data_4819 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; High precision NMR structure of YhhP, a novel Esherichia coli protein implicated in the cell division ; _BMRB_accession_number 4819 _BMRB_flat_file_name bmr4819.str _Entry_type original _Submission_date 2000-09-05 _Accession_date 2000-09-05 _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 Katoh Etsuko . . 2 Hatta Tomohisa . . 3 Shindo Heisaburo . . 4 Yamada H. . . 5 Mizuno T. . . 6 Yamazaki Toshimasa . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 471 "13C chemical shifts" 379 "15N chemical shifts" 72 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-12-07 update BMRB 'delete outlier: 68 THR N 11.74' 2000-12-21 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; High precision NMR structure of YhhP, a novel escherichia coli protein implicated in cell division ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20534887 _PubMed_ID 11080457 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Katoh Etsuko . . 2 Hatta Tomohisa . . 3 Shindo Heisaburo . . 4 Yamada H. . . 5 Mizuno T. . . 6 Yamazaki Toshimasa . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 304 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 219 _Page_last 229 _Year 2000 _Details . save_ ################################## # Molecular system description # ################################## save_system_Yhh _Saveframe_category molecular_system _Mol_system_name 'Yhh monomer' _Abbreviation_common Yhh _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Yhh monomer' $Yhh_monomer stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Yhh_monomer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Yhh _Abbreviation_common Yhh _Molecular_mass . _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 81 _Mol_residue_sequence ; MTDLFSSPDHTLDALGLRCP EPVMMVRKTVRNMQPGETLL IIADDPATTRDIPGFCTFME HELVAKETDGLPYRYLIRKG G ; loop_ _Residue_seq_code _Residue_label 1 MET 2 THR 3 ASP 4 LEU 5 PHE 6 SER 7 SER 8 PRO 9 ASP 10 HIS 11 THR 12 LEU 13 ASP 14 ALA 15 LEU 16 GLY 17 LEU 18 ARG 19 CYS 20 PRO 21 GLU 22 PRO 23 VAL 24 MET 25 MET 26 VAL 27 ARG 28 LYS 29 THR 30 VAL 31 ARG 32 ASN 33 MET 34 GLN 35 PRO 36 GLY 37 GLU 38 THR 39 LEU 40 LEU 41 ILE 42 ILE 43 ALA 44 ASP 45 ASP 46 PRO 47 ALA 48 THR 49 THR 50 ARG 51 ASP 52 ILE 53 PRO 54 GLY 55 PHE 56 CYS 57 THR 58 PHE 59 MET 60 GLU 61 HIS 62 GLU 63 LEU 64 VAL 65 ALA 66 LYS 67 GLU 68 THR 69 ASP 70 GLY 71 LEU 72 PRO 73 TYR 74 ARG 75 TYR 76 LEU 77 ILE 78 ARG 79 LYS 80 GLY 81 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 1DCJ "Solution Structure Of Yhhp, A Novel Escherichia Coli Protein Implicated In The Cell Division" 100.00 81 100.00 100.00 1.41e-51 PDB 3LVJ "Crystal Structure Of E.Coli Iscs-Tusa Complex (Form 1)" 98.77 82 100.00 100.00 6.84e-51 PDB 3LVK "Crystal Structure Of E.Coli Iscs-Tusa Complex (Form 2)" 98.77 82 100.00 100.00 6.84e-51 DBJ BAB37742 "hypothetical protein [Escherichia coli O157:H7 str. Sakai]" 100.00 81 100.00 100.00 1.41e-51 DBJ BAE77823 "conserved hypothetical protein required for cell growth [Escherichia coli str. K-12 substr. W3110]" 100.00 81 100.00 100.00 1.41e-51 DBJ BAG79262 "conserved hypothetical protein [Escherichia coli SE11]" 100.00 81 100.00 100.00 1.41e-51 DBJ BAI27727 "conserved hypothetical protein [Escherichia coli O26:H11 str. 11368]" 100.00 81 100.00 100.00 1.41e-51 DBJ BAI32898 "conserved hypothetical protein [Escherichia coli O103:H2 str. 12009]" 100.00 81 100.00 100.00 1.41e-51 EMBL CAP77921 "Sulfurtransferase tusA [Escherichia coli LF82]" 100.00 81 100.00 100.00 1.41e-51 EMBL CAQ33789 "sulfur transfer protein [Escherichia coli BL21(DE3)]" 100.00 81 100.00 100.00 1.41e-51 EMBL CAQ90921 "sulfurtransferase [Escherichia fergusonii ATCC 35469]" 98.77 81 100.00 100.00 1.12e-50 EMBL CAR00415 "sulfurtransferase [Escherichia coli IAI1]" 100.00 81 100.00 100.00 1.41e-51 EMBL CAR05085 "sulfurtransferase [Escherichia coli S88]" 100.00 81 100.00 100.00 1.41e-51 GB AAB18445 "unnamed protein product [Escherichia coli str. K-12 substr. MG1655]" 100.00 81 100.00 100.00 1.41e-51 GB AAC76495 "mnm(5)-s(2)U34-tRNA 