data_4771 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignment of the 1H, 15N and 13C resonances of the C-terminal domain of the TolA protein of Escherichia coli, involved in the cell envelope integrity ; _BMRB_accession_number 4771 _BMRB_flat_file_name bmr4771.str _Entry_type original _Submission_date 2000-06-28 _Accession_date 2000-06-28 _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 Blanchard Laurence . . 3 Simorre Jean-Pierre . . 4 Gavioli Marthe . . 5 Guerlesquin Francoise . . 6 Lazdunski Claude . . 7 Lloubes Roland . . 8 Marion Dominique . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 493 "13C chemical shifts" 390 "15N chemical shifts" 91 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-07-21 update author 'addition of relationship loop' 2000-10-30 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 6258 'TolAIII in complex with g3pN1' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Assignment of the 1H, 15N and 13C resonances of the C-terminal domain of the TolA protein of Escherichia coli, involved in cell envelope integrity ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Deprez Christophe . . 2 Blanchard Laurence . . 3 Simorre Jean-Pierre . . 4 Gavioli Marthe . . 5 Guerlesquin Francoise . . 6 Lazdunski Claude . . 7 Lloubes Roland . . 8 Marion Dominique . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 18 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 179 _Page_last 180 _Year 2000 _Details . loop_ _Keyword 'TolA protein' 'Tol-Pal system' 'colicin translocation' 'heteronuclear NMR assignment' stop_ save_ ################################## # Molecular system description # ################################## save_tola3 _Saveframe_category molecular_system _Mol_system_name tola3 _Abbreviation_common tola3 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label tola3 $TolA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_TolA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common TolA _Abbreviation_common TolA _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 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 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 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 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 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 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 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 BMRB 6258 'TolA domain III' 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 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Fraction $TolA 'E. coli' 562 Eubacteria . Escherichia coli periplasm 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 _Details $TolA 'recombinant technology' 'E. coli' Escherichia coli W3110 . 'The protein was overexpressed into the periplasm.' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $TolA 0.5 mM [U-15N] stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 2000 loop_ _Task 'Data processing and visualization' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample save_ ####################### # Sample conditions # ####################### save_condition _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 0.1 n/a temperature 300 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_csr _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Reference_correction_type _Correction_value_citation_label H2O H 1 protons ppm 4.6388 internal direct cylindrical internal parallel_to_Bo 1 $entry_citation 'temperature, pH' $entry_citation 'liquid NH3' N 15 nitrogen ppm 0.00 external indirect cylindrical external_to_the_sample parallel_to_Bo 0.101329118 $entry_citation . $entry_citation DSS C 13 'methyl protons' ppm 0.00 external indirect cylindrical external_to_the_sample parallel_to_Bo 0.251449530 $entry_citation . $entry_citation 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_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample stop_ _Sample_conditions_label $condition _Chem_shift_reference_set_label $csr _Mol_system_component_name tola3 _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 ALA CA C 51.77 0.10 1 2 . 1 ALA CB C 19.33 0.10 1 3 . 1 ALA HA H 3.93 0.01 1 4 . 1 ALA HB H 1.34 0.01 1 5 . 2 GLU C C 175.87 0.10 1 6 . 