data_16932 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shift assignments of the Talin F2F3 domain (residues 196-405) ; _BMRB_accession_number 16932 _BMRB_flat_file_name bmr16932.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" 198 "13C chemical shifts" 207 "15N chemical shifts" 198 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 F2F3 FERM 'Focal adhesion' phospholipid talin stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name F2F3 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label F2F3 $F2F3 stop_ _System_molecular_weight 24891 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_F2F3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common F2F3 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 216 _Mol_residue_sequence ; GIDPFTKFFYSDQNVDSRDP VQLNLLYVQARDDILNGSHP VSFDKACEFAGFQCQIQFGP HNEQKHKAGFLDLKDFLPKE YVKQKGERKIFQAHKNCGQM SEIEAKVRYVKLARSLKTYG VSFFLVKEKMKGKNKLVPRL LGITKECVMRVDEKTKEVIQ EWSLTNIKRWAASPKSFTLD FGDYQDGYYSVQTTEGEQIA QLIAGYIDIILKKKKS ; 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 121 VAL 122 SER 123 PHE 124 PHE 125 LEU 126 VAL 127 LYS 128 GLU 129 LYS 130 MET 131 LYS 132 GLY 133 LYS 134 ASN 135 LYS 136 LEU 137 VAL 138 PRO 139 ARG 140 LEU 141 LEU 142 GLY 143 ILE 144 THR 145 LYS 146 GLU 147 CYS 148 VAL 149 MET 150 ARG 151 VAL 152 ASP 153 GLU 154 LYS 155 THR 156 LYS 157 GLU 158 VAL 159 ILE 160 GLN 161 GLU 162 TRP 163 SER 164 LEU 165 THR 166 ASN 167 ILE 168 LYS 169 ARG 170 TRP 171 ALA 172 ALA 173 SER 174 PRO 175 LYS 176 SER 177 PHE 178 THR 179 LEU 180 ASP 181 PHE 182 GLY 183 ASP 184 TYR 185 GLN 186 ASP 187 GLY 188 TYR 189 TYR 190 SER 191 VAL 192 GLN 193 THR 194 THR 195 GLU 196 GLY 197 GLU 198 GLN 199 ILE 200 ALA 201 GLN 202 LEU 203 ILE 204 ALA 205 GLY 206 TYR 207 ILE 208 ASP 209 ILE 210 ILE 211 LEU 212 LYS 213 LYS 214 LYS 215 LYS 216 SER 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 BMRB 15792 talin-F2F3 93.06 201 100.00 100.00 3.92e-145 BMRB 16930 F2 55.56 120 100.00 100.00 2.59e-82 BMRB 16959 F1F2 50.00 194 100.00 100.00 2.29e-72 PDB 1MIX "Crystal Structure Of A Ferm Domain Of Talin" 94.91 206 97.07 98.54 2.11e-145 PDB 1MIZ "Crystal Structure Of An Integrin Beta3-Talin Chimera" 93.06 201 97.01 98.51 3.41e-142 PDB 1Y19 "Structural Basis For Phosphatidylinositol Phosphate Kinase Type I-Gamma Binding To Talin At Focal Adhesions" 91.20 202 100.00 100.00 1.55e-141 PDB 3IVF "Crystal Structure Of The Talin Head Ferm Domain" 94.91 371 100.00 100.00 1.38e-147 DBJ BAA82979 "KIAA1027 protein [Homo sapiens]" 97.22 2550 99.52 100.00 1.39e-139 DBJ BAC30516 "unnamed protein product [Mus musculus]" 94.44 300 100.00 100.00 2.03e-148 DBJ BAC65702 "mKIAA1027 protein [Mus musculus]" 97.22 2564 100.00 100.00 6.84e-140 DBJ BAE27781 "unnamed protein product [Mus musculus]" 97.22 2541 100.00 100.00 6.57e-140 DBJ BAG09941 "talin-1 [synthetic construct]" 97.22 2541 99.52 100.00 1.37e-139 EMBL CAA39588 "talin [Mus musculus]" 97.22 2541 100.00 100.00 4.53e-140 GB AAD13152 "talin [Homo sapiens]" 97.22 2541 99.52 