2-thiolation sulfurtransferase [Escherichia coli str. K-12 substr. MG1655]" 100.00 81 100.00 100.00 1.41e-51 GB AAG58579 "orf, hypothetical protein [Escherichia coli O157:H7 str. EDL933]" 100.00 81 100.00 100.00 1.41e-51 GB AAN44947 "conserved hypothetical protein [Shigella flexneri 2a str. 301]" 100.00 81 100.00 100.00 1.41e-51 GB AAN82699 "SirA protein [Escherichia coli CFT073]" 100.00 81 100.00 100.00 1.41e-51 REF NP_290018 "sulfur transfer protein SirA [Escherichia coli O157:H7 str. EDL933]" 100.00 81 100.00 100.00 1.41e-51 REF NP_312346 "sulfur transfer protein SirA [Escherichia coli O157:H7 str. Sakai]" 100.00 81 100.00 100.00 1.41e-51 REF NP_417927 "mnm(5)-s(2)U34-tRNA 2-thiolation sulfurtransferase [Escherichia coli str. K-12 substr. MG1655]" 100.00 81 100.00 100.00 1.41e-51 REF NP_709240 "sulfur transfer protein SirA [Shigella flexneri 2a str. 301]" 100.00 81 100.00 100.00 1.41e-51 REF NP_756125 "sulfur transfer protein SirA [Escherichia coli CFT073]" 100.00 81 100.00 100.00 1.41e-51 SP A7ZT06 "RecName: Full=Sulfurtransferase TusA; AltName: Full=tRNA 2-thiouridine synthesizing protein A [Escherichia coli E24377A]" 100.00 81 100.00 100.00 1.41e-51 SP A8A5S8 "RecName: Full=Sulfurtransferase TusA; AltName: Full=tRNA 2-thiouridine synthesizing protein A [Escherichia coli HS]" 100.00 81 100.00 100.00 1.41e-51 SP B1J0G0 "RecName: Full=Sulfurtransferase TusA; AltName: Full=tRNA 2-thiouridine synthesizing protein A [Escherichia coli ATCC 8739]" 100.00 81 100.00 100.00 1.41e-51 SP B1LID3 "RecName: Full=Sulfurtransferase TusA; AltName: Full=tRNA 2-thiouridine synthesizing protein A [Escherichia coli SMS-3-5]" 100.00 81 98.77 98.77 6.36e-51 SP B1X7S8 "RecName: Full=Sulfurtransferase TusA; AltName: Full=tRNA 2-thiouridine synthesizing protein A [Escherichia coli str. K-12 subst" 100.00 81 100.00 100.00 1.41e-51 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Yhh_monomer E.coli 562 Eubacteria . Escherichia coli 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 $Yhh_monomer 'recombinant technology' . . . . . 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 $Yhh_monomer . 1.0 . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer . _Model . _Field_strength . _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample save_ ####################### # Sample conditions # ####################### save_Ex-cond _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.2 0.1 n/a temperature 298 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 TSP H 1 'methyl protons' ppm 0.00 external indirect cylindrical external_to_the_sample parallel_to_Bo 1 TSP C 13 'methyl protons' ppm 0.00 external indirect cylindrical external_to_the_sample parallel_to_Bo 0.25144581 'liquid ammonia' N 15 nitrogen ppm 24.93 external indirect cylindrical external_to_the_sample parallel_to_Bo 0.10132944 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_na _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample stop_ _Sample_conditions_label $Ex-cond _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Yhh monomer' _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 MET HA H 4.03 . 1 2 . 1 MET HB2 H 2.15 . 2 3 . 1 MET HB3 H 2.11 . 2 4 . 1 MET HG2 H 2.62 . 1 5 . 1 MET HG3 H 2.62 . 1 6 . 1 MET CA C 55.55 . 1 7 . 1 MET CB C 34.06 . 1 8 . 1 MET CG C 31.47 . 1 9 . 2 THR HA H 4.35 . 1 10 . 2 THR HB H 4.15 . 1 11 . 2 THR HG2 H 1.19 . 1 12 . 2 THR C C 175.85 . 1 13 . 2 THR CA C 62.32 . 1 14 . 2 THR CB C 69.90 . 1 15 . 2 THR CG2 C 21.71 . 1 16 . 3 ASP H H 8.59 . 1 17 . 3 ASP HA H 4.77 . 1 18 . 3 ASP HB2 H 2.82 . 1 19 . 3 ASP HB3 H 2.82 . 1 20 . 3 ASP C C 177.12 . 1 21 . 3 ASP CA C 53.64 . 1 22 . 3 ASP CB C 41.47 . 1 23 . 3 ASP CG C 180.24 . 1 24 . 3 ASP N N 123.73 . 1 25 . 4 LEU H H 8.51 . 1 26 . 4 LEU HA H 4.00 . 1 27 . 4 LEU HB2 H 1.18 . 1 28 . 4 LEU HB3 H 1.02 . 1 29 . 4 LEU HG H 1.54 . 1 30 . 4 LEU HD1 H 0.80 . 2 31 . 4 LEU HD2 H 0.75 . 2 32 . 4 LEU C C 177.45 . 1 33 . 4 LEU CA C 56.76 . 1 34 . 4 LEU CB C 42.01 . 1 35 . 4 LEU CG C 26.98 . 1 36 . 4 LEU CD1 C 25.33 . 2 37 . 4 LEU CD2 C 23.06 . 2 38 . 4 LEU N N 123.07 . 1 39 . 