 122.511 0.2 1 158 35 35 LEU H H 8.968 0.02 1 159 35 35 LEU C C 172.275 0.2 1 160 35 35 LEU CA C 58.114 0.2 1 161 35 35 LEU CB C 41.096 0.2 1 162 35 35 LEU N N 119.861 0.2 1 163 36 36 ASN H H 8.532 0.02 1 164 36 36 ASN C C 175.125 0.2 1 165 36 36 ASN CA C 52.989 0.2 1 166 36 36 ASN CB C 37.934 0.2 1 167 36 36 ASN N N 114.041 0.2 1 168 37 37 GLY H H 7.494 0.02 1 169 37 37 GLY C C 177.326 0.2 1 170 37 37 GLY CA C 45.623 0.2 1 171 37 37 GLY N N 107.210 0.2 1 172 38 38 SER H H 8.489 0.02 1 173 38 38 SER C C 177.969 0.2 1 174 38 38 SER CA C 61.003 0.2 1 175 38 38 SER CB C 62.698 0.2 1 176 38 38 SER N N 117.653 0.2 1 177 39 39 HIS H H 7.593 0.02 1 178 39 39 HIS CA C 51.057 0.2 1 179 39 39 HIS CB C 31.251 0.2 1 180 39 39 HIS N N 120.490 0.2 1 181 40 40 PRO CA C 63.310 0.2 1 182 40 40 PRO CB C 32.016 0.2 1 183 41 41 VAL H H 8.146 0.02 1 184 41 41 VAL C C 176.422 0.2 1 185 41 41 VAL CA C 58.892 0.2 1 186 41 41 VAL CB C 36.753 0.2 1 187 41 41 VAL N N 115.861 0.2 1 188 42 42 SER H H 8.839 0.02 1 189 42 42 SER C C 178.170 0.2 1 190 42 42 SER CA C 57.565 0.2 1 191 42 42 SER CB C 64.991 0.2 1 192 42 42 SER N N 119.319 0.2 1 193 43 43 PHE H H 9.025 0.02 1 194 43 43 PHE C C 174.675 0.2 1 195 43 43 PHE CA C 60.205 0.2 1 196 43 43 PHE CB C 38.720 0.2 1 197 43 43 PHE N N 123.439 0.2 1 198 44 44 ASP H H 8.465 0.02 1 199 44 44 ASP C C 172.113 0.2 1 200 44 44 ASP CA C 57.616 0.2 1 201 44 44 ASP CB C 40.058 0.2 1 202 44 44 ASP N N 117.171 0.2 1 203 45 45 LYS H H 7.564 0.02 1 204 45 45 LYS C C 174.039 0.2 1 205 45 45 LYS CA C 57.356 0.2 1 206 45 45 LYS CB C 31.013 0.2 1 207 45 45 LYS N N 118.933 0.2 1 208 46 46 ALA H H 9.105 0.02 1 209 46 46 ALA C C 171.126 0.2 1 210 46 46 ALA CA C 56.062 0.2 1 211 46 46 ALA CB C 17.783 0.2 1 212 46 46 ALA N N 122.001 0.2 1 213 47 47 CYS H H 7.707 0.02 1 214 47 47 CYS C C 176.879 0.2 1 215 47 47 CYS CA C 63.977 0.2 1 216 47 47 CYS CB C 26.961 0.2 1 217 47 47 CYS N N 115.613 0.2 1 218 48 48 GLU H H 7.215 0.02 1 219 48 48 GLU C C 172.083 0.2 1 220 48 48 GLU CA C 59.920 0.2 1 221 48 48 GLU CB C 29.132 0.2 1 222 48 48 GLU N N 121.475 0.2 1 223 49 49 PHE H H 8.495 0.02 1 224 49 49 PHE C C 174.049 0.2 1 225 49 49 PHE CA C 63.922 0.2 1 226 49 49 PHE CB C 37.583 0.2 1 227 49 49 PHE