100.00 1.37e-139 GB AAF23322 "talin [Homo sapiens]" 97.22 2541 99.52 100.00 1.37e-139 GB AAF27330 "talin [Homo sapiens]" 97.22 2540 99.52 100.00 1.55e-139 GB AAH42923 "Talin 1 [Homo sapiens]" 97.22 2541 99.52 100.00 1.37e-139 GB AAI22767 "TLN1 protein [Bos taurus]" 96.76 407 99.52 100.00 1.25e-149 PRF 1617167A talin 97.22 2541 100.00 100.00 4.53e-140 REF NP_001034114 "talin-1 [Rattus norvegicus]" 97.22 2541 100.00 100.00 4.53e-140 REF NP_001192357 "talin-1 [Bos taurus]" 97.22 2541 99.52 100.00 1.22e-139 REF NP_006280 "talin-1 [Homo sapiens]" 97.22 2541 99.52 100.00 1.37e-139 REF NP_035732 "talin-1 [Mus musculus]" 97.22 2541 100.00 100.00 6.57e-140 REF NP_989854 "talin-1 [Gallus gallus]" 97.22 2541 97.14 98.57 5.44e-135 SP P26039 "RecName: Full=Talin-1" 97.22 2541 100.00 100.00 6.57e-140 SP P54939 "RecName: Full=Talin-1" 97.22 2541 97.14 98.57 5.44e-135 SP Q9Y490 "RecName: Full=Talin-1" 97.22 2541 99.52 100.00 1.37e-139 TPG DAA26829 "TPA: talin 1 [Bos taurus]" 97.22 2541 99.52 100.00 1.37e-139 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $F2F3 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 $F2F3 '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 $F2F3 0.5 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 800 _Details 'with cryoprobe' 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 F2F3 _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 CA C 60.739 0.2 1 2 3 3 ASP CA C 51.907 0.2 1 3 4 4 PRO CA C 63.739 0.2 1 4 5 5 PHE CA C 58.551 0.2 1 5 6 6 THR H H 7.704 0.02 1 6 6 6 THR CA C 62.917 0.2 1 7 6 6 THR N N 114.113 0.2 1 8 7 7 LYS H H 7.936 0.02 1 9 7 7 LYS CA C 56.930 0.2 1 10 7 7 LYS N N 122.290 0.2 1 11 8 8 PHE CA C 58.016 0.2 1 12 9 9 PHE H H 7.835 0.02 1 13 9 9 PHE CA C 57.911 0.2 1 14 9 9 PHE N N 121.052 0.2 1 15 10 10 TYR H H 7.801 0.02 1 16 10 10 TYR CA C 58.037 0.2 1 17 10 10 TYR N N 120.555 0.2 1 18 11 11 SER H H 7.922 0.02 1 19 11 11 SER CA C 58.307 0.2 1 20 11 11 SER N N 116.951 0.2 1 21 12 12 ASP H H 8.283 0.02 1 22 12 12 ASP CA C 54.349 0.2 1 23 12 12 ASP N N 122.166 0.2 1 24 13 13 GLN H H 8.097 0.02 1 25 13 13 GLN CA C 56.062 0.2 1 26 13 13 GLN N N 118.983 0.2 1 27 14 14 ASN H H 8.344 0.02 1 28 14 14 ASN CA C 53.431 0.2 1 29 14 14 ASN N N 119.158 0.2 1 30 15 15 VAL H H 8.022 0.02 1 31 15 15 VAL CA C 62.404 0.2 1 32 15 15 VAL N N 120.964 0.2 1 33 16 16 ASP H H 8.369 0.02 1 34 16 16 ASP CA C 53.930 0.2 1 35 16 16 ASP N N 124.193 0.2 1 36 17 17 SER H H 8.255 0.02 1 37 17 17 SER CA C 58.777 0.2 1 38 17 17 SER N N 116.197 0.2 1 39 18 18 ARG H H 8.149 0.02 1 40 18 18 ARG CA C 57.164 0.2 1 41 18 18 ARG N N 120.424 0.2 1 42 19 19 ASP H H 7.798 0.02 1 43 19 19 ASP CA C 50.626 0.2 1 44 19 19 ASP N N 118.491 0.2 1 45 20 20 PRO CA C 64.897 0.2 1 46 21 21 VAL H H 7.867 0.02 1 47 21 21 VAL CA C 66.102 0.2 1 48 21 21 VAL N N 120.841 0.2 1 49 22 22 GLN H H 7.535 0.02 1 50 22 22 GLN CA C 58.158 0.2 1 51 22 22 GLN N N 120.740 0.2 1 52 23 23 LEU H H 8.279 0.02 1 53 23 23 LEU CA C 57.858 0.2 1 54 23 23 LEU N N 119.224 0.2 1 55 