5 PHE H H 8.14 . 1 40 . 5 PHE HA H 4.36 . 1 41 . 5 PHE HB2 H 2.99 . 1 42 . 5 PHE HB3 H 3.30 . 1 43 . 5 PHE HD1 H 7.15 . 1 44 . 5 PHE HD2 H 7.15 . 1 45 . 5 PHE HE1 H 7.04 . 1 46 . 5 PHE HE2 H 7.04 . 1 47 . 5 PHE HZ H 6.73 . 1 48 . 5 PHE C C 175.86 . 1 49 . 5 PHE CA C 58.27 . 1 50 . 5 PHE CB C 39.98 . 1 51 . 5 PHE CD1 C 131.39 . 1 52 . 5 PHE CD2 C 131.39 . 1 53 . 5 PHE CE1 C 131.09 . 1 54 . 5 PHE CE2 C 131.09 . 1 55 . 5 PHE CZ C 129.13 . 1 56 . 5 PHE N N 114.67 . 1 57 . 6 SER H H 7.38 . 1 58 . 6 SER HA H 4.30 . 1 59 . 6 SER HB2 H 3.97 . 1 60 . 6 SER HB3 H 3.97 . 1 61 . 6 SER C C 174.67 . 1 62 . 6 SER CA C 60.10 . 1 63 . 6 SER CB C 64.37 . 1 64 . 6 SER N N 112.76 . 1 65 . 7 SER H H 8.58 . 1 66 . 7 SER HA H 4.65 . 1 67 . 7 SER HB2 H 3.86 . 2 68 . 7 SER HB3 H 3.73 . 2 69 . 7 SER C C 171.86 . 1 70 . 7 SER CA C 56.46 . 1 71 . 7 SER CB C 63.27 . 1 72 . 7 SER N N 115.93 . 1 73 . 8 PRO HA H 4.60 . 1 74 . 8 PRO HB2 H 2.19 . 1 75 . 8 PRO HB3 H 1.87 . 1 76 . 8 PRO HG2 H 1.97 . 1 77 . 8 PRO HG3 H 1.86 . 1 78 . 8 PRO HD2 H 3.49 . 1 79 . 8 PRO HD3 H 3.66 . 1 80 . 8 PRO C C 177.49 . 1 81 . 8 PRO CA C 62.22 . 1 82 . 8 PRO CB C 31.91 . 1 83 . 8 PRO CG C 27.25 . 1 84 . 8 PRO CD C 49.60 . 1 85 . 9 ASP H H 8.29 . 1 86 . 9 ASP HA H 4.34 . 1 87 . 9 ASP HB2 H 3.51 . 1 88 . 9 ASP HB3 H 2.40 . 1 89 . 9 ASP C C 173.44 . 1 90 . 9 ASP CA C 58.31 . 1 91 . 9 ASP CB C 41.68 . 1 92 . 9 ASP CG C 179.92 . 1 93 . 9 ASP N N 121.75 . 1 94 . 10 HIS H H 8.08 . 1 95 . 10 HIS HA H 4.84 . 1 96 . 10 HIS HB2 H 2.92 . 1 97 . 10 HIS HB3 H 3.03 . 1 98 . 10 HIS HD2 H 6.88 . 1 99 . 10 HIS HE1 H 7.95 . 1 100 . 10 HIS C C 174.21 . 1 101 . 10 HIS CA C 54.79 . 1 102 . 10 HIS CB C 34.98 . 1 103 . 10 HIS CD2 C 118.82 . 1 104 . 10 HIS CE1 C 138.72 . 1 105 . 10 HIS N N 115.07 . 1 106 . 11 THR H H 8.90 . 1 107 . 11 THR HA H 5.29 . 1 108 . 11 THR HB H 3.99 . 1 109 . 11 THR HG2 H 1.16 . 1 110 . 11 THR C C 172.83 . 1 111 . 11 THR CA C 62.38 . 1 112 . 11 THR CB C 72.02 . 1 113 . 11 THR CG2 C 21.38 . 1 114 . 11 THR N N 116.94 . 1 115 . 12 LEU H H 9.67 . 1 116 . 12 LEU HA H 4.72 . 1 117 . 12 LEU HB2 H 1.45 . 1 118 . 12 LEU HB3 H 1.81 . 1 119 . 12 LEU HG H 1.50 . 1 120 . 12 LEU HD1 H 0.92 . 1 121 . 12 LEU HD2 H 0.82 . 1 122 . 12 LEU C C 173.29 . 1 123 . 12 LEU CA C 53.90 . 1 124 . 12 LEU CB C 45.94 . 1 125 . 12 LEU CG C 27.77 . 1 126 . 12 LEU CD1 C 23.80 . 1 127 . 12 LEU CD2 C 26.50 . 1 128 . 12 LEU N N 128.22 . 1 129 . 13 ASP H H 8.86 . 1 130 . 13 ASP HA H 4.74 . 1 131 . 13 ASP HB2 H 2.50 . 1 132 . 13 ASP HB3 H 3.02 . 1 133 . 13 ASP C C 175.30 . 1 134 . 13 ASP CA C 53.67 . 1 135 . 13 ASP CB C 40.51 . 1 136 . 13 ASP CG C 178.96 . 1 137 . 13 ASP N N 126.51 . 1 138 . 14 ALA H H 9.07 . 1 139 . 14 ALA HA H 4.79 . 1 140 . 14 ALA HB H 1.40 . 1 141 . 14 ALA C C 178.52 . 1 142 . 14 ALA CA C 49.64 . 1 143 . 14 ALA CB C 17.88 . 1 144 . 14 ALA N N 127.98 . 1 145 . 15 LEU H H 8.89 . 1 146 . 15 LEU HA H 4.01 . 1 147 . 15 LEU HB2 H 2.10 . 1 148 . 15 LEU HB3 H 1.28 . 1 149 . 15 LEU HG H 1.64 . 1 150 . 15 LEU HD1 H 0.90 . 1 151 . 15 LEU HD2 H 0.70 . 1 152 . 15 LEU C C 178.81 . 1 153 . 15 LEU CA C 57.79 . 1 154 . 15 LEU CB C 40.61 . 1 155 . 15 LEU CG C 26.98 . 1 156 . 15 LEU CD1 C 25.41 . 1 157 . 15 LEU CD2 C 23.29 . 1 158 . 15 LEU N N 125.09 . 1 159 . 16 GLY H H 10.26 . 1 160 . 16 GLY HA2 H 3.76 . 1 161 . 16 GLY HA3 H 4.32 . 1 162 . 16 GLY C C 174.48 . 1 163 . 16 GLY CA C 45.48 . 1 164 . 16 GLY N N 113.55 . 1 165 . 17 LEU H H 7.44 . 1 166 . 17 LEU HA H 4.70 . 1 167 . 17 LEU HB2 H 1.96 . 1 168 . 17 LEU HB3 H 1.26 . 1 169 . 17 LEU HG H 1.58 . 1 170 . 17 LEU HD1 H 0.87 . 1 171 . 17 LEU HD2 H 0.89 . 1 172 . 17 LEU C C 178.32 . 1 173 . 17 LEU CA C 54.15 . 1 174 . 17 LEU CB C 42.38 . 1 175 . 17 LEU CG C 27.08 . 1 176 . 17 LEU CD1 C 22.02 . 1 177 . 17 LEU CD2 C 25.82 . 1 178 . 17 LEU N N 118.12 . 1 179 . 18 ARG H H 9.50 . 1 180 . 18 ARG HA H 4.92 . 1 181 . 18 ARG HB2 H 1.91 . 1 182 . 18 ARG HB3 H 1.83 . 1 183 . 18 ARG HG2 H 1.83 . 2 184 . 18 ARG HG3 H 1.55 . 2 185 . 18 ARG HD2 H 3.30 . 1 186 . 18 ARG HD3 H 3.30 . 1 187 . 18 ARG C C 175.84 . 1 188 . 18 ARG CA C 53.88 . 1 189 . 18 ARG CB C 33.28 . 1 190 . 