2 GLU CA C 56.25 0.12 1 7 . 2 GLU CB C 30.35 0.10 1 8 . 2 GLU CG C 35.93 0.10 1 9 . 2 GLU HA H 4.21 0.01 1 10 . 2 GLU HB2 H 1.86 0.01 2 11 . 2 GLU HB3 H 1.75 0.01 2 12 . 2 GLU HG2 H 2.08 0.01 2 13 . 2 GLU HG3 H 2.04 0.01 2 14 . 3 PHE C C 176.18 0.10 1 15 . 3 PHE CA C 57.57 0.10 1 16 . 3 PHE CB C 39.58 0.10 1 17 . 3 PHE H H 8.29 0.01 1 18 . 3 PHE HA H 4.55 0.01 1 19 . 3 PHE HB2 H 3.09 0.01 2 20 . 3 PHE HB3 H 2.93 0.01 2 21 . 3 PHE N N 121.05 0.10 1 22 . 4 GLY C C 173.75 0.10 1 23 . 4 GLY CA C 45.22 0.10 1 24 . 4 GLY H H 8.28 0.01 1 25 . 4 GLY HA2 H 3.85 0.01 2 26 . 4 GLY N N 110.28 0.10 1 27 . 5 ASN CA C 53.15 0.10 1 28 . 5 ASN CB C 38.77 0.10 1 29 . 5 ASN H H 8.21 0.01 1 30 . 5 ASN HA H 4.71 0.01 1 31 . 5 ASN HB2 H 2.69 0.01 2 32 . 5 ASN HB3 H 2.77 0.01 2 33 . 5 ASN N N 118.80 0.10 1 34 . 6 THR CA C 61.95 0.10 1 35 . 6 THR CB C 69.78 0.10 1 36 . 6 THR CG2 C 21.44 0.10 1 37 . 6 THR H H 8.04 0.01 1 38 . 6 THR HA H 4.24 0.01 1 39 . 6 THR HB H 4.18 0.01 2 40 . 6 THR HG2 H 1.12 0.01 1 41 . 6 THR N N 114.33 0.10 1 42 . 7 LYS CA C 56.18 0.10 1 43 . 7 LYS CB C 32.75 0.10 1 44 . 7 LYS CD C 28.84 0.10 1 45 . 7 LYS CE C 41.98 0.10 1 46 . 7 LYS CG C 24.54 0.10 1 47 . 7 LYS H H 8.20 0.01 1 48 . 7 LYS HA H 4.23 0.01 1 49 . 7 LYS HB2 H 1.69 0.02 2 50 . 7 LYS HB3 H 1.74 0.01 2 51 . 7 LYS HD2 H 1.58 0.01 2 52 . 7 LYS HE2 H 2.90 0.01 2 53 . 7 LYS HG2 H 1.33 0.01 2 54 . 7 LYS HG3 H 1.31 0.01 2 55 . 7 LYS N N 123.12 0.10 1 56 . 8 ASN C C 176.10 0.10 1 57 . 8 ASN CA C 54.69 0.12 1 58 . 8 ASN CB C 40.71 0.13 1 59 . 8 ASN HA H 4.38 0.01 1 60 . 8 ASN HB2 H 2.72 0.01 2 61 . 8 ASN HB3 H 2.62 0.01 2 62 . 9 ASN C C 175.54 0.10 1 63 . 9 ASN H H 8.12 0.01 1 64 . 9 ASN N N 113.61 0.10 1 65 . 10 GLY C C 173.56 0.10 1 66 . 10 GLY CA C 45.03 0.10 1 67 . 10 GLY H H 8.21 0.01 1 68 . 10 GLY HA2 H 3.80 0.01 2 69 . 10 GLY HA3 H 3.89 0.01 2 70 . 10 GLY N N 108.62 0.10 1 71 . 11 ALA C C 177.19 0.10 1 72 . 11 ALA CA C 51.61 0.10 1 73 . 11 ALA CB C 19.41 0.10 1 74 . 11 ALA H H 8.06 0.01 1 75 . 11 ALA HA H 4.39 0.01 1 76 . 11 ALA HB H 1.21 0.01 1 77 . 11 ALA N N 123.47 0.10 1 78 . 12 SER C C 175.29 0.10 1 79 . 12 SER CA C 57.65 0.10 1 80 . 12 SER CB C 64.55 0.10 1 81 . 12 SER H H 8.71 0.01 1 82 . 12 SER HA H 4.43 0.01 1 83 . 12 SER HB2 H 4.07 0.01 2 84 . 12 SER HB3 H 3.90 0.01 2 85 . 12 SER N N 117.44 0.10 1 86 . 13 GLY C C 175.75 0.10 1 87 . 13 GLY CA C 46.92 0.10 1 88 . 13 GLY H H 8.65 0.01 1 89 . 13 GLY HA2 H 3.78 0.01 2 90 . 13 GLY HA3 H 3.92 0.01 2 91 . 13 GLY N N 110.27 0.10 1 92 . 14 ALA C C 173.02 0.10 5 93 . 14 ALA CA C 54.72 0.10 1 94 . 14 ALA CB C 18.08 0.10 1 95 . 14 ALA H H 8.16 0.01 1 96 . 14 ALA HA H 4.16 0.01 1 97 . 14 ALA HB H 1.33 0.01 1 98 . 14 ALA N N 123.55 0.10 1 99 . 15 ASP C C 177.80 0.10 5 100 . 15 ASP CA C 56.95 0.10 1 101 . 15 ASP CB C 40.26 0.10 1 102 . 15 ASP H H 7.90 0.01 1 103 . 15 ASP HA H 4.37 0.01 1 104 . 15 ASP HB2 H 2.75 0.01 2 105 . 15 ASP HB3 H 2.48 0.01 2 106 . 15 ASP N N 119.29 0.10 1 107 . 16 ILE C C 177.22 0.10 5 108 . 16 ILE CA C 65.31 0.10 1 109 . 16 ILE CB C 38.14 0.10 1 110 . 16 ILE CD1 C 13.35 0.10 1 111 . 16 ILE CG1 C 29.45 0.10 1 112 . 16 ILE CG2 C 17.18 0.10 1 113 . 16 ILE H H 8.02 0.01 1 114 . 16 ILE HA H 3.83 0.01 1 115 . 16 ILE HB H 2.01 0.01 2 116 . 16 ILE HD1 H 0.83 0.01 1 117 . 16 ILE HG12 H 1.71 0.01 2 118 . 16 ILE HG13 H 1.10 0.01 2 119 . 16 ILE HG2 H 1.04 0.01 1 120 . 16 ILE N N 121.38 0.10 1 121 . 17 ASN C C 178.75 0.10 1 122 . 17 ASN CA C 56.20 0.10 1 123 . 17 ASN CB C 38.17 0.10 1 124 . 17 ASN H H 8.33 0.01 1 125 . 17 ASN HA H 4.49 0.01 1 126 . 17 ASN HB2 H 2.79 0.01 2 127 . 17 ASN N N 118.28 0.10 1 128 . 18 ASN C C 178.11 0.10 1 129 . 18 ASN CA C 55.92 0.10 1 130 . 18 ASN CB C 38.22 0.10 1 131 . 18 ASN H H 8.63 0.01 1 132 . 18 ASN HA H 4.46 0.01 1 133 . 18 ASN HB2 H 2.96 0.01 2 134 . 18 ASN HB3 H 2.85 0.01 2 135 . 18 ASN N N 119.40 0.10 1 136 . 19 TYR C C 177.08 0.10 1 137 . 19 TYR CA C 61.16 0.10 1 138 . 19 TYR CB C 37.69 0.10 1 139 . 19 TYR H H 7.93 0.01 1 140 . 19 TYR HA H 4.34 0.01 1 141 . 19 TYR HB2 H 3.00 0.01 2 142 . 19 TYR HB3 H 2.53 0.01 2 143 . 19 TYR N N 121.83 0.10 1 144 . 20 ALA C C 180.30 0.10 1 145 . 20 ALA CA C 55.54 0.10 1 146 . 20 ALA CB C 17.83 0.10 1 147 . 20 ALA H H 8.49 0.01 1 148 . 20 ALA HA H 3.50 0.01 1 149 . 