24 24 ASN H H 7.767 0.02 1 56 24 24 ASN CA C 57.806 0.2 1 57 24 24 ASN N N 115.268 0.2 1 58 25 25 LEU H H 7.479 0.02 1 59 25 25 LEU CA C 58.272 0.2 1 60 25 25 LEU N N 118.003 0.2 1 61 26 26 LEU H H 7.920 0.02 1 62 26 26 LEU CA C 57.511 0.2 1 63 26 26 LEU N N 118.936 0.2 1 64 27 27 TYR H H 8.472 0.02 1 65 27 27 TYR CA C 60.693 0.2 1 66 27 27 TYR N N 120.742 0.2 1 67 28 28 VAL H H 8.395 0.02 1 68 28 28 VAL CA C 66.833 0.2 1 69 28 28 VAL N N 118.026 0.2 1 70 29 29 GLN H H 7.319 0.02 1 71 29 29 GLN CA C 58.635 0.2 1 72 29 29 GLN N N 115.868 0.2 1 73 30 30 ALA H H 7.681 0.02 1 74 30 30 ALA CA C 55.018 0.2 1 75 30 30 ALA N N 120.127 0.2 1 76 31 31 ARG H H 8.628 0.02 1 77 31 31 ARG CA C 56.877 0.2 1 78 31 31 ARG N N 119.339 0.2 1 79 32 32 ASP H H 8.708 0.02 1 80 32 32 ASP CA C 57.633 0.2 1 81 32 32 ASP N N 120.220 0.2 1 82 33 33 ASP H H 7.742 0.02 1 83 33 33 ASP CA C 56.927 0.2 1 84 33 33 ASP N N 119.570 0.2 1 85 34 34 ILE H H 7.558 0.02 1 86 34 34 ILE CA C 64.618 0.2 1 87 34 34 ILE N N 124.429 0.2 1 88 35 35 LEU H H 9.080 0.02 1 89 35 35 LEU CA C 58.123 0.2 1 90 35 35 LEU N N 120.353 0.2 1 91 36 36 ASN H H 8.668 0.02 1 92 36 36 ASN CA C 53.055 0.2 1 93 36 36 ASN N N 114.159 0.2 1 94 37 37 GLY H H 7.448 0.02 1 95 37 37 GLY CA C 45.439 0.2 1 96 37 37 GLY N N 107.394 0.2 1 97 38 38 SER H H 8.386 0.02 1 98 38 38 SER CA C 61.091 0.2 1 99 38 38 SER N N 117.969 0.2 1 100 39 39 HIS H H 7.563 0.02 1 101 39 39 HIS CA C 50.319 0.2 1 102 39 39 HIS N N 120.299 0.2 1 103 42 42 SER CA C 57.781 0.2 1 104 43 43 PHE H H 9.155 0.02 1 105 43 43 PHE CA C 60.121 0.2 1 106 43 43 PHE N N 123.549 0.2 1 107 44 44 ASP H H 8.403 0.02 1 108 44 44 ASP CA C 57.624 0.2 1 109 44 44 ASP N N 117.096 0.2 1 110 45 45 LYS H H 7.585 0.02 1 111 45 45 LYS CA C 57.570 0.2 1 112 45 45 LYS N N 119.375 0.2 1 113 46 46 ALA H H 9.157 0.02 1 114 46 46 ALA CA C 56.043 0.2 1 115 46 46 ALA N N 121.415 0.2 1 116 47 47 CYS H H 7.664 0.02 1 117 47 47 CYS CA C 63.916 0.2 1 118 47 47 CYS N N 115.500 0.2 1 119 48 48 GLU H H 7.192 0.02 1 120 48 48 GLU CA C 59.855 0.2 1 121 48 48 GLU N N 121.538 0.2 1 122 49 49 PHE H H 8.638 0.02 1 123 49 49 PHE CA C 63.735 0.2 1 124 49 49 PHE N N 118.812 0.2 1 125 50 50 ALA H H 8.183 0.02 1 126 50 50 ALA CA C 54.540 0.2 1 127 50 50 ALA N N 119.841 0.2 1 128 51 51 GLY H H 8.095 0.02 1 129 51 51 GLY CA C 48.025 0.2 1 130 51 51 GLY N N 107.155 0.2 1 131 52 52 PHE H H 7.284 0.02 1 132 52 52 PHE CA C 60.456 0.2 1 133 52 52 PHE N N 119.418 0.2 1 134 53 53 GLN H H 9.109 0.02 1 135 53 53 GLN CA C 59.737 0.2 1 136 53 53 GLN N N 121.818 0.2 1 137 54 54 CYS H H 8.816 0.02 1 138 54 54 CYS CA C 64.480 0.2 1 139 54 54 CYS N N 117.822 0.2 1 140 55 55 GLN H H 7.623 0.02 1 141 55 55 GLN CA C 58.707 0.2 1 142 55 55 GLN N N 123.109 0.2 1 143 56 56 ILE H H 8.281 0.02 1 144 56 56 ILE CA C 65.421 0.2 1 145 56 56 ILE N N 119.397 0.2 1 146 57 57 GLN H H 8.248 0.02 1 147 57 57 GLN CA C 58.777 0.2 1 148 57 57 GLN N N 115.784 0.2 1 149 58 58 PHE H H 8.921 0.02 1 150 58 58 PHE CA C 56.472 0.2 1 151 58 58 PHE