data_6258 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, 15N and Cb chemical shift assignments for TolAIII in complex with g3pN1 ; _BMRB_accession_number 6258 _BMRB_flat_file_name bmr6258.str _Entry_type original _Submission_date 2004-06-30 _Accession_date 2004-07-06 _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 Deprez Christophe . . 2 Lloubes Roland . . 3 Gavioli Marthe . . 4 Marion Dominique . . 5 Guerlesquin Francoise . . 6 Blanchard Laurence . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 80 "13C chemical shifts" 225 "15N chemical shifts" 80 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-02-21 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 4771 'C-terminal domain of the TolA protein' stop_ _Original_release_date 2004-07-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Structure of the E.coli TolA C-terminal Domain Reveals Conformational Changes upon Binding to the Phage g3p N-terminal Domain ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15701516 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Deprez Christophe . . 2 Lloubes Roland . . 3 Gavioli Marthe . . 4 Marion Dominique . . 5 Guerlesquin Francoise . . 6 Blanchard Laurence . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 346 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1047 _Page_last 1057 _Year 2005 _Details . loop_ _Keyword 'Tol-Pal system' 'TolA protein' 'conformational changes' g3p 'protein-protein intercations' stop_ save_ ################################## # Molecular system description # ################################## save_system_complexed_TolAIII _Saveframe_category molecular_system _Mol_system_name 'g3pN1 bound TolAIII' _Abbreviation_common 'complexed TolAIII' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label TolAIII $TolAIII g3pN1 $g3pN1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state heterodimer _System_paramagnetic no _System_thiol_state 'not reported' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_TolAIII _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'TolA domain III' _Abbreviation_common TolAIII _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 106 _Mol_residue_sequence ; AEFGNTKNNGASGADINNYA GQIKSAIESKFYDASSYAGK TCTLRIKLAPDGMLLDIKPE GGDPALCQAALAAAKLAKIP KPPSQAVYEVFKNAPLDFKP HHHHHH ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 GLU 3 PHE 4 GLY 5 ASN 6 THR 7 LYS 8 ASN 9 ASN 10 GLY 11 ALA 12 SER 13 GLY 14 ALA 15 ASP 16 ILE 17 ASN 18 ASN 19 TYR 20 ALA 21 GLY 22 GLN 23 ILE 24 LYS 25 SER 26 ALA 27 ILE 28 GLU 29 SER 30 LYS 31 PHE 32 TYR 33 ASP 34 ALA 