20 ALA HB H 1.62 0.01 1 150 . 20 ALA N N 121.15 0.10 1 151 . 21 GLY C C 176.62 0.10 1 152 . 21 GLY CA C 46.89 0.10 1 153 . 21 GLY H H 7.84 0.01 1 154 . 21 GLY HA2 H 3.71 0.01 2 155 . 21 GLY HA3 H 3.94 0.01 2 156 . 21 GLY N N 103.37 0.10 1 157 . 22 GLN C C 179.70 0.10 1 158 . 22 GLN CA C 58.84 0.13 1 159 . 22 GLN CB C 28.50 0.11 1 160 . 22 GLN CG C 34.34 0.10 1 161 . 22 GLN H H 7.65 0.01 1 162 . 22 GLN HA H 4.02 0.01 1 163 . 22 GLN HB2 H 2.17 0.01 2 164 . 22 GLN HB3 H 1.82 0.01 2 165 . 22 GLN HG2 H 2.53 0.01 2 166 . 22 GLN HG3 H 2.30 0.01 2 167 . 22 GLN N N 122.68 0.10 1 168 . 23 ILE C C 177.60 0.10 1 169 . 23 ILE CA C 66.13 0.10 1 170 . 23 ILE CB C 37.69 0.10 1 171 . 23 ILE CD1 C 14.46 0.10 1 172 . 23 ILE CG1 C 27.01 0.11 1 173 . 23 ILE CG2 C 17.20 0.10 1 174 . 23 ILE H H 7.90 0.01 1 175 . 23 ILE HA H 3.23 0.01 1 176 . 23 ILE HB H 1.55 0.01 2 177 . 23 ILE HD1 H 0.08 0.01 1 178 . 23 ILE HG12 H 0.74 0.02 2 179 . 23 ILE HG13 H 0.23 0.01 2 180 . 23 ILE HG2 H 0.60 0.01 1 181 . 23 ILE N N 121.37 0.10 1 182 . 24 LYS C C 178.74 0.10 1 183 . 24 LYS CA C 61.34 0.10 1 184 . 24 LYS CB C 31.86 0.11 1 185 . 24 LYS CD C 29.57 0.15 1 186 . 24 LYS CE C 41.95 0.10 1 187 . 24 LYS CG C 26.60 0.10 1 188 . 24 LYS H H 8.10 0.01 1 189 . 24 LYS HA H 3.69 0.01 1 190 . 24 LYS HB2 H 2.01 0.02 2 191 . 24 LYS HB3 H 1.87 0.02 2 192 . 24 LYS HD2 H 1.78 0.01 2 193 . 24 LYS HD3 H 1.62 0.01 2 194 . 24 LYS HE2 H 2.76 0.01 2 195 . 24 LYS HG2 H 1.68 0.01 2 196 . 24 LYS HG3 H 1.26 0.01 2 197 . 24 LYS N N 118.03 0.10 1 198 . 25 SER C C 176.76 0.10 1 199 . 25 SER CA C 61.67 0.10 1 200 . 25 SER CB C 62.76 0.10 1 201 . 25 SER H H 8.32 0.01 1 202 . 25 SER HA H 4.21 0.01 1 203 . 25 SER HB2 H 3.86 0.01 2 204 . 25 SER N N 113.77 0.10 1 205 . 26 ALA C C 180.50 0.10 1 206 . 26 ALA CA C 55.22 0.11 1 207 . 26 ALA CB C 17.91 0.10 1 208 . 26 ALA H H 7.74 0.01 1 209 . 26 ALA HA H 4.11 0.01 1 210 . 26 ALA HB H 1.44 0.01 1 211 . 26 ALA N N 125.20 0.10 1 212 . 27 ILE C C 177.74 0.10 1 213 . 27 ILE CA C 66.06 0.10 1 214 . 27 ILE CB C 37.86 0.10 1 215 . 27 ILE CD1 C 13.03 0.10 1 216 . 27 ILE CG1 C 28.53 0.10 1 217 . 27 ILE CG2 C 16.96 0.10 1 218 . 27 ILE H H 7.78 0.01 1 219 . 27 ILE HA H 3.25 0.01 1 220 . 27 ILE HB H 1.69 0.01 2 221 . 27 ILE HD1 H 0.41 0.01 1 222 . 27 ILE HG12 H 1.83 0.01 2 223 . 27 ILE HG2 H 0.30 0.01 1 224 . 27 ILE N N 118.31 0.10 1 225 . 28 GLU C C 179.12 0.10 1 226 . 28 GLU CA C 60.18 0.10 1 227 . 28 GLU CB C 29.55 0.10 1 228 . 28 GLU CG C 37.40 0.10 1 229 . 28 GLU H H 8.77 0.01 1 230 . 28 GLU HA H 3.88 0.01 1 231 . 28 GLU HB2 H 2.09 0.01 2 232 . 28 GLU HG2 H 2.24 0.01 2 233 . 28 GLU N N 119.04 0.10 1 234 . 29 SER C C 174.90 0.10 1 235 . 29 SER CA C 61.43 0.10 1 236 . 29 SER CB C 63.27 0.10 1 237 . 29 SER H H 7.94 0.01 1 238 . 29 SER HA H 4.23 0.01 1 239 . 29 SER HB2 H 3.99 0.01 2 240 . 29 SER N N 112.96 0.10 1 241 . 30 LYS C C 175.00 0.10 1 242 . 30 LYS CA C 52.89 0.10 1 243 . 30 LYS CB C 32.05 0.10 1 244 . 30 LYS CD C 27.40 0.10 1 245 . 30 LYS CE C 42.06 0.11 1 246 . 30 LYS CG C 22.85 0.10 1 247 . 30 LYS H H 7.21 0.01 1 248 . 30 LYS HA H 4.47 0.01 1 249 . 30 LYS HB2 H 2.02 0.01 2 250 . 30 LYS HB3 H 1.78 0.01 2 251 . 30 LYS HD2 H 1.64 0.01 2 252 . 30 LYS HD3 H 1.44 0.01 2 253 . 30 LYS HE2 H 2.98 0.01 2 254 . 30 LYS HE3 H 2.90 0.01 2 255 . 30 LYS HG2 H 1.11 0.01 2 256 . 30 LYS HG3 H 1.42 0.01 2 257 . 30 LYS N N 118.09 0.10 1 258 . 31 PHE C C 175.39 0.10 1 259 . 31 PHE CA C 56.18 0.12 1 260 . 31 PHE CB C 39.62 0.10 1 261 . 31 PHE H H 7.61 0.01 1 262 . 31 PHE HA H 4.40 0.01 1 263 . 31 PHE HB2 H 3.27 0.01 2 264 . 31 PHE HB3 H 3.00 0.01 2 265 . 31 PHE N N 122.61 0.10 1 266 . 32 TYR C C 175.76 0.10 1 267 . 32 TYR CA C 59.13 0.10 1 268 . 32 TYR CB C 38.04 0.10 1 269 . 32 TYR H H 7.93 0.01 1 270 . 32 TYR HA H 4.46 0.01 1 271 . 32 TYR HB2 H 3.00 0.01 2 272 . 32 TYR HB3 H 2.89 0.01 2 273 . 32 TYR N N 124.43 0.10 1 274 . 33 ASP C C 176.03 0.10 1 275 . 33 ASP CA C 53.34 0.10 1 276 . 33 ASP CB C 40.15 0.10 1 277 . 33 ASP H H 8.28 0.01 1 278 . 33 ASP HA H 4.62 0.01 1 279 . 33 ASP HB2 H 2.67 0.01 2 280 . 33 ASP HB3 H 2.48 0.01 2 281 . 33 ASP N N 119.35 0.10 1 282 . 34 ALA C C 178.90 0.10 1 283 . 34 ALA CA C 54.94 0.12 1 284 . 34 ALA CB C 18.34 0.10 1 285 . 34 ALA H H 8.16 0.01 1 286 . 34 ALA HA H 3.73 0.01 1 287 . 