N N 114.968 0.2 1 152 59 59 GLY H H 7.649 0.02 1 153 59 59 GLY CA C 44.374 0.2 1 154 59 59 GLY N N 111.231 0.2 1 155 60 60 PRO CA C 62.613 0.2 1 156 61 61 HIS H H 8.894 0.02 1 157 61 61 HIS CA C 58.361 0.2 1 158 61 61 HIS N N 124.240 0.2 1 159 62 62 ASN H H 10.037 0.02 1 160 62 62 ASN CA C 51.229 0.2 1 161 62 62 ASN N N 130.734 0.2 1 162 63 63 GLU H H 9.061 0.02 1 163 63 63 GLU CA C 58.588 0.2 1 164 63 63 GLU N N 125.373 0.2 1 165 64 64 GLN H H 7.558 0.02 1 166 64 64 GLN CA C 57.201 0.2 1 167 64 64 GLN N N 114.509 0.2 1 168 65 65 LYS H H 6.795 0.02 1 169 65 65 LYS CA C 56.027 0.2 1 170 65 65 LYS N N 116.247 0.2 1 171 66 66 HIS H H 7.764 0.02 1 172 66 66 HIS CA C 53.936 0.2 1 173 66 66 HIS N N 122.177 0.2 1 174 67 67 LYS H H 6.585 0.02 1 175 67 67 LYS CA C 53.901 0.2 1 176 67 67 LYS N N 118.115 0.2 1 177 68 68 ALA H H 8.380 0.02 1 178 68 68 ALA CA C 54.081 0.2 1 179 68 68 ALA N N 121.948 0.2 1 180 69 69 GLY H H 10.043 0.02 1 181 69 69 GLY CA C 45.066 0.2 1 182 69 69 GLY N N 114.307 0.2 1 183 70 70 PHE H H 8.558 0.02 1 184 70 70 PHE CA C 59.991 0.2 1 185 70 70 PHE N N 121.571 0.2 1 186 71 71 LEU H H 7.939 0.02 1 187 71 71 LEU CA C 53.693 0.2 1 188 71 71 LEU N N 115.677 0.2 1 189 72 72 ASP H H 8.708 0.02 1 190 72 72 ASP CA C 52.751 0.2 1 191 72 72 ASP N N 123.276 0.2 1 192 73 73 LEU H H 8.548 0.02 1 193 73 73 LEU CA C 58.645 0.2 1 194 73 73 LEU N N 124.760 0.2 1 195 74 74 LYS H H 8.305 0.02 1 196 74 74 LYS CA C 58.204 0.2 1 197 74 74 LYS N N 116.368 0.2 1 198 75 75 ASP H H 7.973 0.02 1 199 75 75 ASP CA C 54.814 0.2 1 200 75 75 ASP N N 117.541 0.2 1 201 76 76 PHE H H 7.467 0.02 1 202 76 76 PHE CA C 58.791 0.2 1 203 76 76 PHE N N 114.866 0.2 1 204 77 77 LEU H H 7.436 0.02 1 205 77 77 LEU CA C 50.904 0.2 1 206 77 77 LEU N N 117.999 0.2 1 207 78 78 PRO CA C 62.299 0.2 1 208 79 79 LYS H H 8.506 0.02 1 209 79 79 LYS CA C 59.767 0.2 1 210 79 79 LYS N N 123.157 0.2 1 211 80 80 GLU H H 9.076 0.02 1 212 80 80 GLU CA C 58.078 0.2 1 213 80 80 GLU N N 116.617 0.2 1 214 81 81 TYR H H 7.980 0.02 1 215 81 81 TYR CA C 55.294 0.2 1 216 81 81 TYR N N 117.575 0.2 1 217 82 82 VAL H H 7.278 0.02 1 218 82 82 VAL CA C 66.515 0.2 1 219 82 82 VAL N N 119.663 0.2 1 220 83 83 LYS H H 8.196 0.02 1 221 83 83 LYS CA C 55.974 0.2 1 222 83 83 LYS N N 118.127 0.2 1 223 84 84 GLN H H 7.458 0.02 1 224 84 84 GLN CA C 56.109 0.2 1 225 84 84 GLN N N 118.652 0.2 1 226 85 85 LYS H H 8.339 0.02 1 227 85 85 LYS CA C 56.715 0.2 1 228 85 85 LYS N N 117.952 0.2 1 229 86 86 GLY H H 8.397 0.02 1 230 86 86 GLY CA C 46.195 0.2 1 231 86 86 GLY N N 106.498 0.2 1 232 87 87 GLU H H 8.871 0.02 1 233 87 87 GLU CA C 61.624 0.2 1 234 87 87 GLU N N 121.152 0.2 1 235 88 88 ARG H H 8.439 0.02 1 236 88 88 ARG CA C 59.753 0.2 1 237 88 88 ARG N N 116.332 0.2 1 238 89 89 LYS H H 7.477 0.02 1 239 89 89 LYS CA C 59.192 0.2 1 240 89 89 LYS N N 119.463 0.2 1 241 90 90 ILE H H 8.033 0.02 1 242 90 90 ILE CA C 65.578 0.2 1 243 90 90 ILE N N 122.281 0.2 1 244 91 91 PHE H H 8.427 0.02 1 245 91 91 PHE CA C 58.732 0.2 1 246 