35 SER 36 SER 37 TYR 38 ALA 39 GLY 40 LYS 41 THR 42 CYS 43 THR 44 LEU 45 ARG 46 ILE 47 LYS 48 LEU 49 ALA 50 PRO 51 ASP 52 GLY 53 MET 54 LEU 55 LEU 56 ASP 57 ILE 58 LYS 59 PRO 60 GLU 61 GLY 62 GLY 63 ASP 64 PRO 65 ALA 66 LEU 67 CYS 68 GLN 69 ALA 70 ALA 71 LEU 72 ALA 73 ALA 74 ALA 75 LYS 76 LEU 77 ALA 78 LYS 79 ILE 80 PRO 81 LYS 82 PRO 83 PRO 84 SER 85 GLN 86 ALA 87 VAL 88 TYR 89 GLU 90 VAL 91 PHE 92 LYS 93 ASN 94 ALA 95 PRO 96 LEU 97 ASP 98 PHE 99 LYS 100 PRO 101 HIS 102 HIS 103 HIS 104 HIS 105 HIS 106 HIS stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 4771 TolA 100.00 106 100.00 100.00 3.66e-55 PDB 1S62 'Solution Structure Of The Escherichia Coli Tola C-Terminal Domain' 100.00 106 100.00 100.00 3.66e-55 PDB 1TOL 'Fusion Of N-Terminal Domain Of The Minor Coat Protein From Gene Iii In Phage M13, And C-Terminal Domain Of E. Coli Protein-Tola' 91.51 222 100.00 100.00 7.78e-44 DBJ BAA35405 'membrane anchored protein in TolA-TolQ-TolR complex [Escherichia coli W3110]' 91.51 421 100.00 100.00 3.34e-54 DBJ BAB34197 'membrane spanning protein TolA [Escherichia coli O157:H7 str. Sakai]' 91.51 394 100.00 100.00 1.21e-53 GenBank AAA24683 tolA 91.51 421 100.00 100.00 3.34e-54 GenBank AAC73833 'membrane anchored protein in TolA-TolQ-TolR complex [Escherichia coli str. K-12 substr. MG1655]' 91.51 421 100.00 100.00 3.34e-54 GenBank AAG55075 'membrane spanning protein, required for outer membrane integrity [Escherichia coli O157:H7 EDL933]' 91.51 394 100.00 100.00 1.21e-53 GenBank AAN42202 'membrane spanning protein [Shigella flexneri 2a str. 301]' 91.51 413 100.00 100.00 5.89e-54 GenBank AAN79291 'TolA protein [Escherichia coli CFT073]' 91.51 421 100.00 100.00 4.05e-54 REF AP_001377 'membrane anchored protein in TolA-TolQ-TolR complex [Escherichia coli W3110]' 91.51 421 100.00 100.00 3.34e-54 REF NP_286467 'cell envelope integrity inner membrane protein TolA [Escherichia coli O157:H7 EDL933]' 91.51 394 100.00 100.00 1.21e-53 REF NP_308801 'cell envelope integrity inner membrane protein TolA [Escherichia coli O157:H7 str. Sakai]' 91.51 394 100.00 100.00 1.21e-53 REF NP_415267 'membrane anchored protein in TolA-TolQ-TolR complex [Escherichia coli str. K-12 substr. MG1655]' 91.51 421 100.00 100.00 3.34e-54 REF NP_706495 'cell envelope integrity inner membrane protein TolA [Shigella flexneri 2a str. 301]' 91.51 413 100.00 100.00 5.89e-54 SWISS-PROT P19934 'Protein tolA' 91.51 421 100.00 100.00 3.34e-54 stop_ save_ save_g3pN1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common g3pN1 _Abbreviation_common g3pN1 _Molecular_mass . _Mol_thiol_state 