18 ARG CG C 26.95 . 1 191 . 18 ARG CD C 43.17 . 1 192 . 18 ARG N N 123.35 . 1 193 . 19 CYS H H 8.95 . 1 194 . 19 CYS HA H 4.58 . 1 195 . 19 CYS HB2 H 3.11 . 1 196 . 19 CYS HB3 H 2.96 . 1 197 . 19 CYS C C 174.75 . 1 198 . 19 CYS CA C 57.74 . 1 199 . 19 CYS CB C 27.36 . 1 200 . 19 CYS N N 124.56 . 1 201 . 20 PRO HA H 5.18 . 1 202 . 20 PRO HB2 H 2.43 . 1 203 . 20 PRO HB3 H 2.21 . 1 204 . 20 PRO HG2 H 1.79 . 1 205 . 20 PRO HG3 H 2.07 . 1 206 . 20 PRO HD2 H 3.65 . 1 207 . 20 PRO HD3 H 3.65 . 1 208 . 20 PRO C C 176.55 . 1 209 . 20 PRO CA C 65.27 . 1 210 . 20 PRO CB C 34.17 . 1 211 . 20 PRO CG C 24.63 . 1 212 . 20 PRO CD C 50.01 . 1 213 . 21 GLU H H 8.87 . 1 214 . 21 GLU HA H 4.28 . 1 215 . 21 GLU HB2 H 2.27 . 1 216 . 21 GLU HB3 H 2.09 . 1 217 . 21 GLU HG2 H 2.55 . 2 218 . 21 GLU HG3 H 2.35 . 2 219 . 21 GLU C C 175.56 . 1 220 . 21 GLU CA C 61.15 . 1 221 . 21 GLU CB C 28.93 . 1 222 . 21 GLU CG C 37.05 . 1 223 . 21 GLU CD C 182.57 . 1 224 . 21 GLU N N 123.89 . 1 225 . 22 PRO HA H 4.02 . 1 226 . 22 PRO HB2 H 1.74 . 1 227 . 22 PRO HB3 H 1.94 . 1 228 . 22 PRO HG2 H 2.40 . 1 229 . 22 PRO HG3 H 1.83 . 1 230 . 22 PRO HD2 H 3.79 . 1 231 . 22 PRO HD3 H 3.38 . 1 232 . 22 PRO C C 177.74 . 1 233 . 22 PRO CA C 67.72 . 1 234 . 22 PRO CB C 31.22 . 1 235 . 22 PRO CG C 28.80 . 1 236 . 22 PRO CD C 49.68 . 1 237 . 23 VAL H H 8.55 . 1 238 . 23 VAL HA H 3.14 . 1 239 . 23 VAL HB H 1.97 . 1 240 . 23 VAL HG1 H 0.75 . 1 241 . 23 VAL HG2 H 0.81 . 1 242 . 23 VAL C C 177.29 . 1 243 . 23 VAL CA C 67.07 . 1 244 . 23 VAL CB C 30.70 . 1 245 . 23 VAL CG1 C 21.83 . 1 246 . 23 VAL CG2 C 25.29 . 1 247 . 23 VAL N N 115.71 . 1 248 . 24 MET H H 7.75 . 1 249 . 24 MET HA H 4.06 . 1 250 . 24 MET HB2 H 2.23 . 1 251 . 24 MET HB3 H 2.75 . 1 252 . 24 MET HG2 H 2.60 . 1 253 . 24 MET HG3 H 2.19 . 1 254 . 24 MET C C 179.53 . 1 255 . 24 MET CA C 59.50 . 1 256 . 24 MET CB C 32.21 . 1 257 . 24 MET CG C 32.21 . 1 258 . 24 MET N N 119.54 . 1 259 . 25 MET H H 8.22 . 1 260 . 25 MET HA H 4.37 . 1 261 . 25 MET HB2 H 2.18 . 1 262 . 25 MET HB3 H 2.02 . 1 263 . 25 MET HG2 H 2.66 . 1 264 . 25 MET HG3 H 2.66 . 1 265 . 25 MET C C 180.02 . 1 266 . 25 MET CA C 57.31 . 1 267 . 25 MET CB C 32.00 . 1 268 . 25 MET CG C 32.45 . 1 269 . 25 MET N N 117.51 . 1 270 . 26 VAL H H 8.52 . 1 271 . 26 VAL HA H 3.15 . 1 272 . 26 VAL HB H 1.76 . 1 273 . 26 VAL HG1 H 0.32 . 1 274 . 26 VAL HG2 H 0.78 . 1 275 . 26 VAL C C 176.84 . 1 276 . 26 VAL CA C 67.52 . 1 277 . 26 VAL CB C 31.32 . 1 278 . 26 VAL CG1 C 22.55 . 1 279 . 26 VAL CG2 C 24.33 . 1 280 . 26 VAL N N 124.20 . 1 281 . 27 ARG H H 8.68 . 1 282 . 27 ARG HA H 3.79 . 1 283 . 27 ARG HB2 H 1.98 . 2 284 . 27 ARG HB3 H 1.89 . 2 285 . 27 ARG HG2 H 1.85 . 2 286 . 27 ARG HG3 H 1.73 . 2 287 . 27 ARG HD2 H 3.32 . 1 288 . 27 ARG HD3 H 3.32 . 1 289 . 27 ARG C C 179.03 . 1 290 . 27 ARG CA C 60.51 . 1 291 . 27 ARG CB C 30.46 . 1 292 . 27 ARG CG C 28.27 . 1 293 . 27 ARG CD C 44.03 . 1 294 . 27 ARG N N 119.39 . 1 295 . 28 LYS H H 7.53 . 1 296 . 28 LYS HA H 4.00 . 1 297 . 28 LYS HB2 H 1.95 . 1 298 . 28 LYS HB3 H 1.95 . 1 299 . 28 LYS HG2 H 1.61 . 2 300 . 28 LYS HG3 H 1.48 . 2 301 . 28 LYS HD2 H 1.72 . 1 302 . 28 LYS HD3 H 1.72 . 1 303 . 28 LYS HE2 H 3.01 . 1 304 . 28 LYS HE3 H 3.01 . 1 305 . 28 LYS C C 178.14 . 1 306 . 28 LYS CA C 59.66 . 1 307 . 28 LYS CB C 32.88 . 1 308 . 28 LYS CG C 25.19 . 1 309 . 28 LYS CD C 29.89 . 1 310 . 28 LYS CE C 42.17 . 1 311 . 28 LYS N N 117.24 . 1 312 . 29 THR H H 7.80 . 1 313 . 29 THR HA H 3.93 . 1 314 . 29 THR HB H 4.07 . 1 315 . 29 THR HG2 H 1.14 . 1 316 . 29 THR C C 177.12 . 1 317 . 29 THR CA C 67.17 . 1 318 . 29 THR CB C 68.66 . 1 319 . 29 THR CG2 C 21.88 . 1 320 . 29 THR N N 116.22 . 1 321 . 30 VAL H H 8.89 . 1 322 . 30 VAL HA H 4.06 . 1 323 . 30 VAL HB H 2.06 . 1 324 . 30 VAL HG1 H 0.74 . 1 325 . 30 VAL HG2 H 0.89 . 1 326 . 30 VAL C C 178.83 . 1 327 . 30 VAL CA C 64.99 . 1 328 . 30 VAL CB C 31.70 . 1 329 . 30 VAL CG1 C 21.58 . 1 330 . 30 VAL CG2 C 23.70 . 1 331 . 30 VAL N N 120.41 . 1 332 . 31 ARG H H 7.47 . 1 333 . 31 ARG HA H 4.19 . 1 334 . 31 ARG HB2 H 2.01 . 1 335 . 31 ARG HB3 H 1.93 . 1 336 . 31 ARG HG2 H 1.73 . 2 337 . 