91 91 PHE N N 117.934 0.2 1 247 92 92 GLN H H 7.967 0.02 1 248 92 92 GLN CA C 58.801 0.2 1 249 92 92 GLN N N 120.164 0.2 1 250 93 93 ALA H H 7.448 0.02 1 251 93 93 ALA CA C 55.026 0.2 1 252 93 93 ALA N N 122.562 0.2 1 253 94 94 HIS H H 8.883 0.02 1 254 94 94 HIS CA C 57.233 0.2 1 255 94 94 HIS N N 119.906 0.2 1 256 95 95 LYS H H 8.543 0.02 1 257 95 95 LYS CA C 60.054 0.2 1 258 95 95 LYS N N 122.138 0.2 1 259 96 96 ASN H H 8.005 0.02 1 260 96 96 ASN CA C 54.636 0.2 1 261 96 96 ASN N N 117.731 0.2 1 262 97 97 CYS H H 7.651 0.02 1 263 97 97 CYS CA C 62.310 0.2 1 264 97 97 CYS N N 116.842 0.2 1 265 98 98 GLY H H 7.855 0.02 1 266 98 98 GLY CA C 47.172 0.2 1 267 98 98 GLY N N 108.686 0.2 1 268 99 99 GLN H H 8.932 0.02 1 269 99 99 GLN CA C 54.211 0.2 1 270 99 99 GLN N N 124.724 0.2 1 271 100 100 MET H H 7.337 0.02 1 272 100 100 MET CA C 57.219 0.2 1 273 100 100 MET N N 121.164 0.2 1 274 101 101 SER H H 8.975 0.02 1 275 101 101 SER CA C 57.880 0.2 1 276 101 101 SER N N 122.023 0.2 1 277 102 102 GLU H H 8.848 0.02 1 278 102 102 GLU CA C 60.013 0.2 1 279 102 102 GLU N N 121.184 0.2 1 280 103 103 ILE H H 7.578 0.02 1 281 103 103 ILE CA C 63.977 0.2 1 282 103 103 ILE N N 116.273 0.2 1 283 104 104 GLU H H 7.540 0.02 1 284 104 104 GLU CA C 59.065 0.2 1 285 104 104 GLU N N 120.465 0.2 1 286 105 105 ALA H H 8.251 0.02 1 287 105 105 ALA CA C 55.527 0.2 1 288 105 105 ALA N N 120.847 0.2 1 289 106 106 LYS H H 7.779 0.02 1 290 106 106 LYS CA C 60.693 0.2 1 291 106 106 LYS N N 118.548 0.2 1 292 107 107 VAL H H 8.106 0.02 1 293 107 107 VAL CA C 67.050 0.2 1 294 107 107 VAL N N 119.103 0.2 1 295 108 108 ARG H H 8.327 0.02 1 296 108 108 ARG CA C 58.952 0.2 1 297 108 108 ARG N N 117.392 0.2 1 298 109 109 TYR H H 8.281 0.02 1 299 109 109 TYR CA C 62.250 0.2 1 300 109 109 TYR N N 122.973 0.2 1 301 110 110 VAL H H 8.278 0.02 1 302 110 110 VAL CA C 67.490 0.2 1 303 110 110 VAL N N 117.868 0.2 1 304 111 111 LYS H H 8.753 0.02 1 305 111 111 LYS CA C 60.325 0.2 1 306 111 111 LYS N N 118.160 0.2 1 307 112 112 LEU H H 8.264 0.02 1 308 112 112 LEU N N 122.068 0.2 1 309 113 113 ALA H H 8.215 0.02 1 310 113 113 ALA CA C 57.665 0.2 1 311 113 113 ALA N N 120.936 0.2 1 312 114 114 ARG H H 7.676 0.02 1 313 114 114 ARG CA C 56.939 0.2 1 314 114 114 ARG N N 118.937 0.2 1 315 118 118 THR H H 7.563 0.02 1 316 118 118 THR N N 115.766 0.2 1 317 120 120 GLY H H 8.369 0.02 1 318 120 120 GLY CA C 45.450 0.2 1 319 120 120 GLY N N 117.897 0.2 1 320 121 121 VAL H H 6.958 0.02 1 321 121 121 VAL CA C 61.565 0.2 1 322 121 121 VAL N N 121.361 0.2 1 323 122 122 SER H H 7.471 0.02 1 324 122 122 SER CA C 58.408 0.2 1 325 122 122 SER N N 122.083 0.2 1 326 123 123 PHE H H 8.610 0.02 1 327 123 123 PHE CA C 58.612 0.2 1 328 123 123 PHE N N 123.141 0.2 1 329 124 124 PHE H H 9.153 0.02 1 330 124 124 PHE CA C 56.764 0.2 1 331 124 124 PHE N N 119.188 0.2 1 332 125 125 LEU H H 9.381 0.02 1 333 125 125 LEU CA C 55.134 0.2 1 334 125 125 LEU N N 126.994 0.2 1 335 126 126 VAL H H 9.264 0.02 1 336 126 126 VAL CA C 58.811 0.2 