34 ALA HB H 1.03 0.01 1 288 . 34 ALA N N 124.23 0.10 1 289 . 35 SER C C 176.43 0.10 1 290 . 35 SER CA C 60.85 0.10 1 291 . 35 SER CB C 62.48 0.10 1 292 . 35 SER H H 8.39 0.01 1 293 . 35 SER HA H 3.86 0.01 1 294 . 35 SER HB2 H 3.72 0.01 2 295 . 35 SER HB3 H 3.69 0.02 2 296 . 35 SER N N 112.21 0.10 1 297 . 36 SER C C 174.34 0.10 1 298 . 36 SER CA C 60.14 0.10 1 299 . 36 SER CB C 62.64 0.10 1 300 . 36 SER H H 7.72 0.01 1 301 . 36 SER HA H 4.12 0.01 1 302 . 36 SER HB2 H 3.54 0.01 2 303 . 36 SER HB3 H 3.50 0.01 2 304 . 36 SER N N 117.41 0.10 1 305 . 37 TYR C C 174.14 0.10 1 306 . 37 TYR CA C 56.68 0.10 1 307 . 37 TYR CB C 39.43 0.10 1 308 . 37 TYR H H 7.69 0.01 1 309 . 37 TYR HA H 4.48 0.01 1 310 . 37 TYR HB2 H 3.29 0.01 2 311 . 37 TYR HB3 H 2.64 0.01 2 312 . 37 TYR N N 119.08 0.10 1 313 . 38 ALA C C 178.47 0.10 1 314 . 38 ALA CA C 53.95 0.10 1 315 . 38 ALA CB C 17.89 0.10 1 316 . 38 ALA H H 7.00 0.01 1 317 . 38 ALA HA H 3.82 0.01 1 318 . 38 ALA HB H 1.11 0.01 1 319 . 38 ALA N N 121.75 0.10 1 320 . 39 GLY C C 174.14 0.10 1 321 . 39 GLY CA C 45.18 0.10 1 322 . 39 GLY H H 8.57 0.01 1 323 . 39 GLY HA2 H 4.16 0.01 2 324 . 39 GLY HA3 H 3.56 0.01 2 325 . 39 GLY N N 111.06 0.10 1 326 . 40 LYS C C 174.43 0.10 1 327 . 40 LYS CA C 54.71 0.10 1 328 . 40 LYS CB C 34.83 0.11 1 329 . 40 LYS CD C 28.94 0.10 1 330 . 40 LYS CE C 42.43 0.10 1 331 . 40 LYS CG C 25.26 0.10 1 332 . 40 LYS H H 7.83 0.01 1 333 . 40 LYS HA H 4.65 0.02 1 334 . 40 LYS HB2 H 2.08 0.01 2 335 . 40 LYS HB3 H 1.81 0.02 2 336 . 40 LYS HD2 H 1.65 0.02 2 337 . 40 LYS HD3 H 1.55 0.01 2 338 . 40 LYS HE2 H 2.98 0.01 2 339 . 40 LYS HG2 H 1.36 0.01 2 340 . 40 LYS N N 120.34 0.10 1 341 . 41 THR C C 173.25 0.10 1 342 . 41 THR CA C 60.83 0.10 1 343 . 41 THR CB C 71.80 0.10 1 344 . 41 THR CG2 C 20.84 0.10 1 345 . 41 THR H H 8.13 0.01 1 346 . 41 THR HA H 4.99 0.01 1 347 . 41 THR HB H 3.81 0.01 2 348 . 41 THR HG2 H 0.92 0.01 1 349 . 41 THR N N 111.81 0.10 1 350 . 42 CYS C C 173.63 0.10 5 351 . 42 CYS CA C 56.58 0.10 1 352 . 42 CYS CB C 48.71 0.10 1 353 . 42 CYS H H 8.58 0.01 1 354 . 42 CYS HA H 5.05 0.01 1 355 . 42 CYS HB2 H 2.96 0.01 2 356 . 42 CYS HB3 H 2.53 0.01 2 357 . 42 CYS N N 121.86 0.10 1 358 . 43 THR C C 172.85 0.10 1 359 . 43 THR CA C 62.48 0.10 1 360 . 43 THR CB C 69.62 0.10 1 361 . 43 THR CG2 C 21.52 0.10 1 362 . 43 THR H H 8.92 0.01 1 363 . 43 THR HA H 4.95 0.01 1 364 . 43 THR HB H 3.62 0.01 2 365 . 43 THR HG2 H 1.04 0.01 1 366 . 43 THR N N 128.91 0.10 1 367 . 44 LEU C C 174.52 0.10 1 368 . 44 LEU CA C 52.89 0.14 1 369 . 44 LEU CB C 44.70 0.10 1 370 . 44 LEU CD1 C 23.87 0.10 2 371 . 44 LEU CD2 C 25.44 0.10 2 372 . 44 LEU CG C 26.13 0.10 1 373 . 44 LEU H H 9.13 0.01 1 374 . 44 LEU HA H 4.74 0.01 1 375 . 44 LEU HB2 H 1.65 0.01 2 376 . 44 LEU HB3 H 1.06 0.01 2 377 . 44 LEU HD1 H 0.57 0.02 2 378 . 44 LEU HD2 H 0.53 0.01 2 379 . 44 LEU HG H 1.60 0.01 2 380 . 44 LEU N N 128.45 0.10 1 381 . 45 ARG C C 175.26 0.10 1 382 . 45 ARG CA C 54.63 0.10 1 383 . 45 ARG CB C 29.72 0.10 1 384 . 45 ARG CD C 41.18 0.10 1 385 . 45 ARG CG C 26.16 0.12 1 386 . 45 ARG H H 9.12 0.01 1 387 . 45 ARG HA H 4.66 0.01 1 388 . 45 ARG HB2 H 1.70 0.01 2 389 . 45 ARG HB3 H 1.58 0.01 2 390 . 45 ARG HD2 H 3.08 0.01 2 391 . 45 ARG HD3 H 2.93 0.01 2 392 . 45 ARG HG2 H 1.36 0.01 2 393 . 45 ARG HG3 H 1.10 0.01 2 394 . 45 ARG N N 123.21 0.10 1 395 . 46 ILE C C 173.01 0.10 1 396 . 46 ILE CA C 59.89 0.11 1 397 . 46 ILE CB C 41.62 0.10 1 398 . 46 ILE CD1 C 14.30 0.10 1 399 . 46 ILE CG1 C 26.70 0.10 1 400 . 46 ILE CG2 C 16.82 0.10 1 401 . 46 ILE H H 8.89 0.01 1 402 . 46 ILE HA H 4.74 0.01 1 403 . 46 ILE HB H 1.69 0.01 2 404 . 46 ILE HD1 H 0.83 0.01 1 405 . 46 ILE HG12 H 1.62 0.01 2 406 . 46 ILE HG13 H 1.17 0.01 2 407 . 46 ILE HG2 H 0.83 0.01 1 408 . 46 ILE N N 126.60 0.10 1 409 . 47 LYS C C 175.40 0.10 1 410 . 47 LYS CA C 55.26 0.10 1 411 . 47 LYS CB C 35.22 0.10 1 412 . 47 LYS CD C 29.64 0.10 1 413 . 47 LYS CE C 42.03 0.10 1 414 . 47 LYS CG C 24.69 0.12 1 415 . 47 LYS H H 7.86 0.01 1 416 . 47 LYS HA H 4.99 0.01 1 417 . 47 LYS HB2 H 1.73 0.01 2 418 . 47 LYS HB3 H 1.58 0.01 2 419 . 47 LYS HD2 H 1.52 0.01 2 420 . 47 LYS HE2 H 2.78 0.01 2 421 . 47 LYS HG2 H 1.40 0.02 2 422 . 47 LYS N N 121.60 0.10 1 423 . 48 LEU C C 177.14 0.10 1 424 . 48 LEU CA C 53.19 0.10 1 425 . 