'not reported' _Details ; G3pN1 is the N-terminal domain of fd phage minor coat gene 3 protein. G3pN1 = G3p (swiss-prot accession number P03662 with one residue difference S11 instead of P11) spanning amino-acids 1-71 of the mature protein followed by six histidine residues was used as a partner of TolAIII. ; _Residue_count 77 _Mol_residue_sequence ; MKKLLFAIPLVVPFYSHSAE TVESCLAKPHTENSFTNVWK DDKTLDRYANYEGCLWNATG VVVCTGDETQCHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LYS 3 LYS 4 LEU 5 LEU 6 PHE 7 ALA 8 ILE 9 PRO 10 LEU 11 VAL 12 VAL 13 PRO 14 PHE 15 TYR 16 SER 17 HIS 18 SER 19 ALA 20 GLU 21 THR 22 VAL 23 GLU 24 SER 25 CYS 26 LEU 27 ALA 28 LYS 29 PRO 30 HIS 31 THR 32 GLU 33 ASN 34 SER 35 PHE 36 THR 37 ASN 38 VAL 39 TRP 40 LYS 41 ASP 42 ASP 43 LYS 44 THR 45 LEU 46 ASP 47 ARG 48 TYR 49 ALA 50 ASN 51 TYR 52 GLU 53 GLY 54 CYS 55 LEU 56 TRP 57 ASN 58 ALA 59 THR 60 GLY 61 VAL 62 VAL 63 VAL 64 CYS 65 THR 66 GLY 67 ASP 68 GLU 69 THR 70 GLN 71 CYS 72 HIS 73 HIS 74 HIS 75 HIS 76 HIS 77 HIS stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 1FGP 'Membrane Penetration Domain Of The Minor Coat Protein G3p Of Phage Fd, Nmr, 15 Structures' 68.83 70 98.11 100.00 8.78e-24 PDB 2G3P 'Structure Of The N-Terminal Two Domains Of The Infectivity Protein G3p Of Filamentous Phage Fd' 70.13 225 98.15 100.00 5.93e-25 DBJ BAF74208 'protein III [Enterobacteria phage f1]' 93.51 424 98.61 100.00 7.03e-39 DBJ BAF74218 'protein III [Enterobacteria phage f1]' 93.51 424 98.61 100.00 7.03e-39 EMBL CAA23862 'structural protein [Enterobacteria phage M13]' 93.51 424 98.61 100.00 7.03e-39 EMBL CAA23872 'unnamed protein product [Enterobacteria phage f1]' 93.51 424 98.61 100.00 7.03e-39 GenBank AAA32215 'protein III' 93.51 424 98.61 100.00 7.03e-39 GenBank AAA32309 'III [Enterobacteria phage fd]' 93.51 424 98.61 100.00 7.03e-39 GenBank AAF75609 'adsorption protein pIII precursor [Filamentous phage cloning vector fd-tet]' 93.51 424 98.61 100.00 7.03e-39 GenBank AAM73889 'adsorption protein pIII precursor [Filamentous phage display vector f8-5]' 93.51 424 98.61 100.00 7.03e-39 GenBank AAM73901 'adsorption protein pIII precursor [Filamentous phage display vector c8-4]' 93.51 424 98.61 100.00 7.03e-39 PIR Z3BPF1 'coat protein A precursor - phage f1' 93.51 424 98.61 100.00 7.03e-39 PRF 0812197D DNA,phage 93.51 424 98.61 100.00 7.03e-39 REF NP_510891 'structural protein [Enterobacteria phage M13]' 93.51 424 98.61 100.00 7.03e-39 SWISS-PROT P03661 'Coat protein A precursor (G3P)' 93.51 424 98.61 100.00 7.03e-39 SWISS-PROT P69168 'Coat protein A precursor (G3P) (Minor coat protein)' 93.51 424 98.61 100.00 7.03e-39 SWISS-PROT P69169 'Coat protein A precursor (G3P) (Minor coat protein)' 93.51 424 98.61 100.00 7.03e-39 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $TolAIII 'E. coli' 562 Eubacteria . . . . $g3pN1 'fd phage' . . . . . 