1 337 126 126 VAL N N 123.401 0.2 1 338 127 127 LYS H H 8.339 0.02 1 339 127 127 LYS CA C 55.079 0.2 1 340 127 127 LYS N N 116.399 0.2 1 341 128 128 GLU H H 9.190 0.02 1 342 128 128 GLU CA C 54.404 0.2 1 343 128 128 GLU N N 123.421 0.2 1 344 129 129 LYS H H 8.797 0.02 1 345 129 129 LYS CA C 55.928 0.2 1 346 129 129 LYS N N 124.052 0.2 1 347 130 130 MET H H 8.878 0.02 1 348 130 130 MET CA C 54.909 0.2 1 349 130 130 MET N N 126.898 0.2 1 350 131 131 LYS H H 8.579 0.02 1 351 131 131 LYS CA C 58.048 0.2 1 352 131 131 LYS N N 124.911 0.2 1 353 132 132 GLY H H 8.879 0.02 1 354 132 132 GLY CA C 45.474 0.2 1 355 132 132 GLY N N 112.995 0.2 1 356 133 133 LYS H H 7.681 0.02 1 357 133 133 LYS CA C 54.690 0.2 1 358 133 133 LYS N N 118.491 0.2 1 359 134 134 ASN CA C 53.271 0.2 1 360 135 135 LYS H H 7.419 0.02 1 361 135 135 LYS CA C 55.550 0.2 1 362 135 135 LYS N N 119.351 0.2 1 363 136 136 LEU H H 8.437 0.02 1 364 136 136 LEU CA C 54.083 0.2 1 365 136 136 LEU N N 124.065 0.2 1 366 137 137 VAL H H 9.231 0.02 1 367 137 137 VAL CA C 58.588 0.2 1 368 137 137 VAL N N 122.179 0.2 1 369 138 138 PRO CA C 62.379 0.2 1 370 139 139 ARG H H 9.180 0.02 1 371 139 139 ARG CA C 54.092 0.2 1 372 139 139 ARG N N 122.566 0.2 1 373 140 140 LEU CA C 54.116 0.2 1 374 141 141 LEU H H 9.718 0.02 1 375 141 141 LEU CA C 53.404 0.2 1 376 141 141 LEU N N 127.791 0.2 1 377 142 142 GLY H H 9.720 0.02 1 378 142 142 GLY CA C 44.975 0.2 1 379 142 142 GLY N N 114.235 0.2 1 380 143 143 ILE H H 8.670 0.02 1 381 143 143 ILE CA C 60.179 0.2 1 382 143 143 ILE N N 123.429 0.2 1 383 144 144 THR H H 8.974 0.02 1 384 144 144 THR CA C 58.770 0.2 1 385 144 144 THR N N 121.761 0.2 1 386 145 145 LYS H H 7.527 0.02 1 387 145 145 LYS CA C 57.905 0.2 1 388 145 145 LYS N N 112.879 0.2 1 389 146 146 GLU H H 7.876 0.02 1 390 146 146 GLU CA C 56.503 0.2 1 391 146 146 GLU N N 111.714 0.2 1 392 147 147 CYS H H 7.996 0.02 1 393 147 147 CYS CA C 56.708 0.2 1 394 147 147 CYS N N 118.663 0.2 1 395 148 148 VAL H H 8.734 0.02 1 396 148 148 VAL CA C 60.635 0.2 1 397 148 148 VAL N N 118.090 0.2 1 398 149 149 MET H H 9.729 0.02 1 399 149 149 MET CA C 53.687 0.2 1 400 149 149 MET N N 122.232 0.2 1 401 150 150 ARG H H 8.667 0.02 1 402 150 150 ARG CA C 55.253 0.2 1 403 150 150 ARG N N 121.947 0.2 1 404 151 151 VAL H H 9.451 0.02 1 405 151 151 VAL CA C 60.577 0.2 1 406 151 151 VAL N N 126.255 0.2 1 407 152 152 ASP H H 8.645 0.02 1 408 152 152 ASP CA C 55.525 0.2 1 409 152 152 ASP N N 128.211 0.2 1 410 153 153 GLU H H 9.362 0.02 1 411 153 153 GLU CA C 58.840 0.2 1 412 153 153 GLU N N 128.586 0.2 1 413 154 154 LYS H H 8.701 0.02 1 414 154 154 LYS CA C 58.084 0.2 1 415 154 154 LYS N N 119.295 0.2 1 416 155 155 THR H H 8.675 0.02 1 417 155 155 THR CA C 62.360 0.2 1 418 155 155 THR N N 109.550 0.2 1 419 156 156 LYS H H 8.497 0.02 1 420 156 156 LYS CA C 59.682 0.2 1 421 156 156 LYS N N 123.103 0.2 1 422 157 157 GLU H H 7.441 0.02 1 423 157 157 GLU CA C 55.936 0.2 1 424 157 157 GLU N N 116.230 0.2 1 425 158 158 VAL H H 8.762 0.02 1 426 