31 ARG HG3 H 1.87 . 2 338 . 31 ARG HD2 H 3.29 . 1 339 . 31 ARG HD3 H 3.29 . 1 340 . 31 ARG C C 176.76 . 1 341 . 31 ARG CA C 59.41 . 1 342 . 31 ARG CB C 30.05 . 1 343 . 31 ARG CG C 27.37 . 1 344 . 31 ARG CD C 43.72 . 1 345 . 31 ARG N N 119.95 . 1 346 . 32 ASN H H 7.04 . 1 347 . 32 ASN HA H 4.86 . 1 348 . 32 ASN HB2 H 3.06 . 1 349 . 32 ASN HB3 H 2.74 . 1 350 . 32 ASN HD21 H 7.64 . 2 351 . 32 ASN HD22 H 6.92 . 2 352 . 32 ASN C C 175.35 . 1 353 . 32 ASN CA C 53.22 . 1 354 . 32 ASN CB C 39.66 . 1 355 . 32 ASN CG C 177.04 . 1 356 . 32 ASN N N 113.19 . 1 357 . 32 ASN ND2 N 112.76 . 1 358 . 33 MET H H 7.20 . 1 359 . 33 MET HA H 4.29 . 1 360 . 33 MET HB2 H 1.95 . 1 361 . 33 MET HB3 H 2.34 . 1 362 . 33 MET HG2 H 1.81 . 1 363 . 33 MET HG3 H 2.31 . 1 364 . 33 MET HE H 1.85 . 1 365 . 33 MET C C 175.84 . 1 366 . 33 MET CA C 55.78 . 1 367 . 33 MET CB C 36.04 . 1 368 . 33 MET CG C 29.29 . 1 369 . 33 MET CE C 15.50 . 1 370 . 33 MET N N 118.70 . 1 371 . 34 GLN H H 8.91 . 1 372 . 34 GLN HA H 4.81 . 1 373 . 34 GLN HB2 H 1.69 . 1 374 . 34 GLN HB3 H 2.26 . 1 375 . 34 GLN HG2 H 2.55 . 2 376 . 34 GLN HG3 H 2.45 . 2 377 . 34 GLN HE21 H 7.68 . 2 378 . 34 GLN HE22 H 6.89 . 2 379 . 34 GLN C C 174.38 . 1 380 . 34 GLN CA C 53.12 . 1 381 . 34 GLN CB C 28.21 . 1 382 . 34 GLN CG C 33.76 . 1 383 . 34 GLN CD C 180.46 . 1 384 . 34 GLN N N 121.09 . 1 385 . 34 GLN NE2 N 113.10 . 1 386 . 35 PRO HA H 3.93 . 1 387 . 35 PRO HB2 H 1.91 . 1 388 . 35 PRO HB3 H 2.31 . 1 389 . 35 PRO HG2 H 2.29 . 1 390 . 35 PRO HG3 H 2.03 . 1 391 . 35 PRO HD2 H 3.71 . 1 392 . 35 PRO HD3 H 3.98 . 1 393 . 35 PRO C C 177.38 . 1 394 . 35 PRO CA C 64.47 . 1 395 . 35 PRO CB C 31.87 . 1 396 . 35 PRO CG C 28.53 . 1 397 . 35 PRO CD C 50.94 . 1 398 . 36 GLY H H 8.95 . 1 399 . 36 GLY HA2 H 4.46 . 2 400 . 36 GLY HA3 H 3.59 . 2 401 . 36 GLY C C 174.69 . 1 402 . 36 GLY CA C 45.59 . 1 403 . 36 GLY N N 112.59 . 1 404 . 37 GLU H H 7.92 . 1 405 . 37 GLU HA H 4.74 . 1 406 . 37 GLU HB2 H 2.60 . 1 407 . 37 GLU HB3 H 2.11 . 1 408 . 37 GLU HG2 H 2.49 . 2 409 . 37 GLU HG3 H 2.31 . 2 410 . 37 GLU C C 176.66 . 1 411 . 37 GLU CA C 56.56 . 1 412 . 37 GLU CB C 33.02 . 1 413 . 37 GLU CG C 38.84 . 1 414 . 37 GLU CD C 184.83 . 1 415 . 37 GLU N N 119.19 . 1 416 . 38 THR H H 9.92 . 1 417 . 38 THR HA H 5.62 . 1 418 . 38 THR HB H 4.18 . 1 419 . 38 THR HG2 H 1.22 . 1 420 . 38 THR C C 174.58 . 1 421 . 38 THR CA C 59.09 . 1 422 . 38 THR CB C 72.81 . 1 423 . 38 THR CG2 C 21.85 . 1 424 . 38 THR N N 109.40 . 1 425 . 39 LEU H H 9.17 . 1 426 . 39 LEU HA H 5.20 . 1 427 . 39 LEU HB2 H 1.48 . 1 428 . 39 LEU HB3 H 1.60 . 1 429 . 39 LEU HG H 1.38 . 1 430 . 39 LEU HD1 H 0.86 . 1 431 . 39 LEU HD2 H 0.75 . 1 432 . 39 LEU C C 174.52 . 1 433 . 39 LEU CA C 52.66 . 1 434 . 39 LEU CB C 45.92 . 1 435 . 39 LEU CG C 27.97 . 1 436 . 39 LEU CD1 C 24.50 . 1 437 . 39 LEU CD2 C 26.96 . 1 438 . 39 LEU N N 121.91 . 1 439 . 40 LEU H H 9.01 . 1 440 . 40 LEU HA H 5.51 . 1 441 . 40 LEU HB2 H 1.37 . 1 442 . 40 LEU HB3 H 2.20 . 1 443 . 40 LEU HG H 1.57 . 1 444 . 40 LEU HD1 H 1.08 . 1 445 . 40 LEU HD2 H 1.12 . 1 446 . 40 LEU C C 174.50 . 1 447 . 40 LEU CA C 53.55 . 1 448 . 40 LEU CB C 44.44 . 1 449 . 40 LEU CG C 28.23 . 1 450 . 40 LEU CD1 C 25.40 . 1 451 . 40 LEU CD2 C 26.84 . 1 452 . 40 LEU N N 129.08 . 1 453 . 41 ILE H H 9.78 . 1 454 . 41 ILE HA H 5.15 . 1 455 . 41 ILE HB H 1.93 . 1 456 . 41 ILE HG12 H 1.69 . 1 457 . 41 ILE HG13 H 1.03 . 1 458 . 41 ILE HG2 H 0.89 . 1 459 . 41 ILE HD1 H 0.87 . 1 460 . 41 ILE C C 174.45 . 1 461 . 41 ILE CA C 60.49 . 1 462 . 41 ILE CB C 41.55 . 1 463 . 41 ILE CG1 C 28.80 . 1 464 . 41 ILE CG2 C 18.51 . 1 465 . 41 ILE CD1 C 17.45 . 1 466 . 41 ILE N N 126.96 . 1 467 . 42 ILE H H 8.33 . 1 468 . 42 ILE HA H 5.11 . 1 469 . 42 ILE HB H 1.85 . 1 470 . 42 ILE HG12 H 1.57 . 1 471 . 42 ILE HG13 H 1.07 . 1 472 . 42 ILE HG2 H 0.95 . 1 473 . 42 ILE HD1 H 0.83 . 1 474 . 42 ILE C C 174.96 . 1 475 . 42 ILE CA C 60.15 . 1 476 . 42 ILE CB C 40.34 . 1 477 . 42 ILE CG1 C 27.93 . 1 478 . 42 ILE CG2 C 18.45 . 1 479 . 42 ILE CD1 C 13.97 . 1 480 . 42 ILE N N 126.36 . 1 481 . 43 ALA H H 9.30 . 1 482 . 43 ALA HA H 4.61 . 1 483 . 43 ALA HB H 1.73 . 