N N 118.582 0.2 1 228 50 50 ALA H H 8.138 0.02 1 229 50 50 ALA C C 172.040 0.2 1 230 50 50 ALA CA C 54.590 0.2 1 231 50 50 ALA CB C 19.226 0.2 1 232 50 50 ALA N N 119.766 0.2 1 233 51 51 GLY H H 8.134 0.02 1 234 51 51 GLY C C 176.473 0.2 1 235 51 51 GLY CA C 48.040 0.2 1 236 51 51 GLY N N 107.274 0.2 1 237 52 52 PHE H H 7.303 0.02 1 238 52 52 PHE C C 174.042 0.2 1 239 52 52 PHE CA C 60.483 0.2 1 240 52 52 PHE CB C 39.808 0.2 1 241 52 52 PHE N N 119.306 0.2 1 242 53 53 GLN H H 9.096 0.02 1 243 53 53 GLN C C 172.730 0.2 1 244 53 53 GLN CA C 59.725 0.2 1 245 53 53 GLN CB C 28.645 0.2 1 246 53 53 GLN N N 121.718 0.2 1 247 54 54 CYS H H 8.802 0.02 1 248 54 54 CYS C C 176.247 0.2 1 249 54 54 CYS CA C 64.521 0.2 1 250 54 54 CYS CB C 24.762 0.2 1 251 54 54 CYS N N 117.821 0.2 1 252 55 55 GLN H H 7.659 0.02 1 253 55 55 GLN C C 172.067 0.2 1 254 55 55 GLN CA C 58.796 0.2 1 255 55 55 GLN CB C 27.045 0.2 1 256 55 55 GLN N N 123.079 0.2 1 257 56 56 ILE H H 8.282 0.02 1 258 56 56 ILE C C 174.821 0.2 1 259 56 56 ILE CA C 65.527 0.2 1 260 56 56 ILE CB C 39.146 0.2 1 261 56 56 ILE N N 119.505 0.2 1 262 57 57 GLN H H 8.247 0.02 1 263 57 57 GLN C C 174.032 0.2 1 264 57 57 GLN CA C 58.868 0.2 1 265 57 57 GLN CB C 28.283 0.2 1 266 57 57 GLN N N 115.735 0.2 1 267 58 58 PHE H H 8.898 0.02 1 268 58 58 PHE C C 174.587 0.2 1 269 58 58 PHE CA C 56.444 0.2 1 270 58 58 PHE CB C 40.269 0.2 1 271 58 58 PHE N N 114.893 0.2 1 272 59 59 GLY H H 7.658 0.02 1 273 59 59 GLY CA C 44.446 0.2 1 274 59 59 GLY N N 111.184 0.2 1 275 60 60 PRO C C 175.996 0.2 1 276 60 60 PRO CA C 62.642 0.2 1 277 60 60 PRO CB C 32.096 0.2 1 278 61 61 HIS H H 8.870 0.02 1 279 61 61 HIS C C 177.261 0.2 1 280 61 61 HIS CA C 58.392 0.2 1 281 61 61 HIS CB C 28.361 0.2 1 282 61 61 HIS N N 124.165 0.2 1 283 62 62 ASN H H 10.033 0.02 1 284 62 62 ASN C C 177.132 0.2 1 285 62 62 ASN CA C 51.209 0.2 1 286 62 62 ASN CB C 39.269 0.2 1 287 62 62 ASN N N 112.025 10.2 1 288 63 63 GLU H H 9.071 0.02 1 289 63 63 GLU C C 175.612 0.2 1 290 63 63 GLU CA C 58.675 0.2 1 291 63 63 GLU CB C 29.379 0.2 1 292 63 63 GLU N N 125.353 0.2 1 293 64 64 GLN H H 7.555 0.02 1 294 64 64 GLN C C 175.992 0.2 1 295 64 64 GLN CA C 57.292 0.2 1 296 64 64 GLN CB C 28.377 0.2 1 297 64 