158 158 VAL CA C 63.553 0.2 1 427 158 158 VAL N N 124.199 0.2 1 428 159 159 ILE H H 8.915 0.02 1 429 159 159 ILE CA C 62.576 0.2 1 430 159 159 ILE N N 128.112 0.2 1 431 160 160 GLN H H 7.351 0.02 1 432 160 160 GLN CA C 55.487 0.2 1 433 160 160 GLN N N 118.124 0.2 1 434 161 161 GLU H H 8.086 0.02 1 435 161 161 GLU CA C 54.630 0.2 1 436 161 161 GLU N N 122.956 0.2 1 437 162 162 TRP H H 9.284 0.02 1 438 162 162 TRP HE1 H 9.029 0.02 1 439 162 162 TRP CA C 56.942 0.2 1 440 162 162 TRP N N 122.102 0.2 1 441 162 162 TRP NE1 N 128.841 0.2 1 442 163 163 SER H H 8.741 0.02 1 443 163 163 SER CA C 58.136 0.2 1 444 163 163 SER N N 117.268 0.2 1 445 164 164 LEU H H 8.157 0.02 1 446 164 164 LEU CA C 58.105 0.2 1 447 164 164 LEU N N 126.595 0.2 1 448 165 165 THR H H 7.769 0.02 1 449 165 165 THR CA C 63.710 0.2 1 450 165 165 THR N N 105.589 0.2 1 451 166 166 ASN H H 7.703 0.02 1 452 166 166 ASN CA C 53.406 0.2 1 453 166 166 ASN N N 118.060 0.2 1 454 167 167 ILE H H 7.296 0.02 1 455 167 167 ILE CA C 62.864 0.2 1 456 167 167 ILE N N 119.291 0.2 1 457 168 168 LYS H H 8.933 0.02 1 458 168 168 LYS CA C 56.644 0.2 1 459 168 168 LYS N N 127.965 0.2 1 460 169 169 ARG H H 7.850 0.02 1 461 169 169 ARG CA C 54.980 0.2 1 462 169 169 ARG N N 114.705 0.2 1 463 170 170 TRP H H 7.311 0.02 1 464 170 170 TRP HE1 H 10.189 0.02 1 465 170 170 TRP CA C 55.981 0.2 1 466 170 170 TRP N N 117.622 0.2 1 467 170 170 TRP NE1 N 129.458 0.2 1 468 171 171 ALA H H 8.311 0.02 1 469 171 171 ALA CA C 51.797 0.2 1 470 171 171 ALA N N 120.313 0.2 1 471 172 172 ALA H H 8.930 0.02 1 472 172 172 ALA CA C 50.861 0.2 1 473 172 172 ALA N N 124.538 0.2 1 474 173 173 SER H H 8.914 0.02 1 475 173 173 SER CA C 56.918 0.2 1 476 173 173 SER N N 120.678 0.2 1 477 174 174 PRO CA C 65.407 0.2 1 478 175 175 LYS H H 7.740 0.02 1 479 175 175 LYS CA C 54.919 0.2 1 480 175 175 LYS N N 111.112 0.2 1 481 176 176 SER H H 7.715 0.02 1 482 176 176 SER CA C 57.615 0.2 1 483 176 176 SER N N 114.898 0.2 1 484 177 177 PHE H H 8.600 0.02 1 485 177 177 PHE CA C 58.048 0.2 1 486 177 177 PHE N N 119.482 0.2 1 487 178 178 THR H H 7.897 0.02 1 488 178 178 THR CA C 61.230 0.2 1 489 178 178 THR N N 122.678 0.2 1 490 179 179 LEU H H 8.952 0.02 1 491 179 179 LEU CA C 53.611 0.2 1 492 179 179 LEU N N 124.198 0.2 1 493 180 180 ASP H H 7.883 0.02 1 494 180 180 ASP CA C 52.218 0.2 1 495 180 180 ASP N N 120.236 0.2 1 496 181 181 PHE H H 8.903 0.02 1 497 181 181 PHE CA C 57.347 0.2 1 498 181 181 PHE N N 124.293 0.2 1 499 182 182 GLY H H 9.000 0.02 1 500 182 182 GLY CA C 46.402 0.2 1 501 182 182 GLY N N 110.347 0.2 1 502 183 183 ASP H H 8.408 0.02 1 503 183 183 ASP CA C 54.320 0.2 1 504 183 183 ASP N N 121.797 0.2 1 505 184 184 TYR H H 8.077 0.02 1 506 184 184 TYR CA C 58.917 0.2 1 507 184 184 TYR N N 120.229 0.2 1 508 185 185 GLN H H 8.056 0.02 1 509 185 185 GLN CA C 56.655 0.2 1 510 185 185 GLN N N 118.745 0.2 1 511 186 186 ASP H H 8.244 0.02 1 512 186 186 ASP CA C 54.833 0.2 1 513 186 186 ASP N N 119.724 0.2 1 514 187 187 GLY H H 8.060 0.02 1 515 