1 484 . 43 ALA C C 174.01 . 1 485 . 43 ALA CA C 51.58 . 1 486 . 43 ALA CB C 24.64 . 1 487 . 43 ALA N N 126.30 . 1 488 . 44 ASP H H 8.64 . 1 489 . 44 ASP HA H 4.64 . 1 490 . 44 ASP HB2 H 3.07 . 1 491 . 44 ASP HB3 H 2.45 . 1 492 . 44 ASP C C 174.66 . 1 493 . 44 ASP CA C 52.84 . 1 494 . 44 ASP CB C 40.49 . 1 495 . 44 ASP CG C 181.17 . 1 496 . 44 ASP N N 114.86 . 1 497 . 45 ASP H H 7.44 . 1 498 . 45 ASP HA H 5.10 . 1 499 . 45 ASP HB2 H 3.69 . 1 500 . 45 ASP HB3 H 3.03 . 1 501 . 45 ASP C C 176.68 . 1 502 . 45 ASP CA C 51.46 . 1 503 . 45 ASP CB C 43.49 . 1 504 . 45 ASP CG C 178.58 . 1 505 . 45 ASP N N 119.81 . 1 506 . 46 PRO HA H 4.55 . 1 507 . 46 PRO HB2 H 2.18 . 1 508 . 46 PRO HB3 H 2.65 . 1 509 . 46 PRO HG2 H 2.32 . 2 510 . 46 PRO HG3 H 2.92 . 2 511 . 46 PRO HD2 H 4.36 . 1 512 . 46 PRO HD3 H 4.54 . 1 513 . 46 PRO C C 177.99 . 1 514 . 46 PRO CA C 65.51 . 1 515 . 46 PRO CB C 32.38 . 1 516 . 46 PRO CG C 27.57 . 1 517 . 46 PRO CD C 52.34 . 1 518 . 47 ALA H H 8.41 . 1 519 . 47 ALA HA H 4.29 . 1 520 . 47 ALA HB H 1.71 . 1 521 . 47 ALA C C 180.76 . 1 522 . 47 ALA CA C 54.72 . 1 523 . 47 ALA CB C 17.90 . 1 524 . 47 ALA N N 119.72 . 1 525 . 48 THR H H 8.49 . 1 526 . 48 THR HA H 3.75 . 1 527 . 48 THR HB H 3.96 . 1 528 . 48 THR HG2 H 1.53 . 1 529 . 48 THR C C 175.60 . 1 530 . 48 THR CA C 66.15 . 1 531 . 48 THR CB C 70.24 . 1 532 . 48 THR CG2 C 23.16 . 1 533 . 48 THR N N 109.18 . 1 534 . 49 THR H H 7.39 . 1 535 . 49 THR HA H 4.20 . 1 536 . 49 THR HB H 4.26 . 1 537 . 49 THR HG2 H 0.95 . 1 538 . 49 THR C C 175.60 . 1 539 . 49 THR CA C 65.21 . 1 540 . 49 THR CB C 68.51 . 1 541 . 49 THR CG2 C 20.65 . 1 542 . 49 THR N N 111.61 . 1 543 . 50 ARG H H 6.99 . 1 544 . 50 ARG HA H 4.59 . 1 545 . 50 ARG HB2 H 1.89 . 1 546 . 50 ARG HB3 H 1.96 . 1 547 . 50 ARG HG2 H 1.75 . 2 548 . 50 ARG HG3 H 1.57 . 2 549 . 50 ARG HD2 H 3.27 . 1 550 . 50 ARG HD3 H 3.27 . 1 551 . 50 ARG C C 179.35 . 1 552 . 50 ARG CA C 57.06 . 1 553 . 50 ARG CB C 31.95 . 1 554 . 50 ARG CG C 27.21 . 1 555 . 50 ARG CD C 43.27 . 1 556 . 50 ARG N N 118.33 . 1 557 . 51 ASP H H 8.81 . 1 558 . 51 ASP HA H 4.48 . 1 559 . 51 ASP HB2 H 2.28 . 1 560 . 51 ASP HB3 H 2.63 . 1 561 . 51 ASP C C 179.22 . 1 562 . 51 ASP CA C 57.94 . 1 563 . 51 ASP CB C 41.06 . 1 564 . 51 ASP CG C 177.02 . 1 565 . 51 ASP N N 120.52 . 1 566 . 52 ILE H H 8.55 . 1 567 . 52 ILE HA H 4.11 . 1 568 . 52 ILE HB H 1.51 . 1 569 . 52 ILE HG12 H 0.85 . 1 570 . 52 ILE HG13 H 0.85 . 1 571 . 52 ILE HG2 H 0.46 . 1 572 . 52 ILE HD1 H 0.34 . 1 573 . 52 ILE C C 175.50 . 1 574 . 52 ILE CA C 65.38 . 1 575 . 52 ILE CB C 32.55 . 1 576 . 52 ILE CG1 C 28.96 . 1 577 . 52 ILE CG2 C 17.47 . 1 578 . 52 ILE CD1 C 10.25 . 1 579 . 52 ILE N N 117.02 . 1 580 . 53 PRO HA H 4.27 . 1 581 . 53 PRO HB2 H 1.89 . 1 582 . 53 PRO HB3 H 2.51 . 1 583 . 53 PRO HG2 H 2.47 . 1 584 . 53 PRO HG3 H 1.74 . 1 585 . 53 PRO HD2 H 3.30 . 1 586 . 53 PRO HD3 H 3.51 . 1 587 . 53 PRO C C 179.07 . 1 588 . 53 PRO CA C 66.74 . 1 589 . 53 PRO CB C 30.95 . 1 590 . 53 PRO CG C 28.79 . 1 591 . 53 PRO CD C 50.02 . 1 592 . 54 GLY H H 7.74 . 1 593 . 54 GLY HA2 H 3.82 . 1 594 . 54 GLY HA3 H 3.94 . 1 595 . 54 GLY C C 175.28 . 1 596 . 54 GLY CA C 47.50 . 1 597 . 54 GLY N N 102.91 . 1 598 . 55 PHE H H 8.02 . 1 599 . 55 PHE HA H 4.34 . 1 600 . 55 PHE HB2 H 3.30 . 1 601 . 55 PHE HB3 H 3.43 . 1 602 . 55 PHE HD1 H 7.27 . 1 603 . 55 PHE HD2 H 7.27 . 1 604 . 55 PHE HE1 H 7.18 . 1 605 . 55 PHE HE2 H 7.18 . 1 606 . 55 PHE HZ H 7.20 . 1 607 . 55 PHE C C 176.68 . 1 608 . 55 PHE CA C 61.33 . 1 609 . 55 PHE CB C 39.19 . 1 610 . 55 PHE CD1 C 131.87 . 1 611 . 55 PHE CD2 C 131.87 . 1 612 . 55 PHE CE1 C 131.49 . 1 613 . 55 PHE CE2 C 131.49 . 1 614 . 55 PHE CZ C 128.93 . 1 615 . 55 PHE N N 123.66 . 1 616 . 56 CYS H H 7.96 . 1 617 . 56 CYS HA H 3.76 . 1 618 . 56 CYS HB2 H 3.26 . 1 619 . 56 CYS HB3 H 3.07 . 1 620 . 56 CYS C C 176.61 . 1 621 . 56 CYS CA C 65.16 . 1 622 . 56 CYS CB C 26.17 . 1 623 . 56 CYS N N 116.45 . 1 624 . 57 THR H H 8.29 . 1 625 . 57 THR HA H 3.98 . 1 626 . 57 THR HB H 4.14 . 1 627 . 57 THR HG2 H 1.18 . 1 628 . 57 THR C C 176.83 . 1 629 . 57 THR CA C 66.16 . 1 630 . 57 THR CB C 68.95 . 