48 LEU CB C 45.76 0.10 1 426 . 48 LEU CD1 C 26.47 0.10 2 427 . 48 LEU CD2 C 24.13 0.10 2 428 . 48 LEU CG C 26.56 0.10 1 429 . 48 LEU H H 8.12 0.01 1 430 . 48 LEU HA H 5.23 0.01 1 431 . 48 LEU HB2 H 1.65 0.02 2 432 . 48 LEU HD1 H 0.96 0.01 2 433 . 48 LEU HD2 H 0.87 0.01 2 434 . 48 LEU HG H 1.86 0.01 2 435 . 48 LEU N N 123.90 0.10 1 436 . 49 ALA CA C 50.31 0.10 1 437 . 49 ALA CB C 19.15 0.10 1 438 . 49 ALA H H 9.02 0.01 1 439 . 49 ALA HA H 4.79 0.01 1 440 . 49 ALA HB H 1.59 0.01 1 441 . 49 ALA N N 126.15 0.10 1 442 . 50 PRO C C 175.78 0.10 1 443 . 50 PRO CA C 64.83 0.10 1 444 . 50 PRO CB C 31.08 0.12 1 445 . 50 PRO CD C 50.27 0.10 1 446 . 50 PRO CG C 27.00 0.10 1 447 . 50 PRO HA H 3.21 0.01 1 448 . 50 PRO HB2 H 1.53 0.01 2 449 . 50 PRO HD2 H 3.70 0.01 2 450 . 50 PRO HD3 H 3.62 0.01 2 451 . 50 PRO HG2 H 1.82 0.01 2 452 . 50 PRO HG3 H 1.47 0.01 2 453 . 51 ASP C C 176.99 0.10 1 454 . 51 ASP CA C 52.60 0.10 1 455 . 51 ASP CB C 39.90 0.10 1 456 . 51 ASP H H 7.47 0.01 1 457 . 51 ASP HA H 4.34 0.01 1 458 . 51 ASP HB2 H 2.89 0.01 2 459 . 51 ASP HB3 H 2.41 0.02 2 460 . 51 ASP N N 111.79 0.10 1 461 . 52 GLY C C 171.58 0.10 1 462 . 52 GLY CA C 44.83 0.10 1 463 . 52 GLY H H 8.40 0.01 1 464 . 52 GLY HA2 H 3.25 0.01 2 465 . 52 GLY HA3 H 4.07 0.01 2 466 . 52 GLY N N 109.03 0.10 1 467 . 53 MET C C 175.76 0.10 1 468 . 53 MET CA C 56.56 0.10 1 469 . 53 MET CB C 32.31 0.10 1 470 . 53 MET CG C 32.61 0.10 1 471 . 53 MET H H 7.37 0.01 1 472 . 53 MET HA H 4.01 0.01 1 473 . 53 MET HB2 H 2.50 0.01 2 474 . 53 MET HB3 H 2.36 0.01 2 475 . 53 MET HG2 H 2.07 0.01 2 476 . 53 MET HG3 H 1.80 0.01 2 477 . 53 MET N N 117.46 0.10 1 478 . 54 LEU C C 176.25 0.10 5 479 . 54 LEU CA C 55.21 0.10 1 480 . 54 LEU CB C 42.19 0.10 1 481 . 54 LEU CD1 C 24.88 0.10 2 482 . 54 LEU CD2 C 25.84 0.10 2 483 . 54 LEU CG C 26.69 0.10 1 484 . 54 LEU H H 8.58 0.01 1 485 . 54 LEU HA H 4.37 0.01 1 486 . 54 LEU HB2 H 1.75 0.01 2 487 . 54 LEU HB3 H 1.31 0.01 2 488 . 54 LEU HD1 H 0.79 0.01 2 489 . 54 LEU HD2 H 0.68 0.01 2 490 . 54 LEU HG H 1.30 0.01 2 491 . 54 LEU N N 125.39 0.10 1 492 . 55 LEU C C 177.53 0.10 1 493 . 55 LEU CA C 55.75 0.10 1 494 . 55 LEU CB C 42.45 0.10 1 495 . 55 LEU CD1 C 25.42 0.10 2 496 . 55 LEU CD2 C 22.03 0.10 2 497 . 55 LEU CG C 26.47 0.10 1 498 . 55 LEU H H 8.92 0.01 1 499 . 55 LEU HA H 4.29 0.01 1 500 . 55 LEU HB2 H 1.49 0.01 2 501 . 55 LEU HB3 H 1.40 0.01 2 502 . 55 LEU HD1 H 0.79 0.01 1 503 . 55 LEU HD2 H 0.79 0.01 1 504 . 55 LEU HG H 1.62 0.01 2 505 . 55 LEU N N 128.91 0.10 1 506 . 56 ASP C C 179.43 0.10 5 507 . 56 ASP CA C 53.55 0.12 1 508 . 56 ASP CB C 44.65 0.10 1 509 . 56 ASP H H 7.72 0.01 1 510 . 56 ASP HA H 4.69 0.01 1 511 . 56 ASP HB2 H 2.68 0.01 2 512 . 56 ASP HB3 H 2.23 0.01 2 513 . 56 ASP N N 115.16 0.10 1 514 . 57 ILE C C 172.21 0.10 1 515 . 57 ILE CA C 59.56 0.10 1 516 . 57 ILE CB C 40.24 0.10 1 517 . 57 ILE CD1 C 15.00 0.10 1 518 . 57 ILE CG1 C 27.77 0.11 1 519 . 57 ILE CG2 C 14.28 0.10 1 520 . 57 ILE H H 7.90 0.01 1 521 . 57 ILE HA H 5.17 0.01 1 522 . 57 ILE HB H 1.87 0.01 2 523 . 57 ILE HD1 H 0.64 0.01 1 524 . 57 ILE HG12 H 1.35 0.03 2 525 . 57 ILE HG13 H 0.76 0.01 2 526 . 57 ILE HG2 H 0.77 0.03 1 527 . 57 ILE N N 119.29 0.10 1 528 . 58 LYS CA C 52.65 0.10 1 529 . 58 LYS CB C 35.71 0.11 1 530 . 58 LYS CD C 28.93 0.10 1 531 . 58 LYS CE C 41.95 0.10 1 532 . 58 LYS CG C 24.07 0.10 1 533 . 58 LYS H H 8.31 0.01 1 534 . 58 LYS HA H 4.86 0.01 1 535 . 58 LYS HB2 H 1.73 0.01 2 536 . 58 LYS HB3 H 1.64 0.01 2 537 . 58 LYS HD2 H 1.61 0.01 2 538 . 58 LYS HE2 H 2.92 0.01 2 539 . 58 LYS HG2 H 1.32 0.01 2 540 . 58 LYS N N 124.67 0.10 1 541 . 59 PRO C C 176.33 0.10 1 542 . 59 PRO CA C 62.60 0.10 1 543 . 59 PRO CB C 31.67 0.10 1 544 . 59 PRO CD C 50.44 0.10 1 545 . 59 PRO CG C 27.37 0.10 1 546 . 59 PRO HA H 4.71 0.01 1 547 . 59 PRO HB2 H 2.02 0.01 2 548 . 59 PRO HB3 H 1.91 0.02 2 549 . 59 PRO HD2 H 3.69 0.01 2 550 . 59 PRO HD3 H 3.66 0.01 2 551 . 59 PRO HG2 H 2.21 0.01 2 552 . 59 PRO HG3 H 1.72 0.01 2 553 . 60 GLU C C 175.77 0.10 1 554 . 60 GLU CA C 56.01 0.10 1 555 . 60 GLU CB C 31.51 0.13 1 556 . 60 GLU CG C 36.95 0.10 1 557 . 60 GLU H H 9.30 0.01 1 558 . 60 GLU HA H 4.48 0.01 1 559 . 60 GLU HB2 H 1.92 0.01 2 560 . 60 GLU HB3 H 1.58 0.01 2 561 . 60 GLU HG2 H 2.05 0.01 2 562 . 