187 187 GLY CA C 45.831 0.2 1 516 187 187 GLY N N 109.338 0.2 1 517 188 188 TYR H H 7.875 0.02 1 518 188 188 TYR CA C 56.264 0.2 1 519 188 188 TYR N N 119.963 0.2 1 520 189 189 TYR H H 8.672 0.02 1 521 189 189 TYR CA C 57.084 0.2 1 522 189 189 TYR N N 124.873 0.2 1 523 190 190 SER H H 8.251 0.02 1 524 190 190 SER CA C 56.240 0.2 1 525 190 190 SER N N 121.979 0.2 1 526 191 191 VAL H H 8.803 0.02 1 527 191 191 VAL CA C 58.356 0.2 1 528 191 191 VAL N N 116.906 0.2 1 529 192 192 GLN H H 9.110 0.02 1 530 192 192 GLN CA C 55.056 0.2 1 531 192 192 GLN N N 120.811 0.2 1 532 193 193 THR H H 7.797 0.02 1 533 193 193 THR CA C 60.199 0.2 1 534 193 193 THR N N 120.445 0.2 1 535 194 194 THR H H 8.702 0.02 1 536 194 194 THR CA C 62.532 0.2 1 537 194 194 THR N N 117.994 0.2 1 538 195 195 GLU H H 9.116 0.02 1 539 195 195 GLU CA C 55.500 0.2 1 540 195 195 GLU N N 124.158 0.2 1 541 196 196 GLY H H 9.208 0.02 1 542 196 196 GLY CA C 47.823 0.2 1 543 196 196 GLY N N 110.563 0.2 1 544 197 197 GLU H H 8.760 0.02 1 545 197 197 GLU CA C 59.480 0.2 1 546 197 197 GLU N N 119.538 0.2 1 547 198 198 GLN H H 7.482 0.02 1 548 198 198 GLN CA C 59.304 0.2 1 549 198 198 GLN N N 119.391 0.2 1 550 199 199 ILE H H 7.450 0.02 1 551 199 199 ILE CA C 65.436 0.2 1 552 199 199 ILE N N 121.222 0.2 1 553 200 200 ALA H H 8.109 0.02 1 554 200 200 ALA CA C 55.007 0.2 1 555 200 200 ALA N N 119.329 0.2 1 556 201 201 GLN H H 7.561 0.02 1 557 201 201 GLN CA C 58.565 0.2 1 558 201 201 GLN N N 115.165 0.2 1 559 202 202 LEU H H 7.283 0.02 1 560 202 202 LEU CA C 57.313 0.2 1 561 202 202 LEU N N 121.181 0.2 1 562 203 203 ILE H H 7.737 0.02 1 563 203 203 ILE CA C 65.447 0.2 1 564 203 203 ILE N N 117.693 0.2 1 565 204 204 ALA H H 8.285 0.02 1 566 204 204 ALA CA C 55.256 0.2 1 567 204 204 ALA N N 120.286 0.2 1 568 205 205 GLY H H 7.545 0.02 1 569 205 205 GLY CA C 46.842 0.2 1 570 205 205 GLY N N 103.855 0.2 1 571 206 206 TYR H H 7.680 0.02 1 572 206 206 TYR CA C 58.141 0.2 1 573 206 206 TYR N N 121.343 0.2 1 574 207 207 ILE H H 8.751 0.02 1 575 207 207 ILE CA C 64.686 0.2 1 576 207 207 ILE N N 122.746 0.2 1 577 208 208 ASP H H 7.923 0.02 1 578 208 208 ASP CA C 57.826 0.2 1 579 208 208 ASP N N 119.844 0.2 1 580 209 209 ILE H H 7.220 0.02 1 581 209 209 ILE CA C 64.647 0.2 1 582 209 209 ILE N N 116.520 0.2 1 583 210 210 ILE H H 7.527 0.02 1 584 210 210 ILE CA C 64.897 0.2 1 585 210 210 ILE N N 121.009 0.2 1 586 211 211 LEU H H 8.405 0.02 1 587 211 211 LEU CA C 56.778 0.2 1 588 211 211 LEU N N 119.627 0.2 1 589 212 212 LYS H H 7.820 0.02 1 590 212 212 LYS CA C 57.603 0.2 1 591 212 212 LYS N N 118.439 0.2 1 592 213 213 LYS H H 7.735 0.02 1 593 213 213 LYS CA C 57.120 0.2 1 594 213 213 LYS N N 119.516 0.2 1 595 214 214 LYS H H 7.916 0.02 1 596 214 214 LYS CA C 56.525 0.2 1 597 214 214 LYS N N 121.190 0.2 1 598 215 215 LYS H H 8.202 0.02 1 599 215 215 LYS CA C 56.391 0.2 1 600 215 215 LYS N N 123.025 0.2 1 601 216 216 SER H H 7.884 0.02 1 602 216 216 SER CA C 59.974 0.2 1 603 216 216 SER N N 122.719 0.2 1 stop_ save_