'G3pN1 is the N-terminal domain of fd phage minor coat gene 3 protein.' 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 $TolAIII 'recombinant technology' . . . . . $g3pN1 'recombinant technology' 'E. coli' . . . BL21(DE3) stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'The NMR tube contains 15N/13C TolAIII (0.4mM) with unlabelled g3pN1 (0.6mM).' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $TolAIII 0.4 mM '[U-13C; U-15N]' $g3pN1 0.6 mM . 'potassium phosphate buffer' 30 mM . NaCl 30 mM . stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _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 . save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label . save_ save_3D_DEPT-CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D DEPT-CBCA(CO)NH' _Sample_label . save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label . save_ ####################### # Sample conditions # ####################### save_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 60 . mM pH 6.8 0.1 n/a temperature 300 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D DEPT-CBCA(CO)NH' '3D HNCO' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name TolAIII _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 . 3 PHE C C 176.14 0.2 1 2 . 3 PHE CB C 41.09 0.2 1 3 . 4 GLY H H 8.19 0.05 1 4 . 4 GLY C C 173.80 0.2 1 5 . 4 GLY CA C 44.68 0.2 1 6 . 4 GLY N N 114.0 0.2 1 7 . 5 ASN H H 8.27 0.05 1 8 . 5 ASN C C 175.55 0.2 1 9 . 5 ASN CA C 52.73 0.2 1 10 . 5 ASN CB C 39.09 0.2 1 11 . 5 ASN N N 119.18 0.2 1 12 . 6 THR H H 8.12 0.05 1 13 . 6 THR CA C 61.48 0.2 1 14 . 6 THR N N 114.92 0.2 1 15 . 9 ASN C C 176.25 0.2 1 16 . 9 ASN CB C 39.81 0.2 1 17 . 10 GLY H H 8.35 0.05 1 18 . 10 GLY C C 173.92 0.2 1 19 . 10 GLY CA C 44.87 0.2 1 20 . 10 GLY N N 110.83 0.2 1 21 . 11 ALA H H 8.32 0.05 1 22 . 11 ALA C C 177.33 0.2 1 23 . 11 ALA CA C 51.10 0.2 1 24 . 11 ALA CB C 19.64 0.2 1 25 . 11 ALA N N 124.0 0.2 1 26 . 12 SER H H 8.74 0.05 1 27 . 12 SER C C 175.47 0.2 1 28 . 12 SER CA C 57.30 0.2 1 29 . 12 SER CB C 64.62 0.2 1 30 . 12 SER N N 118.10 0.2 1 31 . 13 GLY H H 8.76 0.05 1 32 . 13 GLY C C 176.08 0.2 1 33 . 13 GLY CA C 46.74 0.2 1 34 . 13 GLY N N 111.06 0.2 1 35 . 14 ALA H H 8.22 0.05 1 36 . 14 ALA C C 179.56 0.2 1 37 . 14 ALA CA C 54.24 0.2 1 38 . 