64 GLN N N 114.516 0.2 1 298 65 65 LYS H H 6.784 0.02 1 299 65 65 LYS C C 176.423 0.2 1 300 65 65 LYS CA C 56.029 0.2 1 301 65 65 LYS CB C 35.027 0.2 1 302 65 65 LYS N N 116.212 0.2 1 303 66 66 HIS H H 7.759 0.02 1 304 66 66 HIS C C 180.375 0.2 1 305 66 66 HIS CA C 53.934 0.2 1 306 66 66 HIS CB C 29.332 0.2 1 307 66 66 HIS N N 122.249 0.2 1 308 67 67 LYS H H 6.576 0.02 1 309 67 67 LYS C C 176.927 0.2 1 310 67 67 LYS CA C 53.901 0.2 1 311 67 67 LYS CB C 34.693 0.2 1 312 67 67 LYS N N 118.096 0.2 1 313 68 68 ALA H H 8.359 0.02 1 314 68 68 ALA C C 173.241 0.2 1 315 68 68 ALA CA C 54.053 0.2 1 316 68 68 ALA CB C 18.172 0.2 1 317 68 68 ALA N N 121.819 0.2 1 318 69 69 GLY H H 10.109 0.02 1 319 69 69 GLY C C 176.872 0.2 1 320 69 69 GLY CA C 45.080 0.2 1 321 69 69 GLY N N 114.407 0.2 1 322 70 70 PHE H H 8.563 0.02 1 323 70 70 PHE C C 176.445 0.2 1 324 70 70 PHE CA C 60.028 0.2 1 325 70 70 PHE CB C 41.185 0.2 1 326 70 70 PHE N N 121.642 0.2 1 327 71 71 LEU H H 7.963 0.02 1 328 71 71 LEU C C 175.757 0.2 1 329 71 71 LEU CA C 53.769 0.2 1 330 71 71 LEU CB C 43.218 0.2 1 331 71 71 LEU N N 115.663 0.2 1 332 72 72 ASP H H 8.704 0.02 1 333 72 72 ASP C C 174.681 0.2 1 334 72 72 ASP CA C 52.794 0.2 1 335 72 72 ASP CB C 39.962 0.2 1 336 72 72 ASP N N 123.113 0.2 1 337 73 73 LEU H H 8.541 0.02 1 338 73 73 LEU C C 173.803 0.2 1 339 73 73 LEU CA C 58.786 0.2 1 340 73 73 LEU CB C 41.822 0.2 1 341 73 73 LEU N N 124.594 0.2 1 342 74 74 LYS H H 8.307 0.02 1 343 74 74 LYS C C 174.943 0.2 1 344 74 74 LYS CA C 58.213 0.2 1 345 74 74 LYS CB C 31.169 0.2 1 346 74 74 LYS N N 116.425 0.2 1 347 75 75 ASP H H 7.995 0.02 1 348 75 75 ASP C C 176.708 0.2 1 349 75 75 ASP CA C 54.732 0.2 1 350 75 75 ASP CB C 41.359 0.2 1 351 75 75 ASP N N 117.736 0.2 1 352 76 76 PHE H H 7.495 0.02 1 353 76 76 PHE C C 178.624 0.2 1 354 76 76 PHE CA C 58.860 0.2 1 355 76 76 PHE CB C 43.732 0.2 1 356 76 76 PHE N N 114.978 0.2 1 357 77 77 LEU H H 7.438 0.02 1 358 77 77 LEU CA C 50.977 0.2 1 359 77 77 LEU CB C 46.170 0.2 1 360 77 77 LEU N N 118.051 0.2 1 361 78 78 PRO C C 174.470 0.2 1 362 78 78 PRO CA C 62.273 0.2 1 363 78 78 PRO CB C 32.230 0.2 1 364 79 79 LYS H H 8.515 0.02 1 365 79 79 LYS C C 173.603 0.2 1 366 79 79 LYS CA C 59.918 0.2 1 367 