1 631 . 57 THR CG2 C 21.95 . 1 632 . 57 THR N N 114.73 . 1 633 . 58 PHE H H 8.20 . 1 634 . 58 PHE HA H 4.37 . 1 635 . 58 PHE HB2 H 3.20 . 1 636 . 58 PHE HB3 H 3.04 . 1 637 . 58 PHE HD1 H 7.24 . 1 638 . 58 PHE HD2 H 7.24 . 1 639 . 58 PHE HE1 H 7.38 . 1 640 . 58 PHE HE2 H 7.38 . 1 641 . 58 PHE HZ H 7.33 . 1 642 . 58 PHE C C 176.97 . 1 643 . 58 PHE CA C 60.55 . 1 644 . 58 PHE CB C 39.56 . 1 645 . 58 PHE CD1 C 131.55 . 1 646 . 58 PHE CD2 C 131.55 . 1 647 . 58 PHE CE1 C 131.65 . 1 648 . 58 PHE CE2 C 131.65 . 1 649 . 58 PHE CZ C 129.98 . 1 650 . 58 PHE N N 120.36 . 1 651 . 59 MET H H 7.79 . 1 652 . 59 MET HA H 4.32 . 1 653 . 59 MET HB2 H 1.23 . 1 654 . 59 MET HB3 H 1.67 . 1 655 . 59 MET HG2 H 2.24 . 2 656 . 59 MET HG3 H 2.12 . 2 657 . 59 MET C C 174.14 . 1 658 . 59 MET CA C 53.53 . 1 659 . 59 MET CB C 30.84 . 1 660 . 59 MET CG C 32.68 . 1 661 . 59 MET N N 112.87 . 1 662 . 60 GLU H H 7.36 . 1 663 . 60 GLU HA H 3.75 . 1 664 . 60 GLU HB2 H 2.02 . 2 665 . 60 GLU HB3 H 1.99 . 2 666 . 60 GLU HG2 H 2.02 . 2 667 . 60 GLU HG3 H 1.95 . 2 668 . 60 GLU C C 175.53 . 1 669 . 60 GLU CA C 57.59 . 1 670 . 60 GLU CB C 26.44 . 1 671 . 60 GLU CG C 36.94 . 1 672 . 60 GLU CD C 185.05 . 1 673 . 60 GLU N N 113.48 . 1 674 . 61 HIS H H 8.04 . 1 675 . 61 HIS HA H 5.16 . 1 676 . 61 HIS HB2 H 2.49 . 1 677 . 61 HIS HB3 H 3.27 . 1 678 . 61 HIS HD2 H 6.28 . 1 679 . 61 HIS HE1 H 7.73 . 1 680 . 61 HIS C C 174.81 . 1 681 . 61 HIS CA C 54.59 . 1 682 . 61 HIS CB C 33.35 . 1 683 . 61 HIS CD2 C 116.59 . 1 684 . 61 HIS CE1 C 139.57 . 1 685 . 61 HIS N N 117.17 . 1 686 . 62 GLU H H 8.36 . 1 687 . 62 GLU HA H 4.43 . 1 688 . 62 GLU HB2 H 1.95 . 1 689 . 62 GLU HB3 H 2.06 . 1 690 . 62 GLU HG2 H 2.26 . 2 691 . 62 GLU HG3 H 1.93 . 2 692 . 62 GLU C C 175.50 . 1 693 . 62 GLU CA C 55.74 . 1 694 . 62 GLU CB C 32.51 . 1 695 . 62 GLU CG C 35.96 . 1 696 . 62 GLU CD C 183.26 . 1 697 . 62 GLU N N 120.83 . 1 698 . 63 LEU H H 8.95 . 1 699 . 63 LEU HA H 4.79 . 1 700 . 63 LEU HB2 H 1.65 . 1 701 . 63 LEU HB3 H 2.16 . 1 702 . 63 LEU HG H 1.57 . 1 703 . 63 LEU HD1 H 1.10 . 1 704 . 63 LEU HD2 H 1.04 . 1 705 . 63 LEU C C 175.52 . 1 706 . 63 LEU CA C 54.22 . 1 707 . 63 LEU CB C 40.10 . 1 708 . 63 LEU CG C 27.65 . 1 709 . 63 LEU CD1 C 24.80 . 1 710 . 63 LEU CD2 C 27.42 . 1 711 . 63 LEU N N 128.94 . 1 712 . 64 VAL H H 9.00 . 1 713 . 64 VAL HA H 3.68 . 1 714 . 64 VAL HB H 1.77 . 1 715 . 64 VAL HG1 H 0.88 . 1 716 . 64 VAL HG2 H 0.90 . 1 717 . 64 VAL C C 176.42 . 1 718 . 64 VAL CA C 65.24 . 1 719 . 64 VAL CB C 32.72 . 1 720 . 64 VAL CG1 C 22.33 . 1 721 . 64 VAL CG2 C 21.68 . 1 722 . 64 VAL N N 130.31 . 1 723 . 65 ALA H H 7.84 . 1 724 . 65 ALA HA H 4.62 . 1 725 . 65 ALA HB H 1.12 . 1 726 . 65 ALA C C 174.58 . 1 727 . 65 ALA CA C 51.56 . 1 728 . 65 ALA CB C 23.26 . 1 729 . 65 ALA N N 116.44 . 1 730 . 66 LYS H H 8.85 . 1 731 . 66 LYS HA H 5.36 . 1 732 . 66 LYS HB2 H 2.04 . 1 733 . 66 LYS HB3 H 1.83 . 1 734 . 66 LYS HG2 H 1.59 . 1 735 . 66 LYS HG3 H 1.43 . 1 736 . 66 LYS HD2 H 1.73 . 1 737 . 66 LYS HD3 H 1.73 . 1 738 . 66 LYS HE2 H 3.11 . 1 739 . 66 LYS HE3 H 3.11 . 1 740 . 66 LYS C C 173.76 . 1 741 . 66 LYS CA C 55.07 . 1 742 . 66 LYS CB C 36.50 . 1 743 . 66 LYS CG C 23.51 . 1 744 . 66 LYS CD C 29.80 . 1 745 . 66 LYS CE C 42.39 . 1 746 . 66 LYS N N 116.19 . 1 747 . 67 GLU H H 9.12 . 1 748 . 67 GLU HA H 4.73 . 1 749 . 67 GLU HB2 H 1.88 . 1 750 . 67 GLU HB3 H 2.11 . 1 751 . 67 GLU HG2 H 2.32 . 2 752 . 67 GLU HG3 H 2.25 . 2 753 . 67 GLU C C 176.20 . 1 754 . 67 GLU CA C 56.18 . 1 755 . 67 GLU CB C 32.51 . 1 756 . 67 GLU CG C 36.67 . 1 757 . 67 GLU CD C 183.85 . 1 758 . 67 GLU N N 123.72 . 1 759 . 68 THR H H 8.80 . 1 760 . 68 THR HA H 4.87 . 1 761 . 68 THR HB H 4.48 . 1 762 . 68 THR HG2 H 0.94 . 1 763 . 68 THR C C 173.70 . 1 764 . 68 THR CA C 60.14 . 1 765 . 68 THR CB C 69.19 . 1 766 . 68 THR CG2 C 22.08 . 1 767 . 69 ASP H H 8.44 . 1 768 . 69 ASP HA H 4.79 . 1 769 . 69 ASP HB2 H 2.73 . 1 770 . 69 ASP HB3 H 2.83 . 1 771 . 69 ASP C C 175.55 . 1 772 . 69 ASP CA C 55.37 . 1 773 . 69 ASP CB C 41.12 . 1 774 . 69 ASP CG C 181.05 . 1 775 . 69 ASP N N 122.28 . 1 776 . 70 GLY H H 7.80 . 1 777 . 