60 GLU N N 123.66 0.10 1 563 . 61 GLY C C 171.78 0.10 1 564 . 61 GLY CA C 45.05 0.10 1 565 . 61 GLY H H 7.58 0.01 1 566 . 61 GLY HA2 H 3.99 0.01 2 567 . 61 GLY HA3 H 4.16 0.01 2 568 . 61 GLY N N 107.03 0.10 1 569 . 62 GLY C C 174.67 0.10 1 570 . 62 GLY CA C 43.80 0.10 1 571 . 62 GLY H H 8.28 0.01 1 572 . 62 GLY HA2 H 3.68 0.01 2 573 . 62 GLY HA3 H 4.82 0.01 2 574 . 62 GLY N N 106.92 0.10 1 575 . 63 ASP CA C 52.66 0.10 1 576 . 63 ASP CB C 43.61 0.10 1 577 . 63 ASP H H 8.36 0.01 1 578 . 63 ASP HA H 4.80 0.01 1 579 . 63 ASP HB2 H 2.87 0.01 2 580 . 63 ASP HB3 H 2.68 0.01 2 581 . 63 ASP N N 122.61 0.10 1 582 . 64 PRO C C 178.96 0.10 1 583 . 64 PRO CA C 65.92 0.10 1 584 . 64 PRO CB C 32.20 0.11 1 585 . 64 PRO CD C 51.19 0.10 1 586 . 64 PRO CG C 27.46 0.11 1 587 . 64 PRO HA H 4.00 0.01 1 588 . 64 PRO HB2 H 2.31 0.01 2 589 . 64 PRO HB3 H 1.97 0.02 2 590 . 64 PRO HD2 H 4.27 0.01 2 591 . 64 PRO HD3 H 3.78 0.01 2 592 . 64 PRO HG2 H 2.14 0.01 2 593 . 64 PRO HG3 H 2.00 0.02 2 594 . 65 ALA C C 180.94 0.10 1 595 . 65 ALA CA C 55.18 0.10 1 596 . 65 ALA CB C 18.04 0.10 1 597 . 65 ALA H H 7.88 0.01 1 598 . 65 ALA HA H 4.18 0.01 1 599 . 65 ALA HB H 1.63 0.01 1 600 . 65 ALA N N 120.97 0.10 1 601 . 66 LEU C C 178.56 0.10 1 602 . 66 LEU CA C 57.53 0.10 1 603 . 66 LEU CB C 40.30 0.11 1 604 . 66 LEU CD1 C 27.06 0.10 2 605 . 66 LEU CD2 C 22.94 0.10 2 606 . 66 LEU CG C 27.77 0.10 1 607 . 66 LEU H H 8.72 0.01 1 608 . 66 LEU HA H 3.43 0.01 1 609 . 66 LEU HB2 H 1.87 0.01 2 610 . 66 LEU HB3 H 1.41 0.01 2 611 . 66 LEU HD1 H 0.82 0.01 2 612 . 66 LEU HD2 H 0.75 0.01 2 613 . 66 LEU HG H 1.29 0.02 2 614 . 66 LEU N N 121.96 0.10 1 615 . 67 CYS C C 176.53 0.10 1 616 . 67 CYS CA C 56.18 0.10 1 617 . 67 CYS CB C 37.62 0.10 1 618 . 67 CYS H H 9.01 0.01 1 619 . 67 CYS HA H 4.44 0.01 1 620 . 67 CYS HB2 H 2.99 0.01 2 621 . 67 CYS HB3 H 2.52 0.01 2 622 . 67 CYS N N 115.22 0.10 1 623 . 68 GLN C C 178.48 0.10 1 624 . 68 GLN CA C 59.13 0.10 1 625 . 68 GLN CB C 28.19 0.10 1 626 . 68 GLN CG C 33.57 0.10 1 627 . 68 GLN H H 7.97 0.01 1 628 . 68 GLN HA H 3.85 0.01 1 629 . 68 GLN HB2 H 2.08 0.01 2 630 . 68 GLN HE21 H 6.72 0.01 2 631 . 68 GLN HE22 H 7.42 0.01 2 632 . 68 GLN HG2 H 2.38 0.01 2 633 . 68 GLN N N 118.56 0.10 1 634 . 68 GLN NE2 N 112.30 0.10 1 635 . 69 ALA C C 180.15 0.10 1 636 . 69 ALA CA C 54.53 0.10 1 637 . 69 ALA CB C 18.57 0.10 1 638 . 69 ALA H H 7.61 0.01 1 639 . 69 ALA HA H 3.99 0.01 1 640 . 69 ALA HB H 1.21 0.01 1 641 . 69 ALA N N 123.24 0.10 1 642 . 70 ALA C C 178.25 0.10 1 643 . 70 ALA CA C 54.48 0.10 1 644 . 70 ALA CB C 17.79 0.10 1 645 . 70 ALA H H 8.97 0.01 1 646 . 70 ALA HA H 3.46 0.01 1 647 . 70 ALA HB H 0.97 0.01 1 648 . 70 ALA N N 122.38 0.10 1 649 . 71 LEU C C 178.34 0.10 1 650 . 71 LEU CA C 58.33 0.10 1 651 . 71 LEU CB C 41.87 0.10 1 652 . 71 LEU CD1 C 25.32 0.10 2 653 . 71 LEU CD2 C 24.57 0.10 2 654 . 71 LEU CG C 26.97 0.10 1 655 . 71 LEU H H 7.94 0.01 1 656 . 71 LEU HA H 3.60 0.01 1 657 . 71 LEU HB2 H 1.68 0.01 2 658 . 71 LEU HB3 H 1.44 0.01 2 659 . 71 LEU HD1 H 0.70 0.01 2 660 . 71 LEU HD2 H 0.64 0.01 2 661 . 71 LEU HG H 1.69 0.01 2 662 . 71 LEU N N 118.44 0.10 1 663 . 72 ALA C C 180.28 0.10 1 664 . 72 ALA CA C 54.70 0.10 1 665 . 72 ALA CB C 17.64 0.10 1 666 . 72 ALA H H 7.02 0.01 1 667 . 72 ALA HA H 3.88 0.01 1 668 . 72 ALA HB H 1.32 0.01 1 669 . 72 ALA N N 119.11 0.10 1 670 . 73 ALA C C 179.57 0.10 5 671 . 73 ALA CA C 54.39 0.10 1 672 . 73 ALA CB C 18.88 0.10 1 673 . 73 ALA H H 7.26 0.01 1 674 . 73 ALA HA H 3.83 0.01 1 675 . 73 ALA HB H 1.14 0.01 1 676 . 73 ALA N N 119.92 0.10 1 677 . 74 ALA C C 178.73 0.10 1 678 . 74 ALA CA C 55.00 0.10 1 679 . 74 ALA CB C 18.23 0.10 1 680 . 74 ALA H H 8.33 0.01 1 681 . 74 ALA HA H 3.63 0.01 1 682 . 74 ALA HB H 1.17 0.01 1 683 . 74 ALA N N 118.28 0.10 1 684 . 75 LYS C C 177.13 0.10 1 685 . 75 LYS CA C 58.41 0.10 1 686 . 75 LYS CB C 32.48 0.10 1 687 . 75 LYS CD C 29.18 0.10 1 688 . 75 LYS CE C 41.90 0.10 1 689 . 75 LYS CG C 25.59 0.12 1 690 . 75 LYS H H 7.16 0.01 1 691 . 75 LYS HA H 3.91 0.01 1 692 . 75 LYS HB2 H 1.86 0.01 2 693 . 75 LYS HB3 H 1.70 0.01 2 694 . 75 LYS HD2 H 1.57 0.01 2 695 . 75 LYS HE2 H 2.83 0.01 2 696 . 75 LYS HG2 H 1.60 0.01 2 697 . 75 LYS HG3 H 1.36 0.01 2 698 . 75 LYS N N 113.56 0.10 1 699 . 76 LEU C C 176.90 0.10 1 700 . 