14 ALA CB C 18.40 0.2 1 39 . 14 ALA N N 124.20 0.2 1 40 . 15 ASP H H 7.91 0.05 1 41 . 15 ASP C C 179.06 0.2 1 42 . 15 ASP CA C 56.68 0.2 1 43 . 15 ASP CB C 40.76 0.2 1 44 . 15 ASP N N 119.44 0.2 1 45 . 16 ILE H H 8.0 0.05 1 46 . 16 ILE C C 177.0 0.2 1 47 . 16 ILE CA C 65.35 0.2 1 48 . 16 ILE CB C 38.37 0.2 1 49 . 16 ILE N N 121.69 0.2 1 50 . 17 ASN H H 8.08 0.05 1 51 . 17 ASN C C 176.98 0.2 1 52 . 17 ASN CA C 56.56 0.2 1 53 . 17 ASN CB C 39.47 0.2 1 54 . 17 ASN N N 118.18 0.2 1 55 . 18 ASN H H 8.41 0.05 1 56 . 18 ASN CA C 55.44 0.2 1 57 . 18 ASN N N 116.0 0.2 1 58 . 21 GLY C C 176.64 0.2 1 59 . 22 GLN H H 7.43 0.05 1 60 . 22 GLN C C 179.65 0.2 1 61 . 22 GLN CA C 58.30 0.2 1 62 . 22 GLN CB C 28.44 0.2 1 63 . 22 GLN N N 122.49 0.2 1 64 . 23 ILE H H 7.72 0.05 1 65 . 23 ILE CA C 65.97 0.2 1 66 . 23 ILE CB C 37.02 0.2 1 67 . 23 ILE N N 121.92 0.2 1 68 . 24 LYS H H 7.86 0.05 1 69 . 24 LYS C C 177.89 0.2 1 70 . 24 LYS CA C 59.92 0.2 1 71 . 24 LYS N N 119.14 0.2 1 72 . 25 SER H H 8.08 0.05 1 73 . 25 SER C C 177.11 0.2 1 74 . 25 SER CA C 60.92 0.2 1 75 . 25 SER CB C 62.89 0.2 1 76 . 25 SER N N 112.73 0.2 1 77 . 26 ALA H H 7.76 0.05 1 78 . 26 ALA C C 180.06 0.2 1 79 . 26 ALA CA C 54.59 0.2 1 80 . 26 ALA CB C 18.56 0.2 1 81 . 26 ALA N N 124.20 0.2 1 82 . 27 ILE H H 7.73 0.05 1 83 . 27 ILE C C 177.85 0.2 1 84 . 27 ILE CA C 63.78 0.2 1 85 . 27 ILE N N 116.79 0.2 1 86 . 28 GLU H H 8.95 0.05 1 87 . 28 GLU C C 179.39 0.2 1 88 . 28 GLU CA C 59.96 0.2 1 89 . 28 GLU CB C 29.79 0.2 1 90 . 28 GLU N N 120.28 0.2 1 91 . 29 SER H H 7.69 0.05 1 92 . 29 SER C C 174.82 0.2 1 93 . 29 SER CA C 60.57 0.2 1 94 . 29 SER CB C 63.35 0.2 1 95 . 29 SER N N 111.46 0.2 1 96 . 30 LYS H H 7.13 0.05 1 97 . 30 LYS C C 174.58 0.2 1 98 . 30 LYS CA C 52.47 0.2 1 99 . 30 LYS CB C 32.61 0.2 1 100 . 30 LYS N N 117.81 0.2 1 101 . 31 PHE H H 7.44 0.05 1 102 . 31 PHE C C 174.81 0.2 1 103 . 31 PHE CA C 53.03 0.2 1 104 . 31 PHE CB C 37.71 0.2 1 105 . 31 PHE N N 122.15 0.2 1 106 . 32 TYR H H 7.57 0.05 1 107 . 32 TYR C C 176.02 0.2 1 108 . 32 TYR CA C 58.00 0.2 1 109 . 32 TYR CB C 38.68 0.2 1 110 . 32 TYR N N 124.39 0.2 1 111 . 33 ASP H H 8.33 0.05 1 112 . 33 ASP C C 173.93 0.2 1 113 . 33 ASP CA C 52.80 0.2 1 114 . 33 ASP CB C 39.83 0.2 1 115 . 33 ASP N N 118.55 0.2 1 116 . 34 ALA H H 7.09 0.05 1 117 . 34 ALA C C 179.10 0.2 1 118 . 34 ALA CA C 55.14 0.2 1 119 . 34 ALA CB C 19.04 0.2 1 120 . 34 ALA N N 121.89 0.2 1 121 . 35 SER H H 8.36 0.05 1 122 . 35 SER C C 176.75 0.2 1 123 . 35 SER CA C 60.70 0.2 1 124 . 35 SER CB C 62.56 0.2 1 125 . 35 SER N N 110.36 0.2 1 126 . 36 SER H H 7.75 0.05 1 127 . 