79 79 LYS CB C 32.230 0.2 1 368 79 79 LYS N N 122.676 0.2 1 369 80 80 GLU H H 9.223 0.02 1 370 80 80 GLU C C 174.702 0.2 1 371 80 80 GLU CA C 58.640 0.2 1 372 80 80 GLU CB C 28.620 0.2 1 373 80 80 GLU N N 117.622 0.2 1 374 81 81 TYR H H 7.955 0.02 1 375 81 81 TYR C C 175.554 0.2 1 376 81 81 TYR CA C 55.240 0.2 1 377 81 81 TYR CB C 40.045 0.2 1 378 81 81 TYR N N 115.789 0.2 1 379 82 82 VAL H H 7.248 0.02 1 380 82 82 VAL C C 175.783 0.2 1 381 82 82 VAL CA C 66.366 0.2 1 382 82 82 VAL CB C 31.607 0.2 1 383 82 82 VAL N N 119.759 0.2 1 384 83 83 LYS H H 8.131 0.02 1 385 83 83 LYS C C 175.736 0.2 1 386 83 83 LYS CA C 56.054 0.2 1 387 83 83 LYS CB C 31.900 0.2 1 388 83 83 LYS N N 118.308 0.2 1 389 84 84 GLN H H 7.497 0.02 1 390 84 84 GLN C C 176.201 0.2 1 391 84 84 GLN CA C 56.202 0.2 1 392 84 84 GLN CB C 28.803 0.2 1 393 84 84 GLN N N 118.305 0.2 1 394 85 85 LYS H H 8.350 0.02 1 395 85 85 LYS C C 174.247 0.2 1 396 85 85 LYS CA C 56.816 0.2 1 397 85 85 LYS CB C 29.551 0.2 1 398 85 85 LYS N N 118.029 0.2 1 399 86 86 GLY H H 8.389 0.02 1 400 86 86 GLY C C 177.786 0.2 1 401 86 86 GLY CA C 46.319 0.2 1 402 86 86 GLY N N 106.417 0.2 1 403 87 87 GLU H H 8.812 0.02 1 404 87 87 GLU C C 175.125 0.2 1 405 87 87 GLU CA C 61.579 0.2 1 406 87 87 GLU CB C 29.727 0.2 1 407 87 87 GLU N N 121.262 0.2 1 408 88 88 ARG H H 8.433 0.02 1 409 88 88 ARG C C 172.713 0.2 1 410 88 88 ARG CA C 59.733 0.2 1 411 88 88 ARG CB C 29.536 0.2 1 412 88 88 ARG N N 116.328 0.2 1 413 89 89 LYS H H 7.479 0.02 1 414 89 89 LYS C C 171.880 0.2 1 415 89 89 LYS CA C 59.197 0.2 1 416 89 89 LYS CB C 32.480 0.2 1 417 89 89 LYS N N 119.285 0.2 1 418 90 90 ILE H H 8.043 0.02 1 419 90 90 ILE C C 174.047 0.2 1 420 90 90 ILE CA C 65.633 0.2 1 421 90 90 ILE CB C 37.791 0.2 1 422 90 90 ILE N N 122.309 0.2 1 423 91 91 PHE H H 8.436 0.02 1 424 91 91 PHE C C 173.572 0.2 1 425 91 91 PHE CA C 58.690 0.2 1 426 91 91 PHE CB C 37.351 0.2 1 427 91 91 PHE N N 117.944 0.2 1 428 92 92 GLN H H 7.971 0.02 1 429 92 92 GLN C C 174.468 0.2 1 430 92 92 GLN CA C 58.847 0.2 1 431 92 92 GLN CB C 28.387 0.2 1 432 92 92 GLN N N 120.114 0.2 1 433 93 93 ALA H H 7.456 0.02 1 434 93 93 ALA C C 172.446 0.2 1 435 93 93 ALA CA C 55.049 0.2 1 436 93 93 ALA CB C 18.234 0.2 1 