76 LEU CA C 54.21 0.10 1 701 . 76 LEU CB C 43.64 0.10 1 702 . 76 LEU CD1 C 25.49 0.10 2 703 . 76 LEU CD2 C 22.10 0.10 2 704 . 76 LEU CG C 26.24 0.10 1 705 . 76 LEU H H 7.10 0.01 1 706 . 76 LEU HA H 4.33 0.01 1 707 . 76 LEU HB2 H 1.76 0.01 2 708 . 76 LEU HB3 H 1.47 0.02 2 709 . 76 LEU HD1 H 0.90 0.01 2 710 . 76 LEU HD2 H 0.80 0.01 2 711 . 76 LEU HG H 1.69 0.01 2 712 . 76 LEU N N 116.80 0.10 1 713 . 77 ALA C C 176.26 0.10 1 714 . 77 ALA CA C 52.24 0.10 1 715 . 77 ALA CB C 20.02 0.10 1 716 . 77 ALA H H 7.07 0.01 1 717 . 77 ALA HA H 3.93 0.01 1 718 . 77 ALA HB H 1.08 0.01 1 719 . 77 ALA N N 121.65 0.10 1 720 . 78 LYS C C 174.75 0.10 1 721 . 78 LYS CA C 54.26 0.10 1 722 . 78 LYS CB C 31.49 0.10 1 723 . 78 LYS CD C 28.67 0.10 1 724 . 78 LYS CE C 42.09 0.10 1 725 . 78 LYS CG C 24.31 0.10 1 726 . 78 LYS H H 8.43 0.01 1 727 . 78 LYS HA H 4.43 0.01 1 728 . 78 LYS HB2 H 1.67 0.01 2 729 . 78 LYS HB3 H 1.57 0.01 2 730 . 78 LYS HD2 H 1.56 0.01 2 731 . 78 LYS HE2 H 2.89 0.01 2 732 . 78 LYS HG2 H 1.27 0.01 2 733 . 78 LYS HG3 H 1.19 0.01 2 734 . 78 LYS N N 123.24 0.10 1 735 . 79 ILE CA C 58.32 0.10 1 736 . 79 ILE CB C 37.15 0.10 1 737 . 79 ILE CD1 C 11.71 0.10 1 738 . 79 ILE CG1 C 28.44 0.10 1 739 . 79 ILE CG2 C 17.47 0.10 1 740 . 79 ILE H H 8.46 0.01 1 741 . 79 ILE HA H 3.92 0.01 1 742 . 79 ILE HB H 2.20 0.01 2 743 . 79 ILE HD1 H 0.68 0.01 1 744 . 79 ILE HG12 H 1.42 0.01 2 745 . 79 ILE HG13 H 1.01 0.01 2 746 . 79 ILE HG2 H 0.88 0.01 1 747 . 79 ILE N N 129.56 0.10 1 748 . 80 PRO C C 175.09 0.10 1 749 . 80 PRO CA C 61.99 0.10 1 750 . 80 PRO CB C 31.87 0.11 1 751 . 80 PRO CD C 50.54 0.10 1 752 . 80 PRO CG C 27.52 0.10 1 753 . 80 PRO HA H 4.35 0.01 1 754 . 80 PRO HB2 H 2.28 0.01 2 755 . 80 PRO HB3 H 1.86 0.01 2 756 . 80 PRO HD2 H 3.69 0.01 2 757 . 80 PRO HD3 H 3.19 0.01 2 758 . 80 PRO HG2 H 1.84 0.01 2 759 . 81 LYS CA C 54.70 0.10 1 760 . 81 LYS CB C 32.06 0.10 1 761 . 81 LYS CD C 23.82 0.10 1 762 . 81 LYS CE C 41.96 0.10 1 763 . 81 LYS CG C 24.28 0.10 1 764 . 81 LYS H H 8.34 0.01 1 765 . 81 LYS HA H 3.90 0.01 1 766 . 81 LYS HB2 H 1.67 0.01 2 767 . 81 LYS HB3 H 1.54 0.02 2 768 . 81 LYS HD2 H 1.40 0.01 2 769 . 81 LYS HD3 H 1.28 0.01 2 770 . 81 LYS HE2 H 2.86 0.02 2 771 . 81 LYS HG2 H 1.21 0.01 2 772 . 81 LYS N N 122.90 0.10 1 773 . 82 PRO CA C 60.60 0.10 1 774 . 82 PRO CB C 30.53 0.10 1 775 . 82 PRO CD C 49.87 0.10 1 776 . 82 PRO CG C 27.21 0.10 1 777 . 82 PRO HA H 3.65 0.01 1 778 . 82 PRO HB2 H 1.62 0.01 2 779 . 82 PRO HB3 H 1.51 0.01 2 780 . 82 PRO HD2 H 3.49 0.01 2 781 . 82 PRO HG2 H 2.01 0.01 2 782 . 82 PRO HG3 H 1.98 0.01 2 783 . 83 PRO C C 175.17 0.10 1 784 . 83 PRO CA C 63.87 0.10 1 785 . 83 PRO CB C 31.89 0.10 1 786 . 83 PRO CD C 50.75 0.10 1 787 . 83 PRO CG C 26.88 0.10 1 788 . 83 PRO HA H 4.21 0.01 1 789 . 83 PRO HB2 H 2.21 0.01 2 790 . 83 PRO HB3 H 1.93 0.02 2 791 . 83 PRO HD2 H 3.29 0.01 2 792 . 83 PRO HD3 H 2.61 0.01 2 793 . 83 PRO HG2 H 2.10 0.01 2 794 . 83 PRO HG3 H 1.71 0.01 2 795 . 84 SER CA C 56.16 0.10 1 796 . 84 SER CB C 65.97 0.10 1 797 . 84 SER H H 6.73 0.01 1 798 . 84 SER HA H 4.54 0.01 1 799 . 84 SER HB2 H 4.09 0.01 2 800 . 84 SER HB3 H 3.88 0.01 2 801 . 84 SER N N 108.00 0.10 1 802 . 85 GLN C C 177.51 0.10 1 803 . 85 GLN CA C 58.56 0.10 1 804 . 85 GLN CB C 27.67 0.10 1 805 . 85 GLN CG C 33.13 0.10 1 806 . 85 GLN HA H 4.10 0.01 1 807 . 85 GLN HB2 H 2.14 0.01 2 808 . 85 GLN HB3 H 2.02 0.01 2 809 . 85 GLN HG2 H 2.44 0.01 2 810 . 86 ALA C C 180.36 0.10 1 811 . 86 ALA CA C 54.96 0.10 1 812 . 86 ALA CB C 17.97 0.10 1 813 . 86 ALA H H 8.27 0.01 1 814 . 86 ALA HA H 4.04 0.01 1 815 . 86 ALA HB H 1.32 0.01 1 816 . 86 ALA N N 120.28 0.10 1 817 . 87 VAL C C 179.40 0.10 5 818 . 87 VAL CA C 66.26 0.10 1 819 . 87 VAL CB C 31.68 0.10 1 820 . 87 VAL CG1 C 24.03 0.10 2 821 . 87 VAL CG2 C 23.56 0.10 2 822 . 87 VAL H H 7.38 0.01 1 823 . 87 VAL HA H 3.61 0.01 1 824 . 87 VAL HB H 1.69 0.01 2 825 . 87 VAL HG1 H 0.86 0.01 2 826 . 87 VAL HG2 H 0.76 0.01 2 827 . 87 VAL N N 116.41 0.10 1 828 . 88 TYR C C 175.55 0.10 1 829 . 88 TYR CA C 61.43 0.10 1 830 . 88 TYR CB C 37.10 0.10 1 831 . 88 TYR H H 8.02 0.01 1 832 . 88 TYR HA H 3.93 0.01 1 833 . 88 TYR HB2 H 3.14 0.01 2 834 . 88 TYR HB3 H 3.06 0.01 2 835 . 88 TYR N N 121.38 0.10 1 836 . 89 GLU C C 178.67 0.10 1 837 . 89 GLU CA C 59.03 0.10 1 838 . 