36 SER C C 174.15 0.2 1 128 . 36 SER CA C 60.01 0.2 1 129 . 36 SER CB C 62.51 0.2 1 130 . 36 SER N N 118.03 0.2 1 131 . 37 TYR H H 7.65 0.05 1 132 . 37 TYR C C 173.93 0.2 1 133 . 37 TYR CA C 55.99 0.2 1 134 . 37 TYR CB C 40.43 0.2 1 135 . 37 TYR N N 119.10 0.2 1 136 . 38 ALA H H 6.94 0.05 1 137 . 38 ALA C C 178.39 0.2 1 138 . 38 ALA CA C 53.66 0.2 1 139 . 38 ALA CB C 18.04 0.2 1 140 . 38 ALA N N 121.59 0.2 1 141 . 39 GLY H H 8.51 0.05 1 142 . 39 GLY C C 174.14 0.2 1 143 . 39 GLY CA C 44.94 0.2 1 144 . 39 GLY N N 112.22 0.2 1 145 . 40 LYS H H 8.03 0.05 1 146 . 40 LYS C C 174.95 0.2 1 147 . 40 LYS CA C 53.99 0.2 1 148 . 40 LYS CB C 34.96 0.2 1 149 . 40 LYS N N 120.98 0.2 1 150 . 41 THR H H 8.21 0.05 1 151 . 41 THR C C 173.95 0.2 1 152 . 41 THR CA C 60.70 0.2 1 153 . 41 THR CB C 72.08 0.2 1 154 . 41 THR N N 113.34 0.2 1 155 . 42 CYS H H 8.43 0.05 1 156 . 42 CYS C C 172.64 0.2 1 157 . 42 CYS CA C 56.34 0.2 1 158 . 42 CYS CB C 49.71 0.2 1 159 . 42 CYS N N 122.05 0.2 1 160 . 43 THR H H 8.78 0.05 1 161 . 43 THR C C 172.77 0.2 1 162 . 43 THR CA C 60.21 0.2 1 163 . 43 THR CB C 70.71 0.2 1 164 . 43 THR N N 126.54 0.2 1 165 . 44 LEU H H 9.79 0.05 1 166 . 44 LEU C C 174.47 0.2 1 167 . 44 LEU CA C 53.40 0.2 1 168 . 44 LEU N N 127.51 0.2 1 169 . 45 ARG H H 8.71 0.05 1 170 . 45 ARG C C 176.46 0.2 1 171 . 45 ARG CA C 54.09 0.2 1 172 . 45 ARG N N 121.60 0.2 1 173 . 46 ILE H H 8.48 0.05 1 174 . 46 ILE C C 173.94 0.2 1 175 . 46 ILE CA C 59.60 0.2 1 176 . 46 ILE N N 122.60 0.2 1 177 . 47 LYS H H 7.80 0.05 1 178 . 47 LYS C C 175.27 0.2 1 179 . 47 LYS CA C 55.09 0.2 1 180 . 47 LYS CB C 35.17 0.2 1 181 . 47 LYS N N 120.0 0.2 1 182 . 48 LEU H H 8.94 0.05 1 183 . 48 LEU C C 176.93 0.2 1 184 . 48 LEU CA C 53.14 0.2 1 185 . 48 LEU CB C 46.70 0.2 1 186 . 48 LEU N N 127.46 0.2 1 187 . 49 ALA H H 9.37 0.05 1 188 . 49 ALA CA C 50.02 0.2 1 189 . 49 ALA N N 129.72 0.2 1 190 . 50 PRO C C 175.52 0.2 1 191 . 50 PRO CB C 31.40 0.2 1 192 . 51 ASP H H 7.43 0.05 1 193 . 51 ASP C C 176.91 0.2 1 194 . 51 ASP CA C 52.14 0.2 1 195 . 51 ASP CB C 40.29 0.2 1 196 . 51 ASP N N 112.47 0.2 1 197 . 52 GLY H H 8.44 0.05 1 198 . 52 GLY C C 171.88 0.2 1 199 . 52 GLY CA C 44.44 0.2 1 200 . 52 GLY N N 109.21 0.2 1 201 . 53 MET H H 7.42 0.05 1 202 . 53 MET C C 175.81 0.2 1 203 . 53 MET CA C 55.73 0.2 1 204 . 53 MET CB C 32.74 0.2 1 205 . 53 MET N N 117.64 0.2 1 206 . 54 LEU H H 8.69 0.05 1 207 . 54 LEU C C 176.48 0.2 1 208 . 54 LEU CA C 54.35 0.2 1 209 . 54 LEU CB C 41.78 0.2 1 210 . 54 LEU N N 124.68 0.2 1 211 . 55 LEU H H 8.93 0.05 1 212 . 55 LEU C C 177.38 0.2 1 213 . 