437 93 93 ALA N N 122.629 0.2 1 438 94 94 HIS H H 8.905 0.02 1 439 94 94 HIS C C 172.166 0.2 1 440 94 94 HIS CA C 57.300 0.2 1 441 94 94 HIS CB C 33.991 0.2 1 442 94 94 HIS N N 119.871 0.2 1 443 95 95 LYS H H 8.547 0.02 1 444 95 95 LYS C C 172.537 0.2 1 445 95 95 LYS CA C 60.083 0.2 1 446 95 95 LYS CB C 32.057 0.2 1 447 95 95 LYS N N 122.085 0.2 1 448 96 96 ASN H H 8.012 0.02 1 449 96 96 ASN C C 175.153 0.2 1 450 96 96 ASN CA C 54.650 0.2 1 451 96 96 ASN CB C 37.711 0.2 1 452 96 96 ASN N N 117.875 0.2 1 453 97 97 CYS H H 7.656 0.02 1 454 97 97 CYS C C 175.783 0.2 1 455 97 97 CYS CA C 62.386 0.2 1 456 97 97 CYS CB C 26.936 0.2 1 457 97 97 CYS N N 116.836 0.2 1 458 98 98 GLY H H 7.871 0.02 1 459 98 98 GLY C C 176.669 0.2 1 460 98 98 GLY CA C 47.221 0.2 1 461 98 98 GLY N N 108.704 0.2 1 462 99 99 GLN H H 8.936 0.02 1 463 99 99 GLN C C 177.088 0.2 1 464 99 99 GLN CA C 54.330 0.2 1 465 99 99 GLN CB C 27.796 0.2 1 466 99 99 GLN N N 124.835 0.2 1 467 100 100 MET H H 7.358 0.02 1 468 100 100 MET C C 176.211 0.2 1 469 100 100 MET CA C 57.319 0.2 1 470 100 100 MET CB C 35.098 0.2 1 471 100 100 MET N N 121.224 0.2 1 472 101 101 SER H H 8.996 0.02 1 473 101 101 SER C C 178.585 0.2 1 474 101 101 SER CA C 58.030 0.2 1 475 101 101 SER CB C 65.364 0.2 1 476 101 101 SER N N 122.223 0.2 1 477 102 102 GLU H H 8.846 0.02 1 478 102 102 GLU C C 174.082 0.2 1 479 102 102 GLU CA C 60.024 0.2 1 480 102 102 GLU CB C 29.501 0.2 1 481 102 102 GLU N N 121.266 0.2 1 482 103 103 ILE H H 7.576 0.02 1 483 103 103 ILE C C 175.161 0.2 1 484 103 103 ILE CA C 63.999 0.2 1 485 103 103 ILE CB C 37.542 0.2 1 486 103 103 ILE N N 116.222 0.2 1 487 104 104 GLU H H 7.563 0.02 1 488 104 104 GLU C C 173.802 0.2 1 489 104 104 GLU CA C 59.180 0.2 1 490 104 104 GLU CB C 28.643 0.2 1 491 104 104 GLU N N 120.469 0.2 1 492 105 105 ALA H H 8.247 0.02 1 493 105 105 ALA C C 172.979 0.2 1 494 105 105 ALA CA C 55.605 0.2 1 495 105 105 ALA CB C 18.428 0.2 1 496 105 105 ALA N N 120.885 0.2 1 497 106 106 LYS H H 7.823 0.02 1 498 106 106 LYS C C 173.610 0.2 1 499 106 106 LYS CA C 60.796 0.2 1 500 106 106 LYS CB C 33.449 0.2 1 501 106 106 LYS N N 118.340 0.2 1 502 107 107 VAL H H 8.195 0.02 1 503 107 107 VAL C C 173.720 0.2 1 504 107 107 VAL CA