89 GLU CB C 29.02 0.10 1 839 . 89 GLU CG C 36.01 0.10 1 840 . 89 GLU H H 8.08 0.01 1 841 . 89 GLU HA H 3.31 0.01 1 842 . 89 GLU HB2 H 1.94 0.01 2 843 . 89 GLU HG2 H 2.37 0.01 2 844 . 89 GLU N N 114.60 0.10 1 845 . 90 VAL C C 176.89 0.10 1 846 . 90 VAL CA C 65.27 0.10 1 847 . 90 VAL CB C 31.85 0.12 1 848 . 90 VAL CG1 C 21.89 0.10 2 849 . 90 VAL CG2 C 20.61 0.10 2 850 . 90 VAL H H 6.92 0.01 1 851 . 90 VAL HA H 3.56 0.01 1 852 . 90 VAL HB H 2.09 0.01 2 853 . 90 VAL HG1 H 0.94 0.01 2 854 . 90 VAL HG2 H 0.29 0.01 2 855 . 90 VAL N N 116.50 0.10 1 856 . 91 PHE C C 173.93 0.10 1 857 . 91 PHE CA C 60.57 0.11 1 858 . 91 PHE CB C 39.36 0.10 1 859 . 91 PHE H H 7.42 0.01 1 860 . 91 PHE HA H 4.11 0.01 1 861 . 91 PHE HB2 H 3.51 0.01 2 862 . 91 PHE HB3 H 2.54 0.01 2 863 . 91 PHE N N 115.88 0.10 1 864 . 92 LYS C C 177.13 0.10 1 865 . 92 LYS CA C 58.86 0.10 1 866 . 92 LYS CB C 31.39 0.10 1 867 . 92 LYS CD C 29.57 0.10 1 868 . 92 LYS CE C 41.97 0.10 1 869 . 92 LYS CG C 23.87 0.10 1 870 . 92 LYS H H 7.40 0.01 1 871 . 92 LYS HA H 4.08 0.01 1 872 . 92 LYS HB2 H 1.18 0.01 2 873 . 92 LYS HB3 H 1.52 0.01 2 874 . 92 LYS HD2 H 1.44 0.01 2 875 . 92 LYS HD3 H 1.33 0.01 2 876 . 92 LYS HE2 H 2.81 0.01 2 877 . 92 LYS HE3 H 2.88 0.01 2 878 . 92 LYS HG2 H 1.17 0.01 2 879 . 92 LYS HG3 H 0.98 0.01 2 880 . 92 LYS N N 117.66 0.10 1 881 . 93 ASN C C 173.98 0.10 1 882 . 93 ASN CA C 53.24 0.10 1 883 . 93 ASN CB C 37.99 0.10 1 884 . 93 ASN H H 7.20 0.01 1 885 . 93 ASN HA H 5.06 0.01 1 886 . 93 ASN HB2 H 2.76 0.01 2 887 . 93 ASN HB3 H 2.68 0.01 2 888 . 93 ASN N N 115.13 0.10 1 889 . 94 ALA CA C 50.06 0.10 1 890 . 94 ALA CB C 21.38 0.10 1 891 . 94 ALA H H 8.47 0.01 1 892 . 94 ALA HA H 4.78 0.01 1 893 . 94 ALA HB H 1.11 0.01 1 894 . 94 ALA N N 126.21 0.10 1 895 . 95 PRO C C 175.96 0.10 1 896 . 95 PRO CA C 61.06 0.10 1 897 . 95 PRO CB C 31.40 0.10 1 898 . 95 PRO CD C 49.69 0.10 1 899 . 95 PRO CG C 26.18 0.11 1 900 . 95 PRO HA H 5.27 0.01 1 901 . 95 PRO HB2 H 1.75 0.01 2 902 . 95 PRO HD2 H 3.58 0.02 2 903 . 95 PRO HG2 H 2.05 0.01 2 904 . 95 PRO HG3 H 1.94 0.01 2 905 . 96 LEU C C 174.78 0.10 1 906 . 96 LEU CA C 53.95 0.10 1 907 . 96 LEU CB C 46.03 0.10 1 908 . 96 LEU CD1 C 25.22 0.10 2 909 . 96 LEU CD2 C 25.84 0.10 2 910 . 96 LEU CG C 26.89 0.10 1 911 . 96 LEU H H 9.07 0.01 1 912 . 96 LEU HA H 4.48 0.01 1 913 . 96 LEU HB2 H 1.61 0.01 2 914 . 96 LEU HB3 H 1.40 0.01 2 915 . 96 LEU HD1 H 0.91 0.01 2 916 . 96 LEU HD2 H 0.78 0.01 2 917 . 96 LEU HG H 1.49 0.01 2 918 . 96 LEU N N 122.65 0.10 1 919 . 97 ASP C C 174.40 0.10 1 920 . 97 ASP CA C 53.94 0.10 1 921 . 97 ASP CB C 40.69 0.10 1 922 . 97 ASP H H 8.68 0.01 1 923 . 97 ASP HA H 4.92 0.01 1 924 . 97 ASP HB2 H 2.44 0.01 2 925 . 97 ASP HB3 H 2.26 0.01 2 926 . 97 ASP N N 125.91 0.10 1 927 . 98 PHE C C 172.60 0.10 1 928 . 98 PHE CA C 58.34 0.10 1 929 . 98 PHE CB C 41.52 0.10 1 930 . 98 PHE H H 9.08 0.01 1 931 . 98 PHE HA H 4.36 0.01 1 932 . 98 PHE HB2 H 3.04 0.01 2 933 . 98 PHE HB3 H 2.52 0.01 2 934 . 98 PHE N N 125.81 0.10 1 935 . 99 LYS CA C 52.58 0.10 1 936 . 99 LYS CB C 34.09 0.10 1 937 . 99 LYS CD C 29.39 0.10 1 938 . 99 LYS CE C 41.86 0.10 1 939 . 99 LYS CG C 23.80 0.10 1 940 . 99 LYS H H 7.56 0.01 1 941 . 99 LYS HA H 4.77 0.01 1 942 . 99 LYS HB2 H 1.49 0.01 2 943 . 99 LYS HB3 H 1.39 0.01 2 944 . 99 LYS HD2 H 1.38 0.01 2 945 . 99 LYS HE2 H 2.70 0.01 2 946 . 99 LYS HG2 H 1.10 0.01 2 947 . 99 LYS N N 127.51 0.10 1 948 . 100 PRO C C 175.96 0.10 1 949 . 100 PRO CA C 62.48 0.10 1 950 . 100 PRO CB C 31.92 0.10 1 951 . 100 PRO CD C 50.07 0.10 1 952 . 100 PRO CG C 27.24 0.10 1 953 . 100 PRO HA H 3.90 0.01 1 954 . 100 PRO HB2 H 1.59 0.01 2 955 . 100 PRO HB3 H 1.52 0.01 2 956 . 100 PRO HD2 H 3.70 0.01 2 957 . 100 PRO HD3 H 2.90 0.01 2 958 . 100 PRO HG2 H 1.74 0.01 2 959 . 100 PRO HG3 H 1.39 0.01 2 960 . 101 HIS C C 173.86 0.10 1 961 . 101 HIS CA C 56.02 0.10 1 962 . 101 HIS CB C 30.25 0.11 1 963 . 101 HIS H H 8.95 0.01 1 964 . 101 HIS HA H 4.36 0.01 1 965 . 101 HIS HB2 H 3.01 0.01 2 966 . 101 HIS HB3 H 2.85 0.01 2 967 . 101 HIS N N 120.61 0.10 1 968 . 102 HIS CA C 57.22 0.10 1 969 . 102 HIS CB C 30.21 0.10 1 970 . 102 HIS H H 7.96 0.01 1 971 . 102 HIS HA H 4.31 0.01 1 972 . 102 HIS HB2 H 3.09 0.01 2 973 . 102 HIS HB3 H 2.95 0.01 2 974 . 102 HIS N N 125.48 0.10 1 stop_ save_