55 LEU CA C 55.56 0.2 1 214 . 55 LEU CB C 42.99 0.2 1 215 . 55 LEU N N 128.65 0.2 1 216 . 56 ASP H H 7.78 0.05 1 217 . 56 ASP C C 173.50 0.2 1 218 . 56 ASP CA C 52.88 0.2 1 219 . 56 ASP CB C 44.66 0.2 1 220 . 56 ASP N N 115.02 0.2 1 221 . 57 ILE H H 8.04 0.05 1 222 . 57 ILE C C 172.62 0.2 1 223 . 57 ILE CA C 60.10 0.2 1 224 . 57 ILE CB C 40.04 0.2 1 225 . 57 ILE N N 119.01 0.2 1 226 . 58 LYS H H 8.31 0.05 1 227 . 58 LYS CA C 51.99 0.2 1 228 . 58 LYS N N 125.59 0.2 1 229 . 59 PRO C C 174.27 0.2 1 230 . 60 GLU H H 8.28 0.05 1 231 . 60 GLU C C 176.14 0.2 1 232 . 60 GLU CA C 55.76 0.2 1 233 . 60 GLU CB C 61.48 0.2 1 234 . 60 GLU N N 123.78 0.2 1 235 . 61 GLY H H 7.57 0.05 1 236 . 61 GLY C C 171.34 0.2 1 237 . 61 GLY CA C 44.96 0.2 1 238 . 61 GLY N N 107.77 0.2 1 239 . 62 GLY H H 8.3 0.05 1 240 . 62 GLY C C 174.69 0.2 1 241 . 62 GLY CA C 43.24 0.2 1 242 . 62 GLY N N 106.46 0.2 1 243 . 63 ASP H H 8.36 0.05 1 244 . 63 ASP CA C 52.04 0.2 1 245 . 63 ASP N N 122.21 0.2 1 246 . 64 PRO C C 178.86 0.2 1 247 . 64 PRO CB C 32.36 0.2 1 248 . 65 ALA H H 7.90 0.05 1 249 . 65 ALA C C 180.96 0.2 1 250 . 65 ALA CA C 54.90 0.2 1 251 . 65 ALA CB C 18.28 0.2 1 252 . 65 ALA N N 121.37 0.2 1 253 . 66 LEU H H 8.62 0.05 1 254 . 66 LEU C C 178.25 0.2 1 255 . 66 LEU CA C 56.75 0.2 1 256 . 66 LEU CB C 40.06 0.2 1 257 . 66 LEU N N 122.40 0.2 1 258 . 67 CYS H H 9.04 0.05 1 259 . 67 CYS C C 176.74 0.2 1 260 . 67 CYS CA C 55.45 0.2 1 261 . 67 CYS CB C 37.02 0.2 1 262 . 67 CYS N N 115.45 0.2 1 263 . 68 GLN H H 7.86 0.05 1 264 . 68 GLN C C 178.35 0.2 1 265 . 68 GLN CA C 58.59 0.2 1 266 . 68 GLN CB C 28.24 0.2 1 267 . 68 GLN N N 119.37 0.2 1 268 . 69 ALA H H 7.46 0.05 1 269 . 69 ALA C C 180.0 0.2 1 270 . 69 ALA CA C 54.21 0.2 1 271 . 69 ALA CB C 18.34 0.2 1 272 . 69 ALA N N 124.62 0.2 1 273 . 70 ALA H H 8.59 0.05 1 274 . 70 ALA C C 178.15 0.2 1 275 . 70 ALA CA C 54.20 0.2 1 276 . 70 ALA CB C 16.43 0.2 1 277 . 70 ALA N N 123.82 0.2 1 278 . 71 LEU H H 7.80 0.05 1 279 . 71 LEU C C 178.30 0.2 1 280 . 71 LEU CA C 57.88 0.2 1 281 . 71 LEU CB C 42.60 0.2 1 282 . 71 LEU N N 118.5 0.2 1 283 . 72 ALA H H 7.24 0.05 1 284 . 72 ALA C C 180.07 0.2 1 285 . 72 ALA CA C 54.37 0.2 1 286 . 72 ALA CB C 17.78 0.2 1 287 . 72 ALA N N 119.18 0.2 1 288 . 73 ALA H H 7.38 0.05 1 289 . 73 ALA C C 179.22 0.2 1 290 . 73 ALA CA C 54.24 0.2 1 291 . 73 ALA CB C 17.83 0.2 1 292 . 73 ALA N N 119.69 0.2 1 293 . 74 ALA H H 8.23 0.05 1 294 . 74 ALA C C 178.91 0.2 1 295 . 74 ALA CA C 54.68 0.2 1 296 . 74 ALA CB C 18.02 0.2 1 297 . 74 ALA N N 117.87 0.2 1 298 . 75 LYS H H 7.71 0.05 1 299 . 75 LYS C C 177.89 0.2 1 300 . 