70 GLY HA2 H 4.08 . 1 778 . 70 GLY HA3 H 3.81 . 1 779 . 70 GLY C C 170.66 . 1 780 . 70 GLY CA C 44.18 . 1 781 . 70 GLY N N 108.46 . 1 782 . 71 LEU H H 7.84 . 1 783 . 71 LEU HA H 4.00 . 1 784 . 71 LEU HB2 H 1.18 . 1 785 . 71 LEU HB3 H 1.53 . 1 786 . 71 LEU HG H 1.40 . 1 787 . 71 LEU HD1 H 0.83 . 1 788 . 71 LEU HD2 H 0.34 . 1 789 . 71 LEU C C 175.50 . 1 790 . 71 LEU CA C 52.46 . 1 791 . 71 LEU CB C 43.54 . 1 792 . 71 LEU CG C 27.15 . 1 793 . 71 LEU CD1 C 25.46 . 1 794 . 71 LEU CD2 C 23.49 . 1 795 . 71 LEU N N 116.99 . 1 796 . 72 PRO HA H 4.05 . 1 797 . 72 PRO HB2 H 2.01 . 1 798 . 72 PRO HB3 H 2.22 . 1 799 . 72 PRO HG2 H 1.89 . 2 800 . 72 PRO HG3 H 1.69 . 2 801 . 72 PRO HD2 H 3.60 . 2 802 . 72 PRO HD3 H 3.30 . 2 803 . 72 PRO C C 175.18 . 1 804 . 72 PRO CA C 62.50 . 1 805 . 72 PRO CB C 34.06 . 1 806 . 72 PRO CG C 24.17 . 1 807 . 72 PRO CD C 50.01 . 1 808 . 73 TYR H H 8.32 . 1 809 . 73 TYR HA H 4.95 . 1 810 . 73 TYR HB2 H 2.62 . 1 811 . 73 TYR HB3 H 2.95 . 1 812 . 73 TYR HD1 H 6.80 . 1 813 . 73 TYR HD2 H 6.80 . 1 814 . 73 TYR HE1 H 6.43 . 1 815 . 73 TYR HE2 H 6.43 . 1 816 . 73 TYR C C 176.17 . 1 817 . 73 TYR CA C 55.97 . 1 818 . 73 TYR CB C 39.26 . 1 819 . 73 TYR CD1 C 132.09 . 1 820 . 73 TYR CD2 C 132.09 . 1 821 . 73 TYR CE1 C 118.37 . 1 822 . 73 TYR CE2 C 118.37 . 1 823 . 73 TYR N N 120.31 . 1 824 . 74 ARG H H 7.97 . 1 825 . 74 ARG HA H 5.59 . 1 826 . 74 ARG HB2 H 1.27 . 1 827 . 74 ARG HB3 H 1.05 . 1 828 . 74 ARG HG2 H 1.47 . 1 829 . 74 ARG HG3 H 1.59 . 1 830 . 74 ARG HD2 H 2.99 . 2 831 . 74 ARG HD3 H 2.63 . 2 832 . 74 ARG C C 174.59 . 1 833 . 74 ARG CA C 54.74 . 1 834 . 74 ARG CB C 35.33 . 1 835 . 74 ARG CG C 27.34 . 1 836 . 74 ARG CD C 43.90 . 1 837 . 74 ARG N N 117.27 . 1 838 . 75 TYR H H 8.84 . 1 839 . 75 TYR HA H 5.09 . 1 840 . 75 TYR HB2 H 2.91 . 1 841 . 75 TYR HB3 H 2.83 . 1 842 . 75 TYR HD1 H 6.89 . 1 843 . 75 TYR HD2 H 6.89 . 1 844 . 75 TYR HE1 H 6.44 . 1 845 . 75 TYR HE2 H 6.44 . 1 846 . 75 TYR C C 173.29 . 1 847 . 75 TYR CA C 56.25 . 1 848 . 75 TYR CB C 42.32 . 1 849 . 75 TYR CD1 C 133.30 . 1 850 . 75 TYR CD2 C 133.30 . 1 851 . 75 TYR CE1 C 117.08 . 1 852 . 75 TYR CE2 C 117.08 . 1 853 . 75 TYR N N 117.08 . 1 854 . 76 LEU H H 9.18 . 1 855 . 76 LEU HA H 5.75 . 1 856 . 76 LEU HB2 H 1.21 . 1 857 . 76 LEU HB3 H 1.94 . 1 858 . 76 LEU HG H 1.29 . 1 859 . 76 LEU HD1 H 0.98 . 1 860 . 76 LEU HD2 H 0.77 . 1 861 . 76 LEU C C 175.17 . 1 862 . 76 LEU CA C 53.42 . 1 863 . 76 LEU CB C 45.64 . 1 864 . 76 LEU CG C 27.98 . 1 865 . 76 LEU CD1 C 24.50 . 1 866 . 76 LEU CD2 C 26.49 . 1 867 . 76 LEU N N 125.85 . 1 868 . 77 ILE H H 9.37 . 1 869 . 77 ILE HA H 5.44 . 1 870 . 77 ILE HB H 1.81 . 1 871 . 77 ILE HG12 H 1.14 . 1 872 . 77 ILE HG13 H 1.50 . 1 873 . 77 ILE HG2 H 0.79 . 1 874 . 77 ILE HD1 H 0.69 . 1 875 . 77 ILE C C 174.04 . 1 876 . 77 ILE CA C 59.01 . 1 877 . 77 ILE CB C 41.72 . 1 878 . 77 ILE CG1 C 27.46 . 1 879 . 77 ILE CG2 C 17.46 . 1 880 . 77 ILE CD1 C 14.91 . 1 881 . 77 ILE N N 124.44 . 1 882 . 78 ARG H H 9.51 . 1 883 . 78 ARG HA H 5.16 . 1 884 . 78 ARG HB2 H 1.87 . 2 885 . 78 ARG HB3 H 1.35 . 2 886 . 78 ARG HG2 H 1.38 . 1 887 . 78 ARG HG3 H 1.38 . 1 888 . 78 ARG HD2 H 3.25 . 1 889 . 78 ARG HD3 H 3.25 . 1 890 . 78 ARG C C 175.85 . 1 891 . 78 ARG CA C 54.08 . 1 892 . 78 ARG CB C 33.80 . 1 893 . 78 ARG CG C 26.90 . 1 894 . 78 ARG CD C 43.41 . 1 895 . 78 ARG N N 125.21 . 1 896 . 79 LYS H H 8.53 . 1 897 . 79 LYS HA H 4.25 . 1 898 . 79 LYS HB2 H 2.12 . 2 899 . 79 LYS HB3 H 1.41 . 2 900 . 79 LYS HG2 H 1.82 . 2 901 . 79 LYS HG3 H 1.25 . 2 902 . 79 LYS HD2 H 1.70 . 2 903 . 79 LYS HD3 H 1.25 . 2 904 . 79 LYS HE2 H 3.02 . 2 905 . 79 LYS HE3 H 2.93 . 2 906 . 79 LYS C C 177.69 . 1 907 . 79 LYS CA C 57.30 . 1 908 . 79 LYS CB C 33.03 . 1 909 . 79 LYS CG C 26.50 . 1 910 . 79 LYS CD C 29.90 . 1 911 . 79 LYS CE C 42.71 . 1 912 . 79 LYS N N 127.64 . 1 913 . 80 GLY HA2 H 4.36 . 2 914 . 80 GLY HA3 H 4.14 . 2 915 . 80 GLY C C 173.13 . 1 916 . 80 GLY CA C 45.39 . 1 917 . 81 GLY H H 7.88 . 1 918 . 81 GLY HA2 H 3.96 . 2 919 . 81 GLY HA3 H 3.73 . 2 920 . 81 GLY C C 179.21 . 1 921 . 81 GLY CA C 45.98 . 1 922 . 81 GLY N N 113.09 . 1 stop_ save_