C 67.211 0.2 1 505 107 107 VAL CB C 31.315 0.2 1 506 107 107 VAL N N 119.138 0.2 1 507 108 108 ARG H H 8.313 0.02 1 508 108 108 ARG C C 173.319 0.2 1 509 108 108 ARG CA C 59.191 0.2 1 510 108 108 ARG CB C 28.942 0.2 1 511 108 108 ARG N N 117.629 0.2 1 512 109 109 TYR H H 8.273 0.02 1 513 109 109 TYR C C 173.806 0.2 1 514 109 109 TYR CA C 62.328 0.2 1 515 109 109 TYR CB C 39.774 0.2 1 516 109 109 TYR N N 122.752 0.2 1 517 110 110 VAL H H 8.469 0.02 1 518 110 110 VAL C C 173.582 0.2 1 519 110 110 VAL CA C 67.470 0.2 1 520 110 110 VAL CB C 31.766 0.2 1 521 110 110 VAL N N 117.956 0.2 1 522 111 111 LYS H H 8.808 0.02 1 523 111 111 LYS C C 172.288 0.2 1 524 111 111 LYS CA C 60.595 0.2 1 525 111 111 LYS CB C 32.554 0.2 1 526 111 111 LYS N N 119.087 0.2 1 527 112 112 LEU H H 8.291 0.02 1 528 112 112 LEU C C 172.204 0.2 1 529 112 112 LEU CA C 57.630 0.2 1 530 112 112 LEU CB C 40.460 0.2 1 531 112 112 LEU N N 122.202 0.2 1 532 113 113 ALA H H 8.688 0.02 1 533 113 113 ALA C C 172.066 0.2 1 534 113 113 ALA CA C 56.578 0.2 1 535 113 113 ALA CB C 17.747 0.2 1 536 113 113 ALA N N 122.525 0.2 1 537 114 114 ARG H H 8.383 0.02 1 538 114 114 ARG C C 173.189 0.2 1 539 114 114 ARG CA C 58.763 0.2 1 540 114 114 ARG CB C 30.027 0.2 1 541 114 114 ARG N N 116.146 0.2 1 542 115 115 SER H H 8.006 0.02 1 543 115 115 SER C C 176.854 0.2 1 544 115 115 SER CA C 60.720 0.2 1 545 115 115 SER CB C 63.368 0.2 1 546 115 115 SER N N 115.029 0.2 1 547 116 116 LEU H H 7.514 0.02 1 548 116 116 LEU C C 174.247 0.2 1 549 116 116 LEU CA C 55.427 0.2 1 550 116 116 LEU CB C 42.049 0.2 1 551 116 116 LEU N N 121.598 0.2 1 552 117 117 LYS H H 7.716 0.02 1 553 117 117 LYS C C 175.598 0.2 1 554 117 117 LYS CA C 56.597 0.2 1 555 117 117 LYS CB C 32.884 0.2 1 556 117 117 LYS N N 120.994 0.2 1 557 118 118 THR H H 7.853 0.02 1 558 118 118 THR C C 177.970 0.2 1 559 118 118 THR CA C 62.249 0.2 1 560 118 118 THR CB C 69.777 0.2 1 561 118 118 THR N N 114.165 0.2 1 562 119 119 TYR H H 8.099 0.02 1 563 119 119 TYR C C 176.880 0.2 1 564 119 119 TYR CA C 57.926 0.2 1 565 119 119 TYR CB C 39.044 0.2 1 566 119 119 TYR N N 121.973 0.2 1 567 120 120 GLY H H 7.794 0.02 1 568 120 120 GLY CA C 46.134 0.2 1 569 120 120 GLY N N 116.433 0.2 1 stop_ save_