75 LYS CA C 58.34 0.2 1 301 . 75 LYS CB C 32.77 0.2 1 302 . 75 LYS N N 114.28 0.2 1 303 . 76 LEU H H 7.29 0.05 1 304 . 76 LEU C C 177.25 0.2 1 305 . 76 LEU CA C 54.40 0.2 1 306 . 76 LEU CB C 43.79 0.2 1 307 . 76 LEU N N 118.28 0.2 1 308 . 77 ALA H H 7.17 0.05 1 309 . 77 ALA C C 176.59 0.2 1 310 . 77 ALA CA C 51.83 0.2 1 311 . 77 ALA CB C 20.38 0.2 1 312 . 77 ALA N N 121.79 0.2 1 313 . 78 LYS H H 8.56 0.05 1 314 . 78 LYS C C 174.88 0.2 1 315 . 78 LYS CA C 53.53 0.2 1 316 . 78 LYS CB C 31.26 0.2 1 317 . 78 LYS N N 124.28 0.2 1 318 . 79 ILE H H 8.34 0.05 1 319 . 79 ILE CA C 58.43 0.2 1 320 . 79 ILE N N 129.23 0.2 1 321 . 83 PRO C C 175.24 0.2 1 322 . 83 PRO CB C 31.88 0.2 1 323 . 84 SER H H 6.76 0.05 1 324 . 84 SER CA C 55.65 0.2 1 325 . 84 SER N N 108.86 0.2 1 326 . 85 GLN CB C 27.84 0.2 1 327 . 86 ALA H H 8.32 0.2 1 328 . 86 ALA C C 180.49 0.05 1 329 . 86 ALA CA C 54.60 0.2 1 330 . 86 ALA CB C 18.21 0.2 1 331 . 86 ALA N N 120.67 0.2 1 332 . 87 VAL H H 7.44 0.05 1 333 . 87 VAL C C 177.27 0.2 1 334 . 87 VAL CA C 65.62 0.2 1 335 . 87 VAL CB C 31.56 0.2 1 336 . 87 VAL N N 117.09 0.2 1 337 . 88 TYR H H 7.91 0.05 1 338 . 88 TYR C C 176.53 0.2 1 339 . 88 TYR CA C 60.89 0.2 1 340 . 88 TYR CB C 39.10 0.2 1 341 . 88 TYR N N 120.78 0.2 1 342 . 89 GLU H H 8.10 0.05 1 343 . 89 GLU C C 178.69 0.2 1 344 . 89 GLU CA C 58.68 0.2 1 345 . 89 GLU CB C 29.39 0.2 1 346 . 89 GLU N N 114.96 0.2 1 347 . 90 VAL H H 7.04 0.05 1 348 . 90 VAL C C 177.11 0.2 1 349 . 90 VAL CA C 64.35 0.2 1 350 . 90 VAL CB C 31.30 0.2 1 351 . 90 VAL N N 114.91 0.2 1 352 . 91 PHE H H 7.20 0.05 1 353 . 91 PHE CA C 58.90 0.2 1 354 . 91 PHE CB C 41.13 0.2 1 355 . 91 PHE N N 116.57 0.2 1 356 . 95 PRO C C 174.67 0.2 1 357 . 95 PRO CB C 31.86 0.2 1 358 . 96 LEU H H 8.51 0.05 1 359 . 96 LEU C C 175.11 0.2 1 360 . 96 LEU CA C 52.11 0.2 1 361 . 96 LEU CB C 46.55 0.2 1 362 . 96 LEU N N 121.08 0.2 1 363 . 97 ASP H H 9.14 0.05 1 364 . 97 ASP C C 174.83 0.2 1 365 . 97 ASP CA C 50.99 0.2 1 366 . 97 ASP CB C 42.17 0.2 1 367 . 97 ASP N N 121.66 0.2 1 368 . 98 PHE H H 9.05 0.05 1 369 . 98 PHE C C 174.2 0.2 1 370 . 98 PHE CA C 55.93 0.2 1 371 . 98 PHE CB C 41.26 0.2 1 372 . 98 PHE N N 119.02 0.2 1 373 . 99 LYS H H 8.44 0.05 1 374 . 99 LYS CA C 52.71 0.2 1 375 . 99 LYS N N 123.65 0.2 1 376 . 100 PRO C C 176.48 0.2 1 377 . 100 PRO CB C 31.82 0.2 1 378 . 101 HIS H H 9.58 0.05 1 379 . 101 HIS C C 173.97 0.2 1 380 . 101 HIS CA C 55.69 0.2 1 381 . 101 HIS CB C 30.42 0.2 1 382 . 101 HIS N N 123.99 0.2 1 383 . 102 HIS H H 7.98 0.05 1 384 . 102 HIS CA C 56.86 0